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O43318

- M3K7_HUMAN

UniProt

O43318 - M3K7_HUMAN

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Protein

Mitogen-activated protein kinase kinase kinase 7

Gene

MAP3K7

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

Functioni

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Ceramides are also able to activate MAP3K7/TAK1. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B kinase complex (IKK). Both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1), while nuclear factor-kappa B is activated by IKK. MAP3K7 activates also IKBKB and MAPK8/JNK1 in response to TRAF6 signaling and mediates BMP2-induced apoptosis. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Activated by proinflammatory cytokines and in response to physical and chemical stresses, including osmotic stress, oxidative stress, arsenic and ultraviolet light irradiation. Activated by 'Lys-63'-linked polyubiquitination and by autophosphorylation. Association with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2 promotes activation through autophosphorylation, whereas PPM1B/PP2CB, PP2A and PPP6C dephosphorylation leads to inactivation.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631ATP
Active sitei156 – 1561Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 509ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. MAP kinase kinase activity Source: Ensembl
  4. MAP kinase kinase kinase activity Source: UniProtKB
  5. protein kinase activity Source: UniProtKB
  6. protein serine/threonine kinase activity Source: Reactome
  7. scaffold protein binding Source: MGI

GO - Biological processi

  1. activation of MAPK activity Source: UniProtKB
  2. activation of MAPKK activity Source: UniProtKB
  3. activation of NF-kappaB-inducing kinase activity Source: UniProtKB
  4. angiogenesis Source: Ensembl
  5. apoptotic process Source: UniProtKB-KW
  6. Fc-epsilon receptor signaling pathway Source: Reactome
  7. histone H3 acetylation Source: BHF-UCL
  8. I-kappaB kinase/NF-kappaB signaling Source: Reactome
  9. I-kappaB phosphorylation Source: UniProtKB
  10. innate immune response Source: Reactome
  11. JNK cascade Source: UniProtKB
  12. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  13. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  14. negative regulation of apoptotic signaling pathway Source: Ensembl
  15. negative regulation of ripoptosome assembly involved in necroptotic process Source: Ensembl
  16. neural tube formation Source: Ensembl
  17. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  18. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
  19. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  20. positive regulation of interleukin-2 production Source: UniProtKB
  21. positive regulation of JNK cascade Source: Ensembl
  22. positive regulation of JUN kinase activity Source: UniProtKB
  23. positive regulation of NF-kappaB transcription factor activity Source: Reactome
  24. positive regulation of T cell activation Source: UniProtKB
  25. positive regulation of T cell cytokine production Source: UniProtKB
  26. regulation of reactive oxygen species metabolic process Source: Ensembl
  27. stress-activated MAPK cascade Source: UniProtKB
  28. T cell receptor signaling pathway Source: UniProtKB
  29. toll-like receptor 10 signaling pathway Source: Reactome
  30. toll-like receptor 2 signaling pathway Source: Reactome
  31. toll-like receptor 3 signaling pathway Source: Reactome
  32. toll-like receptor 4 signaling pathway Source: Reactome
  33. toll-like receptor 5 signaling pathway Source: Reactome
  34. toll-like receptor 9 signaling pathway Source: Reactome
  35. toll-like receptor signaling pathway Source: Reactome
  36. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  37. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  38. transcription, DNA-templated Source: UniProtKB-KW
  39. transforming growth factor beta receptor signaling pathway Source: ProtInc
  40. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_118656. Activation of NF-kappaB in B cells.
REACT_12555. Downstream TCR signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_172761. Ca2+ pathway.
REACT_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_25351. TRAF6 mediated induction of TAK1 complex.
REACT_25380. IRAK2 mediated activation of TAK1 complex.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinkiO43318.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase kinase kinase 7 (EC:2.7.11.25)
Alternative name(s):
Transforming growth factor-beta-activated kinase 1
Short name:
TGF-beta-activated kinase 1
Gene namesi
Name:MAP3K7
Synonyms:TAK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:6859. MAP3K7.

Subcellular locationi

Cytoplasm 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
Note: Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the cell membrane.

GO - Cellular componenti

  1. Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. endosome membrane Source: Reactome
  5. nucleus Source: UniProt
  6. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631K → W: Loss of kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA30603.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 606606Mitogen-activated protein kinase kinase kinase 7PRO_0000086252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki72 – 72Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei184 – 1841Phosphothreonine; by autocatalysis1 Publication
Modified residuei187 – 1871Phosphothreonine; by autocatalysis4 Publications
Modified residuei192 – 1921Phosphoserine; by autocatalysis2 Publications
Modified residuei389 – 3891Phosphoserine4 Publications
Modified residuei439 – 4391Phosphoserine8 Publications

Post-translational modificationi

Association with TAB1/MAP3K7IP1 promotes autophosphorylation at Ser-192 and subsequent activation. Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7. Dephosphorylation at Ser-192 by PPM1B/PP2CB and at Thr-187 by PP2A and PPP6C leads to inactivation.6 Publications
'Lys-48'-linked polyubiquitination at Lys-72 is induced by TNFalpha, and leads to proteasomal degradation. Requires 'Lys-63'-linked polyubiquitination for autophosphorylation and subsequent activation. 'Lys-63'-linked ubiquitination does not lead to proteasomal degradation. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains. Deubiquitinated by Y.enterocolitica YopP.2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO43318.
PaxDbiO43318.
PRIDEiO43318.

PTM databases

PhosphoSiteiO43318.

Expressioni

Tissue specificityi

Isoform 1A is the most abundant in ovary, skeletal muscle, spleen and blood mononuclear cells. Isoform 1B is highly expressed in brain, kidney and small intestine. Isoform 1C is the major form in prostate. Isoform 1D is the less abundant form.1 Publication

Gene expression databases

BgeeiO43318.
CleanExiHS_MAP3K7.
ExpressionAtlasiO43318. baseline and differential.
GenevestigatoriO43318.

Organism-specific databases

HPAiHPA007633.

Interactioni

Subunit structurei

Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts with TAB1/MAP3K7IP1, TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3. Identified in the TRIKA2 complex composed of MAP3K7/TAK1, TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2. Interacts with PPM1L and PPM1B/PP2CB. Interaction with PP2A and PPP6C leads to its repressed activity. Interacts with TRAF6 and TAB1/MAP3K7IP1; during IL-1 signaling. Interacts with TAOK1 and TAOK2; interaction with TAOK2 interferes with MAP3K7 interaction with IKKA, thus preventing NF-kappa-B activation. Interacts with WDR34 (via WD domains). Interacts with CYLD and RBCK1. Interacts with TGFBR1; induces MAP3K7/TAK1 activation by TRAF6. Interacts with MAPK8IP1 and SMAD6 (By similarity). Interacts with isoform 1 of VRK2. Interacts with DAB2; the interaction is induced by TGF-beta stimulation and may mediate TGF-beta stimulated JNK activation. Interacts with TRIM5.By similarity22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
cagAB5Z6S04EBI-358684,EBI-7287204From a different organism.
CDC37Q165435EBI-358700,EBI-295634
HSP90AA1P079005EBI-358700,EBI-296047
MAP2K7O147333EBI-358684,EBI-492605
MAPK8IP1Q9UQF211EBI-358684,EBI-78404
NLKQ9UBE83EBI-358684,EBI-366978
PPP6CO007434EBI-358684,EBI-359751
STAT3P407634EBI-358684,EBI-518675
TAB1Q157503EBI-358700,EBI-358643
TAB2Q9NYJ85EBI-358684,EBI-358708
TAB3Q8N5C83EBI-358684,EBI-359964
TRAF6Q9Y4K32EBI-358684,EBI-359276
UBCP0CG484EBI-358684,EBI-3390054

Protein-protein interaction databases

BioGridi112748. 120 interactions.
DIPiDIP-27523N.
IntActiO43318. 45 interactions.
MINTiMINT-88554.
STRINGi9606.ENSP00000358335.

Structurei

Secondary structure

1
606
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 353Combined sources
Beta strandi36 – 438Combined sources
Beta strandi46 – 5510Combined sources
Beta strandi58 – 647Combined sources
Helixi70 – 8314Combined sources
Beta strandi92 – 954Combined sources
Turni97 – 1004Combined sources
Beta strandi101 – 1055Combined sources
Helixi112 – 1176Combined sources
Beta strandi119 – 1235Combined sources
Helixi127 – 14519Combined sources
Beta strandi148 – 1503Combined sources
Helixi159 – 1613Combined sources
Beta strandi162 – 1654Combined sources
Turni166 – 1694Combined sources
Beta strandi170 – 1734Combined sources
Helixi193 – 1953Combined sources
Helixi198 – 2014Combined sources
Helixi209 – 22416Combined sources
Turni228 – 2325Combined sources
Helixi236 – 2449Combined sources
Helixi257 – 26610Combined sources
Helixi271 – 2733Combined sources
Helixi277 – 28711Combined sources
Helixi288 – 2903Combined sources
Turni292 – 2954Combined sources
Beta strandi300 – 3023Combined sources
Helixi402 – 41110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EVAX-ray2.00A31-412[»]
2YIYX-ray2.49A31-303[»]
4GS6X-ray2.20A31-303[»]
4L3PX-ray2.68A31-303[»]
4L52X-ray2.54A31-303[»]
4L53X-ray2.55A31-303[»]
4O91X-ray2.39A31-303[»]
ProteinModelPortaliO43318.
SMRiO43318. Positions 4-305.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43318.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 291256Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 300300Interaction with MAPK8IP1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 147Poly-Ser

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118807.
HOGENOMiHOG000231735.
HOVERGENiHBG003485.
InParanoidiO43318.
KOiK04427.
OMAiCKAKWKG.
OrthoDBiEOG7RBZ8D.
PhylomeDBiO43318.
TreeFamiTF105116.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR017421. MAPKKK7.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF038168. MAPKKK7. 1 hit.
PRINTSiPR00109. TYRKINASE.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1B (identifier: O43318-1) [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
MSTASAASSS SSSSAGEMIE APSQVLNFEE IDYKEIEVEE VVGRGAFGVV
60 70 80 90 100
CKAKWRAKDV AIKQIESESE RKAFIVELRQ LSRVNHPNIV KLYGACLNPV
110 120 130 140 150
CLVMEYAEGG SLYNVLHGAE PLPYYTAAHA MSWCLQCSQG VAYLHSMQPK
160 170 180 190 200
ALIHRDLKPP NLLLVAGGTV LKICDFGTAC DIQTHMTNNK GSAAWMAPEV
210 220 230 240 250
FEGSNYSEKC DVFSWGIILW EVITRRKPFD EIGGPAFRIM WAVHNGTRPP
260 270 280 290 300
LIKNLPKPIE SLMTRCWSKD PSQRPSMEEI VKIMTHLMRY FPGADEPLQY
310 320 330 340 350
PCQYSDEGQS NSATSTGSFM DIASTNTSNK SDTNMEQVPA TNDTIKRLES
360 370 380 390 400
KLLKNQAKQQ SESGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIA
410 420 430 440 450
ATTAYSKPKR GHRKTASFGN ILDVPEIVIS GNGQPRRRSI QDLTVTGTEP
460 470 480 490 500
GQVSSRSSSP SVRMITTSGP TSEKPTRSHP WTPDDSTDTN GSDNSIPMAY
510 520 530 540 550
LTLDHQLQPL APCPNSKESM AVFEQHCKMA QEYMKVQTEI ALLLQRKQEL
560 570 580 590 600
VAELDQDEKD QQNTSRLVQE HKKLLDENKS LSTYYQQCKK QLEVIRSQQQ

KRQGTS
Length:606
Mass (Da):67,196
Last modified:June 1, 1998 - v1
Checksum:i3D8F8147CD174013
GO
Isoform 1A (identifier: O43318-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     404-430: Missing.

Show »
Length:579
Mass (Da):64,230
Checksum:i40EDE237BBB568EE
GO
Isoform 1C (identifier: O43318-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     509-518: PLAPCPNSKE → ARTSCRTGPG
     519-606: Missing.

Show »
Length:518
Mass (Da):56,706
Checksum:iA92C927A8621AF90
GO
Isoform 1D (identifier: O43318-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     404-430: Missing.
     509-518: PLAPCPNSKE → ARTSCRTGPG
     519-606: Missing.

Show »
Length:491
Mass (Da):53,740
Checksum:iB7D8832E286A99C5
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei404 – 43027Missing in isoform 1A and isoform 1D. 4 PublicationsVSP_004886Add
BLAST
Alternative sequencei509 – 51810PLAPCPNSKE → ARTSCRTGPG in isoform 1C and isoform 1D. 2 PublicationsVSP_004887
Alternative sequencei519 – 60688Missing in isoform 1C and isoform 1D. 2 PublicationsVSP_004888Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009357 mRNA. Translation: BAA25026.1.
AB009356 mRNA. Translation: BAA25025.1.
AB009358 mRNA. Translation: BAA25027.2.
AF218074 mRNA. Translation: AAF27652.1.
DQ314875 Genomic DNA. Translation: ABC40734.1.
AK315774 mRNA. Translation: BAG38124.1.
AL121964, AL121837 Genomic DNA. Translation: CAI19609.1.
AL121964, AL121837 Genomic DNA. Translation: CAI19610.1.
AL121964, AL121837 Genomic DNA. Translation: CAI19611.1.
AL121964, AL121837 Genomic DNA. Translation: CAI19612.1.
AL121837, AL121964 Genomic DNA. Translation: CAI23530.1.
AL121837, AL121964 Genomic DNA. Translation: CAI23531.1.
AL121837, AL121964 Genomic DNA. Translation: CAI23532.1.
AL121837, AL121964 Genomic DNA. Translation: CAI23533.1.
CH471051 Genomic DNA. Translation: EAW48525.1.
CH471051 Genomic DNA. Translation: EAW48526.1.
CH471051 Genomic DNA. Translation: EAW48527.1.
CH471051 Genomic DNA. Translation: EAW48529.1.
BC017715 mRNA. Translation: AAH17715.1.
CCDSiCCDS5027.1. [O43318-2]
CCDS5028.1. [O43318-1]
CCDS5029.1. [O43318-3]
CCDS5030.1. [O43318-4]
PIRiJC5955.
JC5956.
RefSeqiNP_003179.1. NM_003188.3. [O43318-2]
NP_663304.1. NM_145331.2. [O43318-1]
NP_663305.1. NM_145332.2. [O43318-3]
NP_663306.1. NM_145333.2. [O43318-4]
UniGeneiHs.594838.

Genome annotation databases

EnsembliENST00000369325; ENSP00000358331; ENSG00000135341. [O43318-3]
ENST00000369327; ENSP00000358333; ENSG00000135341. [O43318-4]
ENST00000369329; ENSP00000358335; ENSG00000135341. [O43318-1]
ENST00000369332; ENSP00000358338; ENSG00000135341. [O43318-2]
GeneIDi6885.
KEGGihsa:6885.
UCSCiuc003pnz.2. human. [O43318-1]
uc003poa.2. human. [O43318-3]
uc003pob.2. human. [O43318-2]
uc003poc.2. human. [O43318-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009357 mRNA. Translation: BAA25026.1 .
AB009356 mRNA. Translation: BAA25025.1 .
AB009358 mRNA. Translation: BAA25027.2 .
AF218074 mRNA. Translation: AAF27652.1 .
DQ314875 Genomic DNA. Translation: ABC40734.1 .
AK315774 mRNA. Translation: BAG38124.1 .
AL121964 , AL121837 Genomic DNA. Translation: CAI19609.1 .
AL121964 , AL121837 Genomic DNA. Translation: CAI19610.1 .
AL121964 , AL121837 Genomic DNA. Translation: CAI19611.1 .
AL121964 , AL121837 Genomic DNA. Translation: CAI19612.1 .
AL121837 , AL121964 Genomic DNA. Translation: CAI23530.1 .
AL121837 , AL121964 Genomic DNA. Translation: CAI23531.1 .
AL121837 , AL121964 Genomic DNA. Translation: CAI23532.1 .
AL121837 , AL121964 Genomic DNA. Translation: CAI23533.1 .
CH471051 Genomic DNA. Translation: EAW48525.1 .
CH471051 Genomic DNA. Translation: EAW48526.1 .
CH471051 Genomic DNA. Translation: EAW48527.1 .
CH471051 Genomic DNA. Translation: EAW48529.1 .
BC017715 mRNA. Translation: AAH17715.1 .
CCDSi CCDS5027.1. [O43318-2 ]
CCDS5028.1. [O43318-1 ]
CCDS5029.1. [O43318-3 ]
CCDS5030.1. [O43318-4 ]
PIRi JC5955.
JC5956.
RefSeqi NP_003179.1. NM_003188.3. [O43318-2 ]
NP_663304.1. NM_145331.2. [O43318-1 ]
NP_663305.1. NM_145332.2. [O43318-3 ]
NP_663306.1. NM_145333.2. [O43318-4 ]
UniGenei Hs.594838.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EVA X-ray 2.00 A 31-412 [» ]
2YIY X-ray 2.49 A 31-303 [» ]
4GS6 X-ray 2.20 A 31-303 [» ]
4L3P X-ray 2.68 A 31-303 [» ]
4L52 X-ray 2.54 A 31-303 [» ]
4L53 X-ray 2.55 A 31-303 [» ]
4O91 X-ray 2.39 A 31-303 [» ]
ProteinModelPortali O43318.
SMRi O43318. Positions 4-305.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112748. 120 interactions.
DIPi DIP-27523N.
IntActi O43318. 45 interactions.
MINTi MINT-88554.
STRINGi 9606.ENSP00000358335.

Chemistry

BindingDBi O43318.
ChEMBLi CHEMBL5776.
GuidetoPHARMACOLOGYi 2082.

PTM databases

PhosphoSitei O43318.

Proteomic databases

MaxQBi O43318.
PaxDbi O43318.
PRIDEi O43318.

Protocols and materials databases

DNASUi 6885.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369325 ; ENSP00000358331 ; ENSG00000135341 . [O43318-3 ]
ENST00000369327 ; ENSP00000358333 ; ENSG00000135341 . [O43318-4 ]
ENST00000369329 ; ENSP00000358335 ; ENSG00000135341 . [O43318-1 ]
ENST00000369332 ; ENSP00000358338 ; ENSG00000135341 . [O43318-2 ]
GeneIDi 6885.
KEGGi hsa:6885.
UCSCi uc003pnz.2. human. [O43318-1 ]
uc003poa.2. human. [O43318-3 ]
uc003pob.2. human. [O43318-2 ]
uc003poc.2. human. [O43318-4 ]

Organism-specific databases

CTDi 6885.
GeneCardsi GC06M091282.
HGNCi HGNC:6859. MAP3K7.
HPAi HPA007633.
MIMi 602614. gene.
neXtProti NX_O43318.
PharmGKBi PA30603.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118807.
HOGENOMi HOG000231735.
HOVERGENi HBG003485.
InParanoidi O43318.
KOi K04427.
OMAi CKAKWKG.
OrthoDBi EOG7RBZ8D.
PhylomeDBi O43318.
TreeFami TF105116.

Enzyme and pathway databases

Reactomei REACT_118656. Activation of NF-kappaB in B cells.
REACT_12555. Downstream TCR signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_172761. Ca2+ pathway.
REACT_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_25351. TRAF6 mediated induction of TAK1 complex.
REACT_25380. IRAK2 mediated activation of TAK1 complex.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinki O43318.

Miscellaneous databases

ChiTaRSi MAP3K7. human.
EvolutionaryTracei O43318.
GeneWikii MAP3K7.
GenomeRNAii 6885.
NextBioi 26899.
PROi O43318.
SOURCEi Search...

Gene expression databases

Bgeei O43318.
CleanExi HS_MAP3K7.
ExpressionAtlasi O43318. baseline and differential.
Genevestigatori O43318.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR017421. MAPKKK7.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF038168. MAPKKK7. 1 hit.
PRINTSi PR00109. TYRKINASE.
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "TGF-beta-activated kinase 1 stimulates NF-kappa B activation by an NF-kappa B-inducing kinase-independent mechanism."
    Sakurai H., Shigemori N., Hasegawa K., Sugita T.
    Biochem. Biophys. Res. Commun. 243:545-549(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 1C).
    Tissue: Lung.
  2. "Alternative splicing and gene structure of the transforming growth factor beta-activated kinase 1."
    Dempsey C.E., Sakurai H., Sugita T., Guesdon F.
    Biochim. Biophys. Acta 1517:46-52(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1D), TISSUE SPECIFICITY.
  3. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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] (ISOFORM 1A).
    Tissue: Trachea.
  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] (ISOFORM 1A).
    Tissue: Uterus.
  8. Cited for: FUNCTION IN PHOSPHORYLATION OF MAP2K3/MKK3 AND MAP2K6/MKK6.
  9. "TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction."
    Shibuya H., Yamaguchi K., Shirakabe K., Tonegawa A., Gotoh Y., Ueno N., Irie K., Nishida E., Matsumoto K.
    Science 272:1179-1182(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAB1/MAP3K7IP1.
  10. "TAK1 mediates the ceramide signaling to stress-activated protein kinase/c-Jun N-terminal kinase."
    Shirakabe K., Yamaguchi K., Shibuya H., Irie K., Matsuda S., Moriguchi T., Gotoh Y., Matsumoto K., Nishida E.
    J. Biol. Chem. 272:8141-8144(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, FUNCTION.
  11. "The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway."
    Ninomiya-Tsuji J., Kishimoto K., Hiyama A., Inoue J., Cao Z., Matsumoto K.
    Nature 398:252-256(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF6 AND TAB1/MAP3K7IP1, FUNCTION.
  12. "Phosphorylation-dependent activation of TAK1 mitogen-activated protein kinase kinase kinase by TAB1."
    Sakurai H., Miyoshi H., Mizukami J., Sugita T.
    FEBS Lett. 474:141-145(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAB1, PHOSPHORYLATION AT THR-184; THR-187 AND SER-192, ACTIVATION.
  13. "TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop."
    Kishimoto K., Matsumoto K., Ninomiya-Tsuji J.
    J. Biol. Chem. 275:7359-7364(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-192, ENZYME REGULATION.
  14. Cited for: DEPHOSPHORYLATION BY PPM1B/PP2CB, INTERACTION WITH PPM1B/PP2CB.
  15. "TAK1 is a ubiquitin-dependent kinase of MKK and IKK."
    Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J.
    Nature 412:346-351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, FUNCTION, ENZYME REGULATION, INTERACTION WITH TAB1/MAP3K7IP2 AND TAB2/MAP3K7IP2, IDENTIFICATION IN THE TRIKA2 COMPLEX.
  16. "Interleukin-1 (IL-1) receptor-associated kinase-dependent IL-1-induced signaling complexes phosphorylate TAK1 and TAB2 at the plasma membrane and activate TAK1 in the cytosol."
    Jiang Z., Ninomiya-Tsuji J., Qian Y., Matsumoto K., Li X.
    Mol. Cell. Biol. 22:7158-7167(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IRAK; TAB1/MAP3K7IP1; TAB2/MAP3K7IP2 AND TRAF6, PHOSPHORYLATION, ENZYME REGULATION, SUBCELLULAR LOCATION.
  17. "Pellino2 activates the mitogen activated protein kinase pathway."
    Jensen L.E., Whitehead A.S.
    FEBS Lett. 545:199-202(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PELI1 AND PELI2.
  18. "Pellino3, a novel member of the Pellino protein family, promotes activation of c-Jun and Elk-1 and may act as a scaffolding protein."
    Jensen L.E., Whitehead A.S.
    J. Immunol. 171:1500-1506(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PELI3.
  19. "Transforming growth factor-beta1 (TGF-beta)-induced apoptosis of prostate cancer cells involves Smad7-dependent activation of p38 by TGF-beta-activated kinase 1 and mitogen-activated protein kinase kinase 3."
    Edlund S., Bu S., Schuster N., Aspenstroem P., Heuchel R., Heldin N.E., ten Dijke P., Heldin C.H., Landstrom M.
    Mol. Biol. Cell 14:529-544(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SMAD7; MAP2K3 AND P38 KINASE, MUTAGENESIS OF LYS-63.
  20. "TAB3, a new binding partner of the protein kinase TAK1."
    Cheung P.C., Nebreda A.R., Cohen P.
    Biochem. J. 378:27-34(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAB3/MAP3K7IP3.
  21. "Disabled-2 (Dab2) mediates transforming growth factor beta (TGFbeta)-stimulated fibronectin synthesis through TGFbeta-activated kinase 1 and activation of the JNK pathway."
    Hocevar B.A., Prunier C., Howe P.H.
    J. Biol. Chem. 280:25920-25927(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2.
  22. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "The Yersinia enterocolitica effector YopP inhibits host cell signalling by inactivating the protein kinase TAK1 in the IL-1 signalling pathway."
    Thiefes A., Wolf A., Doerrie A., Grassl G.A., Matsumoto K., Autenrieth I., Bohn E., Sakurai H., Niedenthal R., Resch K., Kracht M.
    EMBO Rep. 7:838-844(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, PHOSPHORYLATION AT THR-187 BY AUTOCATALYSIS, SUBUNIT, FUNCTION.
  24. "Osmotic stress activates the TAK1-JNK pathway while blocking TAK1-mediated NF-kappaB activation: TAO2 regulates TAK1 pathways."
    Huangfu W.C., Omori E., Akira S., Matsumoto K., Ninomiya-Tsuji J.
    J. Biol. Chem. 281:28802-28810(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH TAOK1 AND TAOK2.
  25. "Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway."
    Kajino T., Ren H., Iemura S., Natsume T., Stefansson B., Brautigan D.L., Matsumoto K., Ninomiya-Tsuji J.
    J. Biol. Chem. 281:39891-39896(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PP2A AND PPP6C, DEPHOSPHORYLATION AT THR-187 BY PP2A AND PPP6C.
  26. "RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation."
    Tian Y., Zhang Y., Zhong B., Wang Y.Y., Diao F.C., Wang R.P., Zhang M., Chen D.Y., Zhai Z.H., Shu H.B.
    J. Biol. Chem. 282:16776-16782(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBCK1.
  27. "Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-dependent kinase Tak1 and prevents abnormal T cell responses."
    Reiley W.W., Jin W., Lee A.J., Wright A., Wu X., Tewalt E.F., Leonard T.O., Norbury C.C., Fitzpatrick L., Zhang M., Sun S.C.
    J. Exp. Med. 204:1475-1485(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH CYLD, DEUBIQUITINATION BY CYLD.
  28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  29. "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-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. "The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner."
    Sorrentino A., Thakur N., Grimsby S., Marcusson A., von Bulow V., Schuster N., Zhang S., Heldin C.H., Landstrom M.
    Nat. Cell Biol. 10:1199-1207(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFBR1.
  31. "Modulation of interleukin-1 transcriptional response by the interaction between VRK2 and the JIP1 scaffold protein."
    Blanco S., Sanz-Garcia M., Santos C.R., Lazo P.A.
    PLoS ONE 3:E1660-E1660(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VRK2.
  32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced NF-kappaB activation pathway."
    Gao D., Wang R., Li B., Yang Y., Zhai Z., Chen D.Y.
    Cell. Mol. Life Sci. 66:2573-2584(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WDR34.
  35. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "Direct activation of protein kinases by unanchored polyubiquitin chains."
    Xia Z.-P., Sun L., Chen X., Pineda G., Jiang X., Adhikari A., Zeng W., Chen Z.J.
    Nature 461:114-119(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAB2, PHOSPHORYLATION AT THR-187.
  37. "Ubiquitin-mediated activation of TAK1 and IKK."
    Adhikari A., Xu M., Chen Z.J.
    Oncogene 26:3214-3226(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ENZYME REGULATION.
  38. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  39. Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
  40. "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-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  41. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  42. Cited for: FUNCTION, INTERACTION WITH TRIM5, PHOSPHORYLATION AT THR-187.
  43. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  44. "Lys48-linked TAK1 polyubiquitination at lysine-72 downregulates TNFalpha-induced NF-kappaB activation via mediating TAK1 degradation."
    Fan Y., Shi Y., Liu S., Mao R., An L., Zhao Y., Zhang H., Zhang F., Xu G., Qin J., Yang J.
    Cell. Signal. 24:1381-1389(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-72.
  45. "Structural basis for the interaction of TAK1 kinase with its activating protein TAB1."
    Brown K., Vial S.C., Dedi N., Long J.M., Dunster N.J., Cheetham G.M.T.
    J. Mol. Biol. 354:1013-1020(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-328 IN COMPLEX WITH TAB1 AND ADENOSINE.

Entry informationi

Entry nameiM3K7_HUMAN
AccessioniPrimary (citable) accession number: O43318
Secondary accession number(s): B2RE27
, E1P523, O43317, O43319, Q5TDN2, Q5TDN3, Q5TDT7, Q9NTR3, Q9NZ70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 1, 1998
Last modified: November 26, 2014
This is version 163 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, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3