(data stored in ACNUC16935 zone)

SWISSPROT: UBC_RAT

ID   UBC_RAT                 Reviewed;         810 AA.
AC   Q63429; Q3ZBA1;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   10-MAY-2017, entry version 101.
DE   RecName: Full=Polyubiquitin-C;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=Ubiquitin-related;
DE   Flags: Precursor;
GN   Name=Ubc;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Brain cortex, and Hippocampus;
RX   PubMed=8018730; DOI=10.1016/0167-4781(94)90020-5;
RA   Hayashi T., Noga M., Matsuda M.;
RT   "Nucleotide sequence and expression of the rat polyubiquitin mRNA.";
RL   Biochim. Biophys. Acta 1218:232-234(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 381-810.
RC   TISSUE=Prostate;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-76.
RC   STRAIN=Wistar; TISSUE=Duodenum;
RX   PubMed=8031840; DOI=10.1016/0304-4165(94)90135-X;
RA   Hubbard M.J., Carne A.;
RT   "Differential feeding-related regulation of ubiquitin and
RT   calbindin9kDa in rat duodenum.";
RL   Biochim. Biophys. Acta 1200:191-196(1994).
RN   [4]
RP   PROTEIN SEQUENCE OF 30-42 AND 55-72, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Diao W., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: Ubiquitin: Exists either covalently attached to another
CC       protein, or free (unanchored). When covalently bound, it is
CC       conjugated to target proteins via an isopeptide bond either as a
CC       monomer (monoubiquitin), a polymer linked via different Lys
CC       residues of the ubiquitin (polyubiquitin chains) or a linear
CC       polymer linked via the initiator Met of the ubiquitin (linear
CC       polyubiquitin chains). Polyubiquitin chains, when attached to a
CC       target protein, have different functions depending on the Lys
CC       residue of the ubiquitin that is linked: Lys-6-linked may be
CC       involved in DNA repair; Lys-11-linked is involved in ERAD
CC       (endoplasmic reticulum-associated degradation) and in cell-cycle
CC       regulation; Lys-29-linked is involved in lysosomal degradation;
CC       Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC       involved in protein degradation via the proteasome; Lys-63-linked
CC       is involved in endocytosis, DNA-damage responses as well as in
CC       signaling processes leading to activation of the transcription
CC       factor NF-kappa-B. Linear polymer chains formed via attachment by
CC       the initiator Met lead to cell signaling. Ubiquitin is usually
CC       conjugated to Lys residues of target proteins, however, in rare
CC       cases, conjugation to Cys or Ser residues has been observed. When
CC       polyubiquitin is free (unanchored-polyubiquitin), it also has
CC       distinct roles, such as in activation of protein kinases, and in
CC       signaling (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- PTM: Ubiquitin: Phosphorylated at Ser-65 by PINK1 during
CC       mitophagy. Phosphorylated ubiquitin specifically binds and
CC       activates parkin (PRKN), triggering mitophagy. Phosphorylation
CC       does not affect E1-mediated E2 charging of ubiquitin but affects
CC       discharging of E2 enzymes to form polyubiquitin chains. It also
CC       affects deubiquitination by deubiquitinase enzymes such as USP30.
CC       {ECO:0000250|UniProtKB:P0CG48}.
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. Uba52
CC       and Rps27a genes code for a single copy of ubiquitin fused to the
CC       ribosomal proteins L40 and S27a, respectively. UBB and UBC genes
CC       code for a polyubiquitin precursor with exact head to tail
CC       repeats, the number of repeats differ between species and strains.
CC   -!- MISCELLANEOUS: For the sake of clarity sequence features are
CC       annotated only for the first chain, and are not repeated for each
CC       of the following chains.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
DR   EMBL; D17296; BAA04129.1; -; mRNA.
DR   EMBL; BC103477; AAI03478.1; -; mRNA.
DR   PIR; S45359; S45359.
DR   RefSeq; NP_059010.1; NM_017314.1.
DR   UniGene; Rn.3761; -.
DR   PDB; 5L9U; EM; 6.40 A; S=1-78.
DR   PDBsum; 5L9U; -.
DR   ProteinModelPortal; Q63429; -.
DR   SMR; Q63429; -.
DR   BioGrid; 248372; 817.
DR   IntAct; Q63429; 1.
DR   STRING; 10116.ENSRNOP00000043934; -.
DR   iPTMnet; Q63429; -.
DR   PhosphoSitePlus; Q63429; -.
DR   PaxDb; Q63429; -.
DR   PRIDE; Q63429; -.
DR   GeneID; 50522; -.
DR   KEGG; rno:50522; -.
DR   UCSC; RGD:621244; rat.
DR   CTD; 7316; -.
DR   RGD; 621244; Ubc.
DR   eggNOG; KOG0001; Eukaryota.
DR   eggNOG; COG5272; LUCA.
DR   HOGENOM; HOG000233942; -.
DR   HOVERGEN; HBG000057; -.
DR   InParanoid; Q63429; -.
DR   KO; K08770; -.
DR   PhylomeDB; Q63429; -.
DR   PRO; PR:Q63429; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:RGD.
DR   InterPro; IPR019956; Ubiquitin.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR000626; Ubiquitin_dom.
DR   Pfam; PF00240; ubiquitin; 10.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 10.
DR   SUPFAM; SSF54236; SSF54236; 10.
DR   PROSITE; PS00299; UBIQUITIN_1; 10.
DR   PROSITE; PS50053; UBIQUITIN_2; 10.
PE   1: Evidence at protein level;
DR   PRODOM; Q63429.
DR   SWISS-2DPAGE; Q63429.
KW   3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation.
FT   CHAIN         1     76       Ubiquitin.
FT                                /FTId=PRO_5000139688.
FT   CHAIN        77    152       Ubiquitin.
FT                                /FTId=PRO_5000139689.
FT   CHAIN       153    228       Ubiquitin.
FT                                /FTId=PRO_5000139690.
FT   CHAIN       229    304       Ubiquitin.
FT                                /FTId=PRO_5000139691.
FT   CHAIN       305    380       Ubiquitin.
FT                                /FTId=PRO_5000139692.
FT   CHAIN       381    456       Ubiquitin.
FT                                /FTId=PRO_5000139693.
FT   CHAIN       457    532       Ubiquitin.
FT                                /FTId=PRO_5000139694.
FT   CHAIN       533    608       Ubiquitin.
FT                                /FTId=PRO_5000139695.
FT   CHAIN       609    684       Ubiquitin.
FT                                /FTId=PRO_5000139696.
FT   CHAIN       685    760       Ubiquitin.
FT                                /FTId=PRO_5000139697.
FT   CHAIN       761    810       Ubiquitin-related.
FT                                /FTId=PRO_5000139698.
FT   DOMAIN        1     76       Ubiquitin-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   DOMAIN       77    152       Ubiquitin-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   DOMAIN      153    228       Ubiquitin-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   DOMAIN      229    304       Ubiquitin-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   DOMAIN      305    380       Ubiquitin-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   DOMAIN      381    456       Ubiquitin-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   DOMAIN      457    532       Ubiquitin-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   DOMAIN      533    608       Ubiquitin-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   DOMAIN      609    684       Ubiquitin-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   DOMAIN      685    760       Ubiquitin-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   BINDING     130    130       Activating enzyme. {ECO:0000250}.
FT   BINDING     148    148       Activating enzyme. {ECO:0000250}.
FT   SITE        144    144       Essential for function. {ECO:0000250}.
FT   MOD_RES      65     65       Phosphoserine; by PINK1.
FT                                {ECO:0000250|UniProtKB:P0CG48}.
FT   MOD_RES     141    141       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P0CG48}.
FT   CROSSLNK     48     48       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P0CH28}.
FT   CROSSLNK     76     76       Glycyl lysine isopeptide (Gly-Lys)
FT                                (interchain with K-? in acceptor
FT                                proteins). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   CROSSLNK     82     82       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P0CG48}.
FT   CROSSLNK     87     87       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P0CG48}.
FT   CROSSLNK    105    105       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P0CG48}.
FT   CROSSLNK    124    124       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P0CG48}.
FT   CROSSLNK    139    139       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P0CG48}.
FT   CONFLICT    776    776       E -> D (in Ref. 2; AAI03478).
FT                                {ECO:0000305}.
SQ   SEQUENCE   810 AA;  91087 MW;  4D4ADB697ADA3315 CRC64;
     MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI
     FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE PSDTIENVKA
     KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
     ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
     LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL
     SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ
     QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE
     NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL
     TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH
     LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED
     GRTLSDYNIQ KESTLHLVLR LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI
     PPDQQRLIFA GKQLEDGRTL SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS
     VNTKKVKQED TRTFLTTVSR KSPSCACSWV
//

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