Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9H0H5

- RGAP1_HUMAN

UniProt

Q9H0H5 - RGAP1_HUMAN

Protein

Rac GTPase-activating protein 1

Gene

RACGAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.13 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri286 – 33550Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. alpha-tubulin binding Source: UniProtKB
    2. beta-tubulin binding Source: UniProtKB
    3. gamma-tubulin binding Source: UniProtKB
    4. GTPase activator activity Source: UniProtKB
    5. metal ion binding Source: UniProtKB-KW
    6. microtubule binding Source: UniProtKB
    7. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. actomyosin contractile ring assembly Source: UniProtKB
    2. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    3. blood coagulation Source: Reactome
    4. cytokinesis, initiation of separation Source: UniProtKB
    5. embryo development Source: UniProtKB
    6. microtubule-based movement Source: Reactome
    7. mitotic cytokinesis Source: UniProtKB
    8. neuroblast proliferation Source: UniProtKB
    9. positive regulation of cytokinesis Source: UniProtKB
    10. positive regulation of GTPase activity Source: GOC
    11. regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
    12. regulation of small GTPase mediated signal transduction Source: Reactome
    13. small GTPase mediated signal transduction Source: Reactome
    14. spermatogenesis Source: UniProtKB
    15. spindle midzone assembly involved in mitosis Source: UniProtKB
    16. sulfate transport Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, GTPase activation

    Keywords - Biological processi

    Cell cycle, Cell division, Differentiation, Ion transport, Spermatogenesis, Transport

    Keywords - Ligandi

    Lipid-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_121399. MHC class II antigen presentation.
    REACT_25201. Kinesins.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:RACGAP1Imported
    Synonyms:KIAA1478Imported, MGCRACGAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9804. RACGAP1.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. acrosomal vesicle Source: UniProtKB-SubCell
    2. centralspindlin complex Source: UniProtKB
    3. cleavage furrow Source: UniProtKB
    4. cytosol Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    7. microtubule Source: UniProtKB-KW
    8. midbody Source: UniProtKB
    9. mitotic spindle Source: UniProtKB
    10. nucleus Source: UniProtKB
    11. spindle midzone Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Microtubule, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi149 – 1491S → 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. 1 Publication
    Mutagenesisi157 – 1571S → 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. 2 Publications
    Mutagenesisi164 – 1641S → 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. 2 Publications
    Mutagenesisi170 – 1701S → 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. 2 Publications
    Mutagenesisi214 – 2141S → A: Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-170. 1 Publication
    Mutagenesisi289 – 2891F → G: Cytokinesis failure. 1 Publication
    Mutagenesisi292 – 2921K → L: Cytokinesis failure. Abolishes localization at the cell membrane. 1 Publication
    Mutagenesisi306 – 3061R → L: Cytokinesis failure. Abolishes localization at the cell membrane. 1 Publication
    Mutagenesisi309 – 3091F → A: Cytokinesis failure. Abolishes localization at the cell membrane. 1 Publication
    Mutagenesisi316 – 3161C → G: Cytokinesis failure. 1 Publication
    Mutagenesisi385 – 3851R → A: Abolishes GAP activity towards RAC1. Abolishes GAP activity towards CDC42 in prometaphase. Induces multiple blebs during cytokinesis. 3 Publications

    Organism-specific databases

    PharmGKBiPA34165.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 632632Rac GTPase-activating protein 1PRO_0000228808Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei149 – 1491Phosphoserine; by PLK11 Publication
    Modified residuei154 – 1541Phosphoserine3 Publications
    Modified residuei157 – 1571Phosphoserine; by PLK15 Publications
    Modified residuei161 – 1611Phosphothreonine1 Publication
    Modified residuei164 – 1641Phosphoserine; by PLK13 Publications
    Modified residuei170 – 1701Phosphoserine; by PLK12 Publications
    Modified residuei203 – 2031Phosphoserine5 Publications
    Modified residuei206 – 2061Phosphoserine2 Publications
    Modified residuei214 – 2141Phosphoserine1 Publication
    Modified residuei257 – 2571Phosphoserine1 Publication
    Modified residuei260 – 2601Phosphothreonine1 Publication
    Modified residuei342 – 3421Phosphothreonine2 Publications
    Modified residuei387 – 3871Phosphoserine; by AURKB1 Publication
    Modified residuei410 – 4101Phosphoserine; by AURKB1 Publication
    Modified residuei567 – 5671Phosphothreonine1 Publication
    Modified residuei580 – 5801Phosphothreonine1 Publication
    Modified residuei588 – 5881Phosphothreonine3 Publications
    Modified residuei600 – 6001Phosphoserine1 Publication
    Modified residuei601 – 6011Phosphothreonine1 Publication
    Modified residuei606 – 6061Phosphothreonine1 Publication

    Post-translational modificationi

    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.9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H0H5.
    PaxDbiQ9H0H5.
    PeptideAtlasiQ9H0H5.
    PRIDEiQ9H0H5.

    PTM databases

    PhosphoSiteiQ9H0H5.

    Miscellaneous databases

    PMAP-CutDBQ9H0H5.

    Expressioni

    Tissue specificityi

    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.4 Publications

    Inductioni

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

    Gene expression databases

    ArrayExpressiQ9H0H5.
    BgeeiQ9H0H5.
    CleanExiHS_RACGAP1.
    GenevestigatoriQ9H0H5.

    Organism-specific databases

    HPAiCAB025859.
    HPA039427.
    HPA043912.

    Interactioni

    Subunit structurei

    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.12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KIF23Q022414EBI-717233,EBI-306852
    PPP2R5EQ165375EBI-717233,EBI-968374
    RAB11FIP3O751547EBI-717233,EBI-7942186
    SLC26A8Q96RN12EBI-717233,EBI-1792052

    Protein-protein interaction databases

    BioGridi118892. 27 interactions.
    DIPiDIP-33087N.
    IntActiQ9H0H5. 24 interactions.
    MINTiMINT-256435.
    STRINGi9606.ENSP00000309871.

    Structurei

    Secondary structure

    1
    632
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi289 – 2935
    Turni301 – 3033
    Beta strandi312 – 3209
    Helixi325 – 3306
    Helixi351 – 3544
    Beta strandi357 – 3604
    Helixi364 – 37613
    Turni377 – 3793
    Turni381 – 3855
    Helixi390 – 40112
    Helixi409 – 4113
    Helixi415 – 42713
    Beta strandi429 – 4313
    Turni436 – 4383
    Helixi439 – 4479
    Helixi451 – 46313
    Helixi467 – 48519
    Turni487 – 4893
    Helixi493 – 50412
    Beta strandi508 – 5114
    Helixi514 – 53320
    Helixi536 – 5405
    Helixi541 – 5433

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OVJX-ray1.49A348-546[»]
    3W6RX-ray1.90A348-546[»]
    4B6DX-ray2.20A/B/C/D/E/F284-339[»]
    ProteinModelPortaliQ9H0H5.
    SMRiQ9H0H5. Positions 282-546.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H0H5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini349 – 539191Rho-GAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni106 – 285180Interaction with SLC26A8Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili53 – 11058Sequence AnalysisAdd
    BLAST

    Domaini

    The coiled coil region is indispensible for localization to the midbody during cytokinesis.1 Publication
    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.

    Sequence similaritiesi

    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri286 – 33550Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG305341.
    HOGENOMiHOG000230702.
    HOVERGENiHBG062009.
    InParanoidiQ9H0H5.
    KOiK16733.
    OMAiGKISLKC.
    OrthoDBiEOG7K0ZBT.
    PhylomeDBiQ9H0H5.
    TreeFamiTF318102.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    InterProiIPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view]
    PfamiPF00130. C1_1. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view]
    SMARTiSM00109. C1. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    PROSITEiPS50238. RHOGAP. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9H0H5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDTMMLNVRN LFEQLVRRVE ILSEGNEVQF IQLAKDFEDF RKKWQRTDHE    50
    LGKYKDLLMK AETERSALDV KLKHARNQVD VEIKRRQRAE ADCEKLERQI 100
    QLIREMLMCD TSGSIQLSEE QKSALAFLNR GQPSSSNAGN KRLSTIDESG 150
    SILSDISFDK TDESLDWDSS LVKTFKLKKR EKRRSTSRQF VDGPPGPVKK 200
    TRSIGSAVDQ GNESIVAKTT VTVPNDGGPI EAVSTIETVP YWTRSRRKTG 250
    TLQPWNSDST LNSRQLEPRT ETDSVGTPQS NGGMRLHDFV SKTVIKPESC 300
    VPCGKRIKFG KLSLKCRDCR VVSHPECRDR CPLPCIPTLI GTPVKIGEGM 350
    LADFVSQTSP MIPSIVVHCV NEIEQRGLTE TGLYRISGCD RTVKELKEKF 400
    LRVKTVPLLS KVDDIHAICS LLKDFLRNLK EPLLTFRLNR AFMEAAEITD 450
    EDNSIAAMYQ AVGELPQANR DTLAFLMIHL QRVAQSPHTK MDVANLAKVF 500
    GPTIVAHAVP NPDPVTMLQD IKRQPKVVER LLSLPLEYWS QFMMVEQENI 550
    DPLHVIENSN AFSTPQTPDI KVSLLGPVTT PEHQLLKTPS SSSLSQRVRS 600
    TLTKNTPRFG SKSKSATNLG RQGNFFASPM LK 632
    Length:632
    Mass (Da):71,027
    Last modified:March 1, 2001 - v1
    Checksum:i032B7DF9CEA8F39D
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti155 – 1551D → H in BAA91347. (PubMed:14702039)Curated
    Sequence conflicti518 – 5181L → S in BAA90247. (PubMed:10979956)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS8795.1.
    PIRiD59430.
    RefSeqiNP_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.
    XP_006719422.1. XM_006719359.1.
    XP_006719423.1. XM_006719360.1.
    UniGeneiHs.505469.

    Genome annotation databases

    EnsembliENST00000312377; ENSP00000309871; ENSG00000161800.
    ENST00000427314; ENSP00000404190; ENSG00000161800.
    ENST00000454520; ENSP00000404808; ENSG00000161800.
    ENST00000547905; ENSP00000449370; ENSG00000161800.
    ENST00000551016; ENSP00000449374; ENSG00000161800.
    GeneIDi29127.
    KEGGihsa:29127.
    UCSCiuc001rvs.2. human.

    Polymorphism databases

    DMDMi74762727.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS8795.1.
    PIRi D59430.
    RefSeqi NP_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.
    XP_006719422.1. XM_006719359.1.
    XP_006719423.1. XM_006719360.1.
    UniGenei Hs.505469.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OVJ X-ray 1.49 A 348-546 [» ]
    3W6R X-ray 1.90 A 348-546 [» ]
    4B6D X-ray 2.20 A/B/C/D/E/F 284-339 [» ]
    ProteinModelPortali Q9H0H5.
    SMRi Q9H0H5. Positions 282-546.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118892. 27 interactions.
    DIPi DIP-33087N.
    IntActi Q9H0H5. 24 interactions.
    MINTi MINT-256435.
    STRINGi 9606.ENSP00000309871.

    Chemistry

    ChEMBLi CHEMBL2146306.

    PTM databases

    PhosphoSitei Q9H0H5.

    Polymorphism databases

    DMDMi 74762727.

    Proteomic databases

    MaxQBi Q9H0H5.
    PaxDbi Q9H0H5.
    PeptideAtlasi Q9H0H5.
    PRIDEi Q9H0H5.

    Protocols and materials databases

    DNASUi 29127.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312377 ; ENSP00000309871 ; ENSG00000161800 .
    ENST00000427314 ; ENSP00000404190 ; ENSG00000161800 .
    ENST00000454520 ; ENSP00000404808 ; ENSG00000161800 .
    ENST00000547905 ; ENSP00000449370 ; ENSG00000161800 .
    ENST00000551016 ; ENSP00000449374 ; ENSG00000161800 .
    GeneIDi 29127.
    KEGGi hsa:29127.
    UCSCi uc001rvs.2. human.

    Organism-specific databases

    CTDi 29127.
    GeneCardsi GC12M050370.
    H-InvDB HIX0036723.
    HGNCi HGNC:9804. RACGAP1.
    HPAi CAB025859.
    HPA039427.
    HPA043912.
    MIMi 604980. gene.
    neXtProti NX_Q9H0H5.
    PharmGKBi PA34165.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG305341.
    HOGENOMi HOG000230702.
    HOVERGENi HBG062009.
    InParanoidi Q9H0H5.
    KOi K16733.
    OMAi GKISLKC.
    OrthoDBi EOG7K0ZBT.
    PhylomeDBi Q9H0H5.
    TreeFami TF318102.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_121399. MHC class II antigen presentation.
    REACT_25201. Kinesins.

    Miscellaneous databases

    EvolutionaryTracei Q9H0H5.
    GeneWikii RACGAP1.
    GenomeRNAii 29127.
    NextBioi 52240.
    PMAP-CutDB Q9H0H5.
    PROi Q9H0H5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H0H5.
    Bgeei Q9H0H5.
    CleanExi HS_RACGAP1.
    Genevestigatori Q9H0H5.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    InterProi IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view ]
    Pfami PF00130. C1_1. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view ]
    SMARTi SM00109. C1. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    PROSITEi PS50238. RHOGAP. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: TestisImported.
    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.
      , 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: HepatomaImported.
    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: PlacentaImported and TestisImported.
    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: Brain1 Publication.
    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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiRGAP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9H0H5
    Secondary accession number(s): Q6PJ26
    , Q9NWN2, Q9P250, Q9P2W2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3