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P52815

- RM12_HUMAN

UniProt

P52815 - RM12_HUMAN

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Protein
39S ribosomal protein L12, mitochondrial
Gene
MRPL12, RPML12
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  2. protein binding Source: UniProtKB
  3. structural constituent of ribosome Source: ProtInc

GO - Biological processi

  1. positive regulation of transcription, DNA-templated Source: HGNC
  2. transcription from mitochondrial promoter Source: HGNC
  3. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L12, mitochondrial
Short name:
L12mt
Short name:
MRP-L12
Alternative name(s):
5c5-2
Gene namesi
Name:MRPL12
Synonyms:RPML12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:10378. MRPL12.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30941.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545Mitochondrion Reviewed prediction
Add
BLAST
Chaini46 – 19815339S ribosomal protein L12, mitochondrialUniRule annotation
PRO_0000030458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei138 – 1381N6-acetyllysine By similarity
Modified residuei150 – 1501N6-succinyllysine By similarity
Modified residuei162 – 1621N6-succinyllysine By similarity
Modified residuei178 – 1781N6-succinyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP52815.
PaxDbiP52815.
PeptideAtlasiP52815.
PRIDEiP52815.

2D gel databases

DOSAC-COBS-2DPAGEP52815.
SWISS-2DPAGEP52815.

PTM databases

PhosphoSiteiP52815.

Expressioni

Gene expression databases

BgeeiP52815.
CleanExiHS_MRPL12.
GenevestigatoriP52815.

Organism-specific databases

HPAiHPA022853.
HPA023043.

Interactioni

Subunit structurei

Interacts with NOA1.1 Publication

Protein-protein interaction databases

BioGridi112097. 60 interactions.
DIPiDIP-50865N.
IntActiP52815. 13 interactions.
MINTiMINT-1150069.
STRINGi9606.ENSP00000333837.

Structurei

3D structure databases

ProteinModelPortaliP52815.
SMRiP52815. Positions 64-198.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG312691.
HOGENOMiHOG000248814.
HOVERGENiHBG001832.
InParanoidiP52815.
KOiK02935.
OrthoDBiEOG7B5WXR.
PhylomeDBiP52815.
TreeFamiTF105997.

Family and domain databases

Gene3Di3.30.1390.10. 1 hit.
HAMAPiMF_00368. Ribosomal_L7_L12.
InterProiIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PANTHERiPTHR11809. PTHR11809. 1 hit.
PfamiPF00542. Ribosomal_L12. 1 hit.
[Graphical view]
ProDomiPD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P52815-1 [UniParc]FASTAAdd to Basket

« Hide

MLPAAARPLW GPCLGLRAAA FRLARRQVPC VCAVRHMRSS GHQRCEALAG    50
APLDNAPKEY PPKIQQLVQD IASLTLLEIS DLNELLKKTL KIQDVGLVPM 100
GGVMSGAVPA AAAQEAVEED IPIAKERTHF TVRLTEAKPV DKVKLIKEIK 150
NYIQGINLVQ AKKLVESLPQ EIKANVAKAE AEKIKAALEA VGGTVVLE 198
Length:198
Mass (Da):21,348
Last modified:May 15, 2002 - v2
Checksum:i7F26BEDE9218CEF0
GO

Sequence cautioni

The sequence AAD16894.1 differs from that shown. Reason: Frameshift at several positions.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051S → P.
Corresponds to variant rs11546280 [ dbSNP | Ensembl ].
VAR_052001

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331A → T in CAA56249. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X79865 mRNA. Translation: CAA56249.1.
AF059736 Genomic DNA. Translation: AAG32154.1.
BC002344 mRNA. Translation: AAH02344.1.
BC007497 mRNA. Translation: AAH07497.1.
AF105278 mRNA. Translation: AAD16894.1. Frameshift.
CCDSiCCDS11785.1.
RefSeqiNP_002940.2. NM_002949.3.
UniGeneiHs.109059.

Genome annotation databases

EnsembliENST00000333676; ENSP00000333837; ENSG00000262814.
GeneIDi6182.
KEGGihsa:6182.
UCSCiuc002kbh.2. human.

Polymorphism databases

DMDMi20981709.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X79865 mRNA. Translation: CAA56249.1 .
AF059736 Genomic DNA. Translation: AAG32154.1 .
BC002344 mRNA. Translation: AAH02344.1 .
BC007497 mRNA. Translation: AAH07497.1 .
AF105278 mRNA. Translation: AAD16894.1 . Frameshift.
CCDSi CCDS11785.1.
RefSeqi NP_002940.2. NM_002949.3.
UniGenei Hs.109059.

3D structure databases

ProteinModelPortali P52815.
SMRi P52815. Positions 64-198.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112097. 60 interactions.
DIPi DIP-50865N.
IntActi P52815. 13 interactions.
MINTi MINT-1150069.
STRINGi 9606.ENSP00000333837.

PTM databases

PhosphoSitei P52815.

Polymorphism databases

DMDMi 20981709.

2D gel databases

DOSAC-COBS-2DPAGE P52815.
SWISS-2DPAGE P52815.

Proteomic databases

MaxQBi P52815.
PaxDbi P52815.
PeptideAtlasi P52815.
PRIDEi P52815.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000333676 ; ENSP00000333837 ; ENSG00000262814 .
GeneIDi 6182.
KEGGi hsa:6182.
UCSCi uc002kbh.2. human.

Organism-specific databases

CTDi 6182.
GeneCardsi GC17P079670.
HGNCi HGNC:10378. MRPL12.
HPAi HPA022853.
HPA023043.
MIMi 602375. gene.
neXtProti NX_P52815.
PharmGKBi PA30941.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG312691.
HOGENOMi HOG000248814.
HOVERGENi HBG001832.
InParanoidi P52815.
KOi K02935.
OrthoDBi EOG7B5WXR.
PhylomeDBi P52815.
TreeFami TF105997.

Miscellaneous databases

GeneWikii MRPL12.
GenomeRNAii 6182.
NextBioi 24005.
PROi P52815.
SOURCEi Search...

Gene expression databases

Bgeei P52815.
CleanExi HS_MRPL12.
Genevestigatori P52815.

Family and domain databases

Gene3Di 3.30.1390.10. 1 hit.
HAMAPi MF_00368. Ribosomal_L7_L12.
InterProi IPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view ]
PANTHERi PTHR11809. PTHR11809. 1 hit.
Pfami PF00542. Ribosomal_L12. 1 hit.
[Graphical view ]
ProDomi PD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A delayed-early response nuclear gene encoding MRPL12, the mitochondrial homologue to the bacterial translational regulator L7/L12 protein."
    Marty L., Fort P.
    J. Biol. Chem. 271:11468-11476(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genomic structure and chromosomal localization of human mitochondrial ribosomal protein L12."
    Liu J., Barnoski B.L., O'Brien T.W.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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: Muscle.
  4. Ma F.-R., Yan M., Zhu L.-P.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 47-198.
  5. "hNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis."
    Tang T., Zheng B., Chen S.H., Murphy A.N., Kudlicka K., Zhou H., Farquhar M.G.
    J. Biol. Chem. 284:5414-5424(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOA1.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRM12_HUMAN
AccessioniPrimary (citable) accession number: P52815
Secondary accession number(s): Q969U0, Q9HCA2, Q9UQJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 15, 2002
Last modified: September 3, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Ribosomal proteins
    Ribosomal proteins families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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