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Protein

28S ribosomal protein S15, mitochondrial

Gene

MRPS15

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

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  • mitochondrial translation Source: UniProtKB
  • mitochondrial translational elongation Source: Reactome
  • mitochondrial translational initiation Source: Reactome
  • mitochondrial translational termination Source: Reactome
  • organelle organization Source: Reactome
  • translation Source: UniProtKB
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:
28S ribosomal protein S15, mitochondrial
Short name:
MRP-S15
Short name:
S15mt
Gene namesi
Name:MRPS15
Synonyms:RPMS15
ORF Names:DC37
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:14504. MRPS15.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30999.

Polymorphism and mutation databases

BioMutaiMRPS15.
DMDMi13633907.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5757MitochondrionSequence AnalysisAdd
BLAST
Chaini58 – 25720028S ribosomal protein S15, mitochondrialPRO_0000030614Add
BLAST

Proteomic databases

MaxQBiP82914.
PaxDbiP82914.
PRIDEiP82914.

PTM databases

PhosphoSiteiP82914.

Expressioni

Gene expression databases

BgeeiP82914.
CleanExiHS_MRPS15.
GenevisibleiP82914. HS.

Organism-specific databases

HPAiHPA028100.
HPA028134.

Interactioni

Subunit structurei

Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins.

Protein-protein interaction databases

BioGridi122358. 42 interactions.
IntActiP82914. 6 interactions.
STRINGi9606.ENSP00000362208.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J9Melectron microscopy3.50AL1-257[»]
ProteinModelPortaliP82914.
SMRiP82914. Positions 56-257.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S15P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG298367.
GeneTreeiENSGT00390000001737.
HOGENOMiHOG000231143.
HOVERGENiHBG017757.
InParanoidiP82914.
KOiK02956.
OMAiRKAHRRW.
OrthoDBiEOG74XS86.
PhylomeDBiP82914.
TreeFamiTF319038.

Family and domain databases

Gene3Di1.10.287.10. 1 hit.
HAMAPiMF_01343_B. Ribosomal_S15_B.
InterProiIPR000589. Ribosomal_S15.
IPR005290. Ribosomal_S15_bac-type.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamiPF00312. Ribosomal_S15. 1 hit.
[Graphical view]
SUPFAMiSSF47060. SSF47060. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P82914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRVAWRTLS LIRTRAVTQV LVPGLPGGGS AKFPFNQWGL QPRSLLLQAA
60 70 80 90 100
RGYVVRKPAQ SRLDDDPPPS TLLKDYQNVP GIEKVDDVVK RLLSLEMANK
110 120 130 140 150
KEMLKIKQEQ FMKKIVANPE DTRSLEARII ALSVKIRSYE EHLEKHRKDK
160 170 180 190 200
AHKRYLLMSI DQRKKMLKNL RNTNYDVFEK ICWGLGIEYT FPPLYYRRAH
210 220 230 240 250
RRFVTKKALC IRVFQETQKL KKRRRALKAA AAAQKQAKRR NPDSPAKAIP

KTLKDSQ
Length:257
Mass (Da):29,842
Last modified:March 1, 2001 - v1
Checksum:iB2D951BC47B8FFEB
GO

Sequence cautioni

The sequence AAG44697.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 7953GGGSA…DYQNV → AVGAPSFLSTSGACSLEVSS SRPRADMSSGNQPSLGWMMT HLLLRCSKTTRMS in AAG44697 (Ref. 2) CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049946 mRNA. Translation: BAB40999.1.
AF265439 mRNA. Translation: AAG44697.1. Different initiation.
AK315441 mRNA. Translation: BAG37829.1.
CH471059 Genomic DNA. Translation: EAX07359.1.
BC031336 mRNA. Translation: AAH31336.1.
CCDSiCCDS411.1.
RefSeqiNP_112570.2. NM_031280.3.
UniGeneiHs.352839.

Genome annotation databases

EnsembliENST00000373116; ENSP00000362208; ENSG00000116898.
GeneIDi64960.
KEGGihsa:64960.
UCSCiuc001cas.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049946 mRNA. Translation: BAB40999.1.
AF265439 mRNA. Translation: AAG44697.1. Different initiation.
AK315441 mRNA. Translation: BAG37829.1.
CH471059 Genomic DNA. Translation: EAX07359.1.
BC031336 mRNA. Translation: AAH31336.1.
CCDSiCCDS411.1.
RefSeqiNP_112570.2. NM_031280.3.
UniGeneiHs.352839.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J9Melectron microscopy3.50AL1-257[»]
ProteinModelPortaliP82914.
SMRiP82914. Positions 56-257.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122358. 42 interactions.
IntActiP82914. 6 interactions.
STRINGi9606.ENSP00000362208.

PTM databases

PhosphoSiteiP82914.

Polymorphism and mutation databases

BioMutaiMRPS15.
DMDMi13633907.

Proteomic databases

MaxQBiP82914.
PaxDbiP82914.
PRIDEiP82914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373116; ENSP00000362208; ENSG00000116898.
GeneIDi64960.
KEGGihsa:64960.
UCSCiuc001cas.2. human.

Organism-specific databases

CTDi64960.
GeneCardsiGC01M036921.
HGNCiHGNC:14504. MRPS15.
HPAiHPA028100.
HPA028134.
MIMi611979. gene.
neXtProtiNX_P82914.
PharmGKBiPA30999.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG298367.
GeneTreeiENSGT00390000001737.
HOGENOMiHOG000231143.
HOVERGENiHBG017757.
InParanoidiP82914.
KOiK02956.
OMAiRKAHRRW.
OrthoDBiEOG74XS86.
PhylomeDBiP82914.
TreeFamiTF319038.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMRPS15. human.
GenomeRNAii64960.
NextBioi67134.
PROiP82914.
SOURCEiSearch...

Gene expression databases

BgeeiP82914.
CleanExiHS_MRPS15.
GenevisibleiP82914. HS.

Family and domain databases

Gene3Di1.10.287.10. 1 hit.
HAMAPiMF_01343_B. Ribosomal_S15_B.
InterProiIPR000589. Ribosomal_S15.
IPR005290. Ribosomal_S15_bac-type.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamiPF00312. Ribosomal_S15. 1 hit.
[Graphical view]
SUPFAMiSSF47060. SSF47060. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Proteomic analysis of the mammalian mitochondrial ribosome. Identification of protein components in the 28S small subunit."
    Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A., Watanabe K.
    J. Biol. Chem. 276:33181-33195(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  2. "Novel genes expressed in human dendritic cell."
    Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Dendritic cell.
  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: Heart.
  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: Skin.
  6. "The small subunit of the mammalian mitochondrial ribosome: identification of the full complement of ribosomal proteins present."
    Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.
    J. Biol. Chem. 276:19363-19374(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRT15_HUMAN
AccessioniPrimary (citable) accession number: P82914
Secondary accession number(s): B2RD82, Q9H2K1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 1, 2001
Last modified: July 22, 2015
This is version 131 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 1
    Human chromosome 1: 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.