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Q811P8

- RHG32_MOUSE

UniProt

Q811P8 - RHG32_MOUSE

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Protein

Rho GTPase-activating protein 32

Gene

Arhgap32

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

  1. GTPase activator activity Source: MGI
  2. phosphatidylinositol binding Source: InterPro

GO - Biological processi

  1. positive regulation of GTPase activity Source: GOC
  2. Rho protein signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_210090. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Arhgap32
Synonyms:Grit, Kiaa0712, Rics
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:2450166. Arhgap32.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: MGI
  2. cell cortex Source: MGI
  3. cell junction Source: UniProtKB-KW
  4. cell projection Source: UniProtKB-KW
  5. endoplasmic reticulum Source: UniProtKB-KW
  6. endosome Source: UniProtKB-KW
  7. Golgi apparatus Source: UniProtKB-KW
  8. postsynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

Mice are fertile but display abnormal neurite growth.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581R → K: Does not affect RhoA or CDC42 activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20892089Rho GTPase-activating protein 32PRO_0000345204Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei706 – 7061PhosphoserineBy similarity
Modified residuei1206 – 12061PhosphoserineBy similarity

Post-translational modificationi

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.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ811P8.
PaxDbiQ811P8.
PRIDEiQ811P8.

PTM databases

PhosphoSiteiQ811P8.

Expressioni

Tissue specificityi

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.6 Publications

Developmental stagei

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

Gene expression databases

BgeeiQ811P8.
ExpressionAtlasiQ811P8. baseline and differential.
GenevestigatoriQ811P8.

Interactioni

Subunit structurei

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.By similarity5 Publications

Protein-protein interaction databases

BioGridi237045. 7 interactions.
IntActiQ811P8. 1 interaction.
MINTiMINT-268399.

Structurei

3D structure databases

ProteinModelPortaliQ811P8.
SMRiQ811P8. Positions 264-321, 368-569.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini131 – 245115PX; atypicalAdd
BLAST
Domaini259 – 32163SH3PROSITE-ProRule annotationAdd
BLAST
Domaini372 – 567196Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1395 – 1714320Interaction with GAB2By similarityAdd
BLAST
Regioni1688 – 2089402Interaction with FYNBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1033 – 10386Poly-Pro
Compositional biasi1309 – 13146Poly-Pro

Domaini

The N-terminal PX domain interacts specifically with phosphatidylinositides.1 Publication

Sequence similaritiesi

Belongs to the PX domain-containing GAP family.Curated
Contains 1 PX (phox homology) domain.Curated
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG311367.
GeneTreeiENSGT00720000108475.
HOGENOMiHOG000090208.
HOVERGENiHBG108407.
InParanoidiQ811P8.
OMAiVVSQYDN.
OrthoDBiEOG7WMCHV.
PhylomeDBiQ811P8.
TreeFamiTF351451.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00787. PX. 1 hit.
PF00620. RhoGAP. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q811P8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
METESETSSL GDDSVFWLDC EGVTQLTDGD EEEREESFRK MKSSIHSEED
60 70 80 90 100
DFVPELHRNV HPRERPDWEE TLSAMARGAD VPEIPGDLTL KSCGSTASTK
110 120 130 140 150
VKHVKKLPFT KGHFPKMAEC AHFHYENVEF GSIQLSLSEE QNEVMKNGCE
160 170 180 190 200
SKELVYLVQI ACQGKSWIVK RSYEDFRVLD KHLHLCIYDR RFSQLTELPR
210 220 230 240 250
SDVLKDSPES VTQMLTAYLS RLSTIAGNKI NCGPALTWME IDNKGNHLLV
260 270 280 290 300
HEESSINTPA VGAAHVIKRY TARAPDELTL EVGDIVSVID MPPKVLSTWW
310 320 330 340 350
RGKHGFQVGL FPGHCVELIN QKVPQSVTNS VPKPVSKKHG KLITFLRTFM
360 370 380 390 400
KSRPTKQKLK QRGILKERVF GCDLGEHLLN SGFEVPQVLQ SCTAFIERYG
410 420 430 440 450
IVDGIYRLSG VASNIQRLRH EFDSEHVPDL TKEPYVQDIH SVGSLCKLYF
460 470 480 490 500
RELPNPLLTY QLYEKFSDAV SAATDEERLI KIHDVIQQLP PPHYRTLEFL
510 520 530 540 550
MRHLSLLADY CSITNMHAKN LAIVWAPNLL RSKQIESACF SGTAAFMEVR
560 570 580 590 600
IQSVVVEFIL NHVDVLFSGK ISAVMQEGAA SLSRPKSLLV SSPSTKLLTL
610 620 630 640 650
EEAQARTQAQ VSSPIVTENK YIEVGEGPAA LQGKFHTVIE FPLERKRPQN
660 670 680 690 700
KMKKSPVGSW RSFFNLGKSS SVSKRKLQRN ESEPSEMKAM ALKGGRAEGT
710 720 730 740 750
LRSAKSEESL TSLHAVDGDS KLFRPRRPRS SSDALSASFN GDVLGNRCNS
760 770 780 790 800
YDNLPHDNES EEEVGLLHIP ALVSPHSAED VDLSPPDIGV ASLDFDPMSF
810 820 830 840 850
QCSPPKAESE CLESGASFLD SLGYTRDKLS PSKKDAEAGG SQSQTPGSTA
860 870 880 890 900
SSEPVSPVQE KLSPFFTLDL SPTDDKSSKP SSFTEKVVYA FSPKIGRKLS
910 920 930 940 950
KSPSMNISEP ISVTLPPRVS EVIGTVSNTV AQNASPTSWD KSVEERDVIN
960 970 980 990 1000
RSPTQLQLGK MKAGEREAQE TCEPEAQPLE QGAAEEVELP GTEERPVLSS
1010 1020 1030 1040 1050
QSKAVPSGQS QTGAVTHDPP QDPVPVSSVS LIPPPPPPKN VARMLALALA
1060 1070 1080 1090 1100
ESAQQASSQT LKRPGASQAG CTSYGDTAVV PSEEKLPSSY SSLTLDKTCF
1110 1120 1130 1140 1150
QTDRPAEQFH PQINGLGNCN QPLPEAAAMG GPTQSNTTDS GEQLHQVDLI
1160 1170 1180 1190 1200
GNSLHRNHIS GDPEKARSTS APLTDSEKSD DHGSFPEDHA GKSSVSTVSF
1210 1220 1230 1240 1250
LEQDQSPLHF SCGDQPLSYL GTSVDKPHHS SELTDKSPMP STLPRDKAHH
1260 1270 1280 1290 1300
PLSGSPEENS STATMAYMMA TPARAEPSNS EASRVLAEQP SAADFVAATL
1310 1320 1330 1340 1350
QRTHRTNRPL PPPPSQRPAE QPPVVGQVQE APSIGLNNSH KVQGTAPAPE
1360 1370 1380 1390 1400
RPPESRAMGD PAPIFLSDGT AAAQCPMGAS APQPGLPEKV RESSRAPPLH
1410 1420 1430 1440 1450
LRAESFPGHS CGFAAPVPPT RTMESKMAAA LHSSAADATS SSNYHSFVPS
1460 1470 1480 1490 1500
SASVDDVMPV PLPVSQPKHA SQKIAYSSFA RPDVTAEPFG PENCLHFNMT
1510 1520 1530 1540 1550
PNCQFRPQSV PPHHNKLEPH QVYGARSEPP ASMGPRYNTY VAPGRNMSGH
1560 1570 1580 1590 1600
HSKPCSRVEY VSSLGSSVRN PCCPEDILPY PTIRRVQSLH APPPSMIRSV
1610 1620 1630 1640 1650
PISRTEVPPD DEPAYCPRPV YQYKPYQSSQ ARSDYHVTQL QPYFENGRVH
1660 1670 1680 1690 1700
YRYSPYSSSS SSYYSPEGAL CDVDAYGTVQ LRPLHRLSSR DFAFYNPRLQ
1710 1720 1730 1740 1750
GKNVYNYAGL PPRPRANATG YFSGNDHNVV TMPPTADGKH TYTSWDLEDM
1760 1770 1780 1790 1800
EKYRMQSIRR ESRARQKVKG PIMSQYDNMT PAVQEDLGGI YVIHLRSKSD
1810 1820 1830 1840 1850
PGKTGLLSVA EGKEGRHPAK AVSPEGDERF YRKHPESEFD RAHHHGGYGS
1860 1870 1880 1890 1900
TQAEKPSLPQ KQSSLRNRKL HDMGCSLPEH RAHQEASHRQ LCESKNGPPY
1910 1920 1930 1940 1950
PQGAGQLDYG SKGMPDTSEP SNYHNSGKYM TSGQGSLTLN HKEVRLPKDL
1960 1970 1980 1990 2000
DRPRARQPPG PEKHSRDCYK EEEHFSQSMV PPPKPERSHS LKLHHTQNLE
2010 2020 2030 2040 2050
RDPSVLYQYQ THSKRQSSMT VVSQYDNLED YHSLPQHQRG GFGGAGMGAY
2060 2070 2080
VPSGFVHPQS RTYATALGQG AFLPTELSLP HPDTQIHAE
Length:2,089
Mass (Da):229,719
Last modified:July 22, 2008 - v2
Checksum:iC7C4BD904D903F02
GO
Isoform 2 (identifier: Q811P8-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,740
Mass (Da):190,331
Checksum:iAE701A72F0383D69
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 349349Missing in isoform 2. 2 PublicationsVSP_034937Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS22951.3. [Q811P8-2]
CCDS57666.1. [Q811P8-1]
RefSeqiNP_001182561.1. NM_001195632.1. [Q811P8-1]
NP_796353.3. NM_177379.4. [Q811P8-2]
UniGeneiMm.46683.

Genome annotation databases

EnsembliENSMUST00000168954; ENSMUSP00000128448; ENSMUSG00000041444. [Q811P8-2]
ENSMUST00000174641; ENSMUSP00000133898; ENSMUSG00000041444. [Q811P8-1]
ENSMUST00000182802; ENSMUSP00000138145; ENSMUSG00000041444. [Q811P8-2]
GeneIDi330914.
KEGGimmu:330914.
UCSCiuc009orv.2. mouse. [Q811P8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS22951.3. [Q811P8-2 ]
CCDS57666.1. [Q811P8-1 ]
RefSeqi NP_001182561.1. NM_001195632.1. [Q811P8-1 ]
NP_796353.3. NM_177379.4. [Q811P8-2 ]
UniGenei Mm.46683.

3D structure databases

ProteinModelPortali Q811P8.
SMRi Q811P8. Positions 264-321, 368-569.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 237045. 7 interactions.
IntActi Q811P8. 1 interaction.
MINTi MINT-268399.

PTM databases

PhosphoSitei Q811P8.

Proteomic databases

MaxQBi Q811P8.
PaxDbi Q811P8.
PRIDEi Q811P8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000168954 ; ENSMUSP00000128448 ; ENSMUSG00000041444 . [Q811P8-2 ]
ENSMUST00000174641 ; ENSMUSP00000133898 ; ENSMUSG00000041444 . [Q811P8-1 ]
ENSMUST00000182802 ; ENSMUSP00000138145 ; ENSMUSG00000041444 . [Q811P8-2 ]
GeneIDi 330914.
KEGGi mmu:330914.
UCSCi uc009orv.2. mouse. [Q811P8-1 ]

Organism-specific databases

CTDi 9743.
MGIi MGI:2450166. Arhgap32.
Rougei Search...

Phylogenomic databases

eggNOGi NOG311367.
GeneTreei ENSGT00720000108475.
HOGENOMi HOG000090208.
HOVERGENi HBG108407.
InParanoidi Q811P8.
OMAi VVSQYDN.
OrthoDBi EOG7WMCHV.
PhylomeDBi Q811P8.
TreeFami TF351451.

Enzyme and pathway databases

Reactomei REACT_210090. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSi Arhgap32. mouse.
NextBioi 399621.
PROi Q811P8.
SOURCEi Search...

Gene expression databases

Bgeei Q811P8.
ExpressionAtlasi Q811P8. baseline and differential.
Genevestigatori Q811P8.

Family and domain databases

Gene3Di 1.10.555.10. 1 hit.
3.30.1520.10. 1 hit.
InterProi IPR001683. Phox.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00787. PX. 1 hit.
PF00620. RhoGAP. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
SMARTi SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEi PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRHG32_MOUSE
AccessioniPrimary (citable) accession number: Q811P8
Secondary accession number(s): B9EHJ8, Q6A010
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: November 26, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3