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Protein

39S ribosomal protein L22, mitochondrial

Gene

Mrpl22

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

Functioni

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_270125. Mitochondrial translation elongation.
REACT_270158. Mitochondrial translation termination.
REACT_271096. Mitochondrial translation initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L22, mitochondrial
Short name:
L22mt
Short name:
MRP-L22
Gene namesi
Name:Mrpl22
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1333794. Mrpl22.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. large ribosomal subunit Source: InterPro
  2. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040MitochondrionBy similarityAdd
BLAST
Chaini41 – 20616639S ribosomal protein L22, mitochondrialPRO_0000261645Add
BLAST

Proteomic databases

MaxQBiQ8BU88.
PaxDbiQ8BU88.
PRIDEiQ8BU88.

PTM databases

PhosphoSiteiQ8BU88.

Expressioni

Gene expression databases

BgeeiQ8BU88.
CleanExiMM_MRPL22.
GenevestigatoriQ8BU88.

Interactioni

Protein-protein interaction databases

BioGridi229782. 5 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8BU88.
SMRiQ8BU88. Positions 72-174.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L22P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0091.
GeneTreeiENSGT00390000002110.
HOGENOMiHOG000048027.
HOVERGENiHBG093486.
InParanoidiQ8BU88.
KOiK02890.
OMAiKMWYIAA.
OrthoDBiEOG79CZ0R.
PhylomeDBiQ8BU88.
TreeFamiTF315111.

Family and domain databases

Gene3Di3.90.470.10. 1 hit.
InterProiIPR001063. Ribosomal_L22.
IPR005727. Ribosomal_L22_bac/chlpt-type.
[Graphical view]
PANTHERiPTHR13501. PTHR13501. 1 hit.
PfamiPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMiSSF54843. SSF54843. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q8BU88-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAALLRELG ALRVPNLRIW ATQTLRVLPP SCIHTSASLD ISRKWEKKNK
60 70 80 90 100
IVYPPQLPGE PRRPAEIYHC RRQIKYSKDK MWYLAKMIRG MSIDQALAQL
110 120 130 140 150
EFNDKKGAQI IKEVLLEAQD MAVRDHNVEF RSNLHIAEST SGRGQCLKRI
160 170 180 190 200
RYHGRGRFGI MEKVYCHYFV KLVEGPPPPP EVPKTAVDHA KDYIQQLRSR

TIIHTL
Length:206
Mass (Da):23,805
Last modified:March 1, 2003 - v1
Checksum:iB7326DC02BED3390
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti198 – 1981R → P in BAC36901 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077615 mRNA. Translation: BAC36901.1.
AK086913 mRNA. Translation: BAC39761.1.
AK164417 mRNA. Translation: BAE37779.1.
AL928857 Genomic DNA. Translation: CAI26172.1.
BC061191 mRNA. Translation: AAH61191.1.
CCDSiCCDS24724.1.
RefSeqiNP_778166.2. NM_175001.3.
UniGeneiMm.259907.

Genome annotation databases

EnsembliENSMUST00000020820; ENSMUSP00000020820; ENSMUSG00000020514.
GeneIDi216767.
KEGGimmu:216767.
UCSCiuc007jap.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077615 mRNA. Translation: BAC36901.1.
AK086913 mRNA. Translation: BAC39761.1.
AK164417 mRNA. Translation: BAE37779.1.
AL928857 Genomic DNA. Translation: CAI26172.1.
BC061191 mRNA. Translation: AAH61191.1.
CCDSiCCDS24724.1.
RefSeqiNP_778166.2. NM_175001.3.
UniGeneiMm.259907.

3D structure databases

ProteinModelPortaliQ8BU88.
SMRiQ8BU88. Positions 72-174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229782. 5 interactions.

PTM databases

PhosphoSiteiQ8BU88.

Proteomic databases

MaxQBiQ8BU88.
PaxDbiQ8BU88.
PRIDEiQ8BU88.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020820; ENSMUSP00000020820; ENSMUSG00000020514.
GeneIDi216767.
KEGGimmu:216767.
UCSCiuc007jap.3. mouse.

Organism-specific databases

CTDi29093.
MGIiMGI:1333794. Mrpl22.

Phylogenomic databases

eggNOGiCOG0091.
GeneTreeiENSGT00390000002110.
HOGENOMiHOG000048027.
HOVERGENiHBG093486.
InParanoidiQ8BU88.
KOiK02890.
OMAiKMWYIAA.
OrthoDBiEOG79CZ0R.
PhylomeDBiQ8BU88.
TreeFamiTF315111.

Enzyme and pathway databases

ReactomeiREACT_270125. Mitochondrial translation elongation.
REACT_270158. Mitochondrial translation termination.
REACT_271096. Mitochondrial translation initiation.

Miscellaneous databases

NextBioi375302.
PROiQ8BU88.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BU88.
CleanExiMM_MRPL22.
GenevestigatoriQ8BU88.

Family and domain databases

Gene3Di3.90.470.10. 1 hit.
InterProiIPR001063. Ribosomal_L22.
IPR005727. Ribosomal_L22_bac/chlpt-type.
[Graphical view]
PANTHERiPTHR13501. PTHR13501. 1 hit.
PfamiPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMiSSF54843. SSF54843. 1 hit.
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, Eye and Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
    Tissue: Testis.

Entry informationi

Entry nameiRM22_MOUSE
AccessioniPrimary (citable) accession number: Q8BU88
Secondary accession number(s): Q8BK04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 1, 2003
Last modified: February 4, 2015
This is version 90 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.