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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   03-SEP-2014, entry version 45.
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=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).
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.
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 (By similarity).
CC       Nucleus (By similarity).
CC   -!- PTM: Ubiquitin: Phosphorylated at Ser-65 by PINK1 during
CC       mitophagy. Phosphorylated ubiquitin specifically binds and
CC       activates parkin (PARK2), triggering mitophagy.
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).
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.
CC   -!- SIMILARITY: Contains 3 ubiquitin-like domains.
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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   ProteinModelPortal; P0CG47; -.
DR   SMR; P0CG47; 1-227.
DR   BioGrid; 113162; 59.
DR   IntAct; P0CG47; 66.
DR   MINT; MINT-8084593; -.
DR   PhosphoSite; P0CG47; -.
DR   DMDM; 302595875; -.
DR   MaxQB; P0CG47; -.
DR   PRIDE; P0CG47; -.
DR   DNASU; 7314; -.
DR   Ensembl; ENST00000302182; ENSP00000304697; ENSG00000170315.
DR   Ensembl; ENST00000395837; ENSP00000379178; ENSG00000170315.
DR   Ensembl; ENST00000395839; ENSP00000379180; ENSG00000170315.
DR   GeneID; 7314; -.
DR   KEGG; hsa:7314; -.
DR   UCSC; uc002gpx.3; human.
DR   CTD; 7314; -.
DR   GeneCards; GC17P016301; -.
DR   HGNC; HGNC:12463; UBB.
DR   HPA; CAB013048; -.
DR   HPA; HPA041344; -.
DR   HPA; HPA049132; -.
DR   MIM; 191339; gene.
DR   neXtProt; NX_P0CG47; -.
DR   KO; K04551; -.
DR   OMA; LTHRIKM; -.
DR   PhylomeDB; P0CG47; -.
DR   TreeFam; TF300820; -.
DR   Reactome; REACT_111080; Spry regulation of FGF signaling.
DR   Reactome; REACT_111178; ER-Phagosome pathway.
DR   Reactome; REACT_111184; Negative regulation of FGFR signaling.
DR   Reactome; REACT_1156; Orc1 removal from chromatin.
DR   Reactome; REACT_115662; Downregulation of ERBB2:ERBB3 signaling.
DR   Reactome; REACT_115755; Signaling by ERBB2.
DR   Reactome; REACT_115828; Downregulation of ERBB4 signaling.
DR   Reactome; REACT_115831; ISG15 antiviral mechanism.
DR   Reactome; REACT_115852; Signaling by constitutively active EGFR.
DR   Reactome; REACT_115893; Membrane binding and targetting of GAG proteins.
DR   Reactome; REACT_1181; Association of licensing factors with the pre-replicative complex.
DR   Reactome; REACT_118614; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   Reactome; REACT_118656; Activation of NF-kappaB in B cells.
DR   Reactome; REACT_118780; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; REACT_120726; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR   Reactome; REACT_120727; Downregulation of TGF-beta receptor signaling.
DR   Reactome; REACT_120734; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR   Reactome; REACT_120916; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; REACT_121111; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; REACT_1221; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; REACT_12484; EGFR downregulation.
DR   Reactome; REACT_12555; Downstream TCR signaling.
DR   Reactome; REACT_13415; p75NTR recruits signalling complexes.
DR   Reactome; REACT_13464; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR   Reactome; REACT_13643; NRIF signals cell death from the nucleus.
DR   Reactome; REACT_13696; NF-kB is activated and signals survival.
DR   Reactome; REACT_150471; Separation of Sister Chromatids.
DR   Reactome; REACT_160089; Constitutive Signaling by NOTCH1 HD Domain Mutants.
DR   Reactome; REACT_160189; Stimuli-sensing channels.
DR   Reactome; REACT_160205; NOTCH2 Activation and Transmission of Signal to the Nucleus.
DR   Reactome; REACT_160243; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; REACT_160254; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   Reactome; REACT_160315; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; REACT_1614; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; REACT_163977; Regulation of innate immune responses to cytosolic DNA.
DR   Reactome; REACT_163994; FCERI mediated NF-kB activation.
DR   Reactome; REACT_169168; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; REACT_169208; Glycogen synthesis.
DR   Reactome; REACT_169325; Oncogene Induced Senescence.
DR   Reactome; REACT_169436; Oxidative Stress Induced Senescence.
DR   Reactome; REACT_172638; Asymmetric localization of PCP proteins.
DR   Reactome; REACT_18265; Regulation of the Fanconi anemia pathway.
DR   Reactome; REACT_18410; Fanconi Anemia pathway.
DR   Reactome; REACT_1949; CDT1 association with the CDC6:ORC:origin complex.
DR   Reactome; REACT_199384; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   Reactome; REACT_200716; regulation of FZD by ubiquitination.
DR   Reactome; REACT_200731; deactivation of the beta-catenin transactivating complex.
DR   Reactome; REACT_200766; degradation of AXIN.
DR   Reactome; REACT_200777; TCF dependent signaling in response to WNT.
DR   Reactome; REACT_200783; Myoclonic epilepsy of Lafora.
DR   Reactome; REACT_200841; degradation of DVL.
DR   Reactome; REACT_20549; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; REACT_21281; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
DR   Reactome; REACT_21368; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR   Reactome; REACT_21399; activated TAK1 mediates p38 MAPK activation.
DR   Reactome; REACT_22442; Interleukin-1 signaling.
DR   Reactome; REACT_225574; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   Reactome; REACT_23787; Regulation of signaling by CBL.
DR   Reactome; REACT_24918; IRAK1 recruits IKK complex.
DR   Reactome; REACT_24941; Circadian Clock.
DR   Reactome; REACT_25018; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR   Reactome; REACT_25120; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
DR   Reactome; REACT_25148; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
DR   Reactome; REACT_25271; Negative regulators of RIG-I/MDA5 signaling.
DR   Reactome; REACT_25325; AUF1 (hnRNP D0) destabilizes mRNA.
DR   Reactome; REACT_25351; TRAF6 mediated induction of TAK1 complex.
DR   Reactome; REACT_25354; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR   Reactome; REACT_25359; RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
DR   Reactome; REACT_25374; IKK complex recruitment mediated by RIP1.
DR   Reactome; REACT_25380; IRAK2 mediated activation of TAK1 complex.
DR   Reactome; REACT_27258; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; REACT_4; Ubiquitin-dependent degradation of Cyclin D1.
DR   Reactome; REACT_6359; Budding and maturation of HIV virion.
DR   Reactome; REACT_6761; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; REACT_6785; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; REACT_6818; Assembly Of The HIV Virion.
DR   Reactome; REACT_6820; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; REACT_6821; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; REACT_6871; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; REACT_75776; NOD1/2 Signaling Pathway.
DR   Reactome; REACT_75842; Antigen processing: Ubiquitination & Proteasome degradation.
DR   Reactome; REACT_821; Cyclin D associated events in G1.
DR   Reactome; REACT_9003; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; REACT_9031; Vpu mediated degradation of CD4.
DR   Reactome; REACT_9453; Vif-mediated degradation of APOBEC3G.
DR   ChiTaRS; UBB; human.
DR   GeneWiki; Ubiquitin_B; -.
DR   GenomeRNAi; 7314; -.
DR   NextBio; 28592; -.
DR   PRO; PR:P0CG47; -.
DR   ArrayExpress; P0CG47; -.
DR   Bgee; P0CG47; -.
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:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
DR   GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR   GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
DR   GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
DR   GO; GO:0071456; P:cellular response to hypoxia; TAS:Reactome.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; 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:0006281; P:DNA repair; TAS:Reactome.
DR   GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; 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:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0006006; P:glucose metabolic process; 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: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:0061024; P:membrane organization; TAS:Reactome.
DR   GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
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: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:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0007220; P:Notch receptor processing; TAS:Reactome.
DR   GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR   GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
DR   GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
DR   GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR   GO; GO:0032479; P:regulation of type I interferon production; TAS:Reactome.
DR   GO; GO:0051439; P:regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
DR   GO; GO:0044281; P:small molecule metabolic process; 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:0034166; P:toll-like receptor 10 signaling pathway; TAS:Reactome.
DR   GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome.
DR   GO; GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome.
DR   GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
DR   GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome.
DR   GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
DR   GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
DR   GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR   GO; GO:0006351; P:transcription, DNA-templated; TAS:Reactome.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR   GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0019058; P:viral life cycle; TAS:Reactome.
DR   GO; GO:0016032; P:viral process; TAS:Reactome.
DR   GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR   GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR   InterPro; IPR019956; Ubiquitin.
DR   InterPro; IPR000626; Ubiquitin-like.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   InterPro; IPR019954; Ubiquitin_CS.
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   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.
FT   DOMAIN       77    152       Ubiquitin-like 2.
FT   DOMAIN      153    228       Ubiquitin-like 3.
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   CROSSLNK      6      6       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK     11     11       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK     27     27       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin)
FT                                (Probable).
FT   CROSSLNK     29     29       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK     33     33       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK     48     48       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK     63     63       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
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   MUTAGEN      63     63       K->R: Abolishes HLTF-mediated
FT                                polyubiquitination of PCNA.
FT   MUTAGEN      65     65       S->A: Prevents phosphorylation in case of
FT                                mitophagy.
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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