Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  ATP-dependent DNA helicase Q1  

UniProtKB / Swiss-Prot ID :  RECQ1_HUMAN

Gene Name (Synonyms) : 
RECQL, RECQ1, RECQL1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction. 

Protein Sequence MASVSALTEELDSITSELHAVEIQIQELTERQQELIQKKKVLTKKIKQCLEDSDAGASNEYDSSPAAWNK...
Predicted Secondary Structure CCCCHHHHHHHHCCCCHHHHCCCCCCCCCCHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
102V -> I (in dbSNP:rs1065751). VAR_034679
372V -> I (in dbSNP:rs2230003). VAR_051732
487K -> T (in dbSNP:rs6501). VAR_016140
495D -> H (in dbSNP:rs6499). VAR_016141
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASVSA
---CCCCHH
20.74UniProtKB
Link-
47Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TKKIKQCLE
HCCCCCCCC
43.78Phosphositeplus
Link-
91Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FKLEKFRPL
HCCCCCCHH
58.05Phosphositeplus
Link
99PhosphothreonineLQLETINVT
HHHHHHHHH
26.83Phosphositeplus
Link
166PhosphoserineNASSSKEHV
EEECCCHHH
39.30HPRD
Link
193N6-acetyllysineVTPEKIAKS
ECHHHHHHH
49.52HPRD
Link
193N6-acetyllysineVTPEKIAKS
ECHHHHHHH
49.52Phosphositeplus
Link
193N6-acetyllysine.VTPEKIAKS
ECHHHHHHH
49.52UniProtKB
Link
206N6-acetyllysineSRLEKAYEA
CCCCCCEEE
61.94HPRD
Link
206N6-acetyllysineSRLEKAYEA
CCCCCCEEE
61.94Phosphositeplus
Link
206N6-acetyllysine.SRLEKAYEA
CCCCCCEEE
61.94UniProtKB
Link
208PhosphotyrosineLEKAYEARR
CCCCEEECC
22.61HPRD
Link
208PhosphotyrosineLEKAYEARR
CCCCEEECC
22.61Phosphositeplus
Link
514N6-acetyllysineLTPLKLIDS
HHHHHHHHH
44.60HPRD
Link
514N6-acetyllysineLTPLKLIDS
HHHHHHHHH
44.60Phosphositeplus
Link
514N6-acetyllysine.LTPLKLIDS
HHHHHHHHH
44.60UniProtKB
Link
522N6-acetyllysineSWMGKGAAK
HHCCCCCHH
29.30HPRD
Link
522N6-acetyllysineSWMGKGAAK
HHCCCCCHH
29.30Phosphositeplus
Link
522N6-acetyllysine.SWMGKGAAK
HHCCCCCHH
29.30UniProtKB
Link
634PhosphoserineMLQQSGSKN
CCCCCCCCC
31.88HPRD
Link-
634PhosphoserineMLQQSGSKN
CCCCCCCCC
31.88Phosphositeplus
Link-
636PhosphoserineQQSGSKNTG
CCCCCCCCC
28.16HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
APLF_HUMANphysical interactionMINT-4790124MINT17396150
RECQ1_HUMANphysical interaction
physical interaction
DIP:57233EDIP17227144
17227144
RFA1_HUMANin vitro
in vivo
HPRD:02762HPRD15096578
RECQ1_HUMANin vitroHPRD:02762HPRD12419808
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-193; LYS-206; LYS-514 ANDLYS-522, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures