TRAF7_MOUSE
ID TRAF7_MOUSE Reviewed; 594 AA.
AC Q922B6; Q99JV3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=E3 ubiquitin-protein ligase TRAF7;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase TRAF7 {ECO:0000305};
DE AltName: Full=TNF receptor-associated factor 7;
GN Name=Traf7 {ECO:0000312|EMBL:AAH08598.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAH08598.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH05649.1}; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-15, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 ubiquitin ligase capable of auto-ubiquitination, following
CC phosphorylation by MAP3K3. Potentiates MEKK3-mediated activation of the
CC NF-kappa-B, JUN/AP1 and DDIT3 transcriptional regulators. Induces
CC apoptosis when overexpressed. Plays a role in the phosphorylation of
CC MAPK1 and/or MAPK3, probably via its interaction with MAP3K3.
CC {ECO:0000250|UniProtKB:Q6Q0C0}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. Interacts with MAP3K3 and promotes the kinase
CC activity of this enzyme. {ECO:0000250|UniProtKB:Q6Q0C0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q6Q0C0}. Note=Colocalizes with MAP3K3 to
CC vesicle-like structures throughout the cytoplasm.
CC {ECO:0000250|UniProtKB:Q6Q0C0}.
CC -!- PTM: Phosphorylated by MAP3K3. {ECO:0000250|UniProtKB:Q6Q0C0}.
CC -!- PTM: Ubiquitinates itself upon phosphorylation.
CC {ECO:0000250|UniProtKB:Q6Q0C0}.
CC -!- SIMILARITY: Belongs to the WD repeat TRAF7 family. {ECO:0000305}.
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DR EMBL; BC005649; AAH05649.1; -; mRNA.
DR EMBL; BC008598; AAH08598.1; -; mRNA.
DR AlphaFoldDB; Q922B6; -.
DR SMR; Q922B6; -.
DR STRING; 10090.ENSMUSP00000135267; -.
DR iPTMnet; Q922B6; -.
DR EPD; Q922B6; -.
DR MaxQB; Q922B6; -.
DR PaxDb; Q922B6; -.
DR PRIDE; Q922B6; -.
DR ProteomicsDB; 258963; -.
DR UCSC; uc008awr.2; mouse.
DR MGI; MGI:3042141; Traf7.
DR eggNOG; KOG0274; Eukaryota.
DR eggNOG; KOG0297; Eukaryota.
DR InParanoid; Q922B6; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR ChiTaRS; Traf7; mouse.
DR PRO; PR:Q922B6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q922B6; protein.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0071354; P:cellular response to interleukin-6; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IDA:MGI.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR001293; Znf_TRAF.
DR Pfam; PF00400; WD40; 4.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00184; RING; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50145; ZF_TRAF; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasmic vesicle; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; WD repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..594
FT /note="E3 ubiquitin-protein ligase TRAF7"
FT /id="PRO_0000051297"
FT REPEAT 318..357
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 361..398
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 401..437
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 439..478
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 481..518
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 521..562
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 565..593
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT ZN_FING 55..89
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 146..216
FT /note="TRAF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 594 AA; 66487 MW; 18009319608AD0B2 CRC64;
MPPINTPRRS DSAISVRSLH SESSMSLRST FSLPEEEEEP EPLVFAEQPS VKLCCQLCCS
VFKDPVITTC GHTFCRRCAL KSEKCPVDNA KLTVVVNNIA VAEQIGELFI HCRHGCHAAG
TGKPGVFEVD PRGCPFTIKL SARKDHESSC DYRPVRCPNN PSCPPLLKMN LEAHLKECEH
IKCPHSKYGC TFIGNQDTYE THLETCRFEG LKEFLQQTDD RFHEMHVALA QKDQEIAFLR
SMLGKLSEKI DQLEKSLELK FDVLDENQSK LSEDLMEFRR DASMLNDELS HINARLNMGI
LGSYDPQQIF KCKGTFVGHQ GPVWCLCVYS MGDLLFSGSS DKTIKVWDTC TTYKCQKTLE
GHDGIVLALC IQGCKLYSGS ADCTIIVWDI QNLQKVNTIR AHDNPVCTLV SSHNMLFSGS
LKAIKVWDIV GTELKLKKEL TGLNHWVRAL VAAQSYLYSG SYQTIKIWDI RTLDCIHVLQ
TSGGSVYSIA VTNHHIVCGT YENLIHVWDI ESKEQVRTLT GHVGTVYALA VISTPDQTKV
FSASYDRSLR VWSMDNMICT QTLLRHQGSV TALAVSRGRL FSGAVDSTVK VWTC
