SET1_DROME - dbPTM
SET1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SET1_DROME
UniProt AC Q5LJZ2
Protein Name Histone-lysine N-methyltransferase SETD1 {ECO:0000250|UniProtKB:Q9UPS6}
Gene Name Set1 {ECO:0000312|EMBL:EAL24598.1, ECO:0000312|FlyBase:FBgn0040022}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1641
Subcellular Localization Nucleus . Chromosome . Colocalizes with di- and trimethylated H3 'Lys-4' and with phosphorylated RNA polymerase II at transcriptional puffs on polytene chromosomes.
Protein Description Catalytic component of the SET1 complex that specifically di- and trimethylates 'Lys-4' of histone H3 and is the main di- and trimethyltransferase throughout development. Set1-dependent trimethylation regulates chromatin changes at active promoters that ensure optimal RNA polymerase II release into productive elongation, thereby contributing to optimal transcription..
Protein Sequence MQDVRNINLVNNSSNSHDSSLANSKMPRNFKLLSDPQLVKCGTRLYRYDGLMPGDPSYPTITPRDPRNPLIRIRARAVEPLMLLIPRFVIDSDYVGQPPAVEVTIVNLNDNIDKQFLASMLDKCGTSDEINIYHHPITNKHLGIARIVFDSTKGARQFVEKYNQKSVMGKILDVFCDPFGATLKKSLESLTNSVAGKQLIGPKVTPQWTFQQAALEDTEFIHGYPEKNGEHIKDIYTTQTNHEIPNRSRDRNWNRDKERERDRHFKERSRHSSERSYDRDRGMRENVGTSIRRRRTFYRRRSSDISPEDSRDILIMTRERSRDSDSRPRDYCRSRERESFRDRKRSHEKGRDQPREKREHYYNSSKDREYRGRDRDRSAEIDQRDRGSLKYCSRYSLHEYIETDVRRSSNTISSYYSASSLPIASHGFNSCSFPSIENIKTWSDRRAWTAFQPDFHPVQPPPPPPEEIDNWDEEEHDKNSIVPTHYGCMAKLQPPVPSNVNFATKLQSVTQPNSDPGTVDLDTRIALIFKGKTFGNAPPFLQMDSSDSETDQGKPEVFSDVNSDSNNSENKKRSCEKNNKVLHQPNEASDISSDEELIGKKDKSKLSLICEKEVNDDNMSLSSLSSQEDPIQTKEGAEYKSIMSSYMYSHSNQNPFYYHASGYGHYLSGIPSESASRLFSNGAYVHSEYLKAVASFNFDSFSKPYDYNKGALSDQNDGIRQKVKQVIGYIVEELKQILKRDVNKRMIEITAFKHFETWWDEHTSKARSKPLFEKADSTVNTPLNCIKDTSYNEKNPDINLLINAHREVADFQSYSSIGLRAAMPKLPSFRRIRKHPSPIPTKRNFLERDLSDQEEMVQRSDSDKEDSNVEISDTARSKIKGPVPIQESDSKSHTSGLNSKRKGSASSFFSSSSSSTSSEAEYEAIDCVEKARTSEEDSPRGYGQRNLNQRTTTIRNRNLVGTMDVINVRNLCSGSNEFKKENVTKRTKKNIYSDTDEDNDRTLFPALKEKNISTILSDLEEISKDSCIGLDENGIEPTILRKIPNTPKLNEECRRSLTPVPPPGYNEEEIKKKVDCKQKPSFEYDRIYSDSEEEKEYQERRKRNTEYMAQMEREFLEEQEKRIEKSLDKNLQSPNNIVKNNNSPRNKNDETRKTAISQTRSCFESASKVDTTLVNIISVENDINEFGPHEEGDVLTNGCNKMYTNSKGKTKRTQSPVYSEGGSSQASQASQVALEHCYSLPPHSVSLGDYPSGKVNETKNILKREAENIAIVSQMTRTGPGRPRKDPICIQKKKRDLAPRMSNVKSKMTPNGDEWPDLAHKNVHFVPCDMYKTRDQNEEMVILYTFLTKGIDAEDINFIKMSYLDHLHKEPYAMFLNNTHWVDHCTTDRAFWPPPSKKRRKDDELIRHKTGCARTEGFYKLDVREKAKHKYHYAKANTEDSFNEDRSDEPTALTNHHHNKLISKMQGISREARSNQRRLLTAFGSMGESELLKFNQLKFRKKQLKFAKSAIHDWGLFAMEPIAADEMVIEYVGQMIRPVVADLRETKYEAIGIGSSYLFRIDMETIIDATKCGNLARFINHSCNPNCYAKVITIESEKKIVIYSKQPIGINEEITYDYKFPLEDEKIPCLCGAQGCRGTLN
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
302PhosphorylationRTFYRRRSSDISPED
HHHHHHCCCCCCHHH
19429919
303PhosphorylationTFYRRRSSDISPEDS
HHHHHCCCCCCHHHH
19429919
306PhosphorylationRRRSSDISPEDSRDI
HHCCCCCCHHHHCCE
19429919
310PhosphorylationSDISPEDSRDILIMT
CCCCHHHHCCEEEEE
19429919
378PhosphorylationRGRDRDRSAEIDQRD
CCCCCCCCCCCCHHH
19429919
530AcetylationTRIALIFKGKTFGNA
CEEEEEECCCCCCCC
21791702
589PhosphorylationLHQPNEASDISSDEE
CCCCCCHHCCCCCHH
19429919
592PhosphorylationPNEASDISSDEELIG
CCCHHCCCCCHHHCC
19429919
593PhosphorylationNEASDISSDEELIGK
CCHHCCCCCHHHCCC
19429919
604PhosphorylationLIGKKDKSKLSLICE
HCCCCCHHHHEEEEE
22817900
607PhosphorylationKKDKSKLSLICEKEV
CCCHHHHEEEEEEEE
22817900
620PhosphorylationEVNDDNMSLSSLSSQ
EECCCCCCHHHCCCC
19429919
622PhosphorylationNDDNMSLSSLSSQED
CCCCCCHHHCCCCCC
19429919
623PhosphorylationDDNMSLSSLSSQEDP
CCCCCHHHCCCCCCC
19429919
625PhosphorylationNMSLSSLSSQEDPIQ
CCCHHHCCCCCCCCC
19429919
626PhosphorylationMSLSSLSSQEDPIQT
CCHHHCCCCCCCCCC
19429919
633PhosphorylationSQEDPIQTKEGAEYK
CCCCCCCCCCHHHHH
19429919
837PhosphorylationRRIRKHPSPIPTKRN
HHHHCCCCCCCCCCC
19429919
851PhosphorylationNFLERDLSDQEEMVQ
CHHHCCCCCHHHHHH
19429919
860PhosphorylationQEEMVQRSDSDKEDS
HHHHHHCCCCCCCCC
22817900
862PhosphorylationEMVQRSDSDKEDSNV
HHHHCCCCCCCCCCC
22817900
867PhosphorylationSDSDKEDSNVEISDT
CCCCCCCCCCCCCHH
22817900
933PhosphorylationDCVEKARTSEEDSPR
HHHHHHCCCCCCCCC
25749252
934PhosphorylationCVEKARTSEEDSPRG
HHHHHCCCCCCCCCC
25749252
938PhosphorylationARTSEEDSPRGYGQR
HCCCCCCCCCCCCCC
25749252
993PhosphorylationRTKKNIYSDTDEDND
HHHCCCCCCCCCCCC
19429919
995PhosphorylationKKNIYSDTDEDNDRT
HCCCCCCCCCCCCCC
25749252
1013PhosphorylationALKEKNISTILSDLE
HHHHCCHHHHHHCHH
19429919
1014PhosphorylationLKEKNISTILSDLEE
HHHCCHHHHHHCHHH
19429919
1017PhosphorylationKNISTILSDLEEISK
CCHHHHHHCHHHHCC
19429919
1023PhosphorylationLSDLEEISKDSCIGL
HHCHHHHCCCCCCCC
19429919
1046PhosphorylationILRKIPNTPKLNEEC
HHHCCCCCCCCCHHH
27626673
1056PhosphorylationLNEECRRSLTPVPPP
CCHHHHHCCCCCCCC
19429919
1058PhosphorylationEECRRSLTPVPPPGY
HHHHHCCCCCCCCCC
19429919
1089PhosphorylationFEYDRIYSDSEEEKE
CCCCCCCCCCHHHHH
19429919
1091PhosphorylationYDRIYSDSEEEKEYQ
CCCCCCCCHHHHHHH
19429919
1133PhosphorylationSLDKNLQSPNNIVKN
HHHHCCCCCCCCCCC
19429919

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 SET1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SET1_DROME !!

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 SET1_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H15_DROMEH15physical
25242320

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SET1_DROME

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Related Literatures of Post-Translational Modification

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