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RHGBA_MOUSE
ID   RHGBA_MOUSE             Reviewed;         987 AA.
AC   Q80Y19; A2AL17; Q6ZQL1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Rho GTPase-activating protein 11A {ECO:0000305};
DE   AltName: Full=Rho-type GTPase-activating protein 11A {ECO:0000305};
GN   Name=Arhgap11a {ECO:0000312|MGI:MGI:2444300};
GN   Synonyms=Kiaa0013 {ECO:0000303|PubMed:14621295};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-317 AND THR-322, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC       to an inactive GDP-bound state. {ECO:0000250|UniProtKB:Q6P4F7}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6P4F7}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97844.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK129034; BAC97844.1; ALT_INIT; mRNA.
DR   EMBL; AL772405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC050875; AAH50875.1; -; mRNA.
DR   CCDS; CCDS16562.1; -.
DR   RefSeq; NP_852081.2; NM_181416.3.
DR   AlphaFoldDB; Q80Y19; -.
DR   SMR; Q80Y19; -.
DR   BioGRID; 230736; 6.
DR   STRING; 10090.ENSMUSP00000099604; -.
DR   iPTMnet; Q80Y19; -.
DR   PhosphoSitePlus; Q80Y19; -.
DR   EPD; Q80Y19; -.
DR   jPOST; Q80Y19; -.
DR   MaxQB; Q80Y19; -.
DR   PaxDb; Q80Y19; -.
DR   PeptideAtlas; Q80Y19; -.
DR   PRIDE; Q80Y19; -.
DR   ProteomicsDB; 254974; -.
DR   DNASU; 228482; -.
DR   Ensembl; ENSMUST00000102545; ENSMUSP00000099604; ENSMUSG00000041219.
DR   Ensembl; ENSMUST00000110949; ENSMUSP00000106574; ENSMUSG00000041219.
DR   GeneID; 228482; -.
DR   KEGG; mmu:228482; -.
DR   UCSC; uc008lpr.2; mouse.
DR   CTD; 9824; -.
DR   MGI; MGI:2444300; Arhgap11a.
DR   VEuPathDB; HostDB:ENSMUSG00000041219; -.
DR   eggNOG; KOG2710; Eukaryota.
DR   GeneTree; ENSGT00940000155312; -.
DR   HOGENOM; CLU_010134_1_0_1; -.
DR   InParanoid; Q80Y19; -.
DR   OMA; RQPIRHK; -.
DR   OrthoDB; 213929at2759; -.
DR   PhylomeDB; Q80Y19; -.
DR   TreeFam; TF332212; -.
DR   Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR   BioGRID-ORCS; 228482; 6 hits in 73 CRISPR screens.
DR   ChiTaRS; Arhgap11a; mouse.
DR   PRO; PR:Q80Y19; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q80Y19; protein.
DR   Bgee; ENSMUSG00000041219; Expressed in cleaving embryo and 221 other tissues.
DR   ExpressionAtlas; Q80Y19; baseline and differential.
DR   Genevisible; Q80Y19; MM.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.555.10; -; 1.
DR   InterPro; IPR042869; ARHGAP11A/B.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR15670; PTHR15670; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   GTPase activation; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..987
FT                   /note="Rho GTPase-activating protein 11A"
FT                   /id="PRO_0000267214"
FT   DOMAIN          52..239
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          297..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          700..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..724
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         305
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P4F7"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P4F7"
FT   MOD_RES         317
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         322
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         338
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P4F7"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P4F7"
FT   MOD_RES         481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P4F7"
FT   MOD_RES         505
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P4F7"
FT   MOD_RES         581
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P4F7"
FT   MOD_RES         655
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P4F7"
FT   MOD_RES         819
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P4F7"
FT   MOD_RES         840
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P4F7"
FT   CONFLICT        723
FT                   /note="G -> V (in Ref. 1; BAC97844 and 3; AAH50875)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        867
FT                   /note="L -> H (in Ref. 1; BAC97844 and 3; AAH50875)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   987 AA;  108436 MW;  E7566F732548997D CRC64;
     MWDQRLVRLA LLQQLRAVYG IKVKGGRGQC DRRRHETAAT EIKGKVFGVP FNSLPHSVVP
     EFGHIPSFLV DACASLKEHI HTEGLFRKSG SVVRLKALKS KLDQGEACLS SALPCDVAGL
     LKQFFRELPE PVLPADLHEA LFKAQQLGAE ERNKATLLLS CLMANPTVDI LRYFFNFLKS
     VSLRASENKM DSSNLAVIFA PNLLQTSEGH EKMSANTEKK LRLQAAVVQT FIDCASDIGR
     VPDFILEKIP AMLGIDGLCT TPSLEGFEGD FETPGECKRK RRQSVGDFVN GALNKLKSSR
     TPSITPQQDR TAQASASPLI LTPSVKRKLP GESSHAFSSK KRKSIKHNLN FELLPSHFFS
     SNSTPVSVHL DTSPDGSSQT SLSPIAMSGN HLVSTELRRS KRIASKKVYR VESGKAGCFS
     PKVSRKEKTR RSLRLKFSLG KNRDSDGCSV INRYENVGRR LANQQNLKSR IDSVKTGLLF
     SPDIDERLLK KGSEKISKSE EHLLTPDQLD GTGYRMSWTE PSNSSFQDMS ANGTSPIMQN
     LEVKSFSLEP DITVEKSPVV SCELRPSTFH SQPDSSVLSL SGDEGNLASE TLQKIQKAFS
     ESGSDLHMVI NHEQSSVTNT GEEVEFRDVT VTESKGHDGS CAGEEENCPS ERNFSPDQSP
     EFAREADEEC YSTQMKVECE GLHSETPKAD PLILQAFPGE EPAEEPQSPR NQLSTPSRGN
     ENGGESAGAS GAPGEDESTC SVAVLSKPRP QRLSRQQSLV EKCDSVAPGA LQVTEHGKVS
     DHIQWFNKLS LNEPNRGKVK SPLKFQRTPV RQSVRRINSL LEYGRQPVRQ KLAIFGDAAS
     PLVKSVSCDS ALPSCVQNTS KGPTAPLITS GLEAQKSTSC NKSSVELTSK SFTKMKRHPD
     PLSASLGTPR LCKQENKSNG HIKFPLDDLT NHERLKFVVN NNVAFSPGMK NRVVRKPSEK
     ERVWYKGSPK NPIGKTQLLP TSKPVDL
 
 
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