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Polyubiquitin-B [Cleaved into: Ubiquitin]

 UBB_HUMAN               Reviewed;         229 AA.
P0CG47; P02248; P02249; P02250; P62988; Q29120; Q6LBL4; Q6LDU5;
Q8WYN8; Q91887; Q91888; Q9BWD6; Q9BX98; Q9UEF2; Q9UEG1; Q9UEK8;
10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 1.
07-NOV-2018, entry version 92.
RecName: Full=Polyubiquitin-B;
RecName: Full=Ubiquitin;
Flags: Precursor;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
PubMed=3029682; DOI=10.1093/nar/15.2.443;
Baker R.T., Board P.G.;
"The human ubiquitin gene family: structure of a gene and pseudogenes
from the Ub B subfamily.";
Nucleic Acids Res. 15:443-463(1987).
PubMed=14745543; DOI=10.1007/s00239-003-2532-4;
Tachikui H., Saitou N., Nakajima T., Hayasaka I., Ishida T., Inoue I.;
"Lineage-specific homogenization of the polyubiquitin gene among human
and great apes.";
J. Mol. Evol. 57:737-744(2003).
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
TISSUE=Brain, Liver, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
PubMed=1128706; DOI=10.1038/255423a0;
Schlesinger D.H., Goldstein G.;
"Molecular conservation of 74 amino acid sequence of ubiquitin between
cattle and man.";
Nature 255:423-424(1975).
PubMed=16443603; DOI=10.1074/jbc.M512786200;
Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.;
"Alzheimer disease-specific conformation of hyperphosphorylated paired
helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and
Lys-6 ubiquitin conjugation.";
J. Biol. Chem. 281:10825-10838(2006).
PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018;
Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
"Differential regulation of EGF receptor internalization and
degradation by multiubiquitination within the kinase domain.";
Mol. Cell 21:737-748(2006).
PubMed=15466860; DOI=10.1074/jbc.M402916200;
Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.;
"Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B
contributes to neuritogenesis.";
J. Biol. Chem. 279:53533-53543(2004).
PubMed=18719106; DOI=10.1073/pnas.0805685105;
Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X.,
Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
"Polyubiquitination of proliferating cell nuclear antigen by HLTF and
SHPRH prevents genomic instability from stalled replication forks.";
Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
PubMed=19754430; DOI=10.1042/BST0370937;
Komander D.;
"The emerging complexity of protein ubiquitination.";
Biochem. Soc. Trans. 37:937-953(2009).
PubMed=21762696; DOI=10.1016/j.febslet.2011.06.037;
Dennissen F.J., Kholod N., Hermes D.J., Kemmerling N.,
Steinbusch H.W., Dantuma N.P., van Leeuwen F.W.;
"Mutant ubiquitin (UBB(+1)) associated with neurodegenerative
disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-
FEBS Lett. 585:2568-2574(2011).
PubMed=9422699; DOI=10.1126/science.279.5348.242;
van Leeuwen F.W., de Kleijn D.P., van den Hurk H.H., Neubauer A.,
Sonnemans M.A., Sluijs J.A., Koycu S., Ramdjielal R.D., Salehi A.,
Martens G.J., Grosveld F.G., Peter J., Burbach H., Hol E.M.;
"Frameshift mutants of beta amyloid precursor protein and ubiquitin-B
in Alzheimer's and Down patients.";
Science 279:242-247(1998).
PubMed=14597671; DOI=10.1096/fj.03-0205com;
Fischer D.F., De Vos R.A., Van Dijk R., De Vrij F.M., Proper E.A.,
Sonnemans M.A., Verhage M.C., Sluijs J.A., Hobo B., Zouambia M.,
Steur E.N., Kamphorst W., Hol E.M., Van Leeuwen F.W.;
"Disease-specific accumulation of mutant ubiquitin as a marker for
proteasomal dysfunction in the brain.";
FASEB J. 17:2014-2024(2003).
PubMed=24660806; DOI=10.1042/BJ20140334;
Kazlauskaite A., Kondapalli C., Gourlay R., Campbell D.G.,
Ritorto M.S., Hofmann K., Alessi D.R., Knebel A., Trost M.,
Muqit M.M.;
"Parkin is activated by PINK1-dependent phosphorylation of ubiquitin
at Ser65.";
Biochem. J. 460:127-139(2014).
PubMed=24751536; DOI=10.1083/jcb.201402104;
Kane L.A., Lazarou M., Fogel A.I., Li Y., Yamano K., Sarraf S.A.,
Banerjee S., Youle R.J.;
"PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase
J. Cell Biol. 205:143-153(2014).
PubMed=24784582; DOI=10.1038/nature13392;
Koyano F., Okatsu K., Kosako H., Tamura Y., Go E., Kimura M.,
Kimura Y., Tsuchiya H., Yoshihara H., Hirokawa T., Endo T., Fon E.A.,
Trempe J.F., Saeki Y., Tanaka K., Matsuda N.;
"Ubiquitin is phosphorylated by PINK1 to activate parkin.";
Nature 510:162-166(2014).
PubMed=25527291; DOI=10.15252/embj.201489847;
Wauer T., Swatek K.N., Wagstaff J.L., Gladkova C., Pruneda J.N.,
Michel M.A., Gersch M., Johnson C.M., Freund S.M., Komander D.;
"Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain
assembly and hydrolysis.";
EMBO J. 34:307-325(2015).
PubMed=28525742; DOI=10.1016/j.molcel.2017.04.028;
Yang C.S., Jividen K., Spencer A., Dworak N., Ni L., Oostdyk L.T.,
Chatterjee M., Kusmider B., Reon B., Parlak M., Gorbunova V.,
Abbas T., Jeffery E., Sherman N.E., Paschal B.M.;
"Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase
Mol. Cell 66:503-516(2017).
-!- FUNCTION: Ubiquitin: Exists either covalently attached to another
protein, or free (unanchored). When covalently bound, it is
conjugated to target proteins via an isopeptide bond either as a
monomer (monoubiquitin), a polymer linked via different Lys
residues of the ubiquitin (polyubiquitin chains) or a linear
polymer linked via the initiator Met of the ubiquitin (linear
polyubiquitin chains). Polyubiquitin chains, when attached to a
target protein, have different functions depending on the Lys
residue of the ubiquitin that is linked: Lys-6-linked may be
involved in DNA repair; Lys-11-linked is involved in ERAD
(endoplasmic reticulum-associated degradation) and in cell-cycle
regulation; Lys-29-linked is involved in lysosomal degradation;
Lys-33-linked is involved in kinase modification; Lys-48-linked is
involved in protein degradation via the proteasome; Lys-63-linked
is involved in endocytosis, DNA-damage responses as well as in
signaling processes leading to activation of the transcription
factor NF-kappa-B. Linear polymer chains formed via attachment by
the initiator Met lead to cell signaling. Ubiquitin is usually
conjugated to Lys residues of target proteins, however, in rare
cases, conjugation to Cys or Ser residues has been observed. When
polyubiquitin is free (unanchored-polyubiquitin), it also has
distinct roles, such as in activation of protein kinases, and in
signaling. {ECO:0000269|PubMed:16543144,
Q8IVM0:CCDC50; NbExp=2; IntAct=EBI-413034, EBI-723996;
Q15038:DAZAP2; NbExp=6; IntAct=EBI-413034, EBI-724310;
P28562:DUSP1; NbExp=2; IntAct=EBI-413034, EBI-975493;
Q9UJY5:GGA1; NbExp=3; IntAct=EBI-413034, EBI-447141;
Q9NZ52:GGA3; NbExp=2; IntAct=EBI-413034, EBI-447404;
Q60592:Mast2 (xeno); NbExp=2; IntAct=EBI-413034, EBI-493888;
P33993:MCM7; NbExp=2; IntAct=EBI-413034, EBI-355924;
Q9DLK6:NP (xeno); NbExp=2; IntAct=EBI-413034, EBI-8433218;
P24610:Pax3 (xeno); NbExp=2; IntAct=EBI-413034, EBI-1208116;
Q9UJ41:RABGEF1; NbExp=6; IntAct=EBI-413034, EBI-913954;
P54727:RAD23B; NbExp=4; IntAct=EBI-413034, EBI-954531;
Q9Y3C5:RNF11; NbExp=2; IntAct=EBI-413034, EBI-396669;
Q68DV7:RNF43; NbExp=2; IntAct=EBI-413034, EBI-1647060;
Q9HAU4:SMURF2; NbExp=4; IntAct=EBI-413034, EBI-396727;
-!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus
-!- PTM: Ubiquitin: Phosphorylated at Ser-65 by PINK1 during
mitophagy. Phosphorylated ubiquitin specifically binds and
activates parkin (PRKN), triggering mitophagy (PubMed:24660806,
PubMed:24751536, PubMed:24784582, PubMed:25527291).
Phosphorylation does not affect E1-mediated E2 charging of
ubiquitin but affects discharging of E2 enzymes to form
polyubiquitin chains. It also affects deubiquitination by
deubiquitinase enzymes such as USP30 (PubMed:25527291).
{ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536,
ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291}.
-!- PTM: Ubiquitin: Mono-ADP-riblosylated at the C-terminus by PARP9,
a component of the PPAR9-DTX3L complex. ADP-ribosylation requires
processing by E1 and E2 enzymes and prevents ubiquitin conjugation
to substrates such as histones. {ECO:0000269|PubMed:28525742}.
-!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. UBA52
and RPS27A genes code for a single copy of ubiquitin fused to the
ribosomal proteins L40 and S27a, respectively. UBB and UBC genes
code for a polyubiquitin precursor with exact head to tail
repeats, the number of repeats differ between species and strains.
-!- MISCELLANEOUS: The mRNA encoding variant UBB(+1) is produced by an
unknown mechanism involving the deletion of a GT dinucleotide in
the close proximity of a GAGAG motif (PubMed:9422699). This
variant mRNA is found in normal brain, but the encoded protein
accumulates only in brain neurofibrillary tangles and neuritic
plaques in Alzheimer disease and other tauopathies, as well as
polyglutaminopathies (PubMed:14597671). UBB(+1) variant cannot be
used for polyubiquitination, is not effectively degraded by the
proteasome when ubiquitinated and ubiquitinated UBB(+1) is
refractory to disassembly by deubiquitinating enzymes (DUBs). In
healthy brain, UBB(+1) C-terminus can be cleaved by UCHL3
(PubMed:21762696). {ECO:0000305|PubMed:14597671,
ECO:0000305|PubMed:21762696, ECO:0000305|PubMed:9422699}.
-!- MISCELLANEOUS: For a better understanding, features related to
ubiquitin are only indicated for the first chain.
-!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; X04803; CAA28495.1; -; Genomic_DNA.
EMBL; AB089617; BAC56955.1; -; Genomic_DNA.
EMBL; AC093484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000379; AAH00379.1; -; mRNA.
EMBL; BC009301; AAH09301.1; -; mRNA.
EMBL; BC015127; AAH15127.1; -; mRNA.
EMBL; BC026301; AAH26301.1; -; mRNA.
EMBL; BC031027; AAH31027.1; -; mRNA.
EMBL; BC046123; AAH46123.1; -; mRNA.
CCDS; CCDS11177.1; -.
PIR; A26437; UQHUB.
RefSeq; NP_001268645.1; NM_001281716.1.
RefSeq; NP_001268646.1; NM_001281717.1.
RefSeq; NP_001268647.1; NM_001281718.1.
RefSeq; NP_001268648.1; NM_001281719.1.
RefSeq; NP_001268649.1; NM_001281720.1.
RefSeq; NP_061828.1; NM_018955.3.
UniGene; Hs.356190; -.
UniGene; Hs.730603; -.
UniGene; Hs.741549; -.
PDB; 2KHW; NMR; -; B=153-228.
PDB; 2MBB; NMR; -; B=153-228.
PDB; 2MRO; NMR; -; A=153-228.
PDB; 2MSG; NMR; -; A=153-224.
PDB; 2N13; NMR; -; B=153-228, C=153-229.
PDB; 4UEL; X-ray; 2.30 A; B=153-228.
PDB; 4UF6; X-ray; 3.69 A; B/E/H/K=153-227.
PDB; 4WHV; X-ray; 8.30 A; A/F/G/L=153-228.
PDB; 4WLR; X-ray; 2.00 A; C=153-228.
PDB; 4WUR; X-ray; 3.16 A; B=153-228.
PDB; 4XOF; X-ray; 1.15 A; A=153-228.
PDB; 4ZFR; X-ray; 1.72 A; B=153-228.
PDB; 4ZFT; X-ray; 2.30 A; B/D=153-228.
PDB; 4ZPZ; X-ray; 1.54 A; A/B=153-225.
PDB; 4ZUX; X-ray; 3.82 A; X/c/h/m=153-228.
PDB; 5BNB; X-ray; 2.49 A; E/F/G/I=153-229.
PDB; 5CAW; X-ray; 2.62 A; B/D=153-228.
PDB; 5CRA; X-ray; 2.64 A; C/D=153-227.
PDB; 5CVM; X-ray; 1.90 A; B=153-211.
PDB; 5CVN; X-ray; 3.36 A; D=153-228.
PDB; 5CVO; X-ray; 3.88 A; C/F=153-228.
PDB; 5D0K; X-ray; 2.65 A; B/E/H/K=153-228.
PDB; 5D0M; X-ray; 1.91 A; B=153-228.
PDB; 5DFL; X-ray; 2.10 A; B=153-228.
PDB; 5DK8; X-ray; 1.32 A; A/B=154-227.
PDB; 5E6J; X-ray; 2.85 A; C/F=153-227.
PDB; 5EDV; X-ray; 3.48 A; E/F/G/H=153-228.
PDB; 5EMZ; X-ray; 1.66 A; A/B/C/D/E/F=1-76.
PDB; 5EYA; X-ray; 2.40 A; C/D=153-228.
PDB; 5GJQ; EM; 4.50 A; y=153-228.
PDB; 5GO7; X-ray; 1.80 A; A=1-76.
PDB; 5GO8; X-ray; 2.21 A; A=1-76.
PDB; 5GOB; X-ray; 1.15 A; A=1-76.
PDB; 5GOC; X-ray; 1.73 A; A=1-76.
PDB; 5GOD; X-ray; 1.15 A; A/B=1-76.
PDB; 5GOG; X-ray; 1.98 A; A=1-76.
PDB; 5GOH; X-ray; 1.95 A; A=1-76.
PDB; 5GOI; X-ray; 1.59 A; A/B=1-76.
PDB; 5GOJ; X-ray; 1.55 A; A=1-76.
PDB; 5GOK; X-ray; 1.84 A; A=1-76.
PDB; 5H7S; X-ray; 3.49 A; E/F=1-76.
PDB; 5IBK; X-ray; 2.50 A; C/F=151-226.
PDB; 5IFR; X-ray; 2.20 A; B=153-227.
PDB; 5JBY; X-ray; 1.99 A; A/C/E=153-228.
PDB; 5JG6; X-ray; 2.00 A; B/C=76-153.
PDB; 5JP3; X-ray; 2.90 A; B/D/F/H=153-227.
PDB; 5JTJ; X-ray; 3.32 A; B=153-228.
PDB; 5JTV; X-ray; 3.31 A; B/D/F/H=1-76.
PDB; 5K9P; X-ray; 1.55 A; A=153-228.
PDB; 5KGF; EM; 4.54 A; M/O=153-228.
PDB; 5KHY; X-ray; 3.50 A; A=153-225, B=153-227.
PDB; 5KYC; X-ray; 1.43 A; C=153-228.
PDB; 5KYD; X-ray; 1.62 A; D=153-228.
PDB; 5KYE; X-ray; 1.97 A; C/D=153-228.
PDB; 5KYF; X-ray; 1.45 A; C=153-228.
PDB; 5L8H; X-ray; 1.85 A; B=1-76.
PDB; 5L8W; X-ray; 2.79 A; C=1-75.
PDB; 5L9T; EM; 6.40 A; S=1-73.
PDB; 5LN1; X-ray; 3.14 A; U=1-76.
PDB; 5LRV; X-ray; 2.80 A; B=1-76, C=1-75.
PDB; 5LRW; X-ray; 2.00 A; B/D=1-75.
PDB; 5LRX; X-ray; 2.85 A; B/D=1-76.
PDB; 5M93; X-ray; 1.79 A; A/B/C=1-76.
PDB; 5MNJ; X-ray; 2.16 A; B/F=1-76.
PDB; 5N2W; X-ray; 2.68 A; B=1-76.
PDB; 5N38; X-ray; 2.60 A; B=1-76.
PDB; 5NL5; X-ray; 1.96 A; A/B/C=1-76.
PDB; 5NLJ; X-ray; 1.53 A; A/B/C=1-76.
PDB; 5NVG; X-ray; 1.07 A; A=1-76.
PDB; 5O44; X-ray; 3.14 A; B/C=1-74, D/F=1-76.
PDB; 5O6T; X-ray; 1.57 A; C/D=1-76.
PDB; 5OHK; X-ray; 2.34 A; B=1-76.
PDB; 5OHL; X-ray; 2.50 A; I/J/K/L/M/N/O/P=1-76.
PDB; 5OHN; X-ray; 3.60 A; B/D=1-76.
PDB; 5OHP; X-ray; 2.80 A; B/C=1-76.
PDB; 5TOF; X-ray; 1.12 A; A=1-76.
PDB; 5TOG; X-ray; 1.08 A; A=1-76.
PDB; 5TUT; X-ray; 2.60 A; B=1-76.
PDB; 5UCL; X-ray; 2.35 A; A=1-78.
PDB; 5UJL; NMR; -; A/B=1-76.
PDB; 5UJN; NMR; -; A/B=1-76.
PDB; 5ULF; X-ray; 1.80 A; B/D=1-76.
PDB; 5ULH; X-ray; 1.95 A; B=1-76.
PDB; 5ULK; X-ray; 2.38 A; B=1-76.
PDB; 5V1Y; X-ray; 1.42 A; C/D=1-76.
PDB; 5V1Z; X-ray; 2.00 A; C/D=1-76.
PDB; 5VEY; NMR; -; B=1-76.
PDB; 5VF0; NMR; -; A=1-76.
PDB; 5VNZ; X-ray; 3.41 A; C/F=1-76.
PDB; 5VO0; X-ray; 3.90 A; C/F=1-76.
PDB; 5VZM; NMR; -; A=153-228.
PDB; 5VZW; X-ray; 2.28 A; C/D=153-228.
PDB; 5W46; X-ray; 1.18 A; A/B=153-228.
PDB; 5WFI; X-ray; 1.85 A; C/D=1-76.
PDB; 5X3M; X-ray; 1.82 A; A=1-76.
PDB; 5X3N; X-ray; 1.65 A; A=1-76.
PDB; 5X3O; X-ray; 2.19 A; A=1-76.
PDB; 5XBO; NMR; -; A=1-76.
PDB; 5XDP; X-ray; 2.38 A; A=1-76.
PDB; 5XK4; NMR; -; A=153-228.
PDB; 5XK5; NMR; -; A=153-228.
PDB; 5XPK; X-ray; 2.27 A; A=153-228.
PDB; 5YDR; X-ray; 2.00 A; A/D=153-225.
PDB; 5YIJ; X-ray; 3.18 A; C/D/G=153-228.
PDB; 5YIK; X-ray; 3.10 A; C/D/F=153-228.
PDB; 5YT6; X-ray; 1.50 A; A/C/E/G=1-76.
PDB; 6ASR; X-ray; 2.36 A; A/C=153-228.
PDB; 6BVA; X-ray; 2.66 A; A/B=76-152.
PDB; 6BYH; X-ray; 2.61 A; C/D/H=76-152.
PDB; 6C16; X-ray; 3.27 A; D/H=77-152.
PDB; 6CP2; X-ray; 2.90 A; C=75-152.
PDB; 6EI1; X-ray; 1.73 A; B=153-227.
PDB; 6FDK; X-ray; 1.60 A; B=1-76.
PDB; 6FGE; X-ray; 1.74 A; C=153-227.
PDB; 6FTX; EM; 4.50 A; N/O=1-76.
PDB; 6GLC; X-ray; 1.80 A; B=153-228.
PDBsum; 2KHW; -.
PDBsum; 2MBB; -.
PDBsum; 2MRO; -.
PDBsum; 2MSG; -.
PDBsum; 2N13; -.
PDBsum; 4UEL; -.
PDBsum; 4UF6; -.
PDBsum; 4WHV; -.
PDBsum; 4WLR; -.
PDBsum; 4WUR; -.
PDBsum; 4XOF; -.
PDBsum; 4ZFR; -.
PDBsum; 4ZFT; -.
PDBsum; 4ZPZ; -.
PDBsum; 4ZUX; -.
PDBsum; 5BNB; -.
PDBsum; 5CAW; -.
PDBsum; 5CRA; -.
PDBsum; 5CVM; -.
PDBsum; 5CVN; -.
PDBsum; 5CVO; -.
PDBsum; 5D0K; -.
PDBsum; 5D0M; -.
PDBsum; 5DFL; -.
PDBsum; 5DK8; -.
PDBsum; 5E6J; -.
PDBsum; 5EDV; -.
PDBsum; 5EMZ; -.
PDBsum; 5EYA; -.
PDBsum; 5GJQ; -.
PDBsum; 5GO7; -.
PDBsum; 5GO8; -.
PDBsum; 5GOB; -.
PDBsum; 5GOC; -.
PDBsum; 5GOD; -.
PDBsum; 5GOG; -.
PDBsum; 5GOH; -.
PDBsum; 5GOI; -.
PDBsum; 5GOJ; -.
PDBsum; 5GOK; -.
PDBsum; 5H7S; -.
PDBsum; 5IBK; -.
PDBsum; 5IFR; -.
PDBsum; 5JBY; -.
PDBsum; 5JG6; -.
PDBsum; 5JP3; -.
PDBsum; 5JTJ; -.
PDBsum; 5JTV; -.
PDBsum; 5K9P; -.
PDBsum; 5KGF; -.
PDBsum; 5KHY; -.
PDBsum; 5KYC; -.
PDBsum; 5KYD; -.
PDBsum; 5KYE; -.
PDBsum; 5KYF; -.
PDBsum; 5L8H; -.
PDBsum; 5L8W; -.
PDBsum; 5L9T; -.
PDBsum; 5LN1; -.
PDBsum; 5LRV; -.
PDBsum; 5LRW; -.
PDBsum; 5LRX; -.
PDBsum; 5M93; -.
PDBsum; 5MNJ; -.
PDBsum; 5N2W; -.
PDBsum; 5N38; -.
PDBsum; 5NL5; -.
PDBsum; 5NLJ; -.
PDBsum; 5NVG; -.
PDBsum; 5O44; -.
PDBsum; 5O6T; -.
PDBsum; 5OHK; -.
PDBsum; 5OHL; -.
PDBsum; 5OHN; -.
PDBsum; 5OHP; -.
PDBsum; 5TOF; -.
PDBsum; 5TOG; -.
PDBsum; 5TUT; -.
PDBsum; 5UCL; -.
PDBsum; 5UJL; -.
PDBsum; 5UJN; -.
PDBsum; 5ULF; -.
PDBsum; 5ULH; -.
PDBsum; 5ULK; -.
PDBsum; 5V1Y; -.
PDBsum; 5V1Z; -.
PDBsum; 5VEY; -.
PDBsum; 5VF0; -.
PDBsum; 5VNZ; -.
PDBsum; 5VO0; -.
PDBsum; 5VZM; -.
PDBsum; 5VZW; -.
PDBsum; 5W46; -.
PDBsum; 5WFI; -.
PDBsum; 5X3M; -.
PDBsum; 5X3N; -.
PDBsum; 5X3O; -.
PDBsum; 5XBO; -.
PDBsum; 5XDP; -.
PDBsum; 5XK4; -.
PDBsum; 5XK5; -.
PDBsum; 5XPK; -.
PDBsum; 5YDR; -.
PDBsum; 5YIJ; -.
PDBsum; 5YIK; -.
PDBsum; 5YT6; -.
PDBsum; 6ASR; -.
PDBsum; 6BVA; -.
PDBsum; 6BYH; -.
PDBsum; 6C16; -.
PDBsum; 6CP2; -.
PDBsum; 6EI1; -.
PDBsum; 6FDK; -.
PDBsum; 6FGE; -.
PDBsum; 6FTX; -.
PDBsum; 6GLC; -.
ProteinModelPortal; P0CG47; -.
SMR; P0CG47; -.
BioGrid; 113162; 190.
IntAct; P0CG47; 80.
MINT; P0CG47; -.
STRING; 9606.ENSP00000304697; -.
DrugBank; DB02542; (4s)-5-Fluoro-L-Leucine.
MoonDB; P0CG47; Predicted.
iPTMnet; P0CG47; -.
PhosphoSitePlus; P0CG47; -.
SwissPalm; P0CG47; -.
DMDM; 302595875; -.
EPD; P0CG47; -.
PaxDb; P0CG47; -.
PeptideAtlas; P0CG47; -.
PRIDE; P0CG47; -.
ProteomicsDB; 52474; -.
TopDownProteomics; P0CG47; -.
DNASU; 7314; -.
Ensembl; ENST00000302182; ENSP00000304697; ENSG00000170315.
Ensembl; ENST00000395837; ENSP00000379178; ENSG00000170315.
Ensembl; ENST00000395839; ENSP00000379180; ENSG00000170315.
Ensembl; ENST00000614404; ENSP00000478771; ENSG00000170315.
GeneID; 7314; -.
KEGG; hsa:7314; -.
CTD; 7314; -.
DisGeNET; 7314; -.
EuPathDB; HostDB:ENSG00000170315.13; -.
GeneCards; UBB; -.
HGNC; HGNC:12463; UBB.
HPA; CAB013048; -.
HPA; HPA041344; -.
HPA; HPA049132; -.
MalaCards; UBB; -.
MIM; 191339; gene.
neXtProt; NX_P0CG47; -.
OpenTargets; ENSG00000170315; -.
Orphanet; 99771; Bifid uvula.
Orphanet; 101023; Cleft hard palate.
Orphanet; 99772; Cleft velum.
Orphanet; 155878; Submucosal cleft palate.
eggNOG; KOG0001; Eukaryota.
eggNOG; COG5272; LUCA.
GeneTree; ENSGT00810000125435; -.
InParanoid; P0CG47; -.
KO; K04551; -.
OrthoDB; EOG091G178I; -.
PhylomeDB; P0CG47; -.
TreeFam; TF300820; -.
Reactome; R-HSA-110312; Translesion synthesis by REV1.
Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-HSA-110320; Translesion Synthesis by POLH.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1253288; Downregulation of ERBB4 signaling.
Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
Reactome; R-HSA-1358803; Downregulation of ERBB2:ERBB3 signaling.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
Reactome; R-HSA-175474; Assembly Of The HIV Virion.
Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-182971; EGFR downregulation.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-205043; NRIF signals cell death from the nucleus.
Reactome; R-HSA-209543; p75NTR recruits signalling complexes.
Reactome; R-HSA-209560; NF-kB is activated and signals survival.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
Reactome; R-HSA-2691232; Constitutive Signaling by NOTCH1 HD Domain Mutants.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
Reactome; R-HSA-3134975; Regulation of innate immune responses to cytosolic DNA.
Reactome; R-HSA-3322077; Glycogen synthesis.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-3785653; Myoclonic epilepsy of Lafora.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
Reactome; R-HSA-5205685; Pink/Parkin Mediated Mitophagy.
Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-HSA-5655862; Translesion synthesis by POLK.
Reactome; R-HSA-5656121; Translesion synthesis by POLI.
Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689877; Josephin domain DUBs.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
Reactome; R-HSA-5696400; Dual Incision in GG-NER.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-HSA-6807004; Negative regulation of MET activity.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69541; Stabilization of p53.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
Reactome; R-HSA-8876493; InlA-mediated entry of Listeria monocytogenes into host cells.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948747; Regulation of PTEN localization.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
Reactome; R-HSA-9013973; TICAM1-dependent activation of IRF3/IRF7.
Reactome; R-HSA-9014325; TICAM1,TRAF6-dependent induction of TAK1 complex.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-9033241; Peroxisomal protein import.
Reactome; R-HSA-912631; Regulation of signaling by CBL.
Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
Reactome; R-HSA-917937; Iron uptake and transport.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
Reactome; R-HSA-937039; IRAK1 recruits IKK complex.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-HSA-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
Reactome; R-HSA-977225; Amyloid fiber formation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; UBB; human.
GeneWiki; Ubiquitin_B; -.
GenomeRNAi; 7314; -.
PRO; PR:P0CG47; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000170315; Expressed in 236 organ(s), highest expression level in hypothalamus.
ExpressionAtlas; P0CG47; baseline and differential.
Genevisible; P0CG47; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0031386; F:protein tag; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
GO; GO:0016197; P:endosomal transport; TAS:Reactome.
GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
GO; GO:0070987; P:error-free translesion synthesis; TAS:Reactome.
GO; GO:0042276; P:error-prone translesion synthesis; TAS:Reactome.
GO; GO:0060613; P:fat pad development; IEA:Ensembl.
GO; GO:0008585; P:female gonad development; IEA:Ensembl.
GO; GO:0007144; P:female meiosis I; IEA:Ensembl.
GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0021888; P:hypothalamus gonadotrophin-releasing hormone neuron development; IEA:Ensembl.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0036297; P:interstrand cross-link repair; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0007254; P:JNK cascade; TAS:Reactome.
GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0047497; P:mitochondrion transport along microtubule; IDA:MGI.
GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:MGI.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; TAS:Reactome.
GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IDA:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
GO; GO:1902527; P:positive regulation of protein monoubiquitination; IMP:ParkinsonsUK-UCL.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006625; P:protein targeting to peroxisome; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA:MGI.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:1901214; P:regulation of neuron death; IDA:MGI.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:MGI.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0019985; P:translesion synthesis; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
GO; GO:0019068; P:virion assembly; TAS:Reactome.
GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
InterPro; IPR019956; Ubiquitin.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR019954; Ubiquitin_CS.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF00240; ubiquitin; 3.
SMART; SM00213; UBQ; 3.
SUPFAM; SSF54236; SSF54236; 3.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 76 Ubiquitin.
CHAIN 77 152 Ubiquitin.
CHAIN 153 228 Ubiquitin.
PROPEP 229 229
DOMAIN 1 76 Ubiquitin-like 1. {ECO:0000255|PROSITE-
DOMAIN 77 152 Ubiquitin-like 2. {ECO:0000255|PROSITE-
DOMAIN 153 228 Ubiquitin-like 3. {ECO:0000255|PROSITE-
BINDING 54 54 Activating enzyme.
BINDING 72 72 Activating enzyme.
SITE 68 68 Essential for function.
MOD_RES 65 65 Phosphoserine; by PINK1.
CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys)
(interchain with K-? in acceptor
DPDRQDHHPGSGAQ (in UBB(+1); loss of
polyubiquitination; impairs the
ubiquitin-proteasome pathway; refractory
to disassembly by DUBs; slow degradation
by UCHL3).
MUTAGEN 48 48 K->R: No effect on HLTF-mediated
polyubiquitination of PCNA.
MUTAGEN 63 63 K->R: Abolishes HLTF-mediated
polyubiquitination of PCNA.
MUTAGEN 65 65 S->A: Prevents phosphorylation in case of
mitophagy. {ECO:0000269|PubMed:24660806,
MUTAGEN 65 65 S->D: Phosphomimetic mutant that binds
and activates PRKN.
MUTAGEN 68 68 H->G: Loss of DTX3L-mediated
polyubiquitination of histone H3 and H4.
MUTAGEN 72 72 R->G: No effect on ADP-ribosylation.
MUTAGEN 72 72 R->K: No effect on ADP-ribosylation, when
associated with K-74.
MUTAGEN 74 74 R->G: No effect on ADP-ribosylation.
MUTAGEN 74 74 R->K: No effect on ADP-ribosylation, when
associated with K-72.
MUTAGEN 76 76 G->A: Loss of ADP-ribosylation.
STRAND 77 82 {ECO:0000244|PDB:5JG6}.
STRAND 88 93 {ECO:0000244|PDB:5JG6}.
HELIX 99 110 {ECO:0000244|PDB:5JG6}.
HELIX 114 116 {ECO:0000244|PDB:5JG6}.
STRAND 117 121 {ECO:0000244|PDB:5JG6}.
HELIX 133 135 {ECO:0000244|PDB:5JG6}.
STRAND 142 148 {ECO:0000244|PDB:5JG6}.
STRAND 154 159 {ECO:0000244|PDB:5NVG}.
STRAND 160 162 {ECO:0000244|PDB:4ZFR}.
STRAND 164 168 {ECO:0000244|PDB:5NVG}.
STRAND 171 174 {ECO:0000244|PDB:5XPK}.
HELIX 175 186 {ECO:0000244|PDB:5NVG}.
HELIX 190 192 {ECO:0000244|PDB:5NVG}.
STRAND 193 197 {ECO:0000244|PDB:5NVG}.
STRAND 200 202 {ECO:0000244|PDB:5YIJ}.
STRAND 206 208 {ECO:0000244|PDB:5GO7}.
HELIX 209 211 {ECO:0000244|PDB:5NVG}.
STRAND 218 223 {ECO:0000244|PDB:5NVG}.
STRAND 226 228 {ECO:0000244|PDB:6CP2}.
SEQUENCE 229 AA; 25762 MW; 33011162F1C48BB1 CRC64;

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