P0CG48 (UBC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polyubiquitin-C

Cleaved into the following chain:

1. Ubiquitin

Gene names

Name:

UBC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	685 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Cytoplasm Nucleus
Domain	Repeat
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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 G1 phase of mitotic cell cycle Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome I-kappaB kinase/NF-kappaB cascade Traceable author statement. Source: Reactome JNK cascade Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome MyD88-dependent 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 S phase of mitotic cell cycle 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 Toll 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, TAP-dependent Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome cellular membrane organization Traceable author statement. Source: Reactome cytokine-mediated signaling pathway Traceable author statement. Source: Reactome egress of virus within host cell Traceable author statement. Source: Reactome endosomal transport Traceable author statement. Source: Reactome energy homeostasis Inferred from electronic annotation. Source: Compara epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fat pad development Inferred from electronic annotation. Source: Compara female gonad development Inferred from electronic annotation. Source: Compara female meiosis I Inferred from electronic annotation. Source: Compara fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome hypothalamus gonadotrophin-releasing hormone neuron development Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome male meiosis I Inferred from electronic annotation. Source: Compara 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 nerve growth factor 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 cascade Traceable author statement. Source: Reactome positive regulation of NF-kappaB transcription factor activity Traceable author statement. Source: Reactome positive regulation of transcription from RNA polymerase II promoter 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 seminiferous tubule development Inferred from electronic annotation. Source: Compara toll-like receptor 1 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 transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome ubiquitin homeostasis Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 76

76

Ubiquitin

PRO_0000396178

Chain

77 – 152

76

Ubiquitin

PRO_0000396179

Chain

153 – 228

76

Ubiquitin

PRO_0000396180

Chain

229 – 304

76

Ubiquitin

PRO_0000396181

Chain

305 – 380

76

Ubiquitin

PRO_0000396182

Chain

381 – 456

76

Ubiquitin

PRO_0000396183

Chain

457 – 532

76

Ubiquitin

PRO_0000396184

Chain

533 – 608

76

Ubiquitin

PRO_0000396185

Chain

609 – 684

76

Ubiquitin

PRO_0000396186

Propeptide

685

1

PRO_0000396187

Regions

Domain

1 – 76

76

Ubiquitin-like 1

Domain

77 – 152

76

Ubiquitin-like 2

Domain

153 – 228

76

Ubiquitin-like 3

Domain

229 – 304

76

Ubiquitin-like 4

Domain

305 – 380

76

Ubiquitin-like 5

Domain

381 – 456

76

Ubiquitin-like 6

Domain

457 – 532

76

Ubiquitin-like 7

Domain

533 – 608

76

Ubiquitin-like 8

Domain

609 – 684

76

Ubiquitin-like 9

Sites

Binding site

54

1

Activating enzyme

Binding site

72

1

Activating enzyme

Site

68

1

Essential for function

Amino acid modifications

Cross-link

6

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Cross-link

11

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9 Ref.12

Cross-link

27

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable

Cross-link

29

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12

Cross-link

33

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

48

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9 Ref.12 Ref.14

Cross-link

63

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12 Ref.15

Cross-link

76

Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Experimental info

Mutagenesis

48

1

K → R: No effect on HLTF-mediated polyubiquitination of PCNA. Ref.15

Mutagenesis

63

1

K → R: Abolishes HLTF-mediated polyubiquitination of PCNA. Ref.15

Sequence conflict

190

1

P → S in AC126309. Ref.4

Sequence conflict

397

1

V → G in BAA09860. Ref.6

Secondary structure

1

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685

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Beta strand

8 – 10

3

Beta strand

12 – 16

5

Beta strand

19 – 22

4

Helix

23 – 34

12

Helix

38 – 40

3

Beta strand

41 – 45

5

Beta strand

47 – 49

3

Beta strand

52 – 55

4

Helix

56 – 59

4

Beta strand

66 – 71

6

Beta strand

78 – 83

6

Beta strand

84 – 86

3

Beta strand

88 – 93

6

Helix

99 – 110

12

Helix

114 – 116

3

Beta strand

118 – 121

4

Beta strand

124 – 126

3

Beta strand

130 – 132

3

Helix

133 – 135

3

Beta strand

142 – 146

5

Sequences

	Sequence		Length	Mass (Da)
	P0CG48 [UniParc]. Last modified June 13, 2012. Version 3. Checksum: B6E7BC06FEE77196	FASTA	685	77,039
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"Hybrid troponin reconstituted from vertebrate and arthropod subunits." 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, 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, 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, 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, MASS SPECTROMETRY. 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.
+	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.

IPI

IPI00969566.

PIR

UQHU. A02574.
UQHUC. A22005.
A29526.

UniGene

Hs.520348.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C3T	NMR	-	A	1-76	[»]
1CMX	X-ray	2.25	B/D	1-76	[»]
1D3Z	NMR	-	A	1-76	[»]
1F9J	X-ray	2.70	A/B	1-76	[»]
1FXT	NMR	-	B	1-76	[»]
1G6J	NMR	-	A	1-76	[»]
1GJZ	NMR	-	A/B	1-51	[»]
1NBF	X-ray	2.30	C/D	1-76	[»]
1OGW	X-ray	1.32	A	1-76	[»]
1Q5W	NMR	-	B	1-76	[»]
1S1Q	X-ray	2.00	B/D	1-76	[»]
1SIF	X-ray	2.18	A	6-76	[»]
1TBE	X-ray	2.40	A/B	1-76	[»]
1UBI	X-ray	1.80	A	1-76	[»]
1UBQ	X-ray	1.80	A	1-76	[»]
1UD7	NMR	-	A	1-76	[»]
1XD3	X-ray	1.45	B/D	1-75	[»]
1XQQ	NMR	-	A	1-76	[»]
1YX5	NMR	-	B	1-76	[»]
1YX6	NMR	-	B	1-76	[»]
1ZGU	NMR	-	B	1-76	[»]
1ZO6	model	-	B/C	1-76	[»]
2AYO	X-ray	3.50	B	1-76	[»]
2BGF	NMR	-	A/B	1-76	[»]
2DEN	NMR	-	B	1-76	[»]
2FUH	NMR	-	B	1-76	[»]
2G45	X-ray	1.99	B/E	1-76	[»]
2GBJ	X-ray	1.35	A/B	1-76	[»]
2GBK	X-ray	1.99	A/B/C/D	10-76	[»]
2GBM	X-ray	1.55	A/B/C/D	1-76	[»]
2GBN	X-ray	1.60	A	1-76	[»]
2GBR	X-ray	2.00	A/B/C	1-76	[»]
2GMI	X-ray	2.50	C	1-76	[»]
2HTH	X-ray	2.70	A	1-76	[»]
2IBI	X-ray	2.20	B	1-75	[»]
2J7Q	X-ray	1.80	B/D	1-75	[»]
2JF5	X-ray	1.95	A/B	1-76	[»]
2JRI	NMR	-	B/C	1-76	[»]
2JY6	NMR	-	A	1-76	[»]
2JZZ	NMR	-	A	1-76	[»]
2K25	NMR	-	A	1-75	[»]
2K6D	NMR	-	B	1-75	[»]
2K8B	NMR	-	A	1-76	[»]
2K8C	NMR	-	A	1-76	[»]
2KDF	NMR	-	B/C	1-76	[»]
2KHW	NMR	-	B	1-76	[»]
2KJH	NMR	-	B	1-75	[»]
2KLG	NMR	-	A	1-76	[»]
2KN5	NMR	-	A	1-76	[»]
2KX0	NMR	-	A	74-151	[»]
2L3Z	NMR	-	A	1-76	[»]
2LD9	NMR	-	A	76-152	[»]
2LVO	NMR	-	A	1-76	[»]
2LVP	NMR	-	A/B	1-76	[»]
2LVQ	NMR	-	A/B	1-76	[»]
2NR2	NMR	-	A	1-76	[»]
2O6V	X-ray	2.20	A/B/C/D/E/F/G/H	1-76	[»]
2OJR	X-ray	2.60	A	1-76	[»]
2PE9	NMR	-	A/B	1-76	[»]
2PEA	NMR	-	A/B	1-76	[»]
2RR9	NMR	-	A/B	1-76	[»]
2W9N	X-ray	2.25	A	1-152	[»]
2WDT	X-ray	2.30	B/D	1-75	[»]
2XEW	X-ray	2.20	A/B/C/D/E/F/G/H/I/J/K/L	1-76	[»]
2Y5B	X-ray	2.70	B/F	1-152	[»]
2Z59	NMR	-	B	1-76	[»]
2ZCB	X-ray	1.60	A/B/C	1-76	[»]
2ZVN	X-ray	3.00	A/C/E/G	1-152	[»]
2ZVO	X-ray	2.90	A/G	1-152	[»]
3A33	X-ray	2.20	B	1-76	[»]
3ALB	X-ray	1.85	A/B/C/D	1-76	[»]
3AUL	X-ray	2.39	A/B	1-76	[»]
3B08	X-ray	1.70	A/D/G/J	1-152	[»]
3B0A	X-ray	1.90	A/D	1-152	[»]
3BY4	X-ray	1.55	B	1-75	[»]
3C0R	X-ray	2.31	B/D	1-75	[»]
3DVG	X-ray	2.60	X/Y	1-76	[»]
3DVN	X-ray	2.70	U/V/X/Y	1-76	[»]
3EEC	X-ray	3.00	A/B	1-76	[»]
3EFU	X-ray	1.84	A	1-76	[»]
3EHV	X-ray	1.81	A/B/C	1-76	[»]
3H7P	X-ray	1.90	A/B	1-76	[»]
3H7S	X-ray	2.30	A/B	1-76	[»]
3HM3	X-ray	1.96	A/B/C/D	1-76	[»]
3I3T	X-ray	2.59	B/D/F/H	1-75	[»]
3IFW	X-ray	2.40	B	1-75	[»]
3IHP	X-ray	2.80	C/D	1-75	[»]
3JSV	X-ray	2.70	A/B	1-76	[»]
3JVZ	X-ray	3.30	X/Y	1-76	[»]
3JW0	X-ray	3.10	X/Y	1-76	[»]
3K9O	X-ray	1.80	B	76-151	[»]
3K9P	X-ray	2.80	B	1-76	[»]
3KVF	X-ray	2.80	B	1-75	[»]
3KW5	X-ray	2.83	B	1-75	[»]
3LDZ	X-ray	2.60	E/F/G	1-73	[»]
3MHS	X-ray	1.89	D	1-76	[»]
3MTN	X-ray	2.70	B/D	1-76	[»]
3N30	X-ray	3.00	A/B	1-76	[»]
3N32	X-ray	1.80	A	1-76	[»]
3N3K	X-ray	2.60	B	5-76	[»]
3NS8	X-ray	1.71	A/B	1-76	[»]
3O65	X-ray	2.70	B/D/F/H	1-75	[»]
3OFI	X-ray	2.35	C/D	1-76	[»]
3OJ3	X-ray	2.50	A/B/C/D/E/F/G/H	1-76	[»]
3OJ4	X-ray	3.40	B/E	1-76	[»]
3ONS	X-ray	1.80	A	1-72	[»]
3PRM	X-ray	2.30	B/D	1-75	[»]
3PT2	X-ray	2.50	B	1-75	[»]
3PTF	X-ray	2.70	C/D	1-76	[»]
3Q3F	X-ray	2.17	A	2-76	[»]
3RUL	X-ray	2.50	A/B/C/D	1-75	[»]
3TMP	X-ray	1.91	B/D/F/H	1-76	[»]
3U30	X-ray	2.43	A/D	1-152	[»]
3UGB	X-ray	2.35	B	1-76	[»]
3V6C	X-ray	1.70	B	74-150	[»]
3V6E	X-ray	2.10	B	74-150	[»]
3VFK	X-ray	2.80	A	1-75	[»]
3VUW	X-ray	1.95	A/B/C	1-76	[»]
3VUX	X-ray	1.70	A/B/C	1-76	[»]
3VUY	X-ray	1.98	A/B/C	1-76	[»]
3ZNH	X-ray	2.30	B	1-75	[»]
4AUQ	X-ray	2.18	C/F	1-76	[»]
4DDG	X-ray	3.30	D/E/F/G/H/I/M/N/O/P/Q/R	1-76	[»]
4DDI	X-ray	3.80	G/H/I/J/K/L	1-76	[»]
4DHJ	X-ray	2.35	B/F/J/M	1-76	[»]
			D/H	1-75	[»]
4DHZ	X-ray	3.11	B	1-76	[»]
			E	1-75	[»]
4HK2	X-ray	1.40	A/B/C/D	1-76	[»]
4HXD	X-ray	2.85	A/C	1-75	[»]
4I6L	X-ray	2.49	B	77-150	[»]
4IUM	X-ray	1.45	B	1-75	[»]

ProteinModelPortal

P0CG48.

SMR

P0CG48. Positions 1-683.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0CG48. 7 interactions.

PTM databases

PhosphoSite

P0CG48.

Polymorphism databases

DMDM

308153512.

Proteomic databases

PRIDE

P0CG48.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000339647; ENSP00000344818; ENSG00000150991.
ENST00000536769; ENSP00000441543; ENSG00000150991.

UCSC

uc001ugs.4. human.

Organism-specific databases

GeneCards

GC12M125396.

HGNC

HGNC:12468. UBC.

HPA

CAB000362.
CAB005419.
HPA041344.
HPA049132.

MIM

191340. gene.

neXtProt

NX_P0CG48.

GenAtlas

Search...

Enzyme and pathway databases

Reactome

REACT_107772. Immune System.
REACT_111102. Signal Transduction.
REACT_11123. Membrane Trafficking.
REACT_115202. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
REACT_2001. Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_216. DNA Repair.
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.
REACT_81380. Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
REACT_97910. Signal Transduction.

Gene expression databases

ArrayExpress

P0CG48.

Bgee

P0CG48.

GermOnline

ENSG00000150991. Homo sapiens.

Family and domain databases

InterPro

IPR000626. Ubiquitin.
IPR019954. Ubiquitin_CS.
IPR019956. Ubiquitin_subgr.
IPR019955. Ubiquitin_supergroup.
[Graphical view]

Pfam

PF00240. ubiquitin. 9 hits.
[Graphical view]

PRINTS

PR00348. UBIQUITIN.

SMART

SM00213. UBQ. 9 hits.
[Graphical view]

PROSITE

PS00299. UBIQUITIN_1. 9 hits.
PS50053. UBIQUITIN_2. 9 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

UBC. human.

EvolutionaryTrace

P0CG48.

NextBio

33412565.

SOURCE

Search...

Entry information

Entry name

UBC_HUMAN

Accession

Primary (citable) accession number: P0CG48
Secondary accession number(s): P02248 , 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:	May 1, 2013
This is version 32 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.