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Protein

40S ribosomal protein S17-like

Gene

RPS17L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S17-like
Gene namesi
Name:RPS17L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:40029. RPS17L.

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi338819320.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 13513440S ribosomal protein S17-likePRO_0000410726Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131Phosphoserine4 Publications
Modified residuei130 – 1301Phosphothreonine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP0CW22.
PRIDEiP0CW22.

PTM databases

PhosphoSiteiP0CW22.

Expressioni

Gene expression databases

BgeeiP0CW22.
ExpressionAtlasiP0CW22. baseline.

Organism-specific databases

HPAiHPA055060.

Interactioni

Protein-protein interaction databases

BioGridi112132. 77 interactions.
1527840. 16 interactions.
IntActiP0CW22. 3 interactions.
MINTiMINT-8395037.

Structurei

3D structure databases

ProteinModelPortaliP0CW22.
SMRiP0CW22. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S17e family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000006548.
InParanoidiP0CW22.
KOiK02962.
OrthoDBiEOG72C52C.
PhylomeDBiP0CW22.
TreeFamiTF317992.

Family and domain databases

Gene3Di1.10.60.20. 1 hit.
HAMAPiMF_00511. Ribosomal_S17e.
InterProiIPR001210. Ribosomal_S17e.
IPR018273. Ribosomal_S17e_CS.
[Graphical view]
PANTHERiPTHR10732. PTHR10732. 1 hit.
PfamiPF00833. Ribosomal_S17e. 1 hit.
[Graphical view]
SUPFAMiSSF116820. SSF116820. 1 hit.
PROSITEiPS00712. RIBOSOMAL_S17E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0CW22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRVRTKTVK KAARVIIEKY YTRLGNDFHT NKRVCEEIAI IPSKKLRNKI
60 70 80 90 100
AGYVTHLMKR IQRGPVRGIS IKLQEEERER RDNYVPEVSA LDQEIIEVDP
110 120 130
DTKEMLKLLD FGSLSNLQVT QPTVGMNFKT PRGPV
Length:135
Mass (Da):15,550
Last modified:June 28, 2011 - v1
Checksum:i299AD605C5401325
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC010724 Genomic DNA. No translation available.
RefSeqiNP_001012.1. NM_001021.4.
UniGeneiHs.433427.
Hs.512525.

Genome annotation databases

GeneIDi6218.
KEGGihsa:6218.
UCSCiuc002bhr.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC010724 Genomic DNA. No translation available.
RefSeqiNP_001012.1. NM_001021.4.
UniGeneiHs.433427.
Hs.512525.

3D structure databases

ProteinModelPortaliP0CW22.
SMRiP0CW22. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112132. 77 interactions.
1527840. 16 interactions.
IntActiP0CW22. 3 interactions.
MINTiMINT-8395037.

PTM databases

PhosphoSiteiP0CW22.

Polymorphism and mutation databases

DMDMi338819320.

Proteomic databases

MaxQBiP0CW22.
PRIDEiP0CW22.

Protocols and materials databases

DNASUi6218.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6218.
KEGGihsa:6218.
UCSCiuc002bhr.1. human.

Organism-specific databases

CTDi6218.
GeneCardsiGC15M083202.
HGNCiHGNC:40029. RPS17L.
HPAiHPA055060.
neXtProtiNX_P0CW22.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000006548.
InParanoidiP0CW22.
KOiK02962.
OrthoDBiEOG72C52C.
PhylomeDBiP0CW22.
TreeFamiTF317992.

Miscellaneous databases

ChiTaRSiRPS17L. human.
NextBioi24145.
PROiP0CW22.

Gene expression databases

BgeeiP0CW22.
ExpressionAtlasiP0CW22. baseline.

Family and domain databases

Gene3Di1.10.60.20. 1 hit.
HAMAPiMF_00511. Ribosomal_S17e.
InterProiIPR001210. Ribosomal_S17e.
IPR018273. Ribosomal_S17e_CS.
[Graphical view]
PANTHERiPTHR10732. PTHR10732. 1 hit.
PfamiPF00833. Ribosomal_S17e. 1 hit.
[Graphical view]
SUPFAMiSSF116820. SSF116820. 1 hit.
PROSITEiPS00712. RIBOSOMAL_S17E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND THR-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  3. 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. 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].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRS17L_HUMAN
AccessioniPrimary (citable) accession number: P0CW22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: April 29, 2015
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.