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Protein

60S ribosomal protein L10a

Gene

RPL10A

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: GO_Central
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L10a
Alternative name(s):
CSA-19
Neural precursor cell expressed developmentally down-regulated protein 6
Short name:
NEDD-6
Gene namesi
Name:RPL10A
Synonyms:NEDD6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:10299. RPL10A.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34661.

Polymorphism and mutation databases

BioMutaiRPL10A.
DMDMi51702773.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 21721660S ribosomal protein L10aPRO_0000125818Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei11 – 111PhosphotyrosineBy similarity
Modified residuei91 – 911N6-acetyllysineBy similarity
Modified residuei106 – 1061N6-acetyllysineCombined sources
Modified residuei118 – 1181N6-acetyllysine; alternateCombined sources
Cross-linki118 – 118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki118 – 118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP62906.
MaxQBiP62906.
PaxDbiP62906.
PeptideAtlasiP62906.
PRIDEiP62906.
TopDownProteomicsiP62906.

2D gel databases

SWISS-2DPAGEP62906.

PTM databases

iPTMnetiP62906.
PhosphoSiteiP62906.
SwissPalmiP62906.

Expressioni

Gene expression databases

BgeeiP62906.
CleanExiHS_RPL10A.
GenevisibleiP62906. HS.

Organism-specific databases

HPAiHPA053803.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0072EBI-356860,EBI-5323863
RGS17Q9UGC63EBI-356860,EBI-3918154

Protein-protein interaction databases

BioGridi110813. 176 interactions.
IntActiP62906. 31 interactions.
MINTiMINT-4999991.
STRINGi9606.ENSP00000363018.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-Lz1-217[»]
4V6Xelectron microscopy5.00Cz1-217[»]
5AJ0electron microscopy3.50Au1-217[»]
ProteinModelPortaliP62906.
SMRiP62906. Positions 5-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L1P family.Curated

Phylogenomic databases

eggNOGiKOG1570. Eukaryota.
COG0081. LUCA.
GeneTreeiENSGT00390000008767.
HOGENOMiHOG000207014.
HOVERGENiHBG055239.
InParanoidiP62906.
KOiK02865.
OMAiDFFIAQA.
OrthoDBiEOG7S7SG8.
PhylomeDBiP62906.
TreeFamiTF300791.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
InterProiIPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
[Graphical view]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62906-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKVSRDTL YEAVREVLHG NQRKRRKFLE TVELQISLKN YDPQKDKRFS
60 70 80 90 100
GTVRLKSTPR PKFSVCVLGD QQHCDEAKAV DIPHMDIEAL KKLNKNKKLV
110 120 130 140 150
KKLAKKYDAF LASESLIKQI PRILGPGLNK AGKFPSLLTH NENMVAKVDE
160 170 180 190 200
VKSTIKFQMK KVLCLAVAVG HVKMTDDELV YNIHLAVNFL VSLLKKNWQN
210
VRALYIKSTM GKPQRLY
Length:217
Mass (Da):24,831
Last modified:January 23, 2007 - v2
Checksum:i38F1A31119A751D3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041A → V in AAA86463 (PubMed:7609734).Curated
Sequence conflicti209 – 2091T → P in BAC16802 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti154 – 1541T → P.
Corresponds to variant rs17838763 [ dbSNP | Ensembl ].
VAR_034458

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12404 mRNA. Translation: AAA86463.1.
AB082926 mRNA. Translation: BAC16802.1.
BT020040 mRNA. Translation: AAV38843.1.
BT020041 mRNA. Translation: AAV38844.1.
AK313181 mRNA. Translation: BAG35998.1.
AL022721 Genomic DNA. Translation: CAB38627.1.
CH471081 Genomic DNA. Translation: EAX03831.1.
BC006791 mRNA. Translation: AAH06791.1.
BC011366 mRNA. Translation: AAH11366.1.
BC070216 mRNA. Translation: AAH70216.1.
CCDSiCCDS4806.1.
RefSeqiNP_009035.3. NM_007104.4.
UniGeneiHs.148340.
Hs.546269.

Genome annotation databases

EnsembliENST00000322203; ENSP00000363018; ENSG00000198755.
GeneIDi4736.
KEGGihsa:4736.
UCSCiuc003okp.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12404 mRNA. Translation: AAA86463.1.
AB082926 mRNA. Translation: BAC16802.1.
BT020040 mRNA. Translation: AAV38843.1.
BT020041 mRNA. Translation: AAV38844.1.
AK313181 mRNA. Translation: BAG35998.1.
AL022721 Genomic DNA. Translation: CAB38627.1.
CH471081 Genomic DNA. Translation: EAX03831.1.
BC006791 mRNA. Translation: AAH06791.1.
BC011366 mRNA. Translation: AAH11366.1.
BC070216 mRNA. Translation: AAH70216.1.
CCDSiCCDS4806.1.
RefSeqiNP_009035.3. NM_007104.4.
UniGeneiHs.148340.
Hs.546269.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-Lz1-217[»]
4V6Xelectron microscopy5.00Cz1-217[»]
5AJ0electron microscopy3.50Au1-217[»]
ProteinModelPortaliP62906.
SMRiP62906. Positions 5-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110813. 176 interactions.
IntActiP62906. 31 interactions.
MINTiMINT-4999991.
STRINGi9606.ENSP00000363018.

PTM databases

iPTMnetiP62906.
PhosphoSiteiP62906.
SwissPalmiP62906.

Polymorphism and mutation databases

BioMutaiRPL10A.
DMDMi51702773.

2D gel databases

SWISS-2DPAGEP62906.

Proteomic databases

EPDiP62906.
MaxQBiP62906.
PaxDbiP62906.
PeptideAtlasiP62906.
PRIDEiP62906.
TopDownProteomicsiP62906.

Protocols and materials databases

DNASUi4736.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322203; ENSP00000363018; ENSG00000198755.
GeneIDi4736.
KEGGihsa:4736.
UCSCiuc003okp.2. human.

Organism-specific databases

CTDi4736.
GeneCardsiRPL10A.
HGNCiHGNC:10299. RPL10A.
HPAiHPA053803.
MIMi615660. gene.
neXtProtiNX_P62906.
PharmGKBiPA34661.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1570. Eukaryota.
COG0081. LUCA.
GeneTreeiENSGT00390000008767.
HOGENOMiHOG000207014.
HOVERGENiHBG055239.
InParanoidiP62906.
KOiK02865.
OMAiDFFIAQA.
OrthoDBiEOG7S7SG8.
PhylomeDBiP62906.
TreeFamiTF300791.

Enzyme and pathway databases

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiRPL10A. human.
GeneWikiiRPL10A.
GenomeRNAii4736.
PROiP62906.
SOURCEiSearch...

Gene expression databases

BgeeiP62906.
CleanExiHS_RPL10A.
GenevisibleiP62906. HS.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
InterProiIPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
[Graphical view]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of genes downregulated in the thymus by cyclosporin-A: preliminary characterization of clone CSA-19."
    Fisicaro N., Katerelos M., Williams J., Power D., D'Apice A., Pearse M.
    Mol. Immunol. 32:565-572(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification of a tumor-rejection antigen recognized by HLA-B46 restricted CTL."
    Azuma K., Shichijo S., Itoh K.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Cervix.
  8. "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: ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
  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-106 AND LYS-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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.
  12. "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli."
    Impens F., Radoshevich L., Cossart P., Ribet D.
    Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL10A_HUMAN
AccessioniPrimary (citable) accession number: P62906
Secondary accession number(s): B2R801
, P52859, P53025, Q5TZT6, Q8J013
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 128 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, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

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 one 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.