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Protein

40S ribosomal protein S27

Gene

Rps27

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

Functioni

Cofactori

Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri38 – 6023C4-typeSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: Ensembl
  3. structural constituent of ribosome Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_306375. Mitotic Prometaphase.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S27
Gene namesi
Name:Rps27Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componentsi: Chromosome 3, Chromosome 9

Organism-specific databases

MGIiMGI:1888676. Rps27.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: Ensembl
  2. nucleus Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 848340S ribosomal protein S27PRO_0000149052Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6ZWU9.
PaxDbiQ6ZWU9.
PRIDEiQ6ZWU9.

PTM databases

PhosphoSiteiQ6ZWU9.

Expressioni

Gene expression databases

BgeeiQ6ZWU9.
CleanExiMM_RPS27.
GenevestigatoriQ6ZWU9.

Interactioni

Protein-protein interaction databases

BioGridi208248. 6 interactions.
786971. 4 interactions.
IntActiQ6ZWU9. 2 interactions.
MINTiMINT-1212966.

Structurei

3D structure databases

ProteinModelPortaliQ6ZWU9.
SMRiQ6ZWU9. Positions 2-84.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S27e family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri38 – 6023C4-typeSequence AnalysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG2051.
GeneTreeiENSGT00390000013514.
HOVERGENiHBG000252.
InParanoidiQ6ZWU9.
KOiK02978.
OMAiVVICSSC.
OrthoDBiEOG78SQM9.
PhylomeDBiQ6ZWU9.
TreeFamiTF300265.

Family and domain databases

Gene3Di2.20.25.100. 1 hit.
HAMAPiMF_00371. Ribosomal_S27e.
InterProiIPR000592. Ribosomal_S27e.
IPR023407. Ribosomal_S27e_Zn-bd_dom.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PANTHERiPTHR11594. PTHR11594. 1 hit.
PfamiPF01667. Ribosomal_S27e. 1 hit.
[Graphical view]
ProDomiPD004466. Ribosomal_S27e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01168. RIBOSOMAL_S27E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q6ZWU9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLAKDLLHP SPEEEKRKHK KKRLVQSPNS YFMDVKCPGC YKITTVFSHA
60 70 80
QTVVLCVGCS TVLCQPTGGK ARLTEGCSFR RKQH
Length:84
Mass (Da):9,461
Last modified:January 23, 2007 - v3
Checksum:i242C4466AC8A8900
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014294 mRNA. Translation: BAB29250.1.
AK088320 mRNA. Translation: BAC40279.1.
AK166551 mRNA. Translation: BAE38849.1.
BC048352 mRNA. Translation: AAH48352.1.
BC055693 mRNA. Translation: AAH55693.1.
CCDSiCCDS50970.1.
RefSeqiNP_001177187.1. NM_001190258.1.
NP_081291.1. NM_027015.4.
UniGeneiMm.270283.
Mm.371611.

Genome annotation databases

EnsembliENSMUST00000053150; ENSMUSP00000060523; ENSMUSG00000050621.
ENSMUST00000170122; ENSMUSP00000132102; ENSMUSG00000090733.
GeneIDi100043813.
57294.
KEGGimmu:100043813.
mmu:57294.
UCSCiuc008qbl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014294 mRNA. Translation: BAB29250.1.
AK088320 mRNA. Translation: BAC40279.1.
AK166551 mRNA. Translation: BAE38849.1.
BC048352 mRNA. Translation: AAH48352.1.
BC055693 mRNA. Translation: AAH55693.1.
CCDSiCCDS50970.1.
RefSeqiNP_001177187.1. NM_001190258.1.
NP_081291.1. NM_027015.4.
UniGeneiMm.270283.
Mm.371611.

3D structure databases

ProteinModelPortaliQ6ZWU9.
SMRiQ6ZWU9. Positions 2-84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208248. 6 interactions.
786971. 4 interactions.
IntActiQ6ZWU9. 2 interactions.
MINTiMINT-1212966.

Chemistry

BindingDBiQ6ZWU9.

PTM databases

PhosphoSiteiQ6ZWU9.

Proteomic databases

MaxQBiQ6ZWU9.
PaxDbiQ6ZWU9.
PRIDEiQ6ZWU9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053150; ENSMUSP00000060523; ENSMUSG00000050621.
ENSMUST00000170122; ENSMUSP00000132102; ENSMUSG00000090733.
GeneIDi100043813.
57294.
KEGGimmu:100043813.
mmu:57294.
UCSCiuc008qbl.2. mouse.

Organism-specific databases

CTDi100043813.
6232.
MGIiMGI:1888676. Rps27.

Phylogenomic databases

eggNOGiCOG2051.
GeneTreeiENSGT00390000013514.
HOVERGENiHBG000252.
InParanoidiQ6ZWU9.
KOiK02978.
OMAiVVICSSC.
OrthoDBiEOG78SQM9.
PhylomeDBiQ6ZWU9.
TreeFamiTF300265.

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_306375. Mitotic Prometaphase.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

NextBioi313647.
PROiQ6ZWU9.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZWU9.
CleanExiMM_RPS27.
GenevestigatoriQ6ZWU9.

Family and domain databases

Gene3Di2.20.25.100. 1 hit.
HAMAPiMF_00371. Ribosomal_S27e.
InterProiIPR000592. Ribosomal_S27e.
IPR023407. Ribosomal_S27e_Zn-bd_dom.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PANTHERiPTHR11594. PTHR11594. 1 hit.
PfamiPF01667. Ribosomal_S27e. 1 hit.
[Graphical view]
ProDomiPD004466. Ribosomal_S27e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01168. RIBOSOMAL_S27E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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 and NOD.
    Tissue: Head and Thymus.
  2. "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/6Imported and FVB/N-3.
    Tissue: BrainImported and Mammary gland.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRS27_MOUSE
AccessioniPrimary (citable) accession number: Q6ZWU9
Secondary accession number(s): Q3TLE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 102 of the entry and version 3 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

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.