RAD16_YEAST - dbPTM
RAD16_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAD16_YEAST
UniProt AC P31244
Protein Name DNA repair protein RAD16
Gene Name RAD16
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 790
Subcellular Localization Nucleus.
Protein Description Component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. Involved in differential repair of DNA after UV damage. Will repair preferentially the MAT-alpha locus compared with the HML-alpha locus..
Protein Sequence MQEGGFIRRRRTRSTKKSVNYNELSDDDTAVKNSKTLQLKGNSENVNDSQDEEYRDDATLVKSPDDDDKDFIIDLTGSDKERTATDENTHAIKNDNDEIIEIKEERDVSDDDEPLTKKRKTTARKKKKKTSTKKKSPKVTPYERNTLRLYEHHPELRNVFTDLKNAPPYVPQRSKQPDGMTIKLLPFQLEGLHWLISQEESIYAGGVLADEMGMGKTIQTIALLMNDLTKSPSLVVAPTVALMQWKNEIEQHTKGQLKIYIYHGASRTTDIKDLQGYDVVLTTYAVLESVFRKQNYGFRRKNGLFKQPSVLHNIDFYRVILDEAHNIKDRQSNTARAVNNLKTQKRWCLSGTPLQNRIGEMYSLIRFLNINPFTKYFCTKCDCASKDWKFTDRMHCDHCSHVIMQHTNFFNHFMLKNIQKFGVEGPGLESFNNIQTLLKNIMLRRTKVERADDLGLPPRIVTVRRDFFNEEEKDLYRSLYTDSKRKYNSFVEEGVVLNNYANIFTLITRMRQLADHPDLVLKRLNNFPGDDIGVVICQLCNDEAEEPIESKCHHKFCRLCIKEYVESFMENNNKLTCPVCHIGLSIDLSQPALEVDLDSFKKQSIVSRLNMSGKWQSSTKIEALVEELYKLRSNKRTIKSIVFSQFTSMLDLVEWRLKRAGFQTVKLQGSMSPTQRDETIKYFMNNIQCEVFLVSLKAGGVALNLCEASQVFILDPWWNPSVEWQSGDRVHRIGQYRPVKITRFCIEDSIEARIIELQEKKANMIHATINQDEAAISRLTPADLQFLFNN
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
17UbiquitinationRRTRSTKKSVNYNEL
CCCCCCCCCCCHHHC		60.7823749301
18PhosphorylationRTRSTKKSVNYNELS
CCCCCCCCCCHHHCC		19.7022890988
21PhosphorylationSTKKSVNYNELSDDD
CCCCCCCHHHCCCCC		14.0922890988
25PhosphorylationSVNYNELSDDDTAVK
CCCHHHCCCCCCHHH		32.5822369663
29PhosphorylationNELSDDDTAVKNSKT
HHCCCCCCHHHCCCE		40.1022890988
43PhosphorylationTLQLKGNSENVNDSQ
EEEECCCCCCCCCCC		38.9424961812
49PhosphorylationNSENVNDSQDEEYRD
CCCCCCCCCCHHHHC		34.0422369663
54PhosphorylationNDSQDEEYRDDATLV
CCCCCHHHHCCCEEE		19.7922369663
59PhosphorylationEEYRDDATLVKSPDD
HHHHCCCEEECCCCC		38.7919795423
63PhosphorylationDDATLVKSPDDDDKD
CCCEEECCCCCCCCC		26.5321551504
76PhosphorylationKDFIIDLTGSDKERT
CCEEEECCCCCCCCC		30.7825521595
78PhosphorylationFIIDLTGSDKERTAT
EEEECCCCCCCCCCC		40.0322369663
83PhosphorylationTGSDKERTATDENTH
CCCCCCCCCCCCCCC		34.6928889911
109PhosphorylationIKEERDVSDDDEPLT
EEECCCCCCCCCCCC		39.3425521595
116PhosphorylationSDDDEPLTKKRKTTA
CCCCCCCCHHHHHHH		45.2819823750
217PhosphorylationDEMGMGKTIQTIALL
HHCCCCHHHHHHHHH		16.7621126336
220PhosphorylationGMGKTIQTIALLMND
CCCHHHHHHHHHHCC		12.3621126336
617PhosphorylationNMSGKWQSSTKIEAL
CCCCCCCCCHHHHHH		38.5721551504
618PhosphorylationMSGKWQSSTKIEALV
CCCCCCCCHHHHHHH		20.7221551504
749PhosphorylationTRFCIEDSIEARIIE
EEEEECCCHHHHHHH		14.9921440633
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 RAD16_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAD16_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 RAD16_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADH1_YEASTADH1physical
11805826
MPCP_YEASTMIR1physical
11805826
PDC1_YEASTPDC1physical
11805826
CARP_YEASTPEP4physical
11805826
RIM1_YEASTRIM1physical
11805826
G3P3_YEASTTDH3physical
11805826
VATE_YEASTVMA4physical
11805826
VPS1_YEASTVPS1physical
11805826
SYWC_YEASTWRS1physical
11805826
YM94_YEASTYMR315Wphysical
11805826
TSA2_YEASTTSA2physical
11805837
ODPX_YEASTPDX1physical
11805837
RAD7_YEASTRAD7physical
11805837
H2B2_YEASTHTB2physical
11805837
H4_YEASTHHF1physical
11805837
H2AZ_YEASTHTZ1physical
11805837
UBX1_YEASTSHP1physical
11805837
YM71_YEASTYMR226Cphysical
11805837
6PGD1_YEASTGND1physical
11805837
SGS1_YEASTSGS1physical
11459632
RAD7_YEASTRAD7physical
9001217
ELOC_YEASTELC1physical
15226437
RAD7_YEASTRAD7physical
15226437
ABF1_YEASTABF1physical
10601031
RAD26_YEASTRAD26genetic
12411509
DEF1_YEASTDEF1genetic
11859374
RAD26_YEASTRAD26genetic
11859374
SGS1_YEASTSGS1genetic
11459632
RAD54_YEASTRAD54genetic
8016304
RIM1_YEASTRIM1physical
16429126
VPS1_YEASTVPS1physical
16429126
CARP_YEASTPEP4physical
16429126
SYWC_YEASTWRS1physical
16429126
YM94_YEASTYMR315Wphysical
16429126
RAD33_YEASTRAD33genetic
16595192
RAD7_YEASTRAD7physical
16675952
CUL3_YEASTCUL3physical
16675952
ELOC_YEASTELC1physical
16675952
RAD26_YEASTRAD26genetic
8552076
PFD1_YEASTPFD1genetic
19547744
RAD26_YEASTRAD26genetic
19910266
RAD23_YEASTRAD23genetic
15226437
UBP3_YEASTUBP3genetic
18498751
GCN5_YEASTGCN5genetic
21698136
RTF1_YEASTRTF1genetic
21737840
RPB9_YEASTRPB9genetic
21737840
SIZ1_YEASTSIZ1genetic
21968059
SIZ2_YEASTNFI1genetic
21968059
RPB9_YEASTRPB9genetic
21968059
RPB1_YEASTRPO21genetic
22405652
MON1_YEASTMON1genetic
27708008
ICE2_YEASTICE2genetic
27708008
VRP1_YEASTVRP1genetic
27708008
VAM3_YEASTVAM3genetic
27708008
VPS10_YEASTPEP1genetic
27708008
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
SLX5_YEASTSLX5genetic
27708008
YD089_YEASTYDR089Wgenetic
27708008
SEM1_YEASTSEM1genetic
27708008
LSM6_YEASTLSM6genetic
27708008
YRB30_YEASTYRB30genetic
27708008
XRN1_YEASTXRN1genetic
27708008
BGL2_YEASTBGL2genetic
27708008
RS27B_YEASTRPS27Bgenetic
27708008
KEL1_YEASTKEL1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
RS21B_YEASTRPS21Bgenetic
27708008
DS1P2_YEASTYSR3genetic
27708008
RAD5_YEASTRAD5genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
SST2_YEASTSST2genetic
27708008
LSM7_YEASTLSM7genetic
27708008
DPP3_YEASTYOL057Wgenetic
27708008
GGPPS_YEASTBTS1genetic
27708008
TKT1_YEASTTKL1genetic
27708008
YP098_YEASTYPR098Cgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAD16_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-25; SER-49 AND SER-109,AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-49, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-109, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.

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