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Polyubiquitin-C [Cleaved into: Ubiquitin]

 UBC_HUMAN               Reviewed;         685 AA.
P0CG48; P02248; P02249; P02250; P62988; Q29120; Q6LBL4; Q6LDU5;
Q8WYN8; Q91887; Q91888; Q9BWD6; Q9BX98; Q9UEF2; Q9UEG1; Q9UEK8;
Q9UPK7;
10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
13-JUN-2012, sequence version 3.
30-AUG-2017, entry version 81.
RecName: Full=Polyubiquitin-C;
Contains:
RecName: Full=Ubiquitin;
Flags: Precursor;
Name=UBC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2988935;
Wiborg O., Pedersen M.S., Wind A., Berglund L.E., Marcker K.A.,
Vuust J.;
"The human ubiquitin multigene family: some genes contain multiple
directly repeated ubiquitin coding sequences.";
EMBO J. 4:755-759(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9644242; DOI=10.1093/oxfordjournals.jbchem.a022093;
Kim N.S., Yamaguchi T., Sekine S., Saeki M., Iwamuro S., Kato S.;
"Cloning of human polyubiquitin cDNAs and a ubiquitin-binding assay
involving its in vitro translation product.";
J. Biochem. 124:35-39(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Liver, Lung, and Placenta;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-611.
PubMed=8917096; DOI=10.1016/0378-1119(96)00145-X;
Nenoi M., Mita K., Ichimura S., Cartwright I.L., Takahashi E.,
Yamauchi M., Tsuji H.;
"Heterogeneous structure of the polyubiquitin gene UbC of HeLa S3
cells.";
Gene 175:179-185(1996).
[7]
PROTEIN SEQUENCE OF 1-74.
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).
[8]
PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11
AND LYS-48, AND IDENTIFICATION BY MASS SPECTROMETRY.
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).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-685.
PubMed=9504932;
Nenoi M., Mita K., Ichimura S., Kawano A.;
"Higher frequency of concerted evolutionary events in rodents than in
man at the polyubiquitin gene VNTR locus.";
Genetics 148:867-876(1998).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 417-685.
PubMed=2820408; DOI=10.1016/0006-291X(87)90970-3;
Einspanier R., Sharma H.S., Scheit K.H.;
"Cloning and sequence analysis of a cDNA encoding poly-ubiquitin in
human ovarian granulosa cells.";
Biochem. Biophys. Res. Commun. 147:581-587(1987).
[12]
FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, AND
IDENTIFICATION BY MASS SPECTROMETRY.
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).
[13]
UBIQUITINATION AT LYS-27.
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).
[14]
UBIQUITINATION AT LYS-63, AND MUTAGENESIS OF LYS-48 AND LYS-63.
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).
[15]
REVIEW, AND FUNCTION.
PubMed=19754430; DOI=10.1042/BST0370937;
Komander D.;
"The emerging complexity of protein ubiquitination.";
Biochem. Soc. Trans. 37:937-953(2009).
[16]
PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
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).
[17]
PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
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
activity.";
J. Cell Biol. 205:143-153(2014).
[18]
PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
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).
[19]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=3041007; DOI=10.1016/0022-2836(87)90679-6;
Vijay-Kumar S., Bugg C.E., Cook W.J.;
"Structure of ubiquitin refined at 1.8-A resolution.";
J. Mol. Biol. 194:531-544(1987).
[20]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=8166633; DOI=10.1042/bj2990151;
Ramage R., Green J., Muir T.W., Ogunjobi O.M., Love S., Shaw K.;
"Synthetic, structural and biological studies of the ubiquitin system:
the total chemical synthesis of ubiquitin.";
Biochem. J. 299:151-158(1994).
[21]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=8107144; DOI=10.1006/jmbi.1994.1169;
Cook W.J., Jeffrey L.C., Kasperek E., Pickart C.M.;
"Structure of tetraubiquitin shows how multiubiquitin chains can be
formed.";
J. Mol. Biol. 236:601-609(1994).
[22]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=11173499; DOI=10.1107/S090744490001800X;
Phillips C.L., Thrower J., Pickart C.M., Hill C.P.;
"Structure of a new crystal form of tetraubiquitin.";
Acta Crystallogr. D 57:341-344(2001).
[23]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP7.
PubMed=12507430; DOI=10.1016/S0092-8674(02)01199-6;
Hu M., Li P., Li M., Li W., Yao T., Wu J.-W., Gu W., Cohen R.E.,
Shi Y.;
"Crystal structure of a UBP-family deubiquitinating enzyme in
isolation and in complex with ubiquitin aldehyde.";
Cell 111:1041-1054(2002).
[24]
X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP21.
PubMed=21399617; DOI=10.1038/embor.2011.17;
Ye Y., Akutsu M., Reyes-Turcu F., Enchev R.I., Wilkinson K.D.,
Komander D.;
"Polyubiquitin binding and cross-reactivity in the USP domain
deubiquitinase USP21.";
EMBO Rep. 12:350-357(2011).
[25]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-76.
PubMed=20622874; DOI=10.1038/nsmb.1873;
Bremm A., Freund S.M., Komander D.;
"Lys11-linked ubiquitin chains adopt compact conformations and are
preferentially hydrolyzed by the deubiquitinase Cezanne.";
Nat. Struct. Mol. Biol. 17:939-947(2010).
[26]
X-RAY CRYSTALLOGRAPHY (3.03 ANGSTROMS) OF 1-76 IN COMPLEX WITH YOD1.
PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F.,
Freund S.M., Ovaa H., Komander D.;
"OTU deubiquitinases reveal mechanisms of linkage specificity and
enable ubiquitin chain restriction analysis.";
Cell 154:169-184(2013).
[27]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 153-228 PHOSPHORYLATED AT
SER-65, AND PHOSPHORYLATION AT SER-65.
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).
-!- 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,
ECO:0000269|PubMed:19754430}.
-!- INTERACTION:
Q9UNQ0:ABCG2; NbExp=2; IntAct=EBI-3390054, EBI-1569435;
Q16186:ADRM1; NbExp=10; IntAct=EBI-3390054, EBI-954387;
Q9ULH1:ASAP1; NbExp=2; IntAct=EBI-3390054, EBI-346622;
O43150:ASAP2; NbExp=2; IntAct=EBI-3390054, EBI-310968;
P54252:ATXN3; NbExp=2; IntAct=EBI-3390054, EBI-946046;
Q9HB09-1:BCL2L12; NbExp=3; IntAct=EBI-3390054, EBI-6968951;
P35226:BMI1; NbExp=2; IntAct=EBI-3390054, EBI-2341576;
O60566:BUB1B; NbExp=3; IntAct=EBI-3390054, EBI-1001438;
P06493:CDK1; NbExp=6; IntAct=EBI-3390054, EBI-444308;
Q99062:CSF3R; NbExp=2; IntAct=EBI-3390054, EBI-7331284;
Q9UER7:DAXX; NbExp=2; IntAct=EBI-3390054, EBI-77321;
Q15038:DAZAP2; NbExp=4; IntAct=EBI-3390054, EBI-724310;
P40087:DDI1 (xeno); NbExp=2; IntAct=EBI-3390054, EBI-5717;
O43583:DENR; NbExp=3; IntAct=EBI-3390054, EBI-716083;
Q6ICB0:DESI1; NbExp=4; IntAct=EBI-3390054, EBI-2806959;
P48510:DSK2 (xeno); NbExp=2; IntAct=EBI-3390054, EBI-6174;
Q86Y01:DTX1; NbExp=2; IntAct=EBI-3390054, EBI-1755174;
Q15717:ELAVL1; NbExp=4; IntAct=EBI-3390054, EBI-374260;
Q92567-2:FAM168A; NbExp=4; IntAct=EBI-3390054, EBI-11978259;
Q61088:Fzd4 (xeno); NbExp=3; IntAct=EBI-3390054, EBI-7987880;
P25098:GRK2; NbExp=3; IntAct=EBI-3390054, EBI-3904795;
Q9Y6K9:IKBKG; NbExp=4; IntAct=EBI-3390054, EBI-81279;
O88522:Ikbkg (xeno); NbExp=3; IntAct=EBI-3390054, EBI-998011;
Q13887:KLF5; NbExp=2; IntAct=EBI-3390054, EBI-2696013;
P06239:LCK; NbExp=2; IntAct=EBI-3390054, EBI-1348;
P48357-3:LEPR; NbExp=2; IntAct=EBI-3390054, EBI-7886448;
Q9UDY8:MALT1; NbExp=4; IntAct=EBI-3390054, EBI-1047372;
Q9Y6R4:MAP3K4; NbExp=2; IntAct=EBI-3390054, EBI-448104;
O43318:MAP3K7; NbExp=4; IntAct=EBI-3390054, EBI-358684;
Q9NX47:MARCH5; NbExp=2; IntAct=EBI-3390054, EBI-2341610;
Q00987:MDM2; NbExp=6; IntAct=EBI-3390054, EBI-389668;
P01106:MYC; NbExp=5; IntAct=EBI-3390054, EBI-447544;
O43639:NCK2; NbExp=2; IntAct=EBI-3390054, EBI-713635;
Q14934:NFATC4; NbExp=3; IntAct=EBI-3390054, EBI-3905796;
P25963:NFKBIA; NbExp=3; IntAct=EBI-3390054, EBI-307386;
P09874:PARP1; NbExp=2; IntAct=EBI-3390054, EBI-355676;
P35227:PCGF2; NbExp=2; IntAct=EBI-3390054, EBI-2129767;
Q9Y253:POLH; NbExp=4; IntAct=EBI-3390054, EBI-2827270;
Q9UNA4:POLI; NbExp=4; IntAct=EBI-3390054, EBI-741774;
P17252:PRKCA; NbExp=2; IntAct=EBI-3390054, EBI-1383528;
P55036:PSMD4; NbExp=8; IntAct=EBI-3390054, EBI-359318;
P32628:RAD23 (xeno); NbExp=4; IntAct=EBI-3390054, EBI-14668;
P54727:RAD23B; NbExp=6; IntAct=EBI-3390054, EBI-954531;
Q84L31:RAD23C (xeno); NbExp=2; IntAct=EBI-3390054, EBI-4437395;
P61224:RAP1B; NbExp=2; IntAct=EBI-3390054, EBI-358143;
Q62921:Rbck1 (xeno); NbExp=2; IntAct=EBI-3390054, EBI-7266339;
Q96NR8:RDH12; NbExp=2; IntAct=EBI-3390054, EBI-3916363;
Q04206:RELA; NbExp=6; IntAct=EBI-3390054, EBI-73886;
P04325:rev (xeno); NbExp=2; IntAct=EBI-3390054, EBI-7061954;
P55034:RPN10 (xeno); NbExp=2; IntAct=EBI-3390054, EBI-2620423;
O48726:RPN13 (xeno); NbExp=9; IntAct=EBI-3390054, EBI-7710745;
Q8N488:RYBP; NbExp=3; IntAct=EBI-3390054, EBI-752324;
Q9H4L4:SENP3; NbExp=2; IntAct=EBI-3390054, EBI-2880236;
Q96B97:SH3KBP1; NbExp=6; IntAct=EBI-3390054, EBI-346595;
Q9Y5X1:SNX9; NbExp=2; IntAct=EBI-3390054, EBI-77848;
Q13501:SQSTM1; NbExp=3; IntAct=EBI-3390054, EBI-307104;
Q92783:STAM; NbExp=2; IntAct=EBI-3390054, EBI-752333;
Q86VP1:TAX1BP1; NbExp=7; IntAct=EBI-3390054, EBI-529518;
P04637:TP53; NbExp=15; IntAct=EBI-3390054, EBI-366083;
Q9Y4K3:TRAF6; NbExp=3; IntAct=EBI-3390054, EBI-359276;
Q9EPK8:Trpv4 (xeno); NbExp=3; IntAct=EBI-3390054, EBI-7091763;
Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-3390054, EBI-741480;
P98170:XIAP; NbExp=3; IntAct=EBI-3390054, EBI-517127;
O76080:ZFAND5; NbExp=3; IntAct=EBI-3390054, EBI-8028844;
Q9UGI0:ZRANB1; NbExp=2; IntAct=EBI-3390054, EBI-527853;
-!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- 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}.
-!- 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: For the sake of clarity sequence features are
annotated only for the first chain, and are not repeated for each
of the following chains.
-!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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EMBL; M26880; AAA36789.1; -; mRNA.
EMBL; AB009010; BAA23632.1; -; mRNA.
EMBL; AB089613; BAC56951.1; -; Genomic_DNA.
EMBL; AC126309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC039193; AAH39193.1; -; mRNA.
EMBL; D63791; BAA09860.1; -; Genomic_DNA.
EMBL; AB003730; BAA23486.1; -; Genomic_DNA.
EMBL; M17597; AAA36787.1; -; mRNA.
CCDS; CCDS9260.1; -.
PIR; A02574; UQHU.
PIR; A22005; UQHUC.
PIR; A29526; A29526.
RefSeq; NP_066289.3; NM_021009.6.
UniGene; Hs.520348; -.
UniGene; Hs.707528; -.
UniGene; Hs.731841; -.
PDB; 1C3T; NMR; -; A=1-76.
PDB; 1CMX; X-ray; 2.25 A; B/D=1-76.
PDB; 1D3Z; NMR; -; A=1-76.
PDB; 1F9J; X-ray; 2.70 A; A/B=1-76.
PDB; 1FXT; NMR; -; B=1-76.
PDB; 1G6J; NMR; -; A=1-76.
PDB; 1GJZ; NMR; -; A/B=1-51.
PDB; 1NBF; X-ray; 2.30 A; C/D=1-76.
PDB; 1OGW; X-ray; 1.32 A; A=1-76.
PDB; 1Q5W; NMR; -; B=1-76.
PDB; 1S1Q; X-ray; 2.00 A; B/D=1-76.
PDB; 1SIF; X-ray; 2.18 A; A=6-76.
PDB; 1TBE; X-ray; 2.40 A; A/B=1-76.
PDB; 1UBI; X-ray; 1.80 A; A=1-76.
PDB; 1UBQ; X-ray; 1.80 A; A=1-76.
PDB; 1UD7; NMR; -; A=1-76.
PDB; 1XD3; X-ray; 1.45 A; B/D=1-75.
PDB; 1XQQ; NMR; -; A=1-76.
PDB; 1YX5; NMR; -; B=1-76.
PDB; 1YX6; NMR; -; B=1-76.
PDB; 1ZGU; NMR; -; B=1-76.
PDB; 1ZO6; Model; -; B/C=1-76.
PDB; 2AYO; X-ray; 3.50 A; B=1-76.
PDB; 2BGF; NMR; -; A/B=1-76.
PDB; 2DEN; NMR; -; B=1-76.
PDB; 2FUH; NMR; -; B=1-76.
PDB; 2G45; X-ray; 1.99 A; B/E=1-76.
PDB; 2GBJ; X-ray; 1.35 A; A/B=1-76.
PDB; 2GBK; X-ray; 1.99 A; A/B/C/D=10-76.
PDB; 2GBM; X-ray; 1.55 A; A/B/C/D=1-76.
PDB; 2GBN; X-ray; 1.60 A; A=1-76.
PDB; 2GBR; X-ray; 2.00 A; A/B/C=1-76.
PDB; 2GMI; X-ray; 2.50 A; C=1-76.
PDB; 2HTH; X-ray; 2.70 A; A=1-76.
PDB; 2IBI; X-ray; 2.20 A; B=1-75.
PDB; 2J7Q; X-ray; 1.80 A; B/D=1-75.
PDB; 2JF5; X-ray; 1.95 A; A/B=1-76.
PDB; 2JRI; NMR; -; B/C=1-76.
PDB; 2JY6; NMR; -; A=1-76.
PDB; 2JZZ; NMR; -; A=1-76.
PDB; 2K25; NMR; -; A=1-75.
PDB; 2K6D; NMR; -; B=1-75.
PDB; 2K8B; NMR; -; A=1-76.
PDB; 2K8C; NMR; -; A=1-76.
PDB; 2KDF; NMR; -; B/C=1-76.
PDB; 2KHW; NMR; -; B=1-76.
PDB; 2KJH; NMR; -; B=1-75.
PDB; 2KLG; NMR; -; A=1-76.
PDB; 2KN5; NMR; -; A=1-76.
PDB; 2KX0; NMR; -; A=74-151.
PDB; 2L3Z; NMR; -; A=1-76.
PDB; 2LD9; NMR; -; A=76-152.
PDB; 2LVO; NMR; -; A=1-76.
PDB; 2LVP; NMR; -; A/B=1-76.
PDB; 2LVQ; NMR; -; A/B=1-76.
PDB; 2LZ6; NMR; -; A=609-684.
PDB; 2MBO; NMR; -; A/B=609-684.
PDB; 2MBQ; NMR; -; A/B=609-684.
PDB; 2MCN; NMR; -; B=609-684.
PDB; 2MI8; NMR; -; A=609-684.
PDB; 2MJ5; NMR; -; A=609-684.
PDB; 2MOR; NMR; -; A=609-684.
PDB; 2MRE; NMR; -; A=609-684.
PDB; 2MWS; NMR; -; A=609-684.
PDB; 2N2K; NMR; -; A=609-684, B=609-679.
PDB; 2NR2; NMR; -; A=1-76.
PDB; 2O6V; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-76.
PDB; 2OJR; X-ray; 2.60 A; A=1-76.
PDB; 2PE9; NMR; -; A/B=1-76.
PDB; 2PEA; NMR; -; A/B=1-76.
PDB; 2RR9; NMR; -; A/B=1-76.
PDB; 2RU6; NMR; -; A=609-684.
PDB; 2W9N; X-ray; 2.25 A; A=1-152.
PDB; 2WDT; X-ray; 2.30 A; B/D=1-75.
PDB; 2XEW; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-76.
PDB; 2Y5B; X-ray; 2.70 A; B/F=1-152.
PDB; 2Z59; NMR; -; B=1-76.
PDB; 2ZCB; X-ray; 1.60 A; A/B/C=1-76.
PDB; 2ZVN; X-ray; 3.00 A; A/C/E/G=1-152.
PDB; 2ZVO; X-ray; 2.90 A; A/G=1-152.
PDB; 3A33; X-ray; 2.20 A; B=1-76.
PDB; 3ALB; X-ray; 1.85 A; A/B/C/D=1-76.
PDB; 3AUL; X-ray; 2.39 A; A/B=1-76.
PDB; 3B08; X-ray; 1.70 A; A/D/G/J=1-152.
PDB; 3B0A; X-ray; 1.90 A; A/D=1-152.
PDB; 3BY4; X-ray; 1.55 A; B=1-75.
PDB; 3C0R; X-ray; 2.31 A; B/D=1-75.
PDB; 3DVG; X-ray; 2.60 A; X/Y=1-76.
PDB; 3DVN; X-ray; 2.70 A; U/V/X/Y=1-76.
PDB; 3EEC; X-ray; 3.00 A; A/B=1-76.
PDB; 3EFU; X-ray; 1.84 A; A=1-76.
PDB; 3EHV; X-ray; 1.81 A; A/B/C=1-76.
PDB; 3H7P; X-ray; 1.90 A; A/B=1-76.
PDB; 3H7S; X-ray; 2.30 A; A/B=1-76.
PDB; 3HM3; X-ray; 1.96 A; A/B/C/D=1-76.
PDB; 3I3T; X-ray; 2.59 A; B/D/F/H=1-75.
PDB; 3IFW; X-ray; 2.40 A; B=1-75.
PDB; 3IHP; X-ray; 2.80 A; C/D=1-75.
PDB; 3JSV; X-ray; 2.70 A; A/B=1-76.
PDB; 3JVZ; X-ray; 3.30 A; X/Y=1-76.
PDB; 3JW0; X-ray; 3.10 A; X/Y=1-76.
PDB; 3K9O; X-ray; 1.80 A; B=76-151.
PDB; 3K9P; X-ray; 2.80 A; B=1-76.
PDB; 3KVF; X-ray; 2.80 A; B=1-75.
PDB; 3KW5; X-ray; 2.83 A; B=1-75.
PDB; 3LDZ; X-ray; 2.60 A; E/F/G=1-73.
PDB; 3MHS; X-ray; 1.89 A; D=1-76.
PDB; 3MTN; X-ray; 2.70 A; B/D=1-76.
PDB; 3N30; X-ray; 3.00 A; A/B=1-76.
PDB; 3N32; X-ray; 1.80 A; A=1-76.
PDB; 3N3K; X-ray; 2.60 A; B=5-76.
PDB; 3NS8; X-ray; 1.71 A; A/B=1-76.
PDB; 3O65; X-ray; 2.70 A; B/D/F/H=1-75.
PDB; 3OFI; X-ray; 2.35 A; C/D=1-76.
PDB; 3OJ3; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-76.
PDB; 3OJ4; X-ray; 3.40 A; B/E=1-76.
PDB; 3ONS; X-ray; 1.80 A; A=1-72.
PDB; 3PRM; X-ray; 2.30 A; B/D=1-75.
PDB; 3PT2; X-ray; 2.50 A; B=1-75.
PDB; 3PTF; X-ray; 2.70 A; C/D=1-76.
PDB; 3Q3F; X-ray; 2.17 A; A=2-76.
PDB; 3RUL; X-ray; 2.50 A; A/B/C/D=1-75.
PDB; 3TMP; X-ray; 1.91 A; B/D/F/H=1-76.
PDB; 3U30; X-ray; 2.43 A; A/D=1-152.
PDB; 3UGB; X-ray; 2.35 A; B=1-76.
PDB; 3V6C; X-ray; 1.70 A; B=74-150.
PDB; 3V6E; X-ray; 2.10 A; B=74-150.
PDB; 3VFK; X-ray; 2.80 A; A=1-75.
PDB; 3VUW; X-ray; 1.95 A; A/B/C=1-76.
PDB; 3VUX; X-ray; 1.70 A; A/B/C=1-76.
PDB; 3VUY; X-ray; 1.98 A; A/B/C=1-76.
PDB; 3WXE; X-ray; 2.50 A; B=533-680.
PDB; 3WXF; X-ray; 2.30 A; B/D=533-680.
PDB; 3ZLZ; X-ray; 2.90 A; A/B=1-76.
PDB; 3ZNH; X-ray; 2.30 A; B=1-75.
PDB; 3ZNI; X-ray; 2.21 A; D/H/L/P=1-76.
PDB; 3ZNZ; X-ray; 1.90 A; B=1-152.
PDB; 4AP4; X-ray; 2.21 A; C/F=608-684.
PDB; 4AUQ; X-ray; 2.18 A; C/F=1-76.
PDB; 4BOS; X-ray; 2.35 A; C/E=609-684, F=612-625.
PDB; 4BOZ; X-ray; 3.03 A; B/C/E=1-76.
PDB; 4BVU; X-ray; 2.70 A; C=609-684.
PDB; 4DDG; X-ray; 3.30 A; D/E/F/G/H/I/M/N/O/P/Q/R=1-76.
PDB; 4DDI; X-ray; 3.80 A; G/H/I/J/K/L=1-76.
PDB; 4DHJ; X-ray; 2.35 A; B/F/J/M=1-76, D/H=1-75.
PDB; 4DHZ; X-ray; 3.11 A; B=1-76, E=1-75.
PDB; 4FJV; X-ray; 2.05 A; B/D=1-76.
PDB; 4HK2; X-ray; 1.40 A; A/B/C/D=1-76.
PDB; 4HXD; X-ray; 2.85 A; A/C=1-75.
PDB; 4I6L; X-ray; 2.49 A; B=77-150.
PDB; 4I6N; X-ray; 1.70 A; B/D=1-75.
PDB; 4IG7; X-ray; 2.00 A; B=1-75.
PDB; 4IUM; X-ray; 1.45 A; B=1-75.
PDB; 4JQW; X-ray; 2.90 A; C=609-684.
PDB; 4K1R; X-ray; 1.63 A; B/D=607-684.
PDB; 4K7S; X-ray; 1.76 A; A/B/C=1-76.
PDB; 4K7U; X-ray; 1.76 A; A/B/C=1-76.
PDB; 4K7W; X-ray; 1.76 A; A/B/C=1-76.
PDB; 4KSK; X-ray; 2.40 A; C/D=76-152.
PDB; 4KSL; X-ray; 2.83 A; C/D/F/H/J/L/N/P/R/T/V/X=76-228.
PDB; 4LCD; X-ray; 3.10 A; E/F=609-683.
PDB; 4LDT; X-ray; 1.90 A; B/D=609-684.
PDB; 4MDK; X-ray; 2.61 A; E/F/G/H=608-684.
PDB; 4MM3; X-ray; 2.75 A; A=609-684.
PDB; 4MSM; X-ray; 1.74 A; B/D=609-684.
PDB; 4MSQ; X-ray; 1.95 A; B/D=609-684.
PDB; 4NQK; X-ray; 3.70 A; E/F/G/H/I/J=608-684.
PDB; 4UN2; X-ray; 1.51 A; A=609-684.
PDB; 4V3K; X-ray; 2.04 A; B/E=609-684.
PDB; 4V3L; X-ray; 1.53 A; B/D=609-684.
PDB; 4WZP; X-ray; 1.90 A; A/B/C/D/E/F/G/H=153-228.
PDB; 4XOK; X-ray; 2.20 A; A/B/C=1-76.
PDB; 4XOL; X-ray; 2.91 A; A/B=1-76.
PDB; 4ZQS; X-ray; 1.80 A; A/B=533-684.
PDB; 5A5B; EM; 9.50 A; 9=609-684.
PDB; 5AF4; X-ray; 1.85 A; A/B/C/D/E/F/G/H=1-76.
PDB; 5AF5; X-ray; 1.68 A; A=1-73.
PDB; 5AF6; X-ray; 3.40 A; A/B/C/D/E=1-76.
PDB; 5AIT; X-ray; 3.40 A; C/F=609-684.
PDB; 5AIU; X-ray; 2.21 A; C/F=609-684.
PDB; 5B83; X-ray; 2.69 A; A/D=1-304.
PDB; 5C7J; X-ray; 3.00 A; C/D=1-74.
PDB; 5C7M; X-ray; 3.03 A; B/C=1-75.
PDB; 5E6J; X-ray; 2.85 A; B/E=609-683.
PDB; 5H07; X-ray; 2.59 A; A=1-228.
PDB; 5NL4; X-ray; 1.32 A; A/B/C=1-76.
PDB; 5NLF; X-ray; 1.50 A; A/B/C=1-76.
PDB; 5NLI; X-ray; 1.53 A; A/B/C=1-76.
PDB; 5NMC; X-ray; 1.70 A; A/B/C=1-76.
PDBsum; 1C3T; -.
PDBsum; 1CMX; -.
PDBsum; 1D3Z; -.
PDBsum; 1F9J; -.
PDBsum; 1FXT; -.
PDBsum; 1G6J; -.
PDBsum; 1GJZ; -.
PDBsum; 1NBF; -.
PDBsum; 1OGW; -.
PDBsum; 1Q5W; -.
PDBsum; 1S1Q; -.
PDBsum; 1SIF; -.
PDBsum; 1TBE; -.
PDBsum; 1UBI; -.
PDBsum; 1UBQ; -.
PDBsum; 1UD7; -.
PDBsum; 1XD3; -.
PDBsum; 1XQQ; -.
PDBsum; 1YX5; -.
PDBsum; 1YX6; -.
PDBsum; 1ZGU; -.
PDBsum; 1ZO6; -.
PDBsum; 2AYO; -.
PDBsum; 2BGF; -.
PDBsum; 2DEN; -.
PDBsum; 2FUH; -.
PDBsum; 2G45; -.
PDBsum; 2GBJ; -.
PDBsum; 2GBK; -.
PDBsum; 2GBM; -.
PDBsum; 2GBN; -.
PDBsum; 2GBR; -.
PDBsum; 2GMI; -.
PDBsum; 2HTH; -.
PDBsum; 2IBI; -.
PDBsum; 2J7Q; -.
PDBsum; 2JF5; -.
PDBsum; 2JRI; -.
PDBsum; 2JY6; -.
PDBsum; 2JZZ; -.
PDBsum; 2K25; -.
PDBsum; 2K6D; -.
PDBsum; 2K8B; -.
PDBsum; 2K8C; -.
PDBsum; 2KDF; -.
PDBsum; 2KHW; -.
PDBsum; 2KJH; -.
PDBsum; 2KLG; -.
PDBsum; 2KN5; -.
PDBsum; 2KX0; -.
PDBsum; 2L3Z; -.
PDBsum; 2LD9; -.
PDBsum; 2LVO; -.
PDBsum; 2LVP; -.
PDBsum; 2LVQ; -.
PDBsum; 2LZ6; -.
PDBsum; 2MBO; -.
PDBsum; 2MBQ; -.
PDBsum; 2MCN; -.
PDBsum; 2MI8; -.
PDBsum; 2MJ5; -.
PDBsum; 2MOR; -.
PDBsum; 2MRE; -.
PDBsum; 2MWS; -.
PDBsum; 2N2K; -.
PDBsum; 2NR2; -.
PDBsum; 2O6V; -.
PDBsum; 2OJR; -.
PDBsum; 2PE9; -.
PDBsum; 2PEA; -.
PDBsum; 2RR9; -.
PDBsum; 2RU6; -.
PDBsum; 2W9N; -.
PDBsum; 2WDT; -.
PDBsum; 2XEW; -.
PDBsum; 2Y5B; -.
PDBsum; 2Z59; -.
PDBsum; 2ZCB; -.
PDBsum; 2ZVN; -.
PDBsum; 2ZVO; -.
PDBsum; 3A33; -.
PDBsum; 3ALB; -.
PDBsum; 3AUL; -.
PDBsum; 3B08; -.
PDBsum; 3B0A; -.
PDBsum; 3BY4; -.
PDBsum; 3C0R; -.
PDBsum; 3DVG; -.
PDBsum; 3DVN; -.
PDBsum; 3EEC; -.
PDBsum; 3EFU; -.
PDBsum; 3EHV; -.
PDBsum; 3H7P; -.
PDBsum; 3H7S; -.
PDBsum; 3HM3; -.
PDBsum; 3I3T; -.
PDBsum; 3IFW; -.
PDBsum; 3IHP; -.
PDBsum; 3JSV; -.
PDBsum; 3JVZ; -.
PDBsum; 3JW0; -.
PDBsum; 3K9O; -.
PDBsum; 3K9P; -.
PDBsum; 3KVF; -.
PDBsum; 3KW5; -.
PDBsum; 3LDZ; -.
PDBsum; 3MHS; -.
PDBsum; 3MTN; -.
PDBsum; 3N30; -.
PDBsum; 3N32; -.
PDBsum; 3N3K; -.
PDBsum; 3NS8; -.
PDBsum; 3O65; -.
PDBsum; 3OFI; -.
PDBsum; 3OJ3; -.
PDBsum; 3OJ4; -.
PDBsum; 3ONS; -.
PDBsum; 3PRM; -.
PDBsum; 3PT2; -.
PDBsum; 3PTF; -.
PDBsum; 3Q3F; -.
PDBsum; 3RUL; -.
PDBsum; 3TMP; -.
PDBsum; 3U30; -.
PDBsum; 3UGB; -.
PDBsum; 3V6C; -.
PDBsum; 3V6E; -.
PDBsum; 3VFK; -.
PDBsum; 3VUW; -.
PDBsum; 3VUX; -.
PDBsum; 3VUY; -.
PDBsum; 3WXE; -.
PDBsum; 3WXF; -.
PDBsum; 3ZLZ; -.
PDBsum; 3ZNH; -.
PDBsum; 3ZNI; -.
PDBsum; 3ZNZ; -.
PDBsum; 4AP4; -.
PDBsum; 4AUQ; -.
PDBsum; 4BOS; -.
PDBsum; 4BOZ; -.
PDBsum; 4BVU; -.
PDBsum; 4DDG; -.
PDBsum; 4DDI; -.
PDBsum; 4DHJ; -.
PDBsum; 4DHZ; -.
PDBsum; 4FJV; -.
PDBsum; 4HK2; -.
PDBsum; 4HXD; -.
PDBsum; 4I6L; -.
PDBsum; 4I6N; -.
PDBsum; 4IG7; -.
PDBsum; 4IUM; -.
PDBsum; 4JQW; -.
PDBsum; 4K1R; -.
PDBsum; 4K7S; -.
PDBsum; 4K7U; -.
PDBsum; 4K7W; -.
PDBsum; 4KSK; -.
PDBsum; 4KSL; -.
PDBsum; 4LCD; -.
PDBsum; 4LDT; -.
PDBsum; 4MDK; -.
PDBsum; 4MM3; -.
PDBsum; 4MSM; -.
PDBsum; 4MSQ; -.
PDBsum; 4NQK; -.
PDBsum; 4UN2; -.
PDBsum; 4V3K; -.
PDBsum; 4V3L; -.
PDBsum; 4WZP; -.
PDBsum; 4XOK; -.
PDBsum; 4XOL; -.
PDBsum; 4ZQS; -.
PDBsum; 5A5B; -.
PDBsum; 5AF4; -.
PDBsum; 5AF5; -.
PDBsum; 5AF6; -.
PDBsum; 5AIT; -.
PDBsum; 5AIU; -.
PDBsum; 5B83; -.
PDBsum; 5C7J; -.
PDBsum; 5C7M; -.
PDBsum; 5E6J; -.
PDBsum; 5H07; -.
PDBsum; 5NL4; -.
PDBsum; 5NLF; -.
PDBsum; 5NLI; -.
PDBsum; 5NMC; -.
ProteinModelPortal; P0CG48; -.
SMR; P0CG48; -.
BioGrid; 113164; 1446.
IntAct; P0CG48; 184.
MINT; MINT-97475; -.
STRING; 9606.ENSP00000344818; -.
DrugBank; DB04464; N-Formylmethionine.
iPTMnet; P0CG48; -.
PhosphoSitePlus; P0CG48; -.
SwissPalm; P0CG48; -.
DMDM; 391358178; -.
EPD; P0CG48; -.
MaxQB; P0CG48; -.
PaxDb; P0CG48; -.
PeptideAtlas; P0CG48; -.
PRIDE; P0CG48; -.
TopDownProteomics; P0CG48; -.
Ensembl; ENST00000339647; ENSP00000344818; ENSG00000150991.
Ensembl; ENST00000536769; ENSP00000441543; ENSG00000150991.
GeneID; 7316; -.
KEGG; hsa:7316; -.
UCSC; uc001ugs.5; human.
CTD; 7316; -.
DisGeNET; 7316; -.
GeneCards; UBC; -.
HGNC; HGNC:12468; UBC.
HPA; CAB000362; -.
HPA; CAB005419; -.
HPA; HPA041344; -.
HPA; HPA049132; -.
MIM; 191340; gene.
neXtProt; NX_P0CG48; -.
OpenTargets; ENSG00000150991; -.
eggNOG; KOG0001; Eukaryota.
eggNOG; COG5272; LUCA.
GeneTree; ENSGT00810000125435; -.
InParanoid; P0CG48; -.
KO; K08770; -.
OMA; HINTATF; -.
OrthoDB; EOG091G178I; -.
TreeFam; TF354256; -.
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-168928; RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
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-446652; Interleukin-1 signaling.
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-69298; Association of licensing factors with the pre-replicative complex.
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-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
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 RIG-I/MDA5 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.
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.
SIGNOR; P0CG48; -.
ChiTaRS; UBC; human.
EvolutionaryTrace; P0CG48; -.
GeneWiki; Ubiquitin_C; -.
GenomeRNAi; 7316; -.
PRO; PR:P0CG48; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000150991; -.
ExpressionAtlas; P0CG48; baseline and differential.
Genevisible; P0CG48; HS.
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:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome.
GO; GO:0016197; P:endosomal transport; TAS:Reactome.
GO; GO:0035635; P:entry of bacterium into host cell; TAS:Reactome.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0070987; P:error-free translesion synthesis; TAS:Reactome.
GO; GO:0042276; P:error-prone translesion synthesis; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0005978; P:glycogen biosynthetic process; TAS:Reactome.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0045087; P:innate immune response; TAS:Reactome.
GO; GO:0036297; P:interstrand cross-link repair; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0007254; P:JNK cascade; TAS:Reactome.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
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:0000717; P:nucleotide-excision repair, DNA duplex unwinding; 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:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006457; P:protein folding; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0060544; P:regulation of necroptotic process; TAS:Reactome.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0032479; P:regulation of type I interferon production; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; 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:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0010992; P:ubiquitin homeostasis; IEA:Ensembl.
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.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
InterPro; IPR019956; Ubiquitin.
InterPro; IPR029071; Ubiquitin-rel_dom.
InterPro; IPR019954; Ubiquitin_CS.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF00240; ubiquitin; 9.
PRINTS; PR00348; UBIQUITIN.
SMART; SM00213; UBQ; 9.
SUPFAM; SSF54236; SSF54236; 9.
PROSITE; PS00299; UBIQUITIN_1; 9.
PROSITE; PS50053; UBIQUITIN_2; 9.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Ubl conjugation.
CHAIN 1 76 Ubiquitin.
/FTId=PRO_0000396178.
CHAIN 77 152 Ubiquitin.
/FTId=PRO_0000396179.
CHAIN 153 228 Ubiquitin.
/FTId=PRO_0000396180.
CHAIN 229 304 Ubiquitin.
/FTId=PRO_0000396181.
CHAIN 305 380 Ubiquitin.
/FTId=PRO_0000396182.
CHAIN 381 456 Ubiquitin.
/FTId=PRO_0000396183.
CHAIN 457 532 Ubiquitin.
/FTId=PRO_0000396184.
CHAIN 533 608 Ubiquitin.
/FTId=PRO_0000396185.
CHAIN 609 684 Ubiquitin.
/FTId=PRO_0000396186.
PROPEP 685 685
/FTId=PRO_0000396187.
DOMAIN 1 76 Ubiquitin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 77 152 Ubiquitin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 153 228 Ubiquitin-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 229 304 Ubiquitin-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 305 380 Ubiquitin-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 381 456 Ubiquitin-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 457 532 Ubiquitin-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 533 608 Ubiquitin-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 609 684 Ubiquitin-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
BINDING 54 54 Activating enzyme.
BINDING 72 72 Activating enzyme.
SITE 68 68 Essential for function.
MOD_RES 65 65 Phosphoserine; by PINK1.
{ECO:0000269|PubMed:24660806,
ECO:0000269|PubMed:24751536,
ECO:0000269|PubMed:24784582,
ECO:0000269|PubMed:25527291}.
CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16443603}.
CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16443603,
ECO:0000269|PubMed:16543144}.
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:15466860}.
CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16543144}.
CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16443603,
ECO:0000269|PubMed:16543144}.
CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16543144,
ECO:0000269|PubMed:18719106}.
CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys)
(interchain with K-? in acceptor
proteins).
MUTAGEN 48 48 K->R: No effect on HLTF-mediated
polyubiquitination of PCNA.
{ECO:0000269|PubMed:18719106}.
MUTAGEN 63 63 K->R: Abolishes HLTF-mediated
polyubiquitination of PCNA.
{ECO:0000269|PubMed:18719106}.
MUTAGEN 65 65 S->A: Prevents phosphorylation in case of
mitophagy. {ECO:0000269|PubMed:24660806,
ECO:0000269|PubMed:24751536,
ECO:0000269|PubMed:24784582}.
MUTAGEN 65 65 S->D: Phosphomimetic mutant that binds
and activates PRKN.
{ECO:0000269|PubMed:24751536}.
CONFLICT 190 190 P -> S (in Ref. 4; AC126309).
{ECO:0000305}.
CONFLICT 397 397 V -> G (in Ref. 6; BAA09860).
{ECO:0000305}.
STRAND 383 386 {ECO:0000244|PDB:5B83}.
STRAND 392 395 {ECO:0000244|PDB:5B83}.
HELIX 403 411 {ECO:0000244|PDB:5B83}.
HELIX 418 420 {ECO:0000244|PDB:5B83}.
STRAND 421 425 {ECO:0000244|PDB:5B83}.
STRAND 428 430 {ECO:0000244|PDB:5B83}.
HELIX 436 438 {ECO:0000244|PDB:5B83}.
STRAND 446 451 {ECO:0000244|PDB:5B83}.
STRAND 456 462 {ECO:0000244|PDB:5B83}.
STRAND 468 473 {ECO:0000244|PDB:5B83}.
HELIX 479 490 {ECO:0000244|PDB:5B83}.
HELIX 494 496 {ECO:0000244|PDB:5B83}.
STRAND 497 501 {ECO:0000244|PDB:5B83}.
TURN 512 516 {ECO:0000244|PDB:5B83}.
STRAND 522 527 {ECO:0000244|PDB:5B83}.
STRAND 534 539 {ECO:0000244|PDB:2GBJ}.
STRAND 540 542 {ECO:0000244|PDB:2W9N}.
STRAND 544 548 {ECO:0000244|PDB:2GBM}.
HELIX 555 565 {ECO:0000244|PDB:2GBM}.
STRAND 568 570 {ECO:0000244|PDB:2GBM}.
STRAND 573 577 {ECO:0000244|PDB:3B08}.
STRAND 579 581 {ECO:0000244|PDB:3N3K}.
STRAND 586 588 {ECO:0000244|PDB:1SIF}.
HELIX 589 591 {ECO:0000244|PDB:3B08}.
STRAND 598 603 {ECO:0000244|PDB:3B08}.
STRAND 610 615 {ECO:0000244|PDB:1OGW}.
STRAND 616 618 {ECO:0000244|PDB:4K1R}.
STRAND 620 624 {ECO:0000244|PDB:1OGW}.
STRAND 627 630 {ECO:0000244|PDB:1G6J}.
HELIX 631 642 {ECO:0000244|PDB:1OGW}.
HELIX 646 648 {ECO:0000244|PDB:1OGW}.
STRAND 649 653 {ECO:0000244|PDB:1OGW}.
STRAND 654 657 {ECO:0000244|PDB:4BVU}.
STRAND 660 663 {ECO:0000244|PDB:3JSV}.
HELIX 664 667 {ECO:0000244|PDB:1OGW}.
STRAND 674 679 {ECO:0000244|PDB:1OGW}.
SEQUENCE 685 AA; 77039 MW; B6E7BC06FEE77196 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE PSDTIENVKA
KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL
SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ
QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL
TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH
LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED
GRTLSDYNIQ KESTLHLVLR LRGGV


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