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Protein

SLIT-ROBO Rho GTPase-activating protein 1

Gene

Srgap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Molecular functioni

  • GTPase activator activity Source: MGI
  • Rho GTPase binding Source: MGI

GO - Biological processi

  • cell migration Source: MGI
  • positive regulation of GTPase activity Source: GOC
  • Rho protein signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2152936. Srgap1.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: GOC
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10621062SLIT-ROBO Rho GTPase-activating protein 1PRO_0000056766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei976 – 9761PhosphoserineBy similarity
Modified residuei978 – 9781PhosphothreonineBy similarity
Modified residuei1009 – 10091PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ91Z69.
MaxQBiQ91Z69.
PaxDbiQ91Z69.
PRIDEiQ91Z69.

PTM databases

PhosphoSiteiQ91Z69.

Expressioni

Gene expression databases

BgeeiQ91Z69.
CleanExiMM_SRGAP1.
ExpressionAtlasiQ91Z69. baseline and differential.
GenevisibleiQ91Z69. MM.

Interactioni

Subunit structurei

Homodimer (Probable). Forms a heterooligomer with SRGAP2 and SRGAP3 through its F-BAR domain. Interacts with CDC42 and RHOA. Interacts with FASLG (By similarity). Interacts (via SH3 domain) with ROBO1.By similarityCurated1 Publication

GO - Molecular functioni

  • Rho GTPase binding Source: MGI

Protein-protein interaction databases

BioGridi228239. 4 interactions.
STRINGi10090.ENSMUSP00000080389.

Structurei

Secondary structure

1
1062
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi725 – 7295Combined sources
Beta strandi746 – 7549Combined sources
Beta strandi757 – 7626Combined sources
Beta strandi765 – 7706Combined sources
Helixi771 – 7733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GNCX-ray1.80A/B725-776[»]
ProteinModelPortaliQ91Z69.
SMRiQ91Z69. Positions 722-776.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91Z69.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 314296F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini481 – 671191Rho-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini720 – 77960SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili352 – 38231Sequence analysisAdd
BLAST
Coiled coili933 – 96028Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi831 – 8344Poly-Pro
Compositional biasi886 – 8894Poly-Arg
Compositional biasi1004 – 10096Poly-Ser

Domaini

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

Sequence similaritiesi

Contains 1 F-BAR 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

eggNOGiKOG3565. Eukaryota.
ENOG410XS44. LUCA.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000039980.
HOVERGENiHBG051637.
InParanoidiQ91Z69.
KOiK07526.
OrthoDBiEOG7966FQ.
TreeFamiTF315892.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00018. SH3_1. 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.
PROSITEiPS51741. F_BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91Z69-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPSRFKKD KEIIAEYESQ VKEIRAQLVE QQKCLEQQTE MRVQLLQDLQ
60 70 80 90 100
DFFRKKAEIE TEYSRNLEKL AERFMAKTRS TKDHQQFKKD QNLLSPVNCW
110 120 130 140 150
YLLLNQVRRE SKDHATLSDI YLNNVIMRFM QISEDSTRMF KKSKEIAFQL
160 170 180 190 200
HEDLMKVLNE LYTVMKTYHM YHSESISAES 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
VQAELMLRNQ QLQSRLATLK IESEEVKKTT EATLQTIQDM VTIEDYDVSE
410 420 430 440 450
CFQHSRSTES VKSTVSETYL SKPSIAKRRA NQQETEQFYF MKLREFLEGS
460 470 480 490 500
NLITKLQAKH DLLQRTLGEG HRAEYMTTSR GRRNSHARHQ DSGQVIPLIV
510 520 530 540 550
ESCIRFINLY GLQHQGIFRV SGSQVEVNDI KNSFERGENP LSDEQSNHDI
560 570 580 590 600
NSVAGVLKLY FRGLENPLFP KERFTDLISC IRIDNLYERA LHIRKLLLTL
610 620 630 640 650
PRSVLIVMRY LFAFLNHLSQ YSDENMMDPY NLAICFGPTL MPVPEIQDQV
660 670 680 690 700
SCQAHVNEIV KTIIIHHETI FPDAKELDGP VYEKCMAGGD YCDSPYSEHG
710 720 730 740 750
TLEEVDQDAG TEPHTSEDEC EPIEAIAKFD YVGRSARELS FKKGASLLLY
760 770 780 790 800
HRASEDWWEG RHNGIDGLVP HQYIVVQDMD DTFSDTLSQK ADSEASSGPV
810 820 830 840 850
TEDKSSSKDM NSPTDRHSDS YLARQRKRGE PPPPGRRPGR TSDGHCPLHP
860 870 880 890 900
PHALSNSSID LGSPNLASHP RGLLQNRGLN NDSPERRRRP GHGSLTNISR
910 920 930 940 950
HDSLKKIDSP PIRRSTSSGQ YTGFNDHKPL DPETIAQDIE ETMNTALNEL
960 970 980 990 1000
RELERQSTVK HAPDVVLDTL EQVKNSPTPA TSTESLSPLH NVALRGSEPQ
1010 1020 1030 1040 1050
IRRSTSSSSE TMSTFKPMVA PRMGVQLKPP ALRPKPAVLP KTNPTMGPAA
1060
PSQGPTDKSC TM
Length:1,062
Mass (Da):121,430
Last modified:January 9, 2007 - v2
Checksum:iD0FA749750A9081A
GO

Sequence cautioni

The sequence AAL27030.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti574 – 5741F → V in AAL27030 (PubMed:11672528).Curated
Sequence conflicti721 – 7244EPIE → RGPSR in AAL27030 (PubMed:11672528).Curated
Sequence conflicti797 – 7971S → G in AAL27030 (PubMed:11672528).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC120892 mRNA. Translation: AAI20893.1.
BC120893 mRNA. Translation: AAI20894.1.
AY057898 mRNA. Translation: AAL27030.1. Different initiation.
CCDSiCCDS56751.1.
RefSeqiNP_001229340.1. NM_001242411.1.
UniGeneiMm.288698.

Genome annotation databases

EnsembliENSMUST00000020322; ENSMUSP00000020322; ENSMUSG00000020121.
GeneIDi117600.
KEGGimmu:117600.
UCSCiuc007hgc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC120892 mRNA. Translation: AAI20893.1.
BC120893 mRNA. Translation: AAI20894.1.
AY057898 mRNA. Translation: AAL27030.1. Different initiation.
CCDSiCCDS56751.1.
RefSeqiNP_001229340.1. NM_001242411.1.
UniGeneiMm.288698.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GNCX-ray1.80A/B725-776[»]
ProteinModelPortaliQ91Z69.
SMRiQ91Z69. Positions 722-776.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228239. 4 interactions.
STRINGi10090.ENSMUSP00000080389.

PTM databases

PhosphoSiteiQ91Z69.

Proteomic databases

EPDiQ91Z69.
MaxQBiQ91Z69.
PaxDbiQ91Z69.
PRIDEiQ91Z69.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020322; ENSMUSP00000020322; ENSMUSG00000020121.
GeneIDi117600.
KEGGimmu:117600.
UCSCiuc007hgc.2. mouse.

Organism-specific databases

CTDi57522.
MGIiMGI:2152936. Srgap1.

Phylogenomic databases

eggNOGiKOG3565. Eukaryota.
ENOG410XS44. LUCA.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000039980.
HOVERGENiHBG051637.
InParanoidiQ91Z69.
KOiK07526.
OrthoDBiEOG7966FQ.
TreeFamiTF315892.

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiSrgap1. mouse.
EvolutionaryTraceiQ91Z69.
NextBioi369706.
PROiQ91Z69.
SOURCEiSearch...

Gene expression databases

BgeeiQ91Z69.
CleanExiMM_SRGAP1.
ExpressionAtlasiQ91Z69. baseline and differential.
GenevisibleiQ91Z69. MM.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00018. SH3_1. 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.
PROSITEiPS51741. F_BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

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].
  2. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 353-1062.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. "Structural basis of Robo proline-rich motif recognition by the srGAP1 Src homology 3 domain in the Slit-Robo signaling pathway."
    Li X., Chen Y., Liu Y., Gao J., Gao F., Bartlam M., Wu J.Y., Rao Z.
    J. Biol. Chem. 281:28430-28437(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 725-776, INTERACTION WITH ROBO1.

Entry informationi

Entry nameiSRGP1_MOUSE
AccessioniPrimary (citable) accession number: Q91Z69
Secondary accession number(s): Q08E84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 9, 2007
Last modified: May 11, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.