UBC_HUMAN
ID UBC_HUMAN Reviewed; 685 AA.
AC P0CG48; P02248; P02249; P02250; P62988; Q29120; Q6LBL4; Q6LDU5; Q8WYN8;
AC Q91887; Q91888; Q9BWD6; Q9BX98; Q9UEF2; Q9UEG1; Q9UEK8; Q9UPK7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Polyubiquitin-C;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Flags: Precursor;
GN Name=UBC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2988935; DOI=10.1002/j.1460-2075.1985.tb03693.x;
RA Wiborg O., Pedersen M.S., Wind A., Berglund L.E., Marcker K.A., Vuust J.;
RT "The human ubiquitin multigene family: some genes contain multiple directly
RT repeated ubiquitin coding sequences.";
RL EMBO J. 4:755-759(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9644242; DOI=10.1093/oxfordjournals.jbchem.a022093;
RA Kim N.S., Yamaguchi T., Sekine S., Saeki M., Iwamuro S., Kato S.;
RT "Cloning of human polyubiquitin cDNAs and a ubiquitin-binding assay
RT involving its in vitro translation product.";
RL J. Biochem. 124:35-39(1998).
RN [3]
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 and
RT great apes.";
RL J. Mol. Evol. 57:737-744(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Liver, Lung, and Placenta;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-611.
RX PubMed=8917096; DOI=10.1016/0378-1119(96)00145-x;
RA Nenoi M., Mita K., Ichimura S., Cartwright I.L., Takahashi E., Yamauchi M.,
RA Tsuji H.;
RT "Heterogeneous structure of the polyubiquitin gene UbC of HeLa S3 cells.";
RL Gene 175:179-185(1996).
RN [7]
RP PROTEIN SEQUENCE OF 1-74.
RX PubMed=1128706; DOI=10.1038/255423a0;
RA Schlesinger D.H., Goldstein G.;
RT "Molecular conservation of 74 amino acid sequence of ubiquitin between
RT cattle and man.";
RL Nature 255:423-424(1975).
RN [8]
RP PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11 AND
RP LYS-48, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16443603; DOI=10.1074/jbc.m512786200;
RA Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.;
RT "Alzheimer disease-specific conformation of hyperphosphorylated paired
RT helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6
RT ubiquitin conjugation.";
RL J. Biol. Chem. 281:10825-10838(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-685.
RX PubMed=9504932; DOI=10.1093/genetics/148.2.867;
RA Nenoi M., Mita K., Ichimura S., Kawano A.;
RT "Higher frequency of concerted evolutionary events in rodents than in man
RT at the polyubiquitin gene VNTR locus.";
RL Genetics 148:867-876(1998).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 417-685.
RX PubMed=2820408; DOI=10.1016/0006-291x(87)90970-3;
RA Einspanier R., Sharma H.S., Scheit K.H.;
RT "Cloning and sequence analysis of a cDNA encoding poly-ubiquitin in human
RT ovarian granulosa cells.";
RL Biochem. Biophys. Res. Commun. 147:581-587(1987).
RN [12]
RP FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018;
RA Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
RT "Differential regulation of EGF receptor internalization and degradation by
RT multiubiquitination within the kinase domain.";
RL Mol. Cell 21:737-748(2006).
RN [13]
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 [14]
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., Moinova H.,
RA Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
RT "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH
RT prevents genomic instability from stalled replication forks.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
RN [15]
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 [16]
RP PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
RX PubMed=24660806; DOI=10.1042/bj20140334;
RA Kazlauskaite A., Kondapalli C., Gourlay R., Campbell D.G., Ritorto M.S.,
RA Hofmann K., Alessi D.R., Knebel A., Trost M., Muqit M.M.;
RT "Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at
RT Ser65.";
RL Biochem. J. 460:127-139(2014).
RN [17]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
RX PubMed=24751536; DOI=10.1083/jcb.201402104;
RA Kane L.A., Lazarou M., Fogel A.I., Li Y., Yamano K., Sarraf S.A.,
RA Banerjee S., Youle R.J.;
RT "PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase
RT activity.";
RL J. Cell Biol. 205:143-153(2014).
RN [18]
RP PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
RX PubMed=24784582; DOI=10.1038/nature13392;
RA Koyano F., Okatsu K., Kosako H., Tamura Y., Go E., Kimura M., Kimura Y.,
RA Tsuchiya H., Yoshihara H., Hirokawa T., Endo T., Fon E.A., Trempe J.F.,
RA Saeki Y., Tanaka K., Matsuda N.;
RT "Ubiquitin is phosphorylated by PINK1 to activate parkin.";
RL Nature 510:162-166(2014).
RN [19]
RP ADP-RIBOSYLATION AT GLY-76, AND MUTAGENESIS OF HIS-68; ARG-72; ARG-74 AND
RP GLY-76.
RX PubMed=28525742; DOI=10.1016/j.molcel.2017.04.028;
RA Yang C.S., Jividen K., Spencer A., Dworak N., Ni L., Oostdyk L.T.,
RA Chatterjee M., Kusmider B., Reon B., Parlak M., Gorbunova V., Abbas T.,
RA Jeffery E., Sherman N.E., Paschal B.M.;
RT "Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase
RT Dtx3L/Parp9.";
RL Mol. Cell 66:503-516(2017).
RN [20]
RP FUNCTION (UBIQUITIN), AND UBIQUITINATION AT LYS-29.
RX PubMed=34239127; DOI=10.1038/s41589-021-00823-5;
RA Yu Y., Zheng Q., Erramilli S.K., Pan M., Park S., Xie Y., Li J., Fei J.,
RA Kossiakoff A.A., Liu L., Zhao M.;
RT "K29-linked ubiquitin signaling regulates proteotoxic stress response and
RT cell cycle.";
RL Nat. Chem. Biol. 17:896-905(2021).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=3041007; DOI=10.1016/0022-2836(87)90679-6;
RA Vijay-Kumar S., Bugg C.E., Cook W.J.;
RT "Structure of ubiquitin refined at 1.8-A resolution.";
RL J. Mol. Biol. 194:531-544(1987).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8166633; DOI=10.1042/bj2990151;
RA Ramage R., Green J., Muir T.W., Ogunjobi O.M., Love S., Shaw K.;
RT "Synthetic, structural and biological studies of the ubiquitin system: the
RT total chemical synthesis of ubiquitin.";
RL Biochem. J. 299:151-158(1994).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8107144; DOI=10.1006/jmbi.1994.1169;
RA Cook W.J., Jeffrey L.C., Kasperek E., Pickart C.M.;
RT "Structure of tetraubiquitin shows how multiubiquitin chains can be
RT formed.";
RL J. Mol. Biol. 236:601-609(1994).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=11173499; DOI=10.1107/s090744490001800x;
RA Phillips C.L., Thrower J., Pickart C.M., Hill C.P.;
RT "Structure of a new crystal form of tetraubiquitin.";
RL Acta Crystallogr. D 57:341-344(2001).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP7.
RX PubMed=12507430; DOI=10.1016/s0092-8674(02)01199-6;
RA Hu M., Li P., Li M., Li W., Yao T., Wu J.-W., Gu W., Cohen R.E., Shi Y.;
RT "Crystal structure of a UBP-family deubiquitinating enzyme in isolation and
RT in complex with ubiquitin aldehyde.";
RL Cell 111:1041-1054(2002).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP21.
RX PubMed=21399617; DOI=10.1038/embor.2011.17;
RA Ye Y., Akutsu M., Reyes-Turcu F., Enchev R.I., Wilkinson K.D., Komander D.;
RT "Polyubiquitin binding and cross-reactivity in the USP domain
RT deubiquitinase USP21.";
RL EMBO Rep. 12:350-357(2011).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-76.
RX PubMed=20622874; DOI=10.1038/nsmb.1873;
RA Bremm A., Freund S.M., Komander D.;
RT "Lys11-linked ubiquitin chains adopt compact conformations and are
RT preferentially hydrolyzed by the deubiquitinase Cezanne.";
RL Nat. Struct. Mol. Biol. 17:939-947(2010).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (3.03 ANGSTROMS) OF 1-76 IN COMPLEX WITH YOD1.
RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M.,
RA Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and enable
RT ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 153-228 PHOSPHORYLATED AT SER-65,
RP AND PHOSPHORYLATION AT SER-65.
RX PubMed=25527291; DOI=10.15252/embj.201489847;
RA Wauer T., Swatek K.N., Wagstaff J.L., Gladkova C., Pruneda J.N.,
RA Michel M.A., Gersch M., Johnson C.M., Freund S.M., Komander D.;
RT "Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain
RT assembly and hydrolysis.";
RL EMBO J. 34:307-325(2015).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (3.03 ANGSTROMS) OF 1-76 IN COMPLEX WITH ZRANB1, AND
RP UBIQUITINATION AT LYS-29.
RX PubMed=25752573; DOI=10.1016/j.molcel.2015.01.041;
RA Kristariyanto Y.A., Abdul Rehman S.A., Campbell D.G., Morrice N.A.,
RA Johnson C., Toth R., Kulathu Y.;
RT "K29-selective ubiquitin binding domain reveals structural basis of
RT specificity and heterotypic nature of K29 polyubiquitin.";
RL Mol. Cell 58:83-94(2015).
RN [31] {ECO:0007744|PDB:5AF4, ECO:0007744|PDB:5AF5, ECO:0007744|PDB:5AF6}
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1-76 IN COMPLEX WITH ZRANB1, AND
RP UBIQUITINATION AT LYS-29 AND LYS-33.
RX PubMed=25752577; DOI=10.1016/j.molcel.2015.01.042;
RA Michel M.A., Elliott P.R., Swatek K.N., Simicek M., Pruneda J.N.,
RA Wagstaff J.L., Freund S.M., Komander D.;
RT "Assembly and specific recognition of K29- and K33-linked polyubiquitin.";
RL Mol. Cell 58:95-109(2015).
CC -!- FUNCTION: [Ubiquitin]: Exists either covalently attached to another
CC protein, or free (unanchored). When covalently bound, it is conjugated
CC to target proteins via an isopeptide bond either as a monomer
CC (monoubiquitin), a polymer linked via different Lys residues of the
CC ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC initiator Met of the ubiquitin (linear polyubiquitin chains).
CC Polyubiquitin chains, when attached to a target protein, have different
CC functions depending on the Lys residue of the ubiquitin that is linked:
CC Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved
CC in ERAD (endoplasmic reticulum-associated degradation) and in cell-
CC cycle regulation; Lys-29-linked is involved in proteotoxic stress
CC response and cell cycle; Lys-33-linked is involved in kinase
CC modification; Lys-48-linked is involved in protein degradation via the
CC proteasome; Lys-63-linked is involved in endocytosis, DNA-damage
CC responses as well as in signaling processes leading to activation of
CC the transcription factor NF-kappa-B. Linear polymer chains formed via
CC attachment by the initiator Met lead to cell signaling. Ubiquitin is
CC usually 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 distinct
CC roles, such as in activation of protein kinases, and in signaling.
CC {ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:34239127,
CC ECO:0000303|PubMed:19754430}.
CC -!- INTERACTION:
CC P0CG48; Q9UNQ0: ABCG2; NbExp=2; IntAct=EBI-3390054, EBI-1569435;
CC P0CG48; Q16186: ADRM1; NbExp=11; IntAct=EBI-3390054, EBI-954387;
CC P0CG48; Q9ULH1: ASAP1; NbExp=2; IntAct=EBI-3390054, EBI-346622;
CC P0CG48; O43150: ASAP2; NbExp=2; IntAct=EBI-3390054, EBI-310968;
CC P0CG48; P54252-1: ATXN3; NbExp=2; IntAct=EBI-3390054, EBI-946068;
CC P0CG48; Q9HB09-1: BCL2L12; NbExp=3; IntAct=EBI-3390054, EBI-6968951;
CC P0CG48; P35226: BMI1; NbExp=2; IntAct=EBI-3390054, EBI-2341576;
CC P0CG48; O60566: BUB1B; NbExp=3; IntAct=EBI-3390054, EBI-1001438;
CC P0CG48; Q9H305: CDIP1; NbExp=3; IntAct=EBI-3390054, EBI-2876678;
CC P0CG48; P06493: CDK1; NbExp=6; IntAct=EBI-3390054, EBI-444308;
CC P0CG48; Q99062: CSF3R; NbExp=2; IntAct=EBI-3390054, EBI-7331284;
CC P0CG48; Q9UER7: DAXX; NbExp=2; IntAct=EBI-3390054, EBI-77321;
CC P0CG48; Q15038: DAZAP2; NbExp=6; IntAct=EBI-3390054, EBI-724310;
CC P0CG48; O43583: DENR; NbExp=3; IntAct=EBI-3390054, EBI-716083;
CC P0CG48; Q6ICB0: DESI1; NbExp=3; IntAct=EBI-3390054, EBI-2806959;
CC P0CG48; Q86Y01: DTX1; NbExp=2; IntAct=EBI-3390054, EBI-1755174;
CC P0CG48; Q15717: ELAVL1; NbExp=4; IntAct=EBI-3390054, EBI-374260;
CC P0CG48; O95208-2: EPN2; NbExp=3; IntAct=EBI-3390054, EBI-12135243;
CC P0CG48; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-3390054, EBI-11978259;
CC P0CG48; P25098: GRK2; NbExp=3; IntAct=EBI-3390054, EBI-3904795;
CC P0CG48; P42858: HTT; NbExp=3; IntAct=EBI-3390054, EBI-466029;
CC P0CG48; Q9Y6K9: IKBKG; NbExp=4; IntAct=EBI-3390054, EBI-81279;
CC P0CG48; Q13887: KLF5; NbExp=2; IntAct=EBI-3390054, EBI-2696013;
CC P0CG48; P06239: LCK; NbExp=2; IntAct=EBI-3390054, EBI-1348;
CC P0CG48; P48357-3: LEPR; NbExp=2; IntAct=EBI-3390054, EBI-7886448;
CC P0CG48; Q9UDY8: MALT1; NbExp=4; IntAct=EBI-3390054, EBI-1047372;
CC P0CG48; Q9Y6R4: MAP3K4; NbExp=2; IntAct=EBI-3390054, EBI-448104;
CC P0CG48; O43318: MAP3K7; NbExp=4; IntAct=EBI-3390054, EBI-358684;
CC P0CG48; Q9NX47: MARCHF5; NbExp=2; IntAct=EBI-3390054, EBI-2341610;
CC P0CG48; Q00987: MDM2; NbExp=6; IntAct=EBI-3390054, EBI-389668;
CC P0CG48; Q8N3F0: MTURN; NbExp=3; IntAct=EBI-3390054, EBI-11980301;
CC P0CG48; P01106: MYC; NbExp=5; IntAct=EBI-3390054, EBI-447544;
CC P0CG48; Q14596: NBR1; NbExp=3; IntAct=EBI-3390054, EBI-742698;
CC P0CG48; O43639: NCK2; NbExp=2; IntAct=EBI-3390054, EBI-713635;
CC P0CG48; Q14934: NFATC4; NbExp=3; IntAct=EBI-3390054, EBI-3905796;
CC P0CG48; P25963: NFKBIA; NbExp=3; IntAct=EBI-3390054, EBI-307386;
CC P0CG48; P09874: PARP1; NbExp=2; IntAct=EBI-3390054, EBI-355676;
CC P0CG48; P35227: PCGF2; NbExp=2; IntAct=EBI-3390054, EBI-2129767;
CC P0CG48; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-3390054, EBI-373552;
CC P0CG48; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-3390054, EBI-769257;
CC P0CG48; Q9Y253: POLH; NbExp=4; IntAct=EBI-3390054, EBI-2827270;
CC P0CG48; Q9UNA4: POLI; NbExp=4; IntAct=EBI-3390054, EBI-741774;
CC P0CG48; P17252: PRKCA; NbExp=2; IntAct=EBI-3390054, EBI-1383528;
CC P0CG48; P55036: PSMD4; NbExp=4; IntAct=EBI-3390054, EBI-359318;
CC P0CG48; P54727: RAD23B; NbExp=5; IntAct=EBI-3390054, EBI-954531;
CC P0CG48; Q96NR8: RDH12; NbExp=2; IntAct=EBI-3390054, EBI-3916363;
CC P0CG48; Q04206: RELA; NbExp=6; IntAct=EBI-3390054, EBI-73886;
CC P0CG48; Q8N488: RYBP; NbExp=3; IntAct=EBI-3390054, EBI-752324;
CC P0CG48; Q9H4L4: SENP3; NbExp=2; IntAct=EBI-3390054, EBI-2880236;
CC P0CG48; Q96B97: SH3KBP1; NbExp=6; IntAct=EBI-3390054, EBI-346595;
CC P0CG48; Q9Y5X1: SNX9; NbExp=2; IntAct=EBI-3390054, EBI-77848;
CC P0CG48; Q13501: SQSTM1; NbExp=3; IntAct=EBI-3390054, EBI-307104;
CC P0CG48; Q92783: STAM; NbExp=2; IntAct=EBI-3390054, EBI-752333;
CC P0CG48; Q86VP1: TAX1BP1; NbExp=8; IntAct=EBI-3390054, EBI-529518;
CC P0CG48; P04637: TP53; NbExp=15; IntAct=EBI-3390054, EBI-366083;
CC P0CG48; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-3390054, EBI-359276;
CC P0CG48; Q9BSL1: UBAC1; NbExp=3; IntAct=EBI-3390054, EBI-749370;
CC P0CG48; P60604: UBE2G2; NbExp=3; IntAct=EBI-3390054, EBI-1051028;
CC P0CG48; Q05086-3: UBE3A; NbExp=3; IntAct=EBI-3390054, EBI-11026619;
CC P0CG48; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-3390054, EBI-947187;
CC P0CG48; P98170: XIAP; NbExp=3; IntAct=EBI-3390054, EBI-517127;
CC P0CG48; Q5VVQ6: YOD1; NbExp=3; IntAct=EBI-3390054, EBI-2510804;
CC P0CG48; O76080: ZFAND5; NbExp=3; IntAct=EBI-3390054, EBI-8028844;
CC P0CG48; Q9UGI0: ZRANB1; NbExp=2; IntAct=EBI-3390054, EBI-527853;
CC P0CG48; P40087: DDI1; Xeno; NbExp=2; IntAct=EBI-3390054, EBI-5717;
CC P0CG48; P48510: DSK2; Xeno; NbExp=2; IntAct=EBI-3390054, EBI-6174;
CC P0CG48; Q61088: Fzd4; Xeno; NbExp=3; IntAct=EBI-3390054, EBI-7987880;
CC P0CG48; O88522: Ikbkg; Xeno; NbExp=3; IntAct=EBI-3390054, EBI-998011;
CC P0CG48; P32628: RAD23; Xeno; NbExp=2; IntAct=EBI-3390054, EBI-14668;
CC P0CG48; Q84L31: RAD23C; Xeno; NbExp=2; IntAct=EBI-3390054, EBI-4437395;
CC P0CG48; Q62921: Rbck1; Xeno; NbExp=2; IntAct=EBI-3390054, EBI-7266339;
CC P0CG48; PRO_0000037311 [P0C6X7]: rep; Xeno; NbExp=3; IntAct=EBI-3390054, EBI-25474079;
CC P0CG48; PRO_0000449621 [P0DTD1]: rep; Xeno; NbExp=2; IntAct=EBI-3390054, EBI-25492388;
CC P0CG48; P04325: rev; Xeno; NbExp=2; IntAct=EBI-3390054, EBI-7061954;
CC P0CG48; P55034: RPN10; Xeno; NbExp=2; IntAct=EBI-3390054, EBI-2620423;
CC P0CG48; O48726: RPN13; Xeno; NbExp=9; IntAct=EBI-3390054, EBI-7710745;
CC P0CG48; Q9EPK8: Trpv4; Xeno; NbExp=3; IntAct=EBI-3390054, EBI-7091763;
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:24751536}; Peripheral membrane protein
CC {ECO:0000305|PubMed:24751536}.
CC -!- PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.
CC Phosphorylated ubiquitin specifically binds and activates parkin
CC (PRKN), triggering mitophagy (PubMed:24660806, PubMed:24751536,
CC PubMed:24784582, PubMed:25527291). Phosphorylation does not affect E1-
CC mediated E2 charging of ubiquitin but affects discharging of E2 enzymes
CC to form polyubiquitin chains. It also affects deubiquitination by
CC deubiquitinase enzymes such as USP30 (PubMed:25527291).
CC {ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536,
CC ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291}.
CC -!- PTM: [Ubiquitin]: Mono-ADP-ribosylated at the C-terminus by PARP9, a
CC component of the PPAR9-DTX3L complex. ADP-ribosylation requires
CC processing by E1 and E2 enzymes and prevents ubiquitin conjugation to
CC substrates such as histones. {ECO:0000269|PubMed:28525742}.
CC -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. UBA52 and
CC RPS27A genes code for a single copy of ubiquitin fused to the ribosomal
CC proteins L40 and S27a, respectively. UBB and UBC genes code for a
CC polyubiquitin precursor with exact head to tail repeats, the number of
CC repeats differ between species and strains.
CC -!- MISCELLANEOUS: For the sake of clarity sequence features are annotated
CC only for the first chain, and are not repeated for each of the
CC following chains.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; M26880; AAA36789.1; -; mRNA.
DR EMBL; AB009010; BAA23632.1; -; mRNA.
DR EMBL; AB089613; BAC56951.1; -; Genomic_DNA.
DR EMBL; AC126309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039193; AAH39193.1; -; mRNA.
DR EMBL; D63791; BAA09860.1; -; Genomic_DNA.
DR EMBL; AB003730; BAA23486.1; -; Genomic_DNA.
DR EMBL; M17597; AAA36787.1; -; mRNA.
DR CCDS; CCDS9260.1; -.
DR PIR; A02574; UQHU.
DR PIR; A22005; UQHUC.
DR PIR; A29526; A29526.
DR RefSeq; NP_066289.3; NM_021009.6.
DR PDB; 1C3T; NMR; -; A=1-76.
DR PDB; 1CMX; X-ray; 2.25 A; B/D=1-76.
DR PDB; 1D3Z; NMR; -; A=1-76.
DR PDB; 1F9J; X-ray; 2.70 A; A/B=1-76.
DR PDB; 1FXT; NMR; -; B=1-76.
DR PDB; 1G6J; NMR; -; A=1-76.
DR PDB; 1GJZ; NMR; -; A/B=1-51.
DR PDB; 1NBF; X-ray; 2.30 A; C/D=1-76.
DR PDB; 1OGW; X-ray; 1.32 A; A=1-76.
DR PDB; 1Q5W; NMR; -; B=1-76.
DR PDB; 1S1Q; X-ray; 2.00 A; B/D=1-76.
DR PDB; 1SIF; X-ray; 2.18 A; A=6-76.
DR PDB; 1TBE; X-ray; 2.40 A; A/B=1-76.
DR PDB; 1UBI; X-ray; 1.80 A; A=1-76.
DR PDB; 1UBQ; X-ray; 1.80 A; A=1-76.
DR PDB; 1UD7; NMR; -; A=1-76.
DR PDB; 1XD3; X-ray; 1.45 A; B/D=1-75.
DR PDB; 1XQQ; NMR; -; A=1-76.
DR PDB; 1YX5; NMR; -; B=1-76.
DR PDB; 1YX6; NMR; -; B=1-76.
DR PDB; 1ZGU; NMR; -; B=1-76.
DR PDB; 2AYO; X-ray; 3.50 A; B=1-76.
DR PDB; 2BGF; NMR; -; A/B=1-76.
DR PDB; 2DEN; NMR; -; B=1-76.
DR PDB; 2FUH; NMR; -; B=1-76.
DR PDB; 2G45; X-ray; 1.99 A; B/E=1-76.
DR PDB; 2GBJ; X-ray; 1.35 A; A/B=1-76.
DR PDB; 2GBK; X-ray; 1.99 A; A/B/C/D=10-76.
DR PDB; 2GBM; X-ray; 1.55 A; A/B/C/D=1-76.
DR PDB; 2GBN; X-ray; 1.60 A; A=1-76.
DR PDB; 2GBR; X-ray; 2.00 A; A/B/C=1-76.
DR PDB; 2GMI; X-ray; 2.50 A; C=1-76.
DR PDB; 2HTH; X-ray; 2.70 A; A=1-76.
DR PDB; 2IBI; X-ray; 2.20 A; B=1-75.
DR PDB; 2J7Q; X-ray; 1.80 A; B/D=1-75.
DR PDB; 2JF5; X-ray; 1.95 A; A/B=1-76.
DR PDB; 2JRI; NMR; -; B/C=1-76.
DR PDB; 2JY6; NMR; -; A=1-76.
DR PDB; 2JZZ; NMR; -; A=1-76.
DR PDB; 2K25; NMR; -; A=1-75.
DR PDB; 2K6D; NMR; -; B=1-75.
DR PDB; 2K8B; NMR; -; A=1-76.
DR PDB; 2K8C; NMR; -; A=1-76.
DR PDB; 2KDF; NMR; -; B/C=1-76.
DR PDB; 2KHW; NMR; -; B=1-76.
DR PDB; 2KJH; NMR; -; B=1-75.
DR PDB; 2KLG; NMR; -; A=1-76.
DR PDB; 2KN5; NMR; -; A=1-76.
DR PDB; 2KX0; NMR; -; A=74-151.
DR PDB; 2L3Z; NMR; -; A=1-76.
DR PDB; 2LD9; NMR; -; A=76-152.
DR PDB; 2LVO; NMR; -; A=1-76.
DR PDB; 2LVP; NMR; -; A/B=1-76.
DR PDB; 2LVQ; NMR; -; A/B=1-76.
DR PDB; 2LZ6; NMR; -; A=609-684.
DR PDB; 2MBO; NMR; -; A/B=609-684.
DR PDB; 2MBQ; NMR; -; A/B=609-684.
DR PDB; 2MCN; NMR; -; B=609-684.
DR PDB; 2MI8; NMR; -; A=609-684.
DR PDB; 2MJ5; NMR; -; A=609-684.
DR PDB; 2MOR; NMR; -; A=609-684.
DR PDB; 2MRE; NMR; -; A=609-684.
DR PDB; 2MWS; NMR; -; A=609-684.
DR PDB; 2N2K; NMR; -; A=609-684, B=609-679.
DR PDB; 2NR2; NMR; -; A=1-76.
DR PDB; 2O6V; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-76.
DR PDB; 2OJR; X-ray; 2.60 A; A=1-76.
DR PDB; 2PE9; NMR; -; A/B=1-76.
DR PDB; 2PEA; NMR; -; A/B=1-76.
DR PDB; 2RR9; NMR; -; A/B=1-76.
DR PDB; 2RU6; NMR; -; A=609-684.
DR PDB; 2W9N; X-ray; 2.25 A; A=1-152.
DR PDB; 2WDT; X-ray; 2.30 A; B/D=1-75.
DR PDB; 2XEW; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-76.
DR PDB; 2Y5B; X-ray; 2.70 A; B/F=1-152.
DR PDB; 2Z59; NMR; -; B=1-76.
DR PDB; 2ZCB; X-ray; 1.60 A; A/B/C=1-76.
DR PDB; 2ZVN; X-ray; 3.00 A; A/C/E/G=1-152.
DR PDB; 2ZVO; X-ray; 2.90 A; A/G=1-152.
DR PDB; 3A33; X-ray; 2.20 A; B=1-76.
DR PDB; 3ALB; X-ray; 1.85 A; A/B/C/D=1-76.
DR PDB; 3AUL; X-ray; 2.39 A; A/B=1-76.
DR PDB; 3B08; X-ray; 1.70 A; A/D/G/J=1-152.
DR PDB; 3B0A; X-ray; 1.90 A; A/D=1-152.
DR PDB; 3BY4; X-ray; 1.55 A; B=1-75.
DR PDB; 3C0R; X-ray; 2.31 A; B/D=1-75.
DR PDB; 3DVG; X-ray; 2.60 A; X/Y=1-76.
DR PDB; 3DVN; X-ray; 2.70 A; U/V/X/Y=1-76.
DR PDB; 3EEC; X-ray; 3.00 A; A/B=1-76.
DR PDB; 3EFU; X-ray; 1.84 A; A=1-76.
DR PDB; 3EHV; X-ray; 1.81 A; A/B/C=1-76.
DR PDB; 3H7P; X-ray; 1.90 A; A/B=1-76.
DR PDB; 3H7S; X-ray; 2.30 A; A/B=1-76.
DR PDB; 3HM3; X-ray; 1.96 A; A/B/C/D=1-76.
DR PDB; 3I3T; X-ray; 2.59 A; B/D/F/H=1-75.
DR PDB; 3IFW; X-ray; 2.40 A; B=1-75.
DR PDB; 3IHP; X-ray; 2.80 A; C/D=1-75.
DR PDB; 3JSV; X-ray; 2.70 A; A/B=1-76.
DR PDB; 3JVZ; X-ray; 3.30 A; X/Y=1-76.
DR PDB; 3JW0; X-ray; 3.10 A; X/Y=1-76.
DR PDB; 3K9O; X-ray; 1.80 A; B=76-151.
DR PDB; 3K9P; X-ray; 2.80 A; B=1-76.
DR PDB; 3KVF; X-ray; 2.80 A; B=1-75.
DR PDB; 3KW5; X-ray; 2.83 A; B=1-75.
DR PDB; 3LDZ; X-ray; 2.60 A; E/F/G=1-73.
DR PDB; 3MHS; X-ray; 1.89 A; D=1-76.
DR PDB; 3MTN; X-ray; 2.70 A; B/D=1-76.
DR PDB; 3N30; X-ray; 3.00 A; A/B=1-76.
DR PDB; 3N32; X-ray; 1.80 A; A=1-76.
DR PDB; 3N3K; X-ray; 2.60 A; B=5-76.
DR PDB; 3NS8; X-ray; 1.71 A; A/B=1-76.
DR PDB; 3O65; X-ray; 2.70 A; B/D/F/H=1-75.
DR PDB; 3OFI; X-ray; 2.35 A; C/D=1-76.
DR PDB; 3OJ3; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-76.
DR PDB; 3OJ4; X-ray; 3.40 A; B/E=1-76.
DR PDB; 3ONS; X-ray; 1.80 A; A=1-72.
DR PDB; 3PRM; X-ray; 2.30 A; B/D=1-75.
DR PDB; 3PT2; X-ray; 2.50 A; B=1-75.
DR PDB; 3PTF; X-ray; 2.70 A; C/D=1-76.
DR PDB; 3Q3F; X-ray; 2.17 A; A=2-76.
DR PDB; 3RUL; X-ray; 2.50 A; A/B/C/D=1-75.
DR PDB; 3TMP; X-ray; 1.91 A; B/D/F/H=1-76.
DR PDB; 3U30; X-ray; 2.43 A; A/D=1-152.
DR PDB; 3UGB; X-ray; 2.35 A; B=1-76.
DR PDB; 3V6C; X-ray; 1.70 A; B=74-150.
DR PDB; 3V6E; X-ray; 2.10 A; B=74-150.
DR PDB; 3VFK; X-ray; 2.80 A; A=1-75.
DR PDB; 3VUW; X-ray; 1.95 A; A/B/C=1-76.
DR PDB; 3VUX; X-ray; 1.70 A; A/B/C=1-76.
DR PDB; 3VUY; X-ray; 1.98 A; A/B/C=1-76.
DR PDB; 3WXE; X-ray; 2.50 A; B=533-680.
DR PDB; 3WXF; X-ray; 2.30 A; B/D=533-680.
DR PDB; 3ZLZ; X-ray; 2.90 A; A/B=1-76.
DR PDB; 3ZNH; X-ray; 2.30 A; B=1-75.
DR PDB; 3ZNI; X-ray; 2.21 A; D/H/L/P=1-76.
DR PDB; 3ZNZ; X-ray; 1.90 A; B=1-152.
DR PDB; 4AP4; X-ray; 2.21 A; C/F=608-684.
DR PDB; 4AUQ; X-ray; 2.18 A; C/F=1-76.
DR PDB; 4BOS; X-ray; 2.35 A; C/E=609-684, F=612-625.
DR PDB; 4BOZ; X-ray; 3.03 A; B/C/E=1-76.
DR PDB; 4BVU; X-ray; 2.70 A; C=609-684.
DR PDB; 4DDG; X-ray; 3.30 A; D/E/F/G/H/I/M/N/O/P/Q/R=1-76.
DR PDB; 4DDI; X-ray; 3.80 A; G/H/I/J/K/L=1-76.
DR PDB; 4DHJ; X-ray; 2.35 A; B/F/J/M=1-76, D/H=1-75.
DR PDB; 4DHZ; X-ray; 3.11 A; B=1-76, E=1-75.
DR PDB; 4FJV; X-ray; 2.05 A; B/D=1-76.
DR PDB; 4HK2; X-ray; 1.40 A; A/B/C/D=1-76.
DR PDB; 4HXD; X-ray; 2.85 A; A/C=1-75.
DR PDB; 4I6L; X-ray; 2.49 A; B=77-150.
DR PDB; 4I6N; X-ray; 1.70 A; B/D=1-75.
DR PDB; 4IG7; X-ray; 2.00 A; B=1-75.
DR PDB; 4IUM; X-ray; 1.45 A; B=1-75.
DR PDB; 4JQW; X-ray; 2.90 A; C=609-684.
DR PDB; 4K1R; X-ray; 1.63 A; B/D=607-684.
DR PDB; 4K7S; X-ray; 1.76 A; A/B/C=1-76.
DR PDB; 4K7U; X-ray; 1.76 A; A/B/C=1-76.
DR PDB; 4K7W; X-ray; 1.76 A; A/B/C=1-76.
DR PDB; 4KSK; X-ray; 2.40 A; C/D=76-152.
DR PDB; 4KSL; X-ray; 2.83 A; C/D/F/H/J/L/N/P/R/T/V/X=76-228.
DR PDB; 4LCD; X-ray; 3.10 A; E/F=609-683.
DR PDB; 4LDT; X-ray; 1.90 A; B/D=609-684.
DR PDB; 4MDK; X-ray; 2.61 A; E/F/G/H=608-684.
DR PDB; 4MM3; X-ray; 2.75 A; A=609-684.
DR PDB; 4MSM; X-ray; 1.74 A; B/D=609-684.
DR PDB; 4MSQ; X-ray; 1.95 A; B/D=609-684.
DR PDB; 4NQK; X-ray; 3.70 A; E/F/G/H/I/J=608-684.
DR PDB; 4UN2; X-ray; 1.51 A; A=609-684.
DR PDB; 4V3K; X-ray; 2.04 A; B/E=609-684.
DR PDB; 4V3L; X-ray; 1.53 A; B/D=609-684.
DR PDB; 4WZP; X-ray; 1.90 A; A/B/C/D/E/F/G/H=153-228.
DR PDB; 4XOK; X-ray; 2.20 A; A/B/C=1-76.
DR PDB; 4XOL; X-ray; 2.91 A; A/B=1-76.
DR PDB; 4ZQS; X-ray; 1.80 A; A/B=533-684.
DR PDB; 5A5B; EM; 9.50 A; 9=609-684.
DR PDB; 5AF4; X-ray; 1.85 A; A/B/C/D/E/F/G/H=1-76.
DR PDB; 5AF5; X-ray; 1.68 A; A=1-73.
DR PDB; 5AF6; X-ray; 3.40 A; A/B/C/D/E=1-76.
DR PDB; 5AIT; X-ray; 3.40 A; C/F=609-684.
DR PDB; 5AIU; X-ray; 2.21 A; C/F=609-684.
DR PDB; 5B83; X-ray; 2.69 A; A/D=1-304.
DR PDB; 5C7J; X-ray; 3.00 A; C/D=1-74.
DR PDB; 5C7M; X-ray; 3.03 A; B/C=1-75.
DR PDB; 5E6J; X-ray; 2.85 A; B/E=609-683.
DR PDB; 5H07; X-ray; 2.59 A; A=1-228.
DR PDB; 5NL4; X-ray; 1.32 A; A/B/C=1-76.
DR PDB; 5NLF; X-ray; 1.50 A; A/B/C=1-76.
DR PDB; 5NLI; X-ray; 1.53 A; A/B/C=1-76.
DR PDB; 5NMC; X-ray; 1.70 A; A/B/C=1-76.
DR PDB; 5OE7; X-ray; 2.95 A; B=1-146.
DR PDB; 5OHV; X-ray; 2.80 A; A/C=1-76.
DR PDB; 5OXH; X-ray; 1.60 A; A=1-76.
DR PDB; 5OXI; X-ray; 1.63 A; A/B=1-76.
DR PDB; 5UDH; X-ray; 3.24 A; E=1-76.
DR PDB; 5WQ4; X-ray; 3.00 A; A/B=1-152.
DR PDB; 5ZQ3; X-ray; 2.18 A; C/D=609-684.
DR PDB; 5ZQ4; X-ray; 2.22 A; C/D=609-684.
DR PDB; 5ZQ5; X-ray; 2.49 A; B/D=609-684.
DR PDB; 5ZQ6; X-ray; 3.01 A; B/D=609-684.
DR PDB; 5ZQ7; X-ray; 2.85 A; B/D=609-684.
DR PDB; 6A43; X-ray; 2.40 A; A=1-76.
DR PDB; 6A44; X-ray; 2.40 A; A=1-76.
DR PDB; 6AQR; X-ray; 2.10 A; D=609-684.
DR PDB; 6B7M; X-ray; 1.70 A; B/C=609-684.
DR PDB; 6B7O; X-ray; 1.85 A; B/C=609-684.
DR PDB; 6EQI; X-ray; 3.10 A; A=1-76.
DR PDB; 6K2U; X-ray; 2.55 A; B=1-76.
DR PDB; 6KBE; X-ray; 2.34 A; G=1-152.
DR PDB; 6N13; NMR; -; A=1-76.
DR PDB; 6N6R; X-ray; 1.95 A; A/C=1-76.
DR PDB; 6NQA; EM; 3.54 A; L=1-76.
DR PDB; 6NXK; X-ray; 2.20 A; A/B=1-76.
DR PDB; 6OI4; X-ray; 1.76 A; C/D=1-76.
DR PDB; 6P5B; X-ray; 2.10 A; E=1-76.
DR PDB; 6Q00; X-ray; 0.85 A; A=1-76.
DR PDB; 6QML; X-ray; 2.10 A; C/F=1-76.
DR PDB; 6RYA; X-ray; 2.21 A; B/D/F=1-76.
DR PDB; 6S53; X-ray; 2.80 A; D/F/J/L=1-76.
DR PDB; 6SQR; X-ray; 2.18 A; I=1-76.
DR PDB; 6T7F; X-ray; 2.58 A; C=1-73.
DR PDB; 6T9L; EM; 3.60 A; O=1-76.
DR PDB; 6TNF; EM; 3.80 A; C=1-76.
DR PDB; 6TTU; EM; 3.70 A; U=1-76.
DR PDB; 6TUV; X-ray; 2.16 A; D/H/L=1-76.
DR PDB; 6TXB; X-ray; 2.18 A; D/H/L=1-76.
DR PDB; 6ULH; X-ray; 1.97 A; E=1-76.
DR PDB; 6UMP; X-ray; 2.80 A; E=1-76.
DR PDB; 6UMS; X-ray; 2.34 A; E=1-76.
DR PDB; 6UPU; X-ray; 2.20 A; B/C/D/F/G/H/J/K/L/N/O/P=609-684.
DR PDB; 6V5D; NMR; -; A=1-76.
DR PDB; 6VAE; EM; 3.50 A; C/D=1-76.
DR PDB; 6VAF; EM; 3.90 A; D=1-76.
DR PDB; 6VEN; EM; 3.37 A; K=1-76.
DR PDB; 6W9D; X-ray; 3.19 A; C/F/I=1-76.
DR PDB; 6W9R; X-ray; 1.82 A; M/N/O/P/Q/R/S/T/U/V/W/X=609-683.
DR PDB; 6W9S; X-ray; 2.10 A; B=77-151.
DR PDB; 6WJD; EM; 4.80 A; u=1-76.
DR PDB; 6WKR; EM; 3.50 A; F/T=1-76.
DR PDB; 6WTG; X-ray; 2.63 A; D=1-76.
DR PDB; 6Z7V; X-ray; 2.65 A; C/D/E/F/G/H/I=1-76.
DR PDB; 7B5L; EM; 3.80 A; U=1-75.
DR PDB; 7B5M; EM; 3.91 A; U=1-75.
DR PDB; 7B5N; EM; 3.60 A; U=1-75.
DR PDB; 7BBD; X-ray; 2.20 A; D=1-76.
DR PDB; 7BBF; X-ray; 2.54 A; C/F/I=1-76.
DR PDB; 7BXG; X-ray; 2.71 A; D=1-76.
DR PDB; 7EAL; X-ray; 2.50 A; A/D=1-152.
DR PDB; 7EAO; X-ray; 2.90 A; A=1-228.
DR PDB; 7EB9; X-ray; 3.20 A; A=1-304.
DR PDB; 7JXV; X-ray; 2.35 A; B=1-76.
DR PDB; 7K6P; EM; 3.20 A; L=1-76.
DR PDB; 7K6Q; EM; 3.10 A; L=1-76.
DR PDB; 7KEO; X-ray; 2.90 A; C/D/G/H=1-76.
DR PDB; 7M4M; X-ray; 2.39 A; C/D=1-76.
DR PDB; 7M4N; X-ray; 2.52 A; C/D/E/F=1-76.
DR PDB; 7M4O; X-ray; 2.21 A; B/C=1-76.
DR PDB; 7MEX; EM; 3.35 A; C=1-76.
DR PDB; 7MIC; X-ray; 2.09 A; B=1-75.
DR PDB; 7MYF; X-ray; 3.00 A; C=1-76.
DR PDB; 7NPI; X-ray; 2.81 A; B/C/D/E/F/H/I/J/K/L/N/O/P/Q/R/T/U/V/W/X/Z/a/b/c/d/f/g/h/i/j=609-684.
DR PDB; 7OWD; X-ray; 1.71 A; A=1-76.
DR PDB; 7R70; X-ray; 2.50 A; A/B=1-76.
DR PDBsum; 1C3T; -.
DR PDBsum; 1CMX; -.
DR PDBsum; 1D3Z; -.
DR PDBsum; 1F9J; -.
DR PDBsum; 1FXT; -.
DR PDBsum; 1G6J; -.
DR PDBsum; 1GJZ; -.
DR PDBsum; 1NBF; -.
DR PDBsum; 1OGW; -.
DR PDBsum; 1Q5W; -.
DR PDBsum; 1S1Q; -.
DR PDBsum; 1SIF; -.
DR PDBsum; 1TBE; -.
DR PDBsum; 1UBI; -.
DR PDBsum; 1UBQ; -.
DR PDBsum; 1UD7; -.
DR PDBsum; 1XD3; -.
DR PDBsum; 1XQQ; -.
DR PDBsum; 1YX5; -.
DR PDBsum; 1YX6; -.
DR PDBsum; 1ZGU; -.
DR PDBsum; 2AYO; -.
DR PDBsum; 2BGF; -.
DR PDBsum; 2DEN; -.
DR PDBsum; 2FUH; -.
DR PDBsum; 2G45; -.
DR PDBsum; 2GBJ; -.
DR PDBsum; 2GBK; -.
DR PDBsum; 2GBM; -.
DR PDBsum; 2GBN; -.
DR PDBsum; 2GBR; -.
DR PDBsum; 2GMI; -.
DR PDBsum; 2HTH; -.
DR PDBsum; 2IBI; -.
DR PDBsum; 2J7Q; -.
DR PDBsum; 2JF5; -.
DR PDBsum; 2JRI; -.
DR PDBsum; 2JY6; -.
DR PDBsum; 2JZZ; -.
DR PDBsum; 2K25; -.
DR PDBsum; 2K6D; -.
DR PDBsum; 2K8B; -.
DR PDBsum; 2K8C; -.
DR PDBsum; 2KDF; -.
DR PDBsum; 2KHW; -.
DR PDBsum; 2KJH; -.
DR PDBsum; 2KLG; -.
DR PDBsum; 2KN5; -.
DR PDBsum; 2KX0; -.
DR PDBsum; 2L3Z; -.
DR PDBsum; 2LD9; -.
DR PDBsum; 2LVO; -.
DR PDBsum; 2LVP; -.
DR PDBsum; 2LVQ; -.
DR PDBsum; 2LZ6; -.
DR PDBsum; 2MBO; -.
DR PDBsum; 2MBQ; -.
DR PDBsum; 2MCN; -.
DR PDBsum; 2MI8; -.
DR PDBsum; 2MJ5; -.
DR PDBsum; 2MOR; -.
DR PDBsum; 2MRE; -.
DR PDBsum; 2MWS; -.
DR PDBsum; 2N2K; -.
DR PDBsum; 2NR2; -.
DR PDBsum; 2O6V; -.
DR PDBsum; 2OJR; -.
DR PDBsum; 2PE9; -.
DR PDBsum; 2PEA; -.
DR PDBsum; 2RR9; -.
DR PDBsum; 2RU6; -.
DR PDBsum; 2W9N; -.
DR PDBsum; 2WDT; -.
DR PDBsum; 2XEW; -.
DR PDBsum; 2Y5B; -.
DR PDBsum; 2Z59; -.
DR PDBsum; 2ZCB; -.
DR PDBsum; 2ZVN; -.
DR PDBsum; 2ZVO; -.
DR PDBsum; 3A33; -.
DR PDBsum; 3ALB; -.
DR PDBsum; 3AUL; -.
DR PDBsum; 3B08; -.
DR PDBsum; 3B0A; -.
DR PDBsum; 3BY4; -.
DR PDBsum; 3C0R; -.
DR PDBsum; 3DVG; -.
DR PDBsum; 3DVN; -.
DR PDBsum; 3EEC; -.
DR PDBsum; 3EFU; -.
DR PDBsum; 3EHV; -.
DR PDBsum; 3H7P; -.
DR PDBsum; 3H7S; -.
DR PDBsum; 3HM3; -.
DR PDBsum; 3I3T; -.
DR PDBsum; 3IFW; -.
DR PDBsum; 3IHP; -.
DR PDBsum; 3JSV; -.
DR PDBsum; 3JVZ; -.
DR PDBsum; 3JW0; -.
DR PDBsum; 3K9O; -.
DR PDBsum; 3K9P; -.
DR PDBsum; 3KVF; -.
DR PDBsum; 3KW5; -.
DR PDBsum; 3LDZ; -.
DR PDBsum; 3MHS; -.
DR PDBsum; 3MTN; -.
DR PDBsum; 3N30; -.
DR PDBsum; 3N32; -.
DR PDBsum; 3N3K; -.
DR PDBsum; 3NS8; -.
DR PDBsum; 3O65; -.
DR PDBsum; 3OFI; -.
DR PDBsum; 3OJ3; -.
DR PDBsum; 3OJ4; -.
DR PDBsum; 3ONS; -.
DR PDBsum; 3PRM; -.
DR PDBsum; 3PT2; -.
DR PDBsum; 3PTF; -.
DR PDBsum; 3Q3F; -.
DR PDBsum; 3RUL; -.
DR PDBsum; 3TMP; -.
DR PDBsum; 3U30; -.
DR PDBsum; 3UGB; -.
DR PDBsum; 3V6C; -.
DR PDBsum; 3V6E; -.
DR PDBsum; 3VFK; -.
DR PDBsum; 3VUW; -.
DR PDBsum; 3VUX; -.
DR PDBsum; 3VUY; -.
DR PDBsum; 3WXE; -.
DR PDBsum; 3WXF; -.
DR PDBsum; 3ZLZ; -.
DR PDBsum; 3ZNH; -.
DR PDBsum; 3ZNI; -.
DR PDBsum; 3ZNZ; -.
DR PDBsum; 4AP4; -.
DR PDBsum; 4AUQ; -.
DR PDBsum; 4BOS; -.
DR PDBsum; 4BOZ; -.
DR PDBsum; 4BVU; -.
DR PDBsum; 4DDG; -.
DR PDBsum; 4DDI; -.
DR PDBsum; 4DHJ; -.
DR PDBsum; 4DHZ; -.
DR PDBsum; 4FJV; -.
DR PDBsum; 4HK2; -.
DR PDBsum; 4HXD; -.
DR PDBsum; 4I6L; -.
DR PDBsum; 4I6N; -.
DR PDBsum; 4IG7; -.
DR PDBsum; 4IUM; -.
DR PDBsum; 4JQW; -.
DR PDBsum; 4K1R; -.
DR PDBsum; 4K7S; -.
DR PDBsum; 4K7U; -.
DR PDBsum; 4K7W; -.
DR PDBsum; 4KSK; -.
DR PDBsum; 4KSL; -.
DR PDBsum; 4LCD; -.
DR PDBsum; 4LDT; -.
DR PDBsum; 4MDK; -.
DR PDBsum; 4MM3; -.
DR PDBsum; 4MSM; -.
DR PDBsum; 4MSQ; -.
DR PDBsum; 4NQK; -.
DR PDBsum; 4UN2; -.
DR PDBsum; 4V3K; -.
DR PDBsum; 4V3L; -.
DR PDBsum; 4WZP; -.
DR PDBsum; 4XOK; -.
DR PDBsum; 4XOL; -.
DR PDBsum; 4ZQS; -.
DR PDBsum; 5A5B; -.
DR PDBsum; 5AF4; -.
DR PDBsum; 5AF5; -.
DR PDBsum; 5AF6; -.
DR PDBsum; 5AIT; -.
DR PDBsum; 5AIU; -.
DR PDBsum; 5B83; -.
DR PDBsum; 5C7J; -.
DR PDBsum; 5C7M; -.
DR PDBsum; 5E6J; -.
DR PDBsum; 5H07; -.
DR PDBsum; 5NL4; -.
DR PDBsum; 5NLF; -.
DR PDBsum; 5NLI; -.
DR PDBsum; 5NMC; -.
DR PDBsum; 5OE7; -.
DR PDBsum; 5OHV; -.
DR PDBsum; 5OXH; -.
DR PDBsum; 5OXI; -.
DR PDBsum; 5UDH; -.
DR PDBsum; 5WQ4; -.
DR PDBsum; 5ZQ3; -.
DR PDBsum; 5ZQ4; -.
DR PDBsum; 5ZQ5; -.
DR PDBsum; 5ZQ6; -.
DR PDBsum; 5ZQ7; -.
DR PDBsum; 6A43; -.
DR PDBsum; 6A44; -.
DR PDBsum; 6AQR; -.
DR PDBsum; 6B7M; -.
DR PDBsum; 6B7O; -.
DR PDBsum; 6EQI; -.
DR PDBsum; 6K2U; -.
DR PDBsum; 6KBE; -.
DR PDBsum; 6N13; -.
DR PDBsum; 6N6R; -.
DR PDBsum; 6NQA; -.
DR PDBsum; 6NXK; -.
DR PDBsum; 6OI4; -.
DR PDBsum; 6P5B; -.
DR PDBsum; 6Q00; -.
DR PDBsum; 6QML; -.
DR PDBsum; 6RYA; -.
DR PDBsum; 6S53; -.
DR PDBsum; 6SQR; -.
DR PDBsum; 6T7F; -.
DR PDBsum; 6T9L; -.
DR PDBsum; 6TNF; -.
DR PDBsum; 6TTU; -.
DR PDBsum; 6TUV; -.
DR PDBsum; 6TXB; -.
DR PDBsum; 6ULH; -.
DR PDBsum; 6UMP; -.
DR PDBsum; 6UMS; -.
DR PDBsum; 6UPU; -.
DR PDBsum; 6V5D; -.
DR PDBsum; 6VAE; -.
DR PDBsum; 6VAF; -.
DR PDBsum; 6VEN; -.
DR PDBsum; 6W9D; -.
DR PDBsum; 6W9R; -.
DR PDBsum; 6W9S; -.
DR PDBsum; 6WJD; -.
DR PDBsum; 6WKR; -.
DR PDBsum; 6WTG; -.
DR PDBsum; 6Z7V; -.
DR PDBsum; 7B5L; -.
DR PDBsum; 7B5M; -.
DR PDBsum; 7B5N; -.
DR PDBsum; 7BBD; -.
DR PDBsum; 7BBF; -.
DR PDBsum; 7BXG; -.
DR PDBsum; 7EAL; -.
DR PDBsum; 7EAO; -.
DR PDBsum; 7EB9; -.
DR PDBsum; 7JXV; -.
DR PDBsum; 7K6P; -.
DR PDBsum; 7K6Q; -.
DR PDBsum; 7KEO; -.
DR PDBsum; 7M4M; -.
DR PDBsum; 7M4N; -.
DR PDBsum; 7M4O; -.
DR PDBsum; 7MEX; -.
DR PDBsum; 7MIC; -.
DR PDBsum; 7MYF; -.
DR PDBsum; 7NPI; -.
DR PDBsum; 7OWD; -.
DR PDBsum; 7R70; -.
DR AlphaFoldDB; P0CG48; -.
DR BMRB; P0CG48; -.
DR SASBDB; P0CG48; -.
DR SMR; P0CG48; -.
DR BioGRID; 113164; 1786.
DR IntAct; P0CG48; 202.
DR MINT; P0CG48; -.
DR STRING; 9606.ENSP00000441543; -.
DR ChEMBL; CHEMBL4523179; -.
DR DrugBank; DB04464; N-Formylmethionine.
DR MoonDB; P0CG48; Predicted.
DR GlyGen; P0CG48; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P0CG48; -.
DR PhosphoSitePlus; P0CG48; -.
DR SwissPalm; P0CG48; -.
DR BioMuta; UBC; -.
DR DMDM; 391358178; -.
DR EPD; P0CG48; -.
DR jPOST; P0CG48; -.
DR MassIVE; P0CG48; -.
DR MaxQB; P0CG48; -.
DR PaxDb; P0CG48; -.
DR PeptideAtlas; P0CG48; -.
DR PRIDE; P0CG48; -.
DR ProteomicsDB; 52475; -.
DR TopDownProteomics; P0CG48; -.
DR ABCD; P0CG48; 3 sequenced antibodies.
DR Antibodypedia; 3954; 260 antibodies from 32 providers.
DR DNASU; 7316; -.
DR Ensembl; ENST00000339647.6; ENSP00000344818.5; ENSG00000150991.16.
DR Ensembl; ENST00000536769.1; ENSP00000441543.1; ENSG00000150991.16.
DR GeneID; 7316; -.
DR KEGG; hsa:7316; -.
DR MANE-Select; ENST00000339647.6; ENSP00000344818.5; NM_021009.7; NP_066289.3.
DR UCSC; uc001ugs.5; human.
DR CTD; 7316; -.
DR DisGeNET; 7316; -.
DR GeneCards; UBC; -.
DR HGNC; HGNC:12468; UBC.
DR HPA; ENSG00000150991; Low tissue specificity.
DR MIM; 191340; gene.
DR neXtProt; NX_P0CG48; -.
DR OpenTargets; ENSG00000150991; -.
DR VEuPathDB; HostDB:ENSG00000150991; -.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00940000163900; -.
DR HOGENOM; CLU_010412_1_1_1; -.
DR InParanoid; P0CG48; -.
DR OMA; MASEMQI; -.
DR OrthoDB; 1536766at2759; -.
DR TreeFam; TF354256; -.
DR BioCyc; MetaCyc:ENSG00000150991-MON; -.
DR PathwayCommons; P0CG48; -.
DR Reactome; R-HSA-110312; Translesion synthesis by REV1.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-110320; Translesion Synthesis by POLH.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1253288; Downregulation of ERBB4 signaling.
DR Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
DR Reactome; R-HSA-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
DR Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
DR Reactome; R-HSA-175474; Assembly Of The HIV Virion.
DR Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-182971; EGFR downregulation.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-205043; NRIF signals cell death from the nucleus.
DR Reactome; R-HSA-209543; p75NTR recruits signalling complexes.
DR Reactome; R-HSA-209560; NF-kB is activated and signals survival.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR Reactome; R-HSA-2691232; Constitutive Signaling by NOTCH1 HD Domain Mutants.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-HSA-3134975; Regulation of innate immune responses to cytosolic DNA.
DR Reactome; R-HSA-3322077; Glycogen synthesis.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-3785653; Myoclonic epilepsy of Lafora.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
DR Reactome; R-HSA-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
DR Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
DR Reactome; R-HSA-5655862; Translesion synthesis by POLK.
DR Reactome; R-HSA-5656121; Translesion synthesis by POLI.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689877; Josephin domain DUBs.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR Reactome; R-HSA-5689901; Metalloprotease DUBs.
DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
DR Reactome; R-HSA-6807004; Negative regulation of MET activity.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69541; Stabilization of p53.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
DR Reactome; R-HSA-8876493; InlA-mediated entry of Listeria monocytogenes into host cells.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948747; Regulation of PTEN localization.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-HSA-9013973; TICAM1-dependent activation of IRF3/IRF7.
DR Reactome; R-HSA-9014325; TICAM1,TRAF6-dependent induction of TAK1 complex.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR Reactome; R-HSA-912631; Regulation of signaling by CBL.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
DR Reactome; R-HSA-937039; IRAK1 recruits IKK complex.
DR Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
DR Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR Reactome; R-HSA-9636383; Prevention of phagosomal-lysosomal fusion.
DR Reactome; R-HSA-9637628; Modulation by Mtb of host immune system.
DR Reactome; R-HSA-9645460; Alpha-protein kinase 1 signaling pathway.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR Reactome; R-HSA-9648002; RAS processing.
DR Reactome; R-HSA-9664873; Pexophagy.
DR Reactome; R-HSA-9683683; Maturation of protein E.
DR Reactome; R-HSA-9694493; Maturation of protein E.
DR Reactome; R-HSA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-9706369; Negative regulation of FLT3.
DR Reactome; R-HSA-9706377; FLT3 signaling by CBL mutants.
DR Reactome; R-HSA-9708530; Regulation of BACH1 activity.
DR Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
DR Reactome; R-HSA-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P0CG48; -.
DR SIGNOR; P0CG48; -.
DR BioGRID-ORCS; 7316; 374 hits in 1078 CRISPR screens.
DR ChiTaRS; UBC; human.
DR EvolutionaryTrace; P0CG48; -.
DR GeneWiki; Ubiquitin_C; -.
DR GenomeRNAi; 7316; -.
DR Pharos; P0CG48; Tbio.
DR PRO; PR:P0CG48; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P0CG48; protein.
DR Bgee; ENSG00000150991; Expressed in olfactory bulb and 213 other tissues.
DR ExpressionAtlas; P0CG48; baseline and differential.
DR Genevisible; P0CG48; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 9.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 9.
DR SUPFAM; SSF54236; SSF54236; 9.
DR PROSITE; PS00299; UBIQUITIN_1; 9.
DR PROSITE; PS50053; UBIQUITIN_2; 9.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396178"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396179"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396180"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396181"
FT CHAIN 305..380
FT /note="Ubiquitin"
FT /id="PRO_0000396182"
FT CHAIN 381..456
FT /note="Ubiquitin"
FT /id="PRO_0000396183"
FT CHAIN 457..532
FT /note="Ubiquitin"
FT /id="PRO_0000396184"
FT CHAIN 533..608
FT /note="Ubiquitin"
FT /id="PRO_0000396185"
FT CHAIN 609..684
FT /note="Ubiquitin"
FT /id="PRO_0000396186"
FT PROPEP 685
FT /id="PRO_0000396187"
FT DOMAIN 1..76
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 77..152
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 153..228
FT /note="Ubiquitin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 229..304
FT /note="Ubiquitin-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 305..380
FT /note="Ubiquitin-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 381..456
FT /note="Ubiquitin-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 457..532
FT /note="Ubiquitin-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 533..608
FT /note="Ubiquitin-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 609..684
FT /note="Ubiquitin-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT SITE 54
FT /note="Interacts with activating enzyme"
FT SITE 68
FT /note="Essential for function"
FT SITE 72
FT /note="Interacts with activating enzyme"
FT MOD_RES 65
FT /note="Phosphoserine; by PINK1"
FT /evidence="ECO:0000269|PubMed:24660806,
FT ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582,
FT ECO:0000269|PubMed:25527291"
FT MOD_RES 76
FT /note="ADP-ribosylglycine"
FT /evidence="ECO:0000269|PubMed:28525742"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16443603"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16443603,
FT ECO:0000269|PubMed:16543144"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:15466860"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16543144,
FT ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577,
FT ECO:0000269|PubMed:34239127"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25752577"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16443603,
FT ECO:0000269|PubMed:16543144"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16543144,
FT ECO:0000269|PubMed:18719106"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT MUTAGEN 48
FT /note="K->R: No effect on HLTF-mediated polyubiquitination
FT of PCNA."
FT /evidence="ECO:0000269|PubMed:18719106"
FT MUTAGEN 63
FT /note="K->R: Abolishes HLTF-mediated polyubiquitination of
FT PCNA."
FT /evidence="ECO:0000269|PubMed:18719106"
FT MUTAGEN 65
FT /note="S->A: Prevents phosphorylation in case of mitophagy.
FT Decreased localization of PRKN to mitochondria."
FT /evidence="ECO:0000269|PubMed:24660806,
FT ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582"
FT MUTAGEN 65
FT /note="S->D: Phosphomimetic mutant that binds and activates
FT PRKN."
FT /evidence="ECO:0000269|PubMed:24751536"
FT MUTAGEN 65
FT /note="S->E: Phosphomimetic mutant that binds and activates
FT PRKN."
FT /evidence="ECO:0000269|PubMed:24751536"
FT MUTAGEN 68
FT /note="H->G: Loss of DTX3L-mediated polyubiquitination of
FT histone H3 and H4."
FT /evidence="ECO:0000269|PubMed:28525742"
FT MUTAGEN 72
FT /note="R->G: No effect on ADP-ribosylation."
FT /evidence="ECO:0000269|PubMed:28525742"
FT MUTAGEN 72
FT /note="R->K: No effect on ADP-ribosylation, when associated
FT with K-74."
FT /evidence="ECO:0000269|PubMed:28525742"
FT MUTAGEN 74
FT /note="R->G: No effect on ADP-ribosylation."
FT /evidence="ECO:0000269|PubMed:28525742"
FT MUTAGEN 74
FT /note="R->K: No effect on ADP-ribosylation, when associated
FT with K-72."
FT /evidence="ECO:0000269|PubMed:28525742"
FT MUTAGEN 76
FT /note="G->A: Loss of ADP-ribosylation."
FT /evidence="ECO:0000269|PubMed:28525742"
FT CONFLICT 190
FT /note="P -> S (in Ref. 4; AC126309)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="V -> G (in Ref. 6; BAA09860)"
FT /evidence="ECO:0000305"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:5B83"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:5B83"
FT HELIX 403..411
FT /evidence="ECO:0007829|PDB:5B83"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:5B83"
FT STRAND 421..425
FT /evidence="ECO:0007829|PDB:5B83"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:5B83"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:5B83"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:5B83"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:5H07"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:5H07"
FT HELIX 479..490
FT /evidence="ECO:0007829|PDB:5H07"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:5H07"
FT STRAND 497..501
FT /evidence="ECO:0007829|PDB:5H07"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:5H07"
FT STRAND 522..527
FT /evidence="ECO:0007829|PDB:5H07"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:7EB9"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:3B08"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:6N6R"
FT STRAND 544..548
FT /evidence="ECO:0007829|PDB:3B08"
FT HELIX 555..566
FT /evidence="ECO:0007829|PDB:3B08"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:3B08"
FT STRAND 573..577
FT /evidence="ECO:0007829|PDB:3B08"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:3N3K"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:6N6R"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:3B08"
FT STRAND 598..603
FT /evidence="ECO:0007829|PDB:3B08"
FT STRAND 610..615
FT /evidence="ECO:0007829|PDB:6Q00"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:4K1R"
FT STRAND 620..624
FT /evidence="ECO:0007829|PDB:6Q00"
FT STRAND 627..630
FT /evidence="ECO:0007829|PDB:1G6J"
FT HELIX 631..642
FT /evidence="ECO:0007829|PDB:6Q00"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:6Q00"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:6Q00"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:6TUV"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:3VUX"
FT HELIX 665..667
FT /evidence="ECO:0007829|PDB:6Q00"
FT TURN 668..670
FT /evidence="ECO:0007829|PDB:5OXH"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:6EQI"
FT STRAND 674..679
FT /evidence="ECO:0007829|PDB:6Q00"
FT STRAND 681..683
FT /evidence="ECO:0007829|PDB:6TUV"
SQ 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
