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Protein

Rho GTPase-activating protein 31

Gene

Arhgap31

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

Functioni

Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration.2 Publications

GO - Molecular functioni

  • GTPase activator activity Source: MGI
  • SH3 domain binding Source: MGI

GO - Biological processi

  • small GTPase mediated 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:
Rho GTPase-activating protein 31
Alternative name(s):
Cdc42 GTPase-activating protein
Gene namesi
Name:Arhgap31
Synonyms:Cdgap, Kiaa1204
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1333857. Arhgap31.

Subcellular locationi

GO - Cellular componenti

  • focal adhesion Source: UniProtKB-SubCell
  • intracellular Source: GOC
  • lamellipodium Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561R → A: 70% reduction of GAP activity; when associated with V-169. 1 Publication
Mutagenesisi169 – 1691N → V: 70% reduction of GAP activity; when associated with A-56. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14251425Rho GTPase-activating protein 31PRO_0000320115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei272 – 2721PhosphoserineCombined sources
Modified residuei283 – 2831PhosphothreonineCombined sources
Modified residuei343 – 3431PhosphoserineCombined sources
Modified residuei346 – 3461PhosphoserineCombined sources
Modified residuei384 – 3841PhosphoserineCombined sources
Modified residuei464 – 4641PhosphoserineCombined sources
Modified residuei666 – 6661PhosphothreonineCombined sources
Modified residuei685 – 6851PhosphoserineCombined sources
Modified residuei690 – 6901PhosphoserineCombined sources
Modified residuei765 – 7651PhosphoserineCombined sources
Modified residuei769 – 7691PhosphothreonineCombined sources
Modified residuei776 – 7761Phosphothreonine; by GSK32 Publications
Modified residuei961 – 9611PhosphoserineCombined sources
Modified residuei1092 – 10921PhosphoserineCombined sources
Modified residuei1093 – 10931PhosphoserineCombined sources
Modified residuei1163 – 11631PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on Thr-776 by GSK3; which reduces GAP activity.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiA6X8Z5.
PaxDbiA6X8Z5.
PeptideAtlasiA6X8Z5.
PRIDEiA6X8Z5.

PTM databases

iPTMnetiA6X8Z5.

Expressioni

Tissue specificityi

Expressed at highest levels in heart and lung.1 Publication

Inductioni

By serum (at protein level).1 Publication

Gene expression databases

BgeeiA6X8Z5.
CleanExiMM_CDGAP.
ExpressionAtlasiA6X8Z5. baseline and differential.
GenevisibleiA6X8Z5. MM.

Interactioni

Subunit structurei

Interacts with ITSN1, which inhibits GAP activity. Interacts with PARVA. Interacts with GTP-loaded RHOU (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Itsn1Q9Z0R43EBI-4325995,EBI-645386

GO - Molecular functioni

  • SH3 domain binding Source: MGI

Protein-protein interaction databases

BioGridi198630. 2 interactions.
IntActiA6X8Z5. 1 interaction.
MINTiMINT-8094048.
STRINGi10090.ENSMUSP00000023487.

Structurei

3D structure databases

ProteinModelPortaliA6X8Z5.
SMRiA6X8Z5. Positions 19-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 216196Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi770 – 7778Poly-Pro

Sequence similaritiesi

Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410KCYW. Eukaryota.
ENOG410ZIYP. LUCA.
HOVERGENiHBG105825.
InParanoidiA6X8Z5.
OMAiNTWVTPE.
OrthoDBiEOG7WMCHV.
PhylomeDBiA6X8Z5.
TreeFamiTF351451.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A6X8Z5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNKGAKQKL KRKGAASAFG CDLTEYLESS GQDVPYVLKS CAEFIETHGI
60 70 80 90 100
VDGIYRLSGI TSNIQRLRQE FGSDQCPDLT REVYLQDIHC VGSLCKLYFR
110 120 130 140 150
ELPNPLLTYE LYEKFTEAVS HRPEEGQLAR IQNVILELPP PHYRTLEYLI
160 170 180 190 200
RHLAHIASFS SKTNMHARNL ALVWAPNLLR SKKIEATICN GDAAFLAVRV
210 220 230 240 250
QQVVIEFILN HADQIFNGGA PGALQQDESR TITKSLTLPA LSLPMKLVSL
260 270 280 290 300
EEAQARSLAT NHPARKERRE NSLPEIVPPP FHTVLELPDN KRKLSSKSKK
310 320 330 340 350
WKSIFNLGRS GSDSKSKLSR NGSVFVRGQR LSVEKATIRP AKSMDSLCSV
360 370 380 390 400
PVEGKENKGN FSRTVTTGGF FIPATKMHAS STGSSCDLSK EGEWGQEGMP
410 420 430 440 450
AGAEGGCEVG GQIRPLPEQL KVFRPIGDPE SEQSAPKLLG MFYTSSDSPG
460 470 480 490 500
KSVFTSSLFQ MEPSPRHQRK ALNISEPFAV SVPLRVSAVI STNSTPCRTP
510 520 530 540 550
PKELQSLSSL EEFSFQGSES GGWPEEEKPL GAESFPGSVT KKAATEDTKP
560 570 580 590 600
EPEVPGRAEC SQSPPLDPGT QVEKKTLHVS LGSQVSKEAE KRPKAEKVME
610 620 630 640 650
ESQGASQPKP STPQESLGAG TEPLILHEMD EEDLAQALIW PEIQQELKII
660 670 680 690 700
ESEEEFSSLP PAAQKTSPIP ESSPAPFPFP EAPGSLPSSS APREVWTRDA
710 720 730 740 750
ANQSIQEAAI LTDREKLEPV CSLLESESQQ ELSPDPASLA PLEMLLFEKV
760 770 780 790 800
SSPARIEIGG PRNLSPPLTP APPPPTPLEE EPEVLLSKEG PDREDAARDS
810 820 830 840 850
RTDVYTEQPT PKESPGIPTP CQREEAIASP NEKQNARHAV PENKGPGLPS
860 870 880 890 900
PTKEVDIIPQ EEGGAPHSAQ EPSDCDEDDT VTDPAQHGLE MVEPWEEPQW
910 920 930 940 950
VTSPLHSPTL KEVQESQTQG SQGHRLERRL CHRPSLRQSH SLDSKTTGNS
960 970 980 990 1000
HWTLEAPFSS SCANLETERN YEPLQPPAAR TKIAGLEEKA LKAFREFSGL
1010 1020 1030 1040 1050
KGLEVLPSQK GPSGIQPKPV ETNFMGLAEG KEQEPQLELS NRQMKHSDVP
1060 1070 1080 1090 1100
GPDSSKESSP RAQDSTLPGE HPLQLQLKNT ECGPSKGKHR PSSLNLDSAT
1110 1120 1130 1140 1150
PIADLFRLEN GAPFSSPGIE LSELGDTKVT WMSSSHCKAA PWNSQDTQDL
1160 1170 1180 1190 1200
DIVAHTLTGR RNSAPVSVSA VRTSFMVKMC QAKAVPVIPP KIQYTQIPQP
1210 1220 1230 1240 1250
LPSQSTGEGG AQPLERSQEE PGSTPEIPQK STKDDSPSSL GSPEEEQPKQ
1260 1270 1280 1290 1300
ETGASASRRQ ASITSCMYEG SSCSPEPSAS TLASTQDAVV QCRKRTSETE
1310 1320 1330 1340 1350
PSGDNLLSSK LERASGGPKA FHRSRPGRPQ SLILFPIMDH LPSSPTVIDS
1360 1370 1380 1390 1400
KVLLSPIRSP TQTVSPGLLC GELAENTWIT PEGVTLRNKM TIPKNGQRLE
1410 1420
TSTSCFYQPQ RRSVILDGRS GRQIE
Length:1,425
Mass (Da):155,276
Last modified:August 21, 2007 - v1
Checksum:i00A39A0664D1A558
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti292 – 2921R → K in BAE33406 (PubMed:19468303).Curated
Sequence conflicti1153 – 11531V → F in BAE38872 (PubMed:19468303).Curated
Sequence conflicti1153 – 11531V → F in BAE38901 (PubMed:19468303).Curated
Sequence conflicti1365 – 13651S → C in BAE38872 (PubMed:19468303).Curated
Sequence conflicti1365 – 13651S → C in BAE38901 (PubMed:19468303).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK138417 mRNA. Translation: BAE23651.1.
AK149975 mRNA. Translation: BAE29205.1.
AK150109 mRNA. Translation: BAE29314.1.
AK155729 mRNA. Translation: BAE33406.1.
AK166583 mRNA. Translation: BAE38872.1.
AK166622 mRNA. Translation: BAE38901.1.
CT009576, AC154425 Genomic DNA. Translation: CAO77869.1.
AF151363 mRNA. Translation: AAD38043.1.
AK129309 mRNA. Translation: BAC98119.1.
CCDSiCCDS28172.1.
RefSeqiNP_064656.2. NM_020260.2.
UniGeneiMm.370848.

Genome annotation databases

EnsembliENSMUST00000023487; ENSMUSP00000023487; ENSMUSG00000022799.
GeneIDi12549.
KEGGimmu:12549.
UCSCiuc007zfg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK138417 mRNA. Translation: BAE23651.1.
AK149975 mRNA. Translation: BAE29205.1.
AK150109 mRNA. Translation: BAE29314.1.
AK155729 mRNA. Translation: BAE33406.1.
AK166583 mRNA. Translation: BAE38872.1.
AK166622 mRNA. Translation: BAE38901.1.
CT009576, AC154425 Genomic DNA. Translation: CAO77869.1.
AF151363 mRNA. Translation: AAD38043.1.
AK129309 mRNA. Translation: BAC98119.1.
CCDSiCCDS28172.1.
RefSeqiNP_064656.2. NM_020260.2.
UniGeneiMm.370848.

3D structure databases

ProteinModelPortaliA6X8Z5.
SMRiA6X8Z5. Positions 19-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198630. 2 interactions.
IntActiA6X8Z5. 1 interaction.
MINTiMINT-8094048.
STRINGi10090.ENSMUSP00000023487.

PTM databases

iPTMnetiA6X8Z5.

Proteomic databases

EPDiA6X8Z5.
PaxDbiA6X8Z5.
PeptideAtlasiA6X8Z5.
PRIDEiA6X8Z5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023487; ENSMUSP00000023487; ENSMUSG00000022799.
GeneIDi12549.
KEGGimmu:12549.
UCSCiuc007zfg.1. mouse.

Organism-specific databases

CTDi57514.
MGIiMGI:1333857. Arhgap31.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410KCYW. Eukaryota.
ENOG410ZIYP. LUCA.
HOVERGENiHBG105825.
InParanoidiA6X8Z5.
OMAiNTWVTPE.
OrthoDBiEOG7WMCHV.
PhylomeDBiA6X8Z5.
TreeFamiTF351451.

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiArhgap31. mouse.
PROiA6X8Z5.
SOURCEiSearch...

Gene expression databases

BgeeiA6X8Z5.
CleanExiMM_CDGAP.
ExpressionAtlasiA6X8Z5. baseline and differential.
GenevisibleiA6X8Z5. MM.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Embryo and Hypothalamus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "CdGAP, a novel proline-rich GTPase-activating protein for Cdc42 and Rac."
    Lamarche-Vane N., Hall A.
    J. Biol. Chem. 273:29172-29177(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-820, FUNCTION, TISSUE SPECIFICITY.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-1425.
    Tissue: Embryonic tail.
  5. "The activity of the GTPase-activating protein CdGAP is regulated by the endocytic protein intersectin."
    Jenna S., Hussain N.K., Danek E.I., Triki I., Wasiak S., McPherson P.S., Lamarche-Vane N.
    J. Biol. Chem. 277:6366-6373(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITSN1, SUBCELLULAR LOCATION.
  6. "Extracellular signal-regulated kinase 1 interacts with and phosphorylates CdGAP at an important regulatory site."
    Tcherkezian J., Danek E.I., Jenna S., Triki I., Lamarche-Vane N.
    Mol. Cell. Biol. 25:6314-6329(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, PHOSPHORYLATION AT THR-776.
  7. "CdGAP associates with actopaxin to regulate integrin-dependent changes in cell morphology and motility."
    LaLonde D.P., Grubinger M., Lamarche-Vane N., Turner C.E.
    Curr. Biol. 16:1375-1385(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PARVA, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-56 AND ASN-169.
  8. "Glycogen synthase kinase-3 phosphorylates CdGAP at a consensus ERK 1 regulatory site."
    Danek E.I., Tcherkezian J., Triki I., Meriane M., Lamarche-Vane N.
    J. Biol. Chem. 282:3624-3631(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-776, INDUCTION BY SERUM.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272; THR-283; SER-343; SER-346; SER-384; SER-464; THR-666; SER-685; SER-690; SER-765; THR-769; SER-961; SER-1092; SER-1093 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRHG31_MOUSE
AccessioniPrimary (citable) accession number: A6X8Z5
Secondary accession number(s): Q3TL91
, Q3U1T7, Q3UDE7, Q3UUH4, Q6ZPW0, Q9WV94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: July 6, 2016
This is version 76 of the entry and version 1 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. 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.