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Protein

39S ribosomal protein L14, mitochondrial

Gene

MRPL14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Forms part of 2 intersubunit bridges in the assembled ribosome. Upon binding to MALSU1 intersubunit bridge formation is blocked, preventing ribosome formation and repressing translation (Probable).1 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. mitochondrial translation Source: Reactome
  2. mitochondrial translational elongation Source: Reactome
  3. mitochondrial translational initiation Source: Reactome
  4. mitochondrial translational termination Source: Reactome
  5. organelle organization Source: Reactome
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 L14, mitochondrial
Short name:
L14mt
Short name:
MRP-L14
Alternative name(s):
39S ribosomal protein L32, mitochondrial
Short name:
L32mt
Short name:
MRP-L32
Gene namesi
Name:MRPL14
Synonyms:MRPL32, RPML32
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:14279. MRPL14.

Subcellular locationi

  1. Mitochondrion 2 Publications

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Reactome
  2. ribosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30943.

Polymorphism and mutation databases

BioMutaiMRPL14.
DMDMi74749064.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionBy similarityAdd
BLAST
Chaini31 – 14511539S ribosomal protein L14, mitochondrialPRO_0000261134Add
BLAST

Proteomic databases

MaxQBiQ6P1L8.
PaxDbiQ6P1L8.
PeptideAtlasiQ6P1L8.
PRIDEiQ6P1L8.

PTM databases

PhosphoSiteiQ6P1L8.

Expressioni

Gene expression databases

BgeeiQ6P1L8.
CleanExiHS_MRPL14.
HS_MRPL32.
ExpressionAtlasiQ6P1L8. baseline and differential.
GenevestigatoriQ6P1L8.

Organism-specific databases

HPAiHPA038769.

Interactioni

Subunit structurei

Part of the mitochondrial ribosome large subunit (39S) (By similarity); associates with MALSU1.By similarity1 Publication

Protein-protein interaction databases

BioGridi122350. 32 interactions.
IntActiQ6P1L8. 3 interactions.
MINTiMINT-6776547.
STRINGi9606.ENSP00000361084.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40L1-145[»]
ProteinModelPortaliQ6P1L8.
SMRiQ6P1L8. Positions 31-145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L14P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG331407.
GeneTreeiENSGT00390000001121.
HOGENOMiHOG000183701.
HOVERGENiHBG088508.
InParanoidiQ6P1L8.
KOiK02874.
OMAiALGNTPY.
OrthoDBiEOG78D7MS.
PhylomeDBiQ6P1L8.
TreeFamiTF324586.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
InterProiIPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
[Graphical view]
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q6P1L8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFFTGLWGP FTCVSRVLSH HCFSTTGSLS AIQKMTRVRV VDNSALGNSP
60 70 80 90 100
YHRAPRCIHV YKKNGVGKVG DQILLAIKGQ KKKALIVGHC MPGPRMTPRF
110 120 130 140
DSNNVVLIED NGNPVGTRIK TPIPTSLRKR EGEYSKVLAI AQNFV
Length:145
Mass (Da):15,948
Last modified:July 5, 2004 - v1
Checksum:i841360D2E84071A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK312086 mRNA. Translation: BAG35022.1.
AL109615 Genomic DNA. Translation: CAI19245.1.
CH471081 Genomic DNA. Translation: EAX04243.1.
BC065005 mRNA. Translation: AAH65005.1.
AB051339 Genomic DNA. Translation: BAB54929.2.
CCDSiCCDS34460.1.
RefSeqiNP_115487.2. NM_032111.2.
XP_005249357.1. XM_005249300.2.
XP_005249358.1. XM_005249301.3.
UniGeneiHs.311190.

Genome annotation databases

EnsembliENST00000372014; ENSP00000361084; ENSG00000180992.
GeneIDi64928.
KEGGihsa:64928.
UCSCiuc003owp.3. human.

Polymorphism and mutation databases

BioMutaiMRPL14.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK312086 mRNA. Translation: BAG35022.1.
AL109615 Genomic DNA. Translation: CAI19245.1.
CH471081 Genomic DNA. Translation: EAX04243.1.
BC065005 mRNA. Translation: AAH65005.1.
AB051339 Genomic DNA. Translation: BAB54929.2.
CCDSiCCDS34460.1.
RefSeqiNP_115487.2. NM_032111.2.
XP_005249357.1. XM_005249300.2.
XP_005249358.1. XM_005249301.3.
UniGeneiHs.311190.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40L1-145[»]
ProteinModelPortaliQ6P1L8.
SMRiQ6P1L8. Positions 31-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122350. 32 interactions.
IntActiQ6P1L8. 3 interactions.
MINTiMINT-6776547.
STRINGi9606.ENSP00000361084.

PTM databases

PhosphoSiteiQ6P1L8.

Polymorphism and mutation databases

BioMutaiMRPL14.
DMDMi74749064.

Proteomic databases

MaxQBiQ6P1L8.
PaxDbiQ6P1L8.
PeptideAtlasiQ6P1L8.
PRIDEiQ6P1L8.

Protocols and materials databases

DNASUi64928.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372014; ENSP00000361084; ENSG00000180992.
GeneIDi64928.
KEGGihsa:64928.
UCSCiuc003owp.3. human.

Organism-specific databases

CTDi64928.
GeneCardsiGC06M044128.
HGNCiHGNC:14279. MRPL14.
HPAiHPA038769.
MIMi611827. gene.
neXtProtiNX_Q6P1L8.
PharmGKBiPA30943.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG331407.
GeneTreeiENSGT00390000001121.
HOGENOMiHOG000183701.
HOVERGENiHBG088508.
InParanoidiQ6P1L8.
KOiK02874.
OMAiALGNTPY.
OrthoDBiEOG78D7MS.
PhylomeDBiQ6P1L8.
TreeFamiTF324586.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMRPL14. human.
GenomeRNAii64928.
NextBioi67102.
PROiQ6P1L8.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P1L8.
CleanExiHS_MRPL14.
HS_MRPL32.
ExpressionAtlasiQ6P1L8. baseline and differential.
GenevestigatoriQ6P1L8.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
InterProiIPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
[Graphical view]
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Thymus.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Pancreas.
  5. "The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders."
    Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S., Watanabe K., Tanaka T.
    Genomics 77:65-70(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-76, SUBCELLULAR LOCATION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MALSU1.

Entry informationi

Entry nameiRM14_HUMAN
AccessioniPrimary (citable) accession number: Q6P1L8
Secondary accession number(s): B2R575, Q96Q72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 5, 2004
Last modified: April 29, 2015
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
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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. 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.