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Protein

Deoxynucleotidyltransferase terminal-interacting protein 1

Gene

DNTTIP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi159 – 17315A.T hook1 PublicationAdd
BLAST
DNA bindingi216 – 23722H-T-H motif1 PublicationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

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

HGNCiHGNC:16160. DNTTIP1.

Subcellular locationi

GO - Cellular componenti

  • histone deacetylase complex Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25709.

Polymorphism and mutation databases

BioMutaiDNTTIP1.
DMDMi26400504.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Deoxynucleotidyltransferase terminal-interacting protein 1PRO_0000072473Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H147.
MaxQBiQ9H147.
PaxDbiQ9H147.
PeptideAtlasiQ9H147.
PRIDEiQ9H147.

PTM databases

iPTMnetiQ9H147.
PhosphoSiteiQ9H147.

Expressioni

Gene expression databases

BgeeiENSG00000101457.
CleanExiHS_DNTTIP1.
ExpressionAtlasiQ9H147. baseline and differential.
GenevisibleiQ9H147. HS.

Organism-specific databases

HPAiCAB045968.
HPA042479.
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

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

Protein-protein interaction databases

BioGridi125472. 31 interactions.
IntActiQ9H147. 16 interactions.
STRINGi9606.ENSP00000361705.

Structurei

Secondary structure

1
329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 8723Combined sources
Helixi90 – 10314Combined sources
Helixi110 – 12516Combined sources
Helixi126 – 1294Combined sources
Beta strandi197 – 2026Combined sources
Helixi204 – 2063Combined sources
Beta strandi216 – 2183Combined sources
Turni219 – 2235Combined sources
Turni231 – 2355Combined sources
Turni246 – 2483Combined sources
Helixi249 – 2568Combined sources
Beta strandi262 – 2643Combined sources
Beta strandi267 – 2704Combined sources
Helixi271 – 2777Combined sources
Turni281 – 2855Combined sources
Helixi291 – 2933Combined sources
Helixi303 – 31513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MWINMR-A197-316[»]
4D6KX-ray2.10A/B/C/D/E/F56-147[»]
ProteinModelPortaliQ9H147.
SMRiQ9H147. Positions 59-130, 197-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni56 – 14792Important for dimerization1 PublicationAdd
BLAST
Regioni197 – 316120Important for DNA and nucleosome binding1 PublicationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi164 – 1707Nuclear localization signalSequence analysis

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

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

InterProiIPR026064. TdIF1.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti183 – 1831A → T.
Corresponds to variant rs408911 [ dbSNP | Ensembl ].
VAR_014956

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

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MWINMR-A197-316[»]
4D6KX-ray2.10A/B/C/D/E/F56-147[»]
ProteinModelPortaliQ9H147.
SMRiQ9H147. Positions 59-130, 197-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125472. 31 interactions.
IntActiQ9H147. 16 interactions.
STRINGi9606.ENSP00000361705.

PTM databases

iPTMnetiQ9H147.
PhosphoSiteiQ9H147.

Polymorphism and mutation databases

BioMutaiDNTTIP1.
DMDMi26400504.

Proteomic databases

EPDiQ9H147.
MaxQBiQ9H147.
PaxDbiQ9H147.
PeptideAtlasiQ9H147.
PRIDEiQ9H147.

Protocols and materials databases

DNASUi116092.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi116092.
GeneCardsiDNTTIP1.
HGNCiHGNC:16160. DNTTIP1.
HPAiCAB045968.
HPA042479.
HPA045496.
MIMi611388. gene.
neXtProtiNX_Q9H147.
PharmGKBiPA25709.
GenAtlasiSearch...

Phylogenomic databases

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

Miscellaneous databases

GenomeRNAii116092.
PROiQ9H147.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101457.
CleanExiHS_DNTTIP1.
ExpressionAtlasiQ9H147. baseline and differential.
GenevisibleiQ9H147. HS.

Family and domain databases

InterProiIPR026064. TdIF1.
[Graphical view]
PANTHERiPTHR23399. PTHR23399. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTDIF1_HUMAN
AccessioniPrimary (citable) accession number: Q9H147
Secondary accession number(s): B2RA18
, Q96DE3, Q9BQP2, Q9H148
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: December 6, 2002
Last modified: September 7, 2016
This is version 123 of the entry and version 2 of the sequence. [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

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.