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Protein

Deoxynucleotidyltransferase terminal-interacting protein 1

Gene

DNTTIP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Increases DNTT terminal deoxynucleotidyltransferase activity (in vitro) (PubMed:11473582). Also acts as a transcriptional regulator, binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription. Binds DNA and nucleosomes; may recruit HDAC1 complexes to nucleosomes or naked DNA.1 Publication2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi159 – 173A.T hook1 PublicationAdd BLAST15
DNA bindingi216 – 237H-T-H motif1 PublicationAdd BLAST22

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • nucleosome binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionDNA-binding
Biological processTranscription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxynucleotidyltransferase terminal-interacting protein 1
Alternative name(s):
Terminal deoxynucleotidyltransferase-interacting factor 1
Short name:
TdIF12 Publications
Short name:
TdT-interacting factor 11 Publication
Gene namesi
Name:DNTTIP1
Synonyms:C20orf167, TDIF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

EuPathDBiHostDB:ENSG00000101457.12
HGNCiHGNC:16160 DNTTIP1
MIMi611388 gene
neXtProtiNX_Q9H147

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000101457
PharmGKBiPA25709

Polymorphism and mutation databases

BioMutaiDNTTIP1
DMDMi26400504

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000724731 – 329Deoxynucleotidyltransferase terminal-interacting protein 1Add BLAST329

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei161PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H147
MaxQBiQ9H147
PaxDbiQ9H147
PeptideAtlasiQ9H147
PRIDEiQ9H147
ProteomicsDBi80354

PTM databases

iPTMnetiQ9H147
PhosphoSitePlusiQ9H147

Expressioni

Gene expression databases

BgeeiENSG00000101457
CleanExiHS_DNTTIP1
ExpressionAtlasiQ9H147 baseline and differential
GenevisibleiQ9H147 HS

Organism-specific databases

HPAiHPA042479
HPA045496

Interactioni

Subunit structurei

Monomer and homodimer (PubMed:11473582, PubMed:25653165). A minor proportion may form homotrimers (PubMed:11473582). Interacts with ZNF541 (PubMed:21573134). Interacts with the terminal deoxynucleotidyltransferase DNTT (PubMed:11473582, PubMed:16371131). Interacts with TRERF1 (PubMed:16371131, PubMed:21573134). Identified in a histone deacetylase complex that contains DNTTIP1, HDAC1 and ELMSAN1; this complex assembles into a tetramer that contains four copies of each protein chain (PubMed:25653165). Component of a histone deacetylase complex containing DNTTIP1, ZNF541, HDAC1 and HDAC2 (PubMed:21573134).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HOMEZQ8IX15-33EBI-2795449,EBI-10172004

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi125472, 32 interactors
CORUMiQ9H147
IntActiQ9H147, 19 interactors
MINTiQ9H147
STRINGi9606.ENSP00000361705

Structurei

Secondary structure

1329
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi65 – 87Combined sources23
Helixi90 – 103Combined sources14
Helixi110 – 125Combined sources16
Helixi126 – 129Combined sources4
Beta strandi197 – 202Combined sources6
Helixi204 – 206Combined sources3
Beta strandi216 – 218Combined sources3
Turni219 – 223Combined sources5
Turni231 – 235Combined sources5
Turni246 – 248Combined sources3
Helixi249 – 256Combined sources8
Beta strandi262 – 264Combined sources3
Beta strandi267 – 270Combined sources4
Helixi271 – 277Combined sources7
Turni281 – 285Combined sources5
Helixi291 – 293Combined sources3
Helixi303 – 315Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MWINMR-A197-316[»]
4D6KX-ray2.10A/B/C/D/E/F56-147[»]
ProteinModelPortaliQ9H147
SMRiQ9H147
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni56 – 147Important for dimerization1 PublicationAdd BLAST92
Regioni197 – 316Important for DNA and nucleosome binding1 PublicationAdd BLAST120

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi164 – 170Nuclear localization signalSequence analysis7

Domaini

The N-terminal domain mediates dimerization.1 Publication
The C-terminal domain mediates interaction with DNA and nucleosomes (PubMed:11473582, PubMed:25653165). It contains a HTH motif that mediates recognition of the consensus sequence (PubMed:23874396).3 Publications

Phylogenomic databases

eggNOGiKOG4801 Eukaryota
ENOG410XPIX LUCA
GeneTreeiENSGT00510000047836
HOGENOMiHOG000059597
HOVERGENiHBG057022
InParanoidiQ9H147
KOiK08707
OMAiWMVEKMR
OrthoDBiEOG091G0E9R
PhylomeDBiQ9H147
TreeFamiTF329275

Family and domain databases

InterProiView protein in InterPro
IPR026064 TdIF1
PANTHERiPTHR23399 PTHR23399, 1 hit

Sequencei

Sequence statusi: Complete.

Q9H147-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGATGDAEQP RGPSGAERGG LELGDAGAAG QLVLTNPWNI MIKHRQVQRR
60 70 80 90 100
GRRSQMTTSF TDPAISMDLL RAVLQPSINE EIQTVFNKYM KFFQKAALNV
110 120 130 140 150
RDNVGEEVDA EQLIQEACRS CLEQAKLLFS DGEKVIPRLT HELPGIKRGR
160 170 180 190 200
QAEEECAHRG SPLPKKRKGR PPGHILSSDR AAAGMVWKPK SCEPIRREGP
210 220 230 240 250
KWDPARLNES TTFVLGSRAN KALGMGGTRG RIYIKHPHLF KYAADPQDKH
260 270 280 290 300
WLAEQHHMRA TGGKMAYLLI EEDIRDLAAS DDYRGCLDLK LEELKSFVLP
310 320
SWMVEKMRKY METLRTENEH RAVEAPPQT
Length:329
Mass (Da):37,013
Last modified:December 6, 2002 - v2
Checksum:iFB78297069CD960E
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_014956183A → T. Corresponds to variant dbSNP:rs408911Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035676 mRNA Translation: BAB62888.1
AK314003 mRNA Translation: BAG36715.1
AL050348 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75812.1
BC024290 mRNA Translation: AAH24290.1
BC009535 mRNA Translation: AAH09535.1
CCDSiCCDS13369.1
RefSeqiNP_443183.1, NM_052951.2
UniGeneiHs.472852

Genome annotation databases

EnsembliENST00000372622; ENSP00000361705; ENSG00000101457
GeneIDi116092
KEGGihsa:116092
UCSCiuc002xpk.3 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTDIF1_HUMAN
AccessioniPrimary (citable) accession number: Q9H147
Secondary accession number(s): B2RA18
, Q96DE3, Q9BQP2, Q9H148
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: December 6, 2002
Last modified: June 20, 2018
This is version 133 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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