UBC_BOVIN
ID UBC_BOVIN Reviewed; 690 AA.
AC P0CH28; O97577; P02248; P02249; P02250; P0CG52; P62990; P80169; Q01235;
AC Q24K23; Q28169; Q28170; Q29120; Q3T0V5; Q3ZCE3; Q862C1; Q862F4; Q862M4;
AC Q862T5; Q862X8; Q91887; Q91888;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Polyubiquitin-C;
DE Contains:
DE RecName: Full=Ubiquitin-related;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Flags: Precursor;
GN Name=UBC;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 446-690.
RC TISSUE=Kidney;
RX PubMed=1846490; DOI=10.1016/0042-6822(91)90074-l;
RA Meyers G., Tautz N., Dubovi E.J., Thiel H.-J.;
RT "Viral cytopathogenicity correlated with integration of ubiquitin-coding
RT sequences.";
RL Virology 180:602-616(1991).
RN [3]
RP PROTEIN SEQUENCE OF 1-74.
RX PubMed=1170880; DOI=10.1021/bi00681a026;
RA Schlesinger D.H., Goldstein G., Niall H.D.;
RT "The complete amino acid sequence of ubiquitin, an adenylate cyclase
RT stimulating polypeptide probably universal in living cells.";
RL Biochemistry 14:2214-2218(1975).
RN [4]
RP PROTEIN SEQUENCE OF 1-50.
RX PubMed=6254502; DOI=10.1016/0006-291x(80)91188-2;
RA Hamilton J.W., Rouse J.B.;
RT "The biosynthesis of ubiquitin by parathyroid gland.";
RL Biochem. Biophys. Res. Commun. 96:114-120(1980).
RN [5]
RP PROTEIN SEQUENCE OF 1-20.
RC TISSUE=Brain;
RX PubMed=1333954; DOI=10.1111/j.1432-1033.1992.tb17446.x;
RA Zdebska E., Antoniewicz J., Nilsson B., Sandhoff K., Fuerst W., Janik P.,
RA Koscielak J.;
RT "Ganglioside binding proteins of calf brain with ubiquitin-like N-
RT terminals.";
RL Eur. J. Biochem. 210:483-489(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=1322903; DOI=10.2210/pdb1aar/pdb;
RA Cook W.J., Jeffrey L.C., Carson M., Chen Z., Pickart C.M.;
RT "Structure of a diubiquitin conjugate and a model for interaction with
RT ubiquitin conjugating enzyme (E2).";
RL J. Biol. Chem. 267:16467-16471(1992).
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-6-linked may be involved in DNA repair; Lys-11-linked is involved
CC in ERAD (endoplasmic reticulum-associated degradation) and in cell-
CC cycle regulation; Lys-29-linked is involved in proteotoxic stress
CC response and cell cycle; 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, DNA-damage
CC responses as well as in signaling processes leading to activation of
CC the transcription factor NF-kappa-B. Linear polymer chains formed via
CC attachment by the initiator Met lead to cell signaling. Ubiquitin is
CC usually 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 distinct
CC roles, such as in activation of protein kinases, and in signaling (By
CC similarity). {ECO:0000250|UniProtKB:P0CG48}.
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P0CG48}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P0CG48}.
CC -!- PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.
CC Phosphorylated ubiquitin specifically binds and activates parkin
CC (PRKN), triggering mitophagy. Phosphorylation does not affect E1-
CC mediated E2 charging of ubiquitin but affects discharging of E2 enzymes
CC to form polyubiquitin chains. It also affects deubiquitination by
CC deubiquitinase enzymes such as USP30. {ECO:0000250|UniProtKB:P0CG48}.
CC -!- PTM: [Ubiquitin]: Mono-ADP-ribosylated at the C-terminus by PARP9, a
CC component of the PPAR9-DTX3L complex. ADP-ribosylation requires
CC processing by E1 and E2 enzymes and prevents ubiquitin conjugation to
CC substrates such as histones. {ECO:0000250|UniProtKB:P0CG48}.
CC -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. Uba52 and
CC Rps27a genes code for a single copy of ubiquitin fused to the ribosomal
CC proteins L40 and S27a, respectively. UBB and UBC genes code for a
CC polyubiquitin precursor with exact head to tail repeats, the number of
CC repeats differ between species and strains.
CC -!- MISCELLANEOUS: For the sake of clarity sequence features are annotated
CC only for the first chain, and are not repeated for each of the
CC following chains.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; AAFC03038308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M62428; AAA30719.1; -; mRNA.
DR PIR; A90388; UQBO.
DR RefSeq; NP_001193236.1; NM_001206307.1.
DR PDB; 1AAR; X-ray; 2.30 A; A/B=1-76.
DR PDB; 1E0Q; NMR; -; A=1-17.
DR PDB; 1P3Q; X-ray; 1.70 A; U/V=1-76.
DR PDB; 1UZX; X-ray; 1.85 A; B=1-76.
DR PDB; 1V80; NMR; -; A=1-76.
DR PDB; 1V81; NMR; -; A=1-76.
DR PDB; 1WR6; X-ray; 2.60 A; E/F/G/H=1-76.
DR PDB; 1WRD; X-ray; 1.75 A; B=1-76.
DR PDB; 1YD8; X-ray; 2.80 A; U/V=1-76.
DR PDB; 2C7M; X-ray; 2.40 A; B=1-76.
DR PDB; 2C7N; X-ray; 2.10 A; B/D/F/H/J/L=1-76.
DR PDB; 2D3G; X-ray; 1.70 A; A/B=1-76.
DR PDB; 2DX5; X-ray; 3.35 A; B=1-76.
DR PDB; 2FID; X-ray; 2.80 A; A=1-76.
DR PDB; 2FIF; X-ray; 2.49 A; A/C/E=1-76.
DR PDB; 2HD5; X-ray; 1.85 A; B=1-76.
DR PDB; 2OOB; X-ray; 1.90 A; B=1-76.
DR PDB; 2QHO; X-ray; 1.85 A; A/C/E/G=1-76.
DR PDB; 2WWZ; X-ray; 1.40 A; A/B=1-76.
DR PDB; 2WX0; X-ray; 2.40 A; A/B/E/F=1-76.
DR PDB; 2WX1; X-ray; 3.00 A; A/B=1-76.
DR PDB; 2XBB; X-ray; 2.68 A; C/D=1-76.
DR PDB; 2ZCC; X-ray; 1.40 A; A/B/C=1-76.
DR PDB; 3H1U; X-ray; 3.00 A; A/B=1-76.
DR PDB; 3M3J; X-ray; 1.60 A; A/B/C/D/E/F=1-76.
DR PDB; 4BBN; X-ray; 2.51 A; C=1-76, F=1-75.
DR PDB; 4XKH; X-ray; 3.00 A; A/B/D/F/G/I=1-76.
DR PDB; 4XYZ; X-ray; 1.65 A; A/B=609-684.
DR PDB; 6A42; X-ray; 1.70 A; A=1-76.
DR PDBsum; 1AAR; -.
DR PDBsum; 1E0Q; -.
DR PDBsum; 1P3Q; -.
DR PDBsum; 1UZX; -.
DR PDBsum; 1V80; -.
DR PDBsum; 1V81; -.
DR PDBsum; 1WR6; -.
DR PDBsum; 1WRD; -.
DR PDBsum; 1YD8; -.
DR PDBsum; 2C7M; -.
DR PDBsum; 2C7N; -.
DR PDBsum; 2D3G; -.
DR PDBsum; 2DX5; -.
DR PDBsum; 2FID; -.
DR PDBsum; 2FIF; -.
DR PDBsum; 2HD5; -.
DR PDBsum; 2OOB; -.
DR PDBsum; 2QHO; -.
DR PDBsum; 2WWZ; -.
DR PDBsum; 2WX0; -.
DR PDBsum; 2WX1; -.
DR PDBsum; 2XBB; -.
DR PDBsum; 2ZCC; -.
DR PDBsum; 3H1U; -.
DR PDBsum; 3M3J; -.
DR PDBsum; 4BBN; -.
DR PDBsum; 4XKH; -.
DR PDBsum; 4XYZ; -.
DR PDBsum; 6A42; -.
DR AlphaFoldDB; P0CH28; -.
DR SMR; P0CH28; -.
DR BioGRID; 160681; 16.
DR STRING; 9913.ENSBTAP00000053003; -.
DR PRIDE; P0CH28; -.
DR Ensembl; ENSBTAT00000046011; ENSBTAP00000053003; ENSBTAG00000032436.
DR GeneID; 444874; -.
DR KEGG; bta:444874; -.
DR CTD; 7316; -.
DR VEuPathDB; HostDB:ENSBTAG00000032436; -.
DR VGNC; VGNC:107263; UBC.
DR GeneTree; ENSGT00940000163900; -.
DR InParanoid; P0CH28; -.
DR OMA; HLTMQIF; -.
DR OrthoDB; 1536766at2759; -.
DR EvolutionaryTrace; P0CH28; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000032436; Expressed in intramuscular adipose tissue and 108 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
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 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; 9.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 9.
DR SUPFAM; SSF54236; SSF54236; 9.
DR PROSITE; PS00299; UBIQUITIN_1; 9.
DR PROSITE; PS50053; UBIQUITIN_2; 9.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin-related"
FT /id="PRO_0000114792"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396145"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396146"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396147"
FT CHAIN 305..380
FT /note="Ubiquitin"
FT /id="PRO_0000396148"
FT CHAIN 381..456
FT /note="Ubiquitin"
FT /id="PRO_0000396149"
FT CHAIN 457..532
FT /note="Ubiquitin"
FT /id="PRO_0000396150"
FT CHAIN 533..608
FT /note="Ubiquitin"
FT /id="PRO_0000396151"
FT CHAIN 609..684
FT /note="Ubiquitin"
FT /id="PRO_0000396152"
FT PROPEP 685..690
FT /id="PRO_0000396153"
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 DOMAIN 229..304
FT /note="Ubiquitin-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 305..380
FT /note="Ubiquitin-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 381..456
FT /note="Ubiquitin-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 457..532
FT /note="Ubiquitin-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 533..608
FT /note="Ubiquitin-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 609..684
FT /note="Ubiquitin-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT SITE 54
FT /note="Interacts with activating enzyme"
FT SITE 68
FT /note="Essential for function"
FT SITE 72
FT /note="Interacts with activating enzyme"
FT MOD_RES 65
FT /note="Phosphoserine; by PINK1"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT MOD_RES 76
FT /note="ADP-ribosylglycine"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
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 CONFLICT 609..614
FT /note="MQIFVK -> VLSSPF (in Ref. 2; AAA30719)"
FT /evidence="ECO:0000305"
FT STRAND 610..615
FT /evidence="ECO:0007829|PDB:2WWZ"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:2C7M"
FT STRAND 620..624
FT /evidence="ECO:0007829|PDB:2WWZ"
FT HELIX 631..642
FT /evidence="ECO:0007829|PDB:2WWZ"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:2WWZ"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:2WWZ"
FT STRAND 660..663
FT /evidence="ECO:0007829|PDB:1WR6"
FT HELIX 665..667
FT /evidence="ECO:0007829|PDB:2WWZ"
FT STRAND 674..679
FT /evidence="ECO:0007829|PDB:2WWZ"
SQ SEQUENCE 690 AA; 77570 MW; 9C226467B8A4FBCA CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKGKI QEKEGIPPDQ 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 LRGGVLSSPF
