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Showing Protein STAM-binding protein (HMDBP10111)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP10111
Secondary Accession Numbers
  • 16063
Name STAM-binding protein
Synonyms
  1. Associated molecule with the SH3 domain of STAM
  2. Endosome-associated ubiquitin isopeptidase
Gene Name STAMBP
Protein Type Enzyme
Biological Properties
General Function Involved in metal ion binding
Specific Function Zinc metalloprotease that specifically cleaves 'Lys-63'- linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains. Functions at the endosome and is able to oppose the ubiquitin-dependent sorting of receptors to lysosomes. Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7
Pathways Not Available
Reactions Not Available
GO Classification Not Available
Cellular Location
  1. Nucleus
  2. Cytoplasm
  3. Peripheral membrane protein
  4. Membrane
  5. Early endosome
Gene Properties
Chromosome Location Chromosome:2
Locus 2p13.1
SNPs STAMBP
Gene Sequence 
>1275 bp
ATGTCTGACCATGGAGATGTGAGCCTCCCGCCCGAAGACCGGGTGAGGGCTCTCTCCCAG
CTGGGTAGTGCGGTAGAGGTGAATGAAGACATTCCACCCCGTCGGTACTTCCGCTCTGGA
GTTGAGATTATCCGAATGGCATCCATTTACTCTGAGGAAGGCAACATTGAACATGCCTTC
ATCCTCTATAACAAGTATATCACGCTCTTTATTGAGAAACTACCAAAACATCGAGATTAC
AAATCTGCTGTCATTCCTGAAAAGAAAGACACAGTAAAGAAATTAAAGGAGATTGCATTT
CCCAAAGCAGAAGAGCTGAAGGCAGAGCTGTTAAAACGATATACCAAAGAATATACAGAA
TATAATGAAGAAAAGAAGAAGGAAGCAGAGGAATTGGCCCGGAACATGGCCATCCAGCAA
GAGCTGGAAAAGGAAAAACAGAGGGTAGCACAACAGAAGCAGCAGCAATTGGAACAGGAA
CAGTTCCATGCCTTCGAGGAGATGATCCGGAACCAGGAGCTAGAAAAAGAGCGACTGAAA
ATTGTACAGGAGTTTGGGAAGGTAGACCCTGGCCTAGGTGGCCCGCTAGTGCCTGACTTG
GAGAAGCCCTCCTTAGATGTGTTCCCCACCTTAACAGTCTCATCCATACAGCCTTCAGAC
TGTCACACAACTGTAAGGCCAGCTAAGCCACCTGTGGTGGACAGGTCCTTGAAACCTGGA
GCACTGAGCAACTCAGAAAGTATTCCCACAATCGATGGATTGCGCCATGTGGTGGTGCCT
GGGCGGCTGTGCCCACAGTTTCTCCAGTTAGCCAGTGCCAACACTGCCCGGGGAGTGGAG
ACATGTGGAATTCTCTGTGGAAAACTGATGAGGAATGAATTTACCATTACCCATGTTCTC
ATCCCCAAGCAAAGTGCTGGGTCTGATTACTGCAACACAGAGAACGAAGAAGAACTTTTC
CTCATACAGGATCAGCAGGGCCTCATCACACTGGGCTGGATTCATACTCACCCCACACAG
ACCGCGTTTCTCTCCAGTGTCGACCTACACACTCACTGCTCTTACCAGATGATGTTGCCA
GAGTCAGTAGCCATTGTTTGCTCCCCCAAGTTCCAGGAAACTGGATTCTTTAAACTAACT
GACCATGGACTAGAGGAGATTTCTTCCTGTCGCCAGAAAGGATTTCATCCACACAGCAAG
GATCCACCTCTGTTCTGTAGCTGCAGCCACGTGACTGTTGTGGACAGAGCAGTGACCATC
ACAGACCTTCGATGA
Protein Properties
Number of Residues 424
Molecular Weight 48076.5
Theoretical pI 6.24
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>STAM-binding protein
MSDHGDVSLPPEDRVRALSQLGSAVEVNEDIPPRRYFRSGVEIIRMASIYSEEGNIEHAF
ILYNKYITLFIEKLPKHRDYKSAVIPEKKDTVKKLKEIAFPKAEELKAELLKRYTKEYTE
YNEEKKKEAEELARNMAIQQELEKEKQRVAQQKQQQLEQEQFHAFEEMIRNQELEKERLK
IVQEFGKVDPGLGGPLVPDLEKPSLDVFPTLTVSSIQPSDCHTTVRPAKPPVVDRSLKPG
ALSNSESIPTIDGLRHVVVPGRLCPQFLQLASANTARGVETCGILCGKLMRNEFTITHVL
IPKQSAGSDYCNTENEEELFLIQDQQGLITLGWIHTHPTQTAFLSSVDLHTHCSYQMMLP
ESVAIVCSPKFQETGFFKLTDHGLEEISSCRQKGFHPHSKDPPLFCSCSHVTVVDRAVTI
TDLR
GenBank ID Protein 62630163
UniProtKB/Swiss-Prot ID O95630
UniProtKB/Swiss-Prot Entry Name STABP_HUMAN
PDB IDs Not Available
GenBank Gene ID AC073046
GeneCard ID STAMBP
GenAtlas ID STAMBP
HGNC ID HGNC:16950
References
General References
  1. 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:15815621 ]
  2. 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:15489334 ]
  3. Itoh F, Asao H, Sugamura K, Heldin CH, ten Dijke P, Itoh S: Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads. EMBO J. 2001 Aug 1;20(15):4132-42. [PubMed:11483516 ]
  4. Li H, Seth A: An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein. Oncogene. 2004 Mar 11;23(10):1801-8. [PubMed:14755250 ]
  5. Tanaka N, Kaneko K, Asao H, Kasai H, Endo Y, Fujita T, Takeshita T, Sugamura K: Possible involvement of a novel STAM-associated molecule "AMSH" in intracellular signal transduction mediated by cytokines. J Biol Chem. 1999 Jul 2;274(27):19129-35. [PubMed:10383417 ]
  6. Maytal-Kivity V, Reis N, Hofmann K, Glickman MH: MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function. BMC Biochem. 2002 Sep 20;3:28. [PubMed:12370088 ]
  7. McCullough J, Clague MJ, Urbe S: AMSH is an endosome-associated ubiquitin isopeptidase. J Cell Biol. 2004 Aug 16;166(4):487-92. [PubMed:15314065 ]
  8. Zamborlini A, Usami Y, Radoshitzky SR, Popova E, Palu G, Gottlinger H: Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding. Proc Natl Acad Sci U S A. 2006 Dec 12;103(50):19140-5. Epub 2006 Dec 4. [PubMed:17146056 ]
  9. Ma YM, Boucrot E, Villen J, Affar el B, Gygi SP, Gottlinger HG, Kirchhausen T: Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation. J Biol Chem. 2007 Mar 30;282(13):9805-12. Epub 2007 Jan 29. [PubMed:17261583 ]