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UniProtKB/Swiss-Prot entry P62988


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name UBIQ_HUMAN
Primary accession number P62988
Secondary accession numbers P02248 P02249 P02250 Q29120 Q6LBL4 Q6LDU5 Q8WYN8 Q91887 Q91888 Q9BWD6 Q9BX98 Q9UEF2 Q9UEG1 Q9UEK8 Q9UPK7
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 80)
Name and origin of the protein
Protein name Ubiquitin
Synonyms None
Gene names
Name: RPS27A
Synonyms: UBA80, UBCEP1
and
Name: UBA52
Synonyms: UBCEP2
and
Name: UBB
and
Name: UBC
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2988935 [NCBI, ExPASy, EBI, Israel, Japan]
Wiborg O., Pedersen M.S., Wind A., Berglund L.E., Marcker K.A., Vuust J.;
"The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences.";
EMBO J. 4:755-759(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0006-291X(87)90970-3; PubMed=2820408 [NCBI, ExPASy, EBI, Israel, Japan]
Einspanier R., Sharma H.S., Scheit K.H.;
"Cloning and sequence analysis of a cDNA encoding poly-ubiquitin in human ovarian granulosa cells.";
Biochem. Biophys. Res. Commun. 147:581-587(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UBB).
TISSUE=Lymphocyte;
DOI=10.1093/nar/15.2.443; PubMed=3029682 [NCBI, ExPASy, EBI, Israel, Japan]
Baker R.T., Board P.G.;
"The human ubiquitin gene family: structure of a gene and pseudogenes from the Ub B subfamily.";
Nucleic Acids Res. 15:443-463(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (UBA52).
DOI=10.1093/nar/19.5.1035; PubMed=1850507 [NCBI, ExPASy, EBI, Israel, Japan]
Baker R.T., Board P.G.;
"The human ubiquitin-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes.";
Nucleic Acids Res. 19:1035-1040(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (UBA52).
Wang H., Zhang Y., Okamoto T.;
"Human ubiquitin A-52 residue ribosomal protein fusion product 1 (UBA52) in salivary epithelial cells.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (RPS27A).
DOI=10.1002/eji.1830211113; PubMed=1657614 [NCBI, ExPASy, EBI, Israel, Japan]
Pancre V., Pierce R.J., Fournier F., Mehtali M., Delanoye A., Capron A., Auriault C.;
"Effect of ubiquitin on platelet functions: possible identity with platelet activity suppressive lymphokine (PASL).";
Eur. J. Immunol. 21:2735-2741(1991).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (RPS27A).
PubMed=1370760 [NCBI, ExPASy, EBI, Israel, Japan]
Adams S.M., Sharp M.G., Walker R.A., Brammar W.J., Varley J.M.;
"Differential expression of translation-associated genes in benign and malignant human breast tumours.";
Br. J. Cancer 65:65-71(1992).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UBC).
DOI=10.1016/0378-1119(96)00145-X; PubMed=8917096 [NCBI, ExPASy, EBI, Israel, Japan]
Nenoi M., Mita K., Ichimura S., Cartwright I.L., Takahashi E., Yamauchi M., Tsuji H.;
"Heterogeneous structure of the polyubiquitin gene UbC of HeLa S3 cells.";
Gene 175:179-185(1996).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (UBC).
PubMed=9644242 [NCBI, ExPASy, EBI, Israel, Japan]
Kim N.S., Yamaguchi T., Sekine S., Saeki M., Iwamuro S., Kato S.;
"Cloning of human polyubiquitin cDNAs and a ubiquitin-binding assay involving its in vitro translation product.";
J. Biochem. 124:35-39(1998).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UBC).
PubMed=9504932 [NCBI, ExPASy, EBI, Israel, Japan]
Nenoi M., Mita K., Ichimura S., Kawano A.;
"Higher frequency of concerted evolutionary events in rodents than in man at the polyubiquitin gene VNTR locus.";
Genetics 148:867-876(1998).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UBB AND UBC).
DOI=10.1007/s00239-003-2532-4; PubMed=14745543 [NCBI, ExPASy, EBI, Israel, Japan]
Tachikui H., Saitou N., Nakajima T., Hayasaka I., Ishida T., Inoue I.;
"Lineage-specific homogenization of the polyubiquitin gene among human and great apes.";
J. Mol. Evol. 57:737-744(2003).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (UBA52).
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (RPS27A; UBB AND UBC).
TISSUE=Brain, Liver, Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
DOI=10.1101/gr.214202; PubMed=11875025 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes.";
Genome Res. 12:379-390(2002).
[15]
PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, AND MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-76 (RPS27A).
PubMed=2581967 [NCBI, ExPASy, EBI, Israel, Japan]
Lund P.K., Moats-Staats B.M., Simmons J.G., Hoyt E., D'Ercole A.J., Martin F., van Wyk J.J.;
"Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor.";
J. Biol. Chem. 260:7609-7613(1985).
[17]
PROTEIN SEQUENCE OF 1-74.
DOI=10.1038/255423a0; PubMed=124018 [NCBI, ExPASy, EBI, Israel, Japan]
Schlesinger D.H., Goldstein G.;
"Hybrid troponin reconstituted from vertebrate and arthropod subunits.";
Nature 255:423-424(1975).
[18]
PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11 AND LYS-48, AND MASS SPECTROMETRY.
DOI=10.1074/jbc.M512786200; PubMed=16443603 [NCBI, ExPASy, EBI, Israel, Japan]
Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.;
"Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation.";
J. Biol. Chem. 281:10825-10838(2006).
[19]
UBIQUITINATION AT LYS-27.
DOI=10.1074/jbc.M402916200; PubMed=15466860 [NCBI, ExPASy, EBI, Israel, Japan]
Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.;
"Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis.";
J. Biol. Chem. 279:53533-53543(2004).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[21]
FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2006.02.018; PubMed=16543144 [NCBI, ExPASy, EBI, Israel, Japan]
Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
"Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain.";
Mol. Cell 21:737-748(2006).
[22]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS SPECTROMETRY.
DOI=10.1021/bi061994u; PubMed=17323924 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[23]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS SPECTROMETRY.
TISSUE=Lung adenocarcinoma;
DOI=10.1021/pr060438j; PubMed=17203973 [NCBI, ExPASy, EBI, Israel, Japan]
Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.;
"The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells.";
J. Proteome Res. 6:298-305(2007).
[24]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[25]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1016/0022-2836(87)90679-6; PubMed=3041007 [NCBI, ExPASy, EBI, Israel, Japan]
Vijay-Kumar S., Bugg C.E., Cook W.J.;
"Structure of ubiquitin refined at 1.8-A resolution.";
J. Mol. Biol. 194:531-544(1987).
[26]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=8166633 [NCBI, ExPASy, EBI, Israel, Japan]
Ramage R., Green J., Muir T.W., Ogunjobi O.M., Love S., Shaw K.;
"Synthetic, structural and biological studies of the ubiquitin system: the total chemical synthesis of ubiquitin.";
Biochem. J. 299:151-158(1994).
[27]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1006/jmbi.1994.1169; PubMed=8107144 [NCBI, ExPASy, EBI, Israel, Japan]
Cook W.J., Jeffrey L.C., Kasperek E., Pickart C.M.;
"Structure of tetraubiquitin shows how multiubiquitin chains can be formed.";
J. Mol. Biol. 236:601-609(1994).
[28]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
DOI=10.1107/S090744490001800X; PubMed=11173499 [NCBI, ExPASy, EBI, Israel, Japan]
Phillips C.L., Thrower J., Pickart C.M., Hill C.P.;
"Structure of a new crystal form of tetraubiquitin.";
Acta Crystallogr. D 57:341-344(2001).
[29]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP7.
DOI=10.1016/S0092-8674(02)01199-6; PubMed=12507430 [NCBI, ExPASy, EBI, Israel, Japan]
Hu M., Li P., Li M., Li W., Yao T., Wu J.-W., Gu W., Cohen R.E., Shi Y.;
"Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde.";
Cell 111:1041-1054(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M26880; AAA36789.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17597; AAA36787.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04803; CAA28495.1; ALT_TERM; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X56997; CAA40312.1; ALT_TERM; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X56998; CAA40313.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X56999; CAA40314.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF348700; AAK31162.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X63237; CAA44911.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S79522; AAB21188.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D63791; BAA09860.1; ALT_TERM; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB009010; BAA23632.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB003730; BAA23486.1; ALT_TERM; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB089613; BAC56951.1; ALT_TERM; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB089617; BAC56955.1; ALT_TERM; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005253; AAC25582.1; ALT_TERM; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000379; AAH00379.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009301; AAH09301.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015127; AAH15127.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC026301; AAH26301.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031027; AAH31027.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC039193; AAH39193.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC046123; AAH46123.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066293; AAH66293.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB062071; BAB79490.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M10939; AAA36788.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00798155; -.
PIR A02574; UQHU.
A22005; UQHUC.
A26437; UQHUB.
A29526; A29526.
S34428; UQHUR.
RefSeq NP_061828.1; -.
NP_066289.2; -.
UniGene Hs.311640
3D structure databases
PDB
1C3T; NMR; -; A=1-76.[ExPASy / RCSB / EBI]
1CMX; X-ray; 2.25 A; B/D=1-76.[ExPASy / RCSB / EBI]
1D3Z; NMR; -; A=1-76.[ExPASy / RCSB / EBI]
1F9J; X-ray; 2.70 A; A/B=1-76.[ExPASy / RCSB / EBI]
1FXT; NMR; -; B=1-76.[ExPASy / RCSB / EBI]
1G6J; NMR; -; A=1-76.[ExPASy / RCSB / EBI]
1GJZ; NMR; -; A/B=1-51.[ExPASy / RCSB / EBI]
1NBF; X-ray; 2.30 A; C/D=1-76.[ExPASy / RCSB / EBI]
1OGW; X-ray; 1.32 A; A=1-76.[ExPASy / RCSB / EBI]
1Q5W; NMR; -; B=1-76.[ExPASy / RCSB / EBI]
1S1Q; X-ray; 2.00 A; B/D=1-76.[ExPASy / RCSB / EBI]
1SIF; X-ray; 2.18 A; A=6-76.[ExPASy / RCSB / EBI]
1TBE; X-ray; 2.40 A; A/B=1-76.[ExPASy / RCSB / EBI]
1UBI; X-ray; 1.80 A; A=1-76.[ExPASy / RCSB / EBI]
1UBQ; X-ray; 1.80 A; A=1-76.[ExPASy / RCSB / EBI]
1XD3; X-ray; 1.45 A; B/D=1-75.[ExPASy / RCSB / EBI]
1XQQ; NMR; -; A=1-76.[ExPASy / RCSB / EBI]
1YX5; NMR; -; B=1-76.[ExPASy / RCSB / EBI]
1YX6; NMR; -; B=1-76.[ExPASy / RCSB / EBI]
1ZGU; NMR; -; B=1-76.[ExPASy / RCSB / EBI]
1ZO6; Model; -; B/C=1-76.[ExPASy / RCSB / EBI]
2AYO; X-ray; 3.50 A; B=1-76.[ExPASy / RCSB / EBI]
2BGF; NMR; -; A/B=1-76.[ExPASy / RCSB / EBI]
2DEN; NMR; -; B=1-76.[ExPASy / RCSB / EBI]
2FUH; NMR; -; B=1-76.[ExPASy / RCSB / EBI]
2G45; X-ray; 1.99 A; B/E=1-76.[ExPASy / RCSB / EBI]
2GBJ; X-ray; 1.35 A; A/B=10-76.[ExPASy / RCSB / EBI]
2GBK; X-ray; 1.99 A; A/B/C/D=10-76.[ExPASy / RCSB / EBI]
2GBM; X-ray; 1.55 A; A/B/C/D=1-76.[ExPASy / RCSB / EBI]
2GBN; X-ray; 1.60 A; A=1-76.[ExPASy / RCSB / EBI]
2GBR; X-ray; 2.00 A; A/B/C=1-76.[ExPASy / RCSB / EBI]
2HTH; X-ray; 2.70 A; A=1-76.[ExPASy / RCSB / EBI]
2IBI; X-ray; 2.20 A; B=1-75.[ExPASy / RCSB / EBI]
2J7Q; X-ray; 1.80 A; B/D=1-75.[ExPASy / RCSB / EBI]
2JF5; X-ray; 1.95 A; A/B=1-76.[ExPASy / RCSB / EBI]
2JRI; NMR; -; B/C=1-76.[ExPASy / RCSB / EBI]
2JY6; NMR; -; A=1-76.[ExPASy / RCSB / EBI]
2JZZ; NMR; -; A=1-76.[ExPASy / RCSB / EBI]
2K25; NMR; -; A=1-75.[ExPASy / RCSB / EBI]
2K6D; NMR; -; B=1-75.[ExPASy / RCSB / EBI]
2K8B; NMR; -; A=1-76.[ExPASy / RCSB / EBI]
2K8C; NMR; -; A=1-76.[ExPASy / RCSB / EBI]
2NR2; NMR; -; A=1-76.[ExPASy / RCSB / EBI]
2O6V; X-ray; 2.20 A; A/C/E/G=1-76, B/F=1-76, D/H=1-76.[ExPASy / RCSB / EBI]
2OJR; X-ray; 2.60 A; A=1-76.[ExPASy / RCSB / EBI]
2PE9; NMR; -; A/B=1-76.[ExPASy / RCSB / EBI]
2PEA; NMR; -; A/B=1-76.[ExPASy / RCSB / EBI]
2W9N; X-ray; 2.25 A; A=1-76.[ExPASy / RCSB / EBI]
2Z59; NMR; -; B=1-76.[ExPASy / RCSB / EBI]
2ZCB; X-ray; 1.60 A; A/B/C=1-76.[ExPASy / RCSB / EBI]
2ZVN; X-ray; 3.00 A; A/C/E/G=1-76.[ExPASy / RCSB / EBI]
2ZVO; X-ray; 2.90 A; A/G=1-76.[ExPASy / RCSB / EBI]
3BY4; X-ray; 1.55 A; B=1-75.[ExPASy / RCSB / EBI]
3C0R; X-ray; 2.31 A; B/D=1-75.[ExPASy / RCSB / EBI]
3DVG; X-ray; 2.60 A; X=1-76, Y=1-76.[ExPASy / RCSB / EBI]
3DVN; X-ray; 2.70 A; U/X=1-76, V/Y=1-76.[ExPASy / RCSB / EBI]
3EEC; X-ray; 3.00 A; A/B=1-76.[ExPASy / RCSB / EBI]
3EFU; X-ray; 1.84 A; A=1-76.[ExPASy / RCSB / EBI]
3EHV; X-ray; 1.81 A; A/B/C=1-76.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1C3T; -.
1CMX; -.
1D3Z; -.
1F9J; -.
1FXT; -.
1G6J; -.
1GJZ; -.
1NBF; -.
1OGW; -.
1Q5W; -.
1S1Q; -.
1SIF; -.
1TBE; -.
1UBI; -.
1UBQ; -.
1XD3; -.
1XQQ; -.
1YX5; -.
1YX6; -.
1ZGU; -.
1ZO6; -.
2AYO; -.
2BGF; -.
2DEN; -.
2FUH; -.
2G45; -.
2GBJ; -.
2GBK; -.
2GBM; -.
2GBN; -.
2GBR; -.
2HTH; -.
2IBI; -.
2J7Q; -.
2JF5; -.
2JRI; -.
2JY6; -.
2JZZ; -.
2K25; -.
2K6D; -.
2K8B; -.
2K8C; -.
2NR2; -.
2O6V; -.
2OJR; -.
2PE9; -.
2PEA; -.
2W9N; -.
2Z59; -.
2ZCB; -.
2ZVN; -.
2ZVO; -.
3BY4; -.
3C0R; -.
3DVG; -.
3DVN; -.
3EEC; -.
3EFU; -.
3EHV; -.
ModBase P62988.
Protein-protein interaction databases
IntAct P62988; 68.
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.
2D gel databases
SWISS-2DPAGE P62988; -.
Aarhus/Ghent-2DPAGE 13; IEF.
DOSAC-COBS-2DPAGE P62988; -.
HSC-2DPAGE P62988; -.
Siena-2DPAGE P62988; -.
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.
GenAtlas RPS27A.
HPA CAB000362; -.
CAB005419; -.
MIM 191321; gene. [NCBI / EBI]
191339; gene. [NCBI / EBI]
191340; gene. [NCBI / EBI]
191343; gene. [NCBI / EBI]
PharmGKB PA34821; -.
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.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0030528; Molecular function: transcription regulator activity (inferred from direct assay from UniProtKB).
GO:0031145; Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0007411; Biological process: axon guidance (traceable author statement from UniProtKB).
GO:0030433; Biological process: ER-associated protein catabolic process (traceable author statement from UniProtKB).
GO:0042062; Biological process: long-term strengthening of neuromuscular junction (traceable author statement from UniProtKB).
GO:0051436; Biological process: negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0045941; Biological process: positive regulation of transcription (inferred from direct assay from UniProtKB).
GO:0051437; Biological process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0016567; Biological process: protein ubiquitination (inferred from direct assay from UniProtKB).
GO:0048167; Biological process: regulation of synaptic plasticity (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000626; Ubiquitin.
IPR019954; Ubiquitin_CS.
IPR019956; Ubiquitin_subgroup.
IPR019955; Ubiquitin_supergroup.
Graphical view of domain structure.
Pfam PF00240; ubiquitin; 1.
Pfam graphical view of domain structure.
PRINTS PR00348; UBIQUITIN.
SMART SM00213; UBQ; 1.
SMART graphical view of domain structure.
PROSITE PS00299; UBIQUITIN_1; 1.
PS50053; UBIQUITIN_2; 1.
PROSITE graphical view of domain structure (profiles).
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; -.
Phylogenomic databases
HOVERGEN P62988; -.
Other
NextBio 28592; -.
SOURCE RPS27A; Homo sapiens.
ProtoNet P62988.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   76  76     Ubiquitin. PRO_0000114800
BINDING   54   54        Activating enzyme. 
BINDING   72   72        Activating enzyme. 
SITE   68   68  1     Essential for function. 
MOD_RES   57   57        Phosphoserine (By similarity). 
MOD_RES   65   65        Phosphoserine. 
CROSSLNK   6    6        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   11   11        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   27   27        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) (Probable). 
CROSSLNK   29   29        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   48   48        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   63   63        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   76   76        Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins). 
STRAND   2    7  6      
STRAND   12   16  5      
HELIX   23   34  12      
HELIX   38   40  3      
STRAND   41   43  3      
HELIX   56   59  4      
STRAND   69   71  3      
Sequence information
Length: 76 AA [This is the length of the unprocessed precursor] Molecular weight: 8565 Da [This is the MW of the unprocessed precursor] CRC64: C42A35397FFD9B52 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 

        70 
IQKESTLHLV LRLRGG 

P62988 in FASTA format

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