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Protein

40S ribosomal protein S2

Gene

RPS2

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

Functioni

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • fibroblast growth factor binding Source: UniProtKB
  • mRNA binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

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_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 S2
Alternative name(s):
40S ribosomal protein S4
Protein LLRep3
Gene namesi
Name:RPS2
Synonyms:RPS4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:10404. RPS2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic small ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34806.

Polymorphism and mutation databases

BioMutaiRPS2.
DMDMi1710756.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 29329240S ribosomal protein S2PRO_0000131673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei263 – 2631N6-acetyllysine1 Publication
Modified residuei264 – 2641Phosphoserine2 Publications
Modified residuei275 – 2751N6-acetyllysine1 Publication
Modified residuei281 – 2811Phosphoserine1 Publication

Post-translational modificationi

Citrullinated by PADI4 in the Arg/Gly-rich region.1 Publication
Asymmetric arginine dimethylation by PRMT3 occurs at multiple sites in the Arg/Gly-rich region.

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP15880.
PaxDbiP15880.
PRIDEiP15880.

PTM databases

PhosphoSiteiP15880.

Expressioni

Gene expression databases

BgeeiP15880.
CleanExiHS_RPS2.
ExpressionAtlasiP15880. baseline.
GenevestigatoriP15880.

Organism-specific databases

HPAiHPA055133.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0072EBI-443446,EBI-5323863

Protein-protein interaction databases

BioGridi112101. 232 interactions.
IntActiP15880. 32 interactions.
MINTiMINT-3008399.
STRINGi9606.ENSP00000341885.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AC1-293[»]
ProteinModelPortaliP15880.
SMRiP15880. Positions 53-278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini102 – 16564S5 DRBMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 5332Arg/Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S5P family.Curated
Contains 1 S5 DRBM domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0098.
GeneTreeiENSGT00390000001433.
HOGENOMiHOG000072596.
HOVERGENiHBG000437.
InParanoidiP15880.
KOiK02981.
OMAiGIKDVWT.
OrthoDBiEOG7P5T1Q.
PhylomeDBiP15880.
TreeFamiTF300806.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
InterProiIPR014720. dsRNA-bd_dom.
IPR000851. Ribosomal_S5.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005711. Ribosomal_S5_euk/arc.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]
PANTHERiPTHR13718. PTHR13718. 1 hit.
PfamiPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR01020. uS5_euk_arch. 1 hit.
PROSITEiPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15880-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADDAGAAGG PGGPGGPGMG NRGGFRGGFG SGIRGRGRGR GRGRGRGRGA
60 70 80 90 100
RGGKAEDKEW MPVTKLGRLV KDMKIKSLEE IYLFSLPIKE SEIIDFFLGA
110 120 130 140 150
SLKDEVLKIM PVQKQTRAGQ RTRFKAFVAI GDYNGHVGLG VKCSKEVATA
160 170 180 190 200
IRGAIILAKL SIVPVRRGYW GNKIGKPHTV PCKVTGRCGS VLVRLIPAPR
210 220 230 240 250
GTGIVSAPVP KKLLMMAGID DCYTSARGCT ATLGNFAKAT FDAISKTYSY
260 270 280 290
LTPDLWKETV FTKSPYQEFT DHLVKTHTRV SVQRTQAPAV ATT
Length:293
Mass (Da):31,324
Last modified:October 1, 1996 - v2
Checksum:i66C0DB7ED393B036
GO

Sequence cautioni

The sequence CAA35078.1 differs from that shown. Reason: Frameshift at positions 14, 27, 40, 46, 48 and 52. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17206 mRNA. Translation: CAA35078.1. Frameshift.
AK312173 mRNA. Translation: BAG35107.1.
CH471112 Genomic DNA. Translation: EAW85592.1.
CH471112 Genomic DNA. Translation: EAW85595.1.
BC001795 mRNA. Translation: AAH01795.1.
BC006559 mRNA. Translation: AAH06559.1.
BC008862 mRNA. Translation: AAH08862.1.
BC010165 mRNA. Translation: AAH10165.1.
BC012354 mRNA. Translation: AAH12354.1.
BC016178 mRNA. Translation: AAH16178.1.
BC016951 mRNA. Translation: AAH16951.1.
BC018993 mRNA. Translation: AAH18993.1.
BC021545 mRNA. Translation: AAH21545.1.
BC023541 mRNA. Translation: AAH23541.1.
BC025677 mRNA. Translation: AAH25677.1.
BC066321 mRNA. Translation: AAH66321.1.
BC068051 mRNA. Translation: AAH68051.1.
BC071922 mRNA. Translation: AAH71922.1.
BC071923 mRNA. Translation: AAH71923.1.
BC071924 mRNA. Translation: AAH71924.1.
BC073966 mRNA. Translation: AAH73966.1.
BC075830 mRNA. Translation: AAH75830.1.
BC103756 mRNA. Translation: AAI03757.1.
BC105985 mRNA. Translation: AAI05986.1.
CCDSiCCDS10452.1.
PIRiS08228.
RefSeqiNP_002943.2. NM_002952.3.
UniGeneiHs.356366.
Hs.381079.
Hs.498569.
Hs.506997.

Genome annotation databases

EnsembliENST00000343262; ENSP00000341885; ENSG00000140988.
GeneIDi6187.
KEGGihsa:6187.
UCSCiuc002cnn.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17206 mRNA. Translation: CAA35078.1. Frameshift.
AK312173 mRNA. Translation: BAG35107.1.
CH471112 Genomic DNA. Translation: EAW85592.1.
CH471112 Genomic DNA. Translation: EAW85595.1.
BC001795 mRNA. Translation: AAH01795.1.
BC006559 mRNA. Translation: AAH06559.1.
BC008862 mRNA. Translation: AAH08862.1.
BC010165 mRNA. Translation: AAH10165.1.
BC012354 mRNA. Translation: AAH12354.1.
BC016178 mRNA. Translation: AAH16178.1.
BC016951 mRNA. Translation: AAH16951.1.
BC018993 mRNA. Translation: AAH18993.1.
BC021545 mRNA. Translation: AAH21545.1.
BC023541 mRNA. Translation: AAH23541.1.
BC025677 mRNA. Translation: AAH25677.1.
BC066321 mRNA. Translation: AAH66321.1.
BC068051 mRNA. Translation: AAH68051.1.
BC071922 mRNA. Translation: AAH71922.1.
BC071923 mRNA. Translation: AAH71923.1.
BC071924 mRNA. Translation: AAH71924.1.
BC073966 mRNA. Translation: AAH73966.1.
BC075830 mRNA. Translation: AAH75830.1.
BC103756 mRNA. Translation: AAI03757.1.
BC105985 mRNA. Translation: AAI05986.1.
CCDSiCCDS10452.1.
PIRiS08228.
RefSeqiNP_002943.2. NM_002952.3.
UniGeneiHs.356366.
Hs.381079.
Hs.498569.
Hs.506997.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AC1-293[»]
ProteinModelPortaliP15880.
SMRiP15880. Positions 53-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112101. 232 interactions.
IntActiP15880. 32 interactions.
MINTiMINT-3008399.
STRINGi9606.ENSP00000341885.

PTM databases

PhosphoSiteiP15880.

Polymorphism and mutation databases

BioMutaiRPS2.
DMDMi1710756.

Proteomic databases

MaxQBiP15880.
PaxDbiP15880.
PRIDEiP15880.

Protocols and materials databases

DNASUi6187.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343262; ENSP00000341885; ENSG00000140988.
GeneIDi6187.
KEGGihsa:6187.
UCSCiuc002cnn.2. human.

Organism-specific databases

CTDi6187.
GeneCardsiGC16M002012.
H-InvDBHIX0029256.
HIX0039223.
HIX0202579.
HGNCiHGNC:10404. RPS2.
HPAiHPA055133.
MIMi603624. gene.
neXtProtiNX_P15880.
PharmGKBiPA34806.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0098.
GeneTreeiENSGT00390000001433.
HOGENOMiHOG000072596.
HOVERGENiHBG000437.
InParanoidiP15880.
KOiK02981.
OMAiGIKDVWT.
OrthoDBiEOG7P5T1Q.
PhylomeDBiP15880.
TreeFamiTF300806.

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.

Miscellaneous databases

GeneWikiiRPS2.
GenomeRNAii6187.
NextBioi24025.
PROiP15880.
SOURCEiSearch...

Gene expression databases

BgeeiP15880.
CleanExiHS_RPS2.
ExpressionAtlasiP15880. baseline.
GenevestigatoriP15880.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
InterProiIPR014720. dsRNA-bd_dom.
IPR000851. Ribosomal_S5.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005711. Ribosomal_S5_euk/arc.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]
PANTHERiPTHR13718. PTHR13718. 1 hit.
PfamiPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR01020. uS5_euk_arch. 1 hit.
PROSITEiPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human cDNA sequence homologous to the mouse LLRep3 gene family."
    Slynn G., Jenner D., Potts W., Elvin P., Morten J.E.N., Markham A.F.
    Nucleic Acids Res. 18:681-681(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Colon.
  2. "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: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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, Cervix, Colon, Eye, Kidney, Lung, Mammary gland, Muscle, Placenta, Skin, Testis and Uterus.
  5. "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 276-291.
    Tissue: Placenta.
  6. "Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)."
    Swiercz R., Person M.D., Bedford M.T.
    Biochem. J. 386:85-91(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION BY PRMT3.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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-263 AND LYS-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-264 AND SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Discovery of peptidylarginine deiminase-4 substrates by protein array: antagonistic citrullination and methylation of human ribosomal protein S2."
    Guo Q., Bedford M.T., Fast W.
    Mol. Biosyst. 7:2286-2295(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CITRULLINATION.
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "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.
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRS2_HUMAN
AccessioniPrimary (citable) accession number: P15880
Secondary accession number(s): B2R5G0, D3DU82, Q3MIB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 1, 1996
Last modified: May 27, 2015
This is version 165 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. 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.