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Protein

60S ribosomal protein L13

Gene

RPL13

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
  • RNA binding Source: ProtInc
  • 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 L13
Alternative name(s):
Breast basic conserved protein 1
Gene namesi
Name:RPL13
Synonyms:BBC1
ORF Names:OK/SW-cl.46
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:10303. RPL13.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • cytosolic ribosome Source: ProtInc
  • membrane Source: UniProtKB
  • nucleolus Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34670.

Polymorphism and mutation databases

BioMutaiRPL13.
DMDMi21903462.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21121160S ribosomal protein L13PRO_0000192919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161N6-acetyllysine1 Publication
Modified residuei77 – 771Phosphoserine1 Publication
Modified residuei106 – 1061Phosphoserine1 Publication
Modified residuei177 – 1771N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP26373.
PaxDbiP26373.
PeptideAtlasiP26373.
PRIDEiP26373.

PTM databases

PhosphoSiteiP26373.

Miscellaneous databases

PMAP-CutDBP26373.

Expressioni

Tissue specificityi

Higher levels of expression in benign breast lesions than in carcinomas.

Gene expression databases

BgeeiP26373.
CleanExiHS_RPL13.
ExpressionAtlasiP26373. baseline and differential.
GenevisibleiP26373. HS.

Organism-specific databases

HPAiHPA051702.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP70Q8NHQ13EBI-356849,EBI-739624
LRRK2Q5S0072EBI-356849,EBI-5323863
NCK1P163332EBI-356849,EBI-389883
PIK3R1P279862EBI-356849,EBI-79464

Protein-protein interaction databases

BioGridi112057. 145 interactions.
IntActiP26373. 34 interactions.
MINTiMINT-1148895.
STRINGi9606.ENSP00000307889.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CL1-211[»]
ProteinModelPortaliP26373.
SMRiP26373. Positions 2-211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L13e family.Curated

Phylogenomic databases

eggNOGiCOG4352.
GeneTreeiENSGT00390000007818.
HOGENOMiHOG000170452.
HOVERGENiHBG001156.
InParanoidiP26373.
KOiK02873.
OMAiLNPHFHK.
OrthoDBiEOG74TX1G.
PhylomeDBiP26373.
TreeFamiTF300073.

Family and domain databases

InterProiIPR001380. Ribosomal_L13e.
IPR018256. Ribosomal_L13e_CS.
[Graphical view]
PANTHERiPTHR11722. PTHR11722. 1 hit.
PfamiPF01294. Ribosomal_L13e. 1 hit.
[Graphical view]
PROSITEiPS01104. RIBOSOMAL_L13E. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P26373-1) [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
MAPSRNGMVL KPHFHKDWQR RVATWFNQPA RKIRRRKARQ AKARRIAPRP
60 70 80 90 100
ASGPIRPIVR CPTVRYHTKV RAGRGFSLEE LRVAGIHKKV ARTIGISVDP
110 120 130 140 150
RRRNKSTESL QANVQRLKEY RSKLILFPRK PSAPKKGDSS AEELKLATQL
160 170 180 190 200
TGPVMPVRNV YKKEKARVIT EEEKNFKAFA SLRMARANAR LFGIRAKRAK
210
EAAEQDVEKK K
Length:211
Mass (Da):24,261
Last modified:January 23, 2007 - v4
Checksum:iDB9FC57768E6BEDE
GO
Isoform 2 (identifier: P26373-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     88-134: Missing.

Note: No experimental confirmation available.
Show »
Length:164
Mass (Da):18,845
Checksum:iF631C531204EEFAC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91V → A in BAG59685 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121A → T.2 Publications
Corresponds to variant rs9930567 [ dbSNP | Ensembl ].
VAR_051801
Natural varianti170 – 1701T → P.
Corresponds to variant rs16965839 [ dbSNP | Ensembl ].
VAR_051802

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei88 – 13447Missing in isoform 2. 1 PublicationVSP_046028Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64707 mRNA. Translation: CAA45963.1.
AB062392 mRNA. Translation: BAB93479.1.
AK297198 mRNA. Translation: BAG59685.1.
AC092123 Genomic DNA. No translation available.
BC004954 mRNA. Translation: AAH04954.1.
BC007345 mRNA. Translation: AAH07345.1.
BC007563 mRNA. Translation: AAH07563.1.
BC007805 mRNA. Translation: AAH07805.1.
BC010994 mRNA. Translation: AAH10994.1.
BC013078 mRNA. Translation: AAH13078.1.
BC014167 mRNA. Translation: AAH14167.1.
BC020804 mRNA. Translation: AAH20804.1.
BC027463 mRNA. Translation: AAH27463.1.
BC063378 mRNA. Translation: AAH63378.1.
BC093063 mRNA. Translation: AAH93063.1.
BC106058 mRNA. Translation: AAI06059.1.
CCDSiCCDS10979.1. [P26373-1]
CCDS58492.1. [P26373-2]
PIRiS23753.
RefSeqiNP_000968.2. NM_000977.3. [P26373-1]
NP_001230059.1. NM_001243130.1.
NP_001230060.1. NM_001243131.1. [P26373-2]
NP_150254.1. NM_033251.2. [P26373-1]
UniGeneiHs.410817.

Genome annotation databases

EnsembliENST00000311528; ENSP00000307889; ENSG00000167526. [P26373-1]
ENST00000393099; ENSP00000376811; ENSG00000167526. [P26373-1]
ENST00000452368; ENSP00000438959; ENSG00000167526. [P26373-2]
ENST00000567815; ENSP00000455009; ENSG00000167526. [P26373-1]
GeneIDi6137.
KEGGihsa:6137.
UCSCiuc002fnm.2. human. [P26373-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64707 mRNA. Translation: CAA45963.1.
AB062392 mRNA. Translation: BAB93479.1.
AK297198 mRNA. Translation: BAG59685.1.
AC092123 Genomic DNA. No translation available.
BC004954 mRNA. Translation: AAH04954.1.
BC007345 mRNA. Translation: AAH07345.1.
BC007563 mRNA. Translation: AAH07563.1.
BC007805 mRNA. Translation: AAH07805.1.
BC010994 mRNA. Translation: AAH10994.1.
BC013078 mRNA. Translation: AAH13078.1.
BC014167 mRNA. Translation: AAH14167.1.
BC020804 mRNA. Translation: AAH20804.1.
BC027463 mRNA. Translation: AAH27463.1.
BC063378 mRNA. Translation: AAH63378.1.
BC093063 mRNA. Translation: AAH93063.1.
BC106058 mRNA. Translation: AAI06059.1.
CCDSiCCDS10979.1. [P26373-1]
CCDS58492.1. [P26373-2]
PIRiS23753.
RefSeqiNP_000968.2. NM_000977.3. [P26373-1]
NP_001230059.1. NM_001243130.1.
NP_001230060.1. NM_001243131.1. [P26373-2]
NP_150254.1. NM_033251.2. [P26373-1]
UniGeneiHs.410817.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CL1-211[»]
ProteinModelPortaliP26373.
SMRiP26373. Positions 2-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112057. 145 interactions.
IntActiP26373. 34 interactions.
MINTiMINT-1148895.
STRINGi9606.ENSP00000307889.

PTM databases

PhosphoSiteiP26373.

Polymorphism and mutation databases

BioMutaiRPL13.
DMDMi21903462.

Proteomic databases

MaxQBiP26373.
PaxDbiP26373.
PeptideAtlasiP26373.
PRIDEiP26373.

Protocols and materials databases

DNASUi6137.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311528; ENSP00000307889; ENSG00000167526. [P26373-1]
ENST00000393099; ENSP00000376811; ENSG00000167526. [P26373-1]
ENST00000452368; ENSP00000438959; ENSG00000167526. [P26373-2]
ENST00000567815; ENSP00000455009; ENSG00000167526. [P26373-1]
GeneIDi6137.
KEGGihsa:6137.
UCSCiuc002fnm.2. human. [P26373-1]

Organism-specific databases

CTDi6137.
GeneCardsiGC16P089669.
HGNCiHGNC:10303. RPL13.
HPAiHPA051702.
MIMi113703. gene.
neXtProtiNX_P26373.
PharmGKBiPA34670.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4352.
GeneTreeiENSGT00390000007818.
HOGENOMiHOG000170452.
HOVERGENiHBG001156.
InParanoidiP26373.
KOiK02873.
OMAiLNPHFHK.
OrthoDBiEOG74TX1G.
PhylomeDBiP26373.
TreeFamiTF300073.

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

ChiTaRSiRPL13. human.
GeneWikiiRPL13.
GenomeRNAii6137.
NextBioi23839.
PMAP-CutDBP26373.
PROiP26373.
SOURCEiSearch...

Gene expression databases

BgeeiP26373.
CleanExiHS_RPL13.
ExpressionAtlasiP26373. baseline and differential.
GenevisibleiP26373. HS.

Family and domain databases

InterProiIPR001380. Ribosomal_L13e.
IPR018256. Ribosomal_L13e_CS.
[Graphical view]
PANTHERiPTHR11722. PTHR11722. 1 hit.
PfamiPF01294. Ribosomal_L13e. 1 hit.
[Graphical view]
PROSITEiPS01104. RIBOSOMAL_L13E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a novel gene with differential expression in benign and malignant human breast tumours."
    Adams S.M., Helps N.R., Sharp M.G.F., Brammar W.J., Walker R.A., Varley J.M.
    Hum. Mol. Genet. 1:91-96(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-112.
  2. "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] (ISOFORM 1).
    Tissue: Colon adenocarcinoma.
  3. "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] (ISOFORM 2).
    Tissue: Brain.
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1), VARIANT THR-112.
    Tissue: Blood vessel, Brain, Cervix, Lung, Lymph, Pancreas, Placenta and Uterus.
  6. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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-16 AND LYS-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL13_HUMAN
AccessioniPrimary (citable) accession number: P26373
Secondary accession number(s): B4DLX3
, F5H1S2, Q3KQT8, Q567Q8, Q9BPX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 149 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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.