RAD54_HUMAN - dbPTM
RAD54_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAD54_HUMAN
UniProt AC Q92698
Protein Name DNA repair and recombination protein RAD54-like
Gene Name RAD54L
Organism Homo sapiens (Human).
Sequence Length 747
Subcellular Localization Nucleus .
Protein Description Involved in DNA repair and mitotic recombination. Functions in the recombinational DNA repair (RAD52) pathway. Dissociates RAD51 from nucleoprotein filaments formed on dsDNA. Could be involved in the turnover of RAD51 protein-dsDNA filaments (By similarity). May play also an essential role in telomere length maintenance and telomere capping in mammalian cells..
Protein Sequence MRRSLAPSQLAKRKPEGRSCDDEDWQPGLVTPRKRKSSSETQIQECFLSPFRKPLSQLTNQPPCLDSSQHEAFIRSILSKPFKVPIPNYQGPLGSRALGLKRAGVRRALHDPLEKDALVLYEPPPLSAHDQLKLDKEKLPVHVVVDPILSKVLRPHQREGVKFLWECVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPEIDKAVVVSPSSLVKNWYNEVGKWLGGRIQPLAIDGGSKDEIDQKLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQLGEERLRELTSIVNRCLIRRTSDILSKYLPVKIEQVVCCRLTPLQTELYKRFLRQAKPAEELLEGKMSVSSLSSITSLKKLCNHPALIYDKCVEEEDGFVGALDLFPPGYSSKALEPQLSGKMLVLDYILAVTRSRSSDKVVLVSNYTQTLDLFEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPSSPDFVFMLSSKAGGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSAGTIEEKIFQRQSHKKALSSCVVDEEQDVERHFSLGELKELFILDEASLSDTHDRLHCRRCVNSRQIRPPPDGSDCTSDLAGWNHCTDKWGLRDEVLQAAWDAASTAITFVFHQRSHEEQRGLR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
4Phosphorylation----MRRSLAPSQLA
----CCCCCCHHHHH
20.6525159151
12AcetylationLAPSQLAKRKPEGRS
CCHHHHHHCCCCCCC
70.3325953088
19PhosphorylationKRKPEGRSCDDEDWQ
HCCCCCCCCCCCCCC
32.5228450419
31PhosphorylationDWQPGLVTPRKRKSS
CCCCCCCCCCCCCCC
23.5521815630
37PhosphorylationVTPRKRKSSSETQIQ
CCCCCCCCCCHHHHH
43.0328450419
38PhosphorylationTPRKRKSSSETQIQE
CCCCCCCCCHHHHHH
34.9225159151
39PhosphorylationPRKRKSSSETQIQEC
CCCCCCCCHHHHHHH
52.3228450419
41PhosphorylationKRKSSSETQIQECFL
CCCCCCHHHHHHHHH
32.6828450419
49PhosphorylationQIQECFLSPFRKPLS
HHHHHHHHCCCCCHH
11.1817081983
53UbiquitinationCFLSPFRKPLSQLTN
HHHHCCCCCHHHHHC
51.17-
76PhosphorylationQHEAFIRSILSKPFK
HHHHHHHHHHCCCCC
24.0624719451
80UbiquitinationFIRSILSKPFKVPIP
HHHHHHCCCCCCCCC
51.53-
83UbiquitinationSILSKPFKVPIPNYQ
HHHCCCCCCCCCCCC
56.48-
115UbiquitinationALHDPLEKDALVLYE
HHCCCCCCCCEEEEC
56.86-
121PhosphorylationEKDALVLYEPPPLSA
CCCCEEEECCCCCCH
20.9327642862
133UbiquitinationLSAHDQLKLDKEKLP
CCHHHHHCCCHHHCC
49.35-
138UbiquitinationQLKLDKEKLPVHVVV
HHCCCHHHCCCEEEE
64.92-
176PhosphorylationTSRRIPGSHGCIMAD
HCCCCCCCCCCEEEC
16.0229507054
208UbiquitinationLRQSPECKPEIDKAV
HHHCCCCCCCCCEEE
43.98-
224UbiquitinationVSPSSLVKNWYNEVG
ECHHHHHHHHHHHCH
47.24-
232UbiquitinationNWYNEVGKWLGGRIQ
HHHHHCHHHHCCCCE
44.41-
247PhosphorylationPLAIDGGSKDEIDQK
EEEECCCCHHHHHHH
42.32-
248UbiquitinationLAIDGGSKDEIDQKL
EEECCCCHHHHHHHH
63.76-
254UbiquitinationSKDEIDQKLEGFMNQ
CHHHHHHHHHHHHHH
44.77-
302UbiquitinationCDEGHRLKNSENQTY
CCCCCCCCCCCCHHH
59.382190698
308PhosphorylationLKNSENQTYQALDSL
CCCCCCHHHHHHHHC
29.2328796482
309PhosphorylationKNSENQTYQALDSLN
CCCCCHHHHHHHHCC
5.0928796482
314PhosphorylationQTYQALDSLNTSRRV
HHHHHHHHCCCCCCE
25.1121712546
355UbiquitinationGTAHEFKKHFELPIL
CCHHHHHHHCCCCCC
59.87-
363UbiquitinationHFELPILKGRDAAAS
HCCCCCCCCHHHHHH
53.25-
385PhosphorylationEERLRELTSIVNRCL
HHHHHHHHHHHHHHH
16.2022468782
386PhosphorylationERLRELTSIVNRCLI
HHHHHHHHHHHHHHH
36.8422468782
396PhosphorylationNRCLIRRTSDILSKY
HHHHHHCHHHHHHHH
22.3924719451
402UbiquitinationRTSDILSKYLPVKIE
CHHHHHHHHCCCEEE
47.57-
407UbiquitinationLSKYLPVKIEQVVCC
HHHHCCCEEEEEEEC
38.29-
425UbiquitinationPLQTELYKRFLRQAK
HHCHHHHHHHHHHCC
49.66-
432UbiquitinationKRFLRQAKPAEELLE
HHHHHHCCCHHHHHC
36.10-
441UbiquitinationAEELLEGKMSVSSLS
HHHHHCCCCCHHHHH
20.73-
454UbiquitinationLSSITSLKKLCNHPA
HHHHHHHHHHHCCCH
43.39-
455UbiquitinationSSITSLKKLCNHPAL
HHHHHHHHHHCCCHH
64.66-
503PhosphorylationGKMLVLDYILAVTRS
CCHHHHHHHHHHHCC
8.1522817900
515AcetylationTRSRSSDKVVLVSNY
HCCCCCCCEEEEECC
35.8732457312
522PhosphorylationKVVLVSNYTQTLDLF
CEEEEECCHHHHHHH
7.8530631047
548PhosphorylationVRLDGTMSIKKRAKV
EEECCCEEHHHHHHH
30.9724719451
550UbiquitinationLDGTMSIKKRAKVVE
ECCCEEHHHHHHHHH
28.97-
572PhosphorylationPDFVFMLSSKAGGCG
CCEEEEECCCCCCCC
20.2927264870
623PhosphorylationCYIYRLLSAGTIEEK
EEEEEHHHCCCHHHH
29.2828555341
630UbiquitinationSAGTIEEKIFQRQSH
HCCCHHHHHHHHHHH
35.71-
639UbiquitinationFQRQSHKKALSSCVV
HHHHHHHHHHHHCCC
49.49-
662UbiquitinationHFSLGELKELFILDE
HCCHHHHHHEEEEEC
48.33-
671PhosphorylationLFILDEASLSDTHDR
EEEEECCCCCCCCCH
26.76-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
31TPhosphorylationKinaseCDK2P24941
PSP
49SPhosphorylationKinaseCDK2P24941
PSP
572SPhosphorylationKinaseNEK1Q96PY6
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
572SPhosphorylation

27264870

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RAD54_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NTAQ1_HUMANWDYHV1physical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAD54_HUMAN

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Related Literatures of Post-Translational Modification

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