UBB_RAT
ID UBB_RAT Reviewed; 305 AA.
AC P0CG51; P02248; P02249; P02250; P62989; Q29120; Q63446; Q91887; Q91888;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Polyubiquitin-B;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Flags: Precursor;
GN Name=Ubb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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].
RC TISSUE=Heart, and Pituitary;
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 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 calbindin9kDa in
RT 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.
RN [5]
RP PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF LEU-8; GLN-49; LYS-63 AND
RP GLU-64.
RX PubMed=29475881; DOI=10.15252/embr.201744981;
RA Rasool S., Soya N., Truong L., Croteau N., Lukacs G.L., Trempe J.F.;
RT "PINK1 autophosphorylation is required for ubiquitin recognition.";
RL EMBO Rep. 19:0-0(2018).
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.
CC {ECO:0000250|UniProtKB:P0CG47}.
CC -!- SUBUNIT: Interacts with SKP1-KMD2A and SKP1-KMD2B complexes.
CC {ECO:0000250|UniProtKB:P0CG47}.
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:29475881). Phosphorylated ubiquitin specifically binds and
CC activates parkin (PRKN), triggering mitophagy (By similarity).
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:29475881}.
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}.
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DR EMBL; D16554; BAA03983.1; -; mRNA.
DR EMBL; BC060312; AAH60312.1; -; mRNA.
DR EMBL; BC070919; AAH70919.1; -; mRNA.
DR AlphaFoldDB; P0CG51; -.
DR SMR; P0CG51; -.
DR BioGRID; 251381; 4.
DR CORUM; P0CG51; -.
DR IntAct; P0CG51; 1.
DR MINT; P0CG51; -.
DR iPTMnet; P0CG51; -.
DR PhosphoSitePlus; P0CG51; -.
DR jPOST; P0CG51; -.
DR RGD; 621562; Ubb.
DR InParanoid; P0CG51; -.
DR PRO; PR:P0CG51; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
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:0060612; P:adipose tissue development; ISO:RGD.
DR GO; GO:0097009; P:energy homeostasis; ISO:RGD.
DR GO; GO:0060613; P:fat pad development; ISO:RGD.
DR GO; GO:0008585; P:female gonad development; ISO:RGD.
DR GO; GO:0007144; P:female meiosis I; ISO:RGD.
DR GO; GO:0021888; P:hypothalamus gonadotrophin-releasing hormone neuron development; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:0007141; P:male meiosis I; ISO:RGD.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; ISO:RGD.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR GO; GO:1902527; P:positive regulation of protein monoubiquitination; ISO:RGD.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:RGD.
DR GO; GO:1901214; P:regulation of neuron death; ISO:RGD.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:RGD.
DR GO; GO:0072520; P:seminiferous tubule development; ISO:RGD.
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 ADP-ribosylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000114806"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396238"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396239"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396240"
FT PROPEP 305
FT /id="PRO_0000396241"
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:29475881"
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 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 105
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT MUTAGEN 8
FT /note="L->N: Rate of phosphorylation by an insect Pink1 is
FT very slightly increased."
FT /evidence="ECO:0000269|PubMed:29475881"
FT MUTAGEN 49
FT /note="Q->E: Rate of phosphorylation by an insect Pink1 is
FT slightly decreased."
FT /evidence="ECO:0000269|PubMed:29475881"
FT MUTAGEN 63
FT /note="K->Q: Rate of phosphorylation by an insect Pink1 is
FT very slightly increased."
FT /evidence="ECO:0000269|PubMed:29475881"
FT MUTAGEN 64
FT /note="E->Q: Rate of phosphorylation by an insect Pink1 is
FT increased."
FT /evidence="ECO:0000269|PubMed:29475881"
SQ SEQUENCE 305 AA; 34369 MW; 0B8C7878AE958E68 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
LRGGY
