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Q7Z6B7

- SRGP1_HUMAN

UniProt

Q7Z6B7 - SRGP1_HUMAN

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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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ7Z6B7.
CleanExiHS_SRGAP1.
ExpressionAtlasiQ7Z6B7. baseline and differential.
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.
GeneTreeiENSGT00760000118863.
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

        10         20         30         40         50
MSTPSRFKKD KEIIAEYESQ VKEIRAQLVE QQKCLEQQTE MRVQLLQDLQ
60 70 80 90 100
DFFRKKAEIE TEYSRNLEKL AERFMAKTRS TKDHQQYKKD QNLLSPVNCW
110 120 130 140 150
YLLLNQVRRE SKDHATLSDI YLNNVIMRFM QISEDSTRMF KKSKEIAFQL
160 170 180 190 200
HEDLMKVLNE LYTVMKTYHM YHAESISAES KLKEAEKQEE KQIGRSGDPV
210 220 230 240 250
FHIRLEERHQ RRSSVKKIEK MKEKRQAKYS ENKLKSIKAR NEYLLTLEAT
260 270 280 290 300
NASVFKYYIH DLSDLIDCCD LGYHASLNRA LRTYLSAEYN LETSRHEGLD
310 320 330 340 350
IIENAVDNLE PRSDKQRFME MYPAAFCPPM KFEFQSHMGD EVCQVSAQQP
360 370 380 390 400
VQAELMLRYQ QLQSRLATLK IENEEVKKTT EATLQTIQDM VTIEDYDVSE
410 420 430 440 450
CFQHSRSTES VKSTVSETYL SKPSIAKRRA NQQETEQFYF MKLREYLEGS
460 470 480 490 500
NLITKLQAKH DLLQRTLGEG HRAEYMTTRP PNVPPKPQKH RKSRPRSQYN
510 520 530 540 550
TKLFNGDLET FVKDSGQVIP LIVESCIRFI NLYGLQHQGI FRVSGSQVEV
560 570 580 590 600
NDIKNSFERG ENPLADDQSN HDINSVAGVL KLYFRGLENP LFPKERFNDL
610 620 630 640 650
ISCIRIDNLY ERALHIRKLL LTLPRSVLIV MRYLFAFLNH LSQYSDENMM
660 670 680 690 700
DPYNLAICFG PTLMPVPEIQ DQVSCQAHVN EIIKTIIIHH ETIFPDAKEL
710 720 730 740 750
DGPVYEKCMA GDDYCDSPYS EHGTLEEVDQ DAGTEPHTSE DECEPIEAIA
760 770 780 790 800
KFDYVGRSAR ELSFKKGASL LLYHRASEDW WEGRHNGIDG LVPHQYIVVQ
810 820 830 840 850
DMDDTFSDTL SQKADSEASS GPVTEDKSSS KDMNSPTDRH PDGYLARQRK
860 870 880 890 900
RGEPPPPVRR PGRTSDGHCP LHPPHALSNS SVDLGSPSLA SHPRGLLQNR
910 920 930 940 950
GLNNDSPERR RRPGHGSLTN ISRHDSLKKI DSPPIRRSTS SGQYTGFNDH
960 970 980 990 1000
KPLDPETIAQ DIEETMNTAL NELRELERQS TAKHAPDVVL DTLEQVKNSP
1010 1020 1030 1040 1050
TPATSTESLS PLHNVALRSS EPQIRRSTSS SSDTMSTFKP MVAPRMGVQL
1060 1070 1080
KPPALRPKPA VLPKTNPTIG PAPPPQGPTD KSCTM
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.
GeneTreei ENSGT00760000118863.
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

Bgeei Q7Z6B7.
CleanExi HS_SRGAP1.
ExpressionAtlasi Q7Z6B7. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 112 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