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UBQ12_ARATH
ID   UBQ12_ARATH             Reviewed;         230 AA.
AC   Q3E7K8;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Polyubiquitin 12;
DE   Contains:
DE     RecName: Full=Ubiquitin-related 1;
DE   Contains:
DE     RecName: Full=Ubiquitin-related 2;
DE   Contains:
DE     RecName: Full=Ubiquitin-related 3;
DE   Flags: Precursor;
GN   Name=UBQ12; OrderedLocusNames=At1g55060; ORFNames=T7N22.10;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC       protein, or free (unanchored). When covalently bound, it is conjugated
CC       to target proteins via an isopeptide bond either as a monomer
CC       (monoubiquitin), a polymer linked via different Lys residues of the
CC       ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC       initiator Met of the ubiquitin (linear polyubiquitin chains).
CC       Polyubiquitin chains, when attached to a target protein, have different
CC       functions depending on the Lys residue of the ubiquitin that is linked:
CC       Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated
CC       degradation) and in cell-cycle regulation; Lys-29-linked is involved in
CC       lysosomal degradation; Lys-33-linked is involved in kinase
CC       modification; Lys-48-linked is involved in protein degradation via the
CC       proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage
CC       responses. Linear polymer chains formed via attachment by the initiator
CC       Met lead to cell signaling. Ubiquitin is usually conjugated to Lys
CC       residues of target proteins, however, in rare cases, conjugation to Cys
CC       or Ser residues has been observed. When polyubiquitin is free
CC       (unanchored-polyubiquitin), it also has distinct roles, such as in
CC       activation of protein kinases, and in signaling (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 16 different genes. Ubiquitin is
CC       generally synthesized as a polyubiquitin precursor with tandem head to
CC       tail repeats. Often, there is one to three additional amino acids after
CC       the last repeat, removed in the mature protein. Alternatively,
CC       ubiquitin extension protein is synthesized as a single copy of
CC       ubiquitin fused to a ribosomal protein (either L40 or S27A) or to a
CC       ubiquitin-related protein (either RUB1 or RUB2). Following translation,
CC       extension protein is cleaved from ubiquitin.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR   EMBL; AC073944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002684; AEE33181.1; -; Genomic_DNA.
DR   RefSeq; NP_564675.1; NM_104380.1.
DR   AlphaFoldDB; Q3E7K8; -.
DR   SMR; Q3E7K8; -.
DR   STRING; 3702.AT1G55060.1; -.
DR   iPTMnet; Q3E7K8; -.
DR   PaxDb; Q3E7K8; -.
DR   PRIDE; Q3E7K8; -.
DR   ProteomicsDB; 233026; -.
DR   EnsemblPlants; AT1G55060.1; AT1G55060.1; AT1G55060.
DR   GeneID; 841949; -.
DR   Gramene; AT1G55060.1; AT1G55060.1; AT1G55060.
DR   KEGG; ath:AT1G55060; -.
DR   Araport; AT1G55060; -.
DR   TAIR; locus:2827139; AT1G55060.
DR   eggNOG; KOG0001; Eukaryota.
DR   HOGENOM; CLU_010412_0_0_1; -.
DR   InParanoid; Q3E7K8; -.
DR   OMA; FAGKQHE; -.
DR   OrthoDB; 1536766at2759; -.
DR   PhylomeDB; Q3E7K8; -.
DR   PRO; PR:Q3E7K8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q3E7K8; baseline and differential.
DR   Genevisible; Q3E7K8; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:TAIR.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   Pfam; PF00240; ubiquitin; 3.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 3.
DR   SUPFAM; SSF54236; SSF54236; 3.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 3.
PE   3: Inferred from homology;
KW   Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..76
FT                   /note="Ubiquitin-related 1"
FT                   /id="PRO_0000396929"
FT   CHAIN           77..152
FT                   /note="Ubiquitin-related 2"
FT                   /id="PRO_0000396930"
FT   CHAIN           153..228
FT                   /note="Ubiquitin-related 3"
FT                   /id="PRO_0000396931"
FT   PROPEP          229..230
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000396932"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          77..152
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          153..228
FT                   /note="Ubiquitin-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        76
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        152
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        228
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ   SEQUENCE   230 AA;  25843 MW;  4821A4C587A77DF7 CRC64;
     MQIFLKTLTG KTKVLEVESS DTIDNVKAKI QDIEGIPPDQ HRLIFAGKQL EDGRTLADYN
     VQEDSTLHLL LRFRGGMQIF VKTLTGKTIT LEVESSDTID NLKAKIQDKE GIPPDQQRLI
     FAGKQLEDGR TLADYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE SSDTIDNVKA
     KIQDKEGISP DQQRLIFAGK QHEDGRTLAD YNIQKESTLH LVLRLRGGSF
 
 
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