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Protein

39S ribosomal protein L32, mitochondrial

Gene

Mrpl32

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

Functioni

GO - Molecular functioni

GO - Biological processi

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:
39S ribosomal protein L32, mitochondrial
Short name:
L32mt
Short name:
MRP-L32
Alternative name(s):
Heart-expressed gene 1 protein
Gene namesi
Name:Mrpl32
Synonyms:Heg1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2137226. Mrpl32.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 18739S ribosomal protein L32, mitochondrialPRO_0000030514
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

EPDiQ9DCI9.
MaxQBiQ9DCI9.
PaxDbiQ9DCI9.
PRIDEiQ9DCI9.

PTM databases

PhosphoSiteiQ9DCI9.

Expressioni

Gene expression databases

BgeeiQ9DCI9.
CleanExiMM_MRPL32.
GenevisibleiQ9DCI9. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000015816.

Structurei

3D structure databases

ProteinModelPortaliQ9DCI9.
SMRiQ9DCI9. Positions 78-187.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L32P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG4080. Eukaryota.
COG0333. LUCA.
GeneTreeiENSGT00390000014996.
HOGENOMiHOG000252980.
HOVERGENiHBG036112.
InParanoidiQ9DCI9.
KOiK02911.
OMAiVLRNYWE.
OrthoDBiEOG7C2R2G.
PhylomeDBiQ9DCI9.
TreeFamiTF106139.

Family and domain databases

InterProiIPR002677. Ribosomal_L32p.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PfamiPF01783. Ribosomal_L32p. 1 hit.
[Graphical view]
SUPFAMiSSF57829. SSF57829. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9DCI9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSLLLLSL PWPVRPGPLQ RCWELLQRQL QQSWSRFVSP PWAPALAVQR
60 70 80 90 100
PSILTELAHD TCENKENSSF LDSIFWMAAP KNRRTIEVNR CRRRNPQKLI
110 120 130 140 150
KIKNNIDICP ECGHLKQKHV LCGYCYEKVR QETTKIRQQI GAQEGGPFRA
160 170 180
PSVETMVLYT GEKPSEKDQG KRIVERNIKR PSWFTQN
Length:187
Mass (Da):21,733
Last modified:June 1, 2001 - v1
Checksum:i1AB03A656D404F2D
GO

Sequence cautioni

The sequence AAK69482.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121W → M in AAK69482 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049650 mRNA. Translation: BAB40855.1.
AK002753 mRNA. Translation: BAB22330.1.
AF279255 mRNA. Translation: AAK69482.1. Different initiation.
BC052214 mRNA. Translation: AAH52214.1.
CCDSiCCDS26249.1.
RefSeqiNP_083547.1. NM_029271.2.
UniGeneiMm.36511.

Genome annotation databases

EnsembliENSMUST00000015816; ENSMUSP00000015816; ENSMUSG00000015672.
GeneIDi75398.
KEGGimmu:75398.
UCSCiuc007pnj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049650 mRNA. Translation: BAB40855.1.
AK002753 mRNA. Translation: BAB22330.1.
AF279255 mRNA. Translation: AAK69482.1. Different initiation.
BC052214 mRNA. Translation: AAH52214.1.
CCDSiCCDS26249.1.
RefSeqiNP_083547.1. NM_029271.2.
UniGeneiMm.36511.

3D structure databases

ProteinModelPortaliQ9DCI9.
SMRiQ9DCI9. Positions 78-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000015816.

PTM databases

PhosphoSiteiQ9DCI9.

Proteomic databases

EPDiQ9DCI9.
MaxQBiQ9DCI9.
PaxDbiQ9DCI9.
PRIDEiQ9DCI9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015816; ENSMUSP00000015816; ENSMUSG00000015672.
GeneIDi75398.
KEGGimmu:75398.
UCSCiuc007pnj.1. mouse.

Organism-specific databases

CTDi64983.
MGIiMGI:2137226. Mrpl32.

Phylogenomic databases

eggNOGiKOG4080. Eukaryota.
COG0333. LUCA.
GeneTreeiENSGT00390000014996.
HOGENOMiHOG000252980.
HOVERGENiHBG036112.
InParanoidiQ9DCI9.
KOiK02911.
OMAiVLRNYWE.
OrthoDBiEOG7C2R2G.
PhylomeDBiQ9DCI9.
TreeFamiTF106139.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMrpl32. mouse.
NextBioi342908.
PROiQ9DCI9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DCI9.
CleanExiMM_MRPL32.
GenevisibleiQ9DCI9. MM.

Family and domain databases

InterProiIPR002677. Ribosomal_L32p.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PfamiPF01783. Ribosomal_L32p. 1 hit.
[Graphical view]
SUPFAMiSSF57829. SSF57829. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria."
    Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A., Watanabe K.
    J. Biol. Chem. 276:21724-21736(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Kidney.
  3. "HEG1 (heart expressed gene) - a new marker gene for heart development in the mouse."
    Schepler A., Arnemann J.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  4. "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/6J.
    Tissue: Embryo.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney and Liver.

Entry informationi

Entry nameiRM32_MOUSE
AccessioniPrimary (citable) accession number: Q9DCI9
Secondary accession number(s): Q91XR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 105 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

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.