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Protein

Interleukin-6 receptor subunit alpha

Gene

IL6R

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

Functioni

Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation may lead to the regulation of the immune response, acute-phase reactions and hematopoiesis.
Low concentration of a soluble form of IL6 receptor acts as an agonist of IL6 activity.

GO - Molecular functioni

  • ciliary neurotrophic factor binding Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • interleukin-6 binding Source: BHF-UCL
  • interleukin-6 receptor activity Source: Ensembl
  • protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  • acute-phase response Source: BHF-UCL
  • ciliary neurotrophic factor-mediated signaling pathway Source: BHF-UCL
  • cytokine-mediated signaling pathway Source: BHF-UCL
  • defense response to Gram-negative bacterium Source: BHF-UCL
  • defense response to Gram-positive bacterium Source: BHF-UCL
  • endocrine pancreas development Source: BHF-UCL
  • extrinsic apoptotic signaling pathway Source: BHF-UCL
  • hepatic immune response Source: BHF-UCL
  • interleukin-6-mediated signaling pathway Source: BHF-UCL
  • monocyte chemotaxis Source: BHF-UCL
  • negative regulation of collagen biosynthetic process Source: BHF-UCL
  • negative regulation of interleukin-8 production Source: BHF-UCL
  • neutrophil mediated immunity Source: BHF-UCL
  • positive regulation of activation of Janus kinase activity Source: BHF-UCL
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of chemokine production Source: BHF-UCL
  • positive regulation of interleukin-6 production Source: BHF-UCL
  • positive regulation of leukocyte chemotaxis Source: BHF-UCL
  • positive regulation of MAPK cascade Source: BHF-UCL
  • positive regulation of osteoblast differentiation Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of smooth muscle cell proliferation Source: BHF-UCL
  • positive regulation of tyrosine phosphorylation of Stat3 protein Source: BHF-UCL
  • response to cytokine Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

BioCyciZFISH:ENSG00000160712-MONOMER.
ReactomeiR-HSA-1059683. Interleukin-6 signaling.
R-HSA-110056. MAPK3 (ERK1) activation.
R-HSA-112411. MAPK1 (ERK2) activation.
SignaLinkiP08887.
SIGNORiP08887.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-6 receptor subunit alpha
Short name:
IL-6 receptor subunit alpha
Short name:
IL-6R subunit alpha
Short name:
IL-6R-alpha
Short name:
IL-6RA
Alternative name(s):
IL-6R 1
Membrane glycoprotein 80
Short name:
gp80
CD_antigen: CD126
Gene namesi
Name:IL6R
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6019. IL6R.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 365ExtracellularSequence analysisAdd BLAST346
Transmembranei366 – 386HelicalSequence analysisAdd BLAST21
Topological domaini387 – 468CytoplasmicSequence analysisAdd BLAST82

GO - Cellular componenti

  • apical plasma membrane Source: BHF-UCL
  • basolateral plasma membrane Source: UniProtKB-SubCell
  • cell surface Source: Ensembl
  • ciliary neurotrophic factor receptor complex Source: BHF-UCL
  • extracellular region Source: UniProtKB
  • extracellular space Source: BHF-UCL
  • interleukin-6 receptor complex Source: BHF-UCL
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi121C → S: Complete loss of ligand-binding. 1 Publication1
Mutagenesisi122F → A: No change of ligand-binding and IL6 signaling. 1 Publication1
Mutagenesisi132C → A: Complete loss of ligand-binding. 1 Publication1
Mutagenesisi134W → L: Complete loss of ligand-binding. 1 Publication1
Mutagenesisi140P → G: No change of ligand-binding and IL6 signaling. 1 Publication1
Mutagenesisi153F → L: No change of ligand-binding and IL6 signaling. 1 Publication1
Mutagenesisi165C → L: Complete loss of ligand-binding. 1 Publication1
Mutagenesisi174F → L: No change of ligand-binding and IL6 signaling. 1 Publication1
Mutagenesisi176C → A: Complete loss of ligand-binding. 1 Publication1
Mutagenesisi184D → T: 30% decrease of ligand-binding and IL6 signaling. 1 Publication1
Mutagenesisi190V → G: 80% decrease of ligand-binding and no IL6 signaling. 1 Publication1
Mutagenesisi193C → D: Complete loss of ligand-binding. 1 Publication1
Mutagenesisi211C → A: No change of ligand-binding and IL6 signaling. 1 Publication1
Mutagenesisi217D → V: Complete loss of ligand-binding. 1 Publication1
Mutagenesisi232R → S: 30% decrease of ligand-binding and IL6 signaling. 1 Publication1
Mutagenesisi233W → Q: 30% decrease of ligand-binding and increase of IL6 signaling. 1 Publication1
Mutagenesisi254E → A: 50% decrease of ligand-binding and IL6 signaling. 1 Publication1
Mutagenesisi277C → D: 30% increase of ligand-binding and 100% increase in IL6 signaling. 1 Publication1
Mutagenesisi278V → N: 50% Decrease of ligand-binding and 50% increase in IL6 signaling. 1 Publication1
Mutagenesisi279I → D: Complete loss of ligand-binding. 1 Publication1
Mutagenesisi280H → I: No change of ligand-binding and no IL6 signaling. 1 Publication1
Mutagenesisi281D → G: 70% decrease of ligand-binding and no IL6 signaling. 1 Publication1
Mutagenesisi285G → D: 80% decrease of ligand-binding and no IL6 signaling. 1 Publication1
Mutagenesisi291Q → K: Complete loss of ligand-binding. 1 Publication1
Mutagenesisi293R → G: Complete loss of ligand-binding. 1 Publication1

Organism-specific databases

DisGeNETi3570.
MIMi614689. phenotype.
614752. phenotype.
OpenTargetsiENSG00000160712.
PharmGKBiPA29835.

Chemistry databases

ChEMBLiCHEMBL2364155.
DrugBankiDB06273. Tocilizumab.
GuidetoPHARMACOLOGYi1708.

Polymorphism and mutation databases

BioMutaiIL6R.
DMDMi124343.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000001089520 – 468Interleukin-6 receptor subunit alphaAdd BLAST449

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi25 ↔ 193PROSITE-ProRule annotation1 Publication
Disulfide bondi47 ↔ 96PROSITE-ProRule annotation1 Publication
Glycosylationi55N-linked (GlcNAc...)1 Publication1
Glycosylationi93N-linked (GlcNAc...)1 Publication1
Disulfide bondi121 ↔ 132PROSITE-ProRule annotation1 Publication
Disulfide bondi165 ↔ 176PROSITE-ProRule annotation1 Publication
Glycosylationi221N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

A short soluble form may also be released from the membrane by proteolysis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei245Not glycosylated1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP08887.
PaxDbiP08887.
PeptideAtlasiP08887.
PRIDEiP08887.

PTM databases

iPTMnetiP08887.
PhosphoSitePlusiP08887.

Miscellaneous databases

PMAP-CutDBP08887.

Expressioni

Tissue specificityi

Isoform 2 is expressed in peripheral blood mononuclear cells and weakly found in urine and serum.

Gene expression databases

BgeeiENSG00000160712.
CleanExiHS_IL6R.
ExpressionAtlasiP08887. baseline and differential.
GenevisibleiP08887. HS.

Organism-specific databases

HPAiCAB034142.

Interactioni

Subunit structurei

Hexamer of two molecules each of IL6, IL6R and IL6ST.

Binary interactionsi

WithEntry#Exp.IntActNotes
IL6P052316EBI-299383,EBI-720533
K2Q2HRC73EBI-299383,EBI-9007403From a different organism.

GO - Molecular functioni

  • ciliary neurotrophic factor binding Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • interleukin-6 binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi109784. 15 interactors.
DIPiDIP-162N.
DIP-3777N.
IntActiP08887. 5 interactors.
MINTiMINT-190110.
STRINGi9606.ENSP00000357470.

Structurei

Secondary structure

1468
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 37Combined sources4
Beta strandi43 – 46Combined sources4
Beta strandi56 – 63Combined sources8
Beta strandi65 – 68Combined sources4
Beta strandi72 – 83Combined sources12
Helixi88 – 90Combined sources3
Beta strandi92 – 101Combined sources10
Beta strandi105 – 110Combined sources6
Beta strandi120 – 125Combined sources6
Beta strandi130 – 134Combined sources5
Beta strandi145 – 157Combined sources13
Beta strandi159 – 168Combined sources10
Turni169 – 172Combined sources4
Beta strandi173 – 178Combined sources6
Beta strandi187 – 196Combined sources10
Beta strandi199 – 202Combined sources4
Beta strandi206 – 209Combined sources4
Turni210 – 212Combined sources3
Beta strandi220 – 226Combined sources7
Beta strandi234 – 239Combined sources6
Beta strandi247 – 249Combined sources3
Beta strandi251 – 259Combined sources9
Beta strandi266 – 269Combined sources4
Helixi271 – 273Combined sources3
Beta strandi275 – 281Combined sources7
Beta strandi288 – 296Combined sources9
Turni297 – 299Combined sources3
Beta strandi310 – 312Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N26X-ray2.40A20-344[»]
1N2Qmodel-C/D20-344[»]
1P9MX-ray3.65C115-315[»]
2ARWNMR-A212-336[»]
ProteinModelPortaliP08887.
SMRiP08887.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08887.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 112Ig-like C2-typeAdd BLAST87
Domaini113 – 217Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST105
Domaini218 – 316Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST99

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi303 – 307WSXWS motif5

Domaini

The two fibronectin type-III-like domains, contained in the N-terminal part, form together a cytokine-binding domain.
The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.

Sequence similaritiesi

Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II5K. Eukaryota.
ENOG4111XGC. LUCA.
GeneTreeiENSGT00530000063103.
HOVERGENiHBG052118.
InParanoidiP08887.
KOiK05055.
OrthoDBiEOG091G07XD.
PhylomeDBiP08887.
TreeFamiTF331210.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 3 hits.
InterProiIPR003961. FN3_dom.
IPR003530. Hematopoietin_rcpt_L_F3_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR015321. TypeI_recpt_CBD.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF09240. IL6Ra-bind. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
PS01354. HEMATOPO_REC_L_F3. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: P08887-1) [UniParc]FASTAAdd to basket
Also known as: Long

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
MLAVGCALLA ALLAAPGAAL APRRCPAQEV ARGVLTSLPG DSVTLTCPGV
60 70 80 90 100
EPEDNATVHW VLRKPAAGSH PSRWAGMGRR LLLRSVQLHD SGNYSCYRAG
110 120 130 140 150
RPAGTVHLLV DVPPEEPQLS CFRKSPLSNV VCEWGPRSTP SLTTKAVLLV
160 170 180 190 200
RKFQNSPAED FQEPCQYSQE SQKFSCQLAV PEGDSSFYIV SMCVASSVGS
210 220 230 240 250
KFSKTQTFQG CGILQPDPPA NITVTAVARN PRWLSVTWQD PHSWNSSFYR
260 270 280 290 300
LRFELRYRAE RSKTFTTWMV KDLQHHCVIH DAWSGLRHVV QLRAQEEFGQ
310 320 330 340 350
GEWSEWSPEA MGTPWTESRS PPAENEVSTP MQALTTNKDD DNILFRDSAN
360 370 380 390 400
ATSLPVQDSS SVPLPTFLVA GGSLAFGTLL CIAIVLRFKK TWKLRALKEG
410 420 430 440 450
KTSMHPPYSL GQLVPERPRP TPVLVPLISP PVSPSSLGSD NTSSHNRPDA
460
RDPRSPYDIS NTDYFFPR
Length:468
Mass (Da):51,548
Last modified:November 1, 1988 - v1
Checksum:i62AA239FA14F1B8B
GO
Isoform 2 (identifier: P08887-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     356-365: VQDSSSVPLP → GSRRRGSCGL
     366-468: Missing.

Show »
Length:365
Mass (Da):40,237
Checksum:iECC8FC9E142823F2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti210G → D in BAD97302 (Ref. 5) Curated1

Polymorphismi

Genetic variations in IL6R determine soluble IL6R serum levels [MIMi:614689].
Genetic variations in IL6R define the IL6 serum level quantitative trait locus [MIMi:614752].

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021995358D → A Significantly associated with circulating levels of IL6 and soluble IL6R. 2 PublicationsCorresponds to variant rs2228145dbSNPEnsembl.1
Natural variantiVAR_049166385V → I.Corresponds to variant rs28730736dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001682356 – 365VQDSSSVPLP → GSRRRGSCGL in isoform 2. 3 Publications10
Alternative sequenceiVSP_001683366 – 468Missing in isoform 2. 3 PublicationsAdd BLAST103

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12830 mRNA. Translation: CAA31312.1.
X58298 mRNA. Translation: CAA41231.1.
AK293013 mRNA. Translation: BAF85702.1.
AK312730 mRNA. Translation: BAG35601.1.
AK223582 mRNA. Translation: BAD97302.1.
AL162591 Genomic DNA. Translation: CAH72853.1.
CH471121 Genomic DNA. Translation: EAW53200.1.
BC089410 mRNA. Translation: AAH89410.1.
S72848 mRNA. Translation: AAC60635.1.
CCDSiCCDS1067.1. [P08887-1]
CCDS1068.1. [P08887-2]
PIRiA41242.
RefSeqiNP_000556.1. NM_000565.3. [P08887-1]
NP_001193795.1. NM_001206866.1.
NP_852004.1. NM_181359.2. [P08887-2]
UniGeneiHs.135087.

Genome annotation databases

EnsembliENST00000344086; ENSP00000340589; ENSG00000160712. [P08887-2]
ENST00000368485; ENSP00000357470; ENSG00000160712. [P08887-1]
GeneIDi3570.
KEGGihsa:3570.
UCSCiuc001fez.2. human. [P08887-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12830 mRNA. Translation: CAA31312.1.
X58298 mRNA. Translation: CAA41231.1.
AK293013 mRNA. Translation: BAF85702.1.
AK312730 mRNA. Translation: BAG35601.1.
AK223582 mRNA. Translation: BAD97302.1.
AL162591 Genomic DNA. Translation: CAH72853.1.
CH471121 Genomic DNA. Translation: EAW53200.1.
BC089410 mRNA. Translation: AAH89410.1.
S72848 mRNA. Translation: AAC60635.1.
CCDSiCCDS1067.1. [P08887-1]
CCDS1068.1. [P08887-2]
PIRiA41242.
RefSeqiNP_000556.1. NM_000565.3. [P08887-1]
NP_001193795.1. NM_001206866.1.
NP_852004.1. NM_181359.2. [P08887-2]
UniGeneiHs.135087.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N26X-ray2.40A20-344[»]
1N2Qmodel-C/D20-344[»]
1P9MX-ray3.65C115-315[»]
2ARWNMR-A212-336[»]
ProteinModelPortaliP08887.
SMRiP08887.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109784. 15 interactors.
DIPiDIP-162N.
DIP-3777N.
IntActiP08887. 5 interactors.
MINTiMINT-190110.
STRINGi9606.ENSP00000357470.

Chemistry databases

ChEMBLiCHEMBL2364155.
DrugBankiDB06273. Tocilizumab.
GuidetoPHARMACOLOGYi1708.

PTM databases

iPTMnetiP08887.
PhosphoSitePlusiP08887.

Polymorphism and mutation databases

BioMutaiIL6R.
DMDMi124343.

Proteomic databases

MaxQBiP08887.
PaxDbiP08887.
PeptideAtlasiP08887.
PRIDEiP08887.

Protocols and materials databases

DNASUi3570.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344086; ENSP00000340589; ENSG00000160712. [P08887-2]
ENST00000368485; ENSP00000357470; ENSG00000160712. [P08887-1]
GeneIDi3570.
KEGGihsa:3570.
UCSCiuc001fez.2. human. [P08887-1]

Organism-specific databases

CTDi3570.
DisGeNETi3570.
GeneCardsiIL6R.
HGNCiHGNC:6019. IL6R.
HPAiCAB034142.
MIMi147880. gene.
614689. phenotype.
614752. phenotype.
neXtProtiNX_P08887.
OpenTargetsiENSG00000160712.
PharmGKBiPA29835.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410II5K. Eukaryota.
ENOG4111XGC. LUCA.
GeneTreeiENSGT00530000063103.
HOVERGENiHBG052118.
InParanoidiP08887.
KOiK05055.
OrthoDBiEOG091G07XD.
PhylomeDBiP08887.
TreeFamiTF331210.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000160712-MONOMER.
ReactomeiR-HSA-1059683. Interleukin-6 signaling.
R-HSA-110056. MAPK3 (ERK1) activation.
R-HSA-112411. MAPK1 (ERK2) activation.
SignaLinkiP08887.
SIGNORiP08887.

Miscellaneous databases

ChiTaRSiIL6R. human.
EvolutionaryTraceiP08887.
GeneWikiiInterleukin-6_receptor.
GenomeRNAii3570.
PMAP-CutDBP08887.
PROiP08887.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000160712.
CleanExiHS_IL6R.
ExpressionAtlasiP08887. baseline and differential.
GenevisibleiP08887. HS.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 3 hits.
InterProiIPR003961. FN3_dom.
IPR003530. Hematopoietin_rcpt_L_F3_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR015321. TypeI_recpt_CBD.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF09240. IL6Ra-bind. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
PS01354. HEMATOPO_REC_L_F3. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIL6RA_HUMAN
AccessioniPrimary (citable) accession number: P08887
Secondary accession number(s): A8KAE8
, B2R6V4, Q16202, Q53EQ7, Q5FWG2, Q5VZ23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: November 30, 2016
This is version 196 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 cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.