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Protein

40S ribosomal protein S21

Gene

Rps21

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: MGI
  2. protein N-terminus binding Source: MGI
  3. ribosome binding Source: UniProtKB
  4. structural constituent of ribosome Source: GO_Central

GO - Biological processi

  1. endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: GO_Central
  2. endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: GO_Central
  3. ribosomal small subunit biogenesis Source: GO_Central
  4. translational elongation Source: GO_Central
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 S21
Gene namesi
Name:Rps21
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1913731. Rps21.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosolic small ribosomal subunit Source: MGI
  3. small ribosomal subunit Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 838340S ribosomal protein S21PRO_0000194731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei81 – 811N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CQR2.
PaxDbiQ9CQR2.
PRIDEiQ9CQR2.

PTM databases

PhosphoSiteiQ9CQR2.

Expressioni

Gene expression databases

BgeeiQ9CQR2.
CleanExiMM_RPS21.
ExpressionAtlasiQ9CQR2. baseline and differential.
GenevestigatoriQ9CQR2.

Interactioni

Protein-protein interaction databases

MINTiMINT-1857339.

Structurei

3D structure databases

ProteinModelPortaliQ9CQR2.
SMRiQ9CQR2. Positions 1-82.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S21e family.Curated

Phylogenomic databases

eggNOGiNOG301320.
GeneTreeiENSGT00390000017515.
HOGENOMiHOG000183557.
HOVERGENiHBG005025.
InParanoidiQ9CQR2.
KOiK02971.
OMAiIQINIAE.
OrthoDBiEOG7HQNBQ.
PhylomeDBiQ9CQR2.
TreeFamiTF300167.

Family and domain databases

InterProiIPR001931. Ribosomal_S21e.
IPR018279. Ribosomal_S21e_CS.
[Graphical view]
PANTHERiPTHR10442. PTHR10442. 1 hit.
PfamiPF01249. Ribosomal_S21e. 1 hit.
[Graphical view]
PIRSFiPIRSF002148. Ribosomal_S21e. 1 hit.
ProDomiPD006584. Ribosomal_S21e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS00996. RIBOSOMAL_S21E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CQR2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQNDAGEFVD LYVPRKCSAS NRIIAAKDHA SIQMNVAEVD RTTGRFNGQF
60 70 80
KTYGICGAIR RMGESDDSIL RLAKADGIVS KNF
Length:83
Mass (Da):9,141
Last modified:June 1, 2001 - v1
Checksum:i67961651844D0DB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007846 mRNA. Translation: BAB25301.1.
AK007850 mRNA. Translation: BAB25304.1.
AK010637 mRNA. Translation: BAB27081.1.
AK012488 mRNA. Translation: BAB28274.1.
BC027563 mRNA. Translation: AAH27563.1.
BC086912 mRNA. Translation: AAH86912.1.
CCDSiCCDS38376.1.
RefSeqiNP_079863.1. NM_025587.2.
XP_006500765.1. XM_006500702.1.
UniGeneiMm.289669.

Genome annotation databases

EnsembliENSMUST00000059080; ENSMUSP00000058432; ENSMUSG00000039001.
GeneIDi66481.
KEGGimmu:66481.
UCSCiuc008oiq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007846 mRNA. Translation: BAB25301.1.
AK007850 mRNA. Translation: BAB25304.1.
AK010637 mRNA. Translation: BAB27081.1.
AK012488 mRNA. Translation: BAB28274.1.
BC027563 mRNA. Translation: AAH27563.1.
BC086912 mRNA. Translation: AAH86912.1.
CCDSiCCDS38376.1.
RefSeqiNP_079863.1. NM_025587.2.
XP_006500765.1. XM_006500702.1.
UniGeneiMm.289669.

3D structure databases

ProteinModelPortaliQ9CQR2.
SMRiQ9CQR2. Positions 1-82.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1857339.

PTM databases

PhosphoSiteiQ9CQR2.

Proteomic databases

MaxQBiQ9CQR2.
PaxDbiQ9CQR2.
PRIDEiQ9CQR2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000059080; ENSMUSP00000058432; ENSMUSG00000039001.
GeneIDi66481.
KEGGimmu:66481.
UCSCiuc008oiq.1. mouse.

Organism-specific databases

CTDi6227.
MGIiMGI:1913731. Rps21.

Phylogenomic databases

eggNOGiNOG301320.
GeneTreeiENSGT00390000017515.
HOGENOMiHOG000183557.
HOVERGENiHBG005025.
InParanoidiQ9CQR2.
KOiK02971.
OMAiIQINIAE.
OrthoDBiEOG7HQNBQ.
PhylomeDBiQ9CQR2.
TreeFamiTF300167.

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.

Miscellaneous databases

ChiTaRSiRps21. mouse.
NextBioi321812.
PROiQ9CQR2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQR2.
CleanExiMM_RPS21.
ExpressionAtlasiQ9CQR2. baseline and differential.
GenevestigatoriQ9CQR2.

Family and domain databases

InterProiIPR001931. Ribosomal_S21e.
IPR018279. Ribosomal_S21e_CS.
[Graphical view]
PANTHERiPTHR10442. PTHR10442. 1 hit.
PfamiPF01249. Ribosomal_S21e. 1 hit.
[Graphical view]
PIRSFiPIRSF002148. Ribosomal_S21e. 1 hit.
ProDomiPD006584. Ribosomal_S21e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS00996. RIBOSOMAL_S21E. 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.
    Tissue: Embryo, Embryonic stem cell and Pancreas.
  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].
    Tissue: Heart and Mammary gland.

Entry informationi

Entry nameiRS21_MOUSE
AccessioniPrimary (citable) accession number: Q9CQR2
Secondary accession number(s): Q5M9L3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 91 of the entry and version 1 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.