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Protein

39S ribosomal protein L46, mitochondrial

Gene

MRPL46

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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

ReactomeiREACT_267634. Mitochondrial translation initiation.
REACT_268133. Mitochondrial translation elongation.
REACT_268261. Mitochondrial translation termination.

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L46, mitochondrial
Short name:
L46mt
Short name:
MRP-L46
Alternative name(s):
P2ECSL
Gene namesi
Name:MRPL46
Synonyms:C15orf4, LIECG2
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:1192. MRPL46.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30978.

Polymorphism and mutation databases

BioMutaiMRPL46.
DMDMi52783325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 27939S ribosomal protein L46, mitochondrialPRO_0000030576
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei230 – 2301N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9H2W6.
PaxDbiQ9H2W6.
PRIDEiQ9H2W6.

PTM databases

PhosphoSiteiQ9H2W6.

Expressioni

Gene expression databases

BgeeiQ9H2W6.
CleanExiHS_MRPL46.
ExpressionAtlasiQ9H2W6. baseline.
GenevisibleiQ9H2W6. HS.

Organism-specific databases

HPAiHPA050166.

Interactioni

Protein-protein interaction databases

BioGridi117757. 23 interactions.
IntActiQ9H2W6. 3 interactions.
MINTiMINT-4830900.
STRINGi9606.ENSP00000312311.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40e1-279[»]
3J9Melectron microscopy3.50e1-279[»]
ProteinModelPortaliQ9H2W6.
SMRiQ9H2W6. Positions 43-279.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L46 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG256490.
GeneTreeiENSGT00390000015400.
HOGENOMiHOG000047532.
HOVERGENiHBG057426.
InParanoidiQ9H2W6.
KOiK17427.
OMAiGHHVWVT.
OrthoDBiEOG7GN2NC.
PhylomeDBiQ9H2W6.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR015797. NUDIX_hydrolase_dom-like.
IPR021757. Ribosomal_L46.
[Graphical view]
PfamiPF11788. MRP-L46. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9H2W6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPVRRTLL GVAGGWRRFE RLWAGSLSSR SLALAAAPSS NGSPWRLLGA
60 70 80 90 100
LCLQRPPVVS KPLTPLQEEM ASLLQQIEIE RSLYSDHELR ALDENQRLAK
110 120 130 140 150
KKADLHDEED EQDILLAQDL EDMWEQKFLQ FKLGARITEA DEKNDRTSLN
160 170 180 190 200
RKLDRNLVLL VREKFGDQDV WILPQAEWQP GETLRGTAER TLATLSENNM
210 220 230 240 250
EAKFLGNAPC GHYTFKFPQA MRTESNLGAK VFFFKALLLT GDFSQAGNKG
260 270
HHVWVTKDEL GDYLKPKYLA QVRRFVSDL
Length:279
Mass (Da):31,705
Last modified:March 1, 2001 - v1
Checksum:iEDA966D758715378
GO

Sequence cautioni

The sequence AAG33698.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971E → K in AAG33698 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061H → Y.
Corresponds to variant rs16941888 [ dbSNP | Ensembl ].
VAR_052046

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF210056 mRNA. Translation: AAG43507.1.
AF205435 mRNA. Translation: AAG33698.1. Different initiation.
AK315434 mRNA. Translation: BAG37822.1.
CH471101 Genomic DNA. Translation: EAX01995.1.
BC017883 mRNA. Translation: AAH17883.1.
CCDSiCCDS10341.1.
RefSeqiNP_071446.2. NM_022163.3.
UniGeneiHs.534261.

Genome annotation databases

EnsembliENST00000312475; ENSP00000312311; ENSG00000259494.
GeneIDi26589.
KEGGihsa:26589.
UCSCiuc002bmj.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF210056 mRNA. Translation: AAG43507.1.
AF205435 mRNA. Translation: AAG33698.1. Different initiation.
AK315434 mRNA. Translation: BAG37822.1.
CH471101 Genomic DNA. Translation: EAX01995.1.
BC017883 mRNA. Translation: AAH17883.1.
CCDSiCCDS10341.1.
RefSeqiNP_071446.2. NM_022163.3.
UniGeneiHs.534261.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40e1-279[»]
3J9Melectron microscopy3.50e1-279[»]
ProteinModelPortaliQ9H2W6.
SMRiQ9H2W6. Positions 43-279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117757. 23 interactions.
IntActiQ9H2W6. 3 interactions.
MINTiMINT-4830900.
STRINGi9606.ENSP00000312311.

PTM databases

PhosphoSiteiQ9H2W6.

Polymorphism and mutation databases

BioMutaiMRPL46.
DMDMi52783325.

Proteomic databases

MaxQBiQ9H2W6.
PaxDbiQ9H2W6.
PRIDEiQ9H2W6.

Protocols and materials databases

DNASUi26589.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312475; ENSP00000312311; ENSG00000259494.
GeneIDi26589.
KEGGihsa:26589.
UCSCiuc002bmj.2. human.

Organism-specific databases

CTDi26589.
GeneCardsiGC15M089002.
H-InvDBHIX0012555.
HGNCiHGNC:1192. MRPL46.
HPAiHPA050166.
MIMi611851. gene.
neXtProtiNX_Q9H2W6.
PharmGKBiPA30978.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG256490.
GeneTreeiENSGT00390000015400.
HOGENOMiHOG000047532.
HOVERGENiHBG057426.
InParanoidiQ9H2W6.
KOiK17427.
OMAiGHHVWVT.
OrthoDBiEOG7GN2NC.
PhylomeDBiQ9H2W6.

Enzyme and pathway databases

ReactomeiREACT_267634. Mitochondrial translation initiation.
REACT_268133. Mitochondrial translation elongation.
REACT_268261. Mitochondrial translation termination.

Miscellaneous databases

GenomeRNAii26589.
NextBioi48962.
PROiQ9H2W6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H2W6.
CleanExiHS_MRPL46.
ExpressionAtlasiQ9H2W6. baseline.
GenevisibleiQ9H2W6. HS.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR015797. NUDIX_hydrolase_dom-like.
IPR021757. Ribosomal_L46.
[Graphical view]
PfamiPF11788. MRP-L46. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, mapping and expression analysis of C15orf4, a novel human gene with homology to the yeast mitochondrial ribosomal protein Ym130 gene."
    Carim-Todd L., Sumoy L., Andreu N., Estivill X., Escarceller M.
    DNA Seq. 12:91-96(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A novel gene identified in vascular endothelial cells."
    Zhang K.M., Chen B.S.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Skeletal muscle.
  6. "The large subunit of the mammalian mitochondrial ribosome. Analysis of the complement of ribosomal proteins present."
    Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M., Moseley A., Spremulli L.L.
    J. Biol. Chem. 276:43958-43969(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRM46_HUMAN
AccessioniPrimary (citable) accession number: Q9H2W6
Secondary accession number(s): B2RD75, Q9HBU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: March 1, 2001
Last modified: July 22, 2015
This is version 115 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. 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.