The domain within your query sequence starts at position 49 and ends at position 619; the E-value for the MIP-T3 domain shown below is 7e-207.

MKGLYTDAEMKSENVKDKDAKISFLQKAIDVVMMVSGEPLAAKPARIVAGHEPERTNELL
QLIGKCCLSKLSSDEAVKRVLAGDKGDSRGRAQRTSKAQEPNNKSGKEEESRIHKEDKRS
SEAKERSASAEHKQKEELKEDSKPREKERDKEKAKEADRDRHRDPDRDRNRDGEREKARA
RAKDRDRNNRDRDREAERDRERDRRSEGGKEKERVKDRDRDRDKGRDRERRKSKNGEHTR
DPDREKSRDADKPEKKSSSSGEISRKLSDGSFKDVKAEMEADISVGASRSSTLKPSKRRS
KHSLEGDSPSDAEVEAGPAGQDKPEVMENAEVPSELPSSLRRIPRPGSARPAPPRVKRQE
STETLVVDRSGSGKTVSSVIIDSQNSDNEDDEQFVVEAAPQLSEIADIDMVPSGELEDEE
KHGGLVKKILETKKDYEKLQQSLKPGEKERSLIFESAWKKEKDIVSKEIEKLRVSIQTLC
KSALPLGKIMDYIQEDVDAMQNELQLWHSENRQHAEALSQEQSITDSAVEPLKAELSELE
QQIRDQQDKICAVKANILKNEEKIQKMVHSI

MIP-T3

MIP-T3
PFAM accession number:PF10243
Interpro abstract (IPR040468):

TRAF3-interacting protein 1 (TRAF3IP1)recruits TRAF3 (tumour necrosis factor receptor-associated factor 3) and DISC1 (Disrupted-In-Schizophrenia 1) to the microtubules and is conserved from worms to humans [ (PUBMED:12812986) ]. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved [ (PUBMED:10791955) ]. In humans, it plays an inhibitory role on IL13 signaling by binding to IL13RA1. It is involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding [ (PUBMED:10791955) (PUBMED:12935900) ].

This entry represents the N-terminal domain of TRAF3-interacting protein 1.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry MIP-T3