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A7KAX9 (RHG32_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho GTPase-activating protein 32
Alternative name(s):
Brain-specific Rho GTPase-activating protein
GAB-associated Cdc42/Rac GTPase-activating protein
GC-GAP
GTPase regulator interacting with TrkA
Rho-type GTPase-activating protein 32
Rho/Cdc42/Rac GTPase-activating protein RICS
RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling
p200RhoGAP
p250GAP
Gene names
Name:ARHGAP32
Synonyms:GRIT, KIAA0712, RICS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2087 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity By similarity. Ref.1 Ref.2 Ref.3 Ref.4 Ref.8 Ref.9 Ref.10

Subunit structure

Interacts with NTRK1 (via cytoplasmic domain); the interaction is independent of the phosphorylation state of NTRK1. Interacts with SHC3 (via SH2 domain). Interacts with RASA1 (via SH3 domain); the interaction is necessary for the Ras activation and cell transforming activities of ARHGAP32 By similarity. Interacts with GAB1 and GAB2. Interacts with CRK and CRKL. Found in a complex with CRKL and BCAR1; upon EGF stimulation BCAR1 may be replaced by EGFR. Interacts with NCK1 (via SH3 domain); NCK1 recruits phosphorylated BCAR1 to the complex. Isoform 2 interacts with FYN; the interaction appears to be dependent on tyrosine phosphorylation of ARHGAP32. Interacts with EGFR; the interaction requires EGF stimulation and is increased by SHC3. Interacts with CDC42; the interaction requires constitutively active CDC42. Interacts with CTNNB1, DLG4, CDH2 and GRIN2B By similarity. Ref.1 Ref.2 Ref.3 Ref.8 Ref.10

Subcellular location

Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell projectiondendritic spine By similarity. Cytoplasmcell cortex. Endosome membrane By similarity. Golgi apparatus membrane By similarity. Endoplasmic reticulum membrane By similarity. Membrane. Note: Association to membrane via PX domain. Associated with cortical actin in undifferentiated neuroblastoma cells, but localized to dendritic spine and postsynaptic density after differentiation By similarity. Colocalizes with EGFR at the cell membrane upon EGF treatment. Colocalizes with GAB2 at the cell membrane. Ref.1 Ref.3 Ref.4

Tissue specificity

Isoform 1 and isoform 2 are highly expressed in brain and testis. Isoform 1 is also expressed in other tissues such as lung, liver and spleen. Ref.1

Domain

The N-terminal PX domain interacts specifically with phosphatidylinositides By similarity.

Post-translational modification

Isoform 2 is phosphorylated on multiple tyrosine residues by FYN. Phosphorylated tyrosine residues undergo dephosphorylation after stimulation of NMDA receptors By similarity. Phosphorylated in vitro by CaMK2 in the presence of calmodulin and calcium; which inhibits GAP activity By similarity. Ref.1 Ref.8

Sequence similarities

Belongs to the PX domain-containing GAP family.

Contains 1 PX (phox homology) domain.

Contains 1 Rho-GAP domain.

Contains 1 SH3 domain.

Sequence caution

The sequence BAA34432.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainSH3 domain
   Molecular functionGTPase activation
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

actin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Traceable author statement. Source: Reactome

dendritic spine

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionGTPase activator activity

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.8. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FYNP062414EBI-308663,EBI-515315

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: A7KAX9-1)

Also known as: PX-RICS;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: A7KAX9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-349: Missing.
Isoform 3 (identifier: A7KAX9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-290: Missing.
     567-612: FSGRISMAMQ...AQARTQAQVN → LPHFSARTEL...LVQITVCISI
     613-2087: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20872087Rho GTPase-activating protein 32
PRO_0000345203

Regions

Domain131 – 245115PX; atypical
Domain259 – 32163SH3
Domain372 – 567196Rho-GAP
Region1391 – 1711321Interaction with GAB2
Region1685 – 2087403Interaction with FYN
Compositional bias1031 – 10366Poly-Pro
Compositional bias1305 – 13106Poly-Pro

Amino acid modifications

Modified residue7061Phosphoserine Ref.13
Modified residue12031Phosphoserine Ref.12

Natural variations

Alternative sequence1 – 349349Missing in isoform 2.
VSP_034933
Alternative sequence1 – 290290Missing in isoform 3.
VSP_034934
Alternative sequence567 – 61246FSGRI…QAQVN → LPHFSARTELIVPFPLRLLR KQFTPPLLGPMSPLNPLVQI TVCISI in isoform 3.
VSP_034935
Alternative sequence613 – 20871475Missing in isoform 3.
VSP_034936

Experimental info

Mutagenesis1731Y → A: Loss of binding to phospholipids. Cytoplasmic localization. Ref.4
Mutagenesis4071R → A: Mild effect on GAP activity and neurite-promotion upon nerve growth factor stimulation. Ref.1 Ref.2 Ref.4 Ref.9 Ref.10
Mutagenesis4071R → I: Loss of GAP activity. Ref.1 Ref.2 Ref.4 Ref.9 Ref.10
Mutagenesis4071R → M: Loss of GAP activity. In isoform 1, no inhibitory effect on neurite extension. Ref.1 Ref.2 Ref.4 Ref.9 Ref.10
Mutagenesis4471K → A: Loss of GAP activity. Ref.2

Secondary structure

............................. 2087
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PX-RICS) [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 075E5B4902857D06

FASTA2,087230,529
        10         20         30         40         50         60 
METESESSTL GDDSVFWLES EVIIQVTDCE EEEREEKFRK MKSSVHSEED DFVPELHRNV 

        70         80         90        100        110        120 
HPRERPDWEE TLSAMARGAD VPEIPGDLTL KTCGSTASMK VKHVKKLPFT KGHFPKMAEC 

       130        140        150        160        170        180 
AHFHYENVEF GSIQLSLSEE QNEVMKNGCE SKELVYLVQI ACQGKSWIVK RSYEDFRVLD 

       190        200        210        220        230        240 
KHLHLCIYDR RFSQLSELPR SDTLKDSPES VTQMLMAYLS RLSAIAGNKI NCGPALTWME 

       250        260        270        280        290        300 
IDNKGNHLLV HEESSINTPA VGAAHVIKRY TARAPDELTL EVGDIVSVID MPPKVLSTWW 

       310        320        330        340        350        360 
RGKHGFQVGL FPGHCVELIN QKVPQSVTNS VPKPVSKKHG KLITFLRTFM KSRPTKQKLK 

       370        380        390        400        410        420 
QRGILKERVF GCDLGEHLLN SGFEVPQVLQ SCTAFIERYG IVDGIYRLSG VASNIQRLRH 

       430        440        450        460        470        480 
EFDSEHVPDL TKEPYVQDIH SVGSLCKLYF RELPNPLLTY QLYEKFSDAV SAATDEERLI 

       490        500        510        520        530        540 
KIHDVIQQLP PPHYRTLEFL MRHLSLLADY CSITNMHAKN LAIVWAPNLL RSKQIESACF 

       550        560        570        580        590        600 
SGTAAFMEVR IQSVVVEFIL NHVDVLFSGR ISMAMQEGAA SLSRPKSLLV SSPSTKLLTL 

       610        620        630        640        650        660 
EEAQARTQAQ VNSPIVTENK YIEVGEGPAA LQGKFHTIIE FPLERKRPQN KMKKSPVGSW 

       670        680        690        700        710        720 
RSFFNLGKSS SVSKRKLQRN ESEPSEMKAM ALKGGRAEGT LRSAKSEESL TSLHAVDGDS 

       730        740        750        760        770        780 
KLFRPRRPRS SSDALSASFN GEMLGNRCNS YDNLPHDNES EEEGGLLHIP ALMSPHSAED 

       790        800        810        820        830        840 
VDLSPPDIGV ASLDFDPMSF QCSPPKAESE CLESGASFLD SPGYSKDKPS ANKKDAETGS 

       850        860        870        880        890        900 
SQCQTPGSTA SSEPVSPLQE KLSPFFTLDL SPTEDKSSKP SSFTEKVVYA FSPKIGRKLS 

       910        920        930        940        950        960 
KSPSMSISEP ISVTLPPRVS EVIGTVSNTT AQNASSSTWD KCVEERDATN RSPTQIVKMK 

       970        980        990       1000       1010       1020 
TNETVAQEAY ESEVQPLDQV AAEEVELPGK EDQSVSSSQS KAVASGQTQT GAVTHDPPQD 

      1030       1040       1050       1060       1070       1080 
SVPVSSVSLI PPPPPPKNVA RMLALALAES AQQASTQSLK RPGTSQAGYT NYGDIAVATT 

      1090       1100       1110       1120       1130       1140 
EDNLSSSYSA VALDKAYFQT DRPAEQFHLQ NNAPGNCDHP LPETTATGDP THSNTTESGE 

      1150       1160       1170       1180       1190       1200 
QHHQVDLTGN QPHQAYLSGD PEKARITSVP LDSEKSDDHV SFPEDQSGKN SMPTVSFLDQ 

      1210       1220       1230       1240       1250       1260 
DQSPPRFYSG DQPPSYLGAS VDKLHHPLEF ADKSPTPPNL PSDKIYPPSG SPEENTSTAT 

      1270       1280       1290       1300       1310       1320 
MTYMTTTPAT AQMSTKEASW DVAEQPTTAD FAAATLQRTH RTNRPLPPPP SQRSAEQPPV 

      1330       1340       1350       1360       1370       1380 
VGQVQAATNI GLNNSHKVQG VVPVPERPPE PRAMDDPASA FISDSGAAAA QCPMATAVQP 

      1390       1400       1410       1420       1430       1440 
GLPEKVRDGA RVPLLHLRAE SVPAHPCGFP APLPPTRMME SKMIAAIHSS SADATSSSNY 

      1450       1460       1470       1480       1490       1500 
HSFVTASSTS VDDALPLPLP VPQPKHASQK TVYSSFARPD VTTEPFGPDN CLHFNMTPNC 

      1510       1520       1530       1540       1550       1560 
QYRPQSVPPH HNKLEQHQVY GARSEPPASM GLRYNTYVAP GRNASGHHSK PCSRVEYVSS 

      1570       1580       1590       1600       1610       1620 
LSSSVRNTCY PEDIPPYPTI RRVQSLHAPP SSMIRSVPIS RTEVPPDDEP AYCPRPLYQY 

      1630       1640       1650       1660       1670       1680 
KPYQSSQARS DYHVTQLQPY FENGRVHYRY SPYSSSSSSY YSPDGALCDV DAYGTVQLRP 

      1690       1700       1710       1720       1730       1740 
LHRLPNRDFA FYNPRLQGKS LYSYAGLAPR PRANVTGYFS PNDHNVVSMP PAADVKHTYT 

      1750       1760       1770       1780       1790       1800 
SWDLEDMEKY RMQSIRRESR ARQKVKGPVM SQYDNMTPAV QDDLGGIYVI HLRSKSDPGK 

      1810       1820       1830       1840       1850       1860 
TGLLSVAEGK ESRHAAKAIS PEGEDRFYRR HPEAEMDRAH HHGGHGSTQP EKPSLPQKQS 

      1870       1880       1890       1900       1910       1920 
SLRSRKLPDM GCSLPEHRAH QEASHRQFCE SKNGPPYPQG AGQLDYGSKG IPDTSEPVSY 

      1930       1940       1950       1960       1970       1980 
HNSGVKYAAS GQESLRLNHK EVRLSKEMER PWVRQPSAPE KHSRDCYKEE EHLTQSIVPP 

      1990       2000       2010       2020       2030       2040 
PKPERSHSLK LHHTQNVERD PSVLYQYQPH GKRQSSVTVV SQYDNLEDYH SLPQHQRGVF 

      2050       2060       2070       2080 
GGGGMGTYVP PGFPHPQSRT YATALGQGAF LPAELSLQHP ETQIHAE 

« Hide

Isoform 2 [UniParc].

Checksum: 49B5C6F92BDE9A27
Show »

FASTA1,738190,970
Isoform 3 [UniParc].

Checksum: CE60526885AED792
Show »

FASTA32236,669

References

« Hide 'large scale' references
[1]"Grit, a GTPase-activating protein for the Rho family, regulates neurite extension through association with the TrkA receptor and N-Shc and CrkL/Crk adapter molecules."
Nakamura T., Komiya M., Sone K., Hirose E., Gotoh N., Morii H., Ohta Y., Mori N.
Mol. Cell. Biol. 22:8721-8734(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH NTRK1; SHC3; BCAR1; EGFR; CRK AND CRKL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, MUTAGENESIS OF ARG-407.
Tissue: Brain.
[2]"RICS, a novel GTPase-activating protein for Cdc42 and Rac1, is involved in the beta-catenin-N-cadherin and N-methyl-D-aspartate receptor signaling."
Okabe T., Nakamura T., Nishimura Y.N., Kohu K., Ohwada S., Morishita Y., Akiyama T.
J. Biol. Chem. 278:9920-9927(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH CTNNB1, MUTAGENESIS OF ARG-407 AND LYS-447.
[3]"GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2."
Zhao C., Ma H., Bossy-Wetzel E., Lipton S.A., Zhang Z., Feng G.S.
J. Biol. Chem. 278:34641-34653(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH GAB1 AND GAB2; BCAR1; CRK AND NCK1, SUBCELLULAR LOCATION.
Tissue: Brain.
[4]"PX-RICS, a novel splicing variant of RICS, is a main isoform expressed during neural development."
Hayashi T., Okabe T., Nasu-Nishimura Y., Sakaue F., Ohwada S., Matsuura K., Akiyama T., Nakamura T.
Genes Cells 12:929-939(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-173 AND ARG-407.
[5]"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORMS 2 AND 3).
Tissue: Colon and Eye.
[8]"p250GAP, a neural RhoGAP protein, is associated with and phosphorylated by Fyn."
Taniguchi S., Liu H., Nakazawa T., Yokoyama K., Tezuka T., Yamamoto T.
Biochem. Biophys. Res. Commun. 306:151-155(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FYN, PHOSPHORYLATION (ISOFORM 2).
[9]"Characterization of a brain-specific Rho GTPase-activating protein, p200RhoGAP."
Moon S.Y., Zang H., Zheng Y.
J. Biol. Chem. 278:4151-4159(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-407.
[10]"p250GAP, a novel brain-enriched GTPase-activating protein for Rho family GTPases, is involved in the N-methyl-d-aspartate receptor signaling."
Nakazawa T., Watabe A.M., Tezuka T., Yoshida Y., Yokoyama K., Umemori H., Inoue A., Okabe S., Manabe T., Yamamoto T.
Mol. Biol. Cell 14:2921-2934(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GRIN2B, MUTAGENESIS OF ARG-407.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-1203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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-706, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Crystal structure of the Rho-GAP domain of RICS."
Structural genomics consortium (SGC)
Submitted (SEP-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 367-577.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB079856 mRNA. Translation: BAC24802.1.
AY194287 mRNA. Translation: AAO43677.1.
AB088416 mRNA. Translation: BAM34446.1.
EF127492 mRNA. Translation: ABO33171.1.
AB018255 mRNA. Translation: BAA34432.2. Different initiation.
CH471065 Genomic DNA. Translation: EAW67740.1.
BC000277 mRNA. Translation: AAH00277.2.
BC104898 mRNA. Translation: AAI04899.1.
BC113429 mRNA. Translation: AAI13430.1.
CCDSCCDS31718.1. [A7KAX9-2]
CCDS44769.1. [A7KAX9-1]
RefSeqNP_001136157.1. NM_001142685.1. [A7KAX9-1]
NP_055530.2. NM_014715.3. [A7KAX9-2]
UniGeneHs.440379.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IUGX-ray1.77A/B367-577[»]
ProteinModelPortalA7KAX9.
SMRA7KAX9. Positions 263-319, 368-569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115091. 27 interactions.
IntActA7KAX9. 8 interactions.
MINTMINT-268455.

Proteomic databases

MaxQBA7KAX9.
PaxDbA7KAX9.
PRIDEA7KAX9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310343; ENSP00000310561; ENSG00000134909. [A7KAX9-1]
ENST00000392657; ENSP00000376425; ENSG00000134909. [A7KAX9-2]
ENST00000527272; ENSP00000432862; ENSG00000134909. [A7KAX9-2]
GeneID9743.
KEGGhsa:9743.
UCSCuc001qez.3. human. [A7KAX9-1]

Organism-specific databases

CTD9743.
GeneCardsGC11M128834.
H-InvDBHIX0010264.
HGNCHGNC:17399. ARHGAP32.
HPAHPA038389.
MIM608541. gene.
neXtProtNX_A7KAX9.
PharmGKBPA165543138.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG311367.
HOGENOMHOG000090208.
HOVERGENHBG108407.
InParanoidA7KAX9.
OMAVVSQYDN.
OrthoDBEOG7WMCHV.
PhylomeDBA7KAX9.
TreeFamTF351451.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkA7KAX9.

Gene expression databases

ArrayExpressA7KAX9.
BgeeA7KAX9.
GenevestigatorA7KAX9.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
3.30.1520.10. 1 hit.
InterProIPR001683. Phox.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00787. PX. 1 hit.
PF00620. RhoGAP. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTSM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEPS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARHGAP32. human.
EvolutionaryTraceA7KAX9.
GeneWikiRICS_(gene).
GenomeRNAi9743.
NextBio35534637.
PROA7KAX9.
SOURCESearch...

Entry information

Entry nameRHG32_HUMAN
AccessionPrimary (citable) accession number: A7KAX9
Secondary accession number(s): I7H0B0 expand/collapse secondary AC list , O94820, Q86YL6, Q8IUG4, Q9BWG3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: September 11, 2007
Last modified: July 9, 2014
This is version 69 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 11

Human chromosome 11: entries, gene names and cross-references to MIM