TRAIP_HUMAN
ID TRAIP_HUMAN Reviewed; 469 AA.
AC Q9BWF2; B5BU84; B5BUL3; O00467;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=E3 ubiquitin-protein ligase TRAIP {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:17544371, ECO:0000269|PubMed:22945920};
DE AltName: Full=RING finger protein 206 {ECO:0000303|PubMed:26781088};
DE AltName: Full=TRAF-interacting protein {ECO:0000303|PubMed:26595769, ECO:0000303|PubMed:9104814};
GN Name=TRAIP {ECO:0000303|PubMed:26595769, ECO:0000312|HGNC:HGNC:30764};
GN Synonyms=RNF206 {ECO:0000303|PubMed:26781088, ECO:0000312|HGNC:HGNC:30764},
GN TRIP {ECO:0000303|PubMed:9104814};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymocyte;
RX PubMed=9104814; DOI=10.1084/jem.185.7.1275;
RA Lee S.Y., Lee S.Y., Choi Y.;
RT "TRAF-interacting protein (TRIP): a novel component of the tumor necrosis
RT factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits
RT TRAF2-mediated NF-kappaB activation.";
RL J. Exp. Med. 185:1275-1285(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CYLD.
RX PubMed=14676304; DOI=10.1084/jem.20031187;
RA Regamey A., Hohl D., Liu J.W., Roger T., Kogerman P., Toftgaard R.,
RA Huber M.;
RT "The tumor suppressor CYLD interacts with TRIP and regulates negatively
RT nuclear factor kappaB activation by tumor necrosis factor.";
RL J. Exp. Med. 198:1959-1964(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TRAF1; TRAF2; TRAF3; TRAF5
RP AND TRAF6, AND LACK OF INTERACTION WITH CYLD.
RX PubMed=17544371; DOI=10.1016/j.bbrc.2007.05.149;
RA Besse A., Campos A.D., Webster W.K., Darnay B.G.;
RT "TRAF-interacting protein (TRIP) is a RING-dependent ubiquitin ligase.";
RL Biochem. Biophys. Res. Commun. 359:660-664(2007).
RN [6]
RP FUNCTION.
RX PubMed=22945920; DOI=10.1084/jem.20120024;
RA Zhang M., Wang L., Zhao X., Zhao K., Meng H., Zhao W., Gao C.;
RT "TRAF-interacting protein (TRIP) negatively regulates IFN-beta production
RT and antiviral response by promoting proteasomal degradation of TANK-binding
RT kinase 1.";
RL J. Exp. Med. 209:1703-1711(2012).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH POLK AND POLN.
RX PubMed=24553286; DOI=10.1242/dev.101196;
RA Wallace H.A., Merkle J.A., Yu M.C., Berg T.G., Lee E., Bosco G., Lee L.A.;
RT "TRIP/NOPO E3 ubiquitin ligase promotes ubiquitylation of DNA polymerase
RT eta.";
RL Development 141:1332-1341(2014).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-25.
RX PubMed=25335891; DOI=10.1242/jcs.152579;
RA Chapard C., Meraldi P., Gleich T., Bachmann D., Hohl D., Huber M.;
RT "TRAIP is a regulator of the spindle assembly checkpoint.";
RL J. Cell Sci. 127:5149-5156(2014).
RN [9]
RP SUMOYLATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-80; LYS-127;
RP LYS-205; LYS-247 AND LYS-462.
RX PubMed=26820530; DOI=10.1016/j.bbrc.2016.01.141;
RA Park I.S., Han Y.G., Chung H.J., Jung Y.W., Kim Y., Kim H.;
RT "SUMOylation regulates nuclear localization and stability of
RT TRAIP/RNF206.";
RL Biochem. Biophys. Res. Commun. 470:881-887(2016).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UIMC1.
RX PubMed=26781088; DOI=10.1038/ncomms10463;
RA Soo Lee N., Jin Chung H., Kim H.J., Yun Lee S., Ji J.H., Seo Y.,
RA Hun Han S., Choi M., Yun M., Lee S.G., Myung K., Kim Y., Chul Kang H.,
RA Kim H.;
RT "TRAIP/RNF206 is required for recruitment of RAP80 to sites of DNA
RT damage.";
RL Nat. Commun. 7:10463-10463(2016).
RN [11]
RP FUNCTION, INTERACTION WITH PCNA, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-7 AND 460-GLN--LEU-463.
RX PubMed=27462463; DOI=10.1038/celldisc.2016.16;
RA Feng W., Guo Y., Huang J., Deng Y., Zang J., Huen M.S.;
RT "TRAIP regulates replication fork recovery and progression via PCNA.";
RL Cell Discov. 2:16016-16016(2016).
RN [12]
RP INVOLVEMENT IN SCKL9, VARIANT SCKL9 CYS-18, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=26595769; DOI=10.1038/ng.3451;
RA Harley M.E., Murina O., Leitch A., Higgs M.R., Bicknell L.S., Yigit G.,
RA Blackford A.N., Zlatanou A., Mackenzie K.J., Reddy K., Halachev M.,
RA McGlasson S., Reijns M.A., Fluteau A., Martin C.A., Sabbioneda S.,
RA Elcioglu N.H., Altmueller J., Thiele H., Greenhalgh L., Chessa L.,
RA Maghnie M., Salim M., Bober M.B., Nuernberg P., Jackson S.P., Hurles M.E.,
RA Wollnik B., Stewart G.S., Jackson A.P.;
RT "TRAIP promotes DNA damage response during genome replication and is
RT mutated in primordial dwarfism.";
RL Nat. Genet. 48:36-43(2016).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-304, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [14]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 460-GLN--LEU-463.
RX PubMed=30165463; DOI=10.1093/nar/gky775;
RA Chen Y., Li J., Cao F., Lam J., Cheng C.C., Yu C.H., Huen M.S.;
RT "Nucleolar residence of the seckel syndrome protein TRAIP is coupled to
RT ribosomal DNA transcription.";
RL Nucleic Acids Res. 46:10119-10131(2018).
RN [15]
RP FUNCTION.
RX PubMed=31545170; DOI=10.7554/elife.48686;
RA Sonneville R., Bhowmick R., Hoffmann S., Mailand N., Hickson I.D.,
RA Labib K.;
RT "TRAIP drives replisome disassembly and mitotic DNA repair synthesis at
RT sites of incomplete DNA replication.";
RL Elife 8:0-0(2019).
RN [16] {ECO:0007744|PDB:4ZTD}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 459-469 IN COMPLEX WITH PCNA,
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA, MUTAGENESIS OF
RP PHE-466, AND CHARACTERIZATION OF VARIANT SCKL9 CYS-18.
RX PubMed=26711499; DOI=10.1083/jcb.201506071;
RA Hoffmann S., Smedegaard S., Nakamura K., Mortuza G.B., Raschle M.,
RA Ibanez de Opakua A., Oka Y., Feng Y., Blanco F.J., Mann M., Montoya G.,
RA Groth A., Bekker-Jensen S., Mailand N.;
RT "TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability
RT after replication stress.";
RL J. Cell Biol. 212:63-75(2016).
CC -!- FUNCTION: E3 ubiquitin ligase required to protect genome stability in
CC response to replication stress (PubMed:25335891, PubMed:26781088,
CC PubMed:27462463, PubMed:26711499, PubMed:26595769, PubMed:31545170).
CC Acts as a key regulator of interstrand cross-link repair, which takes
CC place when both strands of duplex DNA are covalently tethered together,
CC thereby blocking replication and transcription (By similarity).
CC Controls the choice between the two pathways of replication-coupled
CC interstrand-cross-link repair by mediating ubiquitination of MCM7
CC subunit of the CMG helicase complex (By similarity). Short ubiquitin
CC chains on MCM7 promote recruitment of DNA glycosylase NEIL3 (By
CC similarity). If the interstrand cross-link cannot be cleaved by NEIL3,
CC the ubiquitin chains continue to grow on MCM7, promoting the unloading
CC of the CMG helicase complex by the VCP/p97 ATPase, enabling the Fanconi
CC anemia DNA repair pathway (By similarity). Only catalyzes
CC ubiquitination of MCM7 when forks converge (By similarity). Also
CC involved in the repair of covalent DNA-protein cross-links (DPCs)
CC during DNA synthesis: promotes ubiquitination of DPCs, leading to their
CC degradation by the proteasome (By similarity). Has also been proposed
CC to play a role in promoting translesion synthesis by mediating the
CC assembly of 'Lys-63'-linked poly-ubiquitin chains on the Y-family
CC polymerase POLN in order to facilitate bypass of DNA lesions and
CC preserve genomic integrity (PubMed:24553286). The function in
CC translesion synthesis is however controversial (PubMed:26595769). Acts
CC as a regulator of the spindle assembly checkpoint (PubMed:25335891).
CC Also acts as a negative regulator of innate immune signaling by
CC inhibiting activation of NF-kappa-B mediated by TNF (PubMed:22945920).
CC Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and
CC subsequent IFNB1 production and cellular antiviral response by
CC promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its
CC proteasomal degradation (PubMed:22945920).
CC {ECO:0000250|UniProtKB:Q6NRV0, ECO:0000269|PubMed:22945920,
CC ECO:0000269|PubMed:24553286, ECO:0000269|PubMed:25335891,
CC ECO:0000269|PubMed:26595769, ECO:0000269|PubMed:26711499,
CC ECO:0000269|PubMed:26781088, ECO:0000269|PubMed:27462463,
CC ECO:0000269|PubMed:31545170}.
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:0000269|PubMed:17544371,
CC ECO:0000269|PubMed:22945920};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:17544371, ECO:0000269|PubMed:22945920}.
CC -!- SUBUNIT: Interacts (via PIP-box) with PCNA (PubMed:27462463,
CC PubMed:26711499). Binds TRAF1, TRAF2, TRAF3, TRAF5 and TRAF6 is part of
CC the receptor-TRAF signaling complex (PubMed:17544371). May interact
CC with CYLD; the C-terminus interacts with CYLD, however the interaction
CC was not detected with the full-length protein (PubMed:14676304).
CC Interacts with POLK and POLN (PubMed:24553286). Interacts with UIMC1
CC (PubMed:26781088). {ECO:0000269|PubMed:14676304,
CC ECO:0000269|PubMed:17544371, ECO:0000269|PubMed:24553286,
CC ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:26781088,
CC ECO:0000269|PubMed:27462463}.
CC -!- INTERACTION:
CC Q9BWF2; O15296: ALOX15B; NbExp=3; IntAct=EBI-1756205, EBI-12150557;
CC Q9BWF2; Q96LK0: CEP19; NbExp=3; IntAct=EBI-1756205, EBI-741885;
CC Q9BWF2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-1756205, EBI-1055254;
CC Q9BWF2; Q9BS40: LXN; NbExp=3; IntAct=EBI-1756205, EBI-1044504;
CC Q9BWF2; Q15555: MAPRE2; NbExp=10; IntAct=EBI-1756205, EBI-739717;
CC Q9BWF2; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-1756205, EBI-726739;
CC Q9BWF2; P16333: NCK1; NbExp=3; IntAct=EBI-1756205, EBI-389883;
CC Q9BWF2; O15160: POLR1C; NbExp=3; IntAct=EBI-1756205, EBI-1055079;
CC Q9BWF2; Q9BWF2: TRAIP; NbExp=3; IntAct=EBI-1756205, EBI-1756205;
CC Q9BWF2; P61086: UBE2K; NbExp=3; IntAct=EBI-1756205, EBI-473850;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:24553286, ECO:0000269|PubMed:26595769,
CC ECO:0000269|PubMed:26820530, ECO:0000269|PubMed:30165463}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:14676304, ECO:0000269|PubMed:24553286,
CC ECO:0000269|PubMed:25335891, ECO:0000269|PubMed:27462463,
CC ECO:0000269|PubMed:30165463}. Chromosome {ECO:0000269|PubMed:25335891,
CC ECO:0000269|PubMed:26595769, ECO:0000269|PubMed:26711499,
CC ECO:0000269|PubMed:26781088, ECO:0000269|PubMed:30165463}. Cytoplasm.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:14676304}. Note=In
CC the nucleus, found in close proximity to PCNA, suggesting localization
CC at replication foci (PubMed:26595769). Localizes to DNA damage sites in
CC response to replication stress (PubMed:26781088, PubMed:26595769,
CC PubMed:26711499). {ECO:0000269|PubMed:26595769,
CC ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:26781088}.
CC -!- PTM: Sumoylated; sumoylation is required for nuclear localization
CC (PubMed:26820530). Sumoylation increases protein stability, possibly by
CC preventing ubiquitination (PubMed:26820530).
CC {ECO:0000269|PubMed:26820530}.
CC -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q8VIG6}.
CC -!- DISEASE: Seckel syndrome 9 (SCKL9) [MIM:616777]: A form of Seckel
CC syndrome, a rare autosomal recessive disorder characterized by
CC proportionate dwarfism of prenatal onset associated with low birth
CC weight, growth retardation, severe microcephaly with a bird-headed like
CC appearance, and intellectual disability. {ECO:0000269|PubMed:26595769,
CC ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:30165463}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TRAIP family. {ECO:0000305}.
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DR EMBL; U77845; AAB52993.1; -; mRNA.
DR EMBL; AB451320; BAG70134.1; -; mRNA.
DR EMBL; AB451449; BAG70263.1; -; mRNA.
DR EMBL; BC000310; AAH00310.1; -; mRNA.
DR EMBL; BC019283; AAH19283.1; -; mRNA.
DR CCDS; CCDS2806.1; -.
DR RefSeq; NP_005870.2; NM_005879.2.
DR PDB; 4ZTD; X-ray; 2.20 A; D/E=459-469.
DR PDBsum; 4ZTD; -.
DR AlphaFoldDB; Q9BWF2; -.
DR SMR; Q9BWF2; -.
DR BioGRID; 115581; 73.
DR IntAct; Q9BWF2; 23.
DR STRING; 9606.ENSP00000328203; -.
DR GlyGen; Q9BWF2; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9BWF2; -.
DR PhosphoSitePlus; Q9BWF2; -.
DR BioMuta; TRAIP; -.
DR DMDM; 30580637; -.
DR EPD; Q9BWF2; -.
DR jPOST; Q9BWF2; -.
DR MassIVE; Q9BWF2; -.
DR MaxQB; Q9BWF2; -.
DR PaxDb; Q9BWF2; -.
DR PeptideAtlas; Q9BWF2; -.
DR PRIDE; Q9BWF2; -.
DR ProteomicsDB; 79271; -.
DR Antibodypedia; 30670; 309 antibodies from 32 providers.
DR DNASU; 10293; -.
DR Ensembl; ENST00000331456.7; ENSP00000328203.2; ENSG00000183763.9.
DR GeneID; 10293; -.
DR KEGG; hsa:10293; -.
DR MANE-Select; ENST00000331456.7; ENSP00000328203.2; NM_005879.3; NP_005870.2.
DR UCSC; uc003cxs.2; human.
DR CTD; 10293; -.
DR DisGeNET; 10293; -.
DR GeneCards; TRAIP; -.
DR HGNC; HGNC:30764; TRAIP.
DR HPA; ENSG00000183763; Low tissue specificity.
DR MalaCards; TRAIP; -.
DR MIM; 605958; gene.
DR MIM; 616777; phenotype.
DR neXtProt; NX_Q9BWF2; -.
DR OpenTargets; ENSG00000183763; -.
DR Orphanet; 808; Seckel syndrome.
DR PharmGKB; PA142670705; -.
DR VEuPathDB; HostDB:ENSG00000183763; -.
DR eggNOG; KOG0827; Eukaryota.
DR GeneTree; ENSGT00390000007696; -.
DR InParanoid; Q9BWF2; -.
DR OMA; VMIRPLP; -.
DR OrthoDB; 761263at2759; -.
DR PhylomeDB; Q9BWF2; -.
DR TreeFam; TF317309; -.
DR PathwayCommons; Q9BWF2; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9BWF2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 10293; 559 hits in 1121 CRISPR screens.
DR ChiTaRS; TRAIP; human.
DR GeneWiki; TRAF_interacting_protein; -.
DR GenomeRNAi; 10293; -.
DR Pharos; Q9BWF2; Tbio.
DR PRO; PR:Q9BWF2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BWF2; protein.
DR Bgee; ENSG00000183763; Expressed in ventricular zone and 94 other tissues.
DR ExpressionAtlas; Q9BWF2; baseline and differential.
DR Genevisible; Q9BWF2; HS.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IEA:Ensembl.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:CACAO.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; ISS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Coiled coil; Cytoplasm; Disease variant;
KW DNA damage; DNA repair; Dwarfism; Intellectual disability; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..469
FT /note="E3 ubiquitin-protein ligase TRAIP"
FT /id="PRO_0000056191"
FT ZN_FING 7..50
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 211..469
FT /note="Interaction with CYLD"
FT /evidence="ECO:0000269|PubMed:14676304"
FT COILED 70..177
FT /evidence="ECO:0000255"
FT COILED 201..280
FT /evidence="ECO:0000255"
FT MOTIF 460..469
FT /note="PIP-box"
FT /evidence="ECO:0000269|PubMed:26711499"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 18
FT /note="R -> C (in SCKL9; abolished localization to the
FT nucleolus; dbSNP:rs864622784)"
FT /evidence="ECO:0000269|PubMed:26595769,
FT ECO:0000269|PubMed:26711499"
FT /id="VAR_076530"
FT MUTAGEN 7
FT /note="C->A: Abolished accumulation in nucleolus."
FT /evidence="ECO:0000269|PubMed:27462463"
FT MUTAGEN 25
FT /note="C->A: Abolished ability to regulate nuclear envelope
FT breakdown to anaphase."
FT /evidence="ECO:0000269|PubMed:25335891"
FT MUTAGEN 80
FT /note="K->A: Abolished sumoylation and localization to the
FT nucleus; when associated with A-127, A-205, A-247 and A-
FT 462."
FT /evidence="ECO:0000269|PubMed:26820530"
FT MUTAGEN 127
FT /note="K->A: Abolished sumoylation and localization to the
FT nucleus; when associated with A-80, A-205, A-247 and A-
FT 462."
FT /evidence="ECO:0000269|PubMed:26820530"
FT MUTAGEN 205
FT /note="K->A: Abolished sumoylation and localization to the
FT nucleus; when associated with A-80, A-127, A-247 and A-
FT 462."
FT /evidence="ECO:0000269|PubMed:26820530"
FT MUTAGEN 247
FT /note="K->A: Abolished sumoylation and localization to the
FT nucleus; when associated with A-80, A-127, A-205 and A-
FT 462."
FT /evidence="ECO:0000269|PubMed:26820530"
FT MUTAGEN 460..463
FT /note="QAKL->AAKA: Abolished interaction with PCNA and
FT localization to DNA damage sites."
FT /evidence="ECO:0000269|PubMed:27462463,
FT ECO:0000269|PubMed:30165463"
FT MUTAGEN 462
FT /note="K->A: Abolished sumoylation and localization to the
FT nucleus; when associated with A-80, A-127, A-205 and A-
FT 247."
FT /evidence="ECO:0000269|PubMed:26820530"
FT MUTAGEN 466
FT /note="F->A: Abolished interaction with PCNA."
FT /evidence="ECO:0000269|PubMed:26711499"
FT CONFLICT 37
FT /note="W -> S (in Ref. 1; AAB52993)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="A -> R (in Ref. 1; AAB52993)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="R -> G (in Ref. 1; AAB52993)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="R -> L (in Ref. 1; AAB52993)"
FT /evidence="ECO:0000305"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:4ZTD"
SQ SEQUENCE 469 AA; 53294 MW; B9EF3808FBC5985B CRC64;
MPIRALCTIC SDFFDHSRDV AAIHCGHTFH LQCLIQWFET APSRTCPQCR IQVGKRTIIN
KLFFDLAQEE ENVLDAEFLK NELDNVRAQL SQKDKEKRDS QVIIDTLRDT LEERNATVVS
LQQALGKAEM LCSTLKKQMK YLEQQQDETK QAQEEARRLR SKMKTMEQIE LLLQSQRPEV
EEMIRDMGVG QSAVEQLAVY CVSLKKEYEN LKEARKASGE VADKLRKDLF SSRSKLQTVY
SELDQAKLEL KSAQKDLQSA DKEIMSLKKK LTMLQETLNL PPVASETVDR LVLESPAPVE
VNLKLRRPSF RDDIDLNATF DVDTPPARPS SSQHGYYEKL CLEKSHSPIQ DVPKKICKGP
RKESQLSLGG QSCAGEPDEE LVGAFPIFVR NAILGQKQPK RPRSESSCSK DVVRTGFDGL
GGRTKFIQPT DTVMIRPLPV KPKTKVKQRV RVKTVPSLFQ AKLDTFLWS
