TAF6L_HUMAN - dbPTM
TAF6L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF6L_HUMAN
UniProt AC Q9Y6J9
Protein Name TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L
Gene Name TAF6L
Organism Homo sapiens (Human).
Sequence Length 622
Subcellular Localization Nucleus .
Protein Description Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex..
Protein Sequence MSEREERRFVEIPRESVRLMAESTGLELSDEVAALLAEDVCYRLREATQNSSQFMKHTKRRKLTVEDFNRALRWSSVEAVCGYGSQEALPMRPAREGELYFPEDREVNLVELALATNIPKGCAETAVRVHVSYLDGKGNLAPQGSVPSAVSSLTDDLLKYYHQVTRAVLGDDPQLMKVALQDLQTNSKIGALLPYFVYVVSGVKSVSHDLEQLHRLLQVARSLFRNPHLCLGPYVRCLVGSVLYCVLEPLAASINPLNDHWTLRDGAALLLSHIFWTHGDLVSGLYQHILLSLQKILADPVRPLCCHYGAVVGLHALGWKAVERVLYPHLSTYWTNLQAVLDDYSVSNAQVKADGHKVYGAILVAVERLLKMKAQAAEPNRGGPGGRGCRRLDDLPWDSLLFQESSSGGGAEPSFGSGLPLPPGGAGPEDPSLSVTLADIYRELYAFFGDSLATRFGTGQPAPTAPRPPGDKKEPAAAPDSVRKMPQLTASAIVSPHGDESPRGSGGGGPASASGPAASESRPLPRVHRARGAPRQQGPGTGTRDVFQKSRFAPRGAPHFRFIIAGRQAGRRCRGRLFQTAFPAPYGPSPASRYVQKLPMIGRTSRPARRWALSDYSLYLPL
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
16PhosphorylationFVEIPRESVRLMAES
HCCCCHHHHHHHHHH		17.5128555341
42PhosphorylationLLAEDVCYRLREATQ
HHHHHHHHHHHHHHC		16.72-
56UbiquitinationQNSSQFMKHTKRRKL
CCHHHHHHHHCCCCC		49.78-
62UbiquitinationMKHTKRRKLTVEDFN
HHHHCCCCCCHHHHH		53.17-
85PhosphorylationEAVCGYGSQEALPMR
HHHCCCCCCCCCCCC		19.1617525332
120UbiquitinationALATNIPKGCAETAV
HHHCCCCCCHHHHCE		63.93-
137UbiquitinationHVSYLDGKGNLAPQG
EEEEECCCCCCCCCC		44.27-
145PhosphorylationGNLAPQGSVPSAVSS
CCCCCCCCCCHHHHH		26.1320068231
148PhosphorylationAPQGSVPSAVSSLTD
CCCCCCCHHHHHCHH		38.8620068231
151PhosphorylationGSVPSAVSSLTDDLL
CCCCHHHHHCHHHHH		21.2420068231
152PhosphorylationSVPSAVSSLTDDLLK
CCCHHHHHCHHHHHH		28.7920068231
154PhosphorylationPSAVSSLTDDLLKYY
CHHHHHCHHHHHHHH		29.4320068231
177UbiquitinationGDDPQLMKVALQDLQ
CCCHHHHHHHHHHHH		32.7121906983
292PhosphorylationLYQHILLSLQKILAD
HHHHHHHHHHHHHCC		25.8824719451
327PhosphorylationKAVERVLYPHLSTYW
HHHHHHHHHHHHHHC		5.92-
333PhosphorylationLYPHLSTYWTNLQAV
HHHHHHHHCHHHHHH		13.58-
335PhosphorylationPHLSTYWTNLQAVLD
HHHHHHCHHHHHHHC		18.68-
344PhosphorylationLQAVLDDYSVSNAQV
HHHHHCCCCCCCEEE		15.61-
373UbiquitinationVERLLKMKAQAAEPN
HHHHHHHHHHHCCCC		35.44-
458PhosphorylationSLATRFGTGQPAPTA
HHHHHCCCCCCCCCC		29.9028634298
464PhosphorylationGTGQPAPTAPRPPGD
CCCCCCCCCCCCCCC		51.9428634298
472AcetylationAPRPPGDKKEPAAAP
CCCCCCCCCCCCCCC		66.0226051181
481PhosphorylationEPAAAPDSVRKMPQL
CCCCCCCHHHCCCCC		23.8225159151
489PhosphorylationVRKMPQLTASAIVSP
HHCCCCCCEEEEECC		17.2025850435
491PhosphorylationKMPQLTASAIVSPHG
CCCCCCEEEEECCCC		17.1930266825
495PhosphorylationLTASAIVSPHGDESP
CCEEEEECCCCCCCC		12.6930266825
501PhosphorylationVSPHGDESPRGSGGG
ECCCCCCCCCCCCCC		25.3330266825
505PhosphorylationGDESPRGSGGGGPAS
CCCCCCCCCCCCCCC		35.2322496350
512PhosphorylationSGGGGPASASGPAAS
CCCCCCCCCCCCCCC		26.5426074081
514PhosphorylationGGGPASASGPAASES
CCCCCCCCCCCCCCC		42.7026074081
519PhosphorylationSASGPAASESRPLPR
CCCCCCCCCCCCCCC		37.9126074081
521PhosphorylationSGPAASESRPLPRVH
CCCCCCCCCCCCCHH		36.3826074081
541PhosphorylationPRQQGPGTGTRDVFQ
CCCCCCCCCCHHHHH		38.2128555341
549UbiquitinationGTRDVFQKSRFAPRG
CCHHHHHHHCCCCCC		31.94-
555MethylationQKSRFAPRGAPHFRF
HHHCCCCCCCCCEEE		50.9424129315
555Asymmetric dimethylarginineQKSRFAPRGAPHFRF
HHHCCCCCCCCCEEE		50.94-
561Asymmetric dimethylargininePRGAPHFRFIIAGRQ
CCCCCCEEEEEECCC		20.86-
561MethylationPRGAPHFRFIIAGRQ
CCCCCCEEEEEECCC		20.8624129315
567MethylationFRFIIAGRQAGRRCR
EEEEEECCCCHHCCC		17.7254559813
567DimethylationFRFIIAGRQAGRRCR
EEEEEECCCCHHCCC		17.72-
586PhosphorylationQTAFPAPYGPSPASR
CCCCCCCCCCCHHHH		43.7229396449
589PhosphorylationFPAPYGPSPASRYVQ
CCCCCCCCHHHHHHH		28.8321815630
592PhosphorylationPYGPSPASRYVQKLP
CCCCCHHHHHHHCCC		27.7729396449
593MethylationYGPSPASRYVQKLPM
CCCCHHHHHHHCCCC		37.4324129315
593Asymmetric dimethylarginineYGPSPASRYVQKLPM
CCCCHHHHHHHCCCC		37.43-
594PhosphorylationGPSPASRYVQKLPMI
CCCHHHHHHHCCCCC		12.5322210691
597UbiquitinationPASRYVQKLPMIGRT
HHHHHHHCCCCCCCC		44.51-
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 TAF6L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAF6L_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 TAF6L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAF9B_HUMANTAF9Bphysical
25416956
ATX7_HUMANATXN7physical
28514442
ST65G_HUMANSUPT7Lphysical
28514442
KAT2B_HUMANKAT2Bphysical
28514442
SUPT3_HUMANSUPT3Hphysical
28514442
TAF9B_HUMANTAF9Bphysical
28514442
TAF12_HUMANTAF12physical
28514442
SP20H_HUMANSUPT20Hphysical
28514442
KAT2A_HUMANKAT2Aphysical
28514442
TAF9_HUMANTAF9physical
28514442
TAF10_HUMANTAF10physical
28514442
TRRAP_HUMANTRRAPphysical
28514442
STIP1_HUMANSTIP1physical
28514442
HSP7C_HUMANHSPA8physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TAF6L_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASSSPECTROMETRY.

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