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Q9H0H5 (RGAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rac GTPase-activating protein 1
Alternative name(s):
Male germ cell RacGap
Short name=MgcRacGAP
Protein CYK4 homolog
Short name=CYK4
Short name=HsCYK-4
Gene names
Name:RACGAP1
Synonyms:KIAA1478, MGCRACGAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length632 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during 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. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19 Ref.23 Ref.24 Ref.30

Subunit structure

Heterotetramer of two molecules each of RACGAP1 and KIF23. Found in the centralspindlin complex composed of RACGAP1 and KIF23. Associates with alpha-, beta- and gamma-tubulin and microtubules. Interacts via its Rho-GAP domain with RND2. Associates with AURKB during M phase. Interacts via its Rho-GAP domain and basic region with PRC1. The interaction with PRC1 inhibits its GAP activity towards CDC42 in vitro, which may be required for maintaining normal spindle morphology. Interacts with SLC26A8 via its N-terminus. Interacts with RAB11FIP3. Interacts with ECT2; the interaction is direct, occurs at anaphase and during cytokinesis in a microtubule-dependent manner and is enhanced by phosphorylation by PLK1. Interacts with KIF23; the interaction is direct. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.19 Ref.21 Ref.24 Ref.30

Subcellular location

Nucleus. Cytoplasm. Cytoplasmcytoskeletonspindle. Cytoplasmic vesiclesecretory vesicleacrosome. Cleavage furrow. Midbody. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Colocalizes with RND2 in Golgi-derived proacrosomal vesicles and the acrosome By similarity. During interphase, localized to the nucleus and cytoplasm along with microtubules, in anaphase, is redistributed to the central spindle and, in telophase and cytokinesis, to the midbody. Colocalizes with RHOA at the myosin contractile ring during cytokinesis. Colocalizes with ECT2 to the mitotic spindles during anaphase/metaphase, the cleavage furrow during telophase and at the midbody at the end of cytokinesis. Colocalizes with Cdc42 to spindle microtubules from prometaphase to telophase. Ref.8 Ref.11 Ref.15 Ref.16 Ref.17 Ref.19 Ref.23 Ref.24 Ref.30

Tissue specificity

Highly expressed in testis, thymus and placenta. Expressed at lower levels in spleen and peripheral blood lymphocytes. In testis, expression is restricted to germ cells with the highest levels of expression found in spermatocytes. Expression is regulated in a cell cycle-dependent manner and peaks during G2/M phase. Ref.1 Ref.7 Ref.9 Ref.11

Induction

Expression is down-regulated during macrophage differention of HL-60 cells. Ref.1

Domain

The coiled coil region is indispensible for localization to the midbody during cytokinesis. Ref.8 Ref.30

The phorbol-ester/DAG-type zinc finger domain mediates interaction with membranes enriched in phosphatidylinositol 3,4,5-trisphosphate and is required during mitotic cytokinesis for normal attachment of the midbody to the cell membrane. Ref.8 Ref.30

Post-translational modification

Phosphorylated at multiple sites in the midbody during cytokinesis. Phosphorylation by AURKB on Ser-387 at the midbody is, at least in part, responsible for exerting its latent GAP activity towards RhoA. Phosphorylation on multiple serine residues by PLK1 enhances its association with ECT2 and is critical for cleavage furrow formation. Ref.12 Ref.23 Ref.24

Sequence similarities

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 Rho-GAP domain.

Sequence caution

The sequence AAH24144.1 differs from that shown. Reason: Frameshift at positions 171, 205 and 437.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Differentiation
Ion transport
Spermatogenesis
Transport
   Cellular componentCell membrane
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Membrane
Microtubule
Nucleus
   DomainCoiled coil
Zinc-finger
   LigandLipid-binding
Metal-binding
Zinc
   Molecular functionDevelopmental protein
GTPase activation
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactomyosin contractile ring assembly

Inferred from mutant phenotype Ref.17. Source: UniProtKB

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cytokinesis, initiation of separation

Inferred from mutant phenotype Ref.17. Source: UniProtKB

embryo development

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule-based movement

Traceable author statement. Source: Reactome

mitotic cytokinesis

Inferred from direct assay Ref.8Ref.23. Source: UniProtKB

neuroblast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of GTPase activity

Inferred from direct assay Ref.1. Source: GOC

positive regulation of cytokinesis

Inferred from direct assay Ref.16. Source: UniProtKB

regulation of attachment of spindle microtubules to kinetochore

Inferred from mutant phenotype Ref.15. Source: UniProtKB

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

spermatogenesis

Inferred from expression pattern Ref.11. Source: UniProtKB

spindle midzone assembly involved in mitosis

Inferred from direct assay Ref.16. Source: UniProtKB

sulfate transport

Inferred from direct assay Ref.9. Source: UniProtKB

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

centralspindlin complex

Inferred from direct assay Ref.10Ref.19. Source: UniProtKB

cleavage furrow

Inferred from direct assay Ref.16. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

extrinsic component of cytoplasmic side of plasma membrane

Inferred from direct assay Ref.30. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

midbody

Inferred from direct assay Ref.10Ref.16Ref.21. Source: UniProtKB

mitotic spindle

Inferred from direct assay Ref.16. Source: UniProtKB

nucleus

Inferred from direct assay Ref.8Ref.10Ref.16. Source: UniProtKB

spindle midzone

Inferred from direct assay Ref.23. Source: UniProtKB

   Molecular_functionGTPase activator activity

Inferred from direct assay Ref.1. Source: UniProtKB

alpha-tubulin binding

Inferred from direct assay Ref.8. Source: UniProtKB

beta-tubulin binding

Inferred from direct assay Ref.8. Source: UniProtKB

gamma-tubulin binding

Inferred from direct assay Ref.8. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule binding

Inferred from direct assay Ref.10. Source: UniProtKB

phosphatidylinositol-3,4,5-trisphosphate binding

Inferred from direct assay Ref.30. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.23. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 632632Rac GTPase-activating protein 1
PRO_0000228808

Regions

Domain349 – 539191Rho-GAP
Zinc finger286 – 33550Phorbol-ester/DAG-type
Region106 – 285180Interaction with SLC26A8
Coiled coil53 – 11058 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.29
Modified residue1491Phosphoserine; by PLK1 Ref.24
Modified residue1541Phosphoserine Ref.25 Ref.26 Ref.28
Modified residue1571Phosphoserine; by PLK1 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28
Modified residue1611Phosphothreonine Ref.18
Modified residue1641Phosphoserine; by PLK1 Ref.18 Ref.23 Ref.24
Modified residue1701Phosphoserine; by PLK1 Ref.23 Ref.24
Modified residue2031Phosphoserine Ref.18 Ref.20 Ref.22 Ref.25 Ref.26
Modified residue2061Phosphoserine Ref.22 Ref.25
Modified residue2141Phosphoserine Ref.23
Modified residue2571Phosphoserine Ref.22
Modified residue2601Phosphothreonine Ref.23
Modified residue3421Phosphothreonine Ref.22 Ref.26
Modified residue3871Phosphoserine; by AURKB Ref.12
Modified residue4101Phosphoserine; by AURKB Ref.12
Modified residue5671Phosphothreonine Ref.26
Modified residue5801Phosphothreonine Ref.22
Modified residue5881Phosphothreonine Ref.20 Ref.22 Ref.26
Modified residue6001Phosphoserine Ref.22
Modified residue6011Phosphothreonine Ref.22
Modified residue6061Phosphothreonine Ref.22

Experimental info

Mutagenesis1491S → A: Does not inhibit interaction with ECT2. Reduces strongly phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-170. Ref.24
Mutagenesis1571S → A: Does not inhibit interaction with ECT2. Reduces strongly phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-164 and A-170. Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-164; A-170 and A-214. Ref.23 Ref.24
Mutagenesis1641S → A: Does not inhibit interaction with ECT2. Reduces strongly phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-157 and A-170. Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-170 and A-214. Ref.23 Ref.24
Mutagenesis1701S → A: Does not inhibit interaction with ECT2. Reduces strongly phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-157 and A-164. Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-214. Ref.23 Ref.24
Mutagenesis2141S → A: Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-170. Ref.23
Mutagenesis2891F → G: Cytokinesis failure. Ref.30
Mutagenesis2921K → L: Cytokinesis failure. Abolishes localization at the cell membrane. Ref.30
Mutagenesis3061R → L: Cytokinesis failure. Abolishes localization at the cell membrane. Ref.30
Mutagenesis3091F → A: Cytokinesis failure. Abolishes localization at the cell membrane. Ref.30
Mutagenesis3161C → G: Cytokinesis failure. Ref.30
Mutagenesis3851R → A: Abolishes GAP activity towards RAC1. Abolishes GAP activity towards CDC42 in prometaphase. Induces multiple blebs during cytokinesis. Ref.1 Ref.13 Ref.15
Sequence conflict1551D → H in BAA91347. Ref.3
Sequence conflict5181L → S in BAA90247. Ref.1

Secondary structure

.......................................... 632
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H0H5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 032B7DF9CEA8F39D

FASTA63271,027
        10         20         30         40         50         60 
MDTMMLNVRN LFEQLVRRVE ILSEGNEVQF IQLAKDFEDF RKKWQRTDHE LGKYKDLLMK 

        70         80         90        100        110        120 
AETERSALDV KLKHARNQVD VEIKRRQRAE ADCEKLERQI QLIREMLMCD TSGSIQLSEE 

       130        140        150        160        170        180 
QKSALAFLNR GQPSSSNAGN KRLSTIDESG SILSDISFDK TDESLDWDSS LVKTFKLKKR 

       190        200        210        220        230        240 
EKRRSTSRQF VDGPPGPVKK TRSIGSAVDQ GNESIVAKTT VTVPNDGGPI EAVSTIETVP 

       250        260        270        280        290        300 
YWTRSRRKTG TLQPWNSDST LNSRQLEPRT ETDSVGTPQS NGGMRLHDFV SKTVIKPESC 

       310        320        330        340        350        360 
VPCGKRIKFG KLSLKCRDCR VVSHPECRDR CPLPCIPTLI GTPVKIGEGM LADFVSQTSP 

       370        380        390        400        410        420 
MIPSIVVHCV NEIEQRGLTE TGLYRISGCD RTVKELKEKF LRVKTVPLLS KVDDIHAICS 

       430        440        450        460        470        480 
LLKDFLRNLK EPLLTFRLNR AFMEAAEITD EDNSIAAMYQ AVGELPQANR DTLAFLMIHL 

       490        500        510        520        530        540 
QRVAQSPHTK MDVANLAKVF GPTIVAHAVP NPDPVTMLQD IKRQPKVVER LLSLPLEYWS 

       550        560        570        580        590        600 
QFMMVEQENI DPLHVIENSN AFSTPQTPDI KVSLLGPVTT PEHQLLKTPS SSSLSQRVRS 

       610        620        630 
TLTKNTPRFG SKSKSATNLG RQGNFFASPM LK 

« Hide

References

« Hide 'large scale' references
[1]"MgcRacGAP is involved in the control of growth and differentiation of hematopoietic cells."
Kawashima T., Hirose K., Satoh T., Kaneko A., Ikeda Y., Kaziro Y., Nosaka T., Kitamura T.
Blood 96:2116-2124(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-385, INDUCTION.
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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 T.-O., 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hepatoma.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta and Testis.
[6]"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."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-632.
Tissue: Brain.
[7]"MgcRacGAP, a new human GTPase-activating protein for Rac and Cdc42 similar to Drosophila rotundRacGAP gene product, is expressed in male germ cells."
Toure A., Dorseuil O., Morin L., Timmons P., Jegou B., Reibel L., Gacon G.
J. Biol. Chem. 273:6019-6023(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-632, FUNCTION, TISSUE SPECIFICITY.
Tissue: Placenta.
[8]"MgcRacGAP is involved in cytokinesis through associating with mitotic spindle and midbody."
Hirose K., Kawashima T., Iwamoto I., Nosaka T., Kitamura T.
J. Biol. Chem. 276:5821-5828(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN.
[9]"Tat1, a novel sulfate transporter specifically expressed in human male germ cells and potentially linked to rhogtpase signaling."
Toure A., Morin L., Pineau C., Becq F., Dorseuil O., Gacon G.
J. Biol. Chem. 276:20309-20315(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SLC26A8, TISSUE SPECIFICITY.
[10]"Central spindle assembly and cytokinesis require a kinesin-like protein/RhoGAP complex with microtubule bundling activity."
Mishima M., Kaitna S., Glotzer M.
Dev. Cell 2:41-54(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, ASSOCIATION TO MICROTUBULES, INTERACTION WITH KIF23.
[11]"Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells."
Naud N., Toure A., Liu J., Pineau C., Morin L., Dorseuil O., Escalier D., Chardin P., Gacon G.
Biochem. J. 372:105-112(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RND2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]"Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP during cytokinesis."
Minoshima Y., Kawashima T., Hirose K., Tonozuka Y., Kawajiri A., Bao Y.C., Deng X., Tatsuka M., Narumiya S., May W.S. Jr., Nosaka T., Semba K., Inoue T., Satoh T., Inagaki M., Kitamura T.
Dev. Cell 4:549-560(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AURKB, PHOSPHORYLATION AT SER-387 AND SER-410.
[13]"MgcRacGAP regulates cortical activity through RhoA during cytokinesis."
Lee J.S., Kamijo K., Ohara N., Kitamura T., Miki T.
Exp. Cell Res. 293:275-282(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-385.
[14]"Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP activity toward Cdc42 during the metaphase."
Ban R., Irino Y., Fukami K., Tanaka H.
J. Biol. Chem. 279:16394-16402(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRC1.
[15]"Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in mitosis."
Oceguera-Yanez F., Kimura K., Yasuda S., Higashida C., Kitamura T., Hiraoka Y., Haraguchi T., Narumiya S.
J. Cell Biol. 168:221-232(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-385.
[16]"An ECT2-centralspindlin complex regulates the localization and function of RhoA."
Yuce O., Piekny A., Glotzer M.
J. Cell Biol. 170:571-582(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ECT2 AND KIF23, SUBCELLULAR LOCATION.
[17]"MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis."
Zhao W.-M., Fang G.
Proc. Natl. Acad. Sci. U.S.A. 102:13158-13163(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ECT2, SUBCELLULAR LOCATION.
[18]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161; SER-164 AND SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Dissecting the role of Rho-mediated signaling in contractile ring formation."
Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T.
Mol. Biol. Cell 17:43-55(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, INTERACTION WITH ECT2 AND KIF23, SUBCELLULAR LOCATION.
[20]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Sequential Cyk-4 binding to ECT2 and FIP3 regulates cleavage furrow ingression and abscission during cytokinesis."
Simon G.C., Schonteich E., Wu C.C., Piekny A., Ekiert D., Yu X., Gould G.W., Glotzer M., Prekeris R.
EMBO J. 27:1791-1803(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP3.
[22]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-206; SER-257; THR-342; THR-580; THR-588; SER-600; THR-601 AND THR-606, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Plk1 self-organization and priming phosphorylation of HsCYK-4 at the spindle midzone regulate the onset of division in human cells."
Burkard M.E., Maciejowski J., Rodriguez-Bravo V., Repka M., Lowery D.M., Clauser K.R., Zhang C., Shokat K.M., Carr S.A., Yaffe M.B., Jallepalli P.V.
PLoS Biol. 7:E1000111-E1000111(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-157; SER-164; SER-170; SER-214 AND THR-260, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-157; SER-164; SER-170 AND SER-214.
[24]"Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation."
Wolfe B.A., Takaki T., Petronczki M., Glotzer M.
PLoS Biol. 7:E1000110-E1000110(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ECT2, PHOSPHORYLATION AT SER-149; SER-157; SER-164 AND SER-170, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-149; SER-157; SER-164 AND SER-170.
[25]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-157; SER-203 AND SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[26]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-157; SER-203; THR-342; THR-567 AND THR-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"Centralspindlin links the mitotic spindle to the plasma membrane during cytokinesis."
Lekomtsev S., Su K.C., Pye V.E., Blight K., Sundaramoorthy S., Takaki T., Collinson L.M., Cherepanov P., Divecha N., Petronczki M.
Nature 492:276-279(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 284-339 IN COMPLEX WITH ZINC IONS, FUNCTION, INTERACTION WITH KIF23, DOMAIN, LIPID-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-289; LYS-292; ARG-306; PHE-309 AND CYS-316.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB030251 mRNA. Translation: BAA90247.1.
AL136794 mRNA. Translation: CAB66728.1.
AK000733 mRNA. Translation: BAA91347.1.
CR533565 mRNA. Translation: CAG38596.1.
BC024144 mRNA. Translation: AAH24144.1. Frameshift.
BC032754 mRNA. Translation: AAH32754.1.
AB040911 mRNA. Translation: BAA96002.1.
PIRD59430.
RefSeqNP_001119575.1. NM_001126103.1.
NP_001119576.1. NM_001126104.1.
NP_037409.2. NM_013277.3.
XP_005268869.1. XM_005268812.1.
XP_005268870.1. XM_005268813.1.
XP_005268871.1. XM_005268814.1.
XP_005268872.1. XM_005268815.1.
XP_005268873.1. XM_005268816.1.
UniGeneHs.505469.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OVJX-ray1.49A348-546[»]
3W6RX-ray1.90A348-546[»]
4B6DX-ray2.20A/B/C/D/E/F284-339[»]
ProteinModelPortalQ9H0H5.
SMRQ9H0H5. Positions 282-546.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118892. 26 interactions.
DIPDIP-33087N.
IntActQ9H0H5. 24 interactions.
MINTMINT-256435.
STRING9606.ENSP00000309871.

Chemistry

ChEMBLCHEMBL2146306.

PTM databases

PhosphoSiteQ9H0H5.

Polymorphism databases

DMDM74762727.

Proteomic databases

PaxDbQ9H0H5.
PeptideAtlasQ9H0H5.
PRIDEQ9H0H5.

Protocols and materials databases

DNASU29127.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312377; ENSP00000309871; ENSG00000161800.
ENST00000427314; ENSP00000404190; ENSG00000161800.
ENST00000434422; ENSP00000413241; ENSG00000161800.
ENST00000454520; ENSP00000404808; ENSG00000161800.
ENST00000547905; ENSP00000449370; ENSG00000161800.
ENST00000551016; ENSP00000449374; ENSG00000161800.
GeneID29127.
KEGGhsa:29127.
UCSCuc001rvs.2. human.

Organism-specific databases

CTD29127.
GeneCardsGC12M050370.
H-InvDBHIX0036723.
HGNCHGNC:9804. RACGAP1.
HPACAB025859.
HPA039427.
HPA043912.
MIM604980. gene.
neXtProtNX_Q9H0H5.
PharmGKBPA34165.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG305341.
HOGENOMHOG000230702.
HOVERGENHBG062009.
InParanoidQ9H0H5.
KOK16733.
OMAGKISLKC.
OrthoDBEOG7K0ZBT.
PhylomeDBQ9H0H5.
TreeFamTF318102.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9H0H5.
BgeeQ9H0H5.
CleanExHS_RACGAP1.
GenevestigatorQ9H0H5.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
InterProIPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamPF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTSM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
PROSITEPS50238. RHOGAP. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9H0H5.
GeneWikiRACGAP1.
GenomeRNAi29127.
NextBio52240.
PMAP-CutDBQ9H0H5.
PROQ9H0H5.
SOURCESearch...

Entry information

Entry nameRGAP1_HUMAN
AccessionPrimary (citable) accession number: Q9H0H5
Secondary accession number(s): Q6PJ26 expand/collapse secondary AC list , Q9NWN2, Q9P250, Q9P2W2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM