Q6PCN7 · HLTF_MOUSE
- ProteinHelicase-like transcription factor
- GeneHltf
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1003 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Has both helicase and E3 ubiquitin ligase activities. Possesses intrinsic ATP-dependent nucleosome-remodeling activity. This activity may be required for transcriptional activation or repression of specific target promoters (By similarity).
These may include the SERPINE1, to which this protein can bind directly. Plays a role in error-free postreplication repair (PRR) of damaged DNA and maintains genomic stability through acting as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA (By similarity).
These may include the SERPINE1, to which this protein can bind directly. Plays a role in error-free postreplication repair (PRR) of damaged DNA and maintains genomic stability through acting as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA (By similarity).
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nuclear matrix | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | RNA polymerase II transcription regulator complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent activity, acting on DNA | |
Molecular Function | ATP-dependent chromatin remodeler activity | |
Molecular Function | DNA binding | |
Molecular Function | helicase activity | |
Molecular Function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides | |
Molecular Function | transferase activity | |
Molecular Function | ubiquitin protein ligase binding | |
Molecular Function | zinc ion binding | |
Biological Process | mRNA transcription by RNA polymerase II | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | protein ubiquitination | |
Biological Process | regulation of neurogenesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHelicase-like transcription factor
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ6PCN7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Nuclear localization is stimulated by progesterone.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056185 | 1-1003 | Helicase-like transcription factor | |||
Sequence: MSYTFTRGPVWKYSQSVQYGSHENIPRLSYSTFLPHFEFQDIIPPDDFLTSDEEQDLVLFGTMRGQVVGLRYYTGVVNNNEMVALQREPNNPYDKNAIKVNNVNGNQVGHIKREIAAAVAYIMDNKLAQVEGVVPFGASNTFTMPLYMTFWGKEENRNVVLEQLKKHGFKLGPTPKTLGSSLENAWGSGRAGPSYSRPAHVAVQMTTDQLKTEFDKLFEDLKEDDRTVEMEPAEAIETPLLPHQKQALAWMIARENSKELPPFWEQRNDLYYNTITNFSVKERPENVHGGILADDMGLGKTLTAIAVILTNFDDGRPLLSKRGKKNHPGKEYKDETIKRRGSNMDKKEDGHSESSTCGEEPSISGTPEKSSCTLSQLSSVCPKRRKISVQYIESSDSEEIETSELPQKMKGKLKNVQLNTKSRVKGSSKVKEDSKFALTFFASATQRKMLKKGMSMMECSEACDTGERTRATLIICPLSVLSNWIDQFGQHVKSEVHLNFYVYYGPDRIRDSAWLSKQDIILTTYNILTHDYGTKDDSPLHSIKWLRVILDEGHAIRNPNAQQTKAVLELEAERRWVLTGTPIQNSLKDLWSLLSFLKLKPFIDREWWYRIIQRPVTTGDEGGLRRLQSLIKNITLRRTKTSKIKGKPVLELPERKVFIQHITLSEEERKIYQSVKNEGKAAIGRYFTEGTVLAHYADVLGLLLRLRQICCHTHLLTNGMSSSGPSRSDTPEELRKMLIEKMKIILSSGSDEECAICLDSLTFPVITHCAHVFCKPCICQVIHSEQPHAKCPLCRNEIHGDNLLECPPEELACDSDKESSMEWKSSSKINALMHALIELRTKDPNIKSLVVSQFTTFLSLIETPLKASGFVFTRLDGSMAQKKRVESIQRFQNTEAGSPTIMLLSLKAGGVGLNLCAASRVFLMDPAWNPAAEDQCFDRCHRLGQKQEVIITKFIVKDSVEENMLKIQNTKRDLAAGAFGTKKTDANDMKQAKINEIRTLIDL | ||||||
Modified residue | 27 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Cross-link | 112 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 195 | Phosphotyrosine; by JAK2 | ||||
Sequence: Y | ||||||
Cross-link | 211 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 394 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 395 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 397 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 730 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle.
Developmental stage
Expressed in the heart from 11.5 dpc. Gradually increases in skeletal muscle to 18.5 dpc.
Gene expression databases
Interaction
Subunit
Interacts with SP1 and SP3 independently of DNA; the interaction with these transcriptional factors may be required for basal transcription of target genes. Interacts with EGR1; the interaction requires prior binding to DNA and represses c-Rel via a DNA looping mechanism. Interacts with GATA4. Interacts with PCNA; the interaction promotes polyubiquitination of PCNA through association with the UBE2B-RAD18 and UBE2V2-UBE2N ubiquitin ligase complexes. Interacts with RAD18, SHPRH, UBE2V2 and UBE2N (By similarity).
Complex viewer
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, motif, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 38-287 | DNA-binding | ||||
Sequence: EFQDIIPPDDFLTSDEEQDLVLFGTMRGQVVGLRYYTGVVNNNEMVALQREPNNPYDKNAIKVNNVNGNQVGHIKREIAAAVAYIMDNKLAQVEGVVPFGASNTFTMPLYMTFWGKEENRNVVLEQLKKHGFKLGPTPKTLGSSLENAWGSGRAGPSYSRPAHVAVQMTTDQLKTEFDKLFEDLKEDDRTVEMEPAEAIETPLLPHQKQALAWMIARENSKELPPFWEQRNDLYYNTITNFSVKERPENV | ||||||
Compositional bias | 317-355 | Basic and acidic residues | ||||
Sequence: PLLSKRGKKNHPGKEYKDETIKRRGSNMDKKEDGHSESS | ||||||
Region | 317-373 | Disordered | ||||
Sequence: PLLSKRGKKNHPGKEYKDETIKRRGSNMDKKEDGHSESSTCGEEPSISGTPEKSSCT | ||||||
Compositional bias | 356-373 | Polar residues | ||||
Sequence: TCGEEPSISGTPEKSSCT | ||||||
Domain | 433-600 | Helicase ATP-binding | ||||
Sequence: DSKFALTFFASATQRKMLKKGMSMMECSEACDTGERTRATLIICPLSVLSNWIDQFGQHVKSEVHLNFYVYYGPDRIRDSAWLSKQDIILTTYNILTHDYGTKDDSPLHSIKWLRVILDEGHAIRNPNAQQTKAVLELEAERRWVLTGTPIQNSLKDLWSLLSFLKLK | ||||||
Motif | 551-554 | DEGH box | ||||
Sequence: DEGH | ||||||
Zinc finger | 754-795 | RING-type | ||||
Sequence: CAICLDSLTFPVITHCAHVFCKPCICQVIHSEQPHAKCPLCR | ||||||
Domain | 831-990 | Helicase C-terminal | ||||
Sequence: ALMHALIELRTKDPNIKSLVVSQFTTFLSLIETPLKASGFVFTRLDGSMAQKKRVESIQRFQNTEAGSPTIMLLSLKAGGVGLNLCAASRVFLMDPAWNPAAEDQCFDRCHRLGQKQEVIITKFIVKDSVEENMLKIQNTKRDLAAGAFGTKKTDANDMK | ||||||
Region | 919-1003 | Interaction with SP1 and SP3 | ||||
Sequence: SRVFLMDPAWNPAAEDQCFDRCHRLGQKQEVIITKFIVKDSVEENMLKIQNTKRDLAAGAFGTKKTDANDMKQAKINEIRTLIDL |
Sequence similarities
Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,003
- Mass (Da)113,317
- Last updated2004-07-05 v1
- Checksum91F08509ACEA5513
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 150 | in Ref. 1; AAB64175/AAB63915 | ||||
Sequence: F → Y | ||||||
Sequence conflict | 191 | in Ref. 1; AAB64175/AAB63915 | ||||
Sequence: A → R | ||||||
Compositional bias | 317-355 | Basic and acidic residues | ||||
Sequence: PLLSKRGKKNHPGKEYKDETIKRRGSNMDKKEDGHSESS | ||||||
Compositional bias | 356-373 | Polar residues | ||||
Sequence: TCGEEPSISGTPEKSSCT | ||||||
Sequence conflict | 394 | in Ref. 1; AAB64175/AAB63915 | ||||
Sequence: S → N | ||||||
Sequence conflict | 648 | in Ref. 1; AAB64175/AAB63915 | ||||
Sequence: P → S | ||||||
Sequence conflict | 902-905 | in Ref. 1; AAB64175 | ||||
Sequence: MLLS → STV | ||||||
Sequence conflict | 918 | in Ref. 1; AAB64175 | ||||
Sequence: A → R | ||||||
Sequence conflict | 980 | in Ref. 1; AAB64175 | ||||
Sequence: G → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF010138 EMBL· GenBank· DDBJ | AAB64175.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF010600 EMBL· GenBank· DDBJ | AAB63915.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC039796 EMBL· GenBank· DDBJ | AAH39796.1 EMBL· GenBank· DDBJ | mRNA | ||
BC057116 EMBL· GenBank· DDBJ | AAH57116.1 EMBL· GenBank· DDBJ | mRNA | ||
BC059240 EMBL· GenBank· DDBJ | AAH59240.1 EMBL· GenBank· DDBJ | mRNA |