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ASB3_MOUSE
ID   ASB3_MOUSE              Reviewed;         525 AA.
AC   Q9WV72; Q5SSV5;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Ankyrin repeat and SOCS box protein 3;
DE            Short=ASB-3;
GN   Name=Asb3;
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 [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=11111040; DOI=10.1016/s0378-1119(00)00402-9;
RA   Kile B.T., Viney E.M., Willson T.A., Brodnicki T.C., Cancilla M.R.,
RA   Herlihy A.S., Croker B.A., Baca M., Nicola N.A., Hilton D.J.,
RA   Alexander W.S.;
RT   "Cloning and characterization of the genes encoding the ankyrin repeat and
RT   SOCS box-containing proteins Asb-1, Asb-2, Asb-3 and Asb-4.";
RL   Gene 258:31-41(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
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   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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   -!- FUNCTION: Probable substrate-recognition component of a SCF-like ECS
CC       (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex
CC       which mediates the ubiquitination and subsequent proteasomal
CC       degradation of target proteins. Recognizes TNFRSF1B (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with ELOB and TNFRSF1B. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed; highest expression in testis and
CC       spleen. {ECO:0000269|PubMed:11111040}.
CC   -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC       BC complex, an adapter module in different E3 ubiquitin-protein ligase
CC       complexes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ankyrin SOCS box (ASB) family.
CC       {ECO:0000305}.
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DR   EMBL; AF155354; AAD38810.1; -; mRNA.
DR   EMBL; AK143580; BAE25448.1; -; mRNA.
DR   EMBL; AL646095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL732621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS24511.1; -.
DR   RefSeq; NP_076395.2; NM_023906.3.
DR   RefSeq; XP_006514834.1; XM_006514771.3.
DR   AlphaFoldDB; Q9WV72; -.
DR   SMR; Q9WV72; -.
DR   BioGRID; 211146; 2.
DR   IntAct; Q9WV72; 2.
DR   STRING; 10090.ENSMUSP00000020551; -.
DR   iPTMnet; Q9WV72; -.
DR   PhosphoSitePlus; Q9WV72; -.
DR   MaxQB; Q9WV72; -.
DR   PaxDb; Q9WV72; -.
DR   PRIDE; Q9WV72; -.
DR   ProteomicsDB; 277042; -.
DR   Antibodypedia; 1141; 163 antibodies from 22 providers.
DR   DNASU; 65257; -.
DR   Ensembl; ENSMUST00000020551; ENSMUSP00000020551; ENSMUSG00000020305.
DR   GeneID; 65257; -.
DR   KEGG; mmu:65257; -.
DR   UCSC; uc007iif.1; mouse.
DR   CTD; 51130; -.
DR   MGI; MGI:1929749; Asb3.
DR   VEuPathDB; HostDB:ENSMUSG00000020305; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   GeneTree; ENSGT00940000159080; -.
DR   InParanoid; Q9WV72; -.
DR   OrthoDB; 1392423at2759; -.
DR   PhylomeDB; Q9WV72; -.
DR   TreeFam; TF315127; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 65257; 4 hits in 71 CRISPR screens.
DR   ChiTaRS; Asb3; mouse.
DR   PRO; PR:Q9WV72; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9WV72; protein.
DR   Bgee; ENSMUSG00000020305; Expressed in spermatocyte and 250 other tissues.
DR   ExpressionAtlas; Q9WV72; baseline and differential.
DR   Genevisible; Q9WV72; MM.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd03722; SOCS_ASB3; 1.
DR   Gene3D; 1.25.40.20; -; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR037329; ASB3_SOCS.
DR   InterPro; IPR001496; SOCS_box.
DR   InterPro; IPR036036; SOCS_box-like_dom_sf.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF13606; Ank_3; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF07525; SOCS_box; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 10.
DR   SMART; SM00969; SOCS_box; 1.
DR   SUPFAM; SSF158235; SSF158235; 1.
DR   SUPFAM; SSF48403; SSF48403; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 6.
DR   PROSITE; PS50225; SOCS; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..525
FT                   /note="Ankyrin repeat and SOCS box protein 3"
FT                   /id="PRO_0000066927"
FT   REPEAT          9..38
FT                   /note="ANK 1"
FT   REPEAT          42..71
FT                   /note="ANK 2"
FT   REPEAT          78..107
FT                   /note="ANK 3"
FT   REPEAT          111..140
FT                   /note="ANK 4"
FT   REPEAT          145..174
FT                   /note="ANK 5"
FT   REPEAT          178..207
FT                   /note="ANK 6"
FT   REPEAT          211..240
FT                   /note="ANK 7"
FT   REPEAT          246..275
FT                   /note="ANK 8"
FT   REPEAT          279..308
FT                   /note="ANK 9"
FT   REPEAT          315..346
FT                   /note="ANK 10"
FT   DOMAIN          442..505
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT   CONFLICT        163
FT                   /note="R -> K (in Ref. 1; AAD38810)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277
FT                   /note="G -> E (in Ref. 1; AAD38810)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        418
FT                   /note="A -> V (in Ref. 1; AAD38810)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   525 AA;  58283 MW;  DEFCAC73EE2AF5E7 CRC64;
     MDFTEAYSDT CSTVGLAARE GNVKILRKLL KKGRSVDVAD NRGWMPIHEA AYHNAVECLQ
     MLIHTDSSEN YIKAKTFEGF CALHLAVSQG HWKITQILLE AGADPNETTL EETTPLFLAV
     ESGRIDVLKL LLQHGANVNG SHSMSGWNSL HQASFQGNAE TIRLLLKQGA DRECQDDFGI
     TPLFVAAQYG KLESMSILIS SGANVNCQAL DKATPLFIAA QEGHTKCVEL LLSSGADPDL
     YCNEDNWQLP IHAAAQMGHT ETLDLLIPRT NRACDTGPDK VSPVYSAVFG GREECLEMLL
     QNGYSPDAQM CLVFGFSSPL CMAFQKDCDF SGIVNILLKY GAQLNELHLA YCLKYEKFSM
     FCSFLKKGSL MVPWNHTSEF ISYAVKAQTK YKAWLPHLLL AGFDPLILLC SSSWVDSASD
     DILIFTLEFS NWKRLPSAVE KMLSVRANSS WALQQHLASV PSLTHLCRLE IRASLKAEHL
     HSDIFIHQLP LPRSLQNYLL YEEVLRMNEI LEPAANQDGE TSKAT
 
 
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