SETB2_HUMAN - dbPTM
SETB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SETB2_HUMAN
UniProt AC Q96T68
Protein Name Histone-lysine N-methyltransferase SETDB2
Gene Name SETDB2
Organism Homo sapiens (Human).
Sequence Length 719
Subcellular Localization Nucleus . Chromosome .
Protein Description Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Contributes to H3K9me3 in both the interspersed repetitive elements and centromere-associated repeats. Plays a role in chromosome condensation and segregation during mitosis..
Protein Sequence MGEKNGDAKTFWMELEDDGKVDFIFEQVQNVLQSLKQKIKDGSATNKEYIQAMILVNEATIINSSTSIKGASQKEVNAQSSDPMPVTQKEQENKSNAFPSTSCENSFPEDCTFLTTENKEILSLEDKVVDFREKDSSSNLSYQSHDCSGACLMKMPLNLKGENPLQLPIKCHFQRRHAKTNSHSSALHVSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSFNTYVQLARNYPKQKEVVSDVDISNGVESVPISFCNEIDSRKLPQFKYRKTVWPRAYNLTNFSSMFTDSCDCSEGCIDITKCACLQLTARNAKTSPLSSDKITTGYKYKRLQRQIPTGIYECSLLCKCNRQLCQNRVVQHGPQVRLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANTEKSYGIDENGRDENTMKNIFSKKRKLEVACSDCEVEVLPLGLETHPRTAKTEKCPPKFSNNPKELTVETKYDNISRIQYHSVIRDPESKTAIFQHNGKKMEFVSSESVTPEDNDGFKPPREHLNSKTKGAQKDSSSNHVDEFEDNLLIESDVIDITKYREETPPRSRCNQATTLDNQNIKKAIEVQIQKPQEGRSTACQRQQVFCDEELLSETKNTSSDSLTKFNKGNVFLLDATKEGNVGRFLNHSCCPNLLVQNVFVETHNRNFPLVAFFTNRYVKARTELTWDYGYEAGTVPEKEIFCQCGVNKCRKKIL
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
49 (in isoform 2)Phosphorylation-10.4322210691
80PhosphorylationQKEVNAQSSDPMPVT
HHHHCCCCCCCCCCC		34.0129759185
81PhosphorylationKEVNAQSSDPMPVTQ
HHHCCCCCCCCCCCH		33.3829759185
87PhosphorylationSSDPMPVTQKEQENK
CCCCCCCCHHHHCCC		28.2229759185
115UbiquitinationPEDCTFLTTENKEIL
CCCCEEEECCCCEEE		28.0729967540
123PhosphorylationTENKEILSLEDKVVD
CCCCEEEECCCEEEC		35.0626714015
127UbiquitinationEILSLEDKVVDFREK
EEEECCCEEECCHHH		34.4829967540
136PhosphorylationVDFREKDSSSNLSYQ
ECCHHHCCCCCCCCC		46.8928450419
137PhosphorylationDFREKDSSSNLSYQS
CCHHHCCCCCCCCCC		33.1228450419
138PhosphorylationFREKDSSSNLSYQSH
CHHHCCCCCCCCCCC		45.8228450419
141PhosphorylationKDSSSNLSYQSHDCS
HCCCCCCCCCCCCCC		25.9428450419
142PhosphorylationDSSSNLSYQSHDCSG
CCCCCCCCCCCCCCC		19.7328450419
144PhosphorylationSSNLSYQSHDCSGAC
CCCCCCCCCCCCCCE		17.0428450419
148PhosphorylationSYQSHDCSGACLMKM
CCCCCCCCCCEEEEC		35.1728450419
180PhosphorylationFQRRHAKTNSHSSAL
EECCCCCCCCCCCEE		42.6130576142
182PhosphorylationRRHAKTNSHSSALHV
CCCCCCCCCCCEEEE		29.9430576142
184PhosphorylationHAKTNSHSSALHVSY
CCCCCCCCCEEEEEE		19.6827461979
185PhosphorylationAKTNSHSSALHVSYK
CCCCCCCCEEEEEEE		29.4427461979
190PhosphorylationHSSALHVSYKTPCGR
CCCEEEEEEECCCCC		15.3427461979
191PhosphorylationSSALHVSYKTPCGRS
CCEEEEEEECCCCCC		20.1430576142
317PhosphorylationLTARNAKTSPLSSDK
HHHCCCCCCCCCCCC		32.9223312004
318PhosphorylationTARNAKTSPLSSDKI
HHCCCCCCCCCCCCC		24.1228348404
321PhosphorylationNAKTSPLSSDKITTG
CCCCCCCCCCCCCCC		39.6223312004
322PhosphorylationAKTSPLSSDKITTGY
CCCCCCCCCCCCCCH		51.0823312004
326PhosphorylationPLSSDKITTGYKYKR
CCCCCCCCCCHHHHH		21.6523312004
327PhosphorylationLSSDKITTGYKYKRL
CCCCCCCCCHHHHHH		41.8223312004
329PhosphorylationSDKITTGYKYKRLQR
CCCCCCCHHHHHHHH		14.7323312004
373AcetylationQVRLQVFKTEQKGWG
EEEEEEEECCCCCCE		52.9088471
408AcetylationLSRANTEKSYGIDEN
HHHCCCCCCCCCCCC		47.117987881
409PhosphorylationSRANTEKSYGIDENG
HHCCCCCCCCCCCCC		23.5126714015
427PhosphorylationNTMKNIFSKKRKLEV
HHHHHHHCCCCCCEE		33.2124719451
437PhosphorylationRKLEVACSDCEVEVL
CCCEEECCCCEEEEE		35.2430108239
475PhosphorylationPKELTVETKYDNISR
CCCEEEEECCCCCCE		30.48-
477PhosphorylationELTVETKYDNISRIQ
CEEEEECCCCCCEEE		22.95-
495MethylationVIRDPESKTAIFQHN
EECCCCCCEEEEEEC		40.07-
496PhosphorylationIRDPESKTAIFQHNG
ECCCCCCEEEEEECC		33.9723532336
504MethylationAIFQHNGKKMEFVSS
EEEEECCEEEEEEEC		55.02-
510PhosphorylationGKKMEFVSSESVTPE
CEEEEEEECCCCCCC		33.4426714015
511PhosphorylationKKMEFVSSESVTPED
EEEEEEECCCCCCCC		28.7026714015
513PhosphorylationMEFVSSESVTPEDND
EEEEECCCCCCCCCC		32.9923532336
515PhosphorylationFVSSESVTPEDNDGF
EEECCCCCCCCCCCC		30.1826714015
564PhosphorylationDVIDITKYREETPPR
CEEEHHHCCCCCCCC		18.01-
568PhosphorylationITKYREETPPRSRCN
HHHCCCCCCCCCCCC		33.5623186163
687PhosphorylationNRYVKARTELTWDYG
CCCCCCCEEEEECCC		39.9625262027
690PhosphorylationVKARTELTWDYGYEA
CCCCEEEEECCCCCC		15.2825262027
693PhosphorylationRTELTWDYGYEAGTV
CEEEEECCCCCCCCC		17.1125262027
695PhosphorylationELTWDYGYEAGTVPE
EEEECCCCCCCCCCH		9.0725262027
699PhosphorylationDYGYEAGTVPEKEIF
CCCCCCCCCCHHHEE		39.6825262027
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 SETB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SETB2_HUMAN !!
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 SETB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AL14E_HUMANARL14EPphysical
25416956
AL14E_HUMANARL14EPphysical
28514442
SENP7_HUMANSENP7physical
28514442
ZN445_HUMANZNF445physical
28514442
DHX16_HUMANDHX16physical
28514442
SBP1_HUMANSELENBP1physical
28514442
DUS14_HUMANDUSP14physical
28514442
DSG4_HUMANDSG4physical
28514442
LYG2_HUMANLYG2physical
28514442
HPHL1_HUMANHEPHL1physical
28514442
LRC15_HUMANLRRC15physical
28514442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SETB2_HUMAN

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Related Literatures of Post-Translational Modification

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