Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

28S ribosomal protein S9, mitochondrial

Gene

MRPS9

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: InterPro

GO - Biological processi

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 S9, mitochondrial
Short name:
MRP-S9
Short name:
S9mt
Gene namesi
Name:MRPS9
Synonyms:RPMS9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:14501. MRPS9.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: Reactome
  • mitochondrial small ribosomal subunit Source: UniProtKB
  • mitochondrion Source: HPA
  • nucleolus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31028.

Polymorphism and mutation databases

BioMutaiMRPS9.
DMDMi218511769.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 39628S ribosomal protein S9, mitochondrialPRO_0000030655
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei287 – 2871N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP82933.
PaxDbiP82933.
PRIDEiP82933.

PTM databases

PhosphoSiteiP82933.

Expressioni

Gene expression databases

BgeeiP82933.
CleanExiHS_MRPS9.
ExpressionAtlasiP82933. baseline and differential.
GenevestigatoriP82933.

Organism-specific databases

HPAiHPA043476.
HPA048479.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
revP046182EBI-721385,EBI-6164309From a different organism.

Protein-protein interaction databases

BioGridi122360. 62 interactions.
IntActiP82933. 9 interactions.
MINTiMINT-1379488.
STRINGi9606.ENSP00000258455.

Structurei

3D structure databases

ProteinModelPortaliP82933.
SMRiP82933. Positions 68-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S9P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0103.
GeneTreeiENSGT00390000011204.
HOGENOMiHOG000020877.
HOVERGENiHBG023132.
InParanoidiP82933.
KOiK02996.
OMAiARPVMKH.
OrthoDBiEOG79PJPF.
PhylomeDBiP82933.
TreeFamiTF106154.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000754. Ribosomal_S9.
IPR020574. Ribosomal_S9_CS.
[Graphical view]
PANTHERiPTHR21569. PTHR21569. 1 hit.
PfamiPF00380. Ribosomal_S9. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P82933-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPCVSYGG AVSYRLLLWG RGSLARKQGL WKTAAPELQT NVRSQILRLR
60 70 80 90 100
HTAFVIPKKN VPTSKRETYT EDFIKKQIEE FNIGKRHLAN MMGEDPETFT
110 120 130 140 150
QEDIDRAIAY LFPSGLFEKR ARPVMKHPEQ IFPRQRAIQW GEDGRPFHYL
160 170 180 190 200
FYTGKQSYYS LMHDVYGMLL NLEKHQSHLQ AKSLLPEKTV TRDVIGSRWL
210 220 230 240 250
IKEELEEMLV EKLSDLDYMQ FIRLLEKLLT SQCGAAEEEF VQRFRRSVTL
260 270 280 290 300
ESKKQLIEPV QYDEQGMAFS KSEGKRKTAK AEAIVYKHGS GRIKVNGIDY
310 320 330 340 350
QLYFPITQDR EQLMFPFHFV DRLGKHDVTC TVSGGGRSAQ AGAIRLAMAK
360 370 380 390
ALCSFVTEDE VEWMRQAGLL TTDPRVRERK KPGQEGARRK FTWKKR
Length:396
Mass (Da):45,835
Last modified:December 16, 2008 - v2
Checksum:i74412E34F0926360
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131S → L.
Corresponds to variant rs13399067 [ dbSNP | Ensembl ].
VAR_047902

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC010884 Genomic DNA. No translation available.
AC107080 Genomic DNA. No translation available.
AC104655 Genomic DNA. No translation available.
CH471127 Genomic DNA. Translation: EAX01767.1.
BC057240 mRNA. Translation: AAH57240.1.
CCDSiCCDS2065.1.
RefSeqiNP_872578.1. NM_182640.2.
UniGeneiHs.590900.

Genome annotation databases

EnsembliENST00000258455; ENSP00000258455; ENSG00000135972.
GeneIDi64965.
KEGGihsa:64965.
UCSCiuc002tcn.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC010884 Genomic DNA. No translation available.
AC107080 Genomic DNA. No translation available.
AC104655 Genomic DNA. No translation available.
CH471127 Genomic DNA. Translation: EAX01767.1.
BC057240 mRNA. Translation: AAH57240.1.
CCDSiCCDS2065.1.
RefSeqiNP_872578.1. NM_182640.2.
UniGeneiHs.590900.

3D structure databases

ProteinModelPortaliP82933.
SMRiP82933. Positions 68-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122360. 62 interactions.
IntActiP82933. 9 interactions.
MINTiMINT-1379488.
STRINGi9606.ENSP00000258455.

PTM databases

PhosphoSiteiP82933.

Polymorphism and mutation databases

BioMutaiMRPS9.
DMDMi218511769.

Proteomic databases

MaxQBiP82933.
PaxDbiP82933.
PRIDEiP82933.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258455; ENSP00000258455; ENSG00000135972.
GeneIDi64965.
KEGGihsa:64965.
UCSCiuc002tcn.4. human.

Organism-specific databases

CTDi64965.
GeneCardsiGC02P105654.
HGNCiHGNC:14501. MRPS9.
HPAiHPA043476.
HPA048479.
MIMi611975. gene.
neXtProtiNX_P82933.
PharmGKBiPA31028.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0103.
GeneTreeiENSGT00390000011204.
HOGENOMiHOG000020877.
HOVERGENiHBG023132.
InParanoidiP82933.
KOiK02996.
OMAiARPVMKH.
OrthoDBiEOG79PJPF.
PhylomeDBiP82933.
TreeFamiTF106154.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMRPS9. human.
GenomeRNAii64965.
NextBioi67144.
PROiP82933.
SOURCEiSearch...

Gene expression databases

BgeeiP82933.
CleanExiHS_MRPS9.
ExpressionAtlasiP82933. baseline and differential.
GenevestigatoriP82933.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000754. Ribosomal_S9.
IPR020574. Ribosomal_S9_CS.
[Graphical view]
PANTHERiPTHR21569. PTHR21569. 1 hit.
PfamiPF00380. Ribosomal_S9. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
  4. "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.
  5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRT09_HUMAN
AccessioniPrimary (citable) accession number: P82933
Secondary accession number(s): Q6PG40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: December 16, 2008
Last modified: April 29, 2015
This is version 116 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. Ribosomal proteins
    Ribosomal proteins families and list of entries
  6. 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.