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Protein

Rho GTPase-activating protein 12

Gene

Arhgap12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.By similarity

GO - Molecular functioni

GO - Biological processi

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 12
Alternative name(s):
Rho-type GTPase-activating protein 12
Gene namesi
Name:Arhgap12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1922665. Arhgap12.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 838838Rho GTPase-activating protein 12PRO_0000056715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei163 – 1631PhosphoserineBy similarity
Modified residuei199 – 1991PhosphoserineCombined sources
Modified residuei211 – 2111PhosphoserineCombined sources
Modified residuei213 – 2131PhosphoserineCombined sources
Modified residuei228 – 2281PhosphothreonineBy similarity
Modified residuei229 – 2291PhosphothreonineBy similarity
Modified residuei238 – 2381PhosphoserineCombined sources
Modified residuei241 – 2411PhosphotyrosineCombined sources
Modified residuei584 – 5841PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8C0D4.
MaxQBiQ8C0D4.
PaxDbiQ8C0D4.
PeptideAtlasiQ8C0D4.
PRIDEiQ8C0D4.

PTM databases

iPTMnetiQ8C0D4.
PhosphoSiteiQ8C0D4.

Expressioni

Gene expression databases

BgeeiQ8C0D4.
CleanExiMM_ARHGAP12.
ExpressionAtlasiQ8C0D4. baseline and differential.
GenevisibleiQ8C0D4. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054209.

Structurei

3D structure databases

ProteinModelPortaliQ8C0D4.
SMRiQ8C0D4. Positions 11-70, 457-566, 629-837.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 7263SH3PROSITE-ProRule annotationAdd
BLAST
Domaini263 – 29634WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini355 – 38834WW 2PROSITE-ProRule annotationAdd
BLAST
Domaini466 – 567102PHPROSITE-ProRule annotationAdd
BLAST
Domaini648 – 836189Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 2 WW domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiENOG410KD3Y. Eukaryota.
ENOG410ZTHP. LUCA.
GeneTreeiENSGT00840000129684.
HOGENOMiHOG000294167.
HOVERGENiHBG005328.
InParanoidiQ8C0D4.
OrthoDBiEOG7CZK7R.
PhylomeDBiQ8C0D4.
TreeFamiTF329345.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR015767. Rho_GTPase_act.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
IPR001202. WW_dom.
[Graphical view]
PANTHERiPTHR23181. PTHR23181. 3 hits.
PfamiPF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF14604. SH3_9. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
SM00456. WW. 2 hits.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51045. SSF51045. 2 hits.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C0D4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAERSGKITA GQAYIEVEYD YEYDAKDRKI VIRQGERYLL VKKTNDDWWQ
60 70 80 90 100
VRPDENSKAF YVPAQYVKEV TRKALMPPVK QATGLPNNSM KTIQSMHLQR
110 120 130 140 150
STENVNKMPE LSSFGKPSSS VQGTGLIRDA NQNFGSNYNS GQTLNLSLDL
160 170 180 190 200
THNNGKFNSD SHSPKVSSQN RTRLFGHFPG PEFLDIEKTS FSQEQSCDSA
210 220 230 240 250
GEGSERIQQD SESGDELSSS STEQMRATTP PNQGRPDSPV YANLQELKIS
260 270 280 290 300
QSALPPLPGS PAIQVNGEWE THKDSSGRCY YYNRTTQERT WKPPRWARDV
310 320 330 340 350
STSRDFQSPG EQEPLSSEEN YHSSCFSQSD SQCGSPPRGW SEELDERGHT
360 370 380 390 400
LYTSDYTKEK WLKHVDDQGR QYYYSADGSR SEWELPKYNA SSQQQREIIK
410 420 430 440 450
SRSLDRRLQE PIVLTKWRHS TIVLDSNDKD SPTTTKLCLP ENESPPTSSK
460 470 480 490 500
HQDPGQEKYG LLNVTKITEN GKKVRKNWLS SWAVLQGSSL LFTKTQGSST
510 520 530 540 550
SWFGSNQSKP EFTVDLKGAV IEMASKDKSS KKNVFELKTR QGTELLIQSD
560 570 580 590 600
NDAVINDWFK VLSSTINNQV AEADEAAEEE TPDSPGVEKH DKEKDQKELK
610 620 630 640 650
KLRSMKGSSM DSSEQKKTKK NLKKFLTRRP TLQAVREKGY IKDQVFGSNL
660 670 680 690 700
ANLCQRENGT VPKFVKLCIE HVEEHGLDVD GIYRVSGNLA VIQKLRFAVN
710 720 730 740 750
HDEKLDLNDS KWEDIHVITG ALKMFFRELP EPLFTFNHFN DFVNAIKQEP
760 770 780 790 800
RQRVTAVKDL IRQLPKPNQD TMQILFRHLK RVIENGEKNR MTYQSIAIVF
810 820 830
GPTLLKPERE TGNIAVHTVY QNQIVELILL ELSTVFGR
Length:838
Mass (Da):95,352
Last modified:May 10, 2004 - v2
Checksum:iC8660927694567AB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421K → N in BAC27494 (PubMed:16141072).Curated
Sequence conflicti86 – 861P → A in BAC36587 (PubMed:16141072).Curated
Sequence conflicti483 – 4831A → P in BAC36587 (PubMed:16141072).Curated
Sequence conflicti530 – 5301S → T in BAC36587 (PubMed:16141072).Curated
Sequence conflicti698 – 6981A → T in BAC36587 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031648 mRNA. Translation: BAC27494.1.
AK077063 mRNA. Translation: BAC36587.1.
CCDSiCCDS37723.1.
RefSeqiNP_001034781.1. NM_001039692.1.
NP_083553.2. NM_029277.2.
UniGeneiMm.239675.

Genome annotation databases

EnsembliENSMUST00000182559; ENSMUSP00000138585; ENSMUSG00000041225.
GeneIDi75415.
KEGGimmu:75415.
UCSCiuc008dzc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031648 mRNA. Translation: BAC27494.1.
AK077063 mRNA. Translation: BAC36587.1.
CCDSiCCDS37723.1.
RefSeqiNP_001034781.1. NM_001039692.1.
NP_083553.2. NM_029277.2.
UniGeneiMm.239675.

3D structure databases

ProteinModelPortaliQ8C0D4.
SMRiQ8C0D4. Positions 11-70, 457-566, 629-837.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054209.

PTM databases

iPTMnetiQ8C0D4.
PhosphoSiteiQ8C0D4.

Proteomic databases

EPDiQ8C0D4.
MaxQBiQ8C0D4.
PaxDbiQ8C0D4.
PeptideAtlasiQ8C0D4.
PRIDEiQ8C0D4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000182559; ENSMUSP00000138585; ENSMUSG00000041225.
GeneIDi75415.
KEGGimmu:75415.
UCSCiuc008dzc.1. mouse.

Organism-specific databases

CTDi94134.
MGIiMGI:1922665. Arhgap12.

Phylogenomic databases

eggNOGiENOG410KD3Y. Eukaryota.
ENOG410ZTHP. LUCA.
GeneTreeiENSGT00840000129684.
HOGENOMiHOG000294167.
HOVERGENiHBG005328.
InParanoidiQ8C0D4.
OrthoDBiEOG7CZK7R.
PhylomeDBiQ8C0D4.
TreeFamiTF329345.

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiArhgap12. mouse.
PROiQ8C0D4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C0D4.
CleanExiMM_ARHGAP12.
ExpressionAtlasiQ8C0D4. baseline and differential.
GenevisibleiQ8C0D4. MM.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR015767. Rho_GTPase_act.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
IPR001202. WW_dom.
[Graphical view]
PANTHERiPTHR23181. PTHR23181. 3 hits.
PfamiPF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF14604. SH3_9. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
SM00456. WW. 2 hits.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51045. SSF51045. 2 hits.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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: Testis.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  3. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238 AND TYR-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-211; SER-213; SER-238 AND TYR-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRHG12_MOUSE
AccessioniPrimary (citable) accession number: Q8C0D4
Secondary accession number(s): Q8BVP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 6, 2016
This is version 119 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. 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.