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Human Metabolome Database Version 2.5

 

Showing metabocard for Sepiapterin (HMDB00238)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2011-07-20 18:10:33
Accession Number HMDB00238
Secondary Accession Numbers Not Available
Common Name Sepiapterin
Description Sepiapterin is an intermediate in the salvage pathway of tetrahydrobiopterin (BH(4)). It is a yellow fluorescing pigment. Sepiapterin accumulates in the brain of patients with sepiapterin reductase (SR) deficiency.
Synonyms
  1. L-sepiapterin
  2. Sepiapterin
  3. Sepiapterine
  4. 2-Amino-6-(S)-lactoyl-7,8-dihydro-4(3H)-pteridinone
  5. (S)-2-amino-7,8-dihydro-6-(2-hydroxy-1-oxopropyl)-4(1H)-Pteridinone
  6. 1-(2-amino-7,8-dihydro-4-hydroxy-6-pteridinyl)-2-hydroxy-1-Propanone
  7. 2-amino-7,8-dihydro-6-[(2S)-2-hydroxy-1-oxopropyl]-4(1H)Pteridinone
  8. Lopac-S-154
Chemical IUPAC Name 2-amino-6-(2-hydroxypropanoyl)-7,8-dihydro-1H-pty oeridin-4-one
Chemical Formula C9H11N5O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Pterins
Sub Class
  • Dihydro-pterins
Family
  • Mammalian Metabolite
Species
  • ketone
  • imine
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • secondary amine
  • secondary aliphatic/aromatic amine (alkylarylamine)
  • oxo(het)arene
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Folate biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 237.215
Monoisotopic Molecular Weight 237.086182
Isomeric SMILES C[C@H](O)C(=O)C1=NC2=C(NC1)NC(N)=NC2=O
Canonical SMILES CC(O)C(=O)C1=NC2=C(NC1)NC(N)=NC2=O
KEGG Compound ID C00835 Link Image
BioCyc ID CPD-374 Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB00238 Link Image
Metagene Link HMDB00238 Link Image
METLIN ID 5244 Link Image
PubChem Compound 65253 Link Image
PubChem Substance 17405679 Link Image
ChEBI ID 16095 Link Image
CAS Registry Number 17094-01-8
InChI Identifier InChI=1/C9H11N5O3/c1-3(15)6(16)4-2-11-7-5(12-4)8(17)14-9(10)13-7/h3,15H,2H2,1H3,(H4,10,11,13,14,17)/t3-/m0/s1
Synthesis Reference Pfleiderer, Wolfgang. Synthesis and absolute configuration of sepiapterin. Chem. Biol. Pteridines, Proc. Int. Symp., 5th (1975), 941-9.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.18 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.09 [Predicted by ALOGPS]; -1.9 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location
  • Cerebrospinal Fluid
Tissue Location Not Available
Concentrations (Normal)
Biofluid CSF
Value 0.0005 (0.0-0.001) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Zorzi G, Redweik U, Trippe H, Penzien JM, Thony B, Blau N: Detection of sepiapterin in CSF of patients with sepiapterin reductase deficiency. Mol Genet Metab. 2002 Feb;75(2):174-7. [PubMed Link Image]
Biofluid CSF
Value <0.0005 uM
Age Children:1-13 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Verbeek MM, Willemsen MA, Wevers RA, Lagerwerf AJ, Abeling NG, Blau N, Thony B, Vargiami E, Zafeiriou DI: Two Greek siblings with sepiapterin reductase deficiency. Mol Genet Metab. 2008 Aug;94(4):403-9. Epub 2008 May 27. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid CSF
Value 0.0083 (0.0056-0.011) uM
Age Adult:>18 yrs old
Sex Both
Condition Sepiapterin reductase deficiency
Comments Not Available
References
  • Zorzi G, Redweik U, Trippe H, Penzien JM, Thony B, Blau N: Detection of sepiapterin in CSF of patients with sepiapterin reductase deficiency. Mol Genet Metab. 2002 Feb;75(2):174-7. [PubMed Link Image]
Biofluid CSF
Value 0.01375 (0.0075-0.02) uM
Age Children:1-13 yrs old
Sex Male
Comments Not Available
References
  • Verbeek MM, Willemsen MA, Wevers RA, Lagerwerf AJ, Abeling NG, Blau N, Thony B, Vargiami E, Zafeiriou DI: Two Greek siblings with sepiapterin reductase deficiency. Mol Genet Metab. 2008 Aug;94(4):403-9. Epub 2008 May 27. [PubMed Link Image]
Associated Disorders
Condition References
Sepiapterin reductase deficiency
  • Zorzi G, Redweik U, Trippe H, Penzien JM, Thony B, Blau N: Detection of sepiapterin in CSF of patients with sepiapterin reductase deficiency. Mol Genet Metab. 2002 Feb;75(2):174-7. [PubMed Link Image]
OMIM ID
  • 182125 Link Image (Sepiapterin reductase deficiency)
Pathways
Name SMPDB Link KEGG Link
Pterine Biosynthesis SMP00005 Link Image map00790 Link Image
General References
  1. Zorzi G, Redweik U, Trippe H, Penzien JM, Thony B, Blau N: Detection of sepiapterin in CSF of patients with sepiapterin reductase deficiency. Mol Genet Metab. 2002 Feb;75(2):174-7. [PubMed Link Image]
Metabolic Enzymes
  1. Sepiapterin reductase
  2. 14-3-3 protein zeta/delta
  3. 14-3-3 protein beta/alpha
  4. 14-3-3 protein gamma
Enzyme 1 [top]
Enzyme 1 ID 5673
Enzyme 1 Name Sepiapterin reductase
Enzyme 1 Synonyms
  1. SPR
Enzyme 1 Gene Name SPR
Enzyme 1 Protein Sequence >Sepiapterin reductase
MEGGLGRAVCLLTGASRGFGRTLAPLLASLLSPGSVLVLSARNDEALRQLEAELGAERSG
LRVVRVPADLGAEAGLQQLLGALRELPRPKGLQRLLLINNAGSLGDVSKGFVDLSDSTQV
NNYWALNLTSMLCLTSSVLKAFPDSPGLNRTVVNISSLCALQPFKGWALYCAGKAARDML
FQVLALEEPNVRVLNYAPGPLDTDMQQLARETSVDPDMRKGLQELKAKGKLVDCKVSAQK
LLSLLEKDEFKSGAHVDFYDK
Enzyme 1 Number of Residues 261
Enzyme 1 Molecular Weight 28048.1
Enzyme 1 Theoretical pI 8.19
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • sepiapterin reductase activity
Process
  • biosynthetic process
  • cellular biosynthetic process
  • heterocycle biosynthetic process
  • metabolic process
  • oxidation reduction
  • pteridine and derivative biosynthetic process
  • tetrahydrobiopterin biosynthetic process
Component
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function Catalyzes the final one or two reductions in tetra- hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (1) 7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+ [RN:R02975]
  • (2) tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+ [RN:R08208]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 338021 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P35270 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name SPRE_HUMAN Link Image
Enzyme 1 PDB ID 1Z6Z Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >786 bp
ATGGAGGGCGGGCTGGGGCGTGCTGTGTGCTTGCTGACCGGGGCCTCCCGCGGCTTCGGC
CGGACGCTGGCCCCGCTCCTGGCCTCGCTGCTGTCGCCCGGCTCCGTGCTTGTCCTTAGC
GCCCGCAACGACGAGGCACTGCGCCAGCTGGAGGCCGAGCTGGGCGCCGAGCGGTCTGGC
CTGCGCGTGGTGCGGGTGCCCGCCGACCTGGGCGCCGAGGCCGGCTTGCAGCAGCTGCTC
GGCGCCCTGCGCGAGCTCCCCCGGCCCAAGGGGCTGCAGCGACTGCTGCTTATCAACAAC
GCGGGCTCTCTTGGGGATGTGTCCAAAGGCTTCGTGGACCTGAGTGACTCCACTCAAGTG
AACAACTACTGGGCACTGAACTTGACCTCCATGCTCTGCCTGACTTCCAGCGTCCTGAAG
GCCTTCCCGGACAGTCCTGGCCTCAACAGAACCGTGGTTAACATCTCGTCCCTCTGTGCC
CTGCAACCTTTCAAAGGCTGGGCGCTGTACTGTGCAGGAAAGGCTGCTCGTGATATGCTG
TTCCAGGTCCTGGCGCTGGAGGAACCTAATGTGAGGGTGCTGAACTATGCCCCAGGTCCT
CTGGACACAGACATGCAGCAGTTGGCCCGGGAGACCTCCGTGGACCCAGACATGCGAAAA
GGGCTGCAGGAGCTGAAGGCAAAGGGGAAGCTGGTGGATTGCAAGGTGTCAGCCCAGAAA
CTGCTGAGCTTACTGGAAAAGGACGAGTTCAAGTCTGGAGCCCACGTGGACTTCTATGAC
AAATAA
Enzyme 1 GenBank Gene ID M76231 Link Image
Enzyme 1 GeneCard ID SPR Link Image
Enzyme 1 GenAtlas ID SPR Link Image
Enzyme 1 HGNC ID HGNC:11257 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2p14-p12
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Ichinose H, Katoh S, Sueoka T, Titani K, Fujita K, Nagatsu T: Cloning and sequencing of cDNA encoding human sepiapterin reductase--an enzyme involved in tetrahydrobiopterin biosynthesis. Biochem Biophys Res Commun. 1991 Aug 30;179(1):183-9. [PubMed Link Image]
  2. Maier J, Schott K, Werner T, Bacher A, Ziegler I: Detection of a novel sepiapterin reductase mRNA: assay of mRNA in various cells and tissues of various species. Exp Cell Res. 1993 Feb;204(2):217-22. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Ohye T, Hori TA, Katoh S, Nagatsu T, Ichinose H: Genomic organization and chromosomal localization of the human sepiapterin reductase gene. Biochem Biophys Res Commun. 1998 Oct 20;251(2):597-602. [PubMed Link Image]
  7. Fujimoto K, Takahashi SY, Katoh S: Mutational analysis of sites in sepiapterin reductase phosphorylated by Ca2+/calmodulin-dependent protein kinase II. Biochim Biophys Acta. 2002 Jan 31;1594(1):191-8. [PubMed Link Image]
  8. Bonafe L, Thony B, Penzien JM, Czarnecki B, Blau N: Mutations in the sepiapterin reductase gene cause a novel tetrahydrobiopterin-dependent monoamine-neurotransmitter deficiency without hyperphenylalaninemia. Am J Hum Genet. 2001 Aug;69(2):269-77. Epub 2001 Jul 6. [PubMed Link Image]
  9. Abeling NG, Duran M, Bakker HD, Stroomer L, Thony B, Blau N, Booij J, Poll-The BT: Sepiapterin reductase deficiency an autosomal recessive DOPA-responsive dystonia. Mol Genet Metab. 2006 Sep-Oct;89(1-2):116-20. Epub 2006 May 2. [PubMed Link Image]
  10. Friedman J, Hyland K, Blau N, MacCollin M: Dopa-responsive hypersomnia and mixed movement disorder due to sepiapterin reductase deficiency. Neurology. 2006 Dec 12;67(11):2032-5. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 8051
Enzyme 2 Name 14-3-3 protein zeta/delta
Enzyme 2 Synonyms
  1. Protein kinase C inhibitor protein 1
  2. KCIP-1
Enzyme 2 Gene Name YWHAZ
Enzyme 2 Protein Sequence >14-3-3 protein zeta/delta
MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWR
VVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLK
MKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYE
ILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAG
EGGEN
Enzyme 2 Number of Residues 245
Enzyme 2 Molecular Weight 27744.8
Enzyme 2 Theoretical pI 4.43
Enzyme 2 GO Classification
Function
  • binding
  • protein binding
  • protein domain specific binding
Process
Component
Enzyme 2 General Function Involved in protein domain specific binding
Enzyme 2 Specific Function Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathway. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID P63104 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name 1433Z_HUMAN Link Image
Enzyme 2 PDB ID 1QJA Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >738 bp
ATGGATAAAAATGAGCTGGTTCAGAAGGCCAAACTGGCCGAGCAGGCTGAGCGATATGAT
GACATGGCAGCCTGCATGAAGTCTGTAACTGAGCAAGGAGCTGAATTATCCAATGAGGAG
AGGAATCTTCTCTCAGTTGCTTATAAAAATGTTGTAGGAGCCCGTAGGTCATCTTGGAGG
GTCGTCTCAAGTATTGAACAAAAGACGGAAGGTGCTGAGAAAAAACAGCAGATGGCTCGA
GAATACAGAGAGAAAATTGAGACGGAGCTAAGAGATATCTGCAATGATGTACTGTCTCTT
TTGGAAAAGTTCTTGATCCCCAATGCTTCACAAGCAGAGAGCAAAGTCTTCTATTTGAAA
ATGAAAGGAGATTACTACCGTTACTTGGCTGAGGTTGCCGCTGGTGATGACAAGAAAGGG
ATTGTCGATCAGTCACAACAAGCATACCAAGAAGCTTTTGAAATCAGCAAAAAGGAAATG
CAACCAACACATCCTATCAGACTGGGTCTGGCCCTTAACTTCTCTGTGTTCTATTATGAG
ATTCTGAACTCCCCAGAGAAAGCCTGCTCTCTTGCAAAGACAGCTTTTGATGAAGCCATT
GCTGAACTTGATACATTAAGTGAAGAGTCATACAAAGACAGCACGCTAATAATGCAATTA
CTGAGAGACAACTTGACATTGTGGACATCGGATACCCAAGGAGACGAAGCTGAAGCAGGA
GAAGGAGGGGAAAATTAA
Enzyme 2 GenBank Gene ID M86400 Link Image
Enzyme 2 GeneCard ID YWHAZ Link Image
Enzyme 2 GenAtlas ID YWHAZ Link Image
Enzyme 2 HGNC ID HGNC:12855 Link Image
Enzyme 2 Chromosome Location 8
Enzyme 2 Locus 8q23.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Zupan LA, Steffens DL, Berry CA, Landt M, Gross RW: Cloning and expression of a human 14-3-3 protein mediating phospholipolysis. Identification of an arachidonoyl-enzyme intermediate during catalysis. J Biol Chem. 1992 May 5;267(13):8707-10. [PubMed Link Image]
  2. Seluja GA, Elias L, Pietromonaco SF: Two unique 5' untranslated regions in mRNAs encoding human 14-3-3 zeta: differential expression in hemopoietic cells. Biochim Biophys Acta. 1998 Feb 11;1395(3):281-7. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Dubois T, Rommel C, Howell S, Steinhussen U, Soneji Y, Morrice N, Moelling K, Aitken A: 14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction. J Biol Chem. 1997 Nov 14;272(46):28882-8. [PubMed Link Image]
  7. Powell DW, Rane MJ, Chen Q, Singh S, McLeish KR: Identification of 14-3-3zeta as a protein kinase B/Akt substrate. J Biol Chem. 2002 Jun 14;277(24):21639-42. Epub 2002 Apr 15. [PubMed Link Image]
  8. Woodcock JM, Murphy J, Stomski FC, Berndt MC, Lopez AF: The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface. J Biol Chem. 2003 Sep 19;278(38):36323-7. Epub 2003 Jul 15. [PubMed Link Image]
  9. Zheng W, Zhang Z, Ganguly S, Weller JL, Klein DC, Cole PA: Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation. Nat Struct Biol. 2003 Dec;10(12):1054-7. Epub 2003 Oct 26. [PubMed Link Image]
  10. Tsuruta F, Sunayama J, Mori Y, Hattori S, Shimizu S, Tsujimoto Y, Yoshioka K, Masuyama N, Gotoh Y: JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins. EMBO J. 2004 Apr 21;23(8):1889-99. Epub 2004 Apr 8. [PubMed Link Image]
  11. Nagata-Ohashi K, Ohta Y, Goto K, Chiba S, Mori R, Nishita M, Ohashi K, Kousaka K, Iwamatsu A, Niwa R, Uemura T, Mizuno K: A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia. J Cell Biol. 2004 May 24;165(4):465-71. [PubMed Link Image]
  12. Obsilova V, Vecer J, Herman P, Pabianova A, Sulc M, Teisinger J, Boura E, Obsil T: 14-3-3 Protein interacts with nuclear localization sequence of forkhead transcription factor FoxO4. Biochemistry. 2005 Aug 30;44(34):11608-17. [PubMed Link Image]
  13. Soosairajah J, Maiti S, Wiggan O, Sarmiere P, Moussi N, Sarcevic B, Sampath R, Bamburg JR, Bernard O: Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin. EMBO J. 2005 Feb 9;24(3):473-86. Epub 2005 Jan 20. [PubMed Link Image]
  14. Ma Y, Pitson S, Hercus T, Murphy J, Lopez A, Woodcock J: Sphingosine activates protein kinase A type II by a novel cAMP-independent mechanism. J Biol Chem. 2005 Jul 15;280(28):26011-7. Epub 2005 May 9. [PubMed Link Image]
  15. Yoshida K, Yamaguchi T, Natsume T, Kufe D, Miki Y: JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage. Nat Cell Biol. 2005 Mar;7(3):278-85. [PubMed Link Image]
  16. Ganguly S, Weller JL, Ho A, Chemineau P, Malpaux B, Klein DC: Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205. Proc Natl Acad Sci U S A. 2005 Jan 25;102(4):1222-7. Epub 2005 Jan 11. [PubMed Link Image]
  17. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  18. Gu YM, Jin YH, Choi JK, Baek KH, Yeo CY, Lee KY: Protein kinase A phosphorylates and regulates dimerization of 14-3-3 epsilon. FEBS Lett. 2006 Jan 9;580(1):305-10. Epub 2005 Dec 19. [PubMed Link Image]
  19. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  20. Kim JS, Diebold BA, Babior BM, Knaus UG, Bokoch GM: Regulation of Nox1 activity via protein kinase A-mediated phosphorylation of NoxA1 and 14-3-3 binding. J Biol Chem. 2007 Nov 30;282(48):34787-800. Epub 2007 Oct 3. [PubMed Link Image]
  21. Zenke FT, Krendel M, DerMardirossian C, King CC, Bohl BP, Bokoch GM: p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-H1, a microtubule-localized Rho exchange factor. J Biol Chem. 2004 Apr 30;279(18):18392-400. Epub 2004 Feb 17. [PubMed Link Image]
  22. Brummer T, Larance M, Herrera Abreu MT, Lyons RJ, Timpson P, Emmerich CH, Fleuren ED, Lehrbach GM, Schramek D, Guilhaus M, James DE, Daly RJ: Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein. EMBO J. 2008 Sep 3;27(17):2305-16. [PubMed Link Image]
  23. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  24. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  25. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  26. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  27. Rittinger K, Budman J, Xu J, Volinia S, Cantley LC, Smerdon SJ, Gamblin SJ, Yaffe MB: Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol Cell. 1999 Aug;4(2):153-66. [PubMed Link Image]
  28. Obsil T, Ghirlando R, Klein DC, Ganguly S, Dyda F: Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation. Cell. 2001 Apr 20;105(2):257-67. [PubMed Link Image]
  29. Macdonald N, Welburn JP, Noble ME, Nguyen A, Yaffe MB, Clynes D, Moggs JG, Orphanides G, Thomson S, Edmunds JW, Clayton AL, Endicott JA, Mahadevan LC: Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3. Mol Cell. 2005 Oct 28;20(2):199-211. [PubMed Link Image]
  30. Ottmann C, Yasmin L, Weyand M, Veesenmeyer JL, Diaz MH, Palmer RH, Francis MS, Hauser AR, Wittinghofer A, Hallberg B: Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. EMBO J. 2007 Feb 7;26(3):902-13. Epub 2007 Jan 18. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 14928
Enzyme 3 Name 14-3-3 protein beta/alpha
Enzyme 3 Synonyms
  1. Protein 1054
  2. Protein kinase C inhibitor protein 1
  3. KCIP-1
  4. 14-3-3 protein beta/alpha, N-terminally processed
Enzyme 3 Gene Name YWHAB
Enzyme 3 Protein Sequence >14-3-3 protein beta/alpha
MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSS
WRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFY
LKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFY
YEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGD
AGEGEN
Enzyme 3 Number of Residues 246
Enzyme 3 Molecular Weight 28082.2
Enzyme 3 Theoretical pI 4.47
Enzyme 3 GO Classification
Function
  • binding
  • protein binding
  • protein domain specific binding
Process
Component
Enzyme 3 General Function Involved in protein domain specific binding
Enzyme 3 Specific Function Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathway. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 158258871 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P31946 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name 1433B_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >741 bp
ATGACAATGGATAAAAGTGAGCTGGTACAGAAAGCCAAACTCGCTGAGCAGGCTGAGCGA
TATGATGATATGGCTGCAGCCATGAAGGCAGTCACAGAACAGGGGCATGAACTCTCCAAC
GAAGAGAGAAATCTGCTCTCTGTTGCCTACAAGAATGTGGTAGGCGCCCGCCGCTCTTCC
TGGCGTGTCATCTCCAGCATTGAGCAGAAAACAGAGAGGAATGAGAAGAAGCAGCAGATG
GGCAAAGAGTACCGTGAGAAGATAGAGGCAGAACTGCAGGACATCTGCAATGATGTTCTG
GAGCTGTTGGACAAATATCTTATTCCCAATGCTACACAACCAGAAAGTAAGGTGTTCTAC
TTGAAAATGAAAGGAGATTATTTTAGGTATCTTTCTGAAGTGGCATCTGGAGACAACAAA
CAAACCACTGTGTCGAACTCCCAGCAGGCTTACCAGGAAGCATTTGAAATTAGTAAGAAA
GAAATGCAGCCTACACACCCAATTCGTCTTGGTCTGGCACTAAATTTCTCAGTCTTTTAC
TATGAGATTCTAAACTCTCCTGAAAAGGCCTGTAGCCTGGCAAAAACGGCATTTGATGAA
GCAATTGCTGAATTGGATACGCTGAATGAAGAGTCTTATAAAGACAGCACTCTGATCATG
CAGTTACTTAGGGACAATCTCACTCTGTGGACATCGGAAAACCAGGGAGACGAAGGAGAC
GCTGGGGAGGGAGAGAACTAA
Enzyme 3 GenBank Gene ID AK292717 Link Image
Enzyme 3 GeneCard ID YWHAB Link Image
Enzyme 3 GenAtlas ID YWHAB Link Image
Enzyme 3 HGNC ID HGNC:12849 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 20q13.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Leffers H, Madsen P, Rasmussen HH, Honore B, Andersen AH, Walbum E, Vandekerckhove J, Celis JE: Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway. J Mol Biol. 1993 Jun 20;231(4):982-98. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Screaton RA, Conkright MD, Katoh Y, Best JL, Canettieri G, Jeffries S, Guzman E, Niessen S, Yates JR 3rd, Takemori H, Okamoto M, Montminy M: The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector. Cell. 2004 Oct 1;119(1):61-74. [PubMed Link Image]
  7. Nagata-Ohashi K, Ohta Y, Goto K, Chiba S, Mori R, Nishita M, Ohashi K, Kousaka K, Iwamatsu A, Niwa R, Uemura T, Mizuno K: A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia. J Cell Biol. 2004 May 24;165(4):465-71. [PubMed Link Image]
  8. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  9. Zhao B, Wei X, Li W, Udan RS, Yang Q, Kim J, Xie J, Ikenoue T, Yu J, Li L, Zheng P, Ye K, Chinnaiyan A, Halder G, Lai ZC, Guan KL: Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control. Genes Dev. 2007 Nov 1;21(21):2747-61. [PubMed Link Image]
  10. Liu Y, Ross JF, Bodine PV, Billiard J: Homodimerization of Ror2 tyrosine kinase receptor induces 14-3-3(beta) phosphorylation and promotes osteoblast differentiation and bone formation. Mol Endocrinol. 2007 Dec;21(12):3050-61. Epub 2007 Aug 23. [PubMed Link Image]
  11. Brummer T, Larance M, Herrera Abreu MT, Lyons RJ, Timpson P, Emmerich CH, Fleuren ED, Lehrbach GM, Schramek D, Guilhaus M, James DE, Daly RJ: Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein. EMBO J. 2008 Sep 3;27(17):2305-16. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  14. Yang X, Lee WH, Sobott F, Papagrigoriou E, Robinson CV, Grossmann JG, Sundstrom M, Doyle DA, Elkins JM: Structural basis for protein-protein interactions in the 14-3-3 protein family. Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17237-42. Epub 2006 Nov 3. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 14929
Enzyme 4 Name 14-3-3 protein gamma
Enzyme 4 Synonyms
  1. Protein kinase C inhibitor protein 1
  2. KCIP-1
  3. 14-3-3 protein gamma, N-terminally processed
Enzyme 4 Gene Name YWHAG
Enzyme 4 Protein Sequence >14-3-3 protein gamma
MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSW
RVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESK
VFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYS
VFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDD
DGGEGNN
Enzyme 4 Number of Residues 247
Enzyme 4 Molecular Weight 28302.3
Enzyme 4 Theoretical pI 4.52
Enzyme 4 GO Classification
Function
  • binding
  • protein binding
  • protein domain specific binding
Process
Component
Enzyme 4 General Function Involved in protein domain specific binding
Enzyme 4 Specific Function Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathway. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 6016838 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P61981 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name 1433G_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >744 bp
ATGGTGGACCGCGAGCAACTGGTGCAGAAAGCCCGGCTGGCCGAGCAGGCGGAGCGCTAC
GACGACATGGCCGCGGCCATGAAGAACGTGACAGAGCTGAATGAGCCACTGTCGAATGAG
GAACGAAACCTTCTGTCTGTGGCCTACAAGAACGTTGTGGGGGCACGCCGCTCTTCCTGG
AGGGTCATCAGTAGCATTGAGCAGAAGACATCTGCAGACGGCAATGAGAAGAAGATTGAG
ATGGTCCGTGCGTACCGGGAGAAGATAGAGAAGGAGTTGGAGGCTGTGTGCCAGGATGTG
CTGAGCCTGCTGGATAACTACCTGATCAAGAATTGCAGCGAGACCCAGTACGAGAGCAAA
GTGTTCTACCTGAAGATGAAAGGGGACTACTACCGCTACCTGGCTGAAGTGGCCACCGGA
GAGAAAAGGGCGACGGTGGTGGAGTCCTCCGAGAAGGCCTACAGCGAAGCCCACGAGATC
AGCAAAGAGCACATGCAGCCCACCCACCCCATCCGATTAGGCCTGGCTCTTAACTACTCC
GTCTTCTACTATGAGATCCAGAACGCCCCAGAGCAAGCGTGCCACTTGGCCAAGACCGCG
TTCGACGACGCCATCGCCGAGCTTGACACCCTCAACGAGGACTCCTACAAGGACTCCACG
CTCATCATGCAGCTCCTCCGCGACAACCTCACGCTCTGGACGAGCGACCAGCAGGACGAC
GATGGCGGCGAAGGCAACAATTAA
Enzyme 4 GenBank Gene ID AB024334 Link Image
Enzyme 4 GeneCard ID YWHAG Link Image
Enzyme 4 GenAtlas ID YWHAG Link Image
Enzyme 4 HGNC ID HGNC:12852 Link Image
Enzyme 4 Chromosome Location 7
Enzyme 4 Locus 7q11.23
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Autieri MV, Carbone CJ: 14-3-3Gamma interacts with and is phosphorylated by multiple protein kinase C isoforms in PDGF-stimulated human vascular smooth muscle cells. DNA Cell Biol. 1999 Jul;18(7):555-64. [PubMed Link Image]
  2. Horie M, Suzuki M, Takahashi E, Tanigami A: Cloning, expression, and chromosomal mapping of the human 14-3-3gamma gene (YWHAG) to 7q11.23. Genomics. 1999 Sep 1;60(2):241-3. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Towbin H, Bair KW, DeCaprio JA, Eck MJ, Kim S, Kinder FR, Morollo A, Mueller DR, Schindler P, Song HK, van Oostrum J, Versace RW, Voshol H, Wood J, Zabludoff S, Phillips PE: Proteomics-based target identification: bengamides as a new class of methionine aminopeptidase inhibitors. J Biol Chem. 2003 Dec 26;278(52):52964-71. Epub 2003 Oct 8. [PubMed Link Image]
  7. Screaton RA, Conkright MD, Katoh Y, Best JL, Canettieri G, Jeffries S, Guzman E, Niessen S, Yates JR 3rd, Takemori H, Okamoto M, Montminy M: The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector. Cell. 2004 Oct 1;119(1):61-74. [PubMed Link Image]
  8. Nagata-Ohashi K, Ohta Y, Goto K, Chiba S, Mori R, Nishita M, Ohashi K, Kousaka K, Iwamatsu A, Niwa R, Uemura T, Mizuno K: A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia. J Cell Biol. 2004 May 24;165(4):465-71. [PubMed Link Image]
  9. Yoshida K, Yamaguchi T, Natsume T, Kufe D, Miki Y: JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage. Nat Cell Biol. 2005 Mar;7(3):278-85. [PubMed Link Image]
  10. Brummer T, Larance M, Herrera Abreu MT, Lyons RJ, Timpson P, Emmerich CH, Fleuren ED, Lehrbach GM, Schramek D, Guilhaus M, James DE, Daly RJ: Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein. EMBO J. 2008 Sep 3;27(17):2305-16. [PubMed Link Image]
  11. Yang X, Lee WH, Sobott F, Papagrigoriou E, Robinson CV, Grossmann JG, Sundstrom M, Doyle DA, Elkins JM: Structural basis for protein-protein interactions in the 14-3-3 protein family. Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17237-42. Epub 2006 Nov 3. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available