Full text data of UBC
UBC
[Confidence: low (only semi-automatic identification from reviews)]
Polyubiquitin-C; Ubiquitin; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Polyubiquitin-C; Ubiquitin; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P0CG48
ID UBC_HUMAN Reviewed; 685 AA.
AC P0CG48; P02248; P02249; P02250; P62988; Q29120; Q6LBL4; Q6LDU5;
read moreAC Q8WYN8; Q91887; Q91888; Q9BWD6; Q9BX98; Q9UEF2; Q9UEG1; Q9UEK8;
AC Q9UPK7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 22-JAN-2014, entry version 40.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2988935;
RA Wiborg O., Pedersen M.S., Wind A., Berglund L.E., Marcker K.A.,
RA Vuust J.;
RT "The human ubiquitin multigene family: some genes contain multiple
RT directly repeated ubiquitin coding sequences.";
RL EMBO J. 4:755-759(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9644242;
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
RT and 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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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
RT project: 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.,
RA Yamauchi M., Tsuji H.;
RT "Heterogeneous structure of the polyubiquitin gene UbC of HeLa S3
RT cells.";
RL Gene 175:179-185(1996).
RN [7]
RP PROTEIN SEQUENCE OF 1-74.
RX PubMed=124018; DOI=10.1038/255423a0;
RA Schlesinger D.H., Goldstein G.;
RT "Hybrid troponin reconstituted from vertebrate and arthropod
RT subunits.";
RL Nature 255:423-424(1975).
RN [8]
RP PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11
RP AND LYS-48, AND MASS SPECTROMETRY.
RX PubMed=16443603; DOI=10.1074/jbc.M512786200;
RA Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.;
RT "Alzheimer disease-specific conformation of hyperphosphorylated paired
RT helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and
RT Lys-6 ubiquitin conjugation.";
RL J. Biol. Chem. 281:10825-10838(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-685.
RX PubMed=9504932;
RA Nenoi M., Mita K., Ichimura S., Kawano A.;
RT "Higher frequency of concerted evolutionary events in rodents than in
RT man 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
RT human 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 MASS SPECTROMETRY.
RX PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018;
RA Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
RT "Differential regulation of EGF receptor internalization and
RT degradation by multiubiquitination within the kinase domain.";
RL Mol. Cell 21:737-748(2006).
RN [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 [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS
RP SPECTROMETRY.
RC TISSUE=Lung adenocarcinoma;
RX PubMed=17203973; DOI=10.1021/pr060438j;
RA Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,
RA Haines D.S., Figeys D.;
RT "The proteomic reactor facilitates the analysis of affinity-purified
RT proteins by mass spectrometry: application for identifying
RT ubiquitinated proteins in human cells.";
RL J. Proteome Res. 6:298-305(2007).
RN [15]
RP UBIQUITINATION AT LYS-63, AND MUTAGENESIS OF LYS-48 AND LYS-63.
RX PubMed=18719106; DOI=10.1073/pnas.0805685105;
RA Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X.,
RA Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
RT "Polyubiquitination of proliferating cell nuclear antigen by HLTF and
RT SHPRH prevents genomic instability from stalled replication forks.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
RN [16]
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 [17]
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 [18]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8166633;
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:
RT the total chemical synthesis of ubiquitin.";
RL Biochem. J. 299:151-158(1994).
RN [19]
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 [20]
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 [21]
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.,
RA Shi Y.;
RT "Crystal structure of a UBP-family deubiquitinating enzyme in
RT isolation and in complex with ubiquitin aldehyde.";
RL Cell 111:1041-1054(2002).
RN [22]
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.,
RA Komander D.;
RT "Polyubiquitin binding and cross-reactivity in the USP domain
RT deubiquitinase USP21.";
RL EMBO Rep. 12:350-357(2011).
RN [23]
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 [24]
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.,
RA Freund S.M., Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and
RT enable ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
CC -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC protein, or free (unanchored). When covalently bound, it is
CC conjugated to target proteins via an isopeptide bond either as a
CC monomer (monoubiquitin), a polymer linked via different Lys
CC residues of the ubiquitin (polyubiquitin chains) or a linear
CC polymer linked via the initiator Met of the ubiquitin (linear
CC polyubiquitin chains). Polyubiquitin chains, when attached to a
CC target protein, have different functions depending on the Lys
CC residue of the ubiquitin that is linked: Lys-6-linked may be
CC involved in DNA repair; Lys-11-linked is involved in ERAD
CC (endoplasmic reticulum-associated degradation) and in cell-cycle
CC regulation; Lys-29-linked is involved in lysosomal degradation;
CC Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC involved in protein degradation via the proteasome; Lys-63-linked
CC is involved in endocytosis, DNA-damage responses as well as in
CC signaling processes leading to activation of the transcription
CC factor NF-kappa-B. Linear polymer chains formed via attachment by
CC the initiator Met lead to cell signaling. Ubiquitin is usually
CC conjugated to Lys residues of target proteins, however, in rare
CC cases, conjugation to Cys or Ser residues has been observed. When
CC polyubiquitin is free (unanchored-polyubiquitin), it also has
CC distinct roles, such as in activation of protein kinases, and in
CC signaling.
CC -!- INTERACTION:
CC Q9UNQ0:ABCG2; NbExp=2; IntAct=EBI-3390054, EBI-1569435;
CC P25098:ADRBK1; NbExp=3; IntAct=EBI-3390054, EBI-3904795;
CC Q16186:ADRM1; NbExp=10; IntAct=EBI-3390054, EBI-954387;
CC Q9ULH1:ASAP1; NbExp=2; IntAct=EBI-3390054, EBI-346622;
CC O43150:ASAP2; NbExp=2; IntAct=EBI-3390054, EBI-310968;
CC P54252:ATXN3; NbExp=2; IntAct=EBI-3390054, EBI-946046;
CC Q9HB09-1:BCL2L12; NbExp=3; IntAct=EBI-3390054, EBI-6968951;
CC P35226:BMI1; NbExp=2; IntAct=EBI-3390054, EBI-2341576;
CC O60566:BUB1B; NbExp=3; IntAct=EBI-3390054, EBI-1001438;
CC P06493:CDK1; NbExp=6; IntAct=EBI-3390054, EBI-444308;
CC Q99062:CSF3R; NbExp=2; IntAct=EBI-3390054, EBI-7331284;
CC Q9UER7:DAXX; NbExp=2; IntAct=EBI-3390054, EBI-77321;
CC P40087:DDI1 (xeno); NbExp=2; IntAct=EBI-3390054, EBI-5717;
CC O43583:DENR; NbExp=3; IntAct=EBI-3390054, EBI-716083;
CC P48510:DSK2 (xeno); NbExp=2; IntAct=EBI-3390054, EBI-6174;
CC Q86Y01:DTX1; NbExp=2; IntAct=EBI-3390054, EBI-1755174;
CC Q15717:ELAVL1; NbExp=4; IntAct=EBI-3390054, EBI-374260;
CC Q61088:Fzd4 (xeno); NbExp=3; IntAct=EBI-3390054, EBI-7987880;
CC Q9Y6K9:IKBKG; NbExp=4; IntAct=EBI-3390054, EBI-81279;
CC O88522:Ikbkg (xeno); NbExp=3; IntAct=EBI-3390054, EBI-998011;
CC Q13887:KLF5; NbExp=2; IntAct=EBI-3390054, EBI-2696013;
CC P06239:LCK; NbExp=2; IntAct=EBI-3390054, EBI-1348;
CC P48357-3:LEPR; NbExp=2; IntAct=EBI-3390054, EBI-7886448;
CC Q9UDY8:MALT1; NbExp=4; IntAct=EBI-3390054, EBI-1047372;
CC Q9Y6R4:MAP3K4; NbExp=2; IntAct=EBI-3390054, EBI-448104;
CC O43318:MAP3K7; NbExp=4; IntAct=EBI-3390054, EBI-358684;
CC Q9NX47:MARCH5; NbExp=2; IntAct=EBI-3390054, EBI-2341610;
CC Q00987:MDM2; NbExp=6; IntAct=EBI-3390054, EBI-389668;
CC P01106:MYC; NbExp=5; IntAct=EBI-3390054, EBI-447544;
CC O43639:NCK2; NbExp=2; IntAct=EBI-3390054, EBI-713635;
CC Q14934:NFATC4; NbExp=3; IntAct=EBI-3390054, EBI-3905796;
CC P25963:NFKBIA; NbExp=3; IntAct=EBI-3390054, EBI-307386;
CC P09874:PARP1; NbExp=2; IntAct=EBI-3390054, EBI-355676;
CC P35227:PCGF2; NbExp=2; IntAct=EBI-3390054, EBI-2129767;
CC Q9Y253:POLH; NbExp=4; IntAct=EBI-3390054, EBI-2827270;
CC Q9UNA4:POLI; NbExp=4; IntAct=EBI-3390054, EBI-741774;
CC P17252:PRKCA; NbExp=2; IntAct=EBI-3390054, EBI-1383528;
CC P55036:PSMD4; NbExp=8; IntAct=EBI-3390054, EBI-359318;
CC P32628:RAD23 (xeno); NbExp=4; IntAct=EBI-3390054, EBI-14668;
CC P54727:RAD23B; NbExp=4; IntAct=EBI-3390054, EBI-954531;
CC Q84L31:RAD23C (xeno); NbExp=2; IntAct=EBI-3390054, EBI-4437395;
CC P61224:RAP1B; NbExp=2; IntAct=EBI-3390054, EBI-358143;
CC Q62921:Rbck1 (xeno); NbExp=2; IntAct=EBI-3390054, EBI-7266339;
CC Q96NR8:RDH12; NbExp=2; IntAct=EBI-3390054, EBI-3916363;
CC Q04206:RELA; NbExp=6; IntAct=EBI-3390054, EBI-73886;
CC P04325:rev (xeno); NbExp=2; IntAct=EBI-3390054, EBI-7061954;
CC P55034:RPN10 (xeno); NbExp=2; IntAct=EBI-3390054, EBI-2620423;
CC O48726:RPN13 (xeno); NbExp=9; IntAct=EBI-3390054, EBI-7710745;
CC Q8N488:RYBP; NbExp=3; IntAct=EBI-3390054, EBI-752324;
CC Q9H4L4:SENP3; NbExp=2; IntAct=EBI-3390054, EBI-2880236;
CC Q96B97:SH3KBP1; NbExp=6; IntAct=EBI-3390054, EBI-346595;
CC Q9Y5X1:SNX9; NbExp=2; IntAct=EBI-3390054, EBI-77848;
CC Q13501:SQSTM1; NbExp=3; IntAct=EBI-3390054, EBI-307104;
CC Q92783:STAM; NbExp=2; IntAct=EBI-3390054, EBI-752333;
CC Q86VP1:TAX1BP1; NbExp=5; IntAct=EBI-3390054, EBI-529518;
CC P04637:TP53; NbExp=15; IntAct=EBI-3390054, EBI-366083;
CC Q9Y4K3:TRAF6; NbExp=4; IntAct=EBI-3390054, EBI-359276;
CC Q9EPK8:Trpv4 (xeno); NbExp=3; IntAct=EBI-3390054, EBI-7091763;
CC Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-3390054, EBI-741480;
CC P98170:XIAP; NbExp=3; IntAct=EBI-3390054, EBI-517127;
CC O76080:ZFAND5; NbExp=3; IntAct=EBI-3390054, EBI-8028844;
CC Q9UGI0:ZRANB1; NbExp=2; IntAct=EBI-3390054, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm (By similarity).
CC Nucleus (By similarity).
CC -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. UBA52
CC and RPS27A genes code for a single copy of ubiquitin fused to the
CC ribosomal proteins L40 and S27a, respectively. UBB and UBC genes
CC code for a polyubiquitin precursor with exact head to tail
CC repeats, the number of repeats differ between species and strains.
CC -!- MISCELLANEOUS: For the sake of clarity sequence features are
CC annotated only for the first chain, and are not repeated for each
CC of the following chains.
CC -!- SIMILARITY: Belongs to the ubiquitin family.
CC -!- SIMILARITY: Contains 9 ubiquitin-like domains.
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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 PIR; A02574; UQHU.
DR PIR; A22005; UQHUC.
DR PIR; A29526; A29526.
DR UniGene; Hs.520348; -.
DR UniGene; Hs.707528; -.
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; 1ZO6; Model; -; B/C=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; 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; 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; 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; 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; 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; 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 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; 1ZO6; -.
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; 2NR2; -.
DR PDBsum; 2O6V; -.
DR PDBsum; 2OJR; -.
DR PDBsum; 2PE9; -.
DR PDBsum; 2PEA; -.
DR PDBsum; 2RR9; -.
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; 3ZLZ; -.
DR PDBsum; 3ZNH; -.
DR PDBsum; 3ZNI; -.
DR PDBsum; 3ZNZ; -.
DR PDBsum; 4AUQ; -.
DR PDBsum; 4BOS; -.
DR PDBsum; 4BOZ; -.
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; 4K7S; -.
DR PDBsum; 4K7U; -.
DR PDBsum; 4K7W; -.
DR PDBsum; 4KSK; -.
DR PDBsum; 4KSL; -.
DR PDBsum; 4LCD; -.
DR PDBsum; 4LDT; -.
DR ProteinModelPortal; P0CG48; -.
DR SMR; P0CG48; 1-683.
DR IntAct; P0CG48; 162.
DR MINT; MINT-97475; -.
DR PhosphoSite; P0CG48; -.
DR DMDM; 308153512; -.
DR PRIDE; P0CG48; -.
DR Ensembl; ENST00000339647; ENSP00000344818; ENSG00000150991.
DR Ensembl; ENST00000536769; ENSP00000441543; ENSG00000150991.
DR UCSC; uc001ugs.4; human.
DR GeneCards; GC12M125396; -.
DR HGNC; HGNC:12468; UBC.
DR HPA; CAB000362; -.
DR HPA; CAB005419; -.
DR HPA; HPA041344; -.
DR HPA; HPA049132; -.
DR MIM; 191340; gene.
DR neXtProt; NX_P0CG48; -.
DR OrthoDB; EOG7JDR1W; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115202; Signal Transduction.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_118324; Disease.
DR Reactome; REACT_118381; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_13487; Ubiquitination of PAK-2p34.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_2001; Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_216; DNA Repair.
DR Reactome; REACT_24941; Circadian Clock.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6782; TRAF6 Mediated Induction of proinflammatory cytokines.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR Reactome; REACT_8017; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; REACT_81380; Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
DR Reactome; REACT_97910; Signal Transduction.
DR ChiTaRS; UBC; human.
DR EvolutionaryTrace; P0CG48; -.
DR NextBio; 33412565; -.
DR PRO; PR:P0CG48; -.
DR ArrayExpress; P0CG48; -.
DR Bgee; P0CG48; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0006281; P:DNA repair; TAS:Reactome.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0060613; P:fat pad development; IEA:Ensembl.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR GO; GO:0007144; P:female meiosis I; IEA:Ensembl.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0021888; P:hypothalamus gonadotrophin-releasing hormone neuron development; IEA:Ensembl.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0007254; P:JNK cascade; TAS:Reactome.
DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0007220; P:Notch receptor processing; TAS:Reactome.
DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR GO; GO:0034166; P:toll-like receptor 10 signaling pathway; TAS:Reactome.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
DR GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
DR GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR GO; GO:0010992; P:ubiquitin homeostasis; IEA:Ensembl.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR InterPro; IPR019956; Ubiquitin.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR000626; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 9.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 9.
DR PROSITE; PS00299; UBIQUITIN_1; 9.
DR PROSITE; PS50053; UBIQUITIN_2; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Nucleus; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1 76 Ubiquitin.
FT /FTId=PRO_0000396178.
FT CHAIN 77 152 Ubiquitin.
FT /FTId=PRO_0000396179.
FT CHAIN 153 228 Ubiquitin.
FT /FTId=PRO_0000396180.
FT CHAIN 229 304 Ubiquitin.
FT /FTId=PRO_0000396181.
FT CHAIN 305 380 Ubiquitin.
FT /FTId=PRO_0000396182.
FT CHAIN 381 456 Ubiquitin.
FT /FTId=PRO_0000396183.
FT CHAIN 457 532 Ubiquitin.
FT /FTId=PRO_0000396184.
FT CHAIN 533 608 Ubiquitin.
FT /FTId=PRO_0000396185.
FT CHAIN 609 684 Ubiquitin.
FT /FTId=PRO_0000396186.
FT PROPEP 685 685
FT /FTId=PRO_0000396187.
FT DOMAIN 1 76 Ubiquitin-like 1.
FT DOMAIN 77 152 Ubiquitin-like 2.
FT DOMAIN 153 228 Ubiquitin-like 3.
FT DOMAIN 229 304 Ubiquitin-like 4.
FT DOMAIN 305 380 Ubiquitin-like 5.
FT DOMAIN 381 456 Ubiquitin-like 6.
FT DOMAIN 457 532 Ubiquitin-like 7.
FT DOMAIN 533 608 Ubiquitin-like 8.
FT DOMAIN 609 684 Ubiquitin-like 9.
FT BINDING 54 54 Activating enzyme.
FT BINDING 72 72 Activating enzyme.
FT SITE 68 68 Essential for function.
FT CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin)
FT (Probable).
FT CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin) (By
FT similarity).
FT CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys)
FT (interchain with K-? in acceptor
FT proteins).
FT MUTAGEN 48 48 K->R: No effect on HLTF-mediated
FT polyubiquitination of PCNA.
FT MUTAGEN 63 63 K->R: Abolishes HLTF-mediated
FT polyubiquitination of PCNA.
FT CONFLICT 190 190 P -> S (in Ref. 4; AC126309).
FT CONFLICT 397 397 V -> G (in Ref. 6; BAA09860).
FT STRAND 534 539
FT STRAND 540 542
FT STRAND 544 548
FT HELIX 555 565
FT STRAND 568 570
FT STRAND 573 577
FT STRAND 579 581
FT STRAND 586 588
FT HELIX 589 591
FT STRAND 598 603
FT STRAND 610 615
FT STRAND 616 618
FT STRAND 620 624
FT STRAND 627 630
FT HELIX 631 642
FT HELIX 646 648
FT STRAND 649 653
FT STRAND 654 657
FT STRAND 660 663
FT HELIX 664 667
FT STRAND 674 679
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
//
ID UBC_HUMAN Reviewed; 685 AA.
AC P0CG48; P02248; P02249; P02250; P62988; Q29120; Q6LBL4; Q6LDU5;
read moreAC Q8WYN8; Q91887; Q91888; Q9BWD6; Q9BX98; Q9UEF2; Q9UEG1; Q9UEK8;
AC Q9UPK7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 22-JAN-2014, entry version 40.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2988935;
RA Wiborg O., Pedersen M.S., Wind A., Berglund L.E., Marcker K.A.,
RA Vuust J.;
RT "The human ubiquitin multigene family: some genes contain multiple
RT directly repeated ubiquitin coding sequences.";
RL EMBO J. 4:755-759(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9644242;
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
RT and 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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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
RT project: 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.,
RA Yamauchi M., Tsuji H.;
RT "Heterogeneous structure of the polyubiquitin gene UbC of HeLa S3
RT cells.";
RL Gene 175:179-185(1996).
RN [7]
RP PROTEIN SEQUENCE OF 1-74.
RX PubMed=124018; DOI=10.1038/255423a0;
RA Schlesinger D.H., Goldstein G.;
RT "Hybrid troponin reconstituted from vertebrate and arthropod
RT subunits.";
RL Nature 255:423-424(1975).
RN [8]
RP PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11
RP AND LYS-48, AND MASS SPECTROMETRY.
RX PubMed=16443603; DOI=10.1074/jbc.M512786200;
RA Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.;
RT "Alzheimer disease-specific conformation of hyperphosphorylated paired
RT helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and
RT Lys-6 ubiquitin conjugation.";
RL J. Biol. Chem. 281:10825-10838(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-685.
RX PubMed=9504932;
RA Nenoi M., Mita K., Ichimura S., Kawano A.;
RT "Higher frequency of concerted evolutionary events in rodents than in
RT man 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
RT human 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 MASS SPECTROMETRY.
RX PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018;
RA Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
RT "Differential regulation of EGF receptor internalization and
RT degradation by multiubiquitination within the kinase domain.";
RL Mol. Cell 21:737-748(2006).
RN [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 [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS
RP SPECTROMETRY.
RC TISSUE=Lung adenocarcinoma;
RX PubMed=17203973; DOI=10.1021/pr060438j;
RA Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,
RA Haines D.S., Figeys D.;
RT "The proteomic reactor facilitates the analysis of affinity-purified
RT proteins by mass spectrometry: application for identifying
RT ubiquitinated proteins in human cells.";
RL J. Proteome Res. 6:298-305(2007).
RN [15]
RP UBIQUITINATION AT LYS-63, AND MUTAGENESIS OF LYS-48 AND LYS-63.
RX PubMed=18719106; DOI=10.1073/pnas.0805685105;
RA Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X.,
RA Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
RT "Polyubiquitination of proliferating cell nuclear antigen by HLTF and
RT SHPRH prevents genomic instability from stalled replication forks.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
RN [16]
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 [17]
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 [18]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8166633;
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:
RT the total chemical synthesis of ubiquitin.";
RL Biochem. J. 299:151-158(1994).
RN [19]
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 [20]
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 [21]
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.,
RA Shi Y.;
RT "Crystal structure of a UBP-family deubiquitinating enzyme in
RT isolation and in complex with ubiquitin aldehyde.";
RL Cell 111:1041-1054(2002).
RN [22]
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.,
RA Komander D.;
RT "Polyubiquitin binding and cross-reactivity in the USP domain
RT deubiquitinase USP21.";
RL EMBO Rep. 12:350-357(2011).
RN [23]
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 [24]
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.,
RA Freund S.M., Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and
RT enable ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
CC -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC protein, or free (unanchored). When covalently bound, it is
CC conjugated to target proteins via an isopeptide bond either as a
CC monomer (monoubiquitin), a polymer linked via different Lys
CC residues of the ubiquitin (polyubiquitin chains) or a linear
CC polymer linked via the initiator Met of the ubiquitin (linear
CC polyubiquitin chains). Polyubiquitin chains, when attached to a
CC target protein, have different functions depending on the Lys
CC residue of the ubiquitin that is linked: Lys-6-linked may be
CC involved in DNA repair; Lys-11-linked is involved in ERAD
CC (endoplasmic reticulum-associated degradation) and in cell-cycle
CC regulation; Lys-29-linked is involved in lysosomal degradation;
CC Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC involved in protein degradation via the proteasome; Lys-63-linked
CC is involved in endocytosis, DNA-damage responses as well as in
CC signaling processes leading to activation of the transcription
CC factor NF-kappa-B. Linear polymer chains formed via attachment by
CC the initiator Met lead to cell signaling. Ubiquitin is usually
CC conjugated to Lys residues of target proteins, however, in rare
CC cases, conjugation to Cys or Ser residues has been observed. When
CC polyubiquitin is free (unanchored-polyubiquitin), it also has
CC distinct roles, such as in activation of protein kinases, and in
CC signaling.
CC -!- INTERACTION:
CC Q9UNQ0:ABCG2; NbExp=2; IntAct=EBI-3390054, EBI-1569435;
CC P25098:ADRBK1; NbExp=3; IntAct=EBI-3390054, EBI-3904795;
CC Q16186:ADRM1; NbExp=10; IntAct=EBI-3390054, EBI-954387;
CC Q9ULH1:ASAP1; NbExp=2; IntAct=EBI-3390054, EBI-346622;
CC O43150:ASAP2; NbExp=2; IntAct=EBI-3390054, EBI-310968;
CC P54252:ATXN3; NbExp=2; IntAct=EBI-3390054, EBI-946046;
CC Q9HB09-1:BCL2L12; NbExp=3; IntAct=EBI-3390054, EBI-6968951;
CC P35226:BMI1; NbExp=2; IntAct=EBI-3390054, EBI-2341576;
CC O60566:BUB1B; NbExp=3; IntAct=EBI-3390054, EBI-1001438;
CC P06493:CDK1; NbExp=6; IntAct=EBI-3390054, EBI-444308;
CC Q99062:CSF3R; NbExp=2; IntAct=EBI-3390054, EBI-7331284;
CC Q9UER7:DAXX; NbExp=2; IntAct=EBI-3390054, EBI-77321;
CC P40087:DDI1 (xeno); NbExp=2; IntAct=EBI-3390054, EBI-5717;
CC O43583:DENR; NbExp=3; IntAct=EBI-3390054, EBI-716083;
CC P48510:DSK2 (xeno); NbExp=2; IntAct=EBI-3390054, EBI-6174;
CC Q86Y01:DTX1; NbExp=2; IntAct=EBI-3390054, EBI-1755174;
CC Q15717:ELAVL1; NbExp=4; IntAct=EBI-3390054, EBI-374260;
CC Q61088:Fzd4 (xeno); NbExp=3; IntAct=EBI-3390054, EBI-7987880;
CC Q9Y6K9:IKBKG; NbExp=4; IntAct=EBI-3390054, EBI-81279;
CC O88522:Ikbkg (xeno); NbExp=3; IntAct=EBI-3390054, EBI-998011;
CC Q13887:KLF5; NbExp=2; IntAct=EBI-3390054, EBI-2696013;
CC P06239:LCK; NbExp=2; IntAct=EBI-3390054, EBI-1348;
CC P48357-3:LEPR; NbExp=2; IntAct=EBI-3390054, EBI-7886448;
CC Q9UDY8:MALT1; NbExp=4; IntAct=EBI-3390054, EBI-1047372;
CC Q9Y6R4:MAP3K4; NbExp=2; IntAct=EBI-3390054, EBI-448104;
CC O43318:MAP3K7; NbExp=4; IntAct=EBI-3390054, EBI-358684;
CC Q9NX47:MARCH5; NbExp=2; IntAct=EBI-3390054, EBI-2341610;
CC Q00987:MDM2; NbExp=6; IntAct=EBI-3390054, EBI-389668;
CC P01106:MYC; NbExp=5; IntAct=EBI-3390054, EBI-447544;
CC O43639:NCK2; NbExp=2; IntAct=EBI-3390054, EBI-713635;
CC Q14934:NFATC4; NbExp=3; IntAct=EBI-3390054, EBI-3905796;
CC P25963:NFKBIA; NbExp=3; IntAct=EBI-3390054, EBI-307386;
CC P09874:PARP1; NbExp=2; IntAct=EBI-3390054, EBI-355676;
CC P35227:PCGF2; NbExp=2; IntAct=EBI-3390054, EBI-2129767;
CC Q9Y253:POLH; NbExp=4; IntAct=EBI-3390054, EBI-2827270;
CC Q9UNA4:POLI; NbExp=4; IntAct=EBI-3390054, EBI-741774;
CC P17252:PRKCA; NbExp=2; IntAct=EBI-3390054, EBI-1383528;
CC P55036:PSMD4; NbExp=8; IntAct=EBI-3390054, EBI-359318;
CC P32628:RAD23 (xeno); NbExp=4; IntAct=EBI-3390054, EBI-14668;
CC P54727:RAD23B; NbExp=4; IntAct=EBI-3390054, EBI-954531;
CC Q84L31:RAD23C (xeno); NbExp=2; IntAct=EBI-3390054, EBI-4437395;
CC P61224:RAP1B; NbExp=2; IntAct=EBI-3390054, EBI-358143;
CC Q62921:Rbck1 (xeno); NbExp=2; IntAct=EBI-3390054, EBI-7266339;
CC Q96NR8:RDH12; NbExp=2; IntAct=EBI-3390054, EBI-3916363;
CC Q04206:RELA; NbExp=6; IntAct=EBI-3390054, EBI-73886;
CC P04325:rev (xeno); NbExp=2; IntAct=EBI-3390054, EBI-7061954;
CC P55034:RPN10 (xeno); NbExp=2; IntAct=EBI-3390054, EBI-2620423;
CC O48726:RPN13 (xeno); NbExp=9; IntAct=EBI-3390054, EBI-7710745;
CC Q8N488:RYBP; NbExp=3; IntAct=EBI-3390054, EBI-752324;
CC Q9H4L4:SENP3; NbExp=2; IntAct=EBI-3390054, EBI-2880236;
CC Q96B97:SH3KBP1; NbExp=6; IntAct=EBI-3390054, EBI-346595;
CC Q9Y5X1:SNX9; NbExp=2; IntAct=EBI-3390054, EBI-77848;
CC Q13501:SQSTM1; NbExp=3; IntAct=EBI-3390054, EBI-307104;
CC Q92783:STAM; NbExp=2; IntAct=EBI-3390054, EBI-752333;
CC Q86VP1:TAX1BP1; NbExp=5; IntAct=EBI-3390054, EBI-529518;
CC P04637:TP53; NbExp=15; IntAct=EBI-3390054, EBI-366083;
CC Q9Y4K3:TRAF6; NbExp=4; IntAct=EBI-3390054, EBI-359276;
CC Q9EPK8:Trpv4 (xeno); NbExp=3; IntAct=EBI-3390054, EBI-7091763;
CC Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-3390054, EBI-741480;
CC P98170:XIAP; NbExp=3; IntAct=EBI-3390054, EBI-517127;
CC O76080:ZFAND5; NbExp=3; IntAct=EBI-3390054, EBI-8028844;
CC Q9UGI0:ZRANB1; NbExp=2; IntAct=EBI-3390054, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm (By similarity).
CC Nucleus (By similarity).
CC -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. UBA52
CC and RPS27A genes code for a single copy of ubiquitin fused to the
CC ribosomal proteins L40 and S27a, respectively. UBB and UBC genes
CC code for a polyubiquitin precursor with exact head to tail
CC repeats, the number of repeats differ between species and strains.
CC -!- MISCELLANEOUS: For the sake of clarity sequence features are
CC annotated only for the first chain, and are not repeated for each
CC of the following chains.
CC -!- SIMILARITY: Belongs to the ubiquitin family.
CC -!- SIMILARITY: Contains 9 ubiquitin-like domains.
CC -----------------------------------------------------------------------
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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 PIR; A02574; UQHU.
DR PIR; A22005; UQHUC.
DR PIR; A29526; A29526.
DR UniGene; Hs.520348; -.
DR UniGene; Hs.707528; -.
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; 1ZO6; Model; -; B/C=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; 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; 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; 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; 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; 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; 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 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; 1ZO6; -.
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; 2NR2; -.
DR PDBsum; 2O6V; -.
DR PDBsum; 2OJR; -.
DR PDBsum; 2PE9; -.
DR PDBsum; 2PEA; -.
DR PDBsum; 2RR9; -.
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; 3ZLZ; -.
DR PDBsum; 3ZNH; -.
DR PDBsum; 3ZNI; -.
DR PDBsum; 3ZNZ; -.
DR PDBsum; 4AUQ; -.
DR PDBsum; 4BOS; -.
DR PDBsum; 4BOZ; -.
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; 4K7S; -.
DR PDBsum; 4K7U; -.
DR PDBsum; 4K7W; -.
DR PDBsum; 4KSK; -.
DR PDBsum; 4KSL; -.
DR PDBsum; 4LCD; -.
DR PDBsum; 4LDT; -.
DR ProteinModelPortal; P0CG48; -.
DR SMR; P0CG48; 1-683.
DR IntAct; P0CG48; 162.
DR MINT; MINT-97475; -.
DR PhosphoSite; P0CG48; -.
DR DMDM; 308153512; -.
DR PRIDE; P0CG48; -.
DR Ensembl; ENST00000339647; ENSP00000344818; ENSG00000150991.
DR Ensembl; ENST00000536769; ENSP00000441543; ENSG00000150991.
DR UCSC; uc001ugs.4; human.
DR GeneCards; GC12M125396; -.
DR HGNC; HGNC:12468; UBC.
DR HPA; CAB000362; -.
DR HPA; CAB005419; -.
DR HPA; HPA041344; -.
DR HPA; HPA049132; -.
DR MIM; 191340; gene.
DR neXtProt; NX_P0CG48; -.
DR OrthoDB; EOG7JDR1W; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115202; Signal Transduction.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_118324; Disease.
DR Reactome; REACT_118381; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_13487; Ubiquitination of PAK-2p34.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_2001; Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_216; DNA Repair.
DR Reactome; REACT_24941; Circadian Clock.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6782; TRAF6 Mediated Induction of proinflammatory cytokines.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR Reactome; REACT_8017; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; REACT_81380; Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
DR Reactome; REACT_97910; Signal Transduction.
DR ChiTaRS; UBC; human.
DR EvolutionaryTrace; P0CG48; -.
DR NextBio; 33412565; -.
DR PRO; PR:P0CG48; -.
DR ArrayExpress; P0CG48; -.
DR Bgee; P0CG48; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0006281; P:DNA repair; TAS:Reactome.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0060613; P:fat pad development; IEA:Ensembl.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR GO; GO:0007144; P:female meiosis I; IEA:Ensembl.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0021888; P:hypothalamus gonadotrophin-releasing hormone neuron development; IEA:Ensembl.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0007254; P:JNK cascade; TAS:Reactome.
DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0007220; P:Notch receptor processing; TAS:Reactome.
DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR GO; GO:0034166; P:toll-like receptor 10 signaling pathway; TAS:Reactome.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
DR GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
DR GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR GO; GO:0010992; P:ubiquitin homeostasis; IEA:Ensembl.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR InterPro; IPR019956; Ubiquitin.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR000626; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 9.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 9.
DR PROSITE; PS00299; UBIQUITIN_1; 9.
DR PROSITE; PS50053; UBIQUITIN_2; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Nucleus; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1 76 Ubiquitin.
FT /FTId=PRO_0000396178.
FT CHAIN 77 152 Ubiquitin.
FT /FTId=PRO_0000396179.
FT CHAIN 153 228 Ubiquitin.
FT /FTId=PRO_0000396180.
FT CHAIN 229 304 Ubiquitin.
FT /FTId=PRO_0000396181.
FT CHAIN 305 380 Ubiquitin.
FT /FTId=PRO_0000396182.
FT CHAIN 381 456 Ubiquitin.
FT /FTId=PRO_0000396183.
FT CHAIN 457 532 Ubiquitin.
FT /FTId=PRO_0000396184.
FT CHAIN 533 608 Ubiquitin.
FT /FTId=PRO_0000396185.
FT CHAIN 609 684 Ubiquitin.
FT /FTId=PRO_0000396186.
FT PROPEP 685 685
FT /FTId=PRO_0000396187.
FT DOMAIN 1 76 Ubiquitin-like 1.
FT DOMAIN 77 152 Ubiquitin-like 2.
FT DOMAIN 153 228 Ubiquitin-like 3.
FT DOMAIN 229 304 Ubiquitin-like 4.
FT DOMAIN 305 380 Ubiquitin-like 5.
FT DOMAIN 381 456 Ubiquitin-like 6.
FT DOMAIN 457 532 Ubiquitin-like 7.
FT DOMAIN 533 608 Ubiquitin-like 8.
FT DOMAIN 609 684 Ubiquitin-like 9.
FT BINDING 54 54 Activating enzyme.
FT BINDING 72 72 Activating enzyme.
FT SITE 68 68 Essential for function.
FT CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin)
FT (Probable).
FT CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin) (By
FT similarity).
FT CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys)
FT (interchain with K-? in acceptor
FT proteins).
FT MUTAGEN 48 48 K->R: No effect on HLTF-mediated
FT polyubiquitination of PCNA.
FT MUTAGEN 63 63 K->R: Abolishes HLTF-mediated
FT polyubiquitination of PCNA.
FT CONFLICT 190 190 P -> S (in Ref. 4; AC126309).
FT CONFLICT 397 397 V -> G (in Ref. 6; BAA09860).
FT STRAND 534 539
FT STRAND 540 542
FT STRAND 544 548
FT HELIX 555 565
FT STRAND 568 570
FT STRAND 573 577
FT STRAND 579 581
FT STRAND 586 588
FT HELIX 589 591
FT STRAND 598 603
FT STRAND 610 615
FT STRAND 616 618
FT STRAND 620 624
FT STRAND 627 630
FT HELIX 631 642
FT HELIX 646 648
FT STRAND 649 653
FT STRAND 654 657
FT STRAND 660 663
FT HELIX 664 667
FT STRAND 674 679
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
//
MIM
191340
*RECORD*
*FIELD* NO
191340
*FIELD* TI
*191340 UBIQUITIN C; UBC
;;POLYUBIQUITIN
*FIELD* TX
DESCRIPTION
Studies of ubiquitin cDNAs and genes show 2 unusual gene structural
read morearrangements (Schlesinger and Bond, 1987). The first type of arrangement
is the polyubiquitin gene, consisting of tandem repeats of a ubiquitin
coding unit, with the number of repeats varying considerably even within
species. Presumably posttranslational cleavage produces ubiquitin
monomers from the primary translation product. The second structural
type is the ubiquitin fusion gene, which encodes a single ubiquitin
moiety fused to an unrelated tail protein. Three types of ubiquitin have
been identified: A, B (191339), and C. The ubiquitin C (UBC) mRNA
corresponds to a 9-coding-unit polyubiquitin gene.
MAPPING
During Northern blot analysis of ubiquitin mRNA, Baker and Board (1989)
observed a UBC mRNA length polymorphism. They characterized this 'mRLP',
showed that it correlated precisely with an HaeIII RFLP, and explained
the origin of the polymorphism on the basis of unequal crossover events.
Using a 5-prime flanking fragment to probe Southern blots of DNA
obtained from somatic cell hybrid cell lines, Board et al. (1992)
determined that the UBC gene is located on chromosome 12. In situ
hybridization with the same probe refined the assignment to 12q24.3.
*FIELD* RF
1. Baker, R. T.; Board, P. G.: Unequal crossover generates variation
in ubiquitin coding unit number at the human UbC polyubiquitin locus. Am.
J. Hum. Genet. 44: 534-542, 1989.
2. Board, P. G.; Coggan, M.; Baker, R. T.; Vuust, J.; Webb, G. C.
: Localization of the human UBC polyubiquitin gene to chromosome band
12q24.3. Genomics 12: 639-642, 1992.
3. Schlesinger, M. J.; Bond, U.: Ubiquitin genes. Oxf. Surv. Euk.
Genes 4: 77-91, 1987.
*FIELD* CD
Victor A. McKusick: 4/7/1989
*FIELD* ED
terry: 09/08/2010
carol: 5/12/2004
mark: 2/20/1997
carol: 3/30/1992
supermim: 3/16/1992
carol: 1/21/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 5/8/1989
*RECORD*
*FIELD* NO
191340
*FIELD* TI
*191340 UBIQUITIN C; UBC
;;POLYUBIQUITIN
*FIELD* TX
DESCRIPTION
Studies of ubiquitin cDNAs and genes show 2 unusual gene structural
read morearrangements (Schlesinger and Bond, 1987). The first type of arrangement
is the polyubiquitin gene, consisting of tandem repeats of a ubiquitin
coding unit, with the number of repeats varying considerably even within
species. Presumably posttranslational cleavage produces ubiquitin
monomers from the primary translation product. The second structural
type is the ubiquitin fusion gene, which encodes a single ubiquitin
moiety fused to an unrelated tail protein. Three types of ubiquitin have
been identified: A, B (191339), and C. The ubiquitin C (UBC) mRNA
corresponds to a 9-coding-unit polyubiquitin gene.
MAPPING
During Northern blot analysis of ubiquitin mRNA, Baker and Board (1989)
observed a UBC mRNA length polymorphism. They characterized this 'mRLP',
showed that it correlated precisely with an HaeIII RFLP, and explained
the origin of the polymorphism on the basis of unequal crossover events.
Using a 5-prime flanking fragment to probe Southern blots of DNA
obtained from somatic cell hybrid cell lines, Board et al. (1992)
determined that the UBC gene is located on chromosome 12. In situ
hybridization with the same probe refined the assignment to 12q24.3.
*FIELD* RF
1. Baker, R. T.; Board, P. G.: Unequal crossover generates variation
in ubiquitin coding unit number at the human UbC polyubiquitin locus. Am.
J. Hum. Genet. 44: 534-542, 1989.
2. Board, P. G.; Coggan, M.; Baker, R. T.; Vuust, J.; Webb, G. C.
: Localization of the human UBC polyubiquitin gene to chromosome band
12q24.3. Genomics 12: 639-642, 1992.
3. Schlesinger, M. J.; Bond, U.: Ubiquitin genes. Oxf. Surv. Euk.
Genes 4: 77-91, 1987.
*FIELD* CD
Victor A. McKusick: 4/7/1989
*FIELD* ED
terry: 09/08/2010
carol: 5/12/2004
mark: 2/20/1997
carol: 3/30/1992
supermim: 3/16/1992
carol: 1/21/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 5/8/1989