UBB_BOVIN
ID UBB_BOVIN Reviewed; 305 AA.
AC P0CG53; O97577; P02248; P02249; P02250; P62990; P80169; Q01235; Q24K23;
AC Q28169; Q28170; Q29120; Q3T0V5; Q3ZCE3; Q862C1; Q862F4; Q862M4; Q862T5;
AC 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 95.
DE RecName: Full=Polyubiquitin-B;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Flags: Precursor;
GN Name=UBB;
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 [MRNA].
RC TISSUE=Seminal vesicle;
RX PubMed=8382528; DOI=10.1016/0167-4781(93)90297-q;
RA Wempe F., Scheit K.H.;
RT "Characterization of a full-length cDNA encoding a bovine four tandem-
RT repeat ubiquitin.";
RL Biochim. Biophys. Acta 1172:209-211(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12658628; DOI=10.1002/mrd.10292;
RA Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T.,
RA Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G.,
RA Izaike Y., Todoroki J., Hashizume K.;
RT "Characterization of gene expression profiles in early bovine pregnancy
RT using a custom cDNA microarray.";
RL Mol. Reprod. Dev. 65:9-18(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum, and Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 142-305.
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 [8]
RP FUNCTION, PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
RX PubMed=26116755; DOI=10.15252/embr.201540352;
RA Kazlauskaite A., Martinez-Torres R.J., Wilkie S., Kumar A., Peltier J.,
RA Gonzalez A., Johnson C., Zhang J., Hope A.G., Peggie M., Trost M.,
RA van Aalten D.M., Alessi D.R., Prescott A.R., Knebel A., Walden H.,
RA Muqit M.M.;
RT "Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal
RT PINK1-dependent phosphorylation and activation.";
RL EMBO Rep. 16:939-954(2015).
CC -!- FUNCTION: [Ubiquitin]: Exists either covalently attached to another
CC protein, or free (unanchored) (By similarity). When covalently bound,
CC it is conjugated to target proteins via an isopeptide bond either as a
CC monomer (monoubiquitin), a polymer linked via different Lys residues of
CC the ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC initiator Met of the ubiquitin (linear polyubiquitin chains)
CC (PubMed:26116755). Polyubiquitin chains, when attached to a target
CC protein, have different functions depending on the Lys residue of the
CC ubiquitin that is linked: Lys-6-linked may be involved in DNA repair;
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 proteotoxic stress response and cell cycle; Lys-33-linked is involved
CC in kinase modification; Lys-48-linked is involved in protein
CC degradation via the proteasome; Lys-63-linked is involved in
CC endocytosis, DNA-damage responses as well as in signaling processes
CC leading to activation of the transcription factor NF-kappa-B (By
CC similarity). Linear polymer chains formed via attachment by the
CC initiator Met lead to cell signaling (By similarity). 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 (By
CC similarity). When polyubiquitin is free (unanchored-polyubiquitin), it
CC also has distinct roles, such as in activation of protein kinases, and
CC in signaling (By similarity). {ECO:0000250|UniProtKB:P0CG47,
CC ECO:0000269|PubMed:26116755}.
CC -!- SUBUNIT: Interacts with SKP1-KMD2A and SKP1-KMD2B complexes.
CC {ECO:0000250|UniProtKB:P0CG47}.
CC -!- INTERACTION:
CC P0CG53; O14964: HGS; Xeno; NbExp=7; IntAct=EBI-5333021, EBI-740220;
CC P0CG53; P38753: HSE1; Xeno; NbExp=2; IntAct=EBI-5333021, EBI-1382;
CC P0CG53; Q92783: STAM; Xeno; NbExp=9; IntAct=EBI-5333021, EBI-752333;
CC P0CG53; P40343: VPS27; Xeno; NbExp=6; IntAct=EBI-5333021, EBI-20380;
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P0CG47}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P0CG47}.
CC -!- PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy
CC (PubMed:26116755). Phosphorylated ubiquitin specifically binds and
CC activates parkin (PRKN), triggering mitophagy (PubMed:26116755).
CC Phosphorylation does not affect E1-mediated E2 charging of ubiquitin
CC but affects discharging of E2 enzymes to form polyubiquitin chains (By
CC similarity). It also affects deubiquitination by deubiquitinase enzymes
CC such as USP30 (By similarity). {ECO:0000250|UniProtKB:P0CG47,
CC ECO:0000269|PubMed:26116755}.
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:P0CG47}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC56573.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC56573.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z18245; CAA79146.1; -; mRNA.
DR EMBL; AB099044; BAC56534.1; -; mRNA.
DR EMBL; AB099083; BAC56573.1; ALT_SEQ; mRNA.
DR EMBL; BC114001; AAI14002.1; -; mRNA.
DR EMBL; M62429; AAA30720.1; -; mRNA.
DR PIR; I45964; I45964.
DR PIR; S29853; S29853.
DR RefSeq; NP_776558.1; NM_174133.2.
DR PDB; 5TR4; X-ray; 2.20 A; B/D=1-76.
DR PDBsum; 5TR4; -.
DR AlphaFoldDB; P0CG53; -.
DR SMR; P0CG53; -.
DR BioGRID; 158705; 2.
DR IntAct; P0CG53; 10.
DR MINT; P0CG53; -.
DR STRING; 9913.ENSBTAP00000022919; -.
DR PaxDb; P0CG53; -.
DR PeptideAtlas; P0CG53; -.
DR PRIDE; P0CG53; -.
DR Ensembl; ENSBTAT00000022919; ENSBTAP00000022919; ENSBTAG00000017246.
DR GeneID; 281370; -.
DR KEGG; bta:281370; -.
DR CTD; 7314; -.
DR VEuPathDB; HostDB:ENSBTAG00000017246; -.
DR VGNC; VGNC:107281; UBB.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00940000162439; -.
DR HOGENOM; CLU_010412_7_0_1; -.
DR InParanoid; P0CG53; -.
DR OMA; VHENTRR; -.
DR OrthoDB; 1536766at2759; -.
DR TreeFam; TF300820; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000017246; Expressed in oocyte 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:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0060613; P:fat pad development; IEA:Ensembl.
DR GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR GO; GO:0007144; P:female meiosis I; IEA:Ensembl.
DR GO; GO:0021888; P:hypothalamus gonadotrophin-releasing hormone neuron development; IEA:Ensembl.
DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; IEA:Ensembl.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
DR GO; GO:1902527; P:positive regulation of protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR GO; GO:1901214; P:regulation of neuron death; IEA:Ensembl.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
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; 4.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 4.
DR SUPFAM; SSF54236; SSF54236; 4.
DR PROSITE; PS00299; UBIQUITIN_1; 4.
DR PROSITE; PS50053; UBIQUITIN_2; 4.
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"
FT /id="PRO_0000396140"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396141"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396142"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396143"
FT PROPEP 305
FT /id="PRO_0000396144"
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 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:0000269|PubMed:26116755"
FT MOD_RES 76
FT /note="ADP-ribosylglycine"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
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 MUTAGEN 65
FT /note="S->A: Non-phosphorylatable. Reduced phosphorylation
FT of human PRKN by an insect Pink1."
FT /evidence="ECO:0000269|PubMed:26116755"
FT CONFLICT 133
FT /note="S -> F (in Ref. 1; CAA79146)"
FT /evidence="ECO:0000305"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:5TR4"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:5TR4"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:5TR4"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:5TR4"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:5TR4"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:5TR4"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5TR4"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:5TR4"
SQ SEQUENCE 305 AA; 34308 MW; 1E6C7878AE958E68 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
LRGGC
