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Protein Page:
RECQL (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
RECQL 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. Interacts with EXO1 and MLH1. High expression in heart, lung, skeletal muscle and kidney, low expression in brain. Belongs to the helicase family. RecQ subfamily. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.4.12; Helicase; EC 3.6.1.-; DNA repair, damage
Molecular Function: ATP-dependent DNA helicase activity; protein binding; DNA helicase activity; DNA binding; ATP-dependent 3'-5' DNA helicase activity; ATP binding
Biological Process: DNA strand renaturation; DNA repair; DNA replication; DNA duplex unwinding; DNA recombination
Reference #:  P46063 (UniProtKB)
Alt. Names/Synonyms: ATP-dependent DNA helicase Q1; DNA helicase Q1-like; DNA helicase, RecQ-like type 1; DNA-dependent ATPase Q1; RecQ protein-like; RecQ protein-like (DNA helicase Q1-like); RecQ protein-like 1; RECQ1; RECQL; RECQL1
Gene Symbols: RECQL
Molecular weight: 73,457 Da
Basal Isoelectric point: 8.13  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RECQL

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 5 K38-u RQQELIQkKKVLTKK
0 4 K47-u KVLTKKIkQCLEDSD
0 2 Y61-p DAGASNEyDSSPAAW
0 1 K88-m1 DILQNVFkLEkFRPL
0 1 K91-u QNVFkLEkFRPLQLE
0 1 K91-m1 QNVFkLEkFRPLQLE
0 1 T99-p FRPLQLEtINVTMAG
0 12 T190-p ELKLIYVtPEkIAKS
0 1 K193-a LIYVtPEkIAKSKMF
0 1 K206-a MFMSRLEkAyEARRF
0 2 K206-u MFMSRLEkAyEARRF
0 1 Y208-p MSRLEkAyEARRFTR
0 1 K487-m1 KDSAFERkNITEYCR
0 1 K514-a NEKLTPLkLIDSWMG
0 1 K522-a LIDSWMGkGAAKLRV
0 4 S597-p VTKSTQNsFRAEssQ
0 3 S602-p QNsFRAEssQTCHSE
0 4 S603-p NsFRAEssQTCHSEQ
0 2 S634-p AANMLQQsGSKNTGA
  mouse

 
R38 RRQELLQRKSVLTGK
K47 SVLTGKIKQYLEDSS
L61 SAEASSDLDTSPAAW
K88 DVLQNVFKLQKFRPL
K91 QNVFKLQKFRPLQLE
K91 QNVFKLQKFRPLQLE
T99 FRPLQLETINVTMAR
T190 QLKLIYVTPEKIAKS
K193 LIYVTPEKIAKSKMF
K206 MFMSRLEKAYEAGRL
K206 MFMSRLEKAYEAGRL
Y208 MSRLEKAYEAGRLTG
K487 KDVSFEKKNVTQHCR
K514 NEKLTPLKLIDAWMG
K522 LIDAWMGKGAAKLRV
S597 VKKSAQSSVRGALSE
- gap
S603 SSVRGALSEARQVEQ
S633 SKSRLQPSGSKNAGA
  rat

 
R38 RQHELLQRKSVLTKR
K47 SVLTKRIKQCLEDSA
C61 AAEASGDCDTSPAAW
K88 HVLRDVFKLQKFRPL
K91 RDVFKLQKFRPLQLE
K91 RDVFKLQKFRPLQLE
T99 FRPLQLETVNATMAR
T190 HLKLIYVTPEKIAKS
K193 LIYVTPEKIAKSKMF
K206 MFMSRLEKAYEAGRL
K206 MFMSRLEKAYEAGRL
Y208 MSRLEKAYEAGRLTG
K487 KDDSFEKKNITEHCQ
K514 NEKLTPLKLIDAWMG
K522 LIDAWMGKGAAKFRV
S597 VKRSTQSSVRAAsPE
S602-p QSSVRAAsPEACEVD
- gap
- gap
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