Full text data of RPS27A
RPS27A
(UBA80, UBCEP1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80; Ubiquitin; 40S ribosomal protein S27a; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80; Ubiquitin; 40S ribosomal protein S27a; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00179330
IPI00179330 Ubiquitin and ribosomal protein S27a, Ubiquitin and ribosomal protein S27a, membrane 2 4 3 3 2 n/a 2 3 16 n/a 6 3 n/a 3 2 n/a 2 3 3 4 intracellular n/a expected molecular weight found in band ~ 31 kDa, between 55-43 kDa and > 188 kDa
IPI00179330 Ubiquitin and ribosomal protein S27a, Ubiquitin and ribosomal protein S27a, membrane 2 4 3 3 2 n/a 2 3 16 n/a 6 3 n/a 3 2 n/a 2 3 3 4 intracellular n/a expected molecular weight found in band ~ 31 kDa, between 55-43 kDa and > 188 kDa
UniProt
P62979
ID RS27A_HUMAN Reviewed; 156 AA.
AC P62979; P02248; P02249; P02250; P14798; P62988; Q29120; Q6LBL4;
read moreAC Q6LDU5; Q8WYN8; Q91887; Q91888; Q9BQ77; Q9BWD6; Q9BX98; Q9UEF2;
AC Q9UEG1; Q9UEK8; Q9UPK7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Ubiquitin-40S ribosomal protein S27a;
DE AltName: Full=Ubiquitin carboxyl extension protein 80;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=40S ribosomal protein S27a;
DE Flags: Precursor;
GN Name=RPS27A; Synonyms=UBA80, UBCEP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1657614; DOI=10.1002/eji.1830211113;
RA Pancre V., Pierce R.J., Fournier F., Mehtali M., Delanoye A.,
RA Capron A., Auriault C.;
RT "Effect of ubiquitin on platelet functions: possible identity with
RT platelet activity suppressive lymphokine (PASL).";
RL Eur. J. Immunol. 21:2735-2741(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1370760;
RA Adams S.M., Sharp M.G., Walker R.A., Brammar W.J., Varley J.M.;
RT "Differential expression of translation-associated genes in benign and
RT malignant human breast tumours.";
RL Br. J. Cancer 65:65-71(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-98.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
RA Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [6]
RP PROTEIN SEQUENCE OF 1-74.
RX PubMed=124018; DOI=10.1038/255423a0;
RA Schlesinger D.H., Goldstein G.;
RT "Hybrid troponin reconstituted from vertebrate and arthropod
RT subunits.";
RL Nature 255:423-424(1975).
RN [7]
RP PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11
RP AND LYS-48, AND MASS SPECTROMETRY.
RX PubMed=16443603; DOI=10.1074/jbc.M512786200;
RA Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.;
RT "Alzheimer disease-specific conformation of hyperphosphorylated paired
RT helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and
RT Lys-6 ubiquitin conjugation.";
RL J. Biol. Chem. 281:10825-10838(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative
RT analysis of 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-156.
RX PubMed=2581967;
RA Lund P.K., Moats-Staats B.M., Simmons J.G., Hoyt E., D'Ercole A.J.,
RA Martin F., van Wyk J.J.;
RT "Nucleotide sequence analysis of a cDNA encoding human ubiquitin
RT reveals that ubiquitin is synthesized as a precursor.";
RL J. Biol. Chem. 260:7609-7613(1985).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-148.
RX PubMed=9582194;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [12]
RP FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, AND
RP MASS SPECTROMETRY.
RX PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018;
RA Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
RT "Differential regulation of EGF receptor internalization and
RT degradation by multiubiquitination within the kinase domain.";
RL Mol. Cell 21:737-748(2006).
RN [13]
RP UBIQUITINATION AT LYS-27.
RX PubMed=15466860; DOI=10.1074/jbc.M402916200;
RA Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.;
RT "Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B
RT contributes to neuritogenesis.";
RL J. Biol. Chem. 279:53533-53543(2004).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS
RP SPECTROMETRY.
RC TISSUE=Lung adenocarcinoma;
RX PubMed=17203973; DOI=10.1021/pr060438j;
RA Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,
RA Haines D.S., Figeys D.;
RT "The proteomic reactor facilitates the analysis of affinity-purified
RT proteins by mass spectrometry: application for identifying
RT ubiquitinated proteins in human cells.";
RL J. Proteome Res. 6:298-305(2007).
RN [15]
RP UBIQUITINATION AT LYS-63, AND MUTAGENESIS OF LYS-48 AND LYS-63.
RX PubMed=18719106; DOI=10.1073/pnas.0805685105;
RA Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X.,
RA Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
RT "Polyubiquitination of proliferating cell nuclear antigen by HLTF and
RT SHPRH prevents genomic instability from stalled replication forks.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
RN [16]
RP REVIEW, AND FUNCTION.
RX PubMed=19754430; DOI=10.1042/BST0370937;
RA Komander D.;
RT "The emerging complexity of protein ubiquitination.";
RL Biochem. Soc. Trans. 37:937-953(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104 AND LYS-113, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC protein, or free (unanchored). When covalently bound, it is
CC conjugated to target proteins via an isopeptide bond either as a
CC monomer (monoubiquitin), a polymer linked via different Lys
CC residues of the ubiquitin (polyubiquitin chains) or a linear
CC polymer linked via the initiator Met of the ubiquitin (linear
CC polyubiquitin chains). Polyubiquitin chains, when attached to a
CC target protein, have different functions depending on the Lys
CC residue of the ubiquitin that is linked: Lys-6-linked may be
CC involved in DNA repair; Lys-11-linked is involved in ERAD
CC (endoplasmic reticulum-associated degradation) and in cell-cycle
CC regulation; Lys-29-linked is involved in lysosomal degradation;
CC Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC involved in protein degradation via the proteasome; Lys-63-linked
CC is involved in endocytosis, DNA-damage responses as well as in
CC signaling processes leading to activation of the transcription
CC factor NF-kappa-B. Linear polymer chains formed via attachment by
CC the initiator Met lead to cell signaling. Ubiquitin is usually
CC conjugated to Lys residues of target proteins, however, in rare
CC cases, conjugation to Cys or Ser residues has been observed. When
CC polyubiquitin is free (unanchored-polyubiquitin), it also has
CC distinct roles, such as in activation of protein kinases, and in
CC signaling.
CC -!- FUNCTION: Ribosomal protein S27a is a component of the 40S subunit
CC of the ribosome.
CC -!- SUBUNIT: Ribosomal protein S27a is part of the 40S ribosomal
CC subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm (By similarity).
CC Nucleus (By similarity).
CC -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. UBA52
CC and RPS27A genes code for a single copy of ubiquitin fused to the
CC ribosomal proteins L40 and S27a, respectively. UBB and UBC genes
CC code for a polyubiquitin precursor with exact head to tail
CC repeats, the number of repeats differ between species and strains.
CC -!- MISCELLANEOUS: For a better understanding, features related to
CC ubiquitin are only indicated for the first chain.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin
CC family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ribosomal
CC protein S27Ae family.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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DR EMBL; X63237; CAA44911.1; -; mRNA.
DR EMBL; S79522; AAB21188.1; -; mRNA.
DR EMBL; AC012358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001392; AAH01392.1; -; mRNA.
DR EMBL; BC066293; AAH66293.1; -; mRNA.
DR EMBL; AB062071; BAB79490.1; -; Genomic_DNA.
DR EMBL; M10939; AAA36788.1; -; mRNA.
DR EMBL; AB007163; BAA25826.1; -; Genomic_DNA.
DR RefSeq; NP_001129064.1; NM_001135592.2.
DR RefSeq; NP_001170884.1; NM_001177413.1.
DR RefSeq; NP_002945.1; NM_002954.5.
DR UniGene; Hs.311640; -.
DR UniGene; Hs.546292; -.
DR UniGene; Hs.743392; -.
DR PDB; 2KHW; NMR; -; B=1-76.
DR PDB; 2KOX; NMR; -; A=1-76.
DR PDB; 2KTF; NMR; -; A=1-76.
DR PDB; 2KWU; NMR; -; B=1-76.
DR PDB; 2KWV; NMR; -; B=1-76.
DR PDB; 2L0F; NMR; -; A=1-76.
DR PDB; 2L0T; NMR; -; A=1-76.
DR PDB; 2XK5; X-ray; 3.00 A; A/B=1-76.
DR PDB; 3AXC; X-ray; 2.19 A; A=1-76.
DR PDB; 3J3A; EM; 5.00 A; f=77-156.
DR PDB; 3K9P; X-ray; 2.80 A; B=1-76.
DR PDB; 3N30; X-ray; 3.00 A; A/B=1-76.
DR PDB; 3N32; X-ray; 1.80 A; A=1-76.
DR PDB; 3NHE; X-ray; 1.26 A; B=1-76.
DR PDB; 3NOB; X-ray; 2.19 A; A/B/C/D/E/F/G/H=1-76.
DR PDB; 3NS8; X-ray; 1.71 A; A/B=1-76.
DR PDB; 3PHD; X-ray; 3.00 A; E/F/G/H=1-76.
DR PDB; 3PHW; X-ray; 2.00 A; B/D/F/H=1-75.
DR PDB; 3TBL; X-ray; 2.90 A; D/E=1-76.
DR PDBsum; 2KHW; -.
DR PDBsum; 2KOX; -.
DR PDBsum; 2KTF; -.
DR PDBsum; 2KWU; -.
DR PDBsum; 2KWV; -.
DR PDBsum; 2L0F; -.
DR PDBsum; 2L0T; -.
DR PDBsum; 2XK5; -.
DR PDBsum; 3AXC; -.
DR PDBsum; 3J3A; -.
DR PDBsum; 3K9P; -.
DR PDBsum; 3N30; -.
DR PDBsum; 3N32; -.
DR PDBsum; 3NHE; -.
DR PDBsum; 3NOB; -.
DR PDBsum; 3NS8; -.
DR PDBsum; 3PHD; -.
DR PDBsum; 3PHW; -.
DR PDBsum; 3TBL; -.
DR ProteinModelPortal; P62979; -.
DR SMR; P62979; 1-76, 82-152.
DR IntAct; P62979; 13.
DR MINT; MINT-1138719; -.
DR STRING; 9606.ENSP00000272317; -.
DR PhosphoSite; P62979; -.
DR DMDM; 302393745; -.
DR UCD-2DPAGE; P02248; -.
DR PaxDb; P62979; -.
DR PRIDE; P62979; -.
DR DNASU; 6233; -.
DR Ensembl; ENST00000272317; ENSP00000272317; ENSG00000143947.
DR Ensembl; ENST00000402285; ENSP00000383981; ENSG00000143947.
DR Ensembl; ENST00000404735; ENSP00000385659; ENSG00000143947.
DR GeneID; 6233; -.
DR KEGG; hsa:6233; -.
DR UCSC; uc002ryk.3; human.
DR CTD; 6233; -.
DR GeneCards; GC02P055459; -.
DR H-InvDB; HIX0161861; -.
DR HGNC; HGNC:10417; RPS27A.
DR HPA; CAB033319; -.
DR HPA; HPA041344; -.
DR MIM; 191343; gene.
DR neXtProt; NX_P62979; -.
DR PharmGKB; PA34821; -.
DR eggNOG; COG5272; -.
DR HOVERGEN; HBG079148; -.
DR InParanoid; P62979; -.
DR KO; K02977; -.
DR OMA; MSILKYY; -.
DR OrthoDB; EOG7JDR1W; -.
DR PhylomeDB; P62979; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115202; Signal Transduction.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_118324; Disease.
DR Reactome; REACT_118381; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_13487; Ubiquitination of PAK-2p34.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_2001; Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_216; DNA Repair.
DR Reactome; REACT_24941; Circadian Clock.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6782; TRAF6 Mediated Induction of proinflammatory cytokines.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR Reactome; REACT_8017; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; REACT_81380; Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
DR Reactome; REACT_97910; Signal Transduction.
DR ChiTaRS; RPS27A; human.
DR EvolutionaryTrace; P62979; -.
DR GeneWiki; RPS27A; -.
DR GenomeRNAi; 6233; -.
DR NextBio; 24197; -.
DR PRO; PR:P62979; -.
DR ArrayExpress; P62979; -.
DR Bgee; P62979; -.
DR CleanEx; HS_RPS27A; -.
DR Genevestigator; P62979; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0006281; P:DNA repair; TAS:Reactome.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0007254; P:JNK cascade; TAS:Reactome.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0007220; P:Notch receptor processing; TAS:Reactome.
DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR GO; GO:0034166; P:toll-like receptor 10 signaling pathway; TAS:Reactome.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
DR GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
DR GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR InterPro; IPR002906; Ribosomal_S27a.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR019956; Ubiquitin.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR000626; Ubiquitin_dom.
DR Pfam; PF01599; Ribosomal_S27; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1 76 Ubiquitin.
FT /FTId=PRO_0000396477.
FT CHAIN 77 156 40S ribosomal protein S27a.
FT /FTId=PRO_0000396478.
FT DOMAIN 1 76 Ubiquitin-like.
FT ZN_FING 121 144 C4-type.
FT COMPBIAS 77 99 Lys-rich (highly basic).
FT BINDING 54 54 Activating enzyme.
FT BINDING 72 72 Activating enzyme.
FT SITE 68 68 Essential for function.
FT MOD_RES 104 104 N6-acetyllysine.
FT MOD_RES 113 113 N6-acetyllysine.
FT CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin)
FT (Probable).
FT CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin) (By
FT similarity).
FT CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys)
FT (interchain with K-? in acceptor
FT proteins).
FT MUTAGEN 48 48 K->R: No effect on HLTF-mediated
FT polyubiquitination of PCNA.
FT MUTAGEN 63 63 K->R: Abolishes HLTF-mediated
FT polyubiquitination of PCNA.
FT STRAND 2 6
FT TURN 8 10
FT STRAND 12 16
FT HELIX 23 34
FT HELIX 38 40
FT STRAND 41 45
FT HELIX 57 59
FT STRAND 66 71
SQ SEQUENCE 156 AA; 17965 MW; 617BC63DF3A904F7 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL AVLKYYKVDE NGKISRLRRE
CPSDECGAGV FMASHFDRHY CGKCCLTYCF NKPEDK
//
ID RS27A_HUMAN Reviewed; 156 AA.
AC P62979; P02248; P02249; P02250; P14798; P62988; Q29120; Q6LBL4;
read moreAC Q6LDU5; Q8WYN8; Q91887; Q91888; Q9BQ77; Q9BWD6; Q9BX98; Q9UEF2;
AC Q9UEG1; Q9UEK8; Q9UPK7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Ubiquitin-40S ribosomal protein S27a;
DE AltName: Full=Ubiquitin carboxyl extension protein 80;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=40S ribosomal protein S27a;
DE Flags: Precursor;
GN Name=RPS27A; Synonyms=UBA80, UBCEP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1657614; DOI=10.1002/eji.1830211113;
RA Pancre V., Pierce R.J., Fournier F., Mehtali M., Delanoye A.,
RA Capron A., Auriault C.;
RT "Effect of ubiquitin on platelet functions: possible identity with
RT platelet activity suppressive lymphokine (PASL).";
RL Eur. J. Immunol. 21:2735-2741(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1370760;
RA Adams S.M., Sharp M.G., Walker R.A., Brammar W.J., Varley J.M.;
RT "Differential expression of translation-associated genes in benign and
RT malignant human breast tumours.";
RL Br. J. Cancer 65:65-71(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-98.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
RA Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [6]
RP PROTEIN SEQUENCE OF 1-74.
RX PubMed=124018; DOI=10.1038/255423a0;
RA Schlesinger D.H., Goldstein G.;
RT "Hybrid troponin reconstituted from vertebrate and arthropod
RT subunits.";
RL Nature 255:423-424(1975).
RN [7]
RP PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11
RP AND LYS-48, AND MASS SPECTROMETRY.
RX PubMed=16443603; DOI=10.1074/jbc.M512786200;
RA Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.;
RT "Alzheimer disease-specific conformation of hyperphosphorylated paired
RT helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and
RT Lys-6 ubiquitin conjugation.";
RL J. Biol. Chem. 281:10825-10838(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative
RT analysis of 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-156.
RX PubMed=2581967;
RA Lund P.K., Moats-Staats B.M., Simmons J.G., Hoyt E., D'Ercole A.J.,
RA Martin F., van Wyk J.J.;
RT "Nucleotide sequence analysis of a cDNA encoding human ubiquitin
RT reveals that ubiquitin is synthesized as a precursor.";
RL J. Biol. Chem. 260:7609-7613(1985).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-148.
RX PubMed=9582194;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [12]
RP FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, AND
RP MASS SPECTROMETRY.
RX PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018;
RA Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
RT "Differential regulation of EGF receptor internalization and
RT degradation by multiubiquitination within the kinase domain.";
RL Mol. Cell 21:737-748(2006).
RN [13]
RP UBIQUITINATION AT LYS-27.
RX PubMed=15466860; DOI=10.1074/jbc.M402916200;
RA Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.;
RT "Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B
RT contributes to neuritogenesis.";
RL J. Biol. Chem. 279:53533-53543(2004).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS
RP SPECTROMETRY.
RC TISSUE=Lung adenocarcinoma;
RX PubMed=17203973; DOI=10.1021/pr060438j;
RA Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,
RA Haines D.S., Figeys D.;
RT "The proteomic reactor facilitates the analysis of affinity-purified
RT proteins by mass spectrometry: application for identifying
RT ubiquitinated proteins in human cells.";
RL J. Proteome Res. 6:298-305(2007).
RN [15]
RP UBIQUITINATION AT LYS-63, AND MUTAGENESIS OF LYS-48 AND LYS-63.
RX PubMed=18719106; DOI=10.1073/pnas.0805685105;
RA Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X.,
RA Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
RT "Polyubiquitination of proliferating cell nuclear antigen by HLTF and
RT SHPRH prevents genomic instability from stalled replication forks.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
RN [16]
RP REVIEW, AND FUNCTION.
RX PubMed=19754430; DOI=10.1042/BST0370937;
RA Komander D.;
RT "The emerging complexity of protein ubiquitination.";
RL Biochem. Soc. Trans. 37:937-953(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104 AND LYS-113, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC protein, or free (unanchored). When covalently bound, it is
CC conjugated to target proteins via an isopeptide bond either as a
CC monomer (monoubiquitin), a polymer linked via different Lys
CC residues of the ubiquitin (polyubiquitin chains) or a linear
CC polymer linked via the initiator Met of the ubiquitin (linear
CC polyubiquitin chains). Polyubiquitin chains, when attached to a
CC target protein, have different functions depending on the Lys
CC residue of the ubiquitin that is linked: Lys-6-linked may be
CC involved in DNA repair; Lys-11-linked is involved in ERAD
CC (endoplasmic reticulum-associated degradation) and in cell-cycle
CC regulation; Lys-29-linked is involved in lysosomal degradation;
CC Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC involved in protein degradation via the proteasome; Lys-63-linked
CC is involved in endocytosis, DNA-damage responses as well as in
CC signaling processes leading to activation of the transcription
CC factor NF-kappa-B. Linear polymer chains formed via attachment by
CC the initiator Met lead to cell signaling. Ubiquitin is usually
CC conjugated to Lys residues of target proteins, however, in rare
CC cases, conjugation to Cys or Ser residues has been observed. When
CC polyubiquitin is free (unanchored-polyubiquitin), it also has
CC distinct roles, such as in activation of protein kinases, and in
CC signaling.
CC -!- FUNCTION: Ribosomal protein S27a is a component of the 40S subunit
CC of the ribosome.
CC -!- SUBUNIT: Ribosomal protein S27a is part of the 40S ribosomal
CC subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm (By similarity).
CC Nucleus (By similarity).
CC -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. UBA52
CC and RPS27A genes code for a single copy of ubiquitin fused to the
CC ribosomal proteins L40 and S27a, respectively. UBB and UBC genes
CC code for a polyubiquitin precursor with exact head to tail
CC repeats, the number of repeats differ between species and strains.
CC -!- MISCELLANEOUS: For a better understanding, features related to
CC ubiquitin are only indicated for the first chain.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin
CC family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ribosomal
CC protein S27Ae family.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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DR EMBL; X63237; CAA44911.1; -; mRNA.
DR EMBL; S79522; AAB21188.1; -; mRNA.
DR EMBL; AC012358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001392; AAH01392.1; -; mRNA.
DR EMBL; BC066293; AAH66293.1; -; mRNA.
DR EMBL; AB062071; BAB79490.1; -; Genomic_DNA.
DR EMBL; M10939; AAA36788.1; -; mRNA.
DR EMBL; AB007163; BAA25826.1; -; Genomic_DNA.
DR RefSeq; NP_001129064.1; NM_001135592.2.
DR RefSeq; NP_001170884.1; NM_001177413.1.
DR RefSeq; NP_002945.1; NM_002954.5.
DR UniGene; Hs.311640; -.
DR UniGene; Hs.546292; -.
DR UniGene; Hs.743392; -.
DR PDB; 2KHW; NMR; -; B=1-76.
DR PDB; 2KOX; NMR; -; A=1-76.
DR PDB; 2KTF; NMR; -; A=1-76.
DR PDB; 2KWU; NMR; -; B=1-76.
DR PDB; 2KWV; NMR; -; B=1-76.
DR PDB; 2L0F; NMR; -; A=1-76.
DR PDB; 2L0T; NMR; -; A=1-76.
DR PDB; 2XK5; X-ray; 3.00 A; A/B=1-76.
DR PDB; 3AXC; X-ray; 2.19 A; A=1-76.
DR PDB; 3J3A; EM; 5.00 A; f=77-156.
DR PDB; 3K9P; X-ray; 2.80 A; B=1-76.
DR PDB; 3N30; X-ray; 3.00 A; A/B=1-76.
DR PDB; 3N32; X-ray; 1.80 A; A=1-76.
DR PDB; 3NHE; X-ray; 1.26 A; B=1-76.
DR PDB; 3NOB; X-ray; 2.19 A; A/B/C/D/E/F/G/H=1-76.
DR PDB; 3NS8; X-ray; 1.71 A; A/B=1-76.
DR PDB; 3PHD; X-ray; 3.00 A; E/F/G/H=1-76.
DR PDB; 3PHW; X-ray; 2.00 A; B/D/F/H=1-75.
DR PDB; 3TBL; X-ray; 2.90 A; D/E=1-76.
DR PDBsum; 2KHW; -.
DR PDBsum; 2KOX; -.
DR PDBsum; 2KTF; -.
DR PDBsum; 2KWU; -.
DR PDBsum; 2KWV; -.
DR PDBsum; 2L0F; -.
DR PDBsum; 2L0T; -.
DR PDBsum; 2XK5; -.
DR PDBsum; 3AXC; -.
DR PDBsum; 3J3A; -.
DR PDBsum; 3K9P; -.
DR PDBsum; 3N30; -.
DR PDBsum; 3N32; -.
DR PDBsum; 3NHE; -.
DR PDBsum; 3NOB; -.
DR PDBsum; 3NS8; -.
DR PDBsum; 3PHD; -.
DR PDBsum; 3PHW; -.
DR PDBsum; 3TBL; -.
DR ProteinModelPortal; P62979; -.
DR SMR; P62979; 1-76, 82-152.
DR IntAct; P62979; 13.
DR MINT; MINT-1138719; -.
DR STRING; 9606.ENSP00000272317; -.
DR PhosphoSite; P62979; -.
DR DMDM; 302393745; -.
DR UCD-2DPAGE; P02248; -.
DR PaxDb; P62979; -.
DR PRIDE; P62979; -.
DR DNASU; 6233; -.
DR Ensembl; ENST00000272317; ENSP00000272317; ENSG00000143947.
DR Ensembl; ENST00000402285; ENSP00000383981; ENSG00000143947.
DR Ensembl; ENST00000404735; ENSP00000385659; ENSG00000143947.
DR GeneID; 6233; -.
DR KEGG; hsa:6233; -.
DR UCSC; uc002ryk.3; human.
DR CTD; 6233; -.
DR GeneCards; GC02P055459; -.
DR H-InvDB; HIX0161861; -.
DR HGNC; HGNC:10417; RPS27A.
DR HPA; CAB033319; -.
DR HPA; HPA041344; -.
DR MIM; 191343; gene.
DR neXtProt; NX_P62979; -.
DR PharmGKB; PA34821; -.
DR eggNOG; COG5272; -.
DR HOVERGEN; HBG079148; -.
DR InParanoid; P62979; -.
DR KO; K02977; -.
DR OMA; MSILKYY; -.
DR OrthoDB; EOG7JDR1W; -.
DR PhylomeDB; P62979; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115202; Signal Transduction.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_118324; Disease.
DR Reactome; REACT_118381; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_13487; Ubiquitination of PAK-2p34.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_2001; Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_216; DNA Repair.
DR Reactome; REACT_24941; Circadian Clock.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6782; TRAF6 Mediated Induction of proinflammatory cytokines.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR Reactome; REACT_8017; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; REACT_81380; Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
DR Reactome; REACT_97910; Signal Transduction.
DR ChiTaRS; RPS27A; human.
DR EvolutionaryTrace; P62979; -.
DR GeneWiki; RPS27A; -.
DR GenomeRNAi; 6233; -.
DR NextBio; 24197; -.
DR PRO; PR:P62979; -.
DR ArrayExpress; P62979; -.
DR Bgee; P62979; -.
DR CleanEx; HS_RPS27A; -.
DR Genevestigator; P62979; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0006281; P:DNA repair; TAS:Reactome.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0007254; P:JNK cascade; TAS:Reactome.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0007220; P:Notch receptor processing; TAS:Reactome.
DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR GO; GO:0034166; P:toll-like receptor 10 signaling pathway; TAS:Reactome.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
DR GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
DR GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR InterPro; IPR002906; Ribosomal_S27a.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR019956; Ubiquitin.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR000626; Ubiquitin_dom.
DR Pfam; PF01599; Ribosomal_S27; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1 76 Ubiquitin.
FT /FTId=PRO_0000396477.
FT CHAIN 77 156 40S ribosomal protein S27a.
FT /FTId=PRO_0000396478.
FT DOMAIN 1 76 Ubiquitin-like.
FT ZN_FING 121 144 C4-type.
FT COMPBIAS 77 99 Lys-rich (highly basic).
FT BINDING 54 54 Activating enzyme.
FT BINDING 72 72 Activating enzyme.
FT SITE 68 68 Essential for function.
FT MOD_RES 104 104 N6-acetyllysine.
FT MOD_RES 113 113 N6-acetyllysine.
FT CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin)
FT (Probable).
FT CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin) (By
FT similarity).
FT CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys)
FT (interchain with K-? in acceptor
FT proteins).
FT MUTAGEN 48 48 K->R: No effect on HLTF-mediated
FT polyubiquitination of PCNA.
FT MUTAGEN 63 63 K->R: Abolishes HLTF-mediated
FT polyubiquitination of PCNA.
FT STRAND 2 6
FT TURN 8 10
FT STRAND 12 16
FT HELIX 23 34
FT HELIX 38 40
FT STRAND 41 45
FT HELIX 57 59
FT STRAND 66 71
SQ SEQUENCE 156 AA; 17965 MW; 617BC63DF3A904F7 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL AVLKYYKVDE NGKISRLRRE
CPSDECGAGV FMASHFDRHY CGKCCLTYCF NKPEDK
//
MIM
191343
*RECORD*
*FIELD* NO
191343
*FIELD* TI
*191343 RIBOSOMAL PROTEIN S27a; RPS27A
;;UBIQUITIN A-80-RESIDUE RIBOSOMAL PROTEIN FUSION PRODUCT; UBA80;;
read moreHUMAN UBIQUITIN CARBOXYL EXTENSION PROTEIN, 80-RESIDUE; HUBCEP80;
CEP80;;
UBIQUITIN CARBOXYL EXTENSION PROTEIN 1; UBCEP1
*FIELD* TX
Ubiquitin is a highly conserved 76-amino acid protein that plays a key
role in protein degradation. Ubiquitin is synthesized as precursor
proteins that consist either of polyubiquitin chains that are cleaved
into moieties of the UBB (191339) or UBC (191340) types, or single
ubiquitin moieties fused 5-prime to unrelated carboxyl extension
proteins (UBA type) such as UBA52 (191321) and UBA80 (RPS27A).
CLONING
By screening a liver cDNA library with probes for IGF1 (147440), Lund et
al. (1985) obtained a partial cDNA encoding all but the N-terminal 4
amino acids of RPS27A. The deduced 156-amino acid protein contains
ubiquitin plus an 80-residue C-terminal extension. Northern blot
analysis revealed expression of an 0.6-kb transcript in liver and
mammary carcinoma cells.
Pancre et al. (1991) obtained a full-length cDNA encoding RPS27A by
screening a Jurkat cDNA library for a platelet activity suppressive
lymphokine.
Using differential screening of mammary carcinoma and fibroadenoma
tumors, Adams et al. (1992) isolated a cDNA encoding RPS27A, which they
called HUBCEP80. They detected higher levels of RPS27A in nonmalignant
fibroadenoma.
BIOCHEMICAL FEATURES
Monia et al. (1989) developed a system for expression of human ubiquitin
carboxyl extension proteins in prokaryotic and eukaryotic hosts. When
expressed in Saccharomyces cerevisiae, the intact proteins were rapidly
processed to free ubiquitin monomer and extension protein. Furthermore,
expression in this host conferred a slow growth phenotype mediated by
the extension protein. Expression in E. coli did not result in
processing of the fusion proteins. However, when the expressed fusion
proteins were purified from E. coli and incubated with a rabbit
reticulocyte extract, the proteins were rapidly processed to free
ubiquitin monomer and extension protein. These results showed that human
ubiquitin carboxyl extension proteins are processed to ubiquitin and
extension protein when expressed in eukaryotic but not prokaryotic cells
and that pre- and cotranslational events are not necessary for their
processing.
GENE STRUCTURE
By PCR and YAC analysis, Kirschner and Stratakis (2000) determined that
the RPS27A gene contains 6 exons, with the initiator ATG in exon 2, and
spans approximately 2.9 kb. Promoter analysis identified a GC-rich
region with an SP1 box but no TATA or CAAT boxes.
MAPPING
By radiation hybrid and physical mapping analyses, Kirschner and
Stratakis (2000) mapped the RPS27A gene to 2p16. They identified a
pseudogene on chromosome 17.
*FIELD* RF
1. Adams, S. M.; Sharp, M. G. F.; Walker, R. A.; Brammar, W. J.; Varley,
J. M.: Differential expression of translation-associated genes in
benign and malignant human breast tumours. Brit. J. Cancer 65: 65-71,
1992.
2. Kirschner, L. S.; Stratakis, C. A.: Structure of the human ubiquitin
fusion gene Uba80 (RPS27a) and one of its pseudogenes. Biochem. Biophys.
Res. Commun. 270: 1106-1110, 2000.
3. 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.
4. Monia, B. P.; Ecker, D. J.; Jonnalagadda, S.; Marsh, J.; Gotlib,
L.; Butt, T. R.; Crooke, S. T.: Gene synthesis, expression, and processing
of human ubiquitin carboxyl extension proteins. J. Biol. Chem. 264:
4093-4103, 1989.
5. 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). Europ.
J. Immun. 21: 2735-2741, 1991.
*FIELD* CN
Paul J. Converse - reorganized: 9/13/2001
Paul J. Converse - updated: 9/13/2001
*FIELD* CD
Victor A. McKusick: 6/7/1994
*FIELD* ED
carol: 05/12/2004
alopez: 3/11/2003
mgross: 9/13/2001
joanna: 9/12/2001
mark: 2/20/1997
jason: 6/7/1994
*RECORD*
*FIELD* NO
191343
*FIELD* TI
*191343 RIBOSOMAL PROTEIN S27a; RPS27A
;;UBIQUITIN A-80-RESIDUE RIBOSOMAL PROTEIN FUSION PRODUCT; UBA80;;
read moreHUMAN UBIQUITIN CARBOXYL EXTENSION PROTEIN, 80-RESIDUE; HUBCEP80;
CEP80;;
UBIQUITIN CARBOXYL EXTENSION PROTEIN 1; UBCEP1
*FIELD* TX
Ubiquitin is a highly conserved 76-amino acid protein that plays a key
role in protein degradation. Ubiquitin is synthesized as precursor
proteins that consist either of polyubiquitin chains that are cleaved
into moieties of the UBB (191339) or UBC (191340) types, or single
ubiquitin moieties fused 5-prime to unrelated carboxyl extension
proteins (UBA type) such as UBA52 (191321) and UBA80 (RPS27A).
CLONING
By screening a liver cDNA library with probes for IGF1 (147440), Lund et
al. (1985) obtained a partial cDNA encoding all but the N-terminal 4
amino acids of RPS27A. The deduced 156-amino acid protein contains
ubiquitin plus an 80-residue C-terminal extension. Northern blot
analysis revealed expression of an 0.6-kb transcript in liver and
mammary carcinoma cells.
Pancre et al. (1991) obtained a full-length cDNA encoding RPS27A by
screening a Jurkat cDNA library for a platelet activity suppressive
lymphokine.
Using differential screening of mammary carcinoma and fibroadenoma
tumors, Adams et al. (1992) isolated a cDNA encoding RPS27A, which they
called HUBCEP80. They detected higher levels of RPS27A in nonmalignant
fibroadenoma.
BIOCHEMICAL FEATURES
Monia et al. (1989) developed a system for expression of human ubiquitin
carboxyl extension proteins in prokaryotic and eukaryotic hosts. When
expressed in Saccharomyces cerevisiae, the intact proteins were rapidly
processed to free ubiquitin monomer and extension protein. Furthermore,
expression in this host conferred a slow growth phenotype mediated by
the extension protein. Expression in E. coli did not result in
processing of the fusion proteins. However, when the expressed fusion
proteins were purified from E. coli and incubated with a rabbit
reticulocyte extract, the proteins were rapidly processed to free
ubiquitin monomer and extension protein. These results showed that human
ubiquitin carboxyl extension proteins are processed to ubiquitin and
extension protein when expressed in eukaryotic but not prokaryotic cells
and that pre- and cotranslational events are not necessary for their
processing.
GENE STRUCTURE
By PCR and YAC analysis, Kirschner and Stratakis (2000) determined that
the RPS27A gene contains 6 exons, with the initiator ATG in exon 2, and
spans approximately 2.9 kb. Promoter analysis identified a GC-rich
region with an SP1 box but no TATA or CAAT boxes.
MAPPING
By radiation hybrid and physical mapping analyses, Kirschner and
Stratakis (2000) mapped the RPS27A gene to 2p16. They identified a
pseudogene on chromosome 17.
*FIELD* RF
1. Adams, S. M.; Sharp, M. G. F.; Walker, R. A.; Brammar, W. J.; Varley,
J. M.: Differential expression of translation-associated genes in
benign and malignant human breast tumours. Brit. J. Cancer 65: 65-71,
1992.
2. Kirschner, L. S.; Stratakis, C. A.: Structure of the human ubiquitin
fusion gene Uba80 (RPS27a) and one of its pseudogenes. Biochem. Biophys.
Res. Commun. 270: 1106-1110, 2000.
3. 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.
4. Monia, B. P.; Ecker, D. J.; Jonnalagadda, S.; Marsh, J.; Gotlib,
L.; Butt, T. R.; Crooke, S. T.: Gene synthesis, expression, and processing
of human ubiquitin carboxyl extension proteins. J. Biol. Chem. 264:
4093-4103, 1989.
5. 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). Europ.
J. Immun. 21: 2735-2741, 1991.
*FIELD* CN
Paul J. Converse - reorganized: 9/13/2001
Paul J. Converse - updated: 9/13/2001
*FIELD* CD
Victor A. McKusick: 6/7/1994
*FIELD* ED
carol: 05/12/2004
alopez: 3/11/2003
mgross: 9/13/2001
joanna: 9/12/2001
mark: 2/20/1997
jason: 6/7/1994