Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Interleukin-1 receptor-associated kinase 1

Gene

IRAK1

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

Functioni

Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei239ATP1
Active sitei340Proton acceptorPROSITE-ProRule annotation1
Binding sitei358ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi218 – 226ATPPROSITE-ProRule annotation9
Nucleotide bindingi342 – 345ATPPROSITE-ProRule annotation4

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • heat shock protein binding Source: Ensembl
  • kinase activity Source: MGI
  • NF-kappaB-inducing kinase activity Source: ProtInc
  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • protein kinase activity Source: MGI
  • protein serine/threonine kinase activity Source: Reactome

GO - Biological processi

  • activation of MAPK activity Source: Reactome
  • activation of NF-kappaB-inducing kinase activity Source: UniProtKB
  • aging Source: Ensembl
  • cellular response to heat Source: Ensembl
  • cellular response to hypoxia Source: Ensembl
  • interleukin-1-mediated signaling pathway Source: BHF-UCL
  • JNK cascade Source: Reactome
  • lipopolysaccharide-mediated signaling pathway Source: BHF-UCL
  • MyD88-dependent toll-like receptor signaling pathway Source: BHF-UCL
  • negative regulation of apoptotic process Source: Reactome
  • negative regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  • nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • positive regulation of MAP kinase activity Source: GO_Central
  • positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  • positive regulation of smooth muscle cell proliferation Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of type I interferon production Source: BHF-UCL
  • protein autophosphorylation Source: BHF-UCL
  • protein complex oligomerization Source: UniProtKB
  • protein phosphorylation Source: ProtInc
  • regulation of cytokine-mediated signaling pathway Source: BHF-UCL
  • response to interleukin-1 Source: BHF-UCL
  • response to lipopolysaccharide Source: BHF-UCL
  • signal transduction Source: ProtInc
  • toll-like receptor 2 signaling pathway Source: BHF-UCL
  • toll-like receptor 4 signaling pathway Source: GO_Central
  • toll-like receptor 9 signaling pathway Source: Reactome
  • toll-like receptor signaling pathway Source: Reactome
  • transmembrane receptor protein serine/threonine kinase signaling pathway Source: UniProtKB
  • type I interferon signaling pathway Source: BHF-UCL
  • viral process Source: UniProtKB-KW

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processHost-virus interaction, Immunity, Innate immunity
LigandATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-1257604 PIP3 activates AKT signaling
R-HSA-166058 MyD88:Mal cascade initiated on plasma membrane
R-HSA-168638 NOD1/2 Signaling Pathway
R-HSA-209543 p75NTR recruits signalling complexes
R-HSA-209560 NF-kB is activated and signals survival
R-HSA-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-HSA-450302 activated TAK1 mediates p38 MAPK activation
R-HSA-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-9020702 Interleukin-1 signaling
R-HSA-937039 IRAK1 recruits IKK complex
R-HSA-975110 TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling
R-HSA-975138 TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation
R-HSA-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-HSA-975155 MyD88 dependent cascade initiated on endosome
R-HSA-975871 MyD88 cascade initiated on plasma membrane
SignaLinkiP51617
SIGNORiP51617

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-1 receptor-associated kinase 1 (EC:2.7.11.1)
Short name:
IRAK-1
Gene namesi
Name:IRAK1
Synonyms:IRAK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

EuPathDBiHostDB:ENSG00000184216.11
HGNCiHGNC:6112 IRAK1
MIMi300283 gene
neXtProtiNX_P51617

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Lipid droplet, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi209T → A: Completely abolishes auto-phosphorylation in the kinase domain. 1 Publication1
Mutagenesisi239K → S: Loss of kinase activity. 1 Publication1
Mutagenesisi387T → A: Loss of kinase activity. 1 Publication1

Organism-specific databases

DisGeNETi3654
MalaCardsiIRAK1
OpenTargetsiENSG00000184216
Orphaneti93552 Pediatric systemic lupus erythematosus
536 Systemic lupus erythematosus
PharmGKBiPA29912

Chemistry databases

ChEMBLiCHEMBL3357
GuidetoPHARMACOLOGYi2042

Polymorphism and mutation databases

BioMutaiIRAK1
DMDMi8928535

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000860301 – 712Interleukin-1 receptor-associated kinase 1Add BLAST712

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66Phosphothreonine; by PKC/PRKCI1 Publication1
Modified residuei131PhosphoserineCombined sources1
Cross-linki134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki180Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei209Phosphothreonine; by IRAK41 Publication1
Modified residuei371PhosphoserineCombined sources1
Modified residuei375PhosphoserineCombined sources1
Modified residuei387Phosphothreonine1 Publication1
Modified residuei556PhosphoserineCombined sources1

Post-translational modificationi

Following recruitment on the activated receptor complex, phosphorylated on Thr-209, probably by IRAK4, resulting in a conformational change of the kinase domain, allowing further phosphorylations to take place. Thr-387 phosphorylation in the activation loop is required to achieve full enzymatic activity.4 Publications
Polyubiquitinated by TRAF6 after cell stimulation with IL-1-beta by PELI1, PELI2 and PELI3. Polyubiquitination occurs with polyubiquitin chains linked through 'Lys-63'. Ubiquitination promotes interaction with NEMO/IKBKG. Also sumoylated; leading to nuclear translocation.3 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP51617
MaxQBiP51617
PaxDbiP51617
PeptideAtlasiP51617
PRIDEiP51617
ProteomicsDBi56349
56350 [P51617-2]
56351 [P51617-3]
56352 [P51617-4]

PTM databases

iPTMnetiP51617
PhosphoSitePlusiP51617

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are ubiquitously expressed in all tissues examined, with isoform 1 being more strongly expressed than isoform 2.1 Publication

Gene expression databases

BgeeiENSG00000184216
CleanExiHS_IRAK1
ExpressionAtlasiP51617 baseline and differential
GenevisibleiP51617 HS

Organism-specific databases

HPAiCAB004461
HPA054476

Interactioni

Subunit structurei

Homodimer (By similarity). Forms a complex with TRAF6, PELI1, IRAK4 and MYD88 (PubMed:16951688). Direct binding of SMAD6 to PELI1 prevents complex formation and hence negatively regulates IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression (PubMed:16951688). The TRAF6-PELI1-IRAK4-MYD88 complex recruits MAP3K7/TAK1, TAB1 and TAB2 to mediate NF-kappa-B activation (PubMed:16951688). Interaction with MYD88 recruits IRAK1 to the stimulated receptor complex (PubMed:9430229). Interacts with TOLLIP; this interaction occurs in the cytosol prior to receptor activation (PubMed:10854325). Interacts with IL1RL1 (PubMed:16286016). Interacts with PELI1 and TRAF6 (PubMed:12496252). Interacts (when polyubiquitinated) with IKBKG/NEMO (PubMed:18347055). Interacts with RSAD2/viperin (By similarity). Interacts with IRAK1BP1 (By similarity). Interacts with PELI2 (By similarity). Interacts with ZC3H12A; this interaction increases the interaction between ZC3H12A and IKBKB/IKKB (By similarity). Interacts with IRAK4 (PubMed:11960013). Interacts with PELI3 (PubMed:12874243). Interacts with INAVA; the interaction takes place upon PRR stimulation (PubMed:28436939).By similarity9 Publications
(Microbial infection) Interacts with mumps virus protein SH; this interaction inhibits downstream NF-kappa-B pathway activation.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • heat shock protein binding Source: Ensembl
  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi109863, 123 interactors
CORUMiP51617
DIPiDIP-397N
ELMiP51617
IntActiP51617, 80 interactors
MINTiP51617
STRINGi9606.ENSP00000358997

Chemistry databases

BindingDBiP51617

Structurei

Secondary structure

1712
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi195 – 197Combined sources3
Helixi202 – 209Combined sources8
Turni210 – 212Combined sources3
Beta strandi217 – 220Combined sources4
Beta strandi222 – 231Combined sources10
Beta strandi234 – 241Combined sources8
Helixi249 – 265Combined sources17
Beta strandi274 – 280Combined sources7
Beta strandi283 – 289Combined sources7
Helixi296 – 301Combined sources6
Beta strandi304 – 307Combined sources4
Helixi312 – 331Combined sources20
Beta strandi332 – 334Combined sources3
Beta strandi345 – 348Combined sources4
Beta strandi354 – 356Combined sources3
Helixi359 – 361Combined sources3
Helixi388 – 390Combined sources3
Helixi393 – 397Combined sources5
Helixi403 – 419Combined sources17
Beta strandi423 – 427Combined sources5
Beta strandi430 – 433Combined sources4
Helixi434 – 436Combined sources3
Helixi437 – 445Combined sources9
Helixi464 – 466Combined sources3
Helixi467 – 476Combined sources10
Helixi487 – 500Combined sources14
Helixi505 – 507Combined sources3
Helixi511 – 521Combined sources11
Helixi522 – 524Combined sources3

3D structure databases

ProteinModelPortaliP51617
SMRiP51617
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 106DeathAdd BLAST80
Domaini212 – 521Protein kinasePROSITE-ProRule annotationAdd BLAST310

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni110 – 211ProST regionAdd BLAST102

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi649 – 655Poly-Ser7
Compositional biasi688 – 691Poly-Ser4

Domaini

The ProST region is composed of many proline and serine residues (more than 20 of each) and some threonines. This region is the site of IRAK-1 hyperphosphorylation.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1187 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00530000063073
HOGENOMiHOG000015226
HOVERGENiHBG052144
InParanoidiP51617
KOiK04730
OMAiGFYCLVY
OrthoDBiEOG091G0YKT
PhylomeDBiP51617
TreeFamiTF328924

Family and domain databases

CDDicd08794 Death_IRAK1, 1 hit
InterProiView protein in InterPro
IPR011029 DEATH-like_dom_sf
IPR000488 Death_domain
IPR035533 Death_IRAK1
IPR035536 IRAK1
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR24419:SF1 PTHR24419:SF1, 1 hit
PfamiView protein in Pfam
PF00531 Death, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF47986 SSF47986, 1 hit
SSF56112 SSF56112, 2 hits
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P51617-1) [UniParc]FASTAAdd to basket
Also known as: a

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
MAGGPGPGEP AAPGAQHFLY EVPPWVMCRF YKVMDALEPA DWCQFAALIV
60 70 80 90 100
RDQTELRLCE RSGQRTASVL WPWINRNARV ADLVHILTHL QLLRARDIIT
110 120 130 140 150
AWHPPAPLPS PGTTAPRPSS IPAPAEAEAW SPRKLPSSAS TFLSPAFPGS
160 170 180 190 200
QTHSGPELGL VPSPASLWPP PPSPAPSSTK PGPESSVSLL QGARPFPFCW
210 220 230 240 250
PLCEISRGTH NFSEELKIGE GGFGCVYRAV MRNTVYAVKR LKENADLEWT
260 270 280 290 300
AVKQSFLTEV EQLSRFRHPN IVDFAGYCAQ NGFYCLVYGF LPNGSLEDRL
310 320 330 340 350
HCQTQACPPL SWPQRLDILL GTARAIQFLH QDSPSLIHGD IKSSNVLLDE
360 370 380 390 400
RLTPKLGDFG LARFSRFAGS SPSQSSMVAR TQTVRGTLAY LPEEYIKTGR
410 420 430 440 450
LAVDTDTFSF GVVVLETLAG QRAVKTHGAR TKYLKDLVEE EAEEAGVALR
460 470 480 490 500
STQSTLQAGL AADAWAAPIA MQIYKKHLDP RPGPCPPELG LGLGQLACCC
510 520 530 540 550
LHRRAKRRPP MTQVYERLEK LQAVVAGVPG HSEAASCIPP SPQENSYVSS
560 570 580 590 600
TGRAHSGAAP WQPLAAPSGA SAQAAEQLQR GPNQPVESDE SLGGLSAALR
610 620 630 640 650
SWHLTPSCPL DPAPLREAGC PQGDTAGESS WGSGPGSRPT AVEGLALGSS
660 670 680 690 700
ASSSSEPPQI IINPARQKMV QKLALYEDGA LDSLQLLSSS SLPGLGLEQD
710
RQGPEESDEF QS
Length:712
Mass (Da):76,537
Last modified:December 1, 2000 - v2
Checksum:iA7ADED75D3A3981D
GO
Isoform 2 (identifier: P51617-2) [UniParc]FASTAAdd to basket
Also known as: b

The sequence of this isoform differs from the canonical sequence as follows:
     513-542: Missing.

Note: Inactive.
Show »
Length:682
Mass (Da):73,421
Checksum:i687C7EB6064FA918
GO
Isoform 3 (identifier: P51617-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     45-45: F → FGGWRRAAGGREARGLLAPTPDAPRPA
     478-492: Missing.
     513-542: Missing.

Note: No experimental confirmation available.
Show »
Length:693
Mass (Da):74,560
Checksum:iD744A32E997E1246
GO
Isoform 4 (identifier: P51617-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     435-513: Missing.

Show »
Length:633
Mass (Da):68,022
Checksum:i419926E55C935F38
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051629194R → H. Corresponds to variant dbSNP:rs11465830Ensembl.1
Natural variantiVAR_051630196F → S1 PublicationCorresponds to variant dbSNP:rs1059702Ensembl.1
Natural variantiVAR_051631203C → S. Corresponds to variant dbSNP:rs10127175Ensembl.1
Natural variantiVAR_040573398T → M1 PublicationCorresponds to variant dbSNP:rs56340948Ensembl.1
Natural variantiVAR_040574412V → M in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_040575421Q → H in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040576532S → L2 PublicationsCorresponds to variant dbSNP:rs1059703Ensembl.1
Natural variantiVAR_040577619G → S1 PublicationCorresponds to variant dbSNP:rs34112487Ensembl.1
Natural variantiVAR_040578625T → M1 PublicationCorresponds to variant dbSNP:rs35638718Ensembl.1
Natural variantiVAR_040579638R → W1 PublicationCorresponds to variant dbSNP:rs56082801Ensembl.1
Natural variantiVAR_040580690S → G in a lung adenocarcinoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01184945F → FGGWRRAAGGREARGLLAPT PDAPRPA in isoform 3. 1 Publication1
Alternative sequenceiVSP_041950435 – 513Missing in isoform 4. 2 PublicationsAdd BLAST79
Alternative sequenceiVSP_011850478 – 492Missing in isoform 3. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_011851513 – 542Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST30

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76191 mRNA Translation: AAC41949.1
AF030876 Genomic DNA Translation: AAC08756.1
AF346607 mRNA Translation: AAK62888.1
DQ054788 mRNA Translation: AAY88246.1
U52112 Genomic DNA No translation available.
CH471172 Genomic DNA Translation: EAW72762.1
CH471172 Genomic DNA Translation: EAW72763.1
CH471172 Genomic DNA Translation: EAW72764.1
CH471172 Genomic DNA Translation: EAW72765.1
BC054000 mRNA Translation: AAH54000.1
BC014963 mRNA Translation: AAH14963.1
CCDSiCCDS14740.1 [P51617-1]
CCDS35443.1 [P51617-4]
CCDS35444.1 [P51617-2]
PIRiG02512
RefSeqiNP_001020413.1, NM_001025242.1 [P51617-2]
NP_001020414.1, NM_001025243.1 [P51617-4]
NP_001560.2, NM_001569.3 [P51617-1]
UniGeneiHs.522819

Genome annotation databases

EnsembliENST00000369974; ENSP00000358991; ENSG00000184216 [P51617-4]
ENST00000369980; ENSP00000358997; ENSG00000184216 [P51617-1]
ENST00000393687; ENSP00000377291; ENSG00000184216 [P51617-2]
GeneIDi3654
KEGGihsa:3654
UCSCiuc004fjr.2 human [P51617-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiIRAK1_HUMAN
AccessioniPrimary (citable) accession number: P51617
Secondary accession number(s): D3DWW3
, D3DWW4, Q7Z5V4, Q96C06, Q96RL2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: July 18, 2018
This is version 195 of the entry and version 2 of the sequence. See 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 X
    Human chromosome X: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families
  8. UniProtKB entry view manual
    User manual for the UniProtKB entry view

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health