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Protein Page:
RECQL4 (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
RECQL4 DNA-dependent ATPase. May modulate chromosome segregation. Interacts with UBR1 and UBR2. Interacts with MCM10; this interaction regulates RECQL4 unwinding activity. Up-regulated in actively dividing cells. Ubiquitously expressed, with highest levels in thymus and testis. Belongs to the helicase family. RecQ subfamily. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.4.12; Helicase
Chromosomal Location of Human Ortholog: 8q24.3
Cellular Component: membrane; cytoplasm; nucleus
Molecular Function: ATP-dependent 3'-5' DNA helicase activity; zinc ion binding; bubble DNA binding; ATP binding
Biological Process: ATP catabolic process; multicellular organismal development; DNA strand renaturation; DNA replication; DNA repair; DNA duplex unwinding; DNA recombination
Reference #:  O94761 (UniProtKB)
Alt. Names/Synonyms: ATP-dependent DNA helicase Q4; DNA helicase, RecQ-like type 4; DNA helicase, RecQ-like, type 4; RecQ protein-like 4; RECQ4; RECQL4; RTS
Gene Symbols: RECQL4
Molecular weight: 133,077 Da
Basal Isoelectric point: 8.45  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RECQL4

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 39 S27-p RQRGRRPsQDDVEAA
0 38 S101-p PGRSRQGsVPDYGQR
0 2 K110-m1 PDYGQRLkANLkGTL
0 4 K114-m1 QRLkANLkGTLQAGP
0 1 S178-p RLQHLQAsLsQRLGS
0 9 S180-p QHLQAsLsQRLGSLD
0 1 S234-p VLGPGAGsQGPEASA
0 3 S251-p EVSIRVGsPQPSSSG
0 3 S323-p NPRYHGLsPSSQARA
0 1 Y353-p ARHDRGNyVRLNMKQ
1 0 K376-ac LRSRLLRkQAWkQkW
1 0 K380-ac LLRkQAWkQkWRkkG
1 0 K382-ac RkQAWkQkWRkkGEC
1 0 K385-ac AWkQkWRkkGECFGG
1 0 K386-ac WkQkWRkkGECFGGG
0 1 K695-ub LLTLLQGkRFQNLDS
0 1 S732-p HAAWVPGsGGRAPKT
0 1 T771-p QLRVVVAtVAFGMGL
0 1 K843-ub STDFLAVkRLVQRVF
0 1 K1101-ub EERSTRLkDLLGRYF
0 1 K1154-ub LSLRPEEkFSSRAVA
  mouse

 
A27 RLHGRRPAKGDVEAA
S102 PKQSLLSSVQDYGKR
K111 QDYGKRLKANLKNTT
K115 KRLKANLKNTTQTGP
S179 QLQQLRSSLSRRLTS
S181 QQLRSSLSRRLTSLD
S235 IADPDIQSEVSVQSP
S256-p PAQVLSQsPKSINSK
- gap
Y345 ASLDRGNYIRLNMKN
K368 NRGRLLRKQVWKQKW
K372 LLRKQVWKQKWKKKQ
K374 RKQVWKQKWKKKQAA
K377 VWKQKWKKKQAAFGG
K378 WKQKWKKKQAAFGGS
D717 LVTLLQGDRFRTLDS
P754 SMVGDSRPRGCGPEA
T793 HLRMVVATVAFGMGL
K865 STDFLAVKRLVQRVF
K1110 EEHSNQVKTLVSYYF
R1162 LSLRPEERFSGRAVA
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