Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0CW22 (RS17L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S17-like
Gene names
Name:RPS17L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein S17e family.

Ontologies

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 13513440S ribosomal protein S17-like HAMAP-Rule MF_00511
PRO_0000410726

Amino acid modifications

Modified residue1131Phosphoserine Ref.2 Ref.4 Ref.5 Ref.7
Modified residue1301Phosphothreonine Ref.2 Ref.5

Sequences

Sequence LengthMass (Da)Tools
P0CW22 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 299AD605C5401325

FASTA13515,550
        10         20         30         40         50         60 
MGRVRTKTVK KAARVIIEKY YTRLGNDFHT NKRVCEEIAI IPSKKLRNKI AGYVTHLMKR 

        70         80         90        100        110        120 
IQRGPVRGIS IKLQEEERER RDNYVPEVSA LDQEIIEVDP DTKEMLKLLD FGSLSNLQVT 

       130 
QPTVGMNFKT PRGPV 

« Hide

References

[1]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND THR-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[3]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[4]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[5]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND THR-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC010724 Genomic DNA. No translation available.
RefSeqNP_001012.1. NM_001021.4.
UniGeneHs.433427.
Hs.512525.

3D structure databases

ProteinModelPortalP0CW22.
SMRP0CW22. Positions 1-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112132. 94 interactions.
1527840. 14 interactions.
IntActP0CW22. 1 interaction.
MINTMINT-8395037.

PTM databases

PhosphoSiteP0CW22.

Polymorphism databases

DMDM338819320.

Proteomic databases

PRIDEP0CW22.

Protocols and materials databases

DNASU6218.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330244; ENSP00000346046; ENSG00000182774.
GeneID6218.
KEGGhsa:100505503.
hsa:6218.
UCSCuc002bhr.1. human.

Organism-specific databases

CTD6218.
GeneCardsGC15M083202.
HGNCHGNC:40029. RPS17L.
HPAHPA055060.
neXtProtNX_P0CW22.
GenAtlasSearch...

Phylogenomic databases

KOK02962.
OrthoDBEOG72C52C.
PhylomeDBP0CW22.
TreeFamTF317992.

Gene expression databases

BgeeP0CW22.

Family and domain databases

Gene3D1.10.60.20. 1 hit.
HAMAPMF_00511. Ribosomal_S17e.
InterProIPR001210. Ribosomal_S17e.
IPR018273. Ribosomal_S17e_CS.
[Graphical view]
PANTHERPTHR10732. PTHR10732. 1 hit.
PfamPF00833. Ribosomal_S17e. 1 hit.
[Graphical view]
SUPFAMSSF116820. SSF116820. 1 hit.
PROSITEPS00712. RIBOSOMAL_S17E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPS17L. human.
NextBio24145.
PROP0CW22.

Entry information

Entry nameRS17L_HUMAN
AccessionPrimary (citable) accession number: P0CW22
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 29 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM