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P42677 (RS27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S27
Alternative name(s):
Metallopan-stimulin 1
Short name=MPS-1
Gene names
Name:RPS27
Synonyms:MPS1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length84 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Cofactor

Binds 1 zinc ion per subunit Potential.

Tissue specificity

Expressed in a wide variety of actively proliferating cells and tumor tissues.

Sequence similarities

Belongs to the ribosomal protein S27e family.

Caution

Was originally (Ref.1) thought to be a protein that could have played a role as a potentially important mediator of cellular proliferative responses to various growth factors and other environmental signals. Capable of specific binding to a cAMP response element in DNA.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MDM2Q009875EBI-356336,EBI-389668

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 848340S ribosomal protein S27
PRO_0000149051

Regions

Zinc finger37 – 5923C4-type

Amino acid modifications

Modified residue51N6-acetyllysine Ref.13
Modified residue111Phosphoserine Ref.7 Ref.9 Ref.10
Modified residue271Phosphoserine Ref.9 Ref.12
Modified residue301Phosphoserine Ref.12
Modified residue311Phosphotyrosine Ref.8 Ref.11
Modified residue781Phosphoserine Ref.7 Ref.9 Ref.12

Experimental info

Sequence conflict51K → R AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P42677 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 242C4466AC8A8900

FASTA849,461
        10         20         30         40         50         60 
MPLAKDLLHP SPEEEKRKHK KKRLVQSPNS YFMDVKCPGC YKITTVFSHA QTVVLCVGCS 

        70         80 
TVLCQPTGGK ARLTEGCSFR RKQH 

« Hide

References

« Hide 'large scale' references
[1]"A growth factor-inducible gene encodes a novel nuclear protein with zinc finger structure."
Fernandez-Pol J.A., Klos D.J., Hamilton P.D.
J. Biol. Chem. 268:21198-21204(1993) [PubMed: 8407955] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary carcinoma.
[2]"Primary structures and sequence analysis of human ribosomal proteins L39 and S27."
Tsui S.K.W., Lee S.M.Y., Fung K.P., Waye M.M.Y., Lee C.Y.
Biochem. Mol. Biol. Int. 40:611-616(1996) [PubMed: 8908372] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[3]"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].
[4]"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: Uterus.
[5]"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 2-11.
[6]"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 6-74.
[7]"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-11 AND SER-78, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-31, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-27 AND SER-78, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-31, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[12]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-30 AND SER-78, MASS SPECTROMETRY.
[13]"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-5, MASS SPECTROMETRY.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19739 mRNA. Translation: AAA59867.1.
U57847 mRNA. Translation: AAB02266.1.
AB061845 Genomic DNA. Translation: BAB79483.1.
BC002658 mRNA. Translation: AAH02658.1.
BC070219 mRNA. Translation: AAH70219.1.
AB007162 Genomic DNA. Translation: BAA25825.1.
IPIIPI00397358.
PIRA48045.
RefSeqNP_001021.1. NM_001030.4.
UniGeneHs.546291.
Hs.654475.

3D structure databases

ProteinModelPortalP42677.
SMRP42677. Positions 31-80.
ModBaseSearch...

Protein-protein interaction databases

IntActP42677. 9 interactions.
MINTMINT-1147961.
STRINGP42677.

PTM databases

PhosphoSiteP42677.

Polymorphism databases

DMDM1171014.

Proteomic databases

PRIDEP42677.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368567; ENSP00000357555; ENSG00000177954.
GeneID6232.
KEGGhsa:6232.
UCSCuc001fdv.1. human.

Organism-specific databases

CTD6232.
GeneCardsGC01P153963.
H-InvDBHIX0001098.
HIX0033569.
HGNCHGNC:10416. RPS27.
MIM603702. gene.
neXtProtNX_P42677.
PharmGKBPA34820.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG000252.
InParanoidP42677.
OMANCQTLLC.
OrthoDBEOG4H19XB.
PhylomeDBP42677.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111217. Metabolism.
REACT_152. Cell Cycle, Mitotic.
REACT_15380. Diabetes pathways.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_383. DNA Replication.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

BgeeP42677.
CleanExHS_RPS27.
GenevestigatorP42677.
GermOnlineENSG00000130041. Homo sapiens.
ENSG00000177954. Homo sapiens.

Family and domain databases

InterProIPR000592. Ribosomal_S27e.
IPR023407. Ribosomal_S27e_Zn-bd_dom.
IPR011332. Ribosomal_zn-bd_dom.
[Graphical view]
Gene3DG3DSA:2.20.25.100. G3DSA:2.20.25.100. 1 hit.
KOK02978.
PANTHERPTHR11594. Ribosomal_S27E. 1 hit.
PfamPF01667. Ribosomal_S27e. 1 hit.
[Graphical view]
ProDomPD004466. Ribosomal_S27e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF57829. Ribosomal_zn-bd. 1 hit.
PROSITEPS01168. RIBOSOMAL_S27E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio24193.
SOURCESearch...

Entry information

Entry nameRS27_HUMAN
AccessionPrimary (citable) accession number: P42677
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

Ribosomal proteins

Ribosomal proteins families and list of entries

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families