TAB1
entrez
10454
canonical
uniprot
Q15750
canonical
ensembl
ENSG00000100324
resolver
ensp
ENSP00000216160
resolver
ensp
ENSP00000333049
resolver
genesymbol
MAP3K7IP1
resolver
genesymbol
TAB1
resolver
genesymbol_syn
MAP3K7IP1
resolver
hgnc
HGNC:18157
resolver
uniprot
A8K6K3
resolver
uniprot
Q2PP09
resolver
uniprot
Q8IZW2
resolver
uniprot_entry
A8K6K3_HUMAN
resolver
uniprot_entry
TAB1_HUMAN
resolver
uniprot_sec
Q2PP09
resolver
uniprot_sec
Q8IZW2
resolver
amino_acid_sequence
MAAQRRSLLQSEQQPSWTDDLPLCHLSGVGSASNRSYSADGKGTESHPPEDSWLKFRSENNCFLYGVFNGYDGNRVTNFVAQRLSAELLLGQLNAEHAEADVRRVLLQAFDVVERSFLESIDDALAEKASLQSQLPEGVPQHQLPPQYQKILERLKTLEREISGGAMAVVAVLLNNKLYVANVGTNRALLCKSTVDGLQVTQLNVDHTTENEDELFRLSQLGLDAGKIKQVGIICGQESTRRIGDYKVKYGYTDIDLLSAAKSKPIIAEPEIHGAQPLDGVTGFLVLMSEGLYKALEAAHGPGQANQEIAAMIDTEFAKQTSLDAVAQAVVDRVKRIHSDTFASGGERARFCPRHEDMTLLVRNFGYPLGEMSQPTPSPAPAAGGRVYPVSVPYSSAQSTSKTSVTLSLVMPSQGQMVNGAHSASTLDEATPTLTNQSPTLTLQSTNTHTQSSSSSSDGGLFRSRPAHSLPPGEDGRVEPYVDFAEFYRLWSVDHGEQSVVTAP
uniprot
proteins
function
FUNCTION: Key adapter protein that plays an essential role in JNK and NF-kappa-B activation and proinflammatory cytokines production in response to stimulation with TLRs and cytokines (PubMed:22307082, PubMed:24403530). Mechanistically, associates with the catalytic domain of MAP3K7/TAK1 to trigger MAP3K7/TAK1 autophosphorylation leading to its full activation (PubMed:10838074, PubMed:25260751, PubMed:37832545). Similarly, associates with MAPK14 and triggers its autophosphorylation and subsequent activation (PubMed:11847341, PubMed:29229647). In turn, MAPK14 phosphorylates TAB1 and inhibits MAP3K7/TAK1 activation in a feedback control mechanism (PubMed:14592977). Also plays a role in recruiting MAPK14 to the TAK1 complex for the phosphorylation of the TAB2 and TAB3 regulatory subunits (PubMed:18021073). {ECO:0000269|PubMed:10838074, ECO:0000269|PubMed:11847341, ECO:0000269|PubMed:14592977, ECO:0000269|PubMed:18021073, ECO:0000269|PubMed:22307082, ECO:0000269|PubMed:24403530, ECO:0000269|PubMed:25260751, ECO:0000269|PubMed:29229647, ECO:0000269|PubMed:37832545}.
uniprot
proteins
mass_dalton
54644
uniprot
proteins
mutagenesis
MUTAGEN 148; /note="Y->A: Complete loss of ITCH-mediated ubiquitination."; /evidence="ECO:0000269|PubMed:29229647"; MUTAGEN 213; /note="D->A: Loss of interaction with XIAP."; /evidence="ECO:0000269|PubMed:17560374"; MUTAGEN 216; /note="F->A: Loss of interaction with XIAP."; /evidence="ECO:0000269|PubMed:17560374"; MUTAGEN 395; /note="S->A: About 50% loss of IL-6 secretion after IL-1alpha stimulation."; /evidence="ECO:0000269|PubMed:22307082"; MUTAGEN 438; /note="S->A: Loss of phosphorylation site."; /evidence="ECO:0000269|PubMed:16845370"; MUTAGEN 484; /note="F->A: Abolishes interaction with MAP3K7."; /evidence="ECO:0000269|PubMed:11323434
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at all three sites Ser-423, Thr-431 and Ser-438 by MAPK14 when cells were exposed to cellular stresses, or stimulated with TNF, IL1 or LPS (PubMed:14592977). These phosphorylations inhibit TAK1 activation by a feedback control mechanism (PubMed:14592977). Dephosphorylated by DUSP14 at Ser-438, leading to TAB1-MAP3K7/TAK1 complex inactivation in T-cells (PubMed:24403530). {ECO:0000269|PubMed:14592977, ECO:0000269|PubMed:24403530}.; PTM: Ubiquitinated by MAP3K1 with 'Lys-63'-linked polyubiquitin; leading to activation of TAK1 and of JNK and p38 MAP kinases following EGF and TGF-beta stimulation (PubMed:25260751). Ubiquitinated by ITCH with 'Lys-48'-linked polyubiquitin; leading to proteasomal degradation (PubMed:25714464). Ubiquitinated by RNF114 during maternal-to-zygotic transition; leading to degradation (By similarity). {ECO:0000250|UniProtKB:Q8CF89, ECO:0000269|PubMed:25260751, ECO:0000269|PubMed:25714464}.; PTM: (Microbial infection) Deubiquitinated by Y.enterocolitica YopP. {ECO:0000269|PubMed:16845370}.; PTM: O-GlcNAcylated at Ser-395 by OGT is required for full MAP3K7/TAK1 activation upon stimulation with IL-1 or osmotic stress (PubMed:22307082). Deglycosylated at Ser-395 by OGA (PubMed:28939839). {ECO:0000269|PubMed:22307082, ECO:0000269|PubMed:28939839}.
uniprot
proteins
pubmed
10094049
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
10838074
uniprot
proteins
pubmed
11323434
uniprot
proteins
pubmed
11460167
uniprot
proteins
pubmed
11847341
uniprot
proteins
pubmed
11865055
uniprot
proteins
pubmed
12429732
uniprot
proteins
pubmed
14592977
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16845370
uniprot
proteins
pubmed
16879102
uniprot
proteins
pubmed
17560374
uniprot
proteins
pubmed
18021073
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22307082
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24403530
uniprot
proteins
pubmed
25260751
uniprot
proteins
pubmed
25714464
uniprot
proteins
pubmed
28939839
uniprot
proteins
pubmed
29229647
uniprot
proteins
pubmed
37832545
uniprot
proteins
pubmed
8638164
uniprot
proteins
sequence_length
504
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:37832545}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:37832545}; Peripheral membrane protein {ECO:0000269|PubMed:37832545}; Cytoplasmic side {ECO:0000269|PubMed:37832545}. Note=Recruited to the endoplasmic reticulum following interaction with STING1. {ECO:0000269|PubMed:37832545}.
uniprot
proteins