Tab1
entrez
66513
canonical
uniprot
Q8CF89
canonical
ensembl
ENSMUSG00000022414
resolver
ensp
ENSMUSP00000023050
resolver
enst
ENSMUST00000023050
resolver
genesymbol
Tab1
resolver
genesymbol_syn
Map3k7ip1
resolver
uniprot
Q7TQJ5
resolver
uniprot
Q80V65
resolver
uniprot
Q8R0D1
resolver
uniprot_entry
TAB1_MOUSE
resolver
uniprot_sec
Q7TQJ5
resolver
uniprot_sec
Q80V65
resolver
uniprot_sec
Q8R0D1
resolver
amino_acid_sequence
MAAQRRSLLQSEQQPSWTDDLPLCHLSGVGSASNRSYSADGKGTESHPPEDNWLKFRSENNCFLYGVFNGYDGNRVTNFVAQRLSAELLLGQLNTEHTEADVRRVLLQAFDVVERSFLESIDDALAEKASLQSQLPEGVPQHQLPPQYQKILERLKALEREISGGAMAVVAVLLNSKLYVANVGTNRALLCKSTVDGLQVTQLNMDHTTENEDELFRLSQLGLDAGKIKQMGVICGQESTRRIGDYKVKYGYTDIDLLSAAKSKPIIAEPEIHGAQPLDGVTGFLVLMSEGLYKALEAAHGPGQANQEIAAMIDTEFAKQTSLDAVAQAVVDRVKRIHSDTFASGGERAKFCPRHEDMTLLVRNFGYPLGEMSQPTPTPAPGGRVYPVSVPYSSAQSTSKTSVTLSLVMPSQGQMVNGSHSASTLDEATPTLTNQSPTLTLQSTNTHTQSSSSSSDGGLFRSRPAHSLPPGEDGRVEPYVDFAEFYRLWSVDHGEQSVMTAP
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:12464436, PubMed:28073917). Mechanistically, associates with the catalytic domain of MAP3K7/TAK1 to trigger MAP3K7/TAK1 autophosphorylation leading to its full activation (PubMed:37832545). Similarly, associates with MAPK14 and triggers its autophosphorylation and subsequent activation (PubMed:24037507). In turn, MAPK14 phosphorylates TAB1 and inhibits MAP3K7/TAK1 activation in a feedback control mechanism. Also plays a role in recruiting MAPK14 to the TAK1 complex for the phosphorylation of the TAB2 and TAB3 regulatory subunits (By similarity). {ECO:0000250|UniProtKB:Q15750, ECO:0000269|PubMed:12464436, ECO:0000269|PubMed:24037507, ECO:0000269|PubMed:28073917, ECO:0000269|PubMed:37832545}.
uniprot
proteins
mass_dalton
54616
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at all three sites Ser-421, Thr-429 and Ser-436 by MAPK14 when cells were exposed to cellular stresses, or stimulated with TNF, IL1 or LPS. These phosphorylations inhibit TAK1 activation by a feedback control mechanism. Dephosphorylated by DUSP14 at Ser-436, leading to TAB1-MAP3K7/TAK1 complex inactivation in T-cells. {ECO:0000250|UniProtKB:Q15750}.; 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. Ubiquitinated by ITCH with 'Lys-48'-linked polyubiquitin; leading to proteasomal degradation (By similarity). Ubiquitinated by RNF114 during maternal-to-zygotic transition; leading to degradation (PubMed:28073917). {ECO:0000250|UniProtKB:Q15750, ECO:0000269|PubMed:28073917}.; PTM: O-GlcNAcylated at Ser-393 is required for full MAP3K7/TAK1 activation upon stimulation with IL-1 or osmotic stress. {ECO:0000250|UniProtKB:Q15750}.
uniprot
proteins
pubmed
12464436
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24037507
uniprot
proteins
pubmed
28073917
uniprot
proteins
pubmed
37832545
uniprot
proteins
sequence_length
502
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