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Protein

Rac GTPase-activating protein 1

Gene

RACGAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Zinc fingeri286 – 335Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST50

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • beta-tubulin binding Source: UniProtKB
  • gamma-tubulin binding Source: UniProtKB
  • GTPase activator activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • microtubule binding Source: UniProtKB
  • phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • actomyosin contractile ring assembly Source: UniProtKB
  • antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  • embryo development Source: UniProtKB
  • intracellular signal transduction Source: InterPro
  • microtubule-based movement Source: Reactome
  • mitotic cytokinesis Source: UniProtKB
  • mitotic spindle midzone assembly Source: UniProtKB
  • neuroblast proliferation Source: UniProtKB
  • positive regulation of cytokinesis Source: UniProtKB
  • regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
  • regulation of small GTPase mediated signal transduction Source: Reactome
  • retrograde vesicle-mediated transport, Golgi to ER Source: Reactome
  • spermatogenesis Source: UniProtKB
  • 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

BioCyciZFISH:ENSG00000161800-MONOMER.
ReactomeiR-HSA-194840. Rho GTPase cycle.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-983189. Kinesins.
SIGNORiQ9H0H5.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9804. RACGAP1.

Subcellular locationi

GO - Cellular componenti

  • acrosomal vesicle Source: UniProtKB-SubCell
  • centralspindlin complex Source: UniProtKB
  • cleavage furrow Source: UniProtKB
  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • midbody Source: UniProtKB
  • mitotic spindle Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi149S → 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 Publication1
Mutagenesisi157S → 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 Publications1
Mutagenesisi164S → 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 Publications1
Mutagenesisi170S → 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 Publications1
Mutagenesisi214S → 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 Publication1
Mutagenesisi289F → G: Cytokinesis failure. 1 Publication1
Mutagenesisi292K → L: Cytokinesis failure. Abolishes localization at the cell membrane. 1 Publication1
Mutagenesisi306R → L: Cytokinesis failure. Abolishes localization at the cell membrane. 1 Publication1
Mutagenesisi309F → A: Cytokinesis failure. Abolishes localization at the cell membrane. 1 Publication1
Mutagenesisi316C → G: Cytokinesis failure. 1 Publication1
Mutagenesisi385R → A: Abolishes GAP activity towards RAC1. Abolishes GAP activity towards CDC42 in prometaphase. Induces multiple blebs during cytokinesis. 3 Publications1

Organism-specific databases

DisGeNETi29127.
OpenTargetsiENSG00000161800.
PharmGKBiPA34165.

Chemistry databases

ChEMBLiCHEMBL2146306.

Polymorphism and mutation databases

BioMutaiRACGAP1.
DMDMi74762727.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002288081 – 632Rac GTPase-activating protein 1Add BLAST632

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei149Phosphoserine; by PLK11 Publication1
Modified residuei154PhosphoserineCombined sources1
Modified residuei157Phosphoserine; by PLK1Combined sources2 Publications1
Modified residuei161PhosphothreonineCombined sources1
Modified residuei164Phosphoserine; by PLK1Combined sources2 Publications1
Modified residuei170Phosphoserine; by PLK12 Publications1
Modified residuei203PhosphoserineCombined sources1
Modified residuei206PhosphoserineCombined sources1
Modified residuei214PhosphoserineCombined sources1 Publication1
Modified residuei249PhosphothreonineCombined sources1
Modified residuei257PhosphoserineCombined sources1
Modified residuei260Phosphothreonine1 Publication1
Modified residuei342PhosphothreonineCombined sources1
Modified residuei387Phosphoserine; by AURKB1 Publication1
Modified residuei410Phosphoserine; by AURKB1 Publication1
Modified residuei567PhosphothreonineCombined sources1
Modified residuei580PhosphothreonineCombined sources1
Modified residuei588PhosphothreonineCombined sources1
Modified residuei600PhosphoserineCombined sources1
Modified residuei601PhosphothreonineCombined sources1
Modified residuei606PhosphothreonineCombined sources1
Modified residuei628PhosphoserineCombined sources1

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.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9H0H5.
MaxQBiQ9H0H5.
PaxDbiQ9H0H5.
PeptideAtlasiQ9H0H5.
PRIDEiQ9H0H5.

PTM databases

iPTMnetiQ9H0H5.
PhosphoSitePlusiQ9H0H5.

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

BgeeiENSG00000161800.
CleanExiHS_RACGAP1.
ExpressionAtlasiQ9H0H5. baseline and differential.
GenevisibleiQ9H0H5. HS.

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
KIF23Q0224112EBI-717233,EBI-306852
MORF4L1Q9UBU83EBI-717233,EBI-399246
PPP2R5EQ165375EBI-717233,EBI-968374
RAB11FIP3O751547EBI-717233,EBI-7942186
SLC26A8Q96RN12EBI-717233,EBI-1792052

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • beta-tubulin binding Source: UniProtKB
  • gamma-tubulin binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi118892. 90 interactors.
DIPiDIP-33087N.
IntActiQ9H0H5. 80 interactors.
MINTiMINT-256435.
STRINGi9606.ENSP00000309871.

Structurei

Secondary structure

1632
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi289 – 293Combined sources5
Turni301 – 303Combined sources3
Beta strandi312 – 320Combined sources9
Helixi325 – 330Combined sources6
Helixi351 – 353Combined sources3
Beta strandi357 – 360Combined sources4
Helixi364 – 376Combined sources13
Turni377 – 379Combined sources3
Turni381 – 385Combined sources5
Helixi390 – 403Combined sources14
Helixi409 – 411Combined sources3
Helixi415 – 427Combined sources13
Beta strandi429 – 431Combined sources3
Turni436 – 438Combined sources3
Helixi439 – 447Combined sources9
Helixi451 – 464Combined sources14
Helixi467 – 485Combined sources19
Turni487 – 489Combined sources3
Helixi493 – 504Combined sources12
Beta strandi508 – 511Combined sources4
Helixi514 – 520Combined sources7
Helixi523 – 532Combined sources10
Helixi536 – 541Combined sources6
Turni542 – 544Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OVJX-ray1.49A348-546[»]
3W6RX-ray1.90A348-546[»]
3WPQX-ray1.84A/B346-546[»]
3WPSX-ray2.70A/B346-546[»]
4B6DX-ray2.20A/B/C/D/E/F284-339[»]
5C2JX-ray2.50A346-546[»]
5C2KX-ray1.42A346-546[»]
ProteinModelPortaliQ9H0H5.
SMRiQ9H0H5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H0H5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini349 – 539Rho-GAPPROSITE-ProRule annotationAdd BLAST191

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni106 – 285Interaction with SLC26A81 PublicationAdd BLAST180

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili53 – 110Sequence analysisAdd BLAST58

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)DescriptionActionsGraphical viewLength
Zinc fingeri286 – 335Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST50

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG3564. Eukaryota.
ENOG410XPK0. LUCA.
GeneTreeiENSGT00860000133689.
HOGENOMiHOG000230702.
HOVERGENiHBG062009.
InParanoidiQ9H0H5.
KOiK16733.
OMAiTPVNAMA.
OrthoDBiEOG091G03O7.
PhylomeDBiQ9H0H5.
TreeFamiTF318102.

Family and domain databases

CDDicd00029. C1. 1 hit.
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 differs from that shown. Reason: Frameshift at positions 171, 205 and 437.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti155D → H in BAA91347 (PubMed:14702039).Curated1
Sequence conflicti518L → S in BAA90247 (PubMed:10979956).Curated1

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_001126103.2.
NP_001119576.1. NM_001126104.2.
NP_001306928.1. NM_001319999.1.
NP_001306929.1. NM_001320000.1.
NP_001306930.1. NM_001320001.1.
NP_001306931.1. NM_001320002.1.
NP_001306932.1. NM_001320003.1.
NP_001306933.1. NM_001320004.1.
NP_001306934.1. NM_001320005.1.
NP_001306935.1. NM_001320006.1.
NP_001306936.1. NM_001320007.1.
NP_037409.2. NM_013277.4.
XP_006719422.1. XM_006719359.1.
XP_011536540.1. XM_011538238.1.
XP_016874709.1. XM_017019220.1.
UniGeneiHs.505469.

Genome annotation databases

EnsembliENST00000312377; ENSP00000309871; ENSG00000161800.
ENST00000427314; ENSP00000404190; ENSG00000161800.
ENST00000454520; ENSP00000404808; ENSG00000161800.
ENST00000547905; ENSP00000449370; ENSG00000161800.
ENST00000551016; ENSP00000449374; ENSG00000161800.
GeneIDi29127.
KEGGihsa:29127.
UCSCiuc001rvs.3. human.

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.
CCDSiCCDS8795.1.
PIRiD59430.
RefSeqiNP_001119575.1. NM_001126103.2.
NP_001119576.1. NM_001126104.2.
NP_001306928.1. NM_001319999.1.
NP_001306929.1. NM_001320000.1.
NP_001306930.1. NM_001320001.1.
NP_001306931.1. NM_001320002.1.
NP_001306932.1. NM_001320003.1.
NP_001306933.1. NM_001320004.1.
NP_001306934.1. NM_001320005.1.
NP_001306935.1. NM_001320006.1.
NP_001306936.1. NM_001320007.1.
NP_037409.2. NM_013277.4.
XP_006719422.1. XM_006719359.1.
XP_011536540.1. XM_011538238.1.
XP_016874709.1. XM_017019220.1.
UniGeneiHs.505469.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OVJX-ray1.49A348-546[»]
3W6RX-ray1.90A348-546[»]
3WPQX-ray1.84A/B346-546[»]
3WPSX-ray2.70A/B346-546[»]
4B6DX-ray2.20A/B/C/D/E/F284-339[»]
5C2JX-ray2.50A346-546[»]
5C2KX-ray1.42A346-546[»]
ProteinModelPortaliQ9H0H5.
SMRiQ9H0H5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118892. 90 interactors.
DIPiDIP-33087N.
IntActiQ9H0H5. 80 interactors.
MINTiMINT-256435.
STRINGi9606.ENSP00000309871.

Chemistry databases

ChEMBLiCHEMBL2146306.

PTM databases

iPTMnetiQ9H0H5.
PhosphoSitePlusiQ9H0H5.

Polymorphism and mutation databases

BioMutaiRACGAP1.
DMDMi74762727.

Proteomic databases

EPDiQ9H0H5.
MaxQBiQ9H0H5.
PaxDbiQ9H0H5.
PeptideAtlasiQ9H0H5.
PRIDEiQ9H0H5.

Protocols and materials databases

DNASUi29127.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312377; ENSP00000309871; ENSG00000161800.
ENST00000427314; ENSP00000404190; ENSG00000161800.
ENST00000454520; ENSP00000404808; ENSG00000161800.
ENST00000547905; ENSP00000449370; ENSG00000161800.
ENST00000551016; ENSP00000449374; ENSG00000161800.
GeneIDi29127.
KEGGihsa:29127.
UCSCiuc001rvs.3. human.

Organism-specific databases

CTDi29127.
DisGeNETi29127.
GeneCardsiRACGAP1.
H-InvDBHIX0036723.
HGNCiHGNC:9804. RACGAP1.
HPAiCAB025859.
HPA039427.
HPA043912.
MIMi604980. gene.
neXtProtiNX_Q9H0H5.
OpenTargetsiENSG00000161800.
PharmGKBiPA34165.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3564. Eukaryota.
ENOG410XPK0. LUCA.
GeneTreeiENSGT00860000133689.
HOGENOMiHOG000230702.
HOVERGENiHBG062009.
InParanoidiQ9H0H5.
KOiK16733.
OMAiTPVNAMA.
OrthoDBiEOG091G03O7.
PhylomeDBiQ9H0H5.
TreeFamiTF318102.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000161800-MONOMER.
ReactomeiR-HSA-194840. Rho GTPase cycle.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-983189. Kinesins.
SIGNORiQ9H0H5.

Miscellaneous databases

ChiTaRSiRACGAP1. human.
EvolutionaryTraceiQ9H0H5.
GeneWikiiRACGAP1.
GenomeRNAii29127.
PMAP-CutDBQ9H0H5.
PROiQ9H0H5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000161800.
CleanExiHS_RACGAP1.
ExpressionAtlasiQ9H0H5. baseline and differential.
GenevisibleiQ9H0H5. HS.

Family and domain databases

CDDicd00029. C1. 1 hit.
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]
ProtoNetiSearch...

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 30, 2016
This is version 155 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.