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Reviewed, UniProtKB/Swiss-Prot P62979 (RS27A_HUMAN)

Last modified February 9, 2010. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    40S ribosomal protein S27a
Gene names
Name: RPS27A
Synonyms: UBA80, UBCEP1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length80 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Miscellaneous

This ribosomal protein is synthesized as a C-terminal extension protein (CEP) of ubiquitin.

Sequence similarities

Belongs to the ribosomal protein S27Ae family.

Ontologies

Keywords
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processtranslational elongation

Inferred from Experiment. Source: Reactome

   Cellular componentcytosolic small ribosomal subunit Ref.6

Inferred from direct assay. Source: UniProtKB

   Molecular functionstructural constituent of ribosome

Inferred from direct assay. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 808040S ribosomal protein S27a
PRO_0000137662

Regions

Zinc finger45 – 6824C4-type
Compositional bias1 – 2323Lys-rich (highly basic)

Amino acid modifications

Modified residue281N6-acetyllysine Ref.9
Modified residue311N6-acetyllysine Ref.9
Modified residue371N6-acetyllysine Ref.9

Sequences

Sequence LengthMass (Da)Tools
P62979-1 [UniParc].

Last modified August 31, 2004. Version 1.
Checksum: 5233F54BB6F9DC1B

FASTA809,418
        10         20         30         40         50         60 
AKKRKKKSYT TPKKNKHKRK KVKLAVLKYY KVDENGKISR LRRECPSDEC GAGVFMASHF 

        70         80 
DRHYCGKCCL TYCFNKPEDK 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"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].
[3]"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].
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta and Urinary bladder.
[6]"Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
Eur. J. Biochem. 239:144-149(1996) [PubMed: 8706699] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-22.
Tissue: Placenta.
[7]"A map of 75 human ribosomal protein genes."
Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
Genome Res. 8:509-523(1998) [PubMed: 9582194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-72.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-31 AND LYS-37, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10939 mRNA. Translation: AAA36788.1. Different initiation.
X63237 mRNA. Translation: CAA44911.1. Different initiation.
S79522 mRNA. Translation: AAB21188.1. Different initiation.
AC012358 Genomic DNA. No translation available.
BC001392 mRNA. Translation: AAH01392.1. Different initiation.
BC066293 mRNA. Translation: AAH66293.1. Different initiation.
AB007163 Genomic DNA. Translation: BAA25826.1.
IPIIPI00179330.
RefSeqNP_001129064.1.
NP_002945.1.
UniGeneHs.311640
Hs.546292

3D structure databases

SMRP62979. Positions 24-79.
ModBaseSearch...

Protein-protein interaction databases

IntActP62979. 7 interactions.
STRINGP62979.

Proteomic databases

PRIDEP62979.

Genome annotation databases

EnsemblENST00000272317; ENSP00000272317; ENSG00000143947; Homo sapiens. [Genome view]
ENST00000402285; ENSP00000383981; ENSG00000143947; Homo sapiens. [Genome view]
ENST00000404735; ENSP00000385659; ENSG00000143947; Homo sapiens. [Genome view]
GeneID6233.
KEGGhsa:6233.
UCSCuc002ryk.1. human.

Organism-specific databases

CTD6233.
GeneCardsGC01P190932.
GC02P055313.
GC06P114010.
H-InvDBHIX0002061.
HGNCHGNC:10417. RPS27A.
MIM191343. gene.
PharmGKBPA34821.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG20257.
InParanoidP62979.
PhylomeDBP62979.

Enzyme and pathway databases

ReactomeREACT_15380. Diabetes pathways.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP62979.
BgeeP62979.
CleanExHS_RPS27A.
GenevestigatorP62979.
GermOnlineENSG00000143947. Homo sapiens.

Family and domain databases

InterProIPR002906. Ribosomal_S27a.
[Graphical view]
PfamPF01599. Ribosomal_S27. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameRS27A_HUMAN
AccessionPrimary (citable) accession number: P62979
Secondary accession number(s): P14798, Q6LBL4, Q9BQ77
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: February 9, 2010
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

MIM cross-references

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

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents