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Q7Z6B7

- SRGP1_HUMAN

UniProt

Q7Z6B7 - SRGP1_HUMAN

Protein

SLIT-ROBO Rho GTPase-activating protein 1

Gene

SRGAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    GTPase-activating protein for RhoA and Cdc42 small GTPases. Together with CDC42 seems to be involved in the pathway mediating the repulsive signaling of Robo and Slit proteins in neuronal migration. SLIT2, probably through interaction with ROBO1, increases the interaction of SRGAP1 with ROBO1 and inactivates CDC42.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. Rho GTPase activator activity Source: Ensembl

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cell migration Source: Ensembl
    3. regulation of small GTPase mediated signal transduction Source: Reactome
    4. Rho protein signal transduction Source: Ensembl
    5. small GTPase mediated signal transduction Source: Reactome

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_19342. Inactivation of Cdc42 and Rac.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SLIT-ROBO Rho GTPase-activating protein 1
    Short name:
    srGAP1
    Alternative name(s):
    Rho GTPase-activating protein 13
    Gene namesi
    Name:SRGAP1
    Synonyms:ARHGAP13, KIAA1304
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:17382. SRGAP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134887956.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10851085SLIT-ROBO Rho GTPase-activating protein 1PRO_0000056765Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei999 – 9991Phosphoserine1 Publication
    Modified residuei1001 – 10011Phosphothreonine1 Publication
    Modified residuei1032 – 10321Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ7Z6B7.
    PaxDbiQ7Z6B7.
    PRIDEiQ7Z6B7.

    PTM databases

    PhosphoSiteiQ7Z6B7.

    Expressioni

    Tissue specificityi

    Expressed in brain, lung, kidney, and testis.1 Publication

    Gene expression databases

    ArrayExpressiQ7Z6B7.
    BgeeiQ7Z6B7.
    CleanExiHS_SRGAP1.
    GenevestigatoriQ7Z6B7.

    Organism-specific databases

    HPAiHPA052416.

    Interactioni

    Subunit structurei

    Homodimer Probable. Forms a heterooligomer with SRGAP2 and SRGAP3 through its F-BAR domain. Interacts with ROBO1, CDC42 and RHOA. Interacts with FASLG.2 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428584EBI-2481729,EBI-466029

    Protein-protein interaction databases

    BioGridi121583. 4 interactions.
    IntActiQ7Z6B7. 3 interactions.
    MINTiMINT-3308471.
    STRINGi9606.ENSP00000347198.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7Z6B7.
    SMRiQ7Z6B7. Positions 482-694, 745-799.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 8766FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini506 – 694189Rho-GAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini743 – 80260SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 516516F-BAR domainAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili351 – 39040Sequence AnalysisAdd
    BLAST
    Coiled coili956 – 98530Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi854 – 8574Poly-Pro
    Compositional biasi909 – 9124Poly-Arg
    Compositional biasi1027 – 10326Poly-Ser

    Domaini

    The F-BAR domain mediates oligomerization, binds membranes, and constrains plasma membrane protrusions.1 Publication

    Sequence similaritiesi

    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG264793.
    HOGENOMiHOG000039980.
    HOVERGENiHBG051637.
    InParanoidiQ7Z6B7.
    KOiK07526.
    OMAiADKSCTM.
    OrthoDBiEOG7966FQ.
    PhylomeDBiQ7Z6B7.
    TreeFamiTF315892.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    InterProiIPR001060. FCH_dom.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00611. FCH. 1 hit.
    PF00620. RhoGAP. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    SMARTiSM00055. FCH. 1 hit.
    SM00324. RhoGAP. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEiPS50133. FCH. 1 hit.
    PS50238. 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: Q7Z6B7-1) [UniParc]FASTAAdd to Basket

    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

    MSTPSRFKKD KEIIAEYESQ VKEIRAQLVE QQKCLEQQTE MRVQLLQDLQ     50
    DFFRKKAEIE TEYSRNLEKL AERFMAKTRS TKDHQQYKKD QNLLSPVNCW 100
    YLLLNQVRRE SKDHATLSDI YLNNVIMRFM QISEDSTRMF KKSKEIAFQL 150
    HEDLMKVLNE LYTVMKTYHM YHAESISAES KLKEAEKQEE KQIGRSGDPV 200
    FHIRLEERHQ RRSSVKKIEK MKEKRQAKYS ENKLKSIKAR NEYLLTLEAT 250
    NASVFKYYIH DLSDLIDCCD LGYHASLNRA LRTYLSAEYN LETSRHEGLD 300
    IIENAVDNLE PRSDKQRFME MYPAAFCPPM KFEFQSHMGD EVCQVSAQQP 350
    VQAELMLRYQ QLQSRLATLK IENEEVKKTT EATLQTIQDM VTIEDYDVSE 400
    CFQHSRSTES VKSTVSETYL SKPSIAKRRA NQQETEQFYF MKLREYLEGS 450
    NLITKLQAKH DLLQRTLGEG HRAEYMTTRP PNVPPKPQKH RKSRPRSQYN 500
    TKLFNGDLET FVKDSGQVIP LIVESCIRFI NLYGLQHQGI FRVSGSQVEV 550
    NDIKNSFERG ENPLADDQSN HDINSVAGVL KLYFRGLENP LFPKERFNDL 600
    ISCIRIDNLY ERALHIRKLL LTLPRSVLIV MRYLFAFLNH LSQYSDENMM 650
    DPYNLAICFG PTLMPVPEIQ DQVSCQAHVN EIIKTIIIHH ETIFPDAKEL 700
    DGPVYEKCMA GDDYCDSPYS EHGTLEEVDQ DAGTEPHTSE DECEPIEAIA 750
    KFDYVGRSAR ELSFKKGASL LLYHRASEDW WEGRHNGIDG LVPHQYIVVQ 800
    DMDDTFSDTL SQKADSEASS GPVTEDKSSS KDMNSPTDRH PDGYLARQRK 850
    RGEPPPPVRR PGRTSDGHCP LHPPHALSNS SVDLGSPSLA SHPRGLLQNR 900
    GLNNDSPERR RRPGHGSLTN ISRHDSLKKI DSPPIRRSTS SGQYTGFNDH 950
    KPLDPETIAQ DIEETMNTAL NELRELERQS TAKHAPDVVL DTLEQVKNSP 1000
    TPATSTESLS PLHNVALRSS EPQIRRSTSS SSDTMSTFKP MVAPRMGVQL 1050
    KPPALRPKPA VLPKTNPTIG PAPPPQGPTD KSCTM 1085
    Length:1,085
    Mass (Da):124,264
    Last modified:October 1, 2003 - v1
    Checksum:iD7ED1F651344F0D9
    GO
    Isoform 2 (identifier: Q7Z6B7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         479-513: RPPNVPPKPQKHRKSRPRSQYNTKLFNGDLETFVK → SRGRRNSHTRHQ

    Note: No experimental confirmation available.

    Show »
    Length:1,062
    Mass (Da):121,594
    Checksum:iC9872F6AA2825358
    GO

    Sequence cautioni

    The sequence BAA92542.1 differs from that shown. Reason: Intron retention.
    The sequence BAA92542.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei479 – 51335RPPNV…ETFVK → SRGRRNSHTRHQ in isoform 2. 1 PublicationVSP_010580Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC053903 mRNA. Translation: AAH53903.1.
    AB037725 mRNA. Translation: BAA92542.1. Different initiation.
    CCDSiCCDS8967.1. [Q7Z6B7-1]
    PIRiG59436.
    RefSeqiNP_065813.1. NM_020762.2. [Q7Z6B7-1]
    XP_005269099.1. XM_005269042.1. [Q7Z6B7-2]
    UniGeneiHs.210751.
    Hs.593803.

    Genome annotation databases

    EnsembliENST00000355086; ENSP00000347198; ENSG00000196935. [Q7Z6B7-1]
    GeneIDi57522.
    KEGGihsa:57522.
    UCSCiuc010ssp.1. human. [Q7Z6B7-1]

    Polymorphism databases

    DMDMi48428624.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC053903 mRNA. Translation: AAH53903.1 .
    AB037725 mRNA. Translation: BAA92542.1 . Different initiation.
    CCDSi CCDS8967.1. [Q7Z6B7-1 ]
    PIRi G59436.
    RefSeqi NP_065813.1. NM_020762.2. [Q7Z6B7-1 ]
    XP_005269099.1. XM_005269042.1. [Q7Z6B7-2 ]
    UniGenei Hs.210751.
    Hs.593803.

    3D structure databases

    ProteinModelPortali Q7Z6B7.
    SMRi Q7Z6B7. Positions 482-694, 745-799.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121583. 4 interactions.
    IntActi Q7Z6B7. 3 interactions.
    MINTi MINT-3308471.
    STRINGi 9606.ENSP00000347198.

    PTM databases

    PhosphoSitei Q7Z6B7.

    Polymorphism databases

    DMDMi 48428624.

    Proteomic databases

    MaxQBi Q7Z6B7.
    PaxDbi Q7Z6B7.
    PRIDEi Q7Z6B7.

    Protocols and materials databases

    DNASUi 57522.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355086 ; ENSP00000347198 ; ENSG00000196935 . [Q7Z6B7-1 ]
    GeneIDi 57522.
    KEGGi hsa:57522.
    UCSCi uc010ssp.1. human. [Q7Z6B7-1 ]

    Organism-specific databases

    CTDi 57522.
    GeneCardsi GC12P064238.
    HGNCi HGNC:17382. SRGAP1.
    HPAi HPA052416.
    MIMi 606523. gene.
    neXtProti NX_Q7Z6B7.
    PharmGKBi PA134887956.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264793.
    HOGENOMi HOG000039980.
    HOVERGENi HBG051637.
    InParanoidi Q7Z6B7.
    KOi K07526.
    OMAi ADKSCTM.
    OrthoDBi EOG7966FQ.
    PhylomeDBi Q7Z6B7.
    TreeFami TF315892.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_19342. Inactivation of Cdc42 and Rac.

    Miscellaneous databases

    ChiTaRSi SRGAP1. human.
    GeneWikii SRGAP1.
    GenomeRNAii 57522.
    NextBioi 63902.
    PROi Q7Z6B7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z6B7.
    Bgeei Q7Z6B7.
    CleanExi HS_SRGAP1.
    Genevestigatori Q7Z6B7.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    InterProi IPR001060. FCH_dom.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00611. FCH. 1 hit.
    PF00620. RhoGAP. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    SMARTi SM00055. FCH. 1 hit.
    SM00324. RhoGAP. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS50238. RHOGAP. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 1).
      Tissue: Uterus.
    2. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-1085 (ISOFORM 2).
      Tissue: Brain.
    3. "Signal transduction in neuronal migration: roles of GTPase activating proteins and the small GTPase Cdc42 in the Slit-Robo pathway."
      Wong K., Ren X.R., Huang Y.Z., Xie Y., Liu G., Saito H., Tang H., Wen L., Brady-Kalnay S.M., Mei L., Wu J.Y., Xiong W.C., Rao Y.
      Cell 107:209-221(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH ROBO1; CDC42 AND RHOA.
    4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-999; THR-1001 AND SER-1032, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "The F-BAR domains from srGAP1, srGAP2, and srGAP3 differentially regulate membrane deformation."
      Coutinho-Budd J., Ghukasyan V., Zylka M.J., Polleux F.
      J. Cell Sci. 125:3390-3401(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: HETEROOLIGOMERIZATION, DOMAIN F-BAR.

    Entry informationi

    Entry nameiSRGP1_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z6B7
    Secondary accession number(s): Q9H8A3, Q9P2P2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 111 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3