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UBAC1_MOUSE
ID   UBAC1_MOUSE             Reviewed;         409 AA.
AC   Q8VDI7; Q3TZH3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Ubiquitin-associated domain-containing protein 1;
DE            Short=UBA domain-containing protein 1;
DE   AltName: Full=E3 ubiquitin-protein ligase subunit KPC2;
DE   AltName: Full=Kip1 ubiquitination-promoting complex protein 2;
GN   Name=Ubac1; Synonyms=Kpc2, Ubadc1;
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   STRAIN=C57BL/6J; TISSUE=Bone marrow;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-252; ALA-269 AND
RP   THR-274.
RC   STRAIN=Czech II; TISSUE=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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, 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   -!- FUNCTION: Non-catalytic subunit of the KPC complex that acts as E3
CC       ubiquitin-protein ligase. Required for poly-ubiquitination and
CC       proteasome-mediated degradation of CDKN1B during G1 phase of the cell
CC       cycle (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the KPC complex composed of RNF123/KPC1 and
CC       UBAC1/KPC2. Interacts with RNF123 via its N-terminal domain. Interacts
CC       with the proteasome via its N-terminal domain (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AK157857; BAE34235.1; -; mRNA.
DR   EMBL; BC021811; AAH21811.1; -; mRNA.
DR   CCDS; CCDS15795.1; -.
DR   RefSeq; NP_598596.2; NM_133835.2.
DR   AlphaFoldDB; Q8VDI7; -.
DR   SMR; Q8VDI7; -.
DR   BioGRID; 221128; 7.
DR   STRING; 10090.ENSMUSP00000040220; -.
DR   iPTMnet; Q8VDI7; -.
DR   PhosphoSitePlus; Q8VDI7; -.
DR   EPD; Q8VDI7; -.
DR   MaxQB; Q8VDI7; -.
DR   PaxDb; Q8VDI7; -.
DR   PeptideAtlas; Q8VDI7; -.
DR   PRIDE; Q8VDI7; -.
DR   ProteomicsDB; 297780; -.
DR   Antibodypedia; 18666; 209 antibodies from 28 providers.
DR   DNASU; 98766; -.
DR   Ensembl; ENSMUST00000036509; ENSMUSP00000040220; ENSMUSG00000036352.
DR   GeneID; 98766; -.
DR   KEGG; mmu:98766; -.
DR   UCSC; uc008itz.2; mouse.
DR   CTD; 10422; -.
DR   MGI; MGI:1920995; Ubac1.
DR   VEuPathDB; HostDB:ENSMUSG00000036352; -.
DR   eggNOG; ENOG502QQQ6; Eukaryota.
DR   GeneTree; ENSGT00390000014658; -.
DR   HOGENOM; CLU_035938_0_0_1; -.
DR   InParanoid; Q8VDI7; -.
DR   OMA; LHVCTME; -.
DR   OrthoDB; 1163759at2759; -.
DR   PhylomeDB; Q8VDI7; -.
DR   TreeFam; TF324579; -.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 98766; 4 hits in 75 CRISPR screens.
DR   ChiTaRS; Ubac1; mouse.
DR   PRO; PR:Q8VDI7; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8VDI7; protein.
DR   Bgee; ENSMUSG00000036352; Expressed in fetal liver hematopoietic progenitor cell and 267 other tissues.
DR   ExpressionAtlas; Q8VDI7; baseline and differential.
DR   Genevisible; Q8VDI7; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd14303; UBA1_KPC2; 1.
DR   CDD; cd14304; UBA2_KPC2; 1.
DR   InterPro; IPR006636; STI1_HS-bd.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR041926; UBA1_UBAC1.
DR   InterPro; IPR041927; UBA2_UBAC1.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   Pfam; PF00627; UBA; 2.
DR   SMART; SM00727; STI1; 1.
DR   SMART; SM00165; UBA; 2.
DR   SUPFAM; SSF46934; SSF46934; 2.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50030; UBA; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Reference proteome; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..409
FT                   /note="Ubiquitin-associated domain-containing protein 1"
FT                   /id="PRO_0000250450"
FT   DOMAIN          14..98
FT                   /note="Ubiquitin-like"
FT   DOMAIN          187..231
FT                   /note="UBA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          292..332
FT                   /note="UBA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          357..396
FT                   /note="STI1"
FT   REGION          101..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BSL1"
FT   VARIANT         252
FT                   /note="A -> G (in strain: Czech II)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT   VARIANT         269
FT                   /note="V -> A (in strain: Czech II)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT   VARIANT         274
FT                   /note="S -> T (in strain: Czech II)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
SQ   SEQUENCE   409 AA;  45531 MW;  7CE7C9ACC5975231 CRC64;
     MFVQEEKIFA GKVLRLHICA ADGAEWLEEA TEDTSVEKLK ESCLKHGAHG SLEDPKNVTH
     HKLIHAASER VLSDSKTILE ENIQDQDVLL LIKKRVPSPL PKMADVSAEE KKKQEQKAPD
     KDAILRATAN LPACSTDRTA VQTTMRDFQT ELRKILVSLI EVAQKLLALN PDAVELFKKA
     NAMLDEDEDE RVDETALRQL TEMGFPESRA SKALRLNHMS VPQAMEWLIE HSEDPAIDTP
     LPGHAAQAGA SAAATTSSTS SEAAVGTSVE DEESRDELTE IFKKIRRKKE FRADARAVIS
     LMEMGFDEKE VIDALRVNNN QQNAACEWLL GDRKPSPEEL DQGIDPNSPL FQAILDNPVV
     QLGLTNPKTL LAFEDMLENP LNSTQWMNDP ETGPVMLQIS RIFQTLNRT
 
 
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