GenomeNet

Database: UniProt
Entry: P0CG47
LinkDB: P0CG47
Original site: P0CG47 
ID   UBB_HUMAN               Reviewed;         229 AA.
AC   P0CG47; P02248; P02249; P02250; P62988; Q29120; Q6LBL4; Q6LDU5;
AC   Q8WYN8; Q91887; Q91888; Q9BWD6; Q9BX98; Q9UEF2; Q9UEG1; Q9UEK8;
AC   Q9UPK7;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   07-SEP-2016, entry version 68.
DE   RecName: Full=Polyubiquitin-B;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Flags: Precursor;
GN   Name=UBB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RX   PubMed=3029682; DOI=10.1093/nar/15.2.443;
RA   Baker R.T., Board P.G.;
RT   "The human ubiquitin gene family: structure of a gene and pseudogenes
RT   from the Ub B subfamily.";
RL   Nucleic Acids Res. 15:443-463(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14745543; DOI=10.1007/s00239-003-2532-4;
RA   Tachikui H., Saitou N., Nakajima T., Hayasaka I., Ishida T., Inoue I.;
RT   "Lineage-specific homogenization of the polyubiquitin gene among human
RT   and great apes.";
RL   J. Mol. Evol. 57:737-744(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Liver, and Lung;
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   [5]
RP   PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Fetal brain cortex;
RA   Lubec G., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [6]
RP   PROTEIN SEQUENCE OF 1-74.
RX   PubMed=1128706; DOI=10.1038/255423a0;
RA   Schlesinger D.H., Goldstein G.;
RT   "Molecular conservation of 74 amino acid sequence of ubiquitin between
RT   cattle and man.";
RL   Nature 255:423-424(1975).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11
RP   AND LYS-48, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16443603; DOI=10.1074/jbc.M512786200;
RA   Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.;
RT   "Alzheimer disease-specific conformation of hyperphosphorylated paired
RT   helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and
RT   Lys-6 ubiquitin conjugation.";
RL   J. Biol. Chem. 281:10825-10838(2006).
RN   [8]
RP   FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018;
RA   Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
RT   "Differential regulation of EGF receptor internalization and
RT   degradation by multiubiquitination within the kinase domain.";
RL   Mol. Cell 21:737-748(2006).
RN   [9]
RP   UBIQUITINATION AT LYS-27.
RX   PubMed=15466860; DOI=10.1074/jbc.M402916200;
RA   Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.;
RT   "Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B
RT   contributes to neuritogenesis.";
RL   J. Biol. Chem. 279:53533-53543(2004).
RN   [10]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48.
RC   TISSUE=Lung adenocarcinoma;
RX   PubMed=17203973; DOI=10.1021/pr060438j;
RA   Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,
RA   Haines D.S., Figeys D.;
RT   "The proteomic reactor facilitates the analysis of affinity-purified
RT   proteins by mass spectrometry: application for identifying
RT   ubiquitinated proteins in human cells.";
RL   J. Proteome Res. 6:298-305(2007).
RN   [11]
RP   UBIQUITINATION AT LYS-63, AND MUTAGENESIS OF LYS-48 AND LYS-63.
RX   PubMed=18719106; DOI=10.1073/pnas.0805685105;
RA   Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X.,
RA   Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
RT   "Polyubiquitination of proliferating cell nuclear antigen by HLTF and
RT   SHPRH prevents genomic instability from stalled replication forks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
RN   [12]
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).
RN   [13]
RP   CLEAVAGE BY UCHL3 (VARIANT UBB(+1)).
RX   PubMed=21762696; DOI=10.1016/j.febslet.2011.06.037;
RA   Dennissen F.J., Kholod N., Hermes D.J., Kemmerling N.,
RA   Steinbusch H.W., Dantuma N.P., van Leeuwen F.W.;
RT   "Mutant ubiquitin (UBB(+1)) associated with neurodegenerative
RT   disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-
RT   L3).";
RL   FEBS Lett. 585:2568-2574(2011).
RN   [14]
RP   IDENTIFICATION OF VARIANT UBB(+1).
RX   PubMed=9422699; DOI=10.1126/science.279.5348.242;
RA   van Leeuwen F.W., de Kleijn D.P., van den Hurk H.H., Neubauer A.,
RA   Sonnemans M.A., Sluijs J.A., Koycu S., Ramdjielal R.D., Salehi A.,
RA   Martens G.J., Grosveld F.G., Peter J., Burbach H., Hol E.M.;
RT   "Frameshift mutants of beta amyloid precursor protein and ubiquitin-B
RT   in Alzheimer's and Down patients.";
RL   Science 279:242-247(1998).
RN   [15]
RP   TISSUE SPECIFICITY (VARIANT UBB(+1)).
RX   PubMed=14597671; DOI=10.1096/fj.03-0205com;
RA   Fischer D.F., De Vos R.A., Van Dijk R., De Vrij F.M., Proper E.A.,
RA   Sonnemans M.A., Verhage M.C., Sluijs J.A., Hobo B., Zouambia M.,
RA   Steur E.N., Kamphorst W., Hol E.M., Van Leeuwen F.W.;
RT   "Disease-specific accumulation of mutant ubiquitin as a marker for
RT   proteasomal dysfunction in the brain.";
RL   FASEB J. 17:2014-2024(2003).
RN   [16]
RP   PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
RX   PubMed=24660806; DOI=10.1042/BJ20140334;
RA   Kazlauskaite A., Kondapalli C., Gourlay R., Campbell D.G.,
RA   Ritorto M.S., Hofmann K., Alessi D.R., Knebel A., Trost M.,
RA   Muqit M.M.;
RT   "Parkin is activated by PINK1-dependent phosphorylation of ubiquitin
RT   at Ser65.";
RL   Biochem. J. 460:127-139(2014).
RN   [17]
RP   PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
RX   PubMed=24751536; DOI=10.1083/jcb.201402104;
RA   Kane L.A., Lazarou M., Fogel A.I., Li Y., Yamano K., Sarraf S.A.,
RA   Banerjee S., Youle R.J.;
RT   "PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase
RT   activity.";
RL   J. Cell Biol. 205:143-153(2014).
RN   [18]
RP   PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
RX   PubMed=24784582; DOI=10.1038/nature13392;
RA   Koyano F., Okatsu K., Kosako H., Tamura Y., Go E., Kimura M.,
RA   Kimura Y., Tsuchiya H., Yoshihara H., Hirokawa T., Endo T., Fon E.A.,
RA   Trempe J.F., Saeki Y., Tanaka K., Matsuda N.;
RT   "Ubiquitin is phosphorylated by PINK1 to activate parkin.";
RL   Nature 510:162-166(2014).
RN   [19]
RP   PHOSPHORYLATION AT SER-65.
RX   PubMed=25527291; DOI=10.15252/embj.201489847;
RA   Wauer T., Swatek K.N., Wagstaff J.L., Gladkova C., Pruneda J.N.,
RA   Michel M.A., Gersch M., Johnson C.M., Freund S.M., Komander D.;
RT   "Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain
RT   assembly and hydrolysis.";
RL   EMBO J. 34:307-325(2015).
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. {ECO:0000269|PubMed:16543144,
CC       ECO:0000269|PubMed:19754430}.
CC   -!- INTERACTION:
CC       Q8IVM0:CCDC50; NbExp=2; IntAct=EBI-413034, EBI-723996;
CC       P28562:DUSP1; NbExp=2; IntAct=EBI-413034, EBI-975493;
CC       Q9UJY5:GGA1; NbExp=3; IntAct=EBI-413034, EBI-447141;
CC       Q9NZ52:GGA3; NbExp=2; IntAct=EBI-413034, EBI-447404;
CC       Q60592:Mast2 (xeno); NbExp=2; IntAct=EBI-413034, EBI-493888;
CC       P33993:MCM7; NbExp=2; IntAct=EBI-413034, EBI-355924;
CC       Q9DLK6:NP (xeno); NbExp=2; IntAct=EBI-413034, EBI-8433218;
CC       P24610:Pax3 (xeno); NbExp=2; IntAct=EBI-413034, EBI-1208116;
CC       Q9UJ41:RABGEF1; NbExp=6; IntAct=EBI-413034, EBI-913954;
CC       Q9Y3C5:RNF11; NbExp=2; IntAct=EBI-413034, EBI-396669;
CC       Q68DV7:RNF43; NbExp=2; IntAct=EBI-413034, EBI-1647060;
CC       Q9HAU4:SMURF2; NbExp=4; IntAct=EBI-413034, EBI-396727;
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 (PARK2), triggering mitophagy (PubMed:24660806,
CC       PubMed:24751536, PubMed:24784582, PubMed:25527291).
CC       Phosphorylation does not affect E1-mediated E2 charging of
CC       ubiquitin but affects discharging of E2 enzymes to form
CC       polyubiquitin chains. It also affects deubiquitination by
CC       deubiquitinase enzymes such as USP30 (PubMed:25527291).
CC       {ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536,
CC       ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291}.
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: The mRNA encoding variant UBB(+1) is produced by an
CC       unknown mechanism involving the deletion of a GT dinucleotide in
CC       the close proximity of a GAGAG motif (PubMed:9422699). This
CC       variant mRNA is found in normal brain, but the encoded protein
CC       accumulates only in brain neurofibrillary tangles and neuritic
CC       plaques in Alzheimer disease and other tauopathies, as well as
CC       polyglutaminopathies (PubMed:14597671). UBB(+1) variant cannot be
CC       used for polyubiquitination, is not effectively degraded by the
CC       proteasome when ubiquitinated and ubiquitinated UBB(+1) is
CC       refractory to disassembly by deubiquitinating enzymes (DUBs). In
CC       healthy brain, UBB(+1) C-terminus can be cleaved by UCHL3
CC       (PubMed:21762696). {ECO:0000305|PubMed:14597671,
CC       ECO:0000305|PubMed:21762696, ECO:0000305|PubMed:9422699}.
CC   -!- MISCELLANEOUS: For a better understanding, features related to
CC       ubiquitin are only indicated for the first chain.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 3 ubiquitin-like domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00214}.
DR   EMBL; X04803; CAA28495.1; -; Genomic_DNA.
DR   EMBL; AB089617; BAC56955.1; -; Genomic_DNA.
DR   EMBL; AC093484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000379; AAH00379.1; -; mRNA.
DR   EMBL; BC009301; AAH09301.1; -; mRNA.
DR   EMBL; BC015127; AAH15127.1; -; mRNA.
DR   EMBL; BC026301; AAH26301.1; -; mRNA.
DR   EMBL; BC031027; AAH31027.1; -; mRNA.
DR   EMBL; BC046123; AAH46123.1; -; mRNA.
DR   CCDS; CCDS11177.1; -.
DR   PIR; A26437; UQHUB.
DR   RefSeq; NP_001268645.1; NM_001281716.1.
DR   RefSeq; NP_001268646.1; NM_001281717.1.
DR   RefSeq; NP_001268647.1; NM_001281718.1.
DR   RefSeq; NP_001268648.1; NM_001281719.1.
DR   RefSeq; NP_001268649.1; NM_001281720.1.
DR   RefSeq; NP_061828.1; NM_018955.3.
DR   UniGene; Hs.356190; -.
DR   UniGene; Hs.730603; -.
DR   UniGene; Hs.741549; -.
DR   PDB; 2KHW; NMR; -; B=153-228.
DR   PDB; 2MBB; NMR; -; B=153-228.
DR   PDB; 2MRO; NMR; -; A=153-228.
DR   PDB; 2MSG; NMR; -; A=153-224.
DR   PDB; 2N13; NMR; -; B=153-228, C=153-229.
DR   PDB; 4UEL; X-ray; 2.30 A; B=153-228.
DR   PDB; 4UF6; X-ray; 3.69 A; B/E/H/K=153-227.
DR   PDB; 4WHV; X-ray; 8.30 A; A/F/G/L=153-228.
DR   PDB; 4WLR; X-ray; 2.00 A; C=153-228.
DR   PDB; 4WUR; X-ray; 3.16 A; B=153-228.
DR   PDB; 4XOF; X-ray; 1.15 A; A=153-228.
DR   PDB; 4ZFR; X-ray; 1.72 A; B=153-228.
DR   PDB; 4ZFT; X-ray; 2.30 A; B/D=153-228.
DR   PDB; 4ZPZ; X-ray; 1.54 A; A/B=153-225.
DR   PDB; 4ZUX; X-ray; 3.82 A; X/c/h/m=153-228.
DR   PDB; 5BNB; X-ray; 2.49 A; E/F/G/I=153-229.
DR   PDB; 5CAW; X-ray; 2.62 A; B/D=153-228.
DR   PDB; 5CRA; X-ray; 2.64 A; C/D=153-227.
DR   PDB; 5CVM; X-ray; 1.90 A; B=153-211.
DR   PDB; 5CVN; X-ray; 3.36 A; D=153-228.
DR   PDB; 5CVO; X-ray; 3.88 A; C/F=153-228.
DR   PDB; 5D0K; X-ray; 2.65 A; B/E/H/K=153-228.
DR   PDB; 5D0M; X-ray; 1.91 A; B=153-228.
DR   PDB; 5DFL; X-ray; 2.10 A; B=153-228.
DR   PDB; 5DK8; X-ray; 1.32 A; A/B=154-227.
DR   PDB; 5E6J; X-ray; 2.85 A; C/F=153-227.
DR   PDB; 5EDV; X-ray; 3.48 A; E/F/G/H=153-228.
DR   PDB; 5IBK; X-ray; 2.50 A; C/F=151-226.
DR   PDB; 5IFR; X-ray; 2.20 A; B=153-227.
DR   PDB; 5JG6; X-ray; 2.00 A; B/C=76-153.
DR   PDBsum; 2KHW; -.
DR   PDBsum; 2MBB; -.
DR   PDBsum; 2MRO; -.
DR   PDBsum; 2MSG; -.
DR   PDBsum; 2N13; -.
DR   PDBsum; 4UEL; -.
DR   PDBsum; 4UF6; -.
DR   PDBsum; 4WHV; -.
DR   PDBsum; 4WLR; -.
DR   PDBsum; 4WUR; -.
DR   PDBsum; 4XOF; -.
DR   PDBsum; 4ZFR; -.
DR   PDBsum; 4ZFT; -.
DR   PDBsum; 4ZPZ; -.
DR   PDBsum; 4ZUX; -.
DR   PDBsum; 5BNB; -.
DR   PDBsum; 5CAW; -.
DR   PDBsum; 5CRA; -.
DR   PDBsum; 5CVM; -.
DR   PDBsum; 5CVN; -.
DR   PDBsum; 5CVO; -.
DR   PDBsum; 5D0K; -.
DR   PDBsum; 5D0M; -.
DR   PDBsum; 5DFL; -.
DR   PDBsum; 5DK8; -.
DR   PDBsum; 5E6J; -.
DR   PDBsum; 5EDV; -.
DR   PDBsum; 5IBK; -.
DR   PDBsum; 5IFR; -.
DR   PDBsum; 5JG6; -.
DR   ProteinModelPortal; P0CG47; -.
DR   SMR; P0CG47; 1-227.
DR   BioGrid; 113162; 163.
DR   IntAct; P0CG47; 70.
DR   MINT; MINT-8084593; -.
DR   STRING; 9606.ENSP00000304697; -.
DR   iPTMnet; P0CG47; -.
DR   PhosphoSite; P0CG47; -.
DR   SwissPalm; P0CG47; -.
DR   DMDM; 302595875; -.
DR   EPD; P0CG47; -.
DR   PaxDb; P0CG47; -.
DR   PeptideAtlas; P0CG47; -.
DR   PRIDE; P0CG47; -.
DR   TopDownProteomics; P0CG47; -.
DR   DNASU; 7314; -.
DR   Ensembl; ENST00000302182; ENSP00000304697; ENSG00000170315.
DR   Ensembl; ENST00000395837; ENSP00000379178; ENSG00000170315.
DR   Ensembl; ENST00000395839; ENSP00000379180; ENSG00000170315.
DR   Ensembl; ENST00000614404; ENSP00000478771; ENSG00000170315.
DR   GeneID; 7314; -.
DR   KEGG; hsa:7314; -.
DR   CTD; 7314; -.
DR   GeneCards; UBB; -.
DR   HGNC; HGNC:12463; UBB.
DR   HPA; CAB013048; -.
DR   HPA; HPA041344; -.
DR   HPA; HPA049132; -.
DR   MalaCards; UBB; -.
DR   MIM; 191339; gene.
DR   neXtProt; NX_P0CG47; -.
DR   eggNOG; KOG0001; Eukaryota.
DR   eggNOG; COG5272; LUCA.
DR   GeneTree; ENSGT00810000125435; -.
DR   InParanoid; P0CG47; -.
DR   KO; K04551; -.
DR   OMA; CPMERIM; -.
DR   OrthoDB; EOG091G178I; -.
DR   PhylomeDB; P0CG47; -.
DR   TreeFam; TF300820; -.
DR   Reactome; R-HSA-110312; Translesion synthesis by REV1.
DR   Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-HSA-110320; Translesion Synthesis by POLH.
DR   Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-HSA-1227986; Signaling by ERBB2.
DR   Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
DR   Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR   Reactome; R-HSA-1253288; Downregulation of ERBB4 signaling.
DR   Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
DR   Reactome; R-HSA-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR   Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR   Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR   Reactome; R-HSA-168928; RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
DR   Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
DR   Reactome; R-HSA-175474; Assembly Of The HIV Virion.
DR   Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR   Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR   Reactome; R-HSA-182971; EGFR downregulation.
DR   Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR   Reactome; R-HSA-202424; Downstream TCR signaling.
DR   Reactome; R-HSA-205043; NRIF signals cell death from the nucleus.
DR   Reactome; R-HSA-209543; p75NTR recruits signalling complexes.
DR   Reactome; R-HSA-209560; NF-kB is activated and signals survival.
DR   Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR   Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
DR   Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR   Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR   Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR   Reactome; R-HSA-2691232; Constitutive Signaling by NOTCH1 HD Domain Mutants.
DR   Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   Reactome; R-HSA-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
DR   Reactome; R-HSA-3134975; Regulation of innate immune responses to cytosolic DNA.
DR   Reactome; R-HSA-3322077; Glycogen synthesis.
DR   Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR   Reactome; R-HSA-3785653; Myoclonic epilepsy of Lafora.
DR   Reactome; R-HSA-400253; Circadian Clock.
DR   Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
DR   Reactome; R-HSA-446652; Interleukin-1 signaling.
DR   Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
DR   Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR   Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-HSA-4641257; Degradation of AXIN.
DR   Reactome; R-HSA-4641258; Degradation of DVL.
DR   Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
DR   Reactome; R-HSA-5205685; Pink/Parkin Mediated Mitophagy.
DR   Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
DR   Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
DR   Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
DR   Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR   Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR   Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
DR   Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
DR   Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
DR   Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
DR   Reactome; R-HSA-5655862; Translesion synthesis by POLK.
DR   Reactome; R-HSA-5656121; Translesion synthesis by POLI.
DR   Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
DR   Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR   Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR   Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR   Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR   Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR   Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR   Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR   Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR   Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
DR   Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
DR   Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR   Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
DR   Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR   Reactome; R-HSA-69298; Association of licensing factors with the pre-replicative complex.
DR   Reactome; R-HSA-69481; G2/M Checkpoints.
DR   Reactome; R-HSA-69541; Stabilization of p53.
DR   Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-HSA-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
DR   Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-HSA-912631; Regulation of signaling by CBL.
DR   Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-HSA-936440; Negative regulators of RIG-I/MDA5 signaling.
DR   Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
DR   Reactome; R-HSA-937039; IRAK1 recruits IKK complex.
DR   Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
DR   Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
DR   Reactome; R-HSA-937072; TRAF6 mediated induction of TAK1 complex.
DR   Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
DR   Reactome; R-HSA-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR   Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR   Reactome; R-HSA-977225; Amyloid fiber formation.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   ChiTaRS; UBB; human.
DR   GeneWiki; Ubiquitin_B; -.
DR   GenomeRNAi; 7314; -.
DR   PRO; PR:P0CG47; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000170315; -.
DR   ExpressionAtlas; P0CG47; baseline and differential.
DR   Genevisible; P0CG47; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
DR   GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR   GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR   GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
DR   GO; GO:0070987; P:error-free translesion synthesis; TAS:Reactome.
DR   GO; GO:0042276; P:error-prone translesion synthesis; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
DR   GO; GO:0005978; P:glycogen biosynthetic process; TAS:Reactome.
DR   GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0036297; P:interstrand cross-link repair; TAS:Reactome.
DR   GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
DR   GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR   GO; GO:0007254; P:JNK cascade; TAS:Reactome.
DR   GO; GO:0016236; P:macroautophagy; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0047497; P:mitochondrion transport along microtubule; IDA:MGI.
DR   GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
DR   GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IMP:MGI.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR   GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR   GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; TAS:Reactome.
DR   GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; TAS:Reactome.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
DR   GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
DR   GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
DR   GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IDA:MGI.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
DR   GO; GO:1902527; P:positive regulation of protein monoubiquitination; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR   GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA:MGI.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0010939; P:regulation of necrotic cell death; TAS:Reactome.
DR   GO; GO:1901214; P:regulation of neuron death; IDA:MGI.
DR   GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:MGI.
DR   GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR   GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR   GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0032479; P:regulation of type I interferon production; TAS:Reactome.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0019985; P:translesion synthesis; TAS:Reactome.
DR   GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0019058; P:viral life cycle; TAS:Reactome.
DR   GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR   GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DR   InterPro; IPR019956; Ubiquitin.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR000626; Ubiquitin_dom.
DR   Pfam; PF00240; ubiquitin; 3.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 3.
DR   SUPFAM; SSF54236; SSF54236; 3.
DR   PROSITE; PS00299; UBIQUITIN_1; 3.
DR   PROSITE; PS50053; UBIQUITIN_2; 3.
PE   1: Evidence at protein level;
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_0000396174.
FT   CHAIN        77    152       Ubiquitin.
FT                                /FTId=PRO_0000396175.
FT   CHAIN       153    228       Ubiquitin.
FT                                /FTId=PRO_0000396176.
FT   PROPEP      229    229
FT                                /FTId=PRO_0000396177.
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   BINDING      54     54       Activating enzyme.
FT   BINDING      72     72       Activating enzyme.
FT   SITE         68     68       Essential for function.
FT   MOD_RES      65     65       Phosphoserine; by PINK1.
FT                                {ECO:0000269|PubMed:24660806,
FT                                ECO:0000269|PubMed:24751536,
FT                                ECO:0000269|PubMed:24784582,
FT                                ECO:0000269|PubMed:25527291}.
FT   CROSSLNK      6      6       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16443603}.
FT   CROSSLNK     11     11       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16443603,
FT                                ECO:0000269|PubMed:16543144}.
FT   CROSSLNK     27     27       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000305|PubMed:15466860}.
FT   CROSSLNK     29     29       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16543144}.
FT   CROSSLNK     48     48       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16443603,
FT                                ECO:0000269|PubMed:16543144,
FT                                ECO:0000269|PubMed:17203973}.
FT   CROSSLNK     63     63       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16543144,
FT                                ECO:0000269|PubMed:18719106}.
FT   CROSSLNK     76     76       Glycyl lysine isopeptide (Gly-Lys)
FT                                (interchain with K-? in acceptor
FT                                proteins).
FT   VARIANT      76    229       GMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
FT                                QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFV
FT                                KTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFA
FT                                GKQLEDGRTLSDYNIQKESTLHLVLRLRGGC -> YADLRE
FT                                DPDRQDHHPGSGAQ (in UBB(+1); loss of
FT                                polyubiquitination; impairs the
FT                                ubiquitin-proteasome pathway; refractory
FT                                to disassembly by DUBs; slow degradation
FT                                by UCHL3).
FT                                /FTId=VAR_066248.
FT   MUTAGEN      48     48       K->R: No effect on HLTF-mediated
FT                                polyubiquitination of PCNA.
FT                                {ECO:0000269|PubMed:18719106}.
FT   MUTAGEN      63     63       K->R: Abolishes HLTF-mediated
FT                                polyubiquitination of PCNA.
FT                                {ECO:0000269|PubMed:18719106}.
FT   MUTAGEN      65     65       S->A: Prevents phosphorylation in case of
FT                                mitophagy. {ECO:0000269|PubMed:24660806,
FT                                ECO:0000269|PubMed:24751536,
FT                                ECO:0000269|PubMed:24784582}.
FT   MUTAGEN      65     65       S->D: Phosphomimetic mutant that binds
FT                                and activates PARK2.
FT                                {ECO:0000269|PubMed:24751536}.
FT   STRAND      154    159       {ECO:0000244|PDB:4XOF}.
FT   STRAND      160    162       {ECO:0000244|PDB:4ZFR}.
FT   STRAND      164    168       {ECO:0000244|PDB:4XOF}.
FT   STRAND      171    174       {ECO:0000244|PDB:2MBB}.
FT   HELIX       175    186       {ECO:0000244|PDB:4XOF}.
FT   HELIX       190    192       {ECO:0000244|PDB:4XOF}.
FT   STRAND      193    197       {ECO:0000244|PDB:4XOF}.
FT   STRAND      206    208       {ECO:0000244|PDB:5CAW}.
FT   HELIX       209    211       {ECO:0000244|PDB:4XOF}.
FT   STRAND      218    223       {ECO:0000244|PDB:4XOF}.
SQ   SEQUENCE   229 AA;  25762 MW;  33011162F1C48BB1 CRC64;
     MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI
     FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE PSDTIENVKA
     KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGC
//
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