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RHG26_MOUSE
ID   RHG26_MOUSE             Reviewed;         814 AA.
AC   Q6ZQ82; E9QLL3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Rho GTPase-activating protein 26;
DE   AltName: Full=Rho-type GTPase-activating protein 26;
GN   Name=Arhgap26; Synonyms=Kiaa0621;
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=Brain;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, 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).
RN   [4]
RP   INTERACTION WITH NYAP1; NYAP2 AND MYO16.
RX   PubMed=21946561; DOI=10.1038/emboj.2011.348;
RA   Yokoyama K., Tezuka T., Kotani M., Nakazawa T., Hoshina N., Shimoda Y.,
RA   Kakuta S., Sudo K., Watanabe K., Iwakura Y., Yamamoto T.;
RT   "NYAP: a phosphoprotein family that links PI3K to WAVE1 signalling in
RT   neurons.";
RL   EMBO J. 30:4739-4754(2011).
CC   -!- FUNCTION: GTPase-activating protein for RHOA and CDC42. {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the C-terminus of PTK2/FAK1 (By similarity).
CC       Interacts with NYAP1, NYAP2 and MYO16. {ECO:0000250,
CC       ECO:0000269|PubMed:21946561}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
CC       Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with actin
CC       stress fibers and cortical actin structures. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97986.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK129176; BAC97986.1; ALT_INIT; mRNA.
DR   EMBL; AC110730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC129603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC133601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC151409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC151580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS29205.1; -.
DR   RefSeq; NP_780373.3; NM_175164.4.
DR   AlphaFoldDB; Q6ZQ82; -.
DR   SMR; Q6ZQ82; -.
DR   BioGRID; 214619; 56.
DR   IntAct; Q6ZQ82; 2.
DR   MINT; Q6ZQ82; -.
DR   STRING; 10090.ENSMUSP00000095200; -.
DR   iPTMnet; Q6ZQ82; -.
DR   PhosphoSitePlus; Q6ZQ82; -.
DR   EPD; Q6ZQ82; -.
DR   MaxQB; Q6ZQ82; -.
DR   PaxDb; Q6ZQ82; -.
DR   PRIDE; Q6ZQ82; -.
DR   ProteomicsDB; 253277; -.
DR   Antibodypedia; 27437; 257 antibodies from 33 providers.
DR   DNASU; 71302; -.
DR   Ensembl; ENSMUST00000097593; ENSMUSP00000095200; ENSMUSG00000036452.
DR   GeneID; 71302; -.
DR   KEGG; mmu:71302; -.
DR   UCSC; uc008esr.1; mouse.
DR   CTD; 23092; -.
DR   MGI; MGI:1918552; Arhgap26.
DR   VEuPathDB; HostDB:ENSMUSG00000036452; -.
DR   eggNOG; KOG1451; Eukaryota.
DR   GeneTree; ENSGT00940000157254; -.
DR   InParanoid; Q6ZQ82; -.
DR   OMA; LAXIFNT; -.
DR   OrthoDB; 693048at2759; -.
DR   PhylomeDB; Q6ZQ82; -.
DR   TreeFam; TF316851; -.
DR   Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR   Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR   Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR   Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR   Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR   Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR   Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR   Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR   Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR   Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR   BioGRID-ORCS; 71302; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Arhgap26; mouse.
DR   PRO; PR:Q6ZQ82; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q6ZQ82; protein.
DR   Bgee; ENSMUSG00000036452; Expressed in interventricular septum and 208 other tissues.
DR   ExpressionAtlas; Q6ZQ82; baseline and differential.
DR   Genevisible; Q6ZQ82; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07636; BAR_GRAF; 1.
DR   CDD; cd12064; SH3_GRAF; 1.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR030061; GRAF.
DR   InterPro; IPR035483; GRAF_BAR.
DR   InterPro; IPR035481; GRAF_SH3.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR12552:SF4; PTHR12552:SF4; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cytoplasm; Cytoskeleton; GTPase activation;
KW   Reference proteome; SH3 domain.
FT   CHAIN           1..814
FT                   /note="Rho GTPase-activating protein 26"
FT                   /id="PRO_0000355553"
FT   DOMAIN          265..369
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          383..568
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   DOMAIN          756..814
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          584..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..657
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..682
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        598
FT                   /note="K -> E (in Ref. 1; BAC97986)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   814 AA;  92071 MW;  B1BA51634549C891 CRC64;
     MGLPALEFSD CCLDSPHFRE TLKSHEAELD KTNKFIKELI KDGKSLISAL KNLSSAKRKF
     ADSLNEFKFQ CIGDAETDDE MCIARSLQEF AAVLRNLEDE RSRMIENASE VLITPLEKFR
     KEQIGAAREA KKKYDKETEK YCGTLEKHLN LSSKKKESQL QEADSQVDLV RQHFYEVSLE
     YVFKVQEVQE RKMFEFVEPL LAFLQGLFTF YHHGYELAKD FGDFKTQLTI SIQNTRNRFE
     GTRSEVESLM KKMKENPLEH KTISPYTMEG YLYVQEKRHF GTSWVKHYCT YQRDSKQITM
     VPFDQKSGGK GGEDESVTLK SCTRRKTDSI EKRFCFDVEA VDRPGVITMQ ALSEEDRRLW
     MEAMDGREPV YNSNRDSQSE GTAQLDSIGF SIIRKCIHAV ETRGINEQGL YRIVGVNSRV
     QKLLSVLMDP KAASETETDI CAEWEIKTVT SALKTYLRML PGPLMMYQFQ RSFIKAAKLE
     NQETRVSEIH SLVHRLPEKN RQMLQLLMNH LANVANNHKQ NLMTVANLGV VFGPTLLRPQ
     EETVAAIMDI KFQNIVIEIL IENHEKIFNT VPDVPLTNAQ LHLSRKKSSD SKPPSCSKRP
     LTLFHAVPST EKQEQRNSII NSSLESVSSS ANSILNSSSS LQPNLNSSDS NLDVVKPSRP
     SSLPPNPSPT SPLSPSWPMF SAPSSPMPTS STSSDSSPIR SVAGFVWFSV AAVVLSLAWS
     SLHAVFSLLV NFVPCHPNLH LLFDRPEEAV REDSSTPFRK AKALYACQAE HDSELSFTAG
     TVFDNVHPSQ EPGWLEGTLN GKTGLIPENY VEFL
 
 
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