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Protein

40S ribosomal protein S6

Gene

RPS6

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

Functioni

May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein kinase binding Source: UniProtKB
  3. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. activation-induced cell death of T cells Source: Ensembl
  2. cellular protein metabolic process Source: Reactome
  3. erythrocyte development Source: Ensembl
  4. G1/S transition of mitotic cell cycle Source: Ensembl
  5. gastrulation Source: Ensembl
  6. gene expression Source: Reactome
  7. glucose homeostasis Source: UniProtKB
  8. insulin receptor signaling pathway Source: Reactome
  9. mitotic cell cycle checkpoint Source: Ensembl
  10. mitotic nuclear division Source: Ensembl
  11. negative regulation of apoptotic process Source: Ensembl
  12. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  13. oogenesis stage Source: Ensembl
  14. placenta development Source: Ensembl
  15. positive regulation of apoptotic process Source: UniProtKB
  16. ribosomal small subunit assembly Source: Ensembl
  17. ribosomal small subunit biogenesis Source: UniProtKB
  18. rRNA processing Source: UniProtKB
  19. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  20. T cell differentiation in thymus Source: Ensembl
  21. T cell proliferation involved in immune response Source: Ensembl
  22. TOR signaling Source: UniProtKB
  23. translation Source: UniProtKB
  24. translational elongation Source: Reactome
  25. translational initiation Source: Reactome
  26. translational termination Source: Reactome
  27. viral life cycle Source: Reactome
  28. viral process Source: Reactome
  29. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

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_6772. S6K1 signalling.
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.
SignaLinkiP62753.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S6
Alternative name(s):
Phosphoprotein NP33
Gene namesi
Name:RPS6
ORF Names:OK/SW-cl.2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:10429. RPS6.

Subcellular locationi

GO - Cellular componenti

  1. cell body Source: ParkinsonsUK-UCL
  2. cytoplasm Source: HPA
  3. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  4. cytosol Source: Reactome
  5. cytosolic small ribosomal subunit Source: UniProtKB
  6. dendrite Source: ParkinsonsUK-UCL
  7. membrane Source: UniProtKB
  8. nucleolus Source: UniProtKB
  9. nucleus Source: UniProtKB
  10. perinuclear region of cytoplasm Source: Ensembl
  11. polysome Source: Ensembl
  12. ribonucleoprotein complex Source: MGI
  13. small ribosomal subunit Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi235 – 2362SS → AA: Abolishes phosphorylation by PASK. 1 Publication

Organism-specific databases

PharmGKBiPA34844.

Polymorphism and mutation databases

BioMutaiRPS6.
DMDMi51338632.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24924940S ribosomal protein S6PRO_0000137312Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei211 – 2111N6-acetyllysine1 Publication
Modified residuei235 – 2351Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK4 Publications
Modified residuei236 – 2361Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK5 Publications
Modified residuei240 – 2401Phosphoserine3 Publications
Modified residuei242 – 2421Phosphoserine1 Publication
Modified residuei244 – 2441Phosphoserine1 Publication
Modified residuei247 – 2471Phosphoserine1 Publication

Post-translational modificationi

Ribosomal protein S6 is the major substrate of protein kinases in eukaryote ribosomes. The phosphorylation is stimulated by growth factors, tumor promoting agents, and mitogens. It is dephosphorylated at growth arrest. Phosphorylated at Ser-235 and Ser-236 by RPS6KA1 and RPS6KA3; phosphorylation at these sites facilitates the assembly of the preinitiation complex.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62753.
PaxDbiP62753.
PRIDEiP62753.

PTM databases

PhosphoSiteiP62753.

Expressioni

Gene expression databases

BgeeiP62753.
CleanExiHS_RPS6.
ExpressionAtlasiP62753. baseline and differential.
GenevestigatoriP62753.

Organism-specific databases

HPAiCAB004027.
HPA031153.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NCBP1Q091613EBI-356625,EBI-464743
PASKQ96RG23EBI-356625,EBI-1042651

Protein-protein interaction databases

BioGridi112108. 175 interactions.
DIPiDIP-31507N.
IntActiP62753. 41 interactions.
MINTiMINT-1162101.
STRINGi9606.ENSP00000369757.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AG1-249[»]
ProteinModelPortaliP62753.
SMRiP62753. Positions 1-237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S6e family.Curated

Phylogenomic databases

eggNOGiCOG2125.
GeneTreeiENSGT00390000009819.
HOGENOMiHOG000190952.
HOVERGENiHBG011441.
InParanoidiP62753.
KOiK02991.
OMAiRGAITNF.
OrthoDBiEOG7Z0JXB.
PhylomeDBiP62753.
TreeFamiTF300035.

Family and domain databases

InterProiIPR014401. Ribosomal_S6_euk.
IPR001377. Ribosomal_S6e.
IPR018282. Ribosomal_S6e_CS.
[Graphical view]
PANTHERiPTHR11502. PTHR11502. 1 hit.
PfamiPF01092. Ribosomal_S6e. 1 hit.
[Graphical view]
PIRSFiPIRSF002129. Ribosom_S6_euk. 1 hit.
PROSITEiPS00578. RIBOSOMAL_S6E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62753-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV
60 70 80 90 100
RISGGNDKQG FPMKQGVLTH GRVRLLLSKG HSCYRPRRTG ERKRKSVRGC
110 120 130 140 150
IVDANLSVLN LVIVKKGEKD IPGLTDTTVP RRLGPKRASR IRKLFNLSKE
160 170 180 190 200
DDVRQYVVRK PLNKEGKKPR TKAPKIQRLV TPRVLQHKRR RIALKKQRTK
210 220 230 240
KNKEEAAEYA KLLAKRMKEA KEKRQEQIAK RRRLSSLRAS TSKSESSQK
Length:249
Mass (Da):28,681
Last modified:August 1, 1988 - v1
Checksum:iA61E435884E636AE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231K → T in AAA60288 (PubMed:2840355).Curated
Sequence conflicti144 – 1441L → R in AAA60288 (PubMed:2840355).Curated
Sequence conflicti155 – 1562QY → EC in AAA60287 (PubMed:3279029).Curated
Sequence conflicti168 – 1681K → R in AAA60287 (PubMed:3279029).Curated
Sequence conflicti196 – 1961K → Q in AAA60288 (PubMed:2840355).Curated
Sequence conflicti219 – 2191E → Q in AAA60287 (PubMed:3279029).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211K → R.1 Publication
Corresponds to variant rs17852447 [ dbSNP | Ensembl ].
VAR_025314

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20020 mRNA. Translation: AAA60288.1.
J03537 mRNA. Translation: AAA60287.1.
X67309 Genomic DNA. Translation: CAA47719.1.
M77232 Genomic DNA. Translation: AAA60289.1.
AB062123 mRNA. Translation: BAB93455.1.
BC000524 mRNA. Translation: AAH00524.1.
BC009427 mRNA. Translation: AAH09427.2.
BC027620 mRNA. Translation: AAH27620.1.
BC071907 mRNA. Translation: AAH71907.1.
BC071908 mRNA. Translation: AAH71908.1.
BC094826 mRNA. Translation: AAH94826.1.
CCDSiCCDS6492.1.
PIRiJC1394. R3HU6.
RefSeqiNP_001001.2. NM_001010.2.
UniGeneiHs.408073.

Genome annotation databases

EnsembliENST00000380394; ENSP00000369757; ENSG00000137154.
GeneIDi6194.
KEGGihsa:6194.
UCSCiuc003znv.1. human.

Polymorphism and mutation databases

BioMutaiRPS6.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20020 mRNA. Translation: AAA60288.1.
J03537 mRNA. Translation: AAA60287.1.
X67309 Genomic DNA. Translation: CAA47719.1.
M77232 Genomic DNA. Translation: AAA60289.1.
AB062123 mRNA. Translation: BAB93455.1.
BC000524 mRNA. Translation: AAH00524.1.
BC009427 mRNA. Translation: AAH09427.2.
BC027620 mRNA. Translation: AAH27620.1.
BC071907 mRNA. Translation: AAH71907.1.
BC071908 mRNA. Translation: AAH71908.1.
BC094826 mRNA. Translation: AAH94826.1.
CCDSiCCDS6492.1.
PIRiJC1394. R3HU6.
RefSeqiNP_001001.2. NM_001010.2.
UniGeneiHs.408073.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AG1-249[»]
ProteinModelPortaliP62753.
SMRiP62753. Positions 1-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112108. 175 interactions.
DIPiDIP-31507N.
IntActiP62753. 41 interactions.
MINTiMINT-1162101.
STRINGi9606.ENSP00000369757.

PTM databases

PhosphoSiteiP62753.

Polymorphism and mutation databases

BioMutaiRPS6.
DMDMi51338632.

Proteomic databases

MaxQBiP62753.
PaxDbiP62753.
PRIDEiP62753.

Protocols and materials databases

DNASUi6194.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380394; ENSP00000369757; ENSG00000137154.
GeneIDi6194.
KEGGihsa:6194.
UCSCiuc003znv.1. human.

Organism-specific databases

CTDi6194.
GeneCardsiGC09M019366.
HGNCiHGNC:10429. RPS6.
HPAiCAB004027.
HPA031153.
MIMi180460. gene.
neXtProtiNX_P62753.
PharmGKBiPA34844.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2125.
GeneTreeiENSGT00390000009819.
HOGENOMiHOG000190952.
HOVERGENiHBG011441.
InParanoidiP62753.
KOiK02991.
OMAiRGAITNF.
OrthoDBiEOG7Z0JXB.
PhylomeDBiP62753.
TreeFamiTF300035.

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_6772. S6K1 signalling.
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.
SignaLinkiP62753.

Miscellaneous databases

ChiTaRSiRPS6. human.
GenomeRNAii6194.
NextBioi24053.
PROiP62753.
SOURCEiSearch...

Gene expression databases

BgeeiP62753.
CleanExiHS_RPS6.
ExpressionAtlasiP62753. baseline and differential.
GenevestigatoriP62753.

Family and domain databases

InterProiIPR014401. Ribosomal_S6_euk.
IPR001377. Ribosomal_S6e.
IPR018282. Ribosomal_S6e_CS.
[Graphical view]
PANTHERiPTHR11502. PTHR11502. 1 hit.
PfamiPF01092. Ribosomal_S6e. 1 hit.
[Graphical view]
PIRSFiPIRSF002129. Ribosom_S6_euk. 1 hit.
PROSITEiPS00578. RIBOSOMAL_S6E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of cloned cDNAs that code for human ribosomal protein S6."
    Lott J.B., Mackie G.A.
    Gene 65:31-39(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The primary structure of the human ribosomal protein S6 derived from a cloned cDNA."
    Heinze H., Arnold H.H., Fischer D., Kruppa J.
    J. Biol. Chem. 263:4139-4144(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The organization of the intron-containing human S6 ribosomal protein (rpS6) gene and determination of its location at chromosome 9p21."
    Antoine M., Fried M.
    Hum. Mol. Genet. 1:565-570(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The human ribosomal protein S6 gene: isolation, primary structure and location in chromosome 9."
    Pata I., Hoth S., Kruppa J., Metspalu A.
    Gene 121:387-392(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
    Shichijo S., Itoh K.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon adenocarcinoma.
  6. "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], VARIANT ARG-221.
    Tissue: Colon, Muscle, Pancreas, Skin and Testis.
  7. "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 1-15.
    Tissue: Placenta.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation."
    Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J., Sonenberg N., Blenis J.
    J. Biol. Chem. 282:14056-14064(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-235 AND SER-236.
  10. "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.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-236; SER-240; SER-244 AND SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Peptide combinatorial libraries identify TSC2 as a death-associated protein kinase (DAPK) death domain-binding protein and reveal a stimulatory role for DAPK in mTORC1 signaling."
    Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O., Hupp T.
    J. Biol. Chem. 284:334-344(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-235 AND SER-236 BY DAPK1.
  13. "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-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Substrate preference and phosphatidylinositol monophosphate inhibition of the catalytic domain of the Per-Arnt-Sim domain kinase PASKIN."
    Schlafli P., Troger J., Eckhardt K., Borter E., Spielmann P., Wenger R.H.
    FEBS J. 278:1757-1768(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-235 AND SER-236, MUTAGENESIS OF 235-SER-SER-236.
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-240 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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.
  20. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRS6_HUMAN
AccessioniPrimary (citable) accession number: P62753
Secondary accession number(s): P08227
, P10660, Q4VBY7, Q8N6Z7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 29, 2015
This is version 123 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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.