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TRAF6_XENTR
ID   TRAF6_XENTR             Reviewed;         558 AA.
AC   Q28DL4; Q641J5;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=TNF receptor-associated factor 6;
DE            EC=2.3.2.27;
DE   AltName: Full=E3 ubiquitin-protein ligase TRAF6;
DE   AltName: Full=RING-type E3 ubiquitin transferase TRAF6 {ECO:0000305};
GN   Name=traf6; ORFNames=TNeu045k15.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin ligase that, together with UBE2N and UBE2V1,
CC       mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains
CC       conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also
CC       mediates ubiquitination of free/unanchored polyubiquitin chain that
CC       leads to MAP3K7 activation. {ECO:0000250|UniProtKB:Q9Y4K3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9Y4K3};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9Y4K3}.
CC   -!- SUBUNIT: Homotrimer. Homooligomer. {ECO:0000250|UniProtKB:Q9Y4K3}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4K3}.
CC       Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9Y4K3}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9Y4K3}. Lipid droplet
CC       {ECO:0000250|UniProtKB:P70196}.
CC   -!- DOMAIN: The coiled coil domain mediates homo- and hetero-
CC       oligomerization. {ECO:0000250}.
CC   -!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TNF receptor-associated factor family. A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR855449; CAJ82470.1; -; mRNA.
DR   EMBL; BC082342; AAH82342.1; -; mRNA.
DR   RefSeq; NP_001008162.2; NM_001008161.2.
DR   AlphaFoldDB; Q28DL4; -.
DR   SMR; Q28DL4; -.
DR   PaxDb; Q28DL4; -.
DR   DNASU; 493524; -.
DR   GeneID; 493524; -.
DR   KEGG; xtr:493524; -.
DR   CTD; 7189; -.
DR   Xenbase; XB-GENE-480628; traf6.
DR   eggNOG; KOG0297; Eukaryota.
DR   InParanoid; Q28DL4; -.
DR   OrthoDB; 918518at2759; -.
DR   Reactome; R-XTR-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
DR   Reactome; R-XTR-193692; Regulated proteolysis of p75NTR.
DR   Reactome; R-XTR-202424; Downstream TCR signaling.
DR   Reactome; R-XTR-209543; p75NTR recruits signalling complexes.
DR   Reactome; R-XTR-209560; NF-kB is activated and signals survival.
DR   Reactome; R-XTR-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-XTR-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR   Reactome; R-XTR-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-XTR-5689880; Ub-specific processing proteases.
DR   Reactome; R-XTR-5689896; Ovarian tumor domain proteases.
DR   Reactome; R-XTR-9020702; Interleukin-1 signaling.
DR   Reactome; R-XTR-937042; IRAK2 mediated activation of TAK1 complex.
DR   Reactome; R-XTR-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR   Reactome; R-XTR-9645460; Alpha-protein kinase 1 signaling pathway.
DR   Reactome; R-XTR-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
DR   Reactome; R-XTR-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR   Reactome; R-XTR-975871; MyD88 cascade initiated on plasma membrane.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000007549; Expressed in 4-cell stage embryo and 12 other tissues.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR   GO; GO:0032813; F:tumor necrosis factor receptor superfamily binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IBA:GO_Central.
DR   CDD; cd03776; MATH_TRAF6; 1.
DR   Gene3D; 2.60.210.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 3.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR043211; TNF_rcpt-assoc_TRAF.
DR   InterPro; IPR012227; TNF_rcpt-assoc_TRAF_met.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR027139; TRAF6.
DR   InterPro; IPR037309; TRAF6_MATH.
DR   InterPro; IPR041310; TRAF6_Z2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   InterPro; IPR001293; Znf_TRAF.
DR   PANTHER; PTHR10131; PTHR10131; 2.
DR   PANTHER; PTHR10131:SF131; PTHR10131:SF131; 2.
DR   Pfam; PF18048; TRAF6_Z2; 1.
DR   Pfam; PF02176; zf-TRAF; 1.
DR   PIRSF; PIRSF015614; TRAF; 1.
DR   SMART; SM00061; MATH; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50144; MATH; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50145; ZF_TRAF; 2.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Lipid droplet; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..558
FT                   /note="TNF receptor-associated factor 6"
FT                   /id="PRO_0000391615"
FT   DOMAIN          386..535
FT                   /note="MATH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT   ZN_FING         72..111
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         148..204
FT                   /note="TRAF-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT   ZN_FING         205..261
FT                   /note="TRAF-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT   COILED          321..384
FT                   /evidence="ECO:0000255"
FT   CONFLICT        19
FT                   /note="C -> S (in Ref. 2; AAH82342)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="V -> L (in Ref. 2; AAH82342)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316
FT                   /note="T -> S (in Ref. 2; AAH82342)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   558 AA;  63411 MW;  C98FD7BD5624C5DD CRC64;
     MSILNCRPSF DGVDTDDACC GAMASACCVN TKEDGESPSA GSPSGTPQSL VLEDVQGYDV
     EFDPPLESKY ECPICLMALR EAVQTPCGHR FCKACILKSI RDAGHKCPVD NESLMENQLF
     PDNFAKREIL SLRVKCPSQG CTETMELRHL ERHLVRCDFA GVECSQCQSS FPKYSLQKHK
     FEECPRRQIF CENCAVAMAL EDKLNHDQTC PLAYVTCEYC QTNLIREQMP AHYSMDCTMA
     PIPCMYYEFG CTEKMQRNDL ARHLQEFTQA HMRMMAQTLR SFSSSVTPTS HMPDISFCDP
     SQFEPAPPSV ATVHSTHTPS QNDCTQETRN LRETIEQLEG RLVRQDHQIR ELIAKMETQC
     TYVNELKHTI RSLDNRLGEM ESQQCSGIFI WRINNFNSLL KNQEEERPVV IHSQGFYTGK
     PGYKLCLRLH LQLPSAQRCA NYISLFVHTM QGEYDSLLPW PLQGTIRLSI LDQSEGVAMQ
     DQEEVMDTKP ELLAFQRPTV ARNPKGFGYV TFMHLQALKQ RQYVKNDTLL VRCSVTTHLD
     LISPRREGFQ PRSGDGAL
 
 
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