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Protein

28S ribosomal protein S30, mitochondrial

Gene

MRPS30

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
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. mitochondrial translation Source: Reactome
  3. mitochondrial translational elongation Source: Reactome
  4. mitochondrial translational initiation Source: Reactome
  5. mitochondrial translational termination Source: Reactome
  6. organelle organization Source: Reactome
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:
28S ribosomal protein S30, mitochondrial
Short name:
MRP-S30
Short name:
S30mt
Alternative name(s):
Programmed cell death protein 9
Gene namesi
Name:MRPS30
Synonyms:PDCD9
ORF Names:BM-047
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:8769. MRPS30.

Subcellular locationi

Mitochondrion 1 Publication

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

PharmGKBiPA31018.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 43943928S ribosomal protein S30, mitochondrialPRO_0000087720Add
BLAST

Proteomic databases

MaxQBiQ9NP92.
PaxDbiQ9NP92.
PeptideAtlasiQ9NP92.
PRIDEiQ9NP92.

PTM databases

PhosphoSiteiQ9NP92.

Expressioni

Tissue specificityi

Heart, skeletal muscle, kidney and liver. Lower expression in placenta and peripheral blood leukocytes.2 Publications

Gene expression databases

BgeeiQ9NP92.
CleanExiHS_MRPS30.
GenevestigatoriQ9NP92.

Organism-specific databases

HPAiHPA018686.
HPA021149.

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

BioGridi116091. 69 interactions.
IntActiQ9NP92. 2 interactions.
MINTiMINT-8052234.
STRINGi9606.ENSP00000230914.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40s1-439[»]
ProteinModelPortaliQ9NP92.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S30/L37 family.Curated

Phylogenomic databases

eggNOGiNOG241777.
GeneTreeiENSGT00390000001442.
HOGENOMiHOG000059255.
HOVERGENiHBG036127.
InParanoidiQ9NP92.
KOiK17409.
OMAiKYVVYPQ.
OrthoDBiEOG7SR4M3.
PhylomeDBiQ9NP92.
TreeFamiTF320686.

Family and domain databases

InterProiIPR010793. Ribosomal_L37/S30.
[Graphical view]
PfamiPF07147. PDCD9. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NP92-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAARCWRPL LRGPRLSLHT AANAAATATE TTCQDVAATP VARYPPIVAS
60 70 80 90 100
MTADSKAARL RRIERWQATV HAAESVDEKL RILTKMQFMK YMVYPQTFAL
110 120 130 140 150
NADRWYQYFT KTVFLSGLPP PPAEPEPEPE PEPEPALDLA ALRAVACDCL
160 170 180 190 200
LQEHFYLRRR RRVHRYEESE VISLPFLDQL VSTLVGLLSP HNPALAAAAL
210 220 230 240 250
DYRCPVHFYW VRGEEIIPRG HRRGRIDDLR YQIDDKPNNQ IRISKQLAEF
260 270 280 290 300
VPLDYSVPIE IPTIKCKPDK LPLFKRQYEN HIFVGSKTAD PCCYGHTQFH
310 320 330 340 350
LLPDKLRRER LLRQNCADQI EVVFRANAIA SLFAWTGAQA MYQGFWSEAD
360 370 380 390 400
VTRPFVSQAV ITDGKYFSFF CYQLNTLALT TQADQNNPRK NICWGTQSKP
410 420 430
LYETIEDNDV KGFNDDVLLQ IVHFLLNRPK EEKSQLLEN
Length:439
Mass (Da):50,365
Last modified:October 17, 2006 - v2
Checksum:i2A22DB6170F6D04F
GO

Sequence cautioni

The sequence AAF67634.1 differs from that shown.Sequencing errors.Curated
The sequence AAF67634.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821I → V in CAB66641 (PubMed:11230166).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331C → S.3 Publications
Corresponds to variant rs3747479 [ dbSNP | Ensembl ].
VAR_028023
Natural varianti102 – 1021A → V.
Corresponds to variant rs35601455 [ dbSNP | Ensembl ].
VAR_052048

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF146192 mRNA. Translation: AAF65227.1.
AL355715 mRNA. Translation: CAB90810.1.
AL355716 mRNA. Translation: CAB90811.1.
AL136706 mRNA. Translation: CAB66641.1.
AK074777 mRNA. Translation: BAC11202.1.
BC007735 mRNA. Translation: AAH07735.1.
AF217523 mRNA. Translation: AAF67634.1. Sequence problems.
AB061211 Genomic DNA. Translation: BAB54961.1.
CCDSiCCDS3951.1.
RefSeqiNP_057724.2. NM_016640.3.
UniGeneiHs.124165.

Genome annotation databases

GeneIDi10884.
KEGGihsa:10884.
UCSCiuc003joh.3. human.

Polymorphism databases

DMDMi116242771.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF146192 mRNA. Translation: AAF65227.1.
AL355715 mRNA. Translation: CAB90810.1.
AL355716 mRNA. Translation: CAB90811.1.
AL136706 mRNA. Translation: CAB66641.1.
AK074777 mRNA. Translation: BAC11202.1.
BC007735 mRNA. Translation: AAH07735.1.
AF217523 mRNA. Translation: AAF67634.1. Sequence problems.
AB061211 Genomic DNA. Translation: BAB54961.1.
CCDSiCCDS3951.1.
RefSeqiNP_057724.2. NM_016640.3.
UniGeneiHs.124165.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40s1-439[»]
ProteinModelPortaliQ9NP92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116091. 69 interactions.
IntActiQ9NP92. 2 interactions.
MINTiMINT-8052234.
STRINGi9606.ENSP00000230914.

PTM databases

PhosphoSiteiQ9NP92.

Polymorphism databases

DMDMi116242771.

Proteomic databases

MaxQBiQ9NP92.
PaxDbiQ9NP92.
PeptideAtlasiQ9NP92.
PRIDEiQ9NP92.

Protocols and materials databases

DNASUi10884.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi10884.
KEGGihsa:10884.
UCSCiuc003joh.3. human.

Organism-specific databases

CTDi10884.
GeneCardsiGC05P044809.
HGNCiHGNC:8769. MRPS30.
HPAiHPA018686.
HPA021149.
MIMi611991. gene.
neXtProtiNX_Q9NP92.
PharmGKBiPA31018.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG241777.
GeneTreeiENSGT00390000001442.
HOGENOMiHOG000059255.
HOVERGENiHBG036127.
InParanoidiQ9NP92.
KOiK17409.
OMAiKYVVYPQ.
OrthoDBiEOG7SR4M3.
PhylomeDBiQ9NP92.
TreeFamiTF320686.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMRPS30. human.
GeneWikiiMRPS30.
GenomeRNAii10884.
NextBioi41327.
PROiQ9NP92.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NP92.
CleanExiHS_MRPS30.
GenevestigatoriQ9NP92.

Family and domain databases

InterProiIPR010793. Ribosomal_L37/S30.
[Graphical view]
PfamiPF07147. PDCD9. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and mapping of PDCD9, the human homolog of Gallus gallus pro-apoptotic protein p52."
    Carim-Todd L., Sumoy L., Nadal M., Estivill X., Escarceller M.
    Cytogenet. Cell Genet. 87:85-88(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT SER-33.
  2. The European IMAGE consortium
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-33.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-33.
    Tissue: Kidney.
  4. "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: Teratocarcinoma.
  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: Muscle.
  6. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-439.
    Tissue: Bone marrow.
  7. "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 275-284.
  8. "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.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRT30_HUMAN
AccessioniPrimary (citable) accession number: Q9NP92
Secondary accession number(s): Q96I91
, Q96Q19, Q9H0P8, Q9NSF9, Q9NZ76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 17, 2006
Last modified: March 4, 2015
This is version 115 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 5
    Human chromosome 5: 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.