Version 5.4
Homo sapiens Protein: HFM1
Summary
InnateDB Protein IDBP-100226.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol HFM1
Protein Name HFM1, ATP-dependent DNA helicase homolog (S. cerevisiae)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000359454
InnateDB Gene IDBG-100222 (HFM1)
Protein Structure
UniProt Annotation
Function
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003676 nucleic acid binding
GO:0003677 DNA binding
GO:0004386 helicase activity
GO:0005524 ATP binding
GO:0016787 hydrolase activity
Biological Process
GO:0000712 resolution of meiotic recombination intermediates
Cellular Component
Protein Structure and Domains
PDB ID
InterPro IPR001650 Helicase, C-terminal
IPR004179 Sec63 domain
IPR006935 Helicase/UvrB domain
IPR011545 DEAD/DEAH box helicase domain
IPR014001 Helicase, superfamily 1/2, ATP-binding domain
IPR027417 P-loop containing nucleoside triphosphate hydrolase
PFAM PF00271
PF02889
PF04851
PF00270
PRINTS
PIRSF
SMART SM00490
SM00611
SM00973
SM00487
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt A2PYH4
PhosphoSite PhosphoSite-A2PYH4
TrEMBL D2KTB2
UniProt Splice Variant
Entrez Gene 164045
UniGene Hs.602333
RefSeq NP_001017975
HUGO HGNC:20193
OMIM 615684
CCDS CCDS30769
HPRD 18568
IMGT
EMBL AB044787 AB204867 AC098691 AK094079 BC144172 BX323048
GenPept AAI44173 BAC04281 BAF45466 BAI63262 CAO03501

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca