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Protein

60S ribosomal protein L17

Gene

RPL17

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: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
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_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L17
Alternative name(s):
60S ribosomal protein L23
PD-1
Gene namesi
Name:RPL17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:10307. RPL17.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34676.

Polymorphism and mutation databases

BioMutaiRPL17.
DMDMi132799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 18418360S ribosomal protein L17PRO_0000125331Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP18621.
PaxDbiP18621.
PRIDEiP18621.

PTM databases

PhosphoSiteiP18621.

Expressioni

Tissue specificityi

Expressed in pancreas, lung, colon, cystic duct, gall bladder, kidney and liver. Expressed at high levels in the well differentiated pancreatic tumor cell lines HPAF, COLO 357 and Capan-1, the moderately differentiated pancreatic tumor cell lines T3M-4, AsPc-1 and BxPc-3, the poorly differentiated pancreatic tumor cell line MIA PaCa-2, and the pancreatic tumor cell lines of undefined differentiation status such as SW979. Expressed at lower levels in the poorly differentiated pancreatic tumor cell lines HCG-25 and PANC-1.1 Publication

Gene expression databases

BgeeiP18621.
CleanExiHS_RPL17.
ExpressionAtlasiP18621. baseline and differential.
GenevisibleiP18621. HS.

Organism-specific databases

HPAiHPA043724.
HPA046385.

Interactioni

Protein-protein interaction databases

BioGridi112059. 104 interactions.
IntActiP18621. 30 interactions.
MINTiMINT-1393841.
STRINGi9606.ENSP00000462023.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CP1-184[»]
5AJ0electron microscopy3.50AP1-184[»]
ProteinModelPortaliP18621.
SMRiP18621. Positions 1-153.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L22P family.Curated

Phylogenomic databases

eggNOGiCOG0091.
GeneTreeiENSGT00390000014873.
HOGENOMiHOG000205045.
HOVERGENiHBG000955.
InParanoidiP18621.
KOiK02880.
OMAiILSEHET.
OrthoDBiEOG70GMHF.
PhylomeDBiP18621.
TreeFamiTF300042.

Family and domain databases

Gene3Di3.90.470.10. 1 hit.
HAMAPiMF_01331_A. Ribosomal_L22_A.
InterProiIPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005721. Ribosomal_L22/L17_euk/arc.
[Graphical view]
PANTHERiPTHR11593. PTHR11593. 1 hit.
PfamiPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMiSSF54843. SSF54843. 1 hit.
TIGRFAMsiTIGR01038. uL22_arch_euk. 1 hit.
PROSITEiPS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P18621-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVRYSLDPEN PTKSCKSRGS NLRVHFKNTR ETAQAIKGMH IRKATKYLKD
60 70 80 90 100
VTLQKQCVPF RRYNGGVGRC AQAKQWGWTQ GRWPKKSAEF LLHMLKNAES
110 120 130 140 150
NAELKGLDVD SLVIEHIQVN KAPKMRRRTY RAHGRINPYM SSPCHIEMIL
160 170 180
TEKEQIVPKP EEEVAQKKKI SQKKLKKQKL MARE
Length:184
Mass (Da):21,397
Last modified:January 23, 2007 - v3
Checksum:i2FC595DD74ED1CA0
GO
Isoform 2 (identifier: P18621-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.

Show »
Length:146
Mass (Da):17,094
Checksum:iF29AFEFE03D5CA59
GO
Isoform 3 (identifier: P18621-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-184: ISQKKLKKQKLMARE → LRSSSLGKWCAFLVSSFQFCSGSTKNSWSHIYTLWFPPSLVVYGLRKQYKNPMIQTKAK

Show »
Length:228
Mass (Da):26,373
Checksum:iDF45454F21504C77
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331H → R in AAH66324 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838Missing in isoform 2. 1 PublicationVSP_045445Add
BLAST
Alternative sequencei170 – 18415ISQKK…LMARE → LRSSSLGKWCAFLVSSFQFC SGSTKNSWSHIYTLWFPPSL VVYGLRKQYKNPMIQTKAK in isoform 3. 1 PublicationVSP_046965Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53777 mRNA. Translation: CAA37793.1.
AB061824 Genomic DNA. Translation: BAB79462.1.
AC100778 Genomic DNA. No translation available.
AK304659 mRNA. Translation: BAG65434.1.
AK311828 mRNA. Translation: BAG34770.1.
BX393840 mRNA. No translation available.
CH471096 Genomic DNA. Translation: EAW62940.1.
BC000502 mRNA. Translation: AAH00502.1.
BC017831 mRNA. Translation: AAH17831.1.
BC066323 mRNA. Translation: AAH66323.1.
BC066324 mRNA. Translation: AAH66324.1.
BC106031 mRNA. Translation: AAI06032.1.
AB007174 Genomic DNA. Translation: BAA25834.1.
CCDSiCCDS45865.1. [P18621-1]
CCDS56070.1. [P18621-2]
PIRiA61192.
S11218. R5HU22.
RefSeqiNP_000976.1. NM_000985.4. [P18621-1]
NP_001030178.1. NM_001035006.2. [P18621-1]
NP_001186269.1. NM_001199340.1. [P18621-1]
NP_001186270.1. NM_001199341.1. [P18621-1]
NP_001186271.1. NM_001199342.1. [P18621-1]
NP_001186272.1. NM_001199343.1. [P18621-1]
NP_001186273.1. NM_001199344.1. [P18621-1]
NP_001186274.1. NM_001199345.1. [P18621-2]
UniGeneiHs.293653.
Hs.374588.
Hs.485081.

Genome annotation databases

EnsembliENST00000418495; ENSP00000397798; ENSG00000265681.
ENST00000579248; ENSP00000462023; ENSG00000265681.
ENST00000579408; ENSP00000463842; ENSG00000265681.
ENST00000580261; ENSP00000462385; ENSG00000265681.
ENST00000581373; ENSP00000462944; ENSG00000265681. [P18621-2]
ENST00000618613; ENSP00000480555; ENSG00000265681.
ENST00000618619; ENSP00000482577; ENSG00000265681.
GeneIDi6139.
KEGGihsa:6139.
UCSCiuc002ldm.2. human.
uc002ldp.3. human. [P18621-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53777 mRNA. Translation: CAA37793.1.
AB061824 Genomic DNA. Translation: BAB79462.1.
AC100778 Genomic DNA. No translation available.
AK304659 mRNA. Translation: BAG65434.1.
AK311828 mRNA. Translation: BAG34770.1.
BX393840 mRNA. No translation available.
CH471096 Genomic DNA. Translation: EAW62940.1.
BC000502 mRNA. Translation: AAH00502.1.
BC017831 mRNA. Translation: AAH17831.1.
BC066323 mRNA. Translation: AAH66323.1.
BC066324 mRNA. Translation: AAH66324.1.
BC106031 mRNA. Translation: AAI06032.1.
AB007174 Genomic DNA. Translation: BAA25834.1.
CCDSiCCDS45865.1. [P18621-1]
CCDS56070.1. [P18621-2]
PIRiA61192.
S11218. R5HU22.
RefSeqiNP_000976.1. NM_000985.4. [P18621-1]
NP_001030178.1. NM_001035006.2. [P18621-1]
NP_001186269.1. NM_001199340.1. [P18621-1]
NP_001186270.1. NM_001199341.1. [P18621-1]
NP_001186271.1. NM_001199342.1. [P18621-1]
NP_001186272.1. NM_001199343.1. [P18621-1]
NP_001186273.1. NM_001199344.1. [P18621-1]
NP_001186274.1. NM_001199345.1. [P18621-2]
UniGeneiHs.293653.
Hs.374588.
Hs.485081.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CP1-184[»]
5AJ0electron microscopy3.50AP1-184[»]
ProteinModelPortaliP18621.
SMRiP18621. Positions 1-153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112059. 104 interactions.
IntActiP18621. 30 interactions.
MINTiMINT-1393841.
STRINGi9606.ENSP00000462023.

PTM databases

PhosphoSiteiP18621.

Polymorphism and mutation databases

BioMutaiRPL17.
DMDMi132799.

Proteomic databases

MaxQBiP18621.
PaxDbiP18621.
PRIDEiP18621.

Protocols and materials databases

DNASUi6139.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000418495; ENSP00000397798; ENSG00000265681.
ENST00000579248; ENSP00000462023; ENSG00000265681.
ENST00000579408; ENSP00000463842; ENSG00000265681.
ENST00000580261; ENSP00000462385; ENSG00000265681.
ENST00000581373; ENSP00000462944; ENSG00000265681. [P18621-2]
ENST00000618613; ENSP00000480555; ENSG00000265681.
ENST00000618619; ENSP00000482577; ENSG00000265681.
GeneIDi6139.
KEGGihsa:6139.
UCSCiuc002ldm.2. human.
uc002ldp.3. human. [P18621-1]

Organism-specific databases

CTDi6139.
GeneCardsiGC18M047014.
HGNCiHGNC:10307. RPL17.
HPAiHPA043724.
HPA046385.
MIMi603661. gene.
neXtProtiNX_P18621.
PharmGKBiPA34676.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0091.
GeneTreeiENSGT00390000014873.
HOGENOMiHOG000205045.
HOVERGENiHBG000955.
InParanoidiP18621.
KOiK02880.
OMAiILSEHET.
OrthoDBiEOG70GMHF.
PhylomeDBiP18621.
TreeFamiTF300042.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
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_9491. Viral mRNA Translation.

Miscellaneous databases

GeneWikiiRPL17.
NextBioi23849.
PROiP18621.
SOURCEiSearch...

Gene expression databases

BgeeiP18621.
CleanExiHS_RPL17.
ExpressionAtlasiP18621. baseline and differential.
GenevisibleiP18621. HS.

Family and domain databases

Gene3Di3.90.470.10. 1 hit.
HAMAPiMF_01331_A. Ribosomal_L22_A.
InterProiIPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005721. Ribosomal_L22/L17_euk/arc.
[Graphical view]
PANTHERiPTHR11593. PTHR11593. 1 hit.
PfamiPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMiSSF54843. SSF54843. 1 hit.
TIGRFAMsiTIGR01038. uL22_arch_euk. 1 hit.
PROSITEiPS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human gene related to the ribosomal protein L23 gene of Halobacterium marismortui."
    Mager D.L., Freeman J.D.
    Nucleic Acids Res. 18:5301-5301(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Blood.
  2. "Isolation and characterization of a complementary DNA (PD-1) differentially expressed by human pancreatic ductal cell tumors."
    Batra S.K., Metzgar R.S., Hollingsworth M.A.
    Cell Growth Differ. 2:385-390(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Pancreatic tumor.
  3. "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].
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Uterus.
  5. Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Neuroblastoma.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Hypothalamus, Lung, Prostate and Testis.
  9. "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
    Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.
    J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10, IDENTIFICATION BY MASS SPECTROMETRY.
  10. Bienvenut W.V., Calvo F., Kolch W.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 31-42; 47-55; 75-82; 86-96 AND 106-124, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  11. "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 170-183.
  12. "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.
  13. "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-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL17_HUMAN
AccessioniPrimary (citable) accession number: P18621
Secondary accession number(s): B2R4H3
, B4E3C2, B5ME31, J3QL51, Q3KQW2, Q6NZ54, Q7M4M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 162 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 18
    Human chromosome 18: 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.