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Q811P8 (RHG32_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2089 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. Ref.1 Ref.7 Ref.8 Ref.10 Ref.11

Subunit structure

Interacts with NTRK1 (via cytoplasmic domain); the interaction is independent of the phosphorylation state of NTRK1 By similarity. Interacts with SHC3 (via SH2 domain) By similarity. Interacts with RASA1 (via SH3 domain); the interaction is necessary for the Ras activation and cell transforming activities of ARHGAP32. 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 By similarity. 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 By similarity. 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. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11

Subcellular location

Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell projectiondendritic spine. Cytoplasmcell cortex. Endosome membrane. Golgi apparatus membrane. Endoplasmic reticulum membrane. Membrane. Note: Association to membrane via PX domain By similarity. Associated with cortical actin in undifferentiated neuroblastoma cells, but localized to dendritic spine and postsynaptic density after differentiation. Colocalizes with EGFR at the cell membrane upon EGF treatment By similarity. Colocalizes with GAB2 at the cell membrane. Ref.6 Ref.8 Ref.9

Tissue specificity

Isoform 1 and isoform 2 are highly expressed in brain, specially in cortex, corpus striatum, hippocampus and thalamus. Low levels in cerebellum, colon, small intestine, and kidney. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Developmental stage

Isoform 1 is detectable by embryonic day 13, whereas isoform 2 is detected postnatally. Ref.1 Ref.6

Domain

The N-terminal PX domain interacts specifically with phosphatidylinositides. Ref.6

Post-translational modification

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

Disruption phenotype

Mice are fertile but display abnormal neurite growth. Ref.10

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q811P8-1)

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: Q811P8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-349: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20892089Rho GTPase-activating protein 32
PRO_0000345204

Regions

Domain131 – 245115PX; atypical
Domain259 – 32163SH3
Domain372 – 567196Rho-GAP
Region1395 – 1714320Interaction with GAB2 By similarity
Region1688 – 2089402Interaction with FYN By similarity
Compositional bias1033 – 10386Poly-Pro
Compositional bias1309 – 13146Poly-Pro

Amino acid modifications

Modified residue7061Phosphoserine By similarity
Modified residue12061Phosphoserine By similarity

Natural variations

Alternative sequence1 – 349349Missing in isoform 2.
VSP_034937

Experimental info

Mutagenesis581R → K: Does not affect RhoA or CDC42 activity. Ref.11

Sequences

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

Last modified July 22, 2008. Version 2.
Checksum: C7C4BD904D903F02

FASTA2,089229,719
        10         20         30         40         50         60 
METESETSSL GDDSVFWLDC EGVTQLTDGD EEEREESFRK MKSSIHSEED DFVPELHRNV 

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

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

       190        200        210        220        230        240 
KHLHLCIYDR RFSQLTELPR SDVLKDSPES VTQMLTAYLS RLSTIAGNKI 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 NHVDVLFSGK ISAVMQEGAA SLSRPKSLLV SSPSTKLLTL 

       610        620        630        640        650        660 
EEAQARTQAQ VSSPIVTENK YIEVGEGPAA LQGKFHTVIE FPLERKRPQN KMKKSPVGSW 

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

       730        740        750        760        770        780 
KLFRPRRPRS SSDALSASFN GDVLGNRCNS YDNLPHDNES EEEVGLLHIP ALVSPHSAED 

       790        800        810        820        830        840 
VDLSPPDIGV ASLDFDPMSF QCSPPKAESE CLESGASFLD SLGYTRDKLS PSKKDAEAGG 

       850        860        870        880        890        900 
SQSQTPGSTA SSEPVSPVQE KLSPFFTLDL SPTDDKSSKP SSFTEKVVYA FSPKIGRKLS 

       910        920        930        940        950        960 
KSPSMNISEP ISVTLPPRVS EVIGTVSNTV AQNASPTSWD KSVEERDVIN RSPTQLQLGK 

       970        980        990       1000       1010       1020 
MKAGEREAQE TCEPEAQPLE QGAAEEVELP GTEERPVLSS QSKAVPSGQS QTGAVTHDPP 

      1030       1040       1050       1060       1070       1080 
QDPVPVSSVS LIPPPPPPKN VARMLALALA ESAQQASSQT LKRPGASQAG CTSYGDTAVV 

      1090       1100       1110       1120       1130       1140 
PSEEKLPSSY SSLTLDKTCF QTDRPAEQFH PQINGLGNCN QPLPEAAAMG GPTQSNTTDS 

      1150       1160       1170       1180       1190       1200 
GEQLHQVDLI GNSLHRNHIS GDPEKARSTS APLTDSEKSD DHGSFPEDHA GKSSVSTVSF 

      1210       1220       1230       1240       1250       1260 
LEQDQSPLHF SCGDQPLSYL GTSVDKPHHS SELTDKSPMP STLPRDKAHH PLSGSPEENS 

      1270       1280       1290       1300       1310       1320 
STATMAYMMA TPARAEPSNS EASRVLAEQP SAADFVAATL QRTHRTNRPL PPPPSQRPAE 

      1330       1340       1350       1360       1370       1380 
QPPVVGQVQE APSIGLNNSH KVQGTAPAPE RPPESRAMGD PAPIFLSDGT AAAQCPMGAS 

      1390       1400       1410       1420       1430       1440 
APQPGLPEKV RESSRAPPLH LRAESFPGHS CGFAAPVPPT RTMESKMAAA LHSSAADATS 

      1450       1460       1470       1480       1490       1500 
SSNYHSFVPS SASVDDVMPV PLPVSQPKHA SQKIAYSSFA RPDVTAEPFG PENCLHFNMT 

      1510       1520       1530       1540       1550       1560 
PNCQFRPQSV PPHHNKLEPH QVYGARSEPP ASMGPRYNTY VAPGRNMSGH HSKPCSRVEY 

      1570       1580       1590       1600       1610       1620 
VSSLGSSVRN PCCPEDILPY PTIRRVQSLH APPPSMIRSV PISRTEVPPD DEPAYCPRPV 

      1630       1640       1650       1660       1670       1680 
YQYKPYQSSQ ARSDYHVTQL QPYFENGRVH YRYSPYSSSS SSYYSPEGAL CDVDAYGTVQ 

      1690       1700       1710       1720       1730       1740 
LRPLHRLSSR DFAFYNPRLQ GKNVYNYAGL PPRPRANATG YFSGNDHNVV TMPPTADGKH 

      1750       1760       1770       1780       1790       1800 
TYTSWDLEDM EKYRMQSIRR ESRARQKVKG PIMSQYDNMT PAVQEDLGGI YVIHLRSKSD 

      1810       1820       1830       1840       1850       1860 
PGKTGLLSVA EGKEGRHPAK AVSPEGDERF YRKHPESEFD RAHHHGGYGS TQAEKPSLPQ 

      1870       1880       1890       1900       1910       1920 
KQSSLRNRKL HDMGCSLPEH RAHQEASHRQ LCESKNGPPY PQGAGQLDYG SKGMPDTSEP 

      1930       1940       1950       1960       1970       1980 
SNYHNSGKYM TSGQGSLTLN HKEVRLPKDL DRPRARQPPG PEKHSRDCYK EEEHFSQSMV 

      1990       2000       2010       2020       2030       2040 
PPPKPERSHS LKLHHTQNLE RDPSVLYQYQ THSKRQSSMT VVSQYDNLED YHSLPQHQRG 

      2050       2060       2070       2080 
GFGGAGMGAY VPSGFVHPQS RTYATALGQG AFLPTELSLP HPDTQIHAE 

« Hide

Isoform 2 [UniParc].

Checksum: AE701A72F0383D69
Show »

FASTA1,740190,331

References

« Hide 'large scale' references
[1]"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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: C57BL/6.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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] (ISOFORM 2).
Tissue: Brain.
[4]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1584-2089.
Tissue: Fetal brain.
[5]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[6]"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: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH CTTNB1; GRIN2B; DLG4 AND CDH2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DOMAIN PX.
[7]"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, TISSUE SPECIFICITY.
[8]"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: FUNCTION, INTERACTION WITH CTTNB1; GRIN2B; DLG4 AND CDH2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"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: INTERACTION WITH GRIN2B, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[10]"Role of the Rho GTPase-activating protein RICS in neurite outgrowth."
Nasu-Nishimura Y., Hayashi T., Ohishi T., Okabe T., Ohwada S., Hasegawa Y., Senda T., Toyoshima C., Nakamura T., Akiyama T.
Genes Cells 11:607-614(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDC42, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[11]"p200 RhoGAP promotes cell proliferation by mediating cross-talk between Ras and Rho signaling pathways."
Shang X., Moon S.Y., Zheng Y.
J. Biol. Chem. 282:8801-8811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RASA1, MUTAGENESIS OF ARG-58.
[12]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY194286 mRNA. Translation: AAO43676.1.
AC134607 Genomic DNA. No translation available.
BC132390 mRNA. Translation: AAI32391.1.
BC138042 mRNA. Translation: AAI38043.1.
AK173008 mRNA. Translation: BAD32286.1.
CCDSCCDS22951.3. [Q811P8-2]
CCDS57666.1. [Q811P8-1]
RefSeqNP_001182561.1. NM_001195632.1. [Q811P8-1]
NP_796353.3. NM_177379.4. [Q811P8-2]
UniGeneMm.46683.

3D structure databases

ProteinModelPortalQ811P8.
SMRQ811P8. Positions 264-319, 368-569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid237045. 7 interactions.
IntActQ811P8. 1 interaction.
MINTMINT-268399.

PTM databases

PhosphoSiteQ811P8.

Proteomic databases

MaxQBQ811P8.
PaxDbQ811P8.
PRIDEQ811P8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000168954; ENSMUSP00000128448; ENSMUSG00000041444. [Q811P8-2]
ENSMUST00000174641; ENSMUSP00000133898; ENSMUSG00000041444. [Q811P8-1]
ENSMUST00000182802; ENSMUSP00000138145; ENSMUSG00000041444. [Q811P8-2]
GeneID330914.
KEGGmmu:330914.
UCSCuc009orv.2. mouse. [Q811P8-1]

Organism-specific databases

CTD9743.
MGIMGI:2450166. Arhgap32.
RougeSearch...

Phylogenomic databases

eggNOGNOG311367.
GeneTreeENSGT00720000108475.
HOGENOMHOG000090208.
HOVERGENHBG108407.
InParanoidQ811P8.
OMAVVSQYDN.
OrthoDBEOG7WMCHV.
PhylomeDBQ811P8.
TreeFamTF351451.

Gene expression databases

BgeeQ811P8.
GenevestigatorQ811P8.

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. mouse.
NextBio399621.
PROQ811P8.
SOURCESearch...

Entry information

Entry nameRHG32_MOUSE
AccessionPrimary (citable) accession number: Q811P8
Secondary accession number(s): B9EHJ8, Q6A010
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot