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AGFG2_MOUSE
ID   AGFG2_MOUSE             Reviewed;         479 AA.
AC   Q80WC7; Q8BKS5; Q99J67;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Arf-GAP domain and FG repeat-containing protein 2;
DE   AltName: Full=HIV-1 Rev-binding protein-like protein;
DE   AltName: Full=Rev/Rex activation domain-binding protein related;
DE            Short=RAB-R;
GN   Name=Agfg2; Synonyms=Hrbl, Rabr;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 247-479 (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH EPS15R.
RX   PubMed=9446614; DOI=10.1074/jbc.273.5.3003;
RA   Coda L., Salcini A.E., Confalonieri S., Pelicci G., Sorkina T., Sorkin A.,
RA   Pelicci P.G., Di Fiore P.P.;
RT   "Eps15R is a tyrosine kinase substrate with characteristics of a docking
RT   protein possibly involved in coated pits-mediated internalization.";
RL   J. Biol. Chem. 273:3003-3012(1998).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
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   -!- SUBUNIT: Interacts with EPS15R. {ECO:0000269|PubMed:9446614}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80WC7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80WC7-2; Sequence=VSP_010669, VSP_010670;
CC   -!- DOMAIN: Contains FG repeats and 4 N-P-F repeats.
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DR   EMBL; BC003330; AAH03330.1; -; mRNA.
DR   EMBL; BC046788; AAH46788.1; -; mRNA.
DR   EMBL; AK050881; BAC34441.1; -; mRNA.
DR   CCDS; CCDS19774.1; -. [Q80WC7-1]
DR   RefSeq; NP_835456.1; NM_178162.3. [Q80WC7-1]
DR   AlphaFoldDB; Q80WC7; -.
DR   BioGRID; 231167; 3.
DR   STRING; 10090.ENSMUSP00000031736; -.
DR   iPTMnet; Q80WC7; -.
DR   PhosphoSitePlus; Q80WC7; -.
DR   EPD; Q80WC7; -.
DR   MaxQB; Q80WC7; -.
DR   PaxDb; Q80WC7; -.
DR   PRIDE; Q80WC7; -.
DR   ProteomicsDB; 281953; -. [Q80WC7-1]
DR   ProteomicsDB; 281954; -. [Q80WC7-2]
DR   Antibodypedia; 16493; 150 antibodies from 27 providers.
DR   DNASU; 231801; -.
DR   Ensembl; ENSMUST00000031736; ENSMUSP00000031736; ENSMUSG00000029722. [Q80WC7-1]
DR   GeneID; 231801; -.
DR   KEGG; mmu:231801; -.
DR   UCSC; uc009adl.2; mouse. [Q80WC7-1]
DR   UCSC; uc009ado.3; mouse. [Q80WC7-2]
DR   CTD; 3268; -.
DR   MGI; MGI:2443267; Agfg2.
DR   VEuPathDB; HostDB:ENSMUSG00000029722; -.
DR   eggNOG; KOG0702; Eukaryota.
DR   GeneTree; ENSGT00940000161071; -.
DR   HOGENOM; CLU_027801_1_0_1; -.
DR   InParanoid; Q80WC7; -.
DR   OMA; SDCKRNK; -.
DR   PhylomeDB; Q80WC7; -.
DR   TreeFam; TF325357; -.
DR   BioGRID-ORCS; 231801; 2 hits in 72 CRISPR screens.
DR   PRO; PR:Q80WC7; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q80WC7; protein.
DR   Bgee; ENSMUSG00000029722; Expressed in thymus and 245 other tissues.
DR   ExpressionAtlas; Q80WC7; baseline and differential.
DR   Genevisible; Q80WC7; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.220.150; -; 1.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; SSF57863; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Metal-binding; Reference proteome;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..479
FT                   /note="Arf-GAP domain and FG repeat-containing protein 2"
FT                   /id="PRO_0000204829"
FT   DOMAIN          27..153
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   ZN_FING         47..70
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REGION          150..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         174
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O95081"
FT   VAR_SEQ         253..289
FT                   /note="VGQTPAHGGFANFDAFSSSPSSSTFGSLPPSVQAPFQ -> GKYYPGAGTRL
FT                   RRICITAKTSLVHRGLTFLCGWGQGA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010669"
FT   VAR_SEQ         290..479
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010670"
SQ   SEQUENCE   479 AA;  48968 MW;  BE299F70C28D6457 CRC64;
     MVMAAKKGPG PGGGVGGSKA EAEAASEVWC RRVRELGGCS QAGNRHCFEC AQRGVTYVDI
     TVGSFVCTTC SGLLRGLNPP HRVKSISMTT FTEPEVLFLQ SRGNEVCRKI WLGLFDARTS
     LIPDSRDPQK VKEFLQEKYE KKRWYVPPEQ VKGPSYSKGS VSATPVQGSV PEGKPIRTLL
     GDPVPSLSDP ASTSSQPGSQ SQARSSSQAR SSQPPSHSST KKASTDLLAD IGGDPFAAPQ
     VVPAFASFPG FGVGQTPAHG GFANFDAFSS SPSSSTFGSL PPSVQAPFQA QPTPAGSGQM
     SAFGVAPLAA ASQPNNLADV GGLLGPRMAA GGLPGSVFGM PSQVPALQSA VPGVSGSGGL
     PFGAYTNPFA TPAQAQLPST NPFQPNGLAS GPGFGMSSVR PGLLQPVPPS GAFASPFSAP
     VFPTQAGLAD QQNGSSFGDL GTSKLGQRPL SQPAGISTNP FMTGSSAFAS KPPTTNPFL
 
 
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