FUN30_YEAST - dbPTM
FUN30_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FUN30_YEAST
UniProt AC P31380
Protein Name ATP-dependent helicase FUN30
Gene Name FUN30
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1131
Subcellular Localization Nucleus. Chromosome. Recruited to double-strand breaks (DSBs) sites of DNA damage.
Protein Description DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs, facilitating single-stranded DNA (ssDNA) production by the EXO1 and SGS1 machinery. Promotes gene silencing at heterochromatin by regulating the chromatin structure within or around silent loci. Also required for heterochromatin organization at centromeres..
Protein Sequence MSGSHSNDEDDVVQVPETSSPTKVASSSPLKPTSPTVPDASVASLRSRFTFKPSDPSEGAHTSKPLPSGSPEVALVNLAREFPDFSQTLVQAVFKSNSFNLQSARERLTRLRQQRQNWTWNKNASPKKSETPPPVKKSLPLANTGRLSSIHGNINNKSSKITVAKQKTSIFDRYSNVINQKQYTFELPTNLNIDSEALSKLPVNYNKKRRLVRADQHPIGKSYESSATQLGSAREKLLANRKYGRHANDNDEEEEESMMTDDDDASGDDYTESTPQINLDEQVLQFINDSDIVDLSDLSDTTMHKAQLIASHRPYSSLNAFVNTNFNDKDTEENASNKRKRRAAASANESERLLDKITQSIRGYNAIESVIKKCSSYGDLVTSQMKKWGVQVEGDNSELDLMNLGEDDDDDNDDGNNDNNNSNNNNTAGADATSKEKEDTKAVVEGFDETSAEPTPAPAPAPVERETKRIRNTTKPKVVEDEDDDVDLEAIDDELPQSEHEDDDYEEEDEDYNDEEEDVEYDDGDDDDDDDDEFVATRKNTHVISTTSRNGRKPIVKFFKGKPRLLSPEISLKDYQQTGINWLNLLYQNKMSCILADDMGLGKTCQVISFFAYLKQINEPGPHLVVVPSSTLENWLREFQKFAPALKIEPYYGSLQEREELRDILERNAGKYDVIVTTYNLAAGNKYDVSFLKNRNFNVVVYDEGHMLKNSTSERFAKLMKIRANFRLLLTGTPLQNNLKELMSLLEFIMPNLFISKKESFDAIFKQRAKTTDDNKNHNPLLAQEAITRAKTMMKPFILRRRKDQVLKHLPPKHTHIQYCELNAIQKKIYDKEIQIVLEHKRMIKDGELPKDAKEKSKLQSSSSKNLIMALRKASLHPLLFRNIYNDKIITKMSDAILDEPAYAENGNKEYIKEDMSYMTDFELHKLCCNFPNTLSKYQLHNDEWMQSGKIDALKKLLKTIIVDKQEKVLIFSLFTQVLDILEMVLSTLDYKFLRLDGSTQVNDRQLLIDKFYEDKDIPIFILSTKAGGFGINLVCANNVIIFDQSFNPHDDRQAADRAHRVGQTKEVNITTLITKDSIEEKIHQLAKNKLALDSYISEDKKSQDVLESKVSDMLEDIIYDENSKPKGTKE
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
2Phosphorylation------MSGSHSNDE
------CCCCCCCCC		61.3822369663
4Phosphorylation----MSGSHSNDEDD
----CCCCCCCCCCC		32.7922369663
6Phosphorylation--MSGSHSNDEDDVV
--CCCCCCCCCCCCE		47.9022369663
18PhosphorylationDVVQVPETSSPTKVA
CCEECCCCCCCCEEC		28.5622369663
19PhosphorylationVVQVPETSSPTKVAS
CEECCCCCCCCEECC		32.4322369663
20PhosphorylationVQVPETSSPTKVASS
EECCCCCCCCEECCC		43.9722369663
22PhosphorylationVPETSSPTKVASSSP
CCCCCCCCEECCCCC		39.8522369663
26PhosphorylationSSPTKVASSSPLKPT
CCCCEECCCCCCCCC		34.0422369663
27PhosphorylationSPTKVASSSPLKPTS
CCCEECCCCCCCCCC		26.6622369663
28PhosphorylationPTKVASSSPLKPTSP
CCEECCCCCCCCCCC		31.5822369663
31AcetylationVASSSPLKPTSPTVP
ECCCCCCCCCCCCCC		50.0324489116
33PhosphorylationSSSPLKPTSPTVPDA
CCCCCCCCCCCCCCC		45.8322369663
34PhosphorylationSSPLKPTSPTVPDAS
CCCCCCCCCCCCCCH		27.4022369663
36PhosphorylationPLKPTSPTVPDASVA
CCCCCCCCCCCCHHH		44.4222369663
41PhosphorylationSPTVPDASVASLRSR
CCCCCCCHHHHHHHC		26.1222369663
44PhosphorylationVPDASVASLRSRFTF
CCCCHHHHHHHCEEE		23.3521551504
47PhosphorylationASVASLRSRFTFKPS
CHHHHHHHCEEECCC		36.7221551504
52AcetylationLRSRFTFKPSDPSEG
HHHCEEECCCCCCCC		40.3224489116
54PhosphorylationSRFTFKPSDPSEGAH
HCEEECCCCCCCCCC		63.8421551504
64AcetylationSEGAHTSKPLPSGSP
CCCCCCCCCCCCCCH		52.2924489116
86PhosphorylationAREFPDFSQTLVQAV
HHHCCCHHHHHHHHH		29.6330377154
88PhosphorylationEFPDFSQTLVQAVFK
HCCCHHHHHHHHHHH		27.9128889911
96PhosphorylationLVQAVFKSNSFNLQS
HHHHHHHCCCCCHHH		26.6621440633
98PhosphorylationQAVFKSNSFNLQSAR
HHHHHCCCCCHHHHH		23.7025752575
109PhosphorylationQSARERLTRLRQQRQ
HHHHHHHHHHHHHHH		33.6021440633
122AcetylationRQNWTWNKNASPKKS
HHHCCCCCCCCCCCC		45.5125381059
129PhosphorylationKNASPKKSETPPPVK
CCCCCCCCCCCCCCC		53.4829136822
131PhosphorylationASPKKSETPPPVKKS
CCCCCCCCCCCCCCC		48.4619823750
136AcetylationSETPPPVKKSLPLAN
CCCCCCCCCCCCCCC		42.2825381059
138PhosphorylationTPPPVKKSLPLANTG
CCCCCCCCCCCCCCC		29.5121126336
148PhosphorylationLANTGRLSSIHGNIN
CCCCCCCCEECCCCC		26.3621440633
149PhosphorylationANTGRLSSIHGNINN
CCCCCCCEECCCCCC		24.1721440633
184PhosphorylationVINQKQYTFELPTNL
CCCCCCEEEECCCCC		14.2430377154
200AcetylationIDSEALSKLPVNYNK
CCHHHHHCCCCCCCC		58.6325381059
207AcetylationKLPVNYNKKRRLVRA
CCCCCCCCCCCEEEC		36.9825381059
221AcetylationADQHPIGKSYESSAT
CCCCCCCCCCCCHHH		51.0524489116
225PhosphorylationPIGKSYESSATQLGS
CCCCCCCCHHHHHHH		19.6230377154
226PhosphorylationIGKSYESSATQLGSA
CCCCCCCHHHHHHHH		24.3223749301
232PhosphorylationSSATQLGSAREKLLA
CHHHHHHHHHHHHHH		32.5128889911
329AcetylationVNTNFNDKDTEENAS
HCCCCCCCCCHHHHH		68.5924489116
331PhosphorylationTNFNDKDTEENASNK
CCCCCCCCHHHHHHH		51.4425882841
336PhosphorylationKDTEENASNKRKRRA
CCCHHHHHHHHHHHH		55.2425882841
369PhosphorylationRGYNAIESVIKKCSS
HHHHHHHHHHHHHHC		24.0325752575
375PhosphorylationESVIKKCSSYGDLVT
HHHHHHHHCCHHHHH		35.1621440633
376PhosphorylationSVIKKCSSYGDLVTS
HHHHHHHCCHHHHHH		42.4821440633
377PhosphorylationVIKKCSSYGDLVTSQ
HHHHHHCCHHHHHHH		9.8129734811
383PhosphorylationSYGDLVTSQMKKWGV
CCHHHHHHHHHHHCC		22.3128889911
450PhosphorylationVVEGFDETSAEPTPA
HHCCCCCCCCCCCCC		34.7722369663
451PhosphorylationVEGFDETSAEPTPAP
HCCCCCCCCCCCCCC		28.7022369663
455PhosphorylationDETSAEPTPAPAPAP
CCCCCCCCCCCCCCC		24.4822369663
467PhosphorylationPAPVERETKRIRNTT
CCCCCHHCHHHCCCC		31.6619823750
541PhosphorylationFVATRKNTHVISTTS
CEEEECCCEEEECCC		22.1328889911
545PhosphorylationRKNTHVISTTSRNGR
ECCCEEEECCCCCCC		25.2530377154
567PhosphorylationKGKPRLLSPEISLKD
CCCCCCCCCCCCHHH		25.6928152593
571PhosphorylationRLLSPEISLKDYQQT
CCCCCCCCHHHHHHH		27.9224961812
641AcetylationNWLREFQKFAPALKI
HHHHHHHHHHHHHCC		49.1424489116
693AcetylationKYDVSFLKNRNFNVV
CEEEEEECCCCCEEE		52.4224489116
760PhosphorylationLFISKKESFDAIFKQ
CCCCCHHHHHHHHHH		36.9930377154
766AcetylationESFDAIFKQRAKTTD
HHHHHHHHHHCCCCC		32.5324489116
861PhosphorylationKEKSKLQSSSSKNLI
HHHHHHCCCCCHHHH		42.4930377154
888AcetylationFRNIYNDKIITKMSD
HCHHHCCHHHHHHHH		32.1624489116
911PhosphorylationAENGNKEYIKEDMSY
HHCCCHHHHHHHHHH		20.9228132839
999PhosphorylationKFLRLDGSTQVNDRQ
CHHCCCCCCCCCCCE		18.4830377154
1024PhosphorylationDIPIFILSTKAGGFG
CCCEEEEECCCCCCC		24.0521126336
1025PhosphorylationIPIFILSTKAGGFGI
CCEEEEECCCCCCCC		22.8221126336
1082AcetylationTKDSIEEKIHQLAKN
EHHHHHHHHHHHHHC		32.4724489116
1095PhosphorylationKNKLALDSYISEDKK
HCHHHHHHHCCCCHH		25.8030377154
1101AcetylationDSYISEDKKSQDVLE
HHHCCCCHHHHHHHH		50.7224489116
1102AcetylationSYISEDKKSQDVLES
HHCCCCHHHHHHHHH		66.7224489116
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 FUN30_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FUN30_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 FUN30_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
C1TM_YEASTMIS1physical
11805826
ATM_YEASTTEL1physical
11805826
ATC3_YEASTDRS2physical
16554755
CSK21_YEASTCKA1physical
16554755
RAD24_YEASTRAD24genetic
19547744
ORC5_YEASTORC5genetic
19956593
FUN30_YEASTFUN30physical
20075079
ARPC3_YEASTARC18genetic
19325107
COG5_YEASTCOG5genetic
19325107
COG6_YEASTCOG6genetic
19325107
COG8_YEASTCOG8genetic
19325107
CWH41_YEASTCWH41genetic
19325107
MNN2_YEASTMNN2genetic
19325107
YHN8_YEASTYHR078Wgenetic
19325107
ISW1_YEASTISW1genetic
21388962
RAD51_YEASTRAD51genetic
23007155
EXO1_YEASTEXO1genetic
23007155
SGS1_YEASTSGS1genetic
23007155
CENPA_YEASTCSE4genetic
23028372
PAP2_YEASTPAP2genetic
23028372
RFA1_YEASTRFA1physical
22960743
EXO1_YEASTEXO1physical
22960743
DNA2_YEASTDNA2physical
22960743
ARP8_YEASTARP8genetic
22960743
RSC2_YEASTRSC2genetic
22960743
RAD54_YEASTRAD54genetic
22960743
DOT1_YEASTDOT1genetic
22960743
RAD9_YEASTRAD9genetic
22960743
EXO1_YEASTEXO1genetic
22960744
SGS1_YEASTSGS1genetic
22960744
COM1_YEASTSAE2genetic
22960744
EXO1_YEASTEXO1genetic
25806814
SRS2_YEASTSRS2genetic
25806814
SNF5_YEASTSNF5genetic
27708008
SWI6_YEASTSWI6genetic
27708008
SIN3_YEASTSIN3genetic
27708008
YP089_YEASTYPR089Wgenetic
27708008
ETR1_YEASTETR1genetic
27708008
YCR3_YEASTYCR023Cgenetic
27708008
NHP10_YEASTNHP10genetic
27708008
VAM6_YEASTVAM6genetic
27708008
VPS41_YEASTVPS41genetic
27708008
PCL6_YEASTPCL6genetic
27708008
IES5_YEASTIES5genetic
27708008
MSH4_YEASTMSH4genetic
27708008
WWM1_YEASTWWM1genetic
27708008
MRM2_YEASTMRM2genetic
27708008
NPR3_YEASTNPR3genetic
27708008
SSF1_YEASTSSF1genetic
27708008
HTD2_YEASTHTD2genetic
27708008
LPLA_YEASTAIM22genetic
27708008
STE24_YEASTSTE24genetic
27708008
MDM35_YEASTMDM35genetic
27708008
MUD2_YEASTMUD2genetic
27708008
SDHB_YEASTSDH2genetic
27708008
RIC1_YEASTRIC1genetic
27708008
LIPB_YEASTLIP2genetic
27708008
YL346_YEASTYLR346Cgenetic
27708008
CTF18_YEASTCTF18genetic
27708008
SCJ1_YEASTSCJ1genetic
27708008
SCS7_YEASTSCS7genetic
27708008
COG5_YEASTCOG5genetic
27708008
ATG3_YEASTATG3genetic
27708008
MSN1_YEASTMSN1genetic
27708008
TRM11_YEASTTRM11genetic
27708008
VAM3_YEASTVAM3genetic
27708008
AZF1_YEASTAZF1genetic
27708008
FABD_YEASTMCT1genetic
27708008
ODC2_YEASTODC2genetic
27708008
ARL3_YEASTARL3genetic
27708008
TBP6_YEASTYTA6genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
COM1_YEASTSAE2genetic
28063255
RAD9_YEASTRAD9genetic
28063255
DPB11_YEASTDPB11physical
28063255
MEC3_YEASTMEC3physical
28063255
EXO1_YEASTEXO1genetic
28065599
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FUN30_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-26; SER-27; SER-28;THR-33; SER-34; THR-88; SER-96; SER-98; THR-131; SER-226; SER-232;SER-369; SER-383 AND SER-451, 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-26 AND SER-28, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34 AND SER-451,AND MASS SPECTROMETRY.

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