Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P63276

- RS17_MOUSE

UniProt

P63276 - RS17_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

40S ribosomal protein S17

Gene

Rps17

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: Ensembl
  2. structural constituent of ribosome Source: MGI

GO - Biological processi

  1. erythrocyte homeostasis Source: Ensembl
  2. ribosomal small subunit assembly Source: RefGenome
  3. rRNA processing Source: Ensembl
  4. translation Source: MGI
  5. translational elongation Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_231519. Eukaryotic Translation Termination.
REACT_236458. Ribosomal scanning and start codon recognition.
REACT_249044. Formation of a pool of free 40S subunits.
REACT_249316. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_253640. Peptide chain elongation.
REACT_256488. Translation initiation complex formation.
REACT_259469. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_262078. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S17
Gene namesi
Name:Rps17
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1309526. Rps17.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: MGI
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 13513440S ribosomal protein S17PRO_0000141526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191N6-succinyllysine1 Publication
Modified residuei113 – 1131PhosphoserineBy similarity
Modified residuei130 – 1301PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP63276.
PaxDbiP63276.
PRIDEiP63276.

PTM databases

PhosphoSiteiP63276.

Expressioni

Gene expression databases

BgeeiP63276.
CleanExiMM_RPS17.
ExpressionAtlasiP63276. baseline and differential.
GenevestigatoriP63276.

Interactioni

Protein-protein interaction databases

BioGridi203005. 9 interactions.

Structurei

3D structure databases

ProteinModelPortaliP63276.
SMRiP63276. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S17e family.Curated

Phylogenomic databases

eggNOGiCOG1383.
HOVERGENiHBG001708.
InParanoidiP63276.
KOiK02962.
OMAiFTTHLMR.
OrthoDBiEOG72C52C.
PhylomeDBiP63276.
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.

P63276-1 [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 PRGAV
Length:135
Mass (Da):15,524
Last modified:January 23, 2007 - v2
Checksum:i29806605C5401325
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D25213 mRNA. Translation: BAA04943.1.
AK007992 mRNA. Translation: BAB25394.1.
AK010647 mRNA. Translation: BAB27087.1.
BC002044 mRNA. No translation available.
BC081466 mRNA. Translation: AAH81466.1.
CCDSiCCDS40006.1.
RefSeqiNP_033118.1. NM_009092.3.
UniGeneiMm.42767.
Mm.431314.

Genome annotation databases

EnsembliENSMUST00000080813; ENSMUSP00000079628; ENSMUSG00000061787.
GeneIDi20068.
KEGGimmu:20068.
UCSCiuc009ibv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D25213 mRNA. Translation: BAA04943.1 .
AK007992 mRNA. Translation: BAB25394.1 .
AK010647 mRNA. Translation: BAB27087.1 .
BC002044 mRNA. No translation available.
BC081466 mRNA. Translation: AAH81466.1 .
CCDSi CCDS40006.1.
RefSeqi NP_033118.1. NM_009092.3.
UniGenei Mm.42767.
Mm.431314.

3D structure databases

ProteinModelPortali P63276.
SMRi P63276. Positions 1-129.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203005. 9 interactions.

PTM databases

PhosphoSitei P63276.

Proteomic databases

MaxQBi P63276.
PaxDbi P63276.
PRIDEi P63276.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000080813 ; ENSMUSP00000079628 ; ENSMUSG00000061787 .
GeneIDi 20068.
KEGGi mmu:20068.
UCSCi uc009ibv.1. mouse.

Organism-specific databases

CTDi 6218.
MGIi MGI:1309526. Rps17.

Phylogenomic databases

eggNOGi COG1383.
HOVERGENi HBG001708.
InParanoidi P63276.
KOi K02962.
OMAi FTTHLMR.
OrthoDBi EOG72C52C.
PhylomeDBi P63276.
TreeFami TF317992.

Enzyme and pathway databases

Reactomei REACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_231519. Eukaryotic Translation Termination.
REACT_236458. Ribosomal scanning and start codon recognition.
REACT_249044. Formation of a pool of free 40S subunits.
REACT_249316. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_253640. Peptide chain elongation.
REACT_256488. Translation initiation complex formation.
REACT_259469. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_262078. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

NextBioi 297571.
PROi P63276.
SOURCEi Search...

Gene expression databases

Bgeei P63276.
CleanExi MM_RPS17.
ExpressionAtlasi P63276. baseline and differential.
Genevestigatori P63276.

Family and domain databases

Gene3Di 1.10.60.20. 1 hit.
HAMAPi MF_00511. Ribosomal_S17e.
InterProi IPR001210. Ribosomal_S17e.
IPR018273. Ribosomal_S17e_CS.
[Graphical view ]
PANTHERi PTHR10732. PTHR10732. 1 hit.
Pfami PF00833. Ribosomal_S17e. 1 hit.
[Graphical view ]
SUPFAMi SSF116820. SSF116820. 1 hit.
PROSITEi PS00712. RIBOSOMAL_S17E. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of a cDNA clone encoding ribosomal protein S17 of Ehrlich ascites carcinoma cells."
    Karasaki Y., Satoh Y., Ohji T., Tsukamoto S., Higashi K., Gotoh S., Mizusaki K.
    Biochem. Genet. 32:409-414(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ddY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pancreas.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain and Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRS17_MOUSE
AccessioniPrimary (citable) accession number: P63276
Secondary accession number(s): P06584
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3