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Protein

39S ribosomal protein L36, mitochondrial

Gene

MRPL36

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

Functioni

Component of the large subunit of the mitochondrial ribosome.Curated

GO - Molecular functioni

  1. 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
  6. ribosome biogenesis Source: GO_Central
  7. translation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_267602. Mitochondrial translation termination.
REACT_267677. Mitochondrial translation elongation.
REACT_267680. Mitochondrial translation initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L36, mitochondrial
Short name:
L36mt
Short name:
MRP-L36
Alternative name(s):
BRCA1-interacting protein 1
Gene namesi
Name:MRPL36
Synonyms:BRIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:14490. MRPL36.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Reactome
  2. mitochondrial large ribosomal subunit Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30967.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 10339S ribosomal protein L36, mitochondrialPRO_0000030529
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

PRIDEiQ9P0J6.

Expressioni

Gene expression databases

BgeeiQ9P0J6.
CleanExiHS_BRIP1.
HS_MRPL36.
ExpressionAtlasiQ9P0J6. baseline and differential.
GenevestigatoriQ9P0J6.

Organism-specific databases

HPAiHPA047238.

Interactioni

Protein-protein interaction databases

BioGridi122366. 3 interactions.
IntActiQ9P0J6. 1 interaction.
MINTiMINT-1526761.
STRINGi9606.ENSP00000372093.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.4041-103[»]
ProteinModelPortaliQ9P0J6.
SMRiQ9P0J6. Positions 67-102.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L36P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG267357.
GeneTreeiENSGT00390000010866.
HOGENOMiHOG000111586.
HOVERGENiHBG029144.
InParanoidiQ9P0J6.
KOiK02919.
OMAiIKERCKD.
OrthoDBiEOG79CZ1X.
PhylomeDBiQ9P0J6.
TreeFamiTF300275.

Family and domain databases

HAMAPiMF_00251. Ribosomal_L36.
InterProiIPR000473. Ribosomal_L36.
[Graphical view]
PANTHERiPTHR18804. PTHR18804. 1 hit.
PfamiPF00444. Ribosomal_L36. 1 hit.
[Graphical view]
SUPFAMiSSF57840. SSF57840. 1 hit.
TIGRFAMsiTIGR01022. rpmJ_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9P0J6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANLFIRKMV NPLLYLSRHT VKPRALSTFL FGSIRGAAPV AVEPGAAVRS
60 70 80 90 100
LLSPGLLPHL LPALGFKNKT VLKKRCKDCY LVKRRGRWYV YCKTHPRHKQ

RQM
Length:103
Mass (Da):11,784
Last modified:October 1, 2000 - v1
Checksum:iCF1720639DE3C34B
GO

Sequence cautioni

The sequence AAF04788.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361G → S in AAF04788 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049654 mRNA. Translation: BAB40859.1.
AF151109 mRNA. Translation: AAF04788.1. Different initiation.
EF036487 mRNA. Translation: ABO65073.1.
AF155653 mRNA. Translation: AAF67010.1.
AK312001 mRNA. Translation: BAG34939.1.
CH471102 Genomic DNA. Translation: EAX08145.1.
BC020642 mRNA. Translation: AAH20642.1.
BC104652 mRNA. Translation: AAI04653.1.
CCDSiCCDS3865.1.
RefSeqiNP_115868.1. NM_032479.3.
UniGeneiHs.719465.

Genome annotation databases

EnsembliENST00000382647; ENSP00000372093; ENSG00000171421.
ENST00000505059; ENSP00000423152; ENSG00000171421.
ENST00000505818; ENSP00000427152; ENSG00000171421.
ENST00000508987; ENSP00000423399; ENSG00000171421.
GeneIDi64979.
KEGGihsa:64979.
UCSCiuc003jcx.4. human.

Polymorphism databases

DMDMi24212267.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049654 mRNA. Translation: BAB40859.1.
AF151109 mRNA. Translation: AAF04788.1. Different initiation.
EF036487 mRNA. Translation: ABO65073.1.
AF155653 mRNA. Translation: AAF67010.1.
AK312001 mRNA. Translation: BAG34939.1.
CH471102 Genomic DNA. Translation: EAX08145.1.
BC020642 mRNA. Translation: AAH20642.1.
BC104652 mRNA. Translation: AAI04653.1.
CCDSiCCDS3865.1.
RefSeqiNP_115868.1. NM_032479.3.
UniGeneiHs.719465.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.4041-103[»]
ProteinModelPortaliQ9P0J6.
SMRiQ9P0J6. Positions 67-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122366. 3 interactions.
IntActiQ9P0J6. 1 interaction.
MINTiMINT-1526761.
STRINGi9606.ENSP00000372093.

Polymorphism databases

DMDMi24212267.

Proteomic databases

PRIDEiQ9P0J6.

Protocols and materials databases

DNASUi64979.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000382647; ENSP00000372093; ENSG00000171421.
ENST00000505059; ENSP00000423152; ENSG00000171421.
ENST00000505818; ENSP00000427152; ENSG00000171421.
ENST00000508987; ENSP00000423399; ENSG00000171421.
GeneIDi64979.
KEGGihsa:64979.
UCSCiuc003jcx.4. human.

Organism-specific databases

CTDi64979.
GeneCardsiGC05M001851.
HGNCiHGNC:14490. MRPL36.
HPAiHPA047238.
MIMi611842. gene.
neXtProtiNX_Q9P0J6.
PharmGKBiPA30967.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG267357.
GeneTreeiENSGT00390000010866.
HOGENOMiHOG000111586.
HOVERGENiHBG029144.
InParanoidiQ9P0J6.
KOiK02919.
OMAiIKERCKD.
OrthoDBiEOG79CZ1X.
PhylomeDBiQ9P0J6.
TreeFamiTF300275.

Enzyme and pathway databases

ReactomeiREACT_267602. Mitochondrial translation termination.
REACT_267677. Mitochondrial translation elongation.
REACT_267680. Mitochondrial translation initiation.

Miscellaneous databases

ChiTaRSiMRPL36. human.
GenomeRNAii64979.
NextBioi67168.
PROiQ9P0J6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P0J6.
CleanExiHS_BRIP1.
HS_MRPL36.
ExpressionAtlasiQ9P0J6. baseline and differential.
GenevestigatoriQ9P0J6.

Family and domain databases

HAMAPiMF_00251. Ribosomal_L36.
InterProiIPR000473. Ribosomal_L36.
[Graphical view]
PANTHERiPTHR18804. PTHR18804. 1 hit.
PfamiPF00444. Ribosomal_L36. 1 hit.
[Graphical view]
SUPFAMiSSF57840. SSF57840. 1 hit.
TIGRFAMsiTIGR01022. rpmJ_bact. 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. "BRIP1, a candidate for BRCA1-interacting protein."
    Wang Q., Zhang H., Greene M.I.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Searching for interaction partners of the transcription factor REST/NRSF by two-hybrid screening."
    Santana-Roman H., Curiel-Quesada E., Tapia-Ramirez J.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adrenal gland.
  5. "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: Thalamus.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Testis.

Entry informationi

Entry nameiRM36_HUMAN
AccessioniPrimary (citable) accession number: Q9P0J6
Secondary accession number(s): A4UCS0
, B2R4Z2, Q3SWV6, Q9UKL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 1, 2000
Last modified: March 4, 2015
This is version 107 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 5
    Human chromosome 5: 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.