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A7KAX9

- RHG32_HUMAN

UniProt

A7KAX9 - RHG32_HUMAN

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Protein

Rho GTPase-activating protein 32

Gene

ARHGAP32

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).By similarity

GO - Molecular functioni

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

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
Name:ARHGAP32
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.By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. cell cortex Source: Ensembl
  3. cell junction Source: UniProtKB-KW
  4. cell projection Source: UniProtKB-KW
  5. cytosol Source: Reactome
  6. endoplasmic reticulum Source: UniProtKB-KW
  7. endosome Source: UniProtKB-KW
  8. Golgi apparatus Source: UniProtKB-KW
  9. 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).By similarity

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

BgeeiA7KAX9.
ExpressionAtlasiA7KAX9. baseline and differential.
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).By similarity

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 – 3818Combined sources
Helixi387 – 39913Combined sources
Turni403 – 4075Combined sources
Helixi412 – 42312Combined sources
Turni433 – 4375Combined sources
Helixi439 – 45214Combined sources
Turni460 – 4623Combined sources
Helixi463 – 4708Combined sources
Beta strandi472 – 4743Combined sources
Helixi475 – 48612Combined sources
Helixi491 – 50818Combined sources
Helixi511 – 5144Combined sources
Helixi518 – 52912Combined sources
Helixi553 – 5619Combined sources
Helixi563 – 5664Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IUGX-ray1.77A/B367-577[»]
ProteinModelPortaliA7KAX9.
SMRiA7KAX9. Positions 263-321, 368-569.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA7KAX9.

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
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

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.
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

        10         20         30         40         50
METESESSTL GDDSVFWLES EVIIQVTDCE EEEREEKFRK MKSSVHSEED
60 70 80 90 100
DFVPELHRNV HPRERPDWEE TLSAMARGAD VPEIPGDLTL KTCGSTASMK
110 120 130 140 150
VKHVKKLPFT KGHFPKMAEC AHFHYENVEF GSIQLSLSEE QNEVMKNGCE
160 170 180 190 200
SKELVYLVQI ACQGKSWIVK RSYEDFRVLD KHLHLCIYDR RFSQLSELPR
210 220 230 240 250
SDTLKDSPES VTQMLMAYLS RLSAIAGNKI 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 NHVDVLFSGR ISMAMQEGAA SLSRPKSLLV SSPSTKLLTL
610 620 630 640 650
EEAQARTQAQ VNSPIVTENK YIEVGEGPAA LQGKFHTIIE FPLERKRPQN
660 670 680 690 700
KMKKSPVGSW RSFFNLGKSS SVSKRKLQRN ESEPSEMKAM ALKGGRAEGT
710 720 730 740 750
LRSAKSEESL TSLHAVDGDS KLFRPRRPRS SSDALSASFN GEMLGNRCNS
760 770 780 790 800
YDNLPHDNES EEEGGLLHIP ALMSPHSAED VDLSPPDIGV ASLDFDPMSF
810 820 830 840 850
QCSPPKAESE CLESGASFLD SPGYSKDKPS ANKKDAETGS SQCQTPGSTA
860 870 880 890 900
SSEPVSPLQE KLSPFFTLDL SPTEDKSSKP SSFTEKVVYA FSPKIGRKLS
910 920 930 940 950
KSPSMSISEP ISVTLPPRVS EVIGTVSNTT AQNASSSTWD KCVEERDATN
960 970 980 990 1000
RSPTQIVKMK TNETVAQEAY ESEVQPLDQV AAEEVELPGK EDQSVSSSQS
1010 1020 1030 1040 1050
KAVASGQTQT GAVTHDPPQD SVPVSSVSLI PPPPPPKNVA RMLALALAES
1060 1070 1080 1090 1100
AQQASTQSLK RPGTSQAGYT NYGDIAVATT EDNLSSSYSA VALDKAYFQT
1110 1120 1130 1140 1150
DRPAEQFHLQ NNAPGNCDHP LPETTATGDP THSNTTESGE QHHQVDLTGN
1160 1170 1180 1190 1200
QPHQAYLSGD PEKARITSVP LDSEKSDDHV SFPEDQSGKN SMPTVSFLDQ
1210 1220 1230 1240 1250
DQSPPRFYSG DQPPSYLGAS VDKLHHPLEF ADKSPTPPNL PSDKIYPPSG
1260 1270 1280 1290 1300
SPEENTSTAT MTYMTTTPAT AQMSTKEASW DVAEQPTTAD FAAATLQRTH
1310 1320 1330 1340 1350
RTNRPLPPPP SQRSAEQPPV VGQVQAATNI GLNNSHKVQG VVPVPERPPE
1360 1370 1380 1390 1400
PRAMDDPASA FISDSGAAAA QCPMATAVQP GLPEKVRDGA RVPLLHLRAE
1410 1420 1430 1440 1450
SVPAHPCGFP APLPPTRMME SKMIAAIHSS SADATSSSNY HSFVTASSTS
1460 1470 1480 1490 1500
VDDALPLPLP VPQPKHASQK TVYSSFARPD VTTEPFGPDN CLHFNMTPNC
1510 1520 1530 1540 1550
QYRPQSVPPH HNKLEQHQVY GARSEPPASM GLRYNTYVAP GRNASGHHSK
1560 1570 1580 1590 1600
PCSRVEYVSS LSSSVRNTCY PEDIPPYPTI RRVQSLHAPP SSMIRSVPIS
1610 1620 1630 1640 1650
RTEVPPDDEP AYCPRPLYQY KPYQSSQARS DYHVTQLQPY FENGRVHYRY
1660 1670 1680 1690 1700
SPYSSSSSSY YSPDGALCDV DAYGTVQLRP LHRLPNRDFA FYNPRLQGKS
1710 1720 1730 1740 1750
LYSYAGLAPR PRANVTGYFS PNDHNVVSMP PAADVKHTYT SWDLEDMEKY
1760 1770 1780 1790 1800
RMQSIRRESR ARQKVKGPVM SQYDNMTPAV QDDLGGIYVI HLRSKSDPGK
1810 1820 1830 1840 1850
TGLLSVAEGK ESRHAAKAIS PEGEDRFYRR HPEAEMDRAH HHGGHGSTQP
1860 1870 1880 1890 1900
EKPSLPQKQS SLRSRKLPDM GCSLPEHRAH QEASHRQFCE SKNGPPYPQG
1910 1920 1930 1940 1950
AGQLDYGSKG IPDTSEPVSY HNSGVKYAAS GQESLRLNHK EVRLSKEMER
1960 1970 1980 1990 2000
PWVRQPSAPE KHSRDCYKEE EHLTQSIVPP PKPERSHSLK LHHTQNVERD
2010 2020 2030 2040 2050
PSVLYQYQPH GKRQSSVTVV SQYDNLEDYH SLPQHQRGVF GGGGMGTYVP
2060 2070 2080
PGFPHPQSRT YATALGQGAF LPAELSLQHP ETQIHAE
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. 5 PublicationsVSP_034933Add
BLAST
Alternative sequencei1 – 290290Missing in isoform 3. 1 PublicationVSP_034934Add
BLAST
Alternative sequencei567 – 61246FSGRI…QAQVN → LPHFSARTELIVPFPLRLLR KQFTPPLLGPMSPLNPLVQI TVCISI in isoform 3. 1 PublicationVSP_034935Add
BLAST
Alternative sequencei613 – 20871475Missing in isoform 3. 1 PublicationVSP_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 263-321, 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.
GeneTreei ENSGT00720000108475.
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

Bgeei A7KAX9.
ExpressionAtlasi A7KAX9. baseline and differential.
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: October 29, 2014
This is version 72 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