Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
RAD18 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
RAD18 a structural maintenance of chromosomes (SMC) protein involved in postreplication repair of UV-damaged DNA. Has ssDNA binding activity. Interacts with Rad6 through a conserved ring-finger motif. Rad6 is an ubiquitin-conjugating enzyme required for post-replication repair of damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin ligase; Ubiquitin conjugating system; EC 6.3.2.19; DNA repair; EC 6.3.2.-; Ligase
Cellular Component: XY body; replication fork; nucleus; chromatin
Molecular Function: Y-form DNA binding; protein binding; zinc ion binding; ubiquitin protein ligase binding; damaged DNA binding; polyubiquitin binding; ligase activity
Biological Process: negative regulation of DNA recombination; protein ubiquitination; spermatogenesis; DNA repair; response to UV
Reference #:  Q9NS91 (UniProtKB)
Alt. Names/Synonyms: E3 ubiquitin-protein ligase RAD18; hHR18; hRAD18; postreplication repair protein hRAD18p; Postreplication repair protein RAD18; RAD18; RAD18 homolog (S. cerevisiae); RAD18, S. cerevisiae, homolog; RING finger protein 73; RNF73
Gene Symbols: RAD18
Molecular weight: 56,223 Da
Basal Isoelectric point: 7.51  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RAD18
Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  DISEASE  |  Source  |  InnateDB  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
molecular association, regulation: S434‑p

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 61 Y56-p CIRKFLSyKTQCPTC
0 2 K83-u RILDELVkSLNFARN
1 21 S99-p LLQFALEsPAksPAs
0 2 K102-u FALEsPAksPAssSs
0 13 S103-p ALEsPAksPAssSsk
0 2 S106-p sPAksPAssSskNLA
0 2 S107-p PAksPAssSskNLAV
0 1 S109-p ksPAssSskNLAVkV
0 6 K110-u sPAssSskNLAVkVY
0 5 K115-u SskNLAVkVYtPVAS
0 3 T118-p NLAVkVYtPVASRQs
0 2 S125-p tPVASRQsLKQGSRL
0 3 K127 VASRQsLKQGSRLMD
0 1 N135 QGSRLMDNFLIREMS
0 12 K151-u STSELLIkENkSKFs
0 1 K154-u ELLIkENkSKFsPQk
0 5 S158-p kENkSKFsPQkEAsP
0 4 K161-u kSKFsPQkEAsPAAk
0 3 S164-p FsPQkEAsPAAkTKE
0 1 K168-u kEAsPAAkTKETRSV
0 11 - gap
0 64 K186-u APDPSEAkRPEPPST
0 68 K197-u PPSTSTLkQVTKVDC
0 43 K218-u IPESHINkHLDSCLS
0 1 K245-u HKRKPLPkTVYNLLS
0 1 K257-u LLSDRDLkKKLkEHG
0 3 K261-u RDLkKKLkEHGLSIQ
0 2 K271-u GLSIQGNkQQLIKRH
0 23 K309-u REIENIEkTRMRLEA
0 11 K318-u RMRLEASkLNEsVMV
0 2 S322-p EASkLNEsVMVFTkD
0 2 K328-u EsVMVFTkDQTEkEI
0 1 K333-u FTkDQTEkEIDEIHS
0 1 K347-u SKYRKKHkSEFQLLV
0 3 S368-p YKKIAGMsQkTVTIT
0 1 K370-a KIAGMsQkTVTITkE
0 1 K370-u KIAGMsQkTVTITkE
0 1 K376-u QkTVTITkEDESTEK
0 1 S385-p DESTEKLssVCMGQE
0 1 S386-p ESTEKLssVCMGQED
1 2 S403-p TSVTNHFsQSKLDsP
0 2 S409-p FsQSKLDsPEELEPD
1 0 S434-p IQEVLSSsESDSCNS
0 1 K462-u EAWEASHkNDLQDTE
0 19 S471-p DLQDTEIsPRQNRRT
8393 : Phospho-Rad18 (Ser403) Antibody
  mouse

 
Y56-p CIRKFLSyKTQCPTC
K83 RLLDELVKSMNFART
S99-p LLQFALEsPPIsPVs
I102 FALEsPPIsPVsSTS
S103-p ALEsPPIsPVsSTSK
S106-p sPPIsPVsSTSKKVV
S107 PPIsPVsSTSKKVVV
S109 IsPVsSTSKKVVVKV
K110 sPVsSTSKKVVVKVH
K115 TSKKVVVKVHNADAA
N118 KVVVKVHNADAAQHP
P125 NADAAQHPVkQANRL
K127-u DAAQHPVkQANRLMD
K135-u QANRLMDkFLIRETG
K151-u CVFELLGkENERKFs
E154 ELLGkENERKFsPQk
S158-p kENERKFsPQkELST
K161-u ERKFsPQkELSTSAE
S164 FsPQkELSTSAEIKE
E168 kELSTSAEIKETSLL
K177-u KETSLLGkPVLGLSD
N186 VLGLSDANGPVTPST
K197-u TPSTSTMkLDTKVSC
K218 IPENHINKHLDSCLS
K245 HKRKPLPKTVYNLLS
K257 LLSDRDLKKKLKQYG
K261 RDLKKKLKQYGLSVQ
K271 GLSVQGNKQQLIKRH
K309 QEIESMEKTRMRLEA
K318-u RMRLEASkLNENVMV
N322 EASkLNENVMVFTKN
K328 ENVMVFTKNQTEKEI
K333 FTKNQTEKEIEEVHS
Q347 SEYRKKHQNAFQLLV
S368-p YKKTGRVsQAAAMRT
A370 KTGRVsQAAAMRTDE
A370 KTGRVsQAAAMRTDE
- gap
P419 DEPAETLPSECIAQE
S420 EPAETLPSECIAQED
P442 VSVTNHFPQPQLDSP
S448 FPQPQLDSPGPSEPE
S470 CTDILFSSDSDSCNR
- gap
S485-p NDQNREVsPQQTRRT
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.