TDIF2_BOVIN
ID TDIF2_BOVIN Reviewed; 766 AA.
AC Q0P5H2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Deoxynucleotidyltransferase terminal-interacting protein 2;
GN Name=DNTTIP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates the transcriptional activity of DNTT and ESR1. May
CC function as a chromatin remodeling protein (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a ternary complex with DNTT and core histone;
CC interaction with PCNA releases DNTT and H2A/H2B histones from this
CC ternary complex. Interacts with ESR1, ESR2, PPARG and RXRA (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; BC120039; AAI20040.1; -; mRNA.
DR RefSeq; NP_001068974.1; NM_001075506.1.
DR AlphaFoldDB; Q0P5H2; -.
DR SMR; Q0P5H2; -.
DR STRING; 9913.ENSBTAP00000010317; -.
DR PaxDb; Q0P5H2; -.
DR PRIDE; Q0P5H2; -.
DR Ensembl; ENSBTAT00000010317; ENSBTAP00000010317; ENSBTAG00000047679.
DR GeneID; 511258; -.
DR KEGG; bta:511258; -.
DR CTD; 30836; -.
DR VEuPathDB; HostDB:ENSBTAG00000047679; -.
DR VGNC; VGNC:28152; DNTTIP2.
DR eggNOG; KOG3100; Eukaryota.
DR GeneTree; ENSGT00510000048142; -.
DR HOGENOM; CLU_018725_0_0_1; -.
DR InParanoid; Q0P5H2; -.
DR OMA; SENMSCD; -.
DR OrthoDB; 887634at2759; -.
DR TreeFam; TF105964; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000047679; Expressed in oocyte and 110 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR InterPro; IPR039883; Fcf2/DNTTIP2.
DR InterPro; IPR014810; Fcf2_C.
DR PANTHER; PTHR21686; PTHR21686; 2.
DR Pfam; PF08698; Fcf2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..766
FT /note="Deoxynucleotidyltransferase terminal-interacting
FT protein 2"
FT /id="PRO_0000318504"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..615
FT /note="TdBR region; mediates interaction with DNTT"
FT /evidence="ECO:0000250"
FT COILED 515..552
FT /evidence="ECO:0000255"
FT COMPBIAS 9..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..540
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R2M2"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 620
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 394
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 568
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 594
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 616
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 636
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 659
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 668
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 696
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 741
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
SQ SEQUENCE 766 AA; 86798 MW; 9BECC639A8F09C0E CRC64;
MVVTRSARPQ ARNEATSVES LRQKNSAVTR LHVHPKGRKG SSPDNPNTTE SQTTPERSPA
PKTRKSGTTG SLPEMNKPAT DGEISEAESD CSSVPEVQDP VFRVTRRRQI LVAGTPVSSV
RKRLKITRVS ESHTEEVVSE ADSHVSGISR IMPPTEITTR RSKAKSQREP KQESHVEVIS
DAESSCSDIS FSGIATRRTT RSMQRKLQAQ TEENNTKIVL ENEKEIIHTP VNLEDSVNRR
TSRLLARSLS QINKPNFSNN EIYNDPDDSF FGISGKKLAV KKTRNFTIRE EKQDSISPLK
EITKQNCKSL DEEAKKIIDG GKEGNEKNSQ LNLSEFQDTG LQQLVSQRHS TPESDKTTSE
SSTLNHEAVM KSLAQTFAVV EMDRWNEERK NAIKTSDCSE PGDGSYSDSD EECTVIGVSE
DMSKEKEVDS ESDTKPSNLE FNTTQDKDDS VLLVLSSDES QQSEHSENEE DTVCFVENNG
NKESLNGDSE NLSHDNALFV IDTTPGLSAD KNFYLDEEDK AGEVATEEEE EEEEEESEEE
LSDHDRNKDN EFSDEDNLLS NTKSKLLKLM SSSIDTGLNI KELGGLYINF NADKVQLNKR
TLTQMKEKRK DELLQKTVIT PEFEKNYCVP PYSESKYKLQ KKRRQERQKT AGDGWFGMKA
PELTDELKND LKALKMRASM DPKRFYKKND RDGFPKYFQI GTIVDNPADF YHSRVPKKQR
KRTIVEELLA DSEFRRYNRR KYSEIMAEKA ANAAGKKFRK KKKFRN
