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P46781

- RS9_HUMAN

UniProt

P46781 - RS9_HUMAN

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Protein

40S ribosomal protein S9

Gene

RPS9

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. rRNA binding Source: UniProtKB-KW
  3. structural constituent of ribosome Source: InterPro
  4. translation regulator activity Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  5. positive regulation of cell proliferation Source: UniProtKB
  6. regulation of translation Source: GOC
  7. RNA metabolic process Source: Reactome
  8. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  9. translation Source: UniProtKB
  10. translational elongation Source: Reactome
  11. translational initiation Source: Reactome
  12. translational termination Source: Reactome
  13. viral life cycle Source: Reactome
  14. viral process Source: Reactome
  15. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S9
Gene namesi
Name:RPS9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:10442. RPS9.

Subcellular locationi

Cytoplasm 1 Publication
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. cytosolic small ribosomal subunit Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
  5. focal adhesion Source: UniProtKB
  6. membrane Source: UniProtKB
  7. nucleolus Source: UniProtKB
  8. nucleus Source: UniProt
  9. ribonucleoprotein complex Source: UniProtKB
  10. ribosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34857.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 19419340S ribosomal protein S9PRO_0000132689Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N6-acetyllysineBy similarity
Modified residuei116 – 1161N6-acetyllysineBy similarity
Modified residuei155 – 1551N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP46781.
PaxDbiP46781.
PeptideAtlasiP46781.
PRIDEiP46781.

PTM databases

PhosphoSiteiP46781.

Expressioni

Gene expression databases

BgeeiP46781.
CleanExiHS_RPS9.
ExpressionAtlasiP46781. baseline and differential.
GenevestigatoriP46781.

Organism-specific databases

HPAiHPA048746.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
STAT3P407632EBI-351206,EBI-518675

Protein-protein interaction databases

BioGridi112117. 116 interactions.
IntActiP46781. 22 interactions.
MINTiMINT-5001013.
STRINGi9606.ENSP00000302896.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00J1-194[»]
ProteinModelPortaliP46781.
SMRiP46781. Positions 2-186.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini108 – 18275S4 RNA-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S4P family.Curated
Contains 1 S4 RNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0522.
GeneTreeiENSGT00550000074829.
HOGENOMiHOG000194525.
HOVERGENiHBG001135.
InParanoidiP46781.
KOiK02997.
OMAiVXSLERR.
PhylomeDBiP46781.
TreeFamiTF300795.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
InterProiIPR022801. Ribosomal_S4/S9.
IPR005710. Ribosomal_S4/S9_euk/arc.
IPR001912. Ribosomal_S4/S9_N.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERiPTHR11831. PTHR11831. 1 hit.
PfamiPF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTiSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01018. rpsD_arch. 1 hit.
PROSITEiPS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P46781-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPVARSWVCR KTYVTPRRPF EKSRLDQELK LIGEYGLRNK REVWRVKFTL
60 70 80 90 100
AKIRKAAREL LTLDEKDPRR LFEGNALLRR LVRIGVLDEG KMKLDYILGL
110 120 130 140 150
KIEDFLERRL QTQVFKLGLA KSIHHARVLI RQRHIRVRKQ VVNIPSFIVR
160 170 180 190
LDSQKHIDFS LRSPYGGGRP GRVKRKNAKK GQGGAGAGDD EEED
Length:194
Mass (Da):22,591
Last modified:January 23, 2007 - v3
Checksum:iE9CE3CBD59524F81
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841I → L in AAA85659. (PubMed:7772601)Curated
Sequence conflicti165 – 1673YGG → TGV in AAA85659. (PubMed:7772601)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251L → F.
Corresponds to variant rs41423149 [ dbSNP | Ensembl ].
VAR_052069
Natural varianti137 – 1371V → F in a breast cancer sample; somatic mutation. 1 Publication
VAR_036543

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14971 mRNA. Translation: AAA85659.1.
AB061839 Genomic DNA. Translation: BAB79477.1.
CU457734 Genomic DNA. Translation: CAP19125.1.
CU151838 Genomic DNA. Translation: CAQ09597.1.
CH471135 Genomic DNA. Translation: EAW72209.1.
BC000802 mRNA. Translation: AAH00802.1.
BC007410 mRNA. Translation: AAH07410.1.
BC007434 mRNA. Translation: AAH07434.1.
BC007857 mRNA. Translation: AAH07857.1.
BC068055 mRNA. Translation: AAH68055.1.
BC071940 mRNA. Translation: AAH71940.1.
BC096756 mRNA. Translation: AAH96756.1.
AB007150 Genomic DNA. Translation: BAA25816.1.
CCDSiCCDS12884.1.
PIRiS55917.
RefSeqiNP_001004.2. NM_001013.3.
XP_005259192.1. XM_005259135.1.
XP_005259193.1. XM_005259136.2.
XP_005277141.1. XM_005277084.2.
XP_005277142.1. XM_005277085.1.
XP_005277331.1. XM_005277274.1.
XP_005277372.1. XM_005277315.1.
XP_005277373.1. XM_005277316.2.
XP_005278344.1. XM_005278287.2.
XP_005278345.1. XM_005278288.1.
XP_006725939.1. XM_006725876.1.
XP_006725940.1. XM_006725877.1.
XP_006726027.1. XM_006725964.1.
XP_006726028.1. XM_006725965.1.
XP_006726126.1. XM_006726063.1.
XP_006726127.1. XM_006726064.1.
XP_006726227.1. XM_006726164.1.
XP_006726228.1. XM_006726165.1.
XP_006726264.1. XM_006726201.1.
XP_006726265.1. XM_006726202.1.
UniGeneiHs.467284.
Hs.546288.

Genome annotation databases

EnsembliENST00000302907; ENSP00000302896; ENSG00000170889.
ENST00000391752; ENSP00000375632; ENSG00000170889.
ENST00000391753; ENSP00000375633; ENSG00000170889.
ENST00000610826; ENSP00000481764; ENSG00000278270.
ENST00000610953; ENSP00000482023; ENSG00000278081.
ENST00000611921; ENSP00000480662; ENSG00000274950.
ENST00000614737; ENSP00000482338; ENSG00000278270.
ENST00000615346; ENSP00000481553; ENSG00000274646.
ENST00000616082; ENSP00000482475; ENSG00000274646.
ENST00000616536; ENSP00000481822; ENSG00000274950.
ENST00000616839; ENSP00000484394; ENSG00000277359.
ENST00000616877; ENSP00000481194; ENSG00000274950.
ENST00000616928; ENSP00000481655; ENSG00000274626.
ENST00000617291; ENSP00000482274; ENSG00000274005.
ENST00000618751; ENSP00000480135; ENSG00000275323.
ENST00000619229; ENSP00000479917; ENSG00000278270.
ENST00000620720; ENSP00000478449; ENSG00000277079.
ENST00000620940; ENSP00000483179; ENSG00000274646.
GeneIDi6203.
KEGGihsa:6203.
UCSCiuc002qdx.3. human.

Polymorphism databases

DMDMi20178311.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14971 mRNA. Translation: AAA85659.1 .
AB061839 Genomic DNA. Translation: BAB79477.1 .
CU457734 Genomic DNA. Translation: CAP19125.1 .
CU151838 Genomic DNA. Translation: CAQ09597.1 .
CH471135 Genomic DNA. Translation: EAW72209.1 .
BC000802 mRNA. Translation: AAH00802.1 .
BC007410 mRNA. Translation: AAH07410.1 .
BC007434 mRNA. Translation: AAH07434.1 .
BC007857 mRNA. Translation: AAH07857.1 .
BC068055 mRNA. Translation: AAH68055.1 .
BC071940 mRNA. Translation: AAH71940.1 .
BC096756 mRNA. Translation: AAH96756.1 .
AB007150 Genomic DNA. Translation: BAA25816.1 .
CCDSi CCDS12884.1.
PIRi S55917.
RefSeqi NP_001004.2. NM_001013.3.
XP_005259192.1. XM_005259135.1.
XP_005259193.1. XM_005259136.2.
XP_005277141.1. XM_005277084.2.
XP_005277142.1. XM_005277085.1.
XP_005277331.1. XM_005277274.1.
XP_005277372.1. XM_005277315.1.
XP_005277373.1. XM_005277316.2.
XP_005278344.1. XM_005278287.2.
XP_005278345.1. XM_005278288.1.
XP_006725939.1. XM_006725876.1.
XP_006725940.1. XM_006725877.1.
XP_006726027.1. XM_006725964.1.
XP_006726028.1. XM_006725965.1.
XP_006726126.1. XM_006726063.1.
XP_006726127.1. XM_006726064.1.
XP_006726227.1. XM_006726164.1.
XP_006726228.1. XM_006726165.1.
XP_006726264.1. XM_006726201.1.
XP_006726265.1. XM_006726202.1.
UniGenei Hs.467284.
Hs.546288.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3A electron microscopy 5.00 J 1-194 [» ]
ProteinModelPortali P46781.
SMRi P46781. Positions 2-186.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112117. 116 interactions.
IntActi P46781. 22 interactions.
MINTi MINT-5001013.
STRINGi 9606.ENSP00000302896.

PTM databases

PhosphoSitei P46781.

Polymorphism databases

DMDMi 20178311.

Proteomic databases

MaxQBi P46781.
PaxDbi P46781.
PeptideAtlasi P46781.
PRIDEi P46781.

Protocols and materials databases

DNASUi 6203.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302907 ; ENSP00000302896 ; ENSG00000170889 .
ENST00000391752 ; ENSP00000375632 ; ENSG00000170889 .
ENST00000391753 ; ENSP00000375633 ; ENSG00000170889 .
ENST00000610826 ; ENSP00000481764 ; ENSG00000278270 .
ENST00000610953 ; ENSP00000482023 ; ENSG00000278081 .
ENST00000611921 ; ENSP00000480662 ; ENSG00000274950 .
ENST00000614737 ; ENSP00000482338 ; ENSG00000278270 .
ENST00000615346 ; ENSP00000481553 ; ENSG00000274646 .
ENST00000616082 ; ENSP00000482475 ; ENSG00000274646 .
ENST00000616536 ; ENSP00000481822 ; ENSG00000274950 .
ENST00000616839 ; ENSP00000484394 ; ENSG00000277359 .
ENST00000616877 ; ENSP00000481194 ; ENSG00000274950 .
ENST00000616928 ; ENSP00000481655 ; ENSG00000274626 .
ENST00000617291 ; ENSP00000482274 ; ENSG00000274005 .
ENST00000618751 ; ENSP00000480135 ; ENSG00000275323 .
ENST00000619229 ; ENSP00000479917 ; ENSG00000278270 .
ENST00000620720 ; ENSP00000478449 ; ENSG00000277079 .
ENST00000620940 ; ENSP00000483179 ; ENSG00000274646 .
GeneIDi 6203.
KEGGi hsa:6203.
UCSCi uc002qdx.3. human.

Organism-specific databases

CTDi 6203.
GeneCardsi GC19P054866.
HGNCi HGNC:10442. RPS9.
HPAi HPA048746.
MIMi 603631. gene.
neXtProti NX_P46781.
PharmGKBi PA34857.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0522.
GeneTreei ENSGT00550000074829.
HOGENOMi HOG000194525.
HOVERGENi HBG001135.
InParanoidi P46781.
KOi K02997.
OMAi VXSLERR.
PhylomeDBi P46781.
TreeFami TF300795.

Enzyme and pathway databases

Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSi RPS9. human.
GeneWikii RPS9.
GenomeRNAii 6203.
NextBioi 24091.
PROi P46781.
SOURCEi Search...

Gene expression databases

Bgeei P46781.
CleanExi HS_RPS9.
ExpressionAtlasi P46781. baseline and differential.
Genevestigatori P46781.

Family and domain databases

Gene3Di 3.10.290.10. 1 hit.
InterProi IPR022801. Ribosomal_S4/S9.
IPR005710. Ribosomal_S4/S9_euk/arc.
IPR001912. Ribosomal_S4/S9_N.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view ]
PANTHERi PTHR11831. PTHR11831. 1 hit.
Pfami PF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view ]
SMARTi SM00363. S4. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01018. rpsD_arch. 1 hit.
PROSITEi PS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs."
    Frigerio J.-M., Dagorn J.-C., Iovanna J.L.
    Biochim. Biophys. Acta 1262:64-68(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Colon.
  2. "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
    Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
    Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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: Brain, Muscle, Placenta and Skin.
  6. "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
    Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
    Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19.
    Tissue: Placenta.
  7. "A map of 75 human ribosomal protein genes."
    Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
    Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-73.
  8. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-137.

Entry informationi

Entry nameiRS9_HUMAN
AccessioniPrimary (citable) accession number: P46781
Secondary accession number(s): A9C4C1, Q4QRK7, Q9BVZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 151 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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