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Protein

Interleukin-1 receptor-associated kinase-like 2

Gene

IRAK2

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

Functioni

Binds to the IL-1 type I receptor following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation and mRNA stabilization.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei237 – 2371ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi216 – 2249ATPPROSITE-ProRule annotation
Nucleotide bindingi337 – 3404ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein heterodimerization activity Source: BHF-UCL
  3. protein homodimerization activity Source: BHF-UCL
  4. protein serine/threonine kinase activity Source: GO_Central

GO - Biological processi

  1. activation of MAPK activity Source: Reactome
  2. I-kappaB kinase/NF-kappaB signaling Source: ProtInc
  3. inflammatory response Source: ProtInc
  4. innate immune response Source: Reactome
  5. interleukin-1-mediated signaling pathway Source: BHF-UCL
  6. intracellular signal transduction Source: GO_Central
  7. JNK cascade Source: Reactome
  8. lipopolysaccharide-mediated signaling pathway Source: Ensembl
  9. MyD88-dependent toll-like receptor signaling pathway Source: BHF-UCL
  10. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  11. negative regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  12. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  13. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
  14. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  15. protein phosphorylation Source: ProtInc
  16. regulation of cytokine-mediated signaling pathway Source: BHF-UCL
  17. response to interleukin-1 Source: BHF-UCL
  18. stress-activated MAPK cascade Source: Reactome
  19. toll-like receptor 10 signaling pathway Source: Reactome
  20. toll-like receptor 2 signaling pathway Source: Reactome
  21. toll-like receptor 3 signaling pathway Source: Reactome
  22. toll-like receptor 4 signaling pathway Source: Reactome
  23. toll-like receptor 5 signaling pathway Source: Reactome
  24. toll-like receptor 9 signaling pathway Source: Reactome
  25. toll-like receptor signaling pathway Source: GO_Central
  26. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  27. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  28. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
REACT_21399. activated TAK1 mediates p38 MAPK activation.
REACT_22442. Interleukin-1 signaling.
REACT_25018. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
REACT_25024. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
REACT_25222. MyD88 dependent cascade initiated on endosome.
REACT_25380. IRAK2 mediated activation of TAK1 complex.
REACT_27215. MyD88 cascade initiated on plasma membrane.
REACT_6788. MyD88:Mal cascade initiated on plasma membrane.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinkiO43187.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-1 receptor-associated kinase-like 2
Short name:
IRAK-2
Gene namesi
Name:IRAK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:6113. IRAK2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. cytosol Source: Reactome
  3. endosome membrane Source: Reactome
  4. interleukin-1 receptor complex Source: GO_Central
  5. nucleus Source: GO_Central
  6. plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29913.

Polymorphism and mutation databases

BioMutaiIRAK2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 625625Interleukin-1 receptor-associated kinase-like 2PRO_0000086032Add
BLAST

Proteomic databases

MaxQBiO43187.
PaxDbiO43187.
PeptideAtlasiO43187.
PRIDEiO43187.

PTM databases

PhosphoSiteiO43187.

Expressioni

Tissue specificityi

Expressed in spleen, thymus, prostate, lung, liver, skeletal muscle, kidney, pancreas and peripheral blood leukocytes.1 Publication

Gene expression databases

BgeeiO43187.
CleanExiHS_IRAK2.
GenevestigatoriO43187.

Organism-specific databases

HPAiCAB013483.
HPA050520.

Interactioni

Subunit structurei

Interacts with MYD88. IL-1 stimulation leads to the formation of a signaling complex which dissociates from the IL-1 receptor following the binding of PELI1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ARAFP103982EBI-447733,EBI-365961
K7RP684672EBI-447733,EBI-8022707From a different organism.
Sarm1Q6PDS32EBI-447733,EBI-6117196From a different organism.
STT3AP469772EBI-447733,EBI-719212
TARDBPQ131482EBI-447733,EBI-372899
TIRAPP587532EBI-447733,EBI-528644
TOLLIPQ9H0E22EBI-447733,EBI-74615
ZC3H12AQ5D1E82EBI-447733,EBI-747793

Protein-protein interaction databases

BioGridi109865. 37 interactions.
DIPiDIP-31800N.
IntActiO43187. 30 interactions.
MINTiMINT-97184.
STRINGi9606.ENSP00000256458.

Structurei

Secondary structure

1
625
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Helixi10 – 167Combined sources
Turni17 – 226Combined sources
Helixi25 – 328Combined sources
Turni33 – 364Combined sources
Helixi39 – 479Combined sources
Helixi48 – 503Combined sources
Helixi56 – 6510Combined sources
Turni66 – 683Combined sources
Helixi72 – 765Combined sources
Turni77 – 815Combined sources
Helixi84 – 874Combined sources
Turni88 – 914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MOPX-ray3.40K/L/M/N2-112[»]
ProteinModelPortaliO43187.
SMRiO43187. Positions 2-94, 196-499.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43187.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 9482DeathAdd
BLAST
Domaini210 – 489280Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The protein kinase domain is predicted to be catalytically inactive.

Sequence similaritiesi

Contains 1 death domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063073.
HOGENOMiHOG000113102.
HOVERGENiHBG052145.
InParanoidiO43187.
KOiK04731.
OMAiLSEWDWM.
OrthoDBiEOG747PHP.
PhylomeDBiO43187.
TreeFamiTF328924.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43187-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACYIYQLPS WVLDDLCRNM DALSEWDWME FASYVITDLT QLRKIKSMER
60 70 80 90 100
VQGVSITREL LWWWGMRQAT VQQLVDLLCR LELYRAAQII LNWKPAPEIR
110 120 130 140 150
CPIPAFPDSV KPEKPLAASV RKAEDEQEEG QPVRMATFPG PGSSPARAHQ
160 170 180 190 200
PAFLQPPEED APHSLRSDLP TSSDSKDFST SIPKQEKLLS LAGDSLFWSE
210 220 230 240 250
ADVVQATDDF NQNRKISQGT FADVYRGHRH GKPFVFKKLR ETACSSPGSI
260 270 280 290 300
ERFFQAELQI CLRCCHPNVL PVLGFCAARQ FHSFIYPYMA NGSLQDRLQG
310 320 330 340 350
QGGSDPLPWP QRVSICSGLL CAVEYLHGLE IIHSNVKSSN VLLDQNLTPK
360 370 380 390 400
LAHPMAHLCP VNKRSKYTMM KTHLLRTSAA YLPEDFIRVG QLTKRVDIFS
410 420 430 440 450
CGIVLAEVLT GIPAMDNNRS PVYLKDLLLS DIPSSTASLC SRKTGVENVM
460 470 480 490 500
AKEICQKYLE KGAGRLPEDC AEALATAACL CLRRRNTSLQ EVCGSVAAVE
510 520 530 540 550
ERLRGRETLL PWSGLSEGTG SSSNTPEETD DVDNSSLDAS SSMSVAPWAG
560 570 580 590 600
AATPLLPTEN GEGRLRVIVG READSSSEAC VGLEPPQDVT ETSWQIEINE
610 620
AKRKLMENIL LYKEEKVDSI ELFGP
Length:625
Mass (Da):69,433
Last modified:February 6, 2007 - v2
Checksum:i715C954BC9452710
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431R → Q.1 Publication
Corresponds to variant rs34945585 [ dbSNP | Ensembl ].
VAR_041342
Natural varianti47 – 471S → Y.1 Publication
Corresponds to variant rs11465864 [ dbSNP | Ensembl ].
VAR_030527
Natural varianti99 – 991I → V.1 Publication
Corresponds to variant rs55898544 [ dbSNP | Ensembl ].
VAR_041343
Natural varianti147 – 1471R → T.1 Publication
Corresponds to variant rs56053222 [ dbSNP | Ensembl ].
VAR_041344
Natural varianti214 – 2141R → G.1 Publication
Corresponds to variant rs35060588 [ dbSNP | Ensembl ].
VAR_041345
Natural varianti249 – 2491S → L in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041346
Natural varianti392 – 3921L → V.1 Publication
Corresponds to variant rs3844283 [ dbSNP | Ensembl ].
VAR_030528
Natural varianti421 – 4211P → T in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041347
Natural varianti431 – 4311D → E.3 Publications
Corresponds to variant rs708035 [ dbSNP | Ensembl ].
VAR_030529
Natural varianti439 – 4391L → V.1 Publication
Corresponds to variant rs11465927 [ dbSNP | Ensembl ].
VAR_030530
Natural varianti469 – 4691D → N.1 Publication
Corresponds to variant rs56242986 [ dbSNP | Ensembl ].
VAR_041348
Natural varianti503 – 5031L → I.1 Publication
Corresponds to variant rs9854688 [ dbSNP | Ensembl ].
VAR_030531
Natural varianti566 – 5661R → W.1 Publication
Corresponds to variant rs55740652 [ dbSNP | Ensembl ].
VAR_041349
Natural varianti574 – 5741D → H.
Corresponds to variant rs11465930 [ dbSNP | Ensembl ].
VAR_030532

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ496794 mRNA. Translation: CAD43180.3.
AK299033 mRNA. Translation: BAG61108.1.
BC125184 mRNA. Translation: AAI25185.1.
AF026273 mRNA. Translation: AAB87669.1.
CCDSiCCDS33697.1.
RefSeqiNP_001561.3. NM_001570.3.
UniGeneiHs.449207.

Genome annotation databases

EnsembliENST00000256458; ENSP00000256458; ENSG00000134070.
GeneIDi3656.
KEGGihsa:3656.
UCSCiuc003bve.1. human.

Polymorphism and mutation databases

BioMutaiIRAK2.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ496794 mRNA. Translation: CAD43180.3.
AK299033 mRNA. Translation: BAG61108.1.
BC125184 mRNA. Translation: AAI25185.1.
AF026273 mRNA. Translation: AAB87669.1.
CCDSiCCDS33697.1.
RefSeqiNP_001561.3. NM_001570.3.
UniGeneiHs.449207.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MOPX-ray3.40K/L/M/N2-112[»]
ProteinModelPortaliO43187.
SMRiO43187. Positions 2-94, 196-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109865. 37 interactions.
DIPiDIP-31800N.
IntActiO43187. 30 interactions.
MINTiMINT-97184.
STRINGi9606.ENSP00000256458.

PTM databases

PhosphoSiteiO43187.

Polymorphism and mutation databases

BioMutaiIRAK2.

Proteomic databases

MaxQBiO43187.
PaxDbiO43187.
PeptideAtlasiO43187.
PRIDEiO43187.

Protocols and materials databases

DNASUi3656.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256458; ENSP00000256458; ENSG00000134070.
GeneIDi3656.
KEGGihsa:3656.
UCSCiuc003bve.1. human.

Organism-specific databases

CTDi3656.
GeneCardsiGC03P010206.
HGNCiHGNC:6113. IRAK2.
HPAiCAB013483.
HPA050520.
MIMi603304. gene.
neXtProtiNX_O43187.
PharmGKBiPA29913.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063073.
HOGENOMiHOG000113102.
HOVERGENiHBG052145.
InParanoidiO43187.
KOiK04731.
OMAiLSEWDWM.
OrthoDBiEOG747PHP.
PhylomeDBiO43187.
TreeFamiTF328924.

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
REACT_21399. activated TAK1 mediates p38 MAPK activation.
REACT_22442. Interleukin-1 signaling.
REACT_25018. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
REACT_25024. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
REACT_25222. MyD88 dependent cascade initiated on endosome.
REACT_25380. IRAK2 mediated activation of TAK1 complex.
REACT_27215. MyD88 cascade initiated on plasma membrane.
REACT_6788. MyD88:Mal cascade initiated on plasma membrane.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinkiO43187.

Miscellaneous databases

EvolutionaryTraceiO43187.
GeneWikiiIRAK2.
GenomeRNAii3656.
NextBioi14303.
PROiO43187.
SOURCEiSearch...

Gene expression databases

BgeeiO43187.
CleanExiHS_IRAK2.
GenevestigatoriO43187.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of Exon 13 and the 3'UTR region of human IRAK-2 and characterisation of the full length gene."
    Rosati O., Martin M.U.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLU-431.
  2. "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].
  3. "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].
  4. "IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling."
    Muzio M., Ni J., Feng P., Dixit V.M.
    Science 278:1612-1615(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-590, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TRAF6; MYD88 AND IL1R1, VARIANT GLU-431.
    Tissue: Endothelial cell.
  5. "IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated kinase (IRAK) family."
    Wesche H., Gao X., Li X., Kirschning C.J., Stark G.R., Cao Z.
    J. Biol. Chem. 274:19403-19410(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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.
  7. "Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling."
    Lin S.-C., Lo Y.-C., Wu H.
    Nature 465:885-890(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 2-112.
  8. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-43; TYR-47; VAL-99; THR-147; GLY-214; LEU-249; VAL-392; THR-421; GLU-431; VAL-439; ASN-469; ILE-503 AND TRP-566.

Entry informationi

Entry nameiIRAK2_HUMAN
AccessioniPrimary (citable) accession number: O43187
Secondary accession number(s): B4DQZ6, Q08AG6, Q5K546
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: February 6, 2007
Last modified: April 29, 2015
This is version 137 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

Caution

Asn-335 is present instead of the conserved Asp which is expected to be an active site residue. This enzyme has been shown to be catalytically inactive.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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

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.