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Q9H0H5

- RGAP1_HUMAN

UniProt

Q9H0H5 - RGAP1_HUMAN

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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

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 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
Complete GO annotation...

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. centralspindlin complex Source: UniProtKB
  2. cleavage furrow Source: UniProtKB
  3. cytoplasmic vesicle Source: UniProtKB-KW
  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
Complete GO annotation...

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

BgeeiQ9H0H5.
CleanExiHS_RACGAP1.
ExpressionAtlasiQ9H0H5. baseline and differential.
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
ECT2Q9H8V38EBI-717233,EBI-1054039
KIF23Q0224110EBI-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 – 2935Combined sources
Turni301 – 3033Combined sources
Beta strandi312 – 3209Combined sources
Helixi325 – 3306Combined sources
Helixi351 – 3544Combined sources
Beta strandi357 – 3604Combined sources
Helixi364 – 37613Combined sources
Turni377 – 3793Combined sources
Turni381 – 3855Combined sources
Helixi390 – 40112Combined sources
Helixi409 – 4113Combined sources
Helixi415 – 42713Combined sources
Beta strandi429 – 4313Combined sources
Turni436 – 4383Combined sources
Helixi439 – 4479Combined sources
Helixi451 – 46313Combined sources
Helixi467 – 48519Combined sources
Turni487 – 4893Combined sources
Helixi493 – 50412Combined sources
Beta strandi508 – 5114Combined sources
Helixi514 – 53320Combined sources
Helixi536 – 5405Combined sources
Helixi541 – 5433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119098.
HOGENOMiHOG000230702.
HOVERGENiHBG062009.
InParanoidiQ9H0H5.
KOiK16733.
OMAiGKISLKC.
OrthoDBiEOG7K0ZBT.
PhylomeDBiQ9H0H5.
TreeFamiTF318102.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR002219. 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

        10         20         30         40         50
MDTMMLNVRN LFEQLVRRVE ILSEGNEVQF IQLAKDFEDF RKKWQRTDHE
60 70 80 90 100
LGKYKDLLMK AETERSALDV KLKHARNQVD VEIKRRQRAE ADCEKLERQI
110 120 130 140 150
QLIREMLMCD TSGSIQLSEE QKSALAFLNR GQPSSSNAGN KRLSTIDESG
160 170 180 190 200
SILSDISFDK TDESLDWDSS LVKTFKLKKR EKRRSTSRQF VDGPPGPVKK
210 220 230 240 250
TRSIGSAVDQ GNESIVAKTT VTVPNDGGPI EAVSTIETVP YWTRSRRKTG
260 270 280 290 300
TLQPWNSDST LNSRQLEPRT ETDSVGTPQS NGGMRLHDFV SKTVIKPESC
310 320 330 340 350
VPCGKRIKFG KLSLKCRDCR VVSHPECRDR CPLPCIPTLI GTPVKIGEGM
360 370 380 390 400
LADFVSQTSP MIPSIVVHCV NEIEQRGLTE TGLYRISGCD RTVKELKEKF
410 420 430 440 450
LRVKTVPLLS KVDDIHAICS LLKDFLRNLK EPLLTFRLNR AFMEAAEITD
460 470 480 490 500
EDNSIAAMYQ AVGELPQANR DTLAFLMIHL QRVAQSPHTK MDVANLAKVF
510 520 530 540 550
GPTIVAHAVP NPDPVTMLQD IKRQPKVVER LLSLPLEYWS QFMMVEQENI
560 570 580 590 600
DPLHVIENSN AFSTPQTPDI KVSLLGPVTT PEHQLLKTPS SSSLSQRVRS
610 620 630
TLTKNTPRFG SKSKSATNLG RQGNFFASPM LK
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00760000119098.
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

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

Gene expression databases

Bgeei Q9H0H5.
CleanExi HS_RACGAP1.
ExpressionAtlasi Q9H0H5. baseline and differential.
Genevestigatori Q9H0H5.

Family and domain databases

Gene3Di 1.10.555.10. 1 hit.
InterProi IPR002219. 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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 132 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