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Q91Z67 (SRGP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Srgap2
Synonyms:Fbp27, Fnbp2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1071 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.9

Subunit structure

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. Ref.6 Ref.7 Ref.8

Subcellular location

Cell membrane By similarity. Cell projectiondendritic spine By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell junctionsynapsepostsynaptic cell membrane. Cell projectionlamellipodium By similarity. Cytoplasmic vesiclephagosome. Nucleus By similarity. Cytoplasm By similarity. Note: Recruited to actin-rich phagosomes during phagocytosis. Translocates from nucleus to cytoplasm during development By similarity. Ref.7 Ref.9

Developmental stage

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). Ref.6

Domain

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

Post-translational modification

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

Disruption phenotype

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. Ref.9

Sequence similarities

Contains 1 FCH domain.

Contains 1 Rho-GAP domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processNeurogenesis
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Membrane
Nucleus
Postsynaptic cell membrane
Synapse
   DomainCoiled coil
SH3 domain
   Molecular functionGTPase activation
   PTMMethylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament severing

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine development

Inferred from mutant phenotype Ref.9. Source: UniProtKB

extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration

Inferred from mutant phenotype Ref.6. Source: UniProtKB

filopodium assembly

Inferred from direct assay Ref.6. Source: UniProtKB

negative regulation of neuron migration

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection morphogenesis

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of Rac GTPase activity

Inferred from direct assay Ref.6. Source: UniProtKB

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Inferred from direct assay Ref.7. Source: UniProtKB

dendritic spine head

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

phagocytic vesicle

Inferred from direct assay Ref.7. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.6. Source: UniProtKB

postsynaptic density

Inferred from direct assay Ref.9. Source: UniProtKB

postsynaptic membrane

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionRac GTPase activator activity

Inferred from direct assay Ref.6. Source: UniProtKB

Rac GTPase binding

Inferred from direct assay Ref.6. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10711071SLIT-ROBO Rho GTPase-activating protein 2
PRO_0000056768

Regions

Domain22 – 8766FCH
Domain489 – 679191Rho-GAP
Domain728 – 78760SH3
Region1 – 502502F-BAR domain By similarity
Coiled coil363 – 40139 Potential
Coiled coil940 – 96829 Potential

Amino acid modifications

Modified residue9271Omega-N-methylated arginine; by PRMT5 By similarity
Modified residue9301Phosphoserine By similarity

Experimental info

Mutagenesis5271R → L: Unable to stimulate RAC1 GTPase activity and to induce neurite branching. No effect on filopodia biogenesis and neurite outgrowth. Ref.6
Mutagenesis7651W → A: Loss of the ability to induce filopodia and to initiate neurite outgrowht. Ref.6
Sequence conflict5981A → V in AAL27032. Ref.3
Sequence conflict6121T → S in AAL27032. Ref.3
Sequence conflict6621A → S in AAL27032. Ref.3
Sequence conflict7371F → C in AAL27032. Ref.3
Sequence conflict7651W → L in AAL27032. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q91Z67 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: 9093C63476BA605D

FASTA1,071120,798
        10         20         30         40         50         60 
MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ DFFRKKAEIE 

        70         80         90        100        110        120 
MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN LLLNQVKRES RDHTTLSDIY 

       130        140        150        160        170        180 
LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ DDLMKVLNEL YSVMKTYHMY NADSISAQSK 

       190        200        210        220        230        240 
LKEAEKQEEK QIGKSVKQED RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT 

       250        260        270        280        290        300 
ENKLKAIKAR NEYLLALEAT NASVFKYYIH DLSDIIDQCC DLGYHASLNR ALRTFLSAEL 

       310        320        330        340        350        360 
NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG DMASQLCAQQ 

       370        380        390        400        410        420 
PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD IVTVEDFDVS DCFQYSNSME 

       430        440        450        460        470        480 
SVKSTVSETF MSKPSIAKRR ANQQETEQFY FTKMKEYLEG RNLITKLQAK HDLLQKTLGE 

       490        500        510        520        530        540 
SQRTDCSLAR RSSTVRKQDS SQAIPLVVES CIRFISRHGL QHEGIFRVSG SQVEVNDIKN 

       550        560        570        580        590        600 
AFERGEDPLA GDQNDHDMDS IAGVLKLYFR GLEHPLFPKD IFHDLIACVT MDNLQERAVH 

       610        620        630        640        650        660 
IRKVLLVLPK PTLIIMRYLF AFLNHLSQFS EENMMDPYNL AICFGPSLMS VPEGHDQVSC 

       670        680        690        700        710        720 
QAHVNELIKT IIIQHENIFP NPRELEGPIY SRGGSMEDYC DSTHGETTSA EDSTQDVTAE 

       730        740        750        760        770        780 
HHTSDDECEP IEAIAKFDYV GRTARELSFK KGASLLLYQR ASDDWWEGRH NGIDGLIPHQ 

       790        800        810        820        830        840 
YIVVQDTEDG VVERSSPKSE IEVMSEPPEE KVTARTGASC PSGGHVADIY LANINKQRKR 

       850        860        870        880        890        900 
PESGSIRKAF RSDSHGLGSS LTDSSSLGVG ASCRPSSQPI MSQNLPKEGP DKCSISGHGS 

       910        920        930        940        950        960 
LNSISRHSSL KNRMDSPQIR KTATAGRSKS FNNHRPMDPE VIAQDIEATM NSALNELQEL 

       970        980        990       1000       1010       1020 
ERQSSAKHTP DVVLDTLEPL KTSPVVAPTS EPSSPLHTQL LKDPEPAFQR SASTAGDIAC 

      1030       1040       1050       1060       1070 
AFRPVKSVKM AAPVKPPATR PKPTVFPKTN ATSPGVNSSA SPQATDKSCT V 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"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].
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: NUCLEOTIDE SEQUENCE [MRNA] OF 432-836.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1071.
Strain: C57BL/6J.
Tissue: Brain.
[5]"Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains."
Chan D.C., Bedford M.T., Leder P.
EMBO J. 15:1045-1054(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 732-782.
Strain: FVB.
[6]"The F-BAR domain of srGAP2 induces membrane protrusions required for neuronal migration and morphogenesis."
Guerrier S., Coutinho-Budd J., Sassa T., Gresset A., Jordan N.V., Chen K., Jin W.L., Frost A., Polleux F.
Cell 138:990-1004(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NEURON MIGRATION AND MORPHOGENESIS, DEVELOPMENTAL STAGE, SUBUNIT, INTERACTION WITH RAC1, MUTAGENESIS OF ARG-527 AND TRP-765.
[7]"Bi-modal regulation of a formin by srGAP2."
Mason F.M., Heimsath E.G., Higgs H.N., Soderling S.H.
J. Biol. Chem. 286:6577-6586(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FMNL1; FMNL3 AND ROBO2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"SH3 domain-based phototrapping in living cells reveals Rho family GAP signaling complexes."
Okada H., Uezu A., Mason F.M., Soderblom E.J., Moseley M.A. III, Soderling S.H.
Sci. Signal. 4:RS13-RS13(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GPHN.
[9]"Inhibition of SRGAP2 function by its human-specific paralogs induces neoteny during spine maturation."
Charrier C., Joshi K., Coutinho-Budd J., Kim J.E., Lambert N., de Marchena J., Jin W.L., Vanderhaeghen P., Ghosh A., Sassa T., Polleux F.
Cell 149:923-935(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DENDRITIC SPINE MATURATION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Branching out - Issue 143 of October 2012

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS64712.
RefSeqNP_001074480.2. NM_001081011.2.
XP_006529197.1. XM_006529134.1.
XP_006529198.1. XM_006529135.1.
UniGeneMm.276259.

3D structure databases

ProteinModelPortalQ91Z67.
SMRQ91Z67. Positions 723-787.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199721. 1 interaction.

PTM databases

PhosphoSiteQ91Z67.

Proteomic databases

PaxDbQ91Z67.
PRIDEQ91Z67.

Protocols and materials databases

DNASU14270.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000097588; ENSMUSP00000095195; ENSMUSG00000026425.
GeneID14270.
KEGGmmu:14270.
UCSCuc007cng.2. mouse.

Organism-specific databases

CTD23380.
MGIMGI:109605. Srgap2.

Phylogenomic databases

eggNOGNOG264793.
GeneTreeENSGT00710000106292.
HOGENOMHOG000039980.
HOVERGENHBG051637.
KOK07526.
OMAANVRIEE.
OrthoDBEOG7966FQ.
PhylomeDBQ91Z67.
TreeFamTF315892.

Gene expression databases

BgeeQ91Z67.
CleanExMM_SRGAP2.
GenevestigatorQ91Z67.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
InterProIPR001060. FCH_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00611. FCH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTSM00055. FCH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEPS50133. FCH. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSRGAP2. mouse.
NextBio285639.
PROQ91Z67.
SOURCESearch...

Entry information

Entry nameSRGP2_MOUSE
AccessionPrimary (citable) accession number: Q91Z67
Secondary accession number(s): B2RY13, Q3V1V8, Q61054
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot