UBC_MOUSE
ID UBC_MOUSE Reviewed; 734 AA.
AC P0CG50; E9QKI0; P02248; P02249; P02250; P62991; Q29120; Q62317; Q64223;
AC Q8VCH1; Q91887; Q91888; Q9CXY4; Q9CZM0; Q9D1R5; Q9D8D9; Q9ET23; Q9ET24;
AC Q9Z0H9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Polyubiquitin-C;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=Ubiquitin-related 1;
DE Contains:
DE RecName: Full=Ubiquitin-related 2;
DE Flags: Precursor;
GN Name=Ubc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12107596; DOI=10.1007/s00239-002-2318-0;
RA Perelygin A.A., Kondrashov F.A., Rogozin I.B., Brinton M.A.;
RT "Evolution of the mouse polyubiquitin-C gene.";
RL J. Mol. Evol. 55:202-210(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 609-734.
RC STRAIN=C57BL/6J;
RX PubMed=8631027;
RA Ishiguro T., Nakajima M., Naito M., Muto T., Tsuruo T.;
RT "Identification of genes differentially expressed in B16 murine melanoma
RT sublines with different metastatic potentials.";
RL Cancer Res. 56:875-879(1996).
RN [4]
RP REVIEW, AND FUNCTION.
RX PubMed=19754430; DOI=10.1042/bst0370937;
RA Komander D.;
RT "The emerging complexity of protein ubiquitination.";
RL Biochem. Soc. Trans. 37:937-953(2009).
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:0000303|PubMed:19754430}.
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; AF285161; AAG00512.1; -; Genomic_DNA.
DR EMBL; AF285162; AAG00513.1; -; Genomic_DNA.
DR EMBL; AC138613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D50527; BAA09096.1; -; mRNA.
DR CCDS; CCDS19684.2; -.
DR PIR; A49007; A49007.
DR PIR; S11296; S11296.
DR RefSeq; NP_062613.3; NM_019639.4.
DR PDB; 2ZNV; X-ray; 1.60 A; B/C/E/F=1-76.
DR PDB; 3A1Q; X-ray; 2.20 A; A/B/D/E=1-76.
DR PDB; 3A9J; X-ray; 1.18 A; A/B=1-76.
DR PDB; 3A9K; X-ray; 1.40 A; A/B=1-76.
DR PDB; 3VHT; X-ray; 2.40 A; C=1-76.
DR PDB; 3WWQ; X-ray; 1.90 A; A/B/D/E/G/H/J/K=609-684.
DR PDB; 3WXG; X-ray; 3.10 A; B/E=609-684, C/F=609-680.
DR PDB; 4NQL; X-ray; 2.30 A; B/C=609-684.
DR PDB; 6N5M; X-ray; 3.01 A; A=1-76.
DR PDBsum; 2ZNV; -.
DR PDBsum; 3A1Q; -.
DR PDBsum; 3A9J; -.
DR PDBsum; 3A9K; -.
DR PDBsum; 3VHT; -.
DR PDBsum; 3WWQ; -.
DR PDBsum; 3WXG; -.
DR PDBsum; 4NQL; -.
DR PDBsum; 6N5M; -.
DR AlphaFoldDB; P0CG50; -.
DR BMRB; P0CG50; -.
DR SMR; P0CG50; -.
DR BioGRID; 204403; 463.
DR IntAct; P0CG50; 2.
DR STRING; 10090.ENSMUSP00000115578; -.
DR iPTMnet; P0CG50; -.
DR PhosphoSitePlus; P0CG50; -.
DR SwissPalm; P0CG50; -.
DR REPRODUCTION-2DPAGE; P62991; -.
DR jPOST; P0CG50; -.
DR MaxQB; P0CG50; -.
DR PaxDb; P0CG50; -.
DR PRIDE; P0CG50; -.
DR Antibodypedia; 3954; 260 antibodies from 32 providers.
DR DNASU; 22190; -.
DR Ensembl; ENSMUST00000136312; ENSMUSP00000114180; ENSMUSG00000008348.
DR Ensembl; ENSMUST00000156249; ENSMUSP00000115578; ENSMUSG00000008348.
DR GeneID; 22190; -.
DR KEGG; mmu:22190; -.
DR UCSC; uc008zri.2; mouse.
DR CTD; 7316; -.
DR MGI; MGI:98889; Ubc.
DR VEuPathDB; HostDB:ENSMUSG00000008348; -.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00940000163900; -.
DR HOGENOM; CLU_010412_1_0_1; -.
DR InParanoid; P0CG50; -.
DR OMA; MASEMQI; -.
DR OrthoDB; 1536766at2759; -.
DR PhylomeDB; P0CG50; -.
DR TreeFam; TF354256; -.
DR BioGRID-ORCS; 22190; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Ubc; mouse.
DR EvolutionaryTrace; P0CG50; -.
DR PRO; PR:P0CG50; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P0CG50; protein.
DR Bgee; ENSMUSG00000008348; Expressed in granulocyte and 262 other tissues.
DR ExpressionAtlas; P0CG50; baseline and differential.
DR Genevisible; P0CG50; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
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; 10.
DR PROSITE; PS00299; UBIQUITIN_1; 9.
DR PROSITE; PS50053; UBIQUITIN_2; 9.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Cytoplasm; Isopeptide bond; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396192"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396193"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396194"
FT CHAIN 229..304
FT /note="Ubiquitin-related 1"
FT /id="PRO_0000396195"
FT CHAIN 305..380
FT /note="Ubiquitin"
FT /id="PRO_0000396196"
FT CHAIN 381..456
FT /note="Ubiquitin"
FT /id="PRO_0000396197"
FT CHAIN 457..532
FT /note="Ubiquitin"
FT /id="PRO_0000396198"
FT CHAIN 533..608
FT /note="Ubiquitin"
FT /id="PRO_0000396199"
FT CHAIN 609..684
FT /note="Ubiquitin"
FT /id="PRO_0000396200"
FT CHAIN 685..734
FT /note="Ubiquitin-related 2"
FT /id="PRO_0000396201"
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 75
FT /note="G -> GGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIF
FT AGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKA
FT KIQDKEGIPPDQQRLIFAGKQLEGGRTLSDYNIQKESTLHLVLRLRG (in Ref. 1;
FT AAG00513)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="P -> S (in Ref. 1; AAG00512/AAG00513)"
FT /evidence="ECO:0000305"
FT STRAND 533..542
FT /evidence="ECO:0007829|PDB:6N5M"
FT STRAND 544..549
FT /evidence="ECO:0007829|PDB:6N5M"
FT HELIX 555..565
FT /evidence="ECO:0007829|PDB:6N5M"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:6N5M"
FT STRAND 573..577
FT /evidence="ECO:0007829|PDB:6N5M"
FT TURN 588..592
FT /evidence="ECO:0007829|PDB:6N5M"
FT STRAND 598..603
FT /evidence="ECO:0007829|PDB:6N5M"
FT STRAND 610..615
FT /evidence="ECO:0007829|PDB:3A9J"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:2ZNV"
FT STRAND 620..624
FT /evidence="ECO:0007829|PDB:3A9J"
FT HELIX 631..642
FT /evidence="ECO:0007829|PDB:3A9J"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:3A9J"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:3A9J"
FT STRAND 660..663
FT /evidence="ECO:0007829|PDB:3WXG"
FT HELIX 665..667
FT /evidence="ECO:0007829|PDB:3A9J"
FT STRAND 674..679
FT /evidence="ECO:0007829|PDB:3A9J"
SQ SEQUENCE 734 AA; 82550 MW; EDD9B8556FF81D5B 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 TLTGKTITLD VEPSVTTKKV KQEDRRTFLT
TVSKKSPPCA CSWV
