RA54B_HUMAN - dbPTM
RA54B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RA54B_HUMAN
UniProt AC Q9Y620
Protein Name DNA repair and recombination protein RAD54B
Gene Name RAD54B
Organism Homo sapiens (Human).
Sequence Length 910
Subcellular Localization Nucleus .
Protein Description Involved in DNA repair and mitotic recombination. May play an active role in recombination processes in concert with other members of the RAD52 epistasis group..
Protein Sequence MRRSAAPSQLQGNSFKKPKFIPPGRSNPGLNEEITKLNPDIKLFEGVAINNTFLPSQNDLRICSLNLPSEESTREINNRDNCSGKYCFEAPTLATLDPPHTVHSAPKEVAVSKEQEEKSDSLVKYFSVVWCKPSKKKHKKWEGDAVLIVKGKSFILKNLEGKDIGRGIGYKFKELEKIEEGQTLMICGKEIEVMGVISPDDFSSGRCFQLGGGSTAISHSSQVARKCFSNPFKSVCKPSSKENRQNDFQNCKPRHDPYTPNSLVMPRPDKNHQWVFNKNCFPLVDVVIDPYLVYHLRPHQKEGIIFLYECVMGMRMNGRCGAILADEMGLGKTLQCISLIWTLQCQGPYGGKPVIKKTLIVTPGSLVNNWKKEFQKWLGSERIKIFTVDQDHKVEEFIKSIFYSVLIISYEMLLRSLDQIKNIKFDLLICDEGHRLKNSAIKTTTALISLSCEKRIILTGTPIQNDLQEFFALIDFVNPGILGSLSSYRKIYEEPIILSREPSASEEEKELGERRAAELTCLTGLFILRRTQEIINKYLPPKIENVVFCRPGALQIELYRKLLNSQVVRFCLQGLLENSPHLICIGALKKLCNHPCLLFNSIKEKECSSTCDKNEEKSLYKGLLSVFPADYNPLLFTEKESGKLQVLSKLLAVIHELRPTEKVVLVSNYTQTLNILQEVCKRHGYAYTRLDGQTPISQRQQIVDGFNSQHSSFFIFLLSSKAGGVGLNLIGGSHLILYDIDWNPATDIQAMSRVWRDGQKYPVHIYRLLTTGTIEEKIYQRQISKQGLCGAVVDLTKTSEHIQFSVEELKNLFTLHESSDCVTHDLLDCECTGEEVHTGDSLEKFIVSRDCQLGPHHQKSNSLKPLSMSQLKQWKHFSGDHLNLTDPFLERITENVSFIFQNITTQATGT
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----MRRSAAPSQLQ
----CCCCCCCHHHC		20.5825159151
8PhosphorylationMRRSAAPSQLQGNSF
CCCCCCCHHHCCCCC		38.5029978859
14PhosphorylationPSQLQGNSFKKPKFI
CHHHCCCCCCCCCCC		45.3123401153
16AcetylationQLQGNSFKKPKFIPP
HHCCCCCCCCCCCCC		68.9025953088
26PhosphorylationKFIPPGRSNPGLNEE
CCCCCCCCCCCCCHH		53.9826074081
36UbiquitinationGLNEEITKLNPDIKL
CCCHHHHHHCCCCEE		52.51-
104 (in isoform 2)Phosphorylation-41.76-
157UbiquitinationKGKSFILKNLEGKDI
CCCEEEECCCCCCCC		55.46-
162UbiquitinationILKNLEGKDIGRGIG
EECCCCCCCCCCCCC		36.48-
226MethylationHSSQVARKCFSNPFK
CHHHHHHHHHCCCCH		29.87100290793
226AcetylationHSSQVARKCFSNPFK
CHHHHHHHHHCCCCH		29.8726051181
226UbiquitinationHSSQVARKCFSNPFK
CHHHHHHHHHCCCCH		29.87-
229PhosphorylationQVARKCFSNPFKSVC
HHHHHHHCCCCHHCC		53.7321712546
237AcetylationNPFKSVCKPSSKENR
CCCHHCCCCCCCCCC		45.8625953088
252UbiquitinationQNDFQNCKPRHDPYT
CCCCCCCCCCCCCCC		53.27-
270UbiquitinationLVMPRPDKNHQWVFN
CCCCCCCCCCCEEEC		60.04-
371UbiquitinationGSLVNNWKKEFQKWL
CHHHHHHHHHHHHHH		44.54-
376UbiquitinationNWKKEFQKWLGSERI
HHHHHHHHHHCCCCE		50.10-
384UbiquitinationWLGSERIKIFTVDQD
HHCCCCEEEEEECCC		37.68-
409PhosphorylationFYSVLIISYEMLLRS
HHHHHHHCHHHHHHC		14.19-
486PhosphorylationPGILGSLSSYRKIYE
CCHHHCHHHHHHHHC		27.3324670416
490UbiquitinationGSLSSYRKIYEEPII
HCHHHHHHHHCCCEE		41.2121906983
492PhosphorylationLSSYRKIYEEPIILS
HHHHHHHHCCCEEEC		19.78-
590UbiquitinationICIGALKKLCNHPCL
EHHHHHHHHCCCCCC		60.15-
603UbiquitinationCLLFNSIKEKECSST
CCCCCCCCCCCCCCC		63.66-
608PhosphorylationSIKEKECSSTCDKNE
CCCCCCCCCCCCCHH		29.7622210691
609PhosphorylationIKEKECSSTCDKNEE
CCCCCCCCCCCCHHH		44.7222210691
610PhosphorylationKEKECSSTCDKNEEK
CCCCCCCCCCCHHHH		14.3922210691
621UbiquitinationNEEKSLYKGLLSVFP
HHHHHHHHHHHHHCC		48.66-
639UbiquitinationNPLLFTEKESGKLQV
CCCEEECCCCCCHHH		54.8721906983
643UbiquitinationFTEKESGKLQVLSKL
EECCCCCCHHHHHHH		45.05-
643AcetylationFTEKESGKLQVLSKL
EECCCCCCHHHHHHH		45.057380821
648PhosphorylationSGKLQVLSKLLAVIH
CCCHHHHHHHHHHHH		23.54-
761PhosphorylationVWRDGQKYPVHIYRL
HHCCCCCCCEEEEEE		11.55-
777UbiquitinationTTGTIEEKIYQRQIS
CCCCHHHHHHHHHHH		33.64-
785UbiquitinationIYQRQISKQGLCGAV
HHHHHHHHCCCCEEE		50.44-
862PhosphorylationPHHQKSNSLKPLSMS
CCCCCCCCCCCCCHH		44.8828555341
864UbiquitinationHQKSNSLKPLSMSQL
CCCCCCCCCCCHHHH		43.67-
872UbiquitinationPLSMSQLKQWKHFSG
CCCHHHHHHCCCCCC		46.61-
875UbiquitinationMSQLKQWKHFSGDHL
HHHHHHCCCCCCCCC		32.07-
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

Oops, there are no upstream regulatory protein records of RA54B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RA54B_HUMAN !!
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 RA54B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCD33_HUMANCCDC33physical
16189514
ZN580_HUMANZNF580physical
16189514
GORS2_HUMANGORASP2physical
16189514
TEANC_HUMANTCEANCphysical
16189514
RIBC2_HUMANRIBC2physical
16189514
TPC6A_HUMANTRAPPC6Aphysical
16189514
FSBP_HUMANRAD54Bphysical
16189514
RA54B_HUMANRAD54Bphysical
16189514
LNX1_HUMANLNX1physical
16189514
RAD51_HUMANRAD51physical
10851248
WRN_HUMANWRNphysical
17118963
FSBP_HUMANRAD54Bphysical
19060904
RA54B_HUMANRAD54Bphysical
19060904
FSBP_HUMANRAD54Bphysical
25416956
RA54B_HUMANRAD54Bphysical
25416956
GMCL1_HUMANGMCL1physical
25416956
ENKD1_HUMANENKD1physical
25416956
ATPF2_HUMANATPAF2physical
25416956
TEANC_HUMANTCEANCphysical
25416956
MDM2_HUMANMDM2physical
25384516
PLCG2_HUMANPLCG2physical
25814554
SH22A_HUMANSH2D2Aphysical
25814554
SUMO1_HUMANSUMO1physical
21516116
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RA54B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.

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