TRIPC_XENTR
ID TRIPC_XENTR Reviewed; 2056 AA.
AC B4F6W9; B2GUA6; F7CNG9; F7D1U0;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=E3 ubiquitin-protein ligase TRIP12;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase TRIP12;
DE AltName: Full=Thyroid receptor-interacting protein 12;
DE Short=TR-interacting protein 12;
DE Short=TRIP-12;
GN Name=trip12;
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 GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1151 (ISOFORM 2).
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion
CC degradation (UFD) pathway and regulation of DNA repair. Part of the
CC ubiquitin fusion degradation (UFD) pathway, a process that mediates
CC ubiquitination of protein at their N-terminus, regardless of the
CC presence of lysine residues in target proteins. Acts as a key regulator
CC of DNA damage response by acting as a suppressor of RNF168, an E3
CC ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked
CC histone H2A and H2AX at DNA damage sites, thereby acting as a guard
CC against excessive spreading of ubiquitinated chromatin at damaged
CC chromosomes. {ECO:0000250|UniProtKB:Q14669}.
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=2.3.2.26; Evidence={ECO:0000250|UniProtKB:Q14669};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q14669}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q14669}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B4F6W9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B4F6W9-2; Sequence=VSP_044333;
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI66201.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AAMC01022090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01022091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01022092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01022093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01022094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01022095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01022096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC168042; AAI68042.1; -; mRNA.
DR EMBL; BC166201; AAI66201.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001136384.1; NM_001142912.1. [B4F6W9-1]
DR RefSeq; XP_012825572.1; XM_012970118.2. [B4F6W9-1]
DR RefSeq; XP_012825576.1; XM_012970122.2. [B4F6W9-2]
DR AlphaFoldDB; B4F6W9; -.
DR SMR; B4F6W9; -.
DR STRING; 8364.ENSXETP00000063204; -.
DR PaxDb; B4F6W9; -.
DR GeneID; 100158539; -.
DR KEGG; xtr:100158539; -.
DR CTD; 9320; -.
DR Xenbase; XB-GENE-6071044; trip12.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR InParanoid; B4F6W9; -.
DR OrthoDB; 34110at2759; -.
DR Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000014757; Expressed in blastula and 14 other tissues.
DR ExpressionAtlas; B4F6W9; baseline.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:2000780; P:negative regulation of double-strand break repair; ISS:UniProtKB.
DR GO; GO:1901315; P:negative regulation of histone H2A K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:2000779; P:regulation of double-strand break repair; IBA:GO_Central.
DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR45670; PTHR45670; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF117839; SSF117839; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50918; WWE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..2056
FT /note="E3 ubiquitin-protein ligase TRIP12"
FT /id="PRO_0000419692"
FT DOMAIN 791..905
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 1949..2056
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 1..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1634
FT /note="K-box"
FT /evidence="ECO:0000250"
FT REGION 1632..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2023
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT VAR_SEQ 33..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_044333"
SQ SEQUENCE 2056 AA; 227673 MW; 7FE6E01AE1F48D57 CRC64;
MSSRPNNNPG GSLRRSQRNT AGAQPQEDTA GGRSNLEQAE NKTHSLPESR KSHFKTPKVQ
SNTTSGPSKG HSSKRGCSSS NLLPNPEDTE RINTTDTQRP KKDHVRGVKR SASPDHSRTN
SPSSAKKPKA LQHPEPSSGP RRPNNKPKKR QGSQEQPFPS ASLPSTSKAH SRKGGSQGTS
PLPKRKRTEL SPCVKSSSAA VISTGAEDRP PKLSKLASKS ATSAKAGCSN ITDSSSSAST
SSSSSAVASV SAAPPGARVK QGKDQNKARR SRSASSPSPR RSSREKEQTK TSSSSKFDWA
ARFSPKVSLP KTKLSLPGSS KTETSKPGPS GLQAKLANLR KSTKKRSESP PAELPSLRRS
TRQKTTGSCA STSRRGSGLG KRAAAEARRQ EKMADPDNQE GANSSAARTD ETAQGAAASS
SVAGAVGMTT SGESESDDSE MGRLQALLEA RGLPPHLFGP LGPRMSQLFH RTIGSGASSK
AQQLLQGLQA TDESQQLQAV IEMCQLLVMG NEETLGGFPV KSVVPALITL LQMEHNFDIM
NHACRALTYM MEALPRSSAV VVDAIPVFLE KLQVIQCIDV AEQALTALEM LSRRHSKAIL
QAGGLADCLL YLEFFSINAQ RNALAIAANC CQSISPDEFH FVADSLPLLT QRLTHQDKKS
VESTCLCFAR LVDNFQHEEN LLQQVASRDL LTNIQQLLVV TPPILSSGMF IMVVRMFSLM
CSNCPTLAVQ LMKQNIAETL HFLLCGASNG SCLEQIDLVP RSPQELYELT SLICELMPCL
PKEGIFAVDT MLKKGNAQNT DGAIWQWRDD RGLWHPYSRI DSRIIEAAHQ VGEDEISLST
LGRVYTIDFN SMQQINEDTG TARAIQRKPN PVANANTTGH SELKRDDARA QLMKEDPELA
KSFIKTLFGV LYEVYSSSAG PAVRHKCLRA ILRIIYFADA ELLKDVLKNH AVSSHIASML
SSQDLKIVVG ALQMAEILMQ KLPDIFSVYF RREGVMHQVK NLAESEALLT SPPKVCTNGS
GSLASTTTIS TGSGTASGNS AADLGSPSLQ HRDDSLDLSP PGRLSDVLKR KRLPKRGPRR
PKYSPPRDED KVDNQAKSPT TTQSPKSFLA SLNPKTWGRL STQSNSNNIE PARTAGVSGL
ARAASKDTIS NNRERIRGWI KEQAHKFVER YFSSENMDGS NPALNVLQRL CNATEQLNLQ
VDGGVECLVE IRSIVSESDV SSFEIQHSGF VKQLLLYLTS KSDKDIVSRD IRLKRFLHVF
FGTPLPGEEP LAKLDPTENR HLLALVHKMN NCLSQMEQFP VKVHDFPSGN GTGSRGSQAL
KFFNTHQLKC QLQRHPDCTN VKQWKGGPVK IDPLALVQAI ERYLVVRGYG RVREDDEDSD
DDGSDEEIDE SLAAQFLNSG NVRHRLQFYI GDHLLPYNMT VYQAVRQYSI QTEEERESTD
DESNPLGRAG IWTKTHTIWY KPVREEEESA KDTVGGKRGR AQTAPTKTSP RNSKKHDELW
HGKDGVCPRI LNPLEVYLIS GPPENITFDD PSLDVVILLR VLHAISRYWY YLYDNAVCKE
IIPTSEFNNS KLTAKANRQL QDPLVIMTGN IPTWLTELGK SCPFFFPFDT RQMLFYVTAF
DRDRAMQRLL DTNPEINQSD SQDSRVAPRL DRKKRTVNRE DLLKQAESVM QDLGSSRAML
EIQYENEVGT GLGPTLEFYA LVSQELQRAD LGLWRGEEVT LPNPKGSQEG TKYIHNLQGL
FALPFGRTAK PAHIAKVKMK FRFLGKLMAK AIMDFRLVDI PLGLPFYKWM LRQESSLATH
DLVNIDPVVA KSVYHLEDIV RQKKRLEQDK AQTKESLQFA LESLNMNGCS VEDLGLDFTL
PGFPNIELKK GGKDVPVTIH NLEDYVRLVI YWALNEGVSR QLDSFRDGFE SVFPLNHLQY
FYPEELDQLL CGSRADPWDV KTLMECCRPD HGYTHDSRAV KFLFEILSSF DKEQQRLFLQ
FVTGSPRLPV GGFRSLNPPL TIVRKTFEAT ENPDDFLPSV MTCVNYLKLP DYSSIDNMRE
KLLMAAREGQ QSFHLS
