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A7KAX9

- RHG32_HUMAN

UniProt

A7KAX9 - RHG32_HUMAN

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
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (11 Sep 2007)
      Previous versions | rss
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    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
    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

    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: 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

    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 – 7061Phosphoserine2 Publications
    Modified residuei1203 – 12031Phosphoserine2 Publications

    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

    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.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 – 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.
    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.
    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. 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 263-319, 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

    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 1, 2014
    This is version 71 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