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Identification
HMDB Protein ID HMDBP10972
Secondary Accession Numbers
  • 17286
Name Rac GTPase-activating protein 1
Synonyms
  1. Male germ cell RacGap
  2. MgcRacGAP
Gene Name RACGAP1
Protein Type Unknown
Biological Properties
General Function Involved in intracellular signaling pathway
Specific Function Essential for the early stages of embryogenesis and may play a role in the microtubule-dependent steps in cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Required for initiation of cleavage furrow ingression by regulating ECT2 and for assembly of the contractile ring. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells
Pathways Not Available
Reactions Not Available
GO Classification
Component
cell part
intracellular
Process
biological regulation
regulation of biological process
regulation of cellular process
signal transduction
intracellular signaling pathway
signaling
signaling pathway
Cellular Location
  1. Nucleus
  2. Cytoplasm
  3. Cytoplasm
  4. Cytoplasmic vesicle
  5. cytoskeleton
  6. secretory vesicle
  7. spindle
  8. acrosome
Gene Properties
Chromosome Location Chromosome:1
Locus 12q13.12
SNPs RACGAP1
Gene Sequence
>1899 bp
ATGGATACTATGATGCTGAATGTGCGGAATCTGTTTGAGCAGCTTGTGCGCCGGGTGGAG
ATTCTCAGTGAAGGAAATGAAGTCCAATTTATCCAGTTGGCGAAGGACTTTGAGGATTTC
CGTAAAAAGTGGCAGAGGACTGACCATGAGCTGGGGAAATACAAGGATCTTTTGATGAAA
GCAGAGACTGAGCGAAGTGCTCTGGATGTTAAGCTGAAGCATGCACGTAATCAGGTGGAT
GTAGAGATCAAACGGAGACAGAGAGCTGAGGCTGACTGCGAAAAGCTGGAACGACAGATT
CAGCTGATTCGAGAGATGCTCATGTGTGACACATCTGGCAGCATTCAACTAAGCGAGGAG
CAAAAATCAGCTCTGGCTTTTCTCAACAGAGGCCAACCATCCAGCAGCAATGCTGGGAAC
AAAAGACTATCAACCATTGATGAATCTGGTTCCATTTTATCAGATATCAGCTTTGACAAG
ACTGATGAATCACTGGATTGGGACTCTTCTTTGGTGAAGACTTTCAAACTGAAGAAGAGA
GAAAAGAGGCGCTCTACTAGCCGACAGTTTGTTGATGGTCCCCCTGGACCTGTAAAGAAA
ACTCGTTCCATTGGCTCTGCAGTAGACCAGGGGAATGAATCCATAGTTGCAAAAACTACA
GTGACTGTTCCCAATGATGGCGGGCCCATCGAAGCTGTGTCCACTATTGAGACTGTGCCA
TATTGGACCAGGAGCCGAAGGAAAACAGGTACTTTACAACCTTGGAACAGTGACTCCACC
CTGAACAGCAGGCAGCTGGAGCCAAGAACTGAGACAGACAGTGTGGGCACGCCACAGAGT
AATGGAGGGATGCGCCTGCATGACTTTGTTTCTAAGACGGTTATTAAACCTGAATCCTGT
GTTCCATGTGGAAAGCGGATAAAATTTGGCAAATTATCTCTGAAGTGTCGAGACTGTCGT
GTGGTCTCTCATCCAGAATGTCGGGACCGCTGTCCCCTTCCCTGCATTCCTACCCTGATA
GGAACACCTGTCAAGATTGGAGAGGGAATGCTGGCAGACTTTGTGTCCCAGACTTCTCCA
ATGATCCCCTCCATTGTTGTGCATTGTGTAAATGAGATTGAGCAAAGAGGTCTGACTGAG
ACAGGCCTGTATAGGATCTCTGGCTGTGACCGCACAGTAAAAGAGCTGAAAGAGAAATTC
CTCAGAGTGAAAACTGTACCCCTCCTCAGCAAAGTGGATGATATCCATGCTATCTGTAGC
CTTCTAAAAGACTTTCTTCGAAACCTCAAAGAACCTCTTCTGACCTTTCGCCTTAACAGA
GCCTTTATGGAAGCAGCAGAAATCACAGATGAAGACAACAGCATAGCTGCCATGTACCAA
GCTGTTGGTGAACTGCCCCAGGCCAACAGGGACACATTAGCTTTCCTCATGATTCACTTG
CAGAGAGTGGCTCAGAGTCCACATACTAAAATGGATGTTGCCAATCTGGCTAAAGTCTTT
GGCCCTACAATAGTGGCCCATGCTGTGCCCAATCCAGACCCAGTGACAATGTCACAGGAC
ATCAAGCGTCAACCCAAGGTGGTTGAGCGCCTGCTTTCCTTGCCTCTGGAGTATTGGAGT
CAGTTCATGATGGTGGAGCAAGAGAACATTGACCCCCTACATGTCATTGAAAACTCAAAT
GCCTTTTCAACACCACAGACACCAGATATTAAAGTGAGTTTACTGGGACCTGTGACCACT
CCTGAACATCAGCTTCTCAAGACTCCTTCATCTAGTTCCCTGTCACAGAGAGTCCGTTCC
ACCCTCACCAAGAACACTCCTAGATTTGGGAGCAAAAGCAAGTCTGCCACTAACCTAGGA
CGACAAGGCAACTTTTTTGCTTCTCCAATGCTCAAGTGA
Protein Properties
Number of Residues 632
Molecular Weight 71025.9
Theoretical pI 9.26
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Rac GTPase-activating protein 1
MDTMMLNVRNLFEQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMK
AETERSALDVKLKHARNQVDVEIKRRQRAEADCEKLERQIQLIREMLMCDTSGSIQLSEE
QKSALAFLNRGQPSSSNAGNKRLSTIDESGSILSDISFDKTDESLDWDSSLVKTFKLKKR
EKRRSTSRQFVDGPPGPVKKTRSIGSAVDQGNESIVAKTTVTVPNDGGPIEAVSTIETVP
YWTRSRRKTGTLQPWNSDSTLNSRQLEPRTETDSVGTPQSNGGMRLHDFVSKTVIKPESC
VPCGKRIKFGKLSLKCRDCRVVSHPECRDRCPLPCIPTLIGTPVKIGEGMLADFVSQTSP
MIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDDIHAICS
LLKDFLRNLKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHL
QRVAQSPHTKMDVANLAKVFGPTIVAHAVPNPDPVTMLQDIKRQPKVVERLLSLPLEYWS
QFMMVEQENIDPLHVIENSNAFSTPQTPDIKVSLLGPVTTPEHQLLKTPSSSSLSQRVRS
TLTKNTPRFGSKSKSATNLGRQGNFFASPMLK
GenBank ID Protein 6759255
UniProtKB/Swiss-Prot ID Q9H0H5
UniProtKB/Swiss-Prot Entry Name RGAP1_HUMAN
PDB IDs Not Available
GenBank Gene ID AB030251
GeneCard ID RACGAP1
GenAtlas ID RACGAP1
HGNC ID HGNC:9804
References
General References
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  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. 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. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  5. 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. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
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  7. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
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  10. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed:17287340 ]
  11. 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 ]
  12. Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed:10819331 ]
  13. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [PubMed:16565220 ]
  14. Minoshima Y, Kawashima T, Hirose K, Tonozuka Y, Kawajiri A, Bao YC, Deng X, Tatsuka M, Narumiya S, May WS Jr, Nosaka T, Semba K, Inoue T, Satoh T, Inagaki M, Kitamura T: Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP during cytokinesis. Dev Cell. 2003 Apr;4(4):549-60. [PubMed:12689593 ]
  15. Toure A, Morin L, Pineau C, Becq F, Dorseuil O, Gacon G: Tat1, a novel sulfate transporter specifically expressed in human male germ cells and potentially linked to rhogtpase signaling. J Biol Chem. 2001 Jun 8;276(23):20309-15. Epub 2001 Mar 5. [PubMed:11278976 ]
  16. Kawashima T, Hirose K, Satoh T, Kaneko A, Ikeda Y, Kaziro Y, Nosaka T, Kitamura T: MgcRacGAP is involved in the control of growth and differentiation of hematopoietic cells. Blood. 2000 Sep 15;96(6):2116-24. [PubMed:10979956 ]
  17. Toure A, Dorseuil O, Morin L, Timmons P, Jegou B, Reibel L, Gacon G: MgcRacGAP, a new human GTPase-activating protein for Rac and Cdc42 similar to Drosophila rotundRacGAP gene product, is expressed in male germ cells. J Biol Chem. 1998 Mar 13;273(11):6019-23. [PubMed:9497316 ]
  18. Hirose K, Kawashima T, Iwamoto I, Nosaka T, Kitamura T: MgcRacGAP is involved in cytokinesis through associating with mitotic spindle and midbody. J Biol Chem. 2001 Feb 23;276(8):5821-8. Epub 2000 Nov 20. [PubMed:11085985 ]
  19. Naud N, Toure A, Liu J, Pineau C, Morin L, Dorseuil O, Escalier D, Chardin P, Gacon G: Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells. Biochem J. 2003 May 15;372(Pt 1):105-12. [PubMed:12590651 ]
  20. Lee JS, Kamijo K, Ohara N, Kitamura T, Miki T: MgcRacGAP regulates cortical activity through RhoA during cytokinesis. Exp Cell Res. 2004 Feb 15;293(2):275-82. [PubMed:14729465 ]
  21. Ban R, Irino Y, Fukami K, Tanaka H: Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP activity toward Cdc42 during the metaphase. J Biol Chem. 2004 Apr 16;279(16):16394-402. Epub 2004 Jan 26. [PubMed:14744859 ]
  22. Zhao WM, Fang G: MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis. Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13158-63. Epub 2005 Aug 29. [PubMed:16129829 ]
  23. Simon GC, Schonteich E, Wu CC, Piekny A, Ekiert D, Yu X, Gould GW, Glotzer M, Prekeris R: Sequential Cyk-4 binding to ECT2 and FIP3 regulates cleavage furrow ingression and abscission during cytokinesis. EMBO J. 2008 Jul 9;27(13):1791-803. doi: 10.1038/emboj.2008.112. Epub 2008 May 29. [PubMed:18511905 ]