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P0CG48 (UBC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyubiquitin-C

Cleaved into the following chain:

  1. Ubiquitin
Gene names
Name:UBC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length685 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. Ref.12 Ref.16

Subcellular location

Ubiquitin: Cytoplasm By similarity. Nucleus By similarity.

Miscellaneous

Ubiquitin is encoded by 4 different genes. UBA52 and RPS27A genes code for a single copy of ubiquitin fused to the ribosomal proteins L40 and S27a, respectively. UBB and UBC genes code for a polyubiquitin precursor with exact head to tail repeats, the number of repeats differ between species and strains.

For the sake of clarity sequence features are annotated only for the first chain, and are not repeated for each of the following chains.

Sequence similarities

Belongs to the ubiquitin family.

Contains 9 ubiquitin-like domains.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   PTMIsopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Traceable author statement. Source: Reactome

DNA repair

Traceable author statement. Source: Reactome

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

I-kappaB kinase/NF-kappaB signaling

Traceable author statement. Source: Reactome

JNK cascade

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

Notch receptor processing

Traceable author statement. Source: Reactome

Notch signaling pathway

Traceable author statement. Source: Reactome

RNA metabolic process

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of MAPK activity

Traceable author statement. Source: Reactome

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

apoptotic signaling pathway

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular response to hypoxia

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

endosomal transport

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

glycogen biosynthetic process

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

intracellular transport of virus

Traceable author statement. Source: Reactome

ion transmembrane transport

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

negative regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of type I interferon production

Traceable author statement. Source: Reactome

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

nucleotide-binding oligomerization domain containing signaling pathway

Traceable author statement. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Traceable author statement. Source: Reactome

positive regulation of NF-kappaB transcription factor activity

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein polyubiquitination

Traceable author statement. Source: Reactome

regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of transcription from RNA polymerase II promoter in response to hypoxia

Traceable author statement. Source: Reactome

regulation of type I interferon production

Traceable author statement. Source: Reactome

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral protein processing

Traceable author statement. Source: Reactome

virion assembly

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

endosome membrane

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protease binding

Inferred from physical interaction PubMed 21185309. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 22795130. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABCG2Q9UNQ02EBI-3390054,EBI-1569435
ADRBK1P250983EBI-3390054,EBI-3904795
ADRM1Q1618610EBI-3390054,EBI-954387
ASAP1Q9ULH12EBI-3390054,EBI-346622
ASAP2O431502EBI-3390054,EBI-310968
ATXN3P542522EBI-3390054,EBI-946046
BCL2L12Q9HB09-13EBI-3390054,EBI-6968951
BMI1P352262EBI-3390054,EBI-2341576
BUB1BO605663EBI-3390054,EBI-1001438
CDK1P064936EBI-3390054,EBI-444308
CSF3RQ990622EBI-3390054,EBI-7331284
DAXXQ9UER72EBI-3390054,EBI-77321
DDI1P400872EBI-3390054,EBI-5717From a different organism.
DENRO435833EBI-3390054,EBI-716083
DSK2P485102EBI-3390054,EBI-6174From a different organism.
DTX1Q86Y012EBI-3390054,EBI-1755174
ELAVL1Q157174EBI-3390054,EBI-374260
Fzd4Q610883EBI-3390054,EBI-7987880From a different organism.
IKBKGQ9Y6K94EBI-3390054,EBI-81279
IkbkgO885223EBI-3390054,EBI-998011From a different organism.
KLF5Q138872EBI-3390054,EBI-2696013
LCKP062392EBI-3390054,EBI-1348
LEPRP48357-32EBI-3390054,EBI-7886448
MALT1Q9UDY84EBI-3390054,EBI-1047372
MAP3K4Q9Y6R42EBI-3390054,EBI-448104
MAP3K7O433184EBI-3390054,EBI-358684
MARCH5Q9NX472EBI-3390054,EBI-2341610
MDM2Q009876EBI-3390054,EBI-389668
MYCP011065EBI-3390054,EBI-447544
NCK2O436392EBI-3390054,EBI-713635
NFATC4Q149343EBI-3390054,EBI-3905796
NFKBIAP259633EBI-3390054,EBI-307386
PARP1P098742EBI-3390054,EBI-355676
PCGF2P352272EBI-3390054,EBI-2129767
POLHQ9Y2534EBI-3390054,EBI-2827270
POLIQ9UNA44EBI-3390054,EBI-741774
PRKCAP172522EBI-3390054,EBI-1383528
PSMD4P550368EBI-3390054,EBI-359318
RAD23P326284EBI-3390054,EBI-14668From a different organism.
RAD23BP547274EBI-3390054,EBI-954531
RAD23CQ84L312EBI-3390054,EBI-4437395From a different organism.
RAP1BP612242EBI-3390054,EBI-358143
Rbck1Q629212EBI-3390054,EBI-7266339From a different organism.
RDH12Q96NR82EBI-3390054,EBI-3916363
RELAQ042066EBI-3390054,EBI-73886
revP043252EBI-3390054,EBI-7061954From a different organism.
RPN10P550342EBI-3390054,EBI-2620423From a different organism.
RPN13O487269EBI-3390054,EBI-7710745From a different organism.
RYBPQ8N4883EBI-3390054,EBI-752324
SENP3Q9H4L42EBI-3390054,EBI-2880236
SH3KBP1Q96B976EBI-3390054,EBI-346595
SNX9Q9Y5X12EBI-3390054,EBI-77848
SQSTM1Q135013EBI-3390054,EBI-307104
STAMQ927832EBI-3390054,EBI-752333
TAX1BP1Q86VP15EBI-3390054,EBI-529518
TP53P0463715EBI-3390054,EBI-366083
TRAF6Q9Y4K34EBI-3390054,EBI-359276
Trpv4Q9EPK83EBI-3390054,EBI-7091763From a different organism.
UBQLN1Q9UMX03EBI-3390054,EBI-741480
XIAPP981703EBI-3390054,EBI-517127
ZFAND5O760803EBI-3390054,EBI-8028844
ZRANB1Q9UGI02EBI-3390054,EBI-527853

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7676Ubiquitin
PRO_0000396178
Chain77 – 15276Ubiquitin
PRO_0000396179
Chain153 – 22876Ubiquitin
PRO_0000396180
Chain229 – 30476Ubiquitin
PRO_0000396181
Chain305 – 38076Ubiquitin
PRO_0000396182
Chain381 – 45676Ubiquitin
PRO_0000396183
Chain457 – 53276Ubiquitin
PRO_0000396184
Chain533 – 60876Ubiquitin
PRO_0000396185
Chain609 – 68476Ubiquitin
PRO_0000396186
Propeptide6851
PRO_0000396187

Regions

Domain1 – 7676Ubiquitin-like 1
Domain77 – 15276Ubiquitin-like 2
Domain153 – 22876Ubiquitin-like 3
Domain229 – 30476Ubiquitin-like 4
Domain305 – 38076Ubiquitin-like 5
Domain381 – 45676Ubiquitin-like 6
Domain457 – 53276Ubiquitin-like 7
Domain533 – 60876Ubiquitin-like 8
Domain609 – 68476Ubiquitin-like 9

Sites

Binding site541Activating enzyme
Binding site721Activating enzyme
Site681Essential for function

Amino acid modifications

Cross-link6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9 Ref.12
Cross-link27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable
Cross-link29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12
Cross-link33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9 Ref.12 Ref.14
Cross-link63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12 Ref.15
Cross-link76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Experimental info

Mutagenesis481K → R: No effect on HLTF-mediated polyubiquitination of PCNA. Ref.15
Mutagenesis631K → R: Abolishes HLTF-mediated polyubiquitination of PCNA. Ref.15
Sequence conflict1901P → S in AC126309. Ref.4
Sequence conflict3971V → G in BAA09860. Ref.6

Secondary structure

.................................... 685
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0CG48 [UniParc].

Last modified June 13, 2012. Version 3.
Checksum: B6E7BC06FEE77196

FASTA68577,039
        10         20         30         40         50         60 
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 

        70         80         90        100        110        120 
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI 

       130        140        150        160        170        180 
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE PSDTIENVKA 

       190        200        210        220        230        240 
KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT 

       250        260        270        280        290        300 
ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR 

       310        320        330        340        350        360 
LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL 

       370        380        390        400        410        420 
SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ 

       430        440        450        460        470        480 
QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE 

       490        500        510        520        530        540 
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL 

       550        560        570        580        590        600 
TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH 

       610        620        630        640        650        660 
LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED 

       670        680 
GRTLSDYNIQ KESTLHLVLR LRGGV 

« Hide

References

« Hide 'large scale' references
[1]"The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences."
Wiborg O., Pedersen M.S., Wind A., Berglund L.E., Marcker K.A., Vuust J.
EMBO J. 4:755-759(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human polyubiquitin cDNAs and a ubiquitin-binding assay involving its in vitro translation product."
Kim N.S., Yamaguchi T., Sekine S., Saeki M., Iwamuro S., Kato S.
J. Biochem. 124:35-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Lineage-specific homogenization of the polyubiquitin gene among human and great apes."
Tachikui H., Saitou N., Nakajima T., Hayasaka I., Ishida T., Inoue I.
J. Mol. Evol. 57:737-744(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Liver, Lung and Placenta.
[6]"Heterogeneous structure of the polyubiquitin gene UbC of HeLa S3 cells."
Nenoi M., Mita K., Ichimura S., Cartwright I.L., Takahashi E., Yamauchi M., Tsuji H.
Gene 175:179-185(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-611.
[7]"Molecular conservation of 74 amino acid sequence of ubiquitin between cattle and man."
Schlesinger D.H., Goldstein G.
Nature 255:423-424(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-74.
[8]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[9]"Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation."
Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.
J. Biol. Chem. 281:10825-10838(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11 AND LYS-48, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Higher frequency of concerted evolutionary events in rodents than in man at the polyubiquitin gene VNTR locus."
Nenoi M., Mita K., Ichimura S., Kawano A.
Genetics 148:867-876(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-685.
[11]"Cloning and sequence analysis of a cDNA encoding poly-ubiquitin in human ovarian granulosa cells."
Einspanier R., Sharma H.S., Scheit K.H.
Biochem. Biophys. Res. Commun. 147:581-587(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 417-685.
[12]"Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain."
Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.
Mol. Cell 21:737-748(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis."
Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.
J. Biol. Chem. 279:53533-53543(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-27.
[14]"The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48.
Tissue: Lung adenocarcinoma.
[15]"Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks."
Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.
Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-63, MUTAGENESIS OF LYS-48 AND LYS-63.
[16]"The emerging complexity of protein ubiquitination."
Komander D.
Biochem. Soc. Trans. 37:937-953(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, FUNCTION.
[17]"Structure of ubiquitin refined at 1.8-A resolution."
Vijay-Kumar S., Bugg C.E., Cook W.J.
J. Mol. Biol. 194:531-544(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[18]"Synthetic, structural and biological studies of the ubiquitin system: the total chemical synthesis of ubiquitin."
Ramage R., Green J., Muir T.W., Ogunjobi O.M., Love S., Shaw K.
Biochem. J. 299:151-158(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[19]"Structure of tetraubiquitin shows how multiubiquitin chains can be formed."
Cook W.J., Jeffrey L.C., Kasperek E., Pickart C.M.
J. Mol. Biol. 236:601-609(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[20]"Structure of a new crystal form of tetraubiquitin."
Phillips C.L., Thrower J., Pickart C.M., Hill C.P.
Acta Crystallogr. D 57:341-344(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[21]"Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde."
Hu M., Li P., Li M., Li W., Yao T., Wu J.-W., Gu W., Cohen R.E., Shi Y.
Cell 111:1041-1054(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP7.
[22]"Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21."
Ye Y., Akutsu M., Reyes-Turcu F., Enchev R.I., Wilkinson K.D., Komander D.
EMBO Rep. 12:350-357(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP21.
[23]"Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne."
Bremm A., Freund S.M., Komander D.
Nat. Struct. Mol. Biol. 17:939-947(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-76.
[24]"OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.03 ANGSTROMS) OF 1-76 IN COMPLEX WITH YOD1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26880 mRNA. Translation: AAA36789.1.
AB009010 mRNA. Translation: BAA23632.1.
AB089613 Genomic DNA. Translation: BAC56951.1.
AC126309 Genomic DNA. No translation available.
BC039193 mRNA. Translation: AAH39193.1.
D63791 Genomic DNA. Translation: BAA09860.1.
AB003730 Genomic DNA. Translation: BAA23486.1.
M17597 mRNA. Translation: AAA36787.1.
PIRUQHU. A02574.
UQHUC. A22005.
A29526.
RefSeqNP_066289.3. NM_021009.6.
UniGeneHs.520348.
Hs.707528.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3TNMR-A1-76[»]
1CMXX-ray2.25B/D1-76[»]
1D3ZNMR-A1-76[»]
1F9JX-ray2.70A/B1-76[»]
1FXTNMR-B1-76[»]
1G6JNMR-A1-76[»]
1GJZNMR-A/B1-51[»]
1NBFX-ray2.30C/D1-76[»]
1OGWX-ray1.32A1-76[»]
1Q5WNMR-B1-76[»]
1S1QX-ray2.00B/D1-76[»]
1SIFX-ray2.18A6-76[»]
1TBEX-ray2.40A/B1-76[»]
1UBIX-ray1.80A1-76[»]
1UBQX-ray1.80A1-76[»]
1UD7NMR-A1-76[»]
1XD3X-ray1.45B/D1-75[»]
1XQQNMR-A1-76[»]
1YX5NMR-B1-76[»]
1YX6NMR-B1-76[»]
1ZGUNMR-B1-76[»]
1ZO6model-B/C1-76[»]
2AYOX-ray3.50B1-76[»]
2BGFNMR-A/B1-76[»]
2DENNMR-B1-76[»]
2FUHNMR-B1-76[»]
2G45X-ray1.99B/E1-76[»]
2GBJX-ray1.35A/B1-76[»]
2GBKX-ray1.99A/B/C/D10-76[»]
2GBMX-ray1.55A/B/C/D1-76[»]
2GBNX-ray1.60A1-76[»]
2GBRX-ray2.00A/B/C1-76[»]
2GMIX-ray2.50C1-76[»]
2HTHX-ray2.70A1-76[»]
2IBIX-ray2.20B1-75[»]
2J7QX-ray1.80B/D1-75[»]
2JF5X-ray1.95A/B1-76[»]
2JRINMR-B/C1-76[»]
2JY6NMR-A1-76[»]
2JZZNMR-A1-76[»]
2K25NMR-A1-75[»]
2K6DNMR-B1-75[»]
2K8BNMR-A1-76[»]
2K8CNMR-A1-76[»]
2KDFNMR-B/C1-76[»]
2KHWNMR-B1-76[»]
2KJHNMR-B1-75[»]
2KLGNMR-A1-76[»]
2KN5NMR-A1-76[»]
2KX0NMR-A74-151[»]
2L3ZNMR-A1-76[»]
2LD9NMR-A76-152[»]
2LVONMR-A1-76[»]
2LVPNMR-A/B1-76[»]
2LVQNMR-A/B1-76[»]
2LZ6NMR-A609-684[»]
2MBONMR-A/B609-684[»]
2MBQNMR-A/B609-684[»]
2MCNNMR-B609-684[»]
2MI8NMR-A609-684[»]
2MJ5NMR-A609-684[»]
2NR2NMR-A1-76[»]
2O6VX-ray2.20A/B/C/D/E/F/G/H1-76[»]
2OJRX-ray2.60A1-76[»]
2PE9NMR-A/B1-76[»]
2PEANMR-A/B1-76[»]
2RR9NMR-A/B1-76[»]
2RU6NMR-A609-684[»]
2W9NX-ray2.25A1-152[»]
2WDTX-ray2.30B/D1-75[»]
2XEWX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-76[»]
2Y5BX-ray2.70B/F1-152[»]
2Z59NMR-B1-76[»]
2ZCBX-ray1.60A/B/C1-76[»]
2ZVNX-ray3.00A/C/E/G1-152[»]
2ZVOX-ray2.90A/G1-152[»]
3A33X-ray2.20B1-76[»]
3ALBX-ray1.85A/B/C/D1-76[»]
3AULX-ray2.39A/B1-76[»]
3B08X-ray1.70A/D/G/J1-152[»]
3B0AX-ray1.90A/D1-152[»]
3BY4X-ray1.55B1-75[»]
3C0RX-ray2.31B/D1-75[»]
3DVGX-ray2.60X/Y1-76[»]
3DVNX-ray2.70U/V/X/Y1-76[»]
3EECX-ray3.00A/B1-76[»]
3EFUX-ray1.84A1-76[»]
3EHVX-ray1.81A/B/C1-76[»]
3H7PX-ray1.90A/B1-76[»]
3H7SX-ray2.30A/B1-76[»]
3HM3X-ray1.96A/B/C/D1-76[»]
3I3TX-ray2.59B/D/F/H1-75[»]
3IFWX-ray2.40B1-75[»]
3IHPX-ray2.80C/D1-75[»]
3JSVX-ray2.70A/B1-76[»]
3JVZX-ray3.30X/Y1-76[»]
3JW0X-ray3.10X/Y1-76[»]
3K9OX-ray1.80B76-151[»]
3K9PX-ray2.80B1-76[»]
3KVFX-ray2.80B1-75[»]
3KW5X-ray2.83B1-75[»]
3LDZX-ray2.60E/F/G1-73[»]
3MHSX-ray1.89D1-76[»]
3MTNX-ray2.70B/D1-76[»]
3N30X-ray3.00A/B1-76[»]
3N32X-ray1.80A1-76[»]
3N3KX-ray2.60B5-76[»]
3NS8X-ray1.71A/B1-76[»]
3O65X-ray2.70B/D/F/H1-75[»]
3OFIX-ray2.35C/D1-76[»]
3OJ3X-ray2.50A/B/C/D/E/F/G/H1-76[»]
3OJ4X-ray3.40B/E1-76[»]
3ONSX-ray1.80A1-72[»]
3PRMX-ray2.30B/D1-75[»]
3PT2X-ray2.50B1-75[»]
3PTFX-ray2.70C/D1-76[»]
3Q3FX-ray2.17A2-76[»]
3RULX-ray2.50A/B/C/D1-75[»]
3TMPX-ray1.91B/D/F/H1-76[»]
3U30X-ray2.43A/D1-152[»]
3UGBX-ray2.35B1-76[»]
3V6CX-ray1.70B74-150[»]
3V6EX-ray2.10B74-150[»]
3VFKX-ray2.80A1-75[»]
3VUWX-ray1.95A/B/C1-76[»]
3VUXX-ray1.70A/B/C1-76[»]
3VUYX-ray1.98A/B/C1-76[»]
3ZLZX-ray2.90A/B1-76[»]
3ZNHX-ray2.30B1-75[»]
3ZNIX-ray2.21D/H/L/P1-76[»]
3ZNZX-ray1.90B1-152[»]
4AUQX-ray2.18C/F1-76[»]
4BOSX-ray2.35C/E609-684[»]
F612-625[»]
4BOZX-ray3.03B/C/E1-76[»]
4BVUX-ray2.70C609-684[»]
4DDGX-ray3.30D/E/F/G/H/I/M/N/O/P/Q/R1-76[»]
4DDIX-ray3.80G/H/I/J/K/L1-76[»]
4DHJX-ray2.35B/F/J/M1-76[»]
D/H1-75[»]
4DHZX-ray3.11B1-76[»]
E1-75[»]
4FJVX-ray2.05B/D1-76[»]
4HK2X-ray1.40A/B/C/D1-76[»]
4HXDX-ray2.85A/C1-75[»]
4I6LX-ray2.49B77-150[»]
4I6NX-ray1.70B/D1-75[»]
4IG7X-ray2.00B1-75[»]
4IUMX-ray1.45B1-75[»]
4JQWX-ray2.90C609-684[»]
4K1RX-ray1.63B/D607-684[»]
4K7SX-ray1.76A/B/C1-76[»]
4K7UX-ray1.76A/B/C1-76[»]
4K7WX-ray1.76A/B/C1-76[»]
4KSKX-ray2.40C/D76-152[»]
4KSLX-ray2.83C/D/F/H/J/L/N/P/R/T/V/X76-228[»]
4LCDX-ray3.10E/F609-683[»]
4LDTX-ray1.90B/D609-684[»]
4MDKX-ray2.61E/F/G/H608-684[»]
4NQKX-ray3.70E/F/G/H/I/J608-684[»]
ProteinModelPortalP0CG48.
SMRP0CG48. Positions 1-683.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113164. 9750 interactions.
IntActP0CG48. 163 interactions.
MINTMINT-97475.

PTM databases

PhosphoSiteP0CG48.

Polymorphism databases

DMDM391358178.

Proteomic databases

PRIDEP0CG48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339647; ENSP00000344818; ENSG00000150991.
ENST00000536769; ENSP00000441543; ENSG00000150991.
GeneID7316.
UCSCuc001ugs.4. human.

Organism-specific databases

GeneCardsGC12M125396.
HGNCHGNC:12468. UBC.
HPACAB000362.
CAB005419.
HPA041344.
HPA049132.
MIM191340. gene.
neXtProtNX_P0CG48.
GenAtlasSearch...

Phylogenomic databases

OrthoDBEOG7JDR1W.
TreeFamTF354256.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_11123. Membrane Trafficking.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_13487. Ubiquitination of PAK-2p34.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
REACT_15518. Transmembrane transport of small molecules.
REACT_188257. Signal Transduction.
REACT_189085. Disease.
REACT_2001. Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
REACT_205386. Signal Transduction.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_216. DNA Repair.
REACT_224568. Disease.
REACT_24941. Circadian Clock.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_71. Gene Expression.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

Gene expression databases

ArrayExpressP0CG48.
BgeeP0CG48.

Family and domain databases

InterProIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamPF00240. ubiquitin. 9 hits.
[Graphical view]
PRINTSPR00348. UBIQUITIN.
SMARTSM00213. UBQ. 9 hits.
[Graphical view]
SUPFAMSSF54236. SSF54236. 9 hits.
PROSITEPS00299. UBIQUITIN_1. 9 hits.
PS50053. UBIQUITIN_2. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBC. human.
EvolutionaryTraceP0CG48.
NextBio33412565.
PROP0CG48.
SOURCESearch...

Entry information

Entry nameUBC_HUMAN
AccessionPrimary (citable) accession number: P0CG48
Secondary accession number(s): P02248 expand/collapse secondary AC list , P02249, P02250, P62988, Q29120, Q6LBL4, Q6LDU5, Q8WYN8, Q91887, Q91888, Q9BWD6, Q9BX98, Q9UEF2, Q9UEG1, Q9UEK8, Q9UPK7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: June 13, 2012
Last modified: July 9, 2014
This is version 46 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM