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Protein Page:
RECQL (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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 3.6.1.-; Helicase; DNA repair, damage; EC 3.6.4.12
Cellular Component: nucleolus; nucleus
Molecular Function: ATP-dependent DNA helicase activity; DNA helicase activity; protein binding; ATP-dependent 3'-5' DNA helicase activity; DNA binding; ATP binding
Biological Process: ATP catabolic process; DNA strand renaturation; DNA replication; DNA repair; 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-ub RQQELIQkKKVLTKK
0 4 K47-ub KVLTKKIkQCLEDsD
0 1 S53-p IkQCLEDsDAGASNE
0 2 Y61-p DAGASNEyDSsPAAW
0 2 S64-p ASNEyDSsPAAWNKE
0 1 K88-ub DILQNVFkLEkFRPL
0 1 K88-m1 DILQNVFkLEkFRPL
0 1 K91-ub QNVFkLEkFRPLQLE
0 1 K91-m1 QNVFkLEkFRPLQLE
0 1 T99-p FRPLQLEtINVTMAG
0 1 K180-ub VHAEMVNkNSELKLI
0 11 T190-p ELKLIYVtPEkIAKS
0 2 K193-ac LIYVtPEkIAKSKMF
0 1 K206-ac MFMSRLEkAyEARRF
0 2 K206-ub MFMSRLEkAyEARRF
0 1 Y208-p MSRLEkAyEARRFTR
0 1 K236-ub HDFRPDYkALGILKR
0 1 K293-ub LYYEVRQkPSNTEDF
0 1 K306-ub DFIEDIVkLINGRYK
0 1 K380-ac AFGMGIDkPDVRFVI
0 1 Y399-p SKSMENYyQESGRAG
0 1 K452-ub SYCQNISkCRRVLMA
0 1 K480-ub KMCDNCCkDSAFERk
0 1 R486 CkDSAFERkNITEYC
0 1 K487-ub kDSAFERkNITEYCR
0 1 K487-m1 kDSAFERkNITEYCR
0 1 K501-ub RDLIKILkQAEELNE
0 1 K509-ac QAEELNEkLTPLkLI
0 1 K509-ub QAEELNEkLTPLkLI
0 1 K514-ac NEkLTPLkLIDSWMG
0 1 K514-ub NEkLTPLkLIDSWMG
0 1 K522-ac LIDSWMGkGAAKLRV
0 1 K522-ub LIDSWMGkGAAKLRV
0 1 Y554-p AHFLIQQyLKEDySF
0 1 Y559-p QQyLKEDySFTAYAT
0 1 K575-ub SYLKIGPkANLLNNE
0 1 N580 GPkANLLNNEAHAIT
0 5 S597-p VTKSTQNsFRAEssQ
0 3 S602-p QNsFRAEssQTCHSE
0 4 S603-p NsFRAEssQTCHSEQ
0 1 K614-ac HSEQGDKkMEEKNSG
0 2 S634-p AANMLQQsGSKNTGA
0 1 K642-ac GSKNTGAkkRKIDDA
0 1 K643-ac SKNTGAkkRKIDDA_
  mouse

 
R38 RRQELLQRKSVLTGK
K47 SVLTGKIKQYLEDSS
S53 IKQYLEDSSAEASSD
L61 SAEASSDLDTSPAAW
S64 ASSDLDTSPAAWNKE
K88 DVLQNVFKLQKFRPL
K88 DVLQNVFKLQKFRPL
K91 QNVFKLQKFRPLQLE
K91 QNVFKLQKFRPLQLE
T99 FRPLQLETINVTMAR
K180 VHAEMVNKNSQLKLI
T190 QLKLIYVTPEKIAKS
K193 LIYVTPEKIAKSKMF
K206 MFMSRLEKAYEAGRL
K206 MFMSRLEKAYEAGRL
Y208 MSRLEKAYEAGRLTG
K236 HDFRPDYKALGILKR
K293 LFYEVRQKPSSAEDF
K306 DFTEDIVKLINGRYK
K380 AFGMGIDKPDVRFVI
Y399 SKSMENYYQESGRAG
K452 SYCQNVSKCRRVLIA
K480 KMCDNCCKDVSFEkK
K486-ub CKDVSFEkKNVTQHC
K487 KDVSFEkKNVTQHCR
K487 KDVSFEkKNVTQHCR
K501 RDLIKILKQAEGLNE
K509 QAEGLNEKLTPLKLI
K509 QAEGLNEKLTPLKLI
K514 NEKLTPLKLIDAWMG
K514 NEKLTPLKLIDAWMG
K522 LIDAWMGKGAAKLRV
K522 LIDAWMGKGAAKLRV
Y554 AHALLQQYLKEDYSF
Y559 QQYLKEDYSFTAYAT
R575 SYLKVGPRACLLsNE
S580-p GPRACLLsNEAHAVT
S597 VKKSAQSSVRGALSE
- gap
S603 SSVRGALSEARQVEQ
K614 QVEQVDSKGEEQSSG
S633 SKSRLQPSGSKNAGA
K641 GSKNAGAKKRKLDDA
K642 SKNAGAKKRKLDDA_
  rat

 
R38 RQHELLQRKSVLTKR
K47 SVLTKRIKQCLEDSA
S53 IKQCLEDSAAEASGD
C61 AAEASGDCDTSPAAW
S64 ASGDCDTSPAAWSKE
K88 HVLRDVFKLQKFRPL
K88 HVLRDVFKLQKFRPL
K91 RDVFKLQKFRPLQLE
K91 RDVFKLQKFRPLQLE
T99 FRPLQLETVNATMAR
K180 VHTEMMNKNSHLKLI
T190 HLKLIYVTPEKIAKS
K193 LIYVTPEKIAKSKMF
K206 MFMSRLEKAYEAGRL
K206 MFMSRLEKAYEAGRL
Y208 MSRLEKAYEAGRLTG
K236 HDFRPDYKALGILKR
K293 LYYEVRQKPSSAEDF
N306 DFIENIANLINGRYK
K380 AFGMGIDKPDVRFVI
Y399 SKSMENYYQESGRAG
K452 SYCQNISKCRRALIA
K480 KMCDNCCKDDSFEKK
K486 CKDDSFEKKNITEHC
K487 KDDSFEKKNITEHCQ
K487 KDDSFEKKNITEHCQ
K501 QALIKILKQAEGLNE
K509 QAEGLNEKLTPLKLI
K509 QAEGLNEKLTPLKLI
K514 NEKLTPLKLIDAWMG
K514 NEKLTPLKLIDAWMG
K522 LIDAWMGKGAAKFRV
K522 LIDAWMGKGAAKFRV
Y554 VHALLQQYLKEDYSF
Y559 QQYLKEDYSFTAYAT
R575 SYLKVGPRASLLSNE
S580 GPRASLLSNEGHAVT
S597 VKRSTQSSVRAAsPE
S602-p QSSVRAAsPEACEVD
- gap
K611 EACEVDSKGKEKSSA
- gap
- gap
- gap
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