Reviewed, UniProtKB/Swiss-Prot P62988 (UBIQ_HUMAN)

Names and origin

Protein names

Recommended name:
    Ubiquitin

Gene names

Name:	RPS27A
Synonyms:	UBA80, UBCEP1
AND
Name:	UBA52
Synonyms:	UBCEP2
AND
Name:	UBB
AND
Name:	UBC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	76 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Protein modifier which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Attachment to proteins as a Lys-48-linked polymer usually leads to their degradation by proteasome. Attachment to proteins as a monomer or as an alternatively linked polymer does not lead to proteasomal degradation and may be required for numerous functions, including maintenance of chromatin structure, regulation of gene expression, stress response, ribosome biogenesis and DNA repair. Ref.21
Subcellular location	Cytoplasm. Nucleus.
Post-translational modification	Several types of polymeric chains can be formed, depending on the lysine used for the assembly.
Miscellaneous	Ubiquitin is synthesized as a polyubiquitin precursor with exact head to tail repeats, the number of repeats differ between species and strains. In some species there is a final amino-acid after the last repeat, here in human a Val. Some ubiquitin genes contain a single copy of ubiquitin fused to a ribosomal protein (either L40 or S27a).
Sequence similarities	Belongs to the ubiquitin family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	ER-associated protein catabolic process Traceable author statement. Source: UniProtKB anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome axon guidance Traceable author statement. Source: UniProtKB long-term strengthening of neuromuscular junction Traceable author statement. Source: UniProtKB negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of transcription Inferred from direct assay. Source: UniProtKB positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome protein ubiquitination Inferred from direct assay. Source: UniProtKB regulation of synaptic plasticity Traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB transcription regulator activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BUL1	P48524	1	EBI-413034,EBI-3881	From a different organism.
CCDC50	Q8IVM0	1	EBI-413034,EBI-723996
CDC6	Q99741	1	EBI-413034,EBI-374862
DUSP1	P28562	1	EBI-413034,EBI-975493
Fbxl20	Q9CZV8	1	EBI-413034,EBI-1551033	From a different organism.
GGA1	Q9UJY5	1	EBI-413034,EBI-447141
ITCH	Q96J02	1	EBI-413034,EBI-1564678
Mast2	Q60592	2	EBI-413034,EBI-493888	From a different organism.
MCM7	P33993	1	EBI-413034,EBI-355924
MDM2	Q00987	1	EBI-413034,EBI-389668
MYO6	Q9UM54	1	EBI-413034,EBI-350606
NEDD4	P46934	1	EBI-413034,EBI-726944
ORC1L	Q13415	1	EBI-413034,EBI-374847
RABGEF1	Q9UJ41	2	EBI-413034,EBI-913954
RNF168	Q8IYW5	1	EBI-413034,EBI-914207
RNF43	Q68DV7	1	EBI-413034,EBI-1647060
SMURF2	Q9HAU4	1	EBI-413034,EBI-396727
TP53	P04637	1	EBI-413034,EBI-366083
ubx2	O14048	1	EBI-413034,EBI-1005194	From a different organism.
ubx3	Q9UT81	1	EBI-413034,EBI-1005297	From a different organism.
WWP2	O00308	1	EBI-413034,EBI-743923
ZNF385A	Q96PM9	1	EBI-413034,EBI-1539778

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 76

76

Ubiquitin

PRO_0000114800

Sites

Binding site

54

1

Activating enzyme

Binding site

72

1

Activating enzyme

Site

68

1

Essential for function

Amino acid modifications

Modified residue

57

1

Phosphoserine By similarity

Modified residue

65

1

Phosphoserine Ref.20

Cross-link

6

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.18

Cross-link

11

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21 Ref.18

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.21

Cross-link

48

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21 Ref.18 Ref.22 Ref.23

Cross-link

63

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21

Cross-link

76

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

76

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Beta strand

12 – 16

5

Helix

23 – 34

12

Helix

38 – 40

3

Beta strand

41 – 43

3

Helix

56 – 59

4

Beta strand

69 – 71

3

Sequences

	Sequence		Length	Mass (Da)
	P62988-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: C42A35397FFD9B52	FASTA	76	8,565
	10 20 30 40 50 60 MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 70 IQKESTLHLV LRLRGG

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: 2988935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 2820408] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The human ubiquitin gene family: structure of a gene and pseudogenes from the Ub B subfamily." Baker R.T., Board P.G. Nucleic Acids Res. 15:443-463(1987) [PubMed: 3029682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UBB). Tissue: Lymphocyte.
[4]	"The human ubiquitin-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes." Baker R.T., Board P.G. Nucleic Acids Res. 19:1035-1040(1991) [PubMed: 1850507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (UBA52).
[5]	"Human ubiquitin A-52 residue ribosomal protein fusion product 1 (UBA52) in salivary epithelial cells." Wang H., Zhang Y., Okamoto T. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (UBA52).
[6]	"Effect of ubiquitin on platelet functions: possible identity with platelet activity suppressive lymphokine (PASL)." Pancre V., Pierce R.J., Fournier F., Mehtali M., Delanoye A., Capron A., Auriault C. Eur. J. Immunol. 21:2735-2741(1991) [PubMed: 1657614] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (RPS27A).
[7]	"Differential expression of translation-associated genes in benign and malignant human breast tumours." Adams S.M., Sharp M.G., Walker R.A., Brammar W.J., Varley J.M. Br. J. Cancer 65:65-71(1992) [PubMed: 1370760] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (RPS27A).
[8]	"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: 8917096] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UBC).
[9]	"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: 9644242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (UBC).
[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: 9504932] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UBC).
[11]	"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: 14745543] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UBB AND UBC).
[12]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (UBA52).
[13]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (RPS27A; UBB AND UBC). Tissue: Brain, Liver, Lung and Placenta.
[14]	"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes." Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N. Genome Res. 12:379-390(2002) [PubMed: 11875025] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[15]	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.
[16]	"Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor." Lund P.K., Moats-Staats B.M., Simmons J.G., Hoyt E., D'Ercole A.J., Martin F., van Wyk J.J. J. Biol. Chem. 260:7609-7613(1985) [PubMed: 2581967] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-76 (RPS27A).
[17]	"Hybrid troponin reconstituted from vertebrate and arthropod subunits." Schlesinger D.H., Goldstein G. Nature 255:423-424(1975) [PubMed: 124018] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-74.
[18]	"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: 16443603] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11 AND LYS-48, MASS SPECTROMETRY.
[19]	"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: 15466860] [Abstract] Cited for: UBIQUITINATION AT LYS-27.
[20]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, MASS SPECTROMETRY. Tissue: Epithelium.
[21]	"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: 16543144] [Abstract] Cited for: FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, MASS SPECTROMETRY.
[22]	"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex." Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L. Biochemistry 46:3553-3565(2007) [PubMed: 17323924] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, MASS SPECTROMETRY.
[23]	"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: 17203973] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, MASS SPECTROMETRY. Tissue: Lung adenocarcinoma.
[24]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[25]	"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: 3041007] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[26]	"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: 8166633] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[27]	"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: 8107144] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[28]	"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: 11173499] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[29]	"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: 12507430] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP7.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M26880 mRNA. Translation: AAA36789.1. Different termination.
M17597 mRNA. Translation: AAA36787.1. Different termination.
X04803 Genomic DNA. Translation: CAA28495.1. Different termination.
X56997 Genomic DNA. Translation: CAA40312.1. Different termination.
X56998 mRNA. Translation: CAA40313.1. Different termination.
X56999 mRNA. Translation: CAA40314.1. Different termination.
AF348700 mRNA. Translation: AAK31162.1. Sequence problems.
X63237 mRNA. Translation: CAA44911.1. Different termination.
S79522 mRNA. Translation: AAB21188.1. Different termination.
D63791 Genomic DNA. Translation: BAA09860.1. Different termination.
AB009010 mRNA. Translation: BAA23632.1. Different termination.
AB003730 Genomic DNA. Translation: BAA23486.1. Different termination.
AB089613 Genomic DNA. Translation: BAC56951.1. Different termination.
AB089617 Genomic DNA. Translation: BAC56955.1. Different termination.
AC005253 Genomic DNA. Translation: AAC25582.1. Different termination.
BC000379 mRNA. Translation: AAH00379.1. Different termination.
BC009301 mRNA. Translation: AAH09301.1. Different termination.
BC015127 mRNA. Translation: AAH15127.1. Different termination.
BC026301 mRNA. Translation: AAH26301.1. Different termination.
BC031027 mRNA. Translation: AAH31027.1. Different termination.
BC039193 mRNA. Translation: AAH39193.1. Different termination.
BC046123 mRNA. Translation: AAH46123.1. Different termination.
BC066293 mRNA. Translation: AAH66293.1. Different termination.
AB062071 Genomic DNA. Translation: BAB79490.1.
M10939 mRNA. Translation: AAA36788.1. Different termination.

IPI

IPI00798155.

PIR

UQHU. A02574.
UQHUC. A22005.
UQHUB. A26437.
A29526.
UQHUR. S34428.

RefSeq

NP_061828.1.
NP_066289.2.

UniGene

Hs.311640
Hs.356190
Hs.520348
Hs.5308
Hs.546292
Hs.700206
Hs.714712

3D structure databases

PDBPDBe

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	[»]
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	10-76	[»]
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	[»]
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	[»]
2NR2	NMR	-	A	1-76	[»]
2O6V	X-ray	2.20	A/C/E/G	1-76	[»]
			B/F	1-76	[»]
			D/H	1-76	[»]
2OJR	X-ray	2.60	A	1-76	[»]
2PE9	NMR	-	A/B	1-76	[»]
2PEA	NMR	-	A/B	1-76	[»]
2W9N	X-ray	2.25	A	1-76	[»]
2Z59	NMR	-	B	1-76	[»]
2ZCB	X-ray	1.60	A/B/C	1-76	[»]
2ZVN	X-ray	3.00	A/C/E/G	1-76	[»]
2ZVO	X-ray	2.90	A/G	1-76	[»]
3BY4	X-ray	1.55	B	1-75	[»]
3C0R	X-ray	2.31	B/D	1-75	[»]
3DVG	X-ray	2.60	X	1-76	[»]
			Y	1-76	[»]
3DVN	X-ray	2.70	U/X	1-76	[»]
			V/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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P62988. 68 interactions.

2-D gel databases

SWISS-2DPAGE

P62988.

Aarhus/Ghent-2DPAGE

13. IEF.

DOSAC-COBS-2DPAGE

P62988.

HSC-2DPAGE

P62988.

Siena-2DPAGE

P62988.

Proteomic databases

PRIDE

P62988.

Genome annotation databases

Ensembl

ENSG00000143947. Homo sapiens. [Contig view]
ENSG00000150991. Homo sapiens. [Contig view]
ENSG00000170315. Homo sapiens. [Contig view]
ENSG00000221983. Homo sapiens. [Contig view]

GeneID

7314.
7316.

KEGG

hsa:7314.
hsa:7316.

Organism-specific databases

GeneCards

GC01P190932.
GC02P055313.
GC06P114010.
GC12M123921.
GC17P016225.
GC19P018548.

H-InvDB

HIX0039999.

HGNC

HGNC:10417. RPS27A.
HGNC:12458. UBA52.
HGNC:12463. UBB.
HGNC:12468. UBC.

HPA

CAB000362.
CAB005419.

MIM

191321. gene.
191339. gene.
191340. gene.
191343. gene.

PharmGKB

PA34821.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P62988.

Enzyme and pathway databases

Reactome

REACT_11045. Signaling by Wnt.
REACT_11061. Signalling by NGF.
REACT_13635. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6185. HIV Infection.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Signaling in Immune system.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.
REACT_9417. Signaling by EGFR.

Gene expression databases

ArrayExpress

P62988.

Bgee

P62988.

CleanEx

HS_RPS27A.
HS_UBB.

GermOnline

ENSG00000143947. Homo sapiens.
ENSG00000150991. Homo sapiens.
ENSG00000170315. Homo sapiens.
ENSG00000196084. Homo sapiens.

Family and domain databases

InterPro

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

Pfam

PF00240. ubiquitin. 1 hit.
[Graphical view]

PRINTS

PR00348. UBIQUITIN.

SMART

SM00213. UBQ. 1 hit.
[Graphical view]

PROSITE

PS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

28592.

SOURCE

Search...

Entry information

Entry name

UBIQ_HUMAN

Accession

Primary (citable) accession number: P62988
Secondary accession number(s): P02248 , P02249, P02250, Q29120, Q6LBL4, Q6LDU5, Q8WYN8, Q91887, Q91888, Q9BWD6, Q9BX98, Q9UEF2, Q9UEG1, Q9UEK8, Q9UPK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)