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Protein

28S ribosomal protein S22, mitochondrial

Gene

Mrps22

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-MMU-5389840. Mitochondrial translation elongation.
R-MMU-5419276. Mitochondrial translation termination.

Names & Taxonomyi

Protein namesi
Recommended name:
28S ribosomal protein S22, mitochondrial
Short name:
MRP-S22
Short name:
S22mt
Gene namesi
Name:Mrps22
Synonyms:Rpms22
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1928137. Mrps22.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial small ribosomal subunit Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 35935928S ribosomal protein S22, mitochondrialPRO_0000087704Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541PhosphoserineBy similarity
Modified residuei210 – 2101N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CXW2.
MaxQBiQ9CXW2.
PaxDbiQ9CXW2.
PeptideAtlasiQ9CXW2.
PRIDEiQ9CXW2.

PTM databases

iPTMnetiQ9CXW2.
PhosphoSiteiQ9CXW2.

Expressioni

Gene expression databases

BgeeiQ9CXW2.
CleanExiMM_MRPS22.
GenevisibleiQ9CXW2. MM.

Interactioni

Subunit structurei

Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins.

Protein-protein interaction databases

BioGridi211091. 2 interactions.
IntActiQ9CXW2. 2 interactions.
MINTiMINT-4133270.
STRINGi10090.ENSMUSP00000035034.

Structurei

3D structure databases

ProteinModelPortaliQ9CXW2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiKOG3890. Eukaryota.
ENOG4111I44. LUCA.
GeneTreeiENSGT00390000006095.
HOGENOMiHOG000154215.
HOVERGENiHBG017759.
InParanoidiQ9CXW2.
KOiK17401.
OMAiTTKRMNQ.
OrthoDBiEOG7TMZS7.
PhylomeDBiQ9CXW2.
TreeFamiTF312882.

Family and domain databases

InterProiIPR019374. Ribosomal_S22_mit.
[Graphical view]
PfamiPF10245. MRP-S22. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CXW2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVRTPLSL WRFQLGSRRA RRVCTRATAQ RHPDALLATR PQPFEVGQPR
60 70 80 90 100
RLLSSEAESG SSEVKKPAFM DEEVQRILTK ITGLDLQKTF RPAIQPLKPP
110 120 130 140 150
TYKLMTQAQL EEATRLAVEA AKVRLKMPPV LEERKPINDV LAEDKILEGT
160 170 180 190 200
ETNKYVFTDI SYNIPHRERF IVVREPSGTL RKASWEERDR VIQIYFPKEG
210 220 230 240 250
RRVLPPVIFK DENLKTMYSQ DRHADVLNLC VAQFEPDSAE YIKVHHQTYE
260 270 280 290 300
DIDRHGKYEL LRSTRHFGGM AWYFVNKKKI DGLLIDQIQR DLVDDATSLV
310 320 330 340 350
QLYHMLHPDG QSAQEAKEQA AEGVDLIKVF AKTEAQRGAY IELALQTYQE

IVTSHSAAS
Length:359
Mass (Da):41,192
Last modified:April 27, 2001 - v1
Checksum:iC258AD152738F1C7
GO

Sequence cautioni

The sequence AAH21882.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003836 mRNA. Translation: BAB23027.2.
AK013925 mRNA. Translation: BAB29061.1.
AK154600 mRNA. Translation: BAE32703.1.
BC021882 mRNA. Translation: AAH21882.1. Different initiation.
BC051198 mRNA. Translation: AAH51198.1.
CCDSiCCDS23427.1.
RefSeqiNP_079761.1. NM_025485.3.
UniGeneiMm.17949.

Genome annotation databases

EnsembliENSMUST00000035034; ENSMUSP00000035034; ENSMUSG00000032459.
GeneIDi64655.
KEGGimmu:64655.
UCSCiuc009rdn.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003836 mRNA. Translation: BAB23027.2.
AK013925 mRNA. Translation: BAB29061.1.
AK154600 mRNA. Translation: BAE32703.1.
BC021882 mRNA. Translation: AAH21882.1. Different initiation.
BC051198 mRNA. Translation: AAH51198.1.
CCDSiCCDS23427.1.
RefSeqiNP_079761.1. NM_025485.3.
UniGeneiMm.17949.

3D structure databases

ProteinModelPortaliQ9CXW2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211091. 2 interactions.
IntActiQ9CXW2. 2 interactions.
MINTiMINT-4133270.
STRINGi10090.ENSMUSP00000035034.

PTM databases

iPTMnetiQ9CXW2.
PhosphoSiteiQ9CXW2.

Proteomic databases

EPDiQ9CXW2.
MaxQBiQ9CXW2.
PaxDbiQ9CXW2.
PeptideAtlasiQ9CXW2.
PRIDEiQ9CXW2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035034; ENSMUSP00000035034; ENSMUSG00000032459.
GeneIDi64655.
KEGGimmu:64655.
UCSCiuc009rdn.3. mouse.

Organism-specific databases

CTDi56945.
MGIiMGI:1928137. Mrps22.

Phylogenomic databases

eggNOGiKOG3890. Eukaryota.
ENOG4111I44. LUCA.
GeneTreeiENSGT00390000006095.
HOGENOMiHOG000154215.
HOVERGENiHBG017759.
InParanoidiQ9CXW2.
KOiK17401.
OMAiTTKRMNQ.
OrthoDBiEOG7TMZS7.
PhylomeDBiQ9CXW2.
TreeFamiTF312882.

Enzyme and pathway databases

ReactomeiR-MMU-5389840. Mitochondrial translation elongation.
R-MMU-5419276. Mitochondrial translation termination.

Miscellaneous databases

PROiQ9CXW2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CXW2.
CleanExiMM_MRPS22.
GenevisibleiQ9CXW2. MM.

Family and domain databases

InterProiIPR019374. Ribosomal_S22_mit.
[Graphical view]
PfamiPF10245. MRP-S22. 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: Embryo and Embryonic head.
  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: Czech II.
    Tissue: Mammary gland.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen and Testis.

Entry informationi

Entry nameiRT22_MOUSE
AccessioniPrimary (citable) accession number: Q9CXW2
Secondary accession number(s): Q3U3T2, Q8VDG9, Q9D185
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: July 6, 2016
This is version 99 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

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 one 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.