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 S18b, mitochondrial

Gene

MRPS18B

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

Functioni

GO - Molecular functioni

  1. structural constituent of ribosome 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
  6. 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 S18b, mitochondrial
Short name:
MRP-S18-b
Short name:
Mrps18-b
Short name:
S18mt-b
Alternative name(s):
28S ribosomal protein S18-2, mitochondrial
Short name:
MRP-S18-2
Gene namesi
Name:MRPS18B
Synonyms:C6orf14
ORF Names:HSPC183, PTD017
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:14516. MRPS18B.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. cell junction Source: HPA
  2. mitochondrial inner membrane Source: Reactome
  3. mitochondrial small ribosomal subunit Source: UniProtKB
  4. mitochondrion Source: HPA
  5. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31004.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 25828S ribosomal protein S18b, mitochondrialPRO_0000030627
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiQ9Y676.
PaxDbiQ9Y676.
PeptideAtlasiQ9Y676.
PRIDEiQ9Y676.

PTM databases

PhosphoSiteiQ9Y676.

Expressioni

Gene expression databases

BgeeiQ9Y676.
CleanExiHS_MRPS18B.
ExpressionAtlasiQ9Y676. baseline and differential.
GenevestigatoriQ9Y676.

Organism-specific databases

HPAiHPA043485.
HPA050334.

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

BioGridi118797. 34 interactions.
DIPiDIP-29894N.
IntActiQ9Y676. 3 interactions.
MINTiMINT-1448435.
STRINGi9606.ENSP00000397790.

Structurei

3D structure databases

ProteinModelPortaliQ9Y676.
SMRiQ9Y676. Positions 102-170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S18P family.1 Publication

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG288650.
GeneTreeiENSGT00390000010554.
HOGENOMiHOG000039992.
HOVERGENiHBG054347.
InParanoidiQ9Y676.
KOiK16174.
OMAiHGLLSYH.
PhylomeDBiQ9Y676.
TreeFamiTF315059.

Family and domain databases

Gene3Di4.10.640.10. 1 hit.
InterProiIPR001648. Ribosomal_S18.
[Graphical view]
PfamiPF01084. Ribosomal_S18. 1 hit.
[Graphical view]
ProDomiPD002239. Ribosomal_S18. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46911. SSF46911. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9Y676-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASVLNTVL RRLPMLSLFR GSHRVQVPLQ TLCTKAPSEE DSLSSVPISP
60 70 80 90 100
YKDEPWKYLE SEEYQERYGS RPVWADYRRN HKGGVPPQRT RKTCIRRNKV
110 120 130 140 150
VGNPCPICRD HKLHVDFRNV KLLEQFVCAH TGIIFYAPYT GVCVKQHKRL
160 170 180 190 200
TQAIQKARDH GLLIYHIPQV EPRDLDFSTS HGAVSATPPA PTLVSGDPWY
210 220 230 240 250
PWYNWKQPPE RELSRLRRLY QGHLQEESGP PPESMPKMPP RTPAEASSTG

QTGPQSAL
Length:258
Mass (Da):29,396
Last modified:October 31, 1999 - v1
Checksum:iB4C83E5593796C5D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961G → S in AAH05373 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti230 – 2301P → A.
Corresponds to variant rs34315095 [ dbSNP | Ensembl ].
VAR_052056

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF100761 mRNA. Translation: AAD43025.1.
AF151017 mRNA. Translation: AAF36103.1.
AL050361 mRNA. Translation: CAH56415.1.
AB110933 Genomic DNA. Translation: BAD13699.1.
AB110934 Genomic DNA. Translation: BAD13700.1.
AB202094 Genomic DNA. Translation: BAE78614.1.
AL662800 Genomic DNA. Translation: CAI18162.2.
AL662825, AL732442 Genomic DNA. Translation: CAI17840.1.
AL732442, AL662825 Genomic DNA. Translation: CAI17765.1.
BX119957 Genomic DNA. Translation: CAM25911.1.
AL845353, BX248507 Genomic DNA. Translation: CAI41878.1.
BX248507, AL845353 Genomic DNA. Translation: CAI18569.1.
CR753328 Genomic DNA. Translation: CAP58452.1.
CH471081 Genomic DNA. Translation: EAX03304.1.
BC005373 mRNA. Translation: AAH05373.1.
CCDSiCCDS4682.1.
RefSeqiNP_054765.1. NM_014046.3.
UniGeneiHs.655329.

Genome annotation databases

GeneIDi28973.
KEGGihsa:28973.
UCSCiuc003nqo.2. human.

Polymorphism databases

DMDMi24212203.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF100761 mRNA. Translation: AAD43025.1.
AF151017 mRNA. Translation: AAF36103.1.
AL050361 mRNA. Translation: CAH56415.1.
AB110933 Genomic DNA. Translation: BAD13699.1.
AB110934 Genomic DNA. Translation: BAD13700.1.
AB202094 Genomic DNA. Translation: BAE78614.1.
AL662800 Genomic DNA. Translation: CAI18162.2.
AL662825, AL732442 Genomic DNA. Translation: CAI17840.1.
AL732442, AL662825 Genomic DNA. Translation: CAI17765.1.
BX119957 Genomic DNA. Translation: CAM25911.1.
AL845353, BX248507 Genomic DNA. Translation: CAI41878.1.
BX248507, AL845353 Genomic DNA. Translation: CAI18569.1.
CR753328 Genomic DNA. Translation: CAP58452.1.
CH471081 Genomic DNA. Translation: EAX03304.1.
BC005373 mRNA. Translation: AAH05373.1.
CCDSiCCDS4682.1.
RefSeqiNP_054765.1. NM_014046.3.
UniGeneiHs.655329.

3D structure databases

ProteinModelPortaliQ9Y676.
SMRiQ9Y676. Positions 102-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118797. 34 interactions.
DIPiDIP-29894N.
IntActiQ9Y676. 3 interactions.
MINTiMINT-1448435.
STRINGi9606.ENSP00000397790.

PTM databases

PhosphoSiteiQ9Y676.

Polymorphism databases

DMDMi24212203.

Proteomic databases

MaxQBiQ9Y676.
PaxDbiQ9Y676.
PeptideAtlasiQ9Y676.
PRIDEiQ9Y676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi28973.
KEGGihsa:28973.
UCSCiuc003nqo.2. human.

Organism-specific databases

CTDi28973.
GeneCardsiGC06P030585.
GC06Pj30575.
GC06Pk30575.
GC06Pl30630.
GC06Pm30663.
GC06Pn30574.
GC06Po30576.
HGNCiHGNC:14516. MRPS18B.
HPAiHPA043485.
HPA050334.
MIMi611982. gene.
neXtProtiNX_Q9Y676.
PharmGKBiPA31004.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG288650.
GeneTreeiENSGT00390000010554.
HOGENOMiHOG000039992.
HOVERGENiHBG054347.
InParanoidiQ9Y676.
KOiK16174.
OMAiHGLLSYH.
PhylomeDBiQ9Y676.
TreeFamiTF315059.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMRPS18B. human.
GeneWikiiMRPS18B.
GenomeRNAii28973.
NextBioi51843.
PROiQ9Y676.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y676.
CleanExiHS_MRPS18B.
ExpressionAtlasiQ9Y676. baseline and differential.
GenevestigatoriQ9Y676.

Family and domain databases

Gene3Di4.10.640.10. 1 hit.
InterProiIPR001648. Ribosomal_S18.
[Graphical view]
PfamiPF01084. Ribosomal_S18. 1 hit.
[Graphical view]
ProDomiPD002239. Ribosomal_S18. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46911. SSF46911. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Zhang Q.H., Guan Z.Q., Dai M., Song H., Mao Y.F., Wu X.Y., Mao M., Fu G., Luo M., Chen J.H., Hu R.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary tumor.
  2. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity."
    Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M., Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K., Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.
    , Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., Inoko H., Bahram S.
    Genetics 173:1555-1570(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Tissue: Peripheral blood leukocyte.
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRT18B_HUMAN
AccessioniPrimary (citable) accession number: Q9Y676
Secondary accession number(s): A6NDQ0, Q659G4, Q9BS27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2002
Last sequence update: October 31, 1999
Last modified: March 31, 2015
This is version 121 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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.