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A7KAX9

- RHG32_HUMAN

UniProt

A7KAX9 - RHG32_HUMAN

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Protein

Rho GTPase-activating protein 32

Gene
ARHGAP32, GRIT, KIAA0712, RICS
Organism
Homo sapiens (Human)
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 By similarity.7 Publications

GO - Molecular functioni

  1. GTPase activator activity Source: UniProtKB-KW
  2. phosphatidylinositol binding Source: InterPro
  3. protein binding Source: IntAct

GO - Biological processi

  1. regulation of small GTPase mediated signal transduction Source: Reactome
  2. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
SignaLinkiA7KAX9.

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
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 namesi
Synonyms:GRIT, KIAA0712, RICS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:17399. ARHGAP32.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. cell cortex Source: UniProtKB-SubCell
  3. cell junction Source: UniProtKB-KW
  4. cytosol Source: Reactome
  5. dendritic spine Source: UniProtKB-SubCell
  6. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  7. endosome membrane Source: UniProtKB-SubCell
  8. Golgi membrane Source: UniProtKB-SubCell
  9. postsynaptic density Source: UniProtKB-SubCell
  10. 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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi173 – 1731Y → A: Loss of binding to phospholipids. Cytoplasmic localization. 1 Publication
Mutagenesisi407 – 4071R → A: Mild effect on GAP activity and neurite-promotion upon nerve growth factor stimulation. 5 Publications
Mutagenesisi407 – 4071R → I: Loss of GAP activity. 5 Publications
Mutagenesisi407 – 4071R → M: Loss of GAP activity. In isoform 1, no inhibitory effect on neurite extension. 5 Publications
Mutagenesisi447 – 4471K → A: Loss of GAP activity. 1 Publication

Organism-specific databases

PharmGKBiPA165543138.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20872087Rho GTPase-activating protein 32PRO_0000345203Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei706 – 7061Phosphoserine1 Publication
Modified residuei1203 – 12031Phosphoserine1 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiA7KAX9.
PaxDbiA7KAX9.
PRIDEiA7KAX9.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

ArrayExpressiA7KAX9.
BgeeiA7KAX9.
GenevestigatoriA7KAX9.

Organism-specific databases

HPAiHPA038389.

Interactioni

Subunit structurei

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FYNP062414EBI-308663,EBI-515315

Protein-protein interaction databases

BioGridi115091. 27 interactions.
IntActiA7KAX9. 8 interactions.
MINTiMINT-268455.

Structurei

Secondary structure

1
2087
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi374 – 3818
Helixi387 – 39913
Turni403 – 4075
Helixi412 – 42312
Turni433 – 4375
Helixi439 – 45214
Turni460 – 4623
Helixi463 – 4708
Beta strandi472 – 4743
Helixi475 – 48612
Helixi491 – 50818
Helixi511 – 5144
Helixi518 – 52912
Helixi553 – 5619
Helixi563 – 5664

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IUGX-ray1.77A/B367-577[»]
ProteinModelPortaliA7KAX9.
SMRiA7KAX9. Positions 263-319, 368-569.

Miscellaneous databases

EvolutionaryTraceiA7KAX9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini131 – 245115PX; atypicalAdd
BLAST
Domaini259 – 32163SH3Add
BLAST
Domaini372 – 567196Rho-GAPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1391 – 1711321Interaction with GAB2Add
BLAST
Regioni1685 – 2087403Interaction with FYNAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1031 – 10366Poly-Pro
Compositional biasi1305 – 13106Poly-Pro

Domaini

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

Sequence similaritiesi

Contains 1 Rho-GAP domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG311367.
HOGENOMiHOG000090208.
HOVERGENiHBG108407.
InParanoidiA7KAX9.
OMAiVVSQYDN.
OrthoDBiEOG7WMCHV.
PhylomeDBiA7KAX9.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: A7KAX9-1) [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

METESESSTL GDDSVFWLES EVIIQVTDCE EEEREEKFRK MKSSVHSEED     50
DFVPELHRNV HPRERPDWEE TLSAMARGAD VPEIPGDLTL KTCGSTASMK 100
VKHVKKLPFT KGHFPKMAEC AHFHYENVEF GSIQLSLSEE QNEVMKNGCE 150
SKELVYLVQI ACQGKSWIVK RSYEDFRVLD KHLHLCIYDR RFSQLSELPR 200
SDTLKDSPES VTQMLMAYLS RLSAIAGNKI NCGPALTWME IDNKGNHLLV 250
HEESSINTPA VGAAHVIKRY TARAPDELTL EVGDIVSVID MPPKVLSTWW 300
RGKHGFQVGL FPGHCVELIN QKVPQSVTNS VPKPVSKKHG KLITFLRTFM 350
KSRPTKQKLK QRGILKERVF GCDLGEHLLN SGFEVPQVLQ SCTAFIERYG 400
IVDGIYRLSG VASNIQRLRH EFDSEHVPDL TKEPYVQDIH SVGSLCKLYF 450
RELPNPLLTY QLYEKFSDAV SAATDEERLI KIHDVIQQLP PPHYRTLEFL 500
MRHLSLLADY CSITNMHAKN LAIVWAPNLL RSKQIESACF SGTAAFMEVR 550
IQSVVVEFIL NHVDVLFSGR ISMAMQEGAA SLSRPKSLLV SSPSTKLLTL 600
EEAQARTQAQ VNSPIVTENK YIEVGEGPAA LQGKFHTIIE FPLERKRPQN 650
KMKKSPVGSW RSFFNLGKSS SVSKRKLQRN ESEPSEMKAM ALKGGRAEGT 700
LRSAKSEESL TSLHAVDGDS KLFRPRRPRS SSDALSASFN GEMLGNRCNS 750
YDNLPHDNES EEEGGLLHIP ALMSPHSAED VDLSPPDIGV ASLDFDPMSF 800
QCSPPKAESE CLESGASFLD SPGYSKDKPS ANKKDAETGS SQCQTPGSTA 850
SSEPVSPLQE KLSPFFTLDL SPTEDKSSKP SSFTEKVVYA FSPKIGRKLS 900
KSPSMSISEP ISVTLPPRVS EVIGTVSNTT AQNASSSTWD KCVEERDATN 950
RSPTQIVKMK TNETVAQEAY ESEVQPLDQV AAEEVELPGK EDQSVSSSQS 1000
KAVASGQTQT GAVTHDPPQD SVPVSSVSLI PPPPPPKNVA RMLALALAES 1050
AQQASTQSLK RPGTSQAGYT NYGDIAVATT EDNLSSSYSA VALDKAYFQT 1100
DRPAEQFHLQ NNAPGNCDHP LPETTATGDP THSNTTESGE QHHQVDLTGN 1150
QPHQAYLSGD PEKARITSVP LDSEKSDDHV SFPEDQSGKN SMPTVSFLDQ 1200
DQSPPRFYSG DQPPSYLGAS VDKLHHPLEF ADKSPTPPNL PSDKIYPPSG 1250
SPEENTSTAT MTYMTTTPAT AQMSTKEASW DVAEQPTTAD FAAATLQRTH 1300
RTNRPLPPPP SQRSAEQPPV VGQVQAATNI GLNNSHKVQG VVPVPERPPE 1350
PRAMDDPASA FISDSGAAAA QCPMATAVQP GLPEKVRDGA RVPLLHLRAE 1400
SVPAHPCGFP APLPPTRMME SKMIAAIHSS SADATSSSNY HSFVTASSTS 1450
VDDALPLPLP VPQPKHASQK TVYSSFARPD VTTEPFGPDN CLHFNMTPNC 1500
QYRPQSVPPH HNKLEQHQVY GARSEPPASM GLRYNTYVAP GRNASGHHSK 1550
PCSRVEYVSS LSSSVRNTCY PEDIPPYPTI RRVQSLHAPP SSMIRSVPIS 1600
RTEVPPDDEP AYCPRPLYQY KPYQSSQARS DYHVTQLQPY FENGRVHYRY 1650
SPYSSSSSSY YSPDGALCDV DAYGTVQLRP LHRLPNRDFA FYNPRLQGKS 1700
LYSYAGLAPR PRANVTGYFS PNDHNVVSMP PAADVKHTYT SWDLEDMEKY 1750
RMQSIRRESR ARQKVKGPVM SQYDNMTPAV QDDLGGIYVI HLRSKSDPGK 1800
TGLLSVAEGK ESRHAAKAIS PEGEDRFYRR HPEAEMDRAH HHGGHGSTQP 1850
EKPSLPQKQS SLRSRKLPDM GCSLPEHRAH QEASHRQFCE SKNGPPYPQG 1900
AGQLDYGSKG IPDTSEPVSY HNSGVKYAAS GQESLRLNHK EVRLSKEMER 1950
PWVRQPSAPE KHSRDCYKEE EHLTQSIVPP PKPERSHSLK LHHTQNVERD 2000
PSVLYQYQPH GKRQSSVTVV SQYDNLEDYH SLPQHQRGVF GGGGMGTYVP 2050
PGFPHPQSRT YATALGQGAF LPAELSLQHP ETQIHAE 2087
Length:2,087
Mass (Da):230,529
Last modified:September 11, 2007 - v1
Checksum:i075E5B4902857D06
GO
Isoform 2 (identifier: A7KAX9-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,738
Mass (Da):190,970
Checksum:i49B5C6F92BDE9A27
GO
Isoform 3 (identifier: A7KAX9-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:322
Mass (Da):36,669
Checksum:iCE60526885AED792
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 349349Missing in isoform 2. VSP_034933Add
BLAST
Alternative sequencei1 – 290290Missing in isoform 3. VSP_034934Add
BLAST
Alternative sequencei567 – 61246FSGRI…QAQVN → LPHFSARTELIVPFPLRLLR KQFTPPLLGPMSPLNPLVQI TVCISI in isoform 3. VSP_034935Add
BLAST
Alternative sequencei613 – 20871475Missing in isoform 3. VSP_034936Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS31718.1. [A7KAX9-2]
CCDS44769.1. [A7KAX9-1]
RefSeqiNP_001136157.1. NM_001142685.1. [A7KAX9-1]
NP_055530.2. NM_014715.3. [A7KAX9-2]
UniGeneiHs.440379.

Genome annotation databases

EnsembliENST00000310343; ENSP00000310561; ENSG00000134909. [A7KAX9-1]
ENST00000392657; ENSP00000376425; ENSG00000134909. [A7KAX9-2]
ENST00000527272; ENSP00000432862; ENSG00000134909. [A7KAX9-2]
GeneIDi9743.
KEGGihsa:9743.
UCSCiuc001qez.3. human. [A7KAX9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS31718.1. [A7KAX9-2 ]
CCDS44769.1. [A7KAX9-1 ]
RefSeqi NP_001136157.1. NM_001142685.1. [A7KAX9-1 ]
NP_055530.2. NM_014715.3. [A7KAX9-2 ]
UniGenei Hs.440379.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IUG X-ray 1.77 A/B 367-577 [» ]
ProteinModelPortali A7KAX9.
SMRi A7KAX9. Positions 263-319, 368-569.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115091. 27 interactions.
IntActi A7KAX9. 8 interactions.
MINTi MINT-268455.

Proteomic databases

MaxQBi A7KAX9.
PaxDbi A7KAX9.
PRIDEi A7KAX9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310343 ; ENSP00000310561 ; ENSG00000134909 . [A7KAX9-1 ]
ENST00000392657 ; ENSP00000376425 ; ENSG00000134909 . [A7KAX9-2 ]
ENST00000527272 ; ENSP00000432862 ; ENSG00000134909 . [A7KAX9-2 ]
GeneIDi 9743.
KEGGi hsa:9743.
UCSCi uc001qez.3. human. [A7KAX9-1 ]

Organism-specific databases

CTDi 9743.
GeneCardsi GC11M128834.
H-InvDB HIX0010264.
HGNCi HGNC:17399. ARHGAP32.
HPAi HPA038389.
MIMi 608541. gene.
neXtProti NX_A7KAX9.
PharmGKBi PA165543138.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG311367.
HOGENOMi HOG000090208.
HOVERGENi HBG108407.
InParanoidi A7KAX9.
OMAi VVSQYDN.
OrthoDBi EOG7WMCHV.
PhylomeDBi A7KAX9.
TreeFami TF351451.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
SignaLinki A7KAX9.

Miscellaneous databases

ChiTaRSi ARHGAP32. human.
EvolutionaryTracei A7KAX9.
GeneWikii RICS_(gene).
GenomeRNAii 9743.
NextBioi 35534637.
PROi A7KAX9.
SOURCEi Search...

Gene expression databases

ArrayExpressi A7KAX9.
Bgeei A7KAX9.
Genevestigatori A7KAX9.

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. "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. 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.

Entry informationi

Entry nameiRHG32_HUMAN
AccessioniPrimary (citable) accession number: A7KAX9
Secondary accession number(s): I7H0B0
, O94820, Q86YL6, Q8IUG4, Q9BWG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: September 11, 2007
Last modified: September 3, 2014
This is version 70 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 11
    Human chromosome 11: 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

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