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 01-MAY-2013, entry version 31.
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 MASS 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=124018; DOI=10.1038/255423a0;
RA Schlesinger D.H., Goldstein G.;
RT "Hybrid troponin reconstituted from vertebrate and arthropod
RT subunits.";
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 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 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, AND MASS
RP SPECTROMETRY.
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).
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 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 -!- 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 IPI; IPI00719280; -.
DR PIR; A26437; UQHUB.
DR RefSeq; NP_061828.1; NM_018955.2.
DR UniGene; Hs.356190; -.
DR UniGene; Hs.740365; -.
DR ProteinModelPortal; P0CG47; -.
DR SMR; P0CG47; 1-227.
DR IntAct; P0CG47; 63.
DR PhosphoSite; P0CG47; -.
DR DMDM; 302595875; -.
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; uc001ugw.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; TIGCVNI; -.
DR OrthoDB; EOG4WDDB6; -.
DR PhylomeDB; P0CG47; -.
DR Reactome; REACT_107772; Immune System.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115202; Signal Transduction.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_2001; Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_216; DNA Repair.
DR Reactome; REACT_24941; Circadian Clock.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6782; TRAF6 Mediated Induction of proinflammatory cytokines.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR Reactome; REACT_8017; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; REACT_81380; Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
DR Reactome; REACT_97910; Signal Transduction.
DR ChiTaRS; UBB; human.
DR GenomeRNAi; 7314; -.
DR NextBio; 28592; -.
DR ArrayExpress; P0CG47; -.
DR Bgee; P0CG47; -.
DR GermOnline; ENSG00000170315; Homo sapiens.
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: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:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0016044; P:cellular membrane organization; 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:0046788; P:egress of virus within host cell; 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:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000080; P:G1 phase of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0007254; P:JNK cascade; TAS:Reactome.
DR GO; GO:0000216; P:M/G1 transition of 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: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:nerve growth factor 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:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; 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: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:0000084; P:S phase of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR GO; GO:0008063; P:Toll signaling pathway; TAS:Reactome.
DR GO; GO:0034130; P:toll-like receptor 1 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:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR InterPro; IPR000626; Ubiquitin.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_subgr.
DR InterPro; IPR019955; Ubiquitin_supergroup.
DR Pfam; PF00240; ubiquitin; 3.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 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; Reference proteome; Repeat; 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 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.
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
//
