Hmdb loader

Showing Protein Brain-specific angiogenesis inhibitor 1-associated protein 2 (HMDBP08316)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP08316
Secondary Accession Numbers
  • 14028
Name Brain-specific angiogenesis inhibitor 1-associated protein 2
Synonyms
  1. BAI-associated protein 2
  2. BAI1-associated protein 2
  3. FLAF3
  4. Fas ligand-associated factor 3
  5. IRS-58
  6. IRSp53
  7. IRSp53/58
  8. Insulin receptor substrate p53
  9. Insulin receptor substrate p53/p58
  10. Insulin receptor substrate protein of 53 kDa
  11. Protein BAP2
Gene Name BAIAP2
Protein Type Unknown
Biological Properties
General Function Involved in cytoskeletal adaptor activity
Specific Function Adapter protein that links membrane-bound small G- proteins to cytoplasmic effector proteins. Necessary for CDC42- mediated reorganization of the actin cytoskeleton and for RAC1- mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
protein binding
sh3 domain binding
cytoskeletal adaptor activity
cytoskeletal protein binding
protein domain specific binding
Process
cellular process
biological regulation
regulation of biological process
cell projection organization
cell projection assembly
microspike assembly
filopodium assembly
regulation of cellular process
signal transduction
Cellular Location
  1. Cytoplasm
  2. Peripheral membrane protein
  3. Membrane
  4. Cell projection
  5. Cell projection
  6. filopodium
  7. ruffle
Gene Properties
Chromosome Location Chromosome:1
Locus 17q25
SNPs BAIAP2
Gene Sequence 
>1659 bp
ATGTCTCTGTCTCGCTCAGAGGAGATGCACCGGCTCACGGAAAATGTCTATAAGACCATC
ATGGAGCAGTTCAACCCTAGCCTCCGGAACTTCATCGCCATGGGGAAGAATTACGAGAAG
GCACTGGCAGGTGTGACGTATGCAGCCAAAGGCTACTTTGACGCCCTGGTGAAGATGGGG
GAGCTGGCCAGCGAGAGCCAGGGCTCCAAAGAACTCGGAGACGTTCTCTTCCAGATGGCT
GAAGTCCACAGGCAGATCCAGAATCAGCTGGAAGAAATGCTGAAGTCTTTTCACAACGAG
CTGCTTACGCAGCTGGAGCAGAAGGTGGAGCTGGACTCCAGGTATCTGAGTGCTGCGCTG
AAGAAATACCAGACTGAGCAAAGGAGCAAAGGCGACGCCCTGGACAAGTGTCAGGCTGAG
CTGAAGAAGCTTCGGAAGAAGAGCCAGGGCAGCAAGAATCCTCAGAAGTACTCGGACAAG
GAGCTGCAGTACATCGACGCCATCAGCAACAAGCAGGGCGAGCTGGAGAATTACGTGTCC
GACGGCTACAAGACCGCACTGACAGAGGAGCGCAGGCGCTTCTGCTTCCTGGTGGAGAAG
CAGTGCGCCGTGGCCAAGAACTCCGCGGCCTACCACTCCAAGGGCAAGGAGCTGCTGGCG
CAGAAGCTGCCGCTGTGGCAACAGGCCTGTGCCGACCCCAGCAAGATCCCGGAGCGCGCG
GTGCAGCTCATGCAGCAGGTGGCCAGCAACGGCGCCACCCTCCCCAGCGCCCTGTCGGCC
TCCAAGTCCAACCTGGTCATTTCCGACCCCATTCCGGGGGCCAAGCCCCTGCCGGTGCCC
CCCGAGCTGGCACCGTTCGTGGGGCGGATGTCTGCCCAGGAGAGCACACCCATCATGAAC
GGCGTCACAGGCCCGGATGGCGAGGACTACAGCCCGTGGGCTGACCGCAAGGCTGCCCAG
CCCAAATCCCTGTCTCCTCCGCAGTCTCAGAGCAAGCTCAGCGACTCCTACTCCAACACA
CTCCCCGTGCGCAAGAGCGTGACCCCAAAAAACAGCTATGCCACCACCGAGAACAAGACT
CTGCCTCGCTCGAGCTCCATGGCAGCCGGCCTGGAGCGCAATGGCCGTATGCGGGTGAAG
GCCATCTTCTCCCACGCTGCTGGGGACAACAGCACCCTCCTGAGCTTCAAGGAGGGTGAC
CTCATTACCCTGCTGGTGCCTGAGGCCCGCGATGGCTGGCACTACGGAGAGAGTGAGAAG
ACCAAGATGCGGGGCTGGTTTCCCTTCTCCTACACCCGGGTCTTGGACAGCGATGGCAGT
GACAGGCTGCACATGAGCCTGCAGCAAGGGAAGAGCAGCAGCACGGGCAACCTCCTGGAC
AAGGACGACCTGGCCATCCCACCCCCCGATTACGGCGCCGCCTCCCGGGCCTTCCCCGCC
CAGACGGCCAGCGGCTTCAAGCAGAGGCCCTACAGTGTGGCCGTGCCCGCCTTCTCCCAG
GGCCTGGATGACTATGGAGCGCGGTCCATGAGCAGGAATCCCTTTGCCCACGTCCAGCTG
AAGCCGACAGTGACCAACGACAGGTGTGATCTGTCCGCCCAAGGGCCAGAAGGCCGGGAG
CACGGGGATGGGAGCGCCCGCACCCTGGCTGGAAGATGA
Protein Properties
Number of Residues 552
Molecular Weight 60867.1
Theoretical pI 9.29
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Brain-specific angiogenesis inhibitor 1-associated protein 2
MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTYAAKGYFDALVKMG
ELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLSAAL
KKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVS
DGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPSKIPERA
VQLMQQVASNGATLPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQESTPIMN
GVTGPDGEDYSPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKT
LPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEK
TKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLAIPPPDYGAASRAFPA
QTASGFKQRPYSVAVPAFSQGLDDYGARSMSRNPFAHVQLKPTVTNDRCDLSAQGPEGRE
HGDGSARTLAGR
GenBank ID Protein 9257199
UniProtKB/Swiss-Prot ID Q9UQB8
UniProtKB/Swiss-Prot Entry Name BAIP2_HUMAN
PDB IDs
GenBank Gene ID NM_017451.2
GeneCard ID BAIAP2
GenAtlas ID BAIAP2
HGNC ID HGNC:947
References
General References
  1. 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 ]
  2. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed:15592455 ]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. 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. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  5. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. doi: 10.1021/pr900044c. [PubMed:19534553 ]
  6. Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM: Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5860-5. Epub 2007 Mar 26. [PubMed:17389395 ]
  7. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. doi: 10.1021/ac801708p. [PubMed:19007248 ]
  8. Miki H, Yamaguchi H, Suetsugu S, Takenawa T: IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature. 2000 Dec 7;408(6813):732-5. [PubMed:11130076 ]
  9. Oda K, Shiratsuchi T, Nishimori H, Inazawa J, Yoshikawa H, Taketani Y, Nakamura Y, Tokino T: Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1. Cytogenet Cell Genet. 1999;84(1-2):75-82. [PubMed:10343108 ]
  10. Okamura-Oho Y, Miyashita T, Ohmi K, Yamada M: Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate. Hum Mol Genet. 1999 Jun;8(6):947-57. [PubMed:10332026 ]
  11. Miyahara A, Okamura-Oho Y, Miyashita T, Hoshika A, Yamada M: Genomic structure and alternative splicing of the insulin receptor tyrosine kinase substrate of 53-kDa protein. J Hum Genet. 2003;48(8):410-4. Epub 2003 Jul 16. [PubMed:12884081 ]
  12. Krugmann S, Jordens I, Gevaert K, Driessens M, Vandekerckhove J, Hall A: Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex. Curr Biol. 2001 Oct 30;11(21):1645-55. [PubMed:11696321 ]
  13. Govind S, Kozma R, Monfries C, Lim L, Ahmed S: Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin. J Cell Biol. 2001 Feb 5;152(3):579-94. [PubMed:11157984 ]
  14. Soltau M, Richter D, Kreienkamp HJ: The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42. Mol Cell Neurosci. 2002 Dec;21(4):575-83. [PubMed:12504591 ]
  15. Funato Y, Terabayashi T, Suenaga N, Seiki M, Takenawa T, Miki H: IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness. Cancer Res. 2004 Aug 1;64(15):5237-44. [PubMed:15289329 ]
  16. Yamagishi A, Masuda M, Ohki T, Onishi H, Mochizuki N: A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein. J Biol Chem. 2004 Apr 9;279(15):14929-36. Epub 2004 Jan 29. [PubMed:14752106 ]
  17. Millard TH, Bompard G, Heung MY, Dafforn TR, Scott DJ, Machesky LM, Futterer K: Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53. EMBO J. 2005 Jan 26;24(2):240-50. Epub 2005 Jan 6. [PubMed:15635447 ]