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Protein

SLIT-ROBO Rho GTPase-activating protein 2

Gene

Srgap2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RAC1 GTPase activating protein (GAP) that binds and deforms membranes, and regulates actin dynamics to regulate cell migration and differentiation. Plays an important role in different aspects of neuronal morphogenesis and migration mainly during development of the cerebral cortex. This includes the biogenesis of neurites, where it is required for both axons and dendrites outgrowth, and the maturation of the dendritic spines. Also stimulates the branching of the leading process and negatively regulates neuron radial migration in the cerebral cortex. May play a role for cognition, learning and memory. In non-neuronal cells, it may also play a role in cell migration by regulating the formation of lamellipodia and filopodia.2 Publications

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • Rac GTPase binding Source: UniProtKB

GO - Biological processi

  • actin filament severing Source: UniProtKB
  • dendritic spine development Source: UniProtKB
  • extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration Source: UniProtKB
  • filopodium assembly Source: UniProtKB
  • lamellipodium assembly involved in ameboidal cell migration Source: MGI
  • negative regulation of cell migration Source: GO_Central
  • negative regulation of neuron migration Source: UniProtKB
  • neuron projection morphogenesis Source: UniProtKB
  • positive regulation of GTPase activity Source: UniProtKB
  • signal transduction Source: InterPro
  • substrate adhesion-dependent cell spreading Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
SLIT-ROBO Rho GTPase-activating protein 2
Short name:
srGAP2
Alternative name(s):
Formin-binding protein 2
Formin-binding protein 27
Short name:
FBP-27
Gene namesi
Name:Srgap2
Synonyms:Fbp27, Fnbp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:109605. Srgap2.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • dendritic spine head Source: UniProtKB
  • lamellipodium Source: MGI
  • mitochondrial inner membrane Source: MGI
  • nucleoplasm Source: MGI
  • phagocytic vesicle Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • postsynaptic density Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

Mice are viable and show no abnormality of cortical lamination. However, a delay in dendritic spine maturation coupled to an increase in spine neck and spine density is observed.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi527R → L: Unable to stimulate RAC1 GTPase activity and to induce neurite branching. No effect on filopodia biogenesis and neurite outgrowth. 1 Publication1
Mutagenesisi765W → A: Loss of the ability to induce filopodia and to initiate neurite outgrowht. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000567681 – 1071SLIT-ROBO Rho GTPase-activating protein 2Add BLAST1071

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei206PhosphoserineBy similarity1
Modified residuei427PhosphoserineBy similarity1
Modified residuei500PhosphoserineCombined sources1
Modified residuei691PhosphoserineBy similarity1
Modified residuei695PhosphoserineCombined sources1
Modified residuei795PhosphoserineBy similarity1
Modified residuei916PhosphoserineBy similarity1
Modified residuei927Omega-N-methylated arginine; by PRMT5By similarity1
Modified residuei930PhosphoserineBy similarity1
Modified residuei990PhosphoserineCombined sources1
Modified residuei994PhosphoserineBy similarity1
Modified residuei1013PhosphoserineBy similarity1
Modified residuei1027PhosphoserineBy similarity1

Post-translational modificationi

Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiQ91Z67.
MaxQBiQ91Z67.
PaxDbiQ91Z67.
PeptideAtlasiQ91Z67.
PRIDEiQ91Z67.

PTM databases

iPTMnetiQ91Z67.
PhosphoSitePlusiQ91Z67.

Expressioni

Developmental stagei

Expressed throughout cortical development culminating at P1. Expression is reduced but still present in the adult cortex. Expressed in the cortical wall both in neuronal progenitors in the ventricular zone and post-mitotic neurons in the cortical plate (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000026425.
CleanExiMM_SRGAP2.
ExpressionAtlasiQ91Z67. baseline and differential.
GenevisibleiQ91Z67. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with FASLG (By similarity). Interacts with PRMT5 (By similarity). Probably interacts with ROBO1 and ROBO2. Interacts with RAC1; specifically stimulates RAC1 GTPase activity. Interacts (via SH3 domain) with FMNL1 (activated by RAC1); regulates the actin filament severing activity of FMNL1. Interacts (via SH3 domain) with FMNL3. Interacts (via SH3 domain) with GPHN.By similarity3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • Rac GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi199721. 1 interactor.
STRINGi10090.ENSMUSP00000095195.

Structurei

3D structure databases

ProteinModelPortaliQ91Z67.
SMRiQ91Z67.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 325F-BARPROSITE-ProRule annotationAdd BLAST304
Domaini489 – 679Rho-GAPPROSITE-ProRule annotationAdd BLAST191
Domaini728 – 787SH3PROSITE-ProRule annotationAdd BLAST60

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili363 – 401Sequence analysisAdd BLAST39
Coiled coili940 – 968Sequence analysisAdd BLAST29

Domaini

The F-BAR domain mediates oligomerization, binds membranes, and induces plasma membrane protrusions.

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.
ENOG4110QCJ. LUCA.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000039980.
HOVERGENiHBG051637.
InParanoidiQ91Z67.
KOiK07526.
OMAiGESQKTD.
OrthoDBiEOG091G0113.
PhylomeDBiQ91Z67.
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.
IPR030252. srGAP2.
[Graphical view]
PANTHERiPTHR14166:SF6. PTHR14166:SF6. 1 hit.
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.

Q91Z67-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ
60 70 80 90 100
DFFRKKAEIE MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN
110 120 130 140 150
LLLNQVKRES RDHTTLSDIY LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ
160 170 180 190 200
DDLMKVLNEL YSVMKTYHMY NADSISAQSK LKEAEKQEEK QIGKSVKQED
210 220 230 240 250
RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT ENKLKAIKAR
260 270 280 290 300
NEYLLALEAT NASVFKYYIH DLSDIIDQCC DLGYHASLNR ALRTFLSAEL
310 320 330 340 350
NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG
360 370 380 390 400
DMASQLCAQQ PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD
410 420 430 440 450
IVTVEDFDVS DCFQYSNSME SVKSTVSETF MSKPSIAKRR ANQQETEQFY
460 470 480 490 500
FTKMKEYLEG RNLITKLQAK HDLLQKTLGE SQRTDCSLAR RSSTVRKQDS
510 520 530 540 550
SQAIPLVVES CIRFISRHGL QHEGIFRVSG SQVEVNDIKN AFERGEDPLA
560 570 580 590 600
GDQNDHDMDS IAGVLKLYFR GLEHPLFPKD IFHDLIACVT MDNLQERAVH
610 620 630 640 650
IRKVLLVLPK PTLIIMRYLF AFLNHLSQFS EENMMDPYNL AICFGPSLMS
660 670 680 690 700
VPEGHDQVSC QAHVNELIKT IIIQHENIFP NPRELEGPIY SRGGSMEDYC
710 720 730 740 750
DSTHGETTSA EDSTQDVTAE HHTSDDECEP IEAIAKFDYV GRTARELSFK
760 770 780 790 800
KGASLLLYQR ASDDWWEGRH NGIDGLIPHQ YIVVQDTEDG VVERSSPKSE
810 820 830 840 850
IEVMSEPPEE KVTARTGASC PSGGHVADIY LANINKQRKR PESGSIRKAF
860 870 880 890 900
RSDSHGLGSS LTDSSSLGVG ASCRPSSQPI MSQNLPKEGP DKCSISGHGS
910 920 930 940 950
LNSISRHSSL KNRMDSPQIR KTATAGRSKS FNNHRPMDPE VIAQDIEATM
960 970 980 990 1000
NSALNELQEL ERQSSAKHTP DVVLDTLEPL KTSPVVAPTS EPSSPLHTQL
1010 1020 1030 1040 1050
LKDPEPAFQR SASTAGDIAC AFRPVKSVKM AAPVKPPATR PKPTVFPKTN
1060 1070
ATSPGVNSSA SPQATDKSCT V
Length:1,071
Mass (Da):120,798
Last modified:January 9, 2007 - v2
Checksum:i9093C63476BA605D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti598A → V in AAL27032 (PubMed:11672528).Curated1
Sequence conflicti612T → S in AAL27032 (PubMed:11672528).Curated1
Sequence conflicti662A → S in AAL27032 (PubMed:11672528).Curated1
Sequence conflicti737F → C in AAL27032 (PubMed:11672528).Curated1
Sequence conflicti765W → L in AAL27032 (PubMed:11672528).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC109299 Genomic DNA. No translation available.
AC120217 Genomic DNA. No translation available.
AC165436 Genomic DNA. No translation available.
BC151081 mRNA. Translation: AAI51082.1.
BC151082 mRNA. Translation: AAI51083.1.
BC158055 mRNA. Translation: AAI58056.1.
BC172152 mRNA. Translation: AAI72152.1.
AY057900 mRNA. Translation: AAL27032.1.
AK132220 mRNA. Translation: BAE21041.1.
U40752 mRNA. Translation: AAC52480.1.
CCDSiCCDS48355.1.
PIRiS64712.
RefSeqiNP_001074480.2. NM_001081011.2.
XP_006529197.1. XM_006529134.3.
UniGeneiMm.276259.

Genome annotation databases

EnsembliENSMUST00000097588; ENSMUSP00000095195; ENSMUSG00000026425.
GeneIDi14270.
KEGGimmu:14270.
UCSCiuc007cng.2. mouse.

Cross-referencesi

Web resourcesi

Protein Spotlight

Branching out - Issue 143 of October 2012

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC109299 Genomic DNA. No translation available.
AC120217 Genomic DNA. No translation available.
AC165436 Genomic DNA. No translation available.
BC151081 mRNA. Translation: AAI51082.1.
BC151082 mRNA. Translation: AAI51083.1.
BC158055 mRNA. Translation: AAI58056.1.
BC172152 mRNA. Translation: AAI72152.1.
AY057900 mRNA. Translation: AAL27032.1.
AK132220 mRNA. Translation: BAE21041.1.
U40752 mRNA. Translation: AAC52480.1.
CCDSiCCDS48355.1.
PIRiS64712.
RefSeqiNP_001074480.2. NM_001081011.2.
XP_006529197.1. XM_006529134.3.
UniGeneiMm.276259.

3D structure databases

ProteinModelPortaliQ91Z67.
SMRiQ91Z67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199721. 1 interactor.
STRINGi10090.ENSMUSP00000095195.

PTM databases

iPTMnetiQ91Z67.
PhosphoSitePlusiQ91Z67.

Proteomic databases

EPDiQ91Z67.
MaxQBiQ91Z67.
PaxDbiQ91Z67.
PeptideAtlasiQ91Z67.
PRIDEiQ91Z67.

Protocols and materials databases

DNASUi14270.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000097588; ENSMUSP00000095195; ENSMUSG00000026425.
GeneIDi14270.
KEGGimmu:14270.
UCSCiuc007cng.2. mouse.

Organism-specific databases

CTDi23380.
MGIiMGI:109605. Srgap2.

Phylogenomic databases

eggNOGiKOG3565. Eukaryota.
ENOG4110QCJ. LUCA.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000039980.
HOVERGENiHBG051637.
InParanoidiQ91Z67.
KOiK07526.
OMAiGESQKTD.
OrthoDBiEOG091G0113.
PhylomeDBiQ91Z67.
TreeFamiTF315892.

Miscellaneous databases

ChiTaRSiSrgap2. mouse.
PROiQ91Z67.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026425.
CleanExiMM_SRGAP2.
ExpressionAtlasiQ91Z67. baseline and differential.
GenevisibleiQ91Z67. 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.
IPR030252. srGAP2.
[Graphical view]
PANTHERiPTHR14166:SF6. PTHR14166:SF6. 1 hit.
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...

Entry informationi

Entry nameiSRGP2_MOUSE
AccessioniPrimary (citable) accession number: Q91Z67
Secondary accession number(s): B2RY13, Q3V1V8, Q61054
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 9, 2007
Last modified: November 30, 2016
This is version 125 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  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.