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Protein

39S ribosomal protein L45, mitochondrial

Gene

MRPL45

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

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 L45, mitochondrial
Short name:
L45mt
Short name:
MRP-L45
Gene namesi
Name:MRPL45
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:16651. MRPL45.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 30639S ribosomal protein L45, mitochondrialPRO_0000030563
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiQ9BRJ2.
PaxDbiQ9BRJ2.
PRIDEiQ9BRJ2.

PTM databases

PhosphoSiteiQ9BRJ2.

Expressioni

Gene expression databases

BgeeiQ9BRJ2.
CleanExiHS_MRPL45.
GenevestigatoriQ9BRJ2.

Organism-specific databases

HPAiHPA023373.
HPA023385.

Interactioni

Protein-protein interaction databases

BioGridi124037. 33 interactions.
DIPiDIP-53786N.
IntActiQ9BRJ2. 4 interactions.
STRINGi9606.ENSP00000308901.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40d1-306[»]
ProteinModelPortaliQ9BRJ2.
SMRiQ9BRJ2. Positions 104-264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L45 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG276760.
HOVERGENiHBG044506.
InParanoidiQ9BRJ2.
OMAiKPEAVQW.
PhylomeDBiQ9BRJ2.
TreeFamiTF105825.

Family and domain databases

InterProiIPR007379. Tim44-like_dom.
[Graphical view]
PfamiPF04280. Tim44. 1 hit.
[Graphical view]
SMARTiSM00978. Tim44. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9BRJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPIPQGFS CLSRFLGWWF RQPVLVTQSA AIVPVRTKKR FTPPIYQPKF
60 70 80 90 100
KTEKEFMQHA RKAGLVIPPE KSDRSIHLAC TAGIFDAYVP PEGDARISSL
110 120 130 140 150
SKEGLIERTE RMKKTMASQV SIRRIKDYDA NFKIKDFPEK AKDIFIEAHL
160 170 180 190 200
CLNNSDHDRL HTLVTEHCFP DMTWDIKYKT VRWSFVESLE PSHVVQVRCS
210 220 230 240 250
SMMNQGNVYG QITVRMHTRQ TLAIYDRFGR LMYGQEDVPK DVLEYVVFEK
260 270 280 290 300
QLTNPYGSWR MHTKIVPPWA PPKQPILKTV MIPGPQLKPE EEYEEAQGEA

QKPQLA
Length:306
Mass (Da):35,351
Last modified:April 4, 2003 - v2
Checksum:iC00CC379D337910A
GO

Sequence cautioni

The sequence BC006235 differs from that shown. Reason: Frameshift at position 40. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391E → G in BAD18730 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti298 – 2981G → V.
Corresponds to variant rs34749623 [ dbSNP | Ensembl ].
VAR_061810

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK172741 mRNA. Translation: BAD18730.1.
BC006235 mRNA. No translation available.
BC130382 mRNA. Translation: AAI30383.1.
BC130384 mRNA. Translation: AAI30385.1.
CCDSiCCDS11326.1.
UniGeneiHs.537279.
Hs.744110.

Genome annotation databases

UCSCiuc002hpy.3. human.

Polymorphism databases

DMDMi29611869.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK172741 mRNA. Translation: BAD18730.1.
BC006235 mRNA. No translation available.
BC130382 mRNA. Translation: AAI30383.1.
BC130384 mRNA. Translation: AAI30385.1.
CCDSiCCDS11326.1.
UniGeneiHs.537279.
Hs.744110.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40d1-306[»]
ProteinModelPortaliQ9BRJ2.
SMRiQ9BRJ2. Positions 104-264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124037. 33 interactions.
DIPiDIP-53786N.
IntActiQ9BRJ2. 4 interactions.
STRINGi9606.ENSP00000308901.

PTM databases

PhosphoSiteiQ9BRJ2.

Polymorphism databases

DMDMi29611869.

Proteomic databases

MaxQBiQ9BRJ2.
PaxDbiQ9BRJ2.
PRIDEiQ9BRJ2.

Protocols and materials databases

DNASUi84311.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc002hpy.3. human.

Organism-specific databases

GeneCardsiGC17P036363.
H-InvDBHIX0013754.
HIX0039493.
HGNCiHGNC:16651. MRPL45.
HPAiHPA023373.
HPA023385.
MIMi611850. gene.
neXtProtiNX_Q9BRJ2.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG276760.
HOVERGENiHBG044506.
InParanoidiQ9BRJ2.
OMAiKPEAVQW.
PhylomeDBiQ9BRJ2.
TreeFamiTF105825.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMRPL45. human.
GenomeRNAii84311.
NextBioi74004.
PROiQ9BRJ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BRJ2.
CleanExiHS_MRPL45.
GenevestigatoriQ9BRJ2.

Family and domain databases

InterProiIPR007379. Tim44-like_dom.
[Graphical view]
PfamiPF04280. Tim44. 1 hit.
[Graphical view]
SMARTiSM00978. Tim44. 1 hit.
[Graphical view]
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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adipose tissue.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Ovary.
  3. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRM45_HUMAN
AccessioniPrimary (citable) accession number: Q9BRJ2
Secondary accession number(s): A1L436, Q6ZMJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: April 4, 2003
Last modified: April 1, 2015
This is version 120 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

3D-structure, 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. 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.