RDH54_YEAST - dbPTM
RDH54_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RDH54_YEAST
UniProt AC P38086
Protein Name DNA repair and recombination protein RDH54
Gene Name RDH54
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 958
Subcellular Localization Nucleus .
Protein Description Involved in the recombinational repair of double-strand breaks (DSB) in DNA during mitosis and meiosis. Has DNA dependent ATPase activity. Promotes D-loop (displacement loop) formation with RAD51 recombinase. Modifies the topology of double-stranded DNA during the D-loop reaction to facilitate the invasion of the homologous duplex molecule by the initiating single-stranded DNA substrate. Required for adaptation from G2/M checkpoint arrest induced by a double strand break, by participating in monitoring the extent of single-stranded DNA produced by resection of DNA ends. This role is distinct from its roles in recombination. Promotes colocalization of RAD51 and DMC1 during meiotic recombination. Involved in crossover interference..
Protein Sequence MAVISVKPRRREKILQEVKNSSVYQTVFDSGTTQMQIPKYENKPFKPPRRVGSNKYTQLKPTATAVTTAPISKAKVTVNLKRSISAGPTLNLAKKPNNLSSNENTRYFTIMYRKPTTKKHKTWSGDGYATLKASSDKLCFYNEAGKFLGSSMLPSDSDSLFETLFKAGSNEVQLDYELKENAEIRSAKEALSQNMGNPSPPTTSTTETVPSTKNDGGKYQMPLSQLFSLNTVKRFKSVTKQTNEHMTTVPKTSQNSKAKKYYPVFDVNKIDNPIVMNKNAAAEVDVIVDPLLGKFLRPHQREGVKFMYDCLMGLARPTIENPDIDCTTKSLVLENDSDISGCLLADDMGLGKTLMSITLIWTLIRQTPFASKVSCSQSGIPLTGLCKKILVVCPVTLIGNWKREFGKWLNLSRIGVLTLSSRNSPDMDKMAVRNFLKVQRTYQVLIIGYEKLLSVSEELEKNKHLIDMLVCDEGHRLKNGASKILNTLKSLDIRRKLLLTGTPIQNDLNEFFTIIDFINPGILGSFASFKRRFIIPITRARDTANRYNEELLEKGEERSKEMIEITKRFILRRTNAILEKYLPPKTDIILFCKPYSQQILAFKDILQGARLDFGQLTFSSSLGLITLLKKVCNSPGLVGSDPYYKSHIKDTQSQDSYSRSLNSGKLKVLMTLLEGIRKGTKEKVVVVSNYTQTLDIIENLMNMAGMSHCRLDGSIPAKQRDSIVTSFNRNPAIFGFLLSAKSGGVGLNLVGASRLILFDNDWNPSVDLQAMSRIHRDGQKKPCFIYRLVTTGCIDEKILQRQLMKNSLSQKFLGDSEMRNKESSNDDLFNKEDLKDLFSVHTDTKSNTHDLICSCDGLGEEIEYPETNQQQNTVELRKRSTTTWTSALDLQKKMNEAATNDDAKKSQYIRQCLVHYKHIDPARQDELFDEVITDSFTELKDSITFAFVKPGEICLREQ
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
7Acetylation-MAVISVKPRRREKI
-CCCEECCCCHHHHH		26.4725381059
53PhosphorylationKPPRRVGSNKYTQLK
CCCCCCCCCCCCCCC		27.5621440633
55AcetylationPRRVGSNKYTQLKPT
CCCCCCCCCCCCCCC		51.9124489116
57PhosphorylationRVGSNKYTQLKPTAT
CCCCCCCCCCCCCEE		29.0919779198
67PhosphorylationKPTATAVTTAPISKA
CCCEEEEECCCCCCC		18.1219779198
83PhosphorylationVTVNLKRSISAGPTL
EEEEEECCHHCCCCC		21.2227017623
85PhosphorylationVNLKRSISAGPTLNL
EEEECCHHCCCCCCC		28.5525533186
89PhosphorylationRSISAGPTLNLAKKP
CCHHCCCCCCCCCCC		27.6228889911
100PhosphorylationAKKPNNLSSNENTRY
CCCCCCCCCCCCCCE		32.9930377154
124PhosphorylationTKKHKTWSGDGYATL
CCCCCCCCCCCCEEE		32.0319779198
128PhosphorylationKTWSGDGYATLKASS
CCCCCCCCEEEEECC		10.9319779198
134PhosphorylationGYATLKASSDKLCFY
CCEEEEECCCCEEEE		37.1719779198
150PhosphorylationEAGKFLGSSMLPSDS
CCCCCCCCCCCCCCC		18.0921551504
151PhosphorylationAGKFLGSSMLPSDSD
CCCCCCCCCCCCCCC		23.6521551504
155PhosphorylationLGSSMLPSDSDSLFE
CCCCCCCCCCCHHHH		45.8721551504
192PhosphorylationRSAKEALSQNMGNPS
HHHHHHHHHCCCCCC		26.9323749301
199PhosphorylationSQNMGNPSPPTTSTT
HHCCCCCCCCCCCCC		47.7323749301
202PhosphorylationMGNPSPPTTSTTETV
CCCCCCCCCCCCEEC		36.4424961812
203PhosphorylationGNPSPPTTSTTETVP
CCCCCCCCCCCEECC		29.8324961812
204PhosphorylationNPSPPTTSTTETVPS
CCCCCCCCCCEECCC		35.4924961812
205PhosphorylationPSPPTTSTTETVPST
CCCCCCCCCEECCCC		26.9324961812
206PhosphorylationSPPTTSTTETVPSTK
CCCCCCCCEECCCCC		29.4423749301
208PhosphorylationPTTSTTETVPSTKND
CCCCCCEECCCCCCC		35.3124961812
218AcetylationSTKNDGGKYQMPLSQ
CCCCCCCCEECCHHH		37.5324489116
219PhosphorylationTKNDGGKYQMPLSQL
CCCCCCCEECCHHHH		17.2030377154
228PhosphorylationMPLSQLFSLNTVKRF
CCHHHHHCCHHHHHH		29.3327017623
242PhosphorylationFKSVTKQTNEHMTTV
HHHHCHHCCCCCCCC		44.1019823750
247PhosphorylationKQTNEHMTTVPKTSQ
HHCCCCCCCCCCCCC		26.9219823750
248PhosphorylationQTNEHMTTVPKTSQN
HCCCCCCCCCCCCCC		27.5119823750
252PhosphorylationHMTTVPKTSQNSKAK
CCCCCCCCCCCCCCC		29.4921440633
253PhosphorylationMTTVPKTSQNSKAKK
CCCCCCCCCCCCCCC		33.2319823750
256PhosphorylationVPKTSQNSKAKKYYP
CCCCCCCCCCCCCCC		26.7619823750
383PhosphorylationSQSGIPLTGLCKKIL
CCCCCCCCCHHCCEE		23.8225704821
420PhosphorylationRIGVLTLSSRNSPDM
HEEEEEECCCCCCCH		23.2430377154
629UbiquitinationLGLITLLKKVCNSPG
HHHHHHHHHHHCCCC		46.3917644757
630UbiquitinationGLITLLKKVCNSPGL
HHHHHHHHHHCCCCC		52.5717644757
645UbiquitinationVGSDPYYKSHIKDTQ
CCCCHHHHHHCCCCC		29.7017644757
649UbiquitinationPYYKSHIKDTQSQDS
HHHHHHCCCCCCCCC		49.6623749301
653PhosphorylationSHIKDTQSQDSYSRS
HHCCCCCCCCCHHHH		37.7430377154
741UbiquitinationFGFLLSAKSGGVGLN
HHHHEECCCCCCCEE		46.3817644757
811AcetylationMKNSLSQKFLGDSEM
HHHCHHHHHHCCHHH		38.9024489116
831AcetylationSNDDLFNKEDLKDLF
CCCCCCCHHHHHHHH		45.3225381059
880PhosphorylationTVELRKRSTTTWTSA
CEEHHHHCCCCHHHH		32.8928889911
881PhosphorylationVELRKRSTTTWTSAL
EEHHHHCCCCHHHHH		32.0725521595
882PhosphorylationELRKRSTTTWTSALD
EHHHHCCCCHHHHHH		22.9125521595
885PhosphorylationKRSTTTWTSALDLQK
HHCCCCHHHHHHHHH		11.3021440633
886PhosphorylationRSTTTWTSALDLQKK
HCCCCHHHHHHHHHH		20.5620377248
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 RDH54_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RDH54_YEAST !!
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 RDH54_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTW1_YEASTMTW1physical
15369670
SPO11_YEASTSPO11genetic
16230461
SCC1_YEASTMCD1genetic
16230461
RAD51_YEASTRAD51physical
16831867
UBP13_YEASTUBP13genetic
17314980
TOP1_YEASTTOP1genetic
19547744
SIZ1_YEASTSIZ1genetic
19109426
SIZ2_YEASTNFI1genetic
19109426
YAJ9_YEASTYAR029Wgenetic
20093466
ODPB_YEASTPDB1genetic
20093466
MTU1_YEASTSLM3genetic
20093466
SLX5_YEASTSLX5genetic
20093466
RM01_YEASTMRPL1genetic
20093466
BCS1_YEASTBCS1genetic
20093466
YOR1_YEASTYOR1genetic
20093466
SRS2_YEASTSRS2genetic
20093466
IME1_YEASTIME1genetic
20093466
MDM35_YEASTMDM35genetic
20093466
RAD5_YEASTRAD5genetic
20093466
COX12_YEASTCOX12genetic
20093466
VID22_YEASTVID22genetic
20093466
ATP10_YEASTATP10genetic
20093466
COX5A_YEASTCOX5Agenetic
20093466
ARE2_YEASTARE2genetic
20093466
HMI1_YEASTHMI1genetic
20093466
MRN1_YEASTMRN1genetic
20093466
RAD54_YEASTRAD54genetic
12702674
ULS1_YEASTULS1genetic
20864034
RAD51_YEASTRAD51genetic
20864034
RAD51_YEASTRAD51genetic
21558173
ULS1_YEASTULS1genetic
21558173
RAD51_YEASTRAD51physical
21558173
RAD9_YEASTRAD9genetic
11470411
MRE11_YEASTMRE11genetic
11470411
RFA1_YEASTRFA1genetic
11470411
RAD53_YEASTRAD53genetic
23473644
RAD51_YEASTRAD51genetic
23473644
ATR_YEASTMEC1genetic
23473644
RAD51_YEASTRAD51genetic
23798704
SLX5_YEASTSLX5genetic
27708008
MTU1_YEASTSLM3genetic
27708008
RM01_YEASTMRPL1genetic
27708008
ESC2_YEASTESC2genetic
27708008
BCS1_YEASTBCS1genetic
27708008
XRN1_YEASTXRN1genetic
27708008
HTD2_YEASTHTD2genetic
27708008
FLX1_YEASTFLX1genetic
27708008
GSH1_YEASTGSH1genetic
27708008
MDM35_YEASTMDM35genetic
27708008
RAD5_YEASTRAD5genetic
27708008
TOP3_YEASTTOP3genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
IRA2_YEASTIRA2genetic
27708008
HMI1_YEASTHMI1genetic
27708008
MSC6_YEASTMSC6genetic
27708008
MRN1_YEASTMRN1genetic
27708008
DMC1_YEASTDMC1physical
24465215
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RDH54_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASSSPECTROMETRY.

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