P42677 (RS27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
40S ribosomal protein S27

Alternative name(s):
Metallopan-stimulin 1
Short name=MPS-1

Gene names

Name:	RPS27
Synonyms:	MPS1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	84 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell proliferation Non-traceable author statement Ref.1. Source: UniProtKB endocrine pancreas development Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome mitotic prometaphase Traceable author statement. Source: Reactome translational elongation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome
Cellular component	cytosolic small ribosomal subunit Inferred from direct assay Ref.5. Source: UniProtKB nucleus Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	DNA binding Non-traceable author statement Ref.2. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct structural constituent of ribosome Inferred from electronic annotation. Source: InterPro zinc ion binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MDM2	Q00987	5	EBI-356336,EBI-389668

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 84	83	40S ribosomal protein S27		PRO_0000149051
Regions
	Zinc finger	37 – 59	23	C4-type
Amino acid modifications
	Modified residue	5	1	N6-acetyllysine Ref.13
	Modified residue	11	1	Phosphoserine Ref.7 Ref.9 Ref.10
	Modified residue	27	1	Phosphoserine Ref.9 Ref.12
	Modified residue	30	1	Phosphoserine Ref.12
	Modified residue	31	1	Phosphotyrosine Ref.8 Ref.11
	Modified residue	78	1	Phosphoserine Ref.7 Ref.9 Ref.12
Experimental info
	Sequence conflict	5	1	K → R AA sequence Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P42677 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 242C4466AC8A8900	FASTA	84	9,461
	10 20 30 40 50 60 MPLAKDLLHP SPEEEKRKHK KKRLVQSPNS YFMDVKCPGC YKITTVFSHA QTVVLCVGCS 70 80 TVLCQPTGGK ARLTEGCSFR RKQH

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00397358.
PIR	A48045.
RefSeq	NP_001021.1. NM_001030.4.
UniGene	Hs.546291. Hs.654475.
3D structure databases
ProteinModelPortal	P42677.
SMR	P42677. Positions 31-80.
ModBase	Search...
Protein-protein interaction databases
IntAct	P42677. 9 interactions.
MINT	MINT-1147961.
STRING	P42677.
PTM databases
PhosphoSite	P42677.
Polymorphism databases
DMDM	1171014.
Proteomic databases
PRIDE	P42677.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000368567; ENSP00000357555; ENSG00000177954.
GeneID	6232.
KEGG	hsa:6232.
UCSC	uc001fdv.1. human.
Organism-specific databases
CTD	6232.
GeneCards	GC01P153963.
H-InvDB	HIX0001098. HIX0033569.
HGNC	HGNC:10416. RPS27.
MIM	603702. gene.
neXtProt	NX_P42677.
PharmGKB	PA34820.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG000252.
InParanoid	P42677.
OMA	NCQTLLC.
OrthoDB	EOG4H19XB.
PhylomeDB	P42677.
Enzyme and pathway databases
Reactome	REACT_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
Bgee	P42677.
CleanEx	HS_RPS27.
Genevestigator	P42677.
GermOnline	ENSG00000130041. Homo sapiens. ENSG00000177954. Homo sapiens.
Family and domain databases
InterPro	IPR000592. Ribosomal_S27e. IPR023407. Ribosomal_S27e_Zn-bd_dom. IPR011332. Ribosomal_zn-bd_dom. [Graphical view]
Gene3D	G3DSA:2.20.25.100. G3DSA:2.20.25.100. 1 hit.
KO	K02978.
PANTHER	PTHR11594. Ribosomal_S27E. 1 hit.
Pfam	PF01667. Ribosomal_S27e. 1 hit. [Graphical view]
ProDom	PD004466. Ribosomal_S27e. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF57829. Ribosomal_zn-bd. 1 hit.
PROSITE	PS01168. RIBOSOMAL_S27E. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	24193.
SOURCE	Search...

Entry information

Entry name

RS27_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.