HEL2_YEAST - dbPTM
HEL2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HEL2_YEAST
UniProt AC Q05580
Protein Name E3 ubiquitin-protein ligase HEL2 {ECO:0000305|PubMed:22570702}
Gene Name HEL2 {ECO:0000303|PubMed:22570702}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 639
Subcellular Localization Cytoplasm .
Protein Description Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation..
Protein Sequence MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTDEENELCVICARKLTYVSLTPCHHKTCHICGFRQRALYNKKSCLICRTENEEVMFTDRIDGDISDKYNFCEKNEKYGINFTSEEVATETLNLLKFFCPLSKDEQVCDFGSFKKYNEHLKSEHNRMICLICATHKHAFPCELEIFTQNQLRNHQTKGNSEGFKGHPMCAFCSGKRFYSDDELYIHMRNQHEKCHICDKMNPASPQYFKDYNQLFDHFKHSHYVCTVQTCLDNKFVVFKDELELQAHILQEHGNILKGKPKFFQSELSTFISAPSRVIRERDDYDLPSISSLPGSSSGSRTDVRSASSPEESRLRLAERAKYYLENSKEDFNKFSSYNEDYSKGRLSAEKLLESYKLLFTKPNADVYLLIHNLAETFPKNSSKYNNLNAIYEQREQTLARQTSLPSLSSDSSLSMSIGRGHWGGTNDGGSAGAALGVRNIKNLPTLKSPSASYDPFATTVKKNTLRPVQNIKRTTPQSVSYRTSTNTVAFSPTYLESKKGSSSTSLNNSKDKLKSLNLPQLPPPKPKVQIPGLNRPQIADPKQWGKKSSTQDTNVHDNLRELNTTSGGNKKKGKQKQLLFHIGV
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
2Acetylation------MSESVKENV
------CCHHHHHCC
22814378
2Phosphorylation------MSESVKENV
------CCHHHHHCC
30377154
4Phosphorylation----MSESVKENVTP
----CCHHHHHCCCC
30377154
44PhosphorylationKQKKNNLSAEPNLTT
HHHHCCCCCCCCCCC
21551504
50PhosphorylationLSAEPNLTTSSADDT
CCCCCCCCCCCCCCC
21440633
51PhosphorylationSAEPNLTTSSADDTD
CCCCCCCCCCCCCCC
20377248
52PhosphorylationAEPNLTTSSADDTDE
CCCCCCCCCCCCCCC
20377248
53PhosphorylationEPNLTTSSADDTDEE
CCCCCCCCCCCCCCC
20377248
57PhosphorylationTTSSADDTDEENELC
CCCCCCCCCCCCCEE
25521595
121PhosphorylationDRIDGDISDKYNFCE
CCCCCCCHHHCCCHH
29734811
124PhosphorylationDGDISDKYNFCEKNE
CCCCHHHCCCHHHCC
29734811
132UbiquitinationNFCEKNEKYGINFTS
CCHHHCCCCCCCCCC
17644757
151UbiquitinationTETLNLLKFFCPLSK
HHHHHHHHHHCCCCC
17644757
158UbiquitinationKFFCPLSKDEQVCDF
HHHCCCCCCCCCCCC
17644757
169UbiquitinationVCDFGSFKKYNEHLK
CCCCCHHHHHHHHHH
17644757
170UbiquitinationCDFGSFKKYNEHLKS
CCCCHHHHHHHHHHH
17644757
176UbiquitinationKKYNEHLKSEHNRMI
HHHHHHHHHHHHCEE
15699485
191UbiquitinationCLICATHKHAFPCEL
EHHHCCCCCCCCCEE
17644757
233PhosphorylationFCSGKRFYSDDELYI
EECCCCCCCCCEEEE
30377154
234PhosphorylationCSGKRFYSDDELYIH
ECCCCCCCCCEEEEE
30377154
254UbiquitinationEKCHICDKMNPASPQ
CCCCCCCCCCCCCHH
24961812
264UbiquitinationPASPQYFKDYNQLFD
CCCHHHHHHHHHHHH
23749301
294UbiquitinationDNKFVVFKDELELQA
CCCEEEECCHHHHHH
23749301
316UbiquitinationNILKGKPKFFQSELS
CHHCCCCCCHHHHHH
17644757
320PhosphorylationGKPKFFQSELSTFIS
CCCCCHHHHHHHHHC
30377154
339PhosphorylationVIRERDDYDLPSISS
HHCCCCCCCCCCHHC
22369663
343PhosphorylationRDDYDLPSISSLPGS
CCCCCCCCHHCCCCC
22369663
345PhosphorylationDYDLPSISSLPGSSS
CCCCCCHHCCCCCCC
22369663
346PhosphorylationYDLPSISSLPGSSSG
CCCCCHHCCCCCCCC
22369663
350PhosphorylationSISSLPGSSSGSRTD
CHHCCCCCCCCCCCC
22369663
351PhosphorylationISSLPGSSSGSRTDV
HHCCCCCCCCCCCCC
22369663
352PhosphorylationSSLPGSSSGSRTDVR
HCCCCCCCCCCCCCC
22369663
354PhosphorylationLPGSSSGSRTDVRSA
CCCCCCCCCCCCCCC
22369663
356PhosphorylationGSSSGSRTDVRSASS
CCCCCCCCCCCCCCC
22369663
360PhosphorylationGSRTDVRSASSPEES
CCCCCCCCCCCHHHH
23749301
363PhosphorylationTDVRSASSPEESRLR
CCCCCCCCHHHHHHH
28889911
376AcetylationLRLAERAKYYLENSK
HHHHHHHHHHHHCCH
24489116
376UbiquitinationLRLAERAKYYLENSK
HHHHHHHHHHHHCCH
15699485
383UbiquitinationKYYLENSKEDFNKFS
HHHHHCCHHHHHHHH
23749301
388UbiquitinationNSKEDFNKFSSYNED
CCHHHHHHHHCCCCC
22817900
405AcetylationKGRLSAEKLLESYKL
HCCCCHHHHHHHHCH
24489116
411UbiquitinationEKLLESYKLLFTKPN
HHHHHHHCHHHCCCC
15699485
416UbiquitinationSYKLLFTKPNADVYL
HHCHHHCCCCHHHEE
15699485
434UbiquitinationNLAETFPKNSSKYNN
HHHHHCCCCCHHHHH
15699485
438UbiquitinationTFPKNSSKYNNLNAI
HCCCCCHHHHHHHHH
23749301
438AcetylationTFPKNSSKYNNLNAI
HCCCCCHHHHHHHHH
24489116
457PhosphorylationEQTLARQTSLPSLSS
HHHHHHHCCCCCCCC
22369663
458PhosphorylationQTLARQTSLPSLSSD
HHHHHHCCCCCCCCC
21440633
461PhosphorylationARQTSLPSLSSDSSL
HHHCCCCCCCCCCCE
22369663
463PhosphorylationQTSLPSLSSDSSLSM
HCCCCCCCCCCCEEE
22369663
464PhosphorylationTSLPSLSSDSSLSMS
CCCCCCCCCCCEEEE
22369663
466PhosphorylationLPSLSSDSSLSMSIG
CCCCCCCCCEEEEEC
22369663
467PhosphorylationPSLSSDSSLSMSIGR
CCCCCCCCEEEEECC
22369663
469PhosphorylationLSSDSSLSMSIGRGH
CCCCCCEEEEECCCC
22369663
471PhosphorylationSDSSLSMSIGRGHWG
CCCCEEEEECCCCCC
22369663
502UbiquitinationIKNLPTLKSPSASYD
CCCCCCCCCCCCCCC
23749301
503PhosphorylationKNLPTLKSPSASYDP
CCCCCCCCCCCCCCC
28889911
505PhosphorylationLPTLKSPSASYDPFA
CCCCCCCCCCCCCCC
28889911
519PhosphorylationATTVKKNTLRPVQNI
CCEECCCCCCCCCCC
28889911
527UbiquitinationLRPVQNIKRTTPQSV
CCCCCCCCCCCCCCE
15699485
530PhosphorylationVQNIKRTTPQSVSYR
CCCCCCCCCCCEEEE
23749301
546PhosphorylationSTNTVAFSPTYLESK
CCCEEEECCCEECCC
28152593
548PhosphorylationNTVAFSPTYLESKKG
CEEEECCCEECCCCC
28132839
552PhosphorylationFSPTYLESKKGSSST
ECCCEECCCCCCCCC
28889911
553UbiquitinationSPTYLESKKGSSSTS
CCCEECCCCCCCCCC
17644757
554UbiquitinationPTYLESKKGSSSTSL
CCEECCCCCCCCCCC
17644757
556PhosphorylationYLESKKGSSSTSLNN
EECCCCCCCCCCCCC
19823750
557PhosphorylationLESKKGSSSTSLNNS
ECCCCCCCCCCCCCC
19823750
558PhosphorylationESKKGSSSTSLNNSK
CCCCCCCCCCCCCCH
19823750
559PhosphorylationSKKGSSSTSLNNSKD
CCCCCCCCCCCCCHH
19795423
560PhosphorylationKKGSSSTSLNNSKDK
CCCCCCCCCCCCHHH
25752575
564PhosphorylationSSTSLNNSKDKLKSL
CCCCCCCCHHHHHHC
28889911

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 HEL2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HEL2_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 HEL2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRPE_YEASTMGE1physical
11805837
CLU_YEASTCLU1physical
11805837
HEL2_YEASTHEL2physical
11967834
RPN4_YEASTRPN4genetic
19547744
AATC_YEASTAAT2genetic
20959818
SSN3_YEASTSSN3genetic
20959818
VMS1_YEASTVMS1genetic
20959818
RPA34_YEASTRPA34genetic
20959818
SET3_YEASTSET3genetic
20959818
YPT6_YEASTYPT6genetic
20959818
RTG3_YEASTRTG3genetic
21127252
HAL4_YEASTSAT4genetic
21127252
UBC4_YEASTUBC4physical
22570702
ASK10_YEASTASK10genetic
27708008
RCY1_YEASTRCY1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
RTF1_YEASTRTF1genetic
27708008
PTK2_YEASTPTK2genetic
27708008
DPH2_YEASTDPH2genetic
27708008
SCS7_YEASTSCS7genetic
27708008
SIN3_YEASTSIN3genetic
27708008
COQ7_YEASTCAT5genetic
27708008
IDH2_YEASTIDH2genetic
27708008
SNC2_YEASTSNC2genetic
27708008
NIP80_YEASTNIP100genetic
27708008
SLH1_YEASTSLH1physical
28223409

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HEL2_YEAST

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Related Literatures of Post-Translational Modification

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