EAF6_HUMAN - dbPTM
EAF6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EAF6_HUMAN
UniProt AC Q9HAF1
Protein Name Chromatin modification-related protein MEAF6
Gene Name MEAF6 {ECO:0000312|HGNC:HGNC:25674}
Organism Homo sapiens (Human).
Sequence Length 191
Subcellular Localization Nucleus, nucleolus . Chromosome, centromere, kinetochore .
Protein Description Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity..
Protein Sequence MAMHNKAAPPQIPDTRRELAELVKRKQELAETLANLERQIYAFEGSYLEDTQMYGNIIRGWDRYLTNQKNSNSKNDRRNRKFKEAERLFSKSSVTSAAAVSALAGVQDQLIEKREPGSGTESDTSPDFHNQENEPSQEDPEDLDGSVQGVKPQKAASSTSSGSHHSSHKKRKNKNRHRIDLKLNKKPRADY
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------MAMHNKAAP
------CCCCCCCCC		14.13-
6Ubiquitination--MAMHNKAAPPQIP
--CCCCCCCCCCCCC		31.11-
24 (in isoform 3)Ubiquitination-67.51-
24UbiquitinationRELAELVKRKQELAE
HHHHHHHHHHHHHHH		67.5132015554
26UbiquitinationLAELVKRKQELAETL
HHHHHHHHHHHHHHH		42.2729967540
26 (in isoform 3)Ubiquitination-42.27-
66PhosphorylationRGWDRYLTNQKNSNS
HHHHHHHHCCCCCCC		27.0327174698
69SumoylationDRYLTNQKNSNSKND
HHHHHCCCCCCCHHH		65.5028112733
69AcetylationDRYLTNQKNSNSKND
HHHHHCCCCCCCHHH		65.5019608861
69UbiquitinationDRYLTNQKNSNSKND
HHHHHCCCCCCCHHH		65.5027667366
69 (in isoform 3)Acetylation-65.50-
71PhosphorylationYLTNQKNSNSKNDRR
HHHCCCCCCCHHHHH		49.9020068231
71 (in isoform 3)Phosphorylation-49.90-
73PhosphorylationTNQKNSNSKNDRRNR
HCCCCCCCHHHHHHH		32.4327174698
74AcetylationNQKNSNSKNDRRNRK
CCCCCCCHHHHHHHH		68.0919608861
74 (in isoform 3)Acetylation-68.09-
74UbiquitinationNQKNSNSKNDRRNRK
CCCCCCCHHHHHHHH		68.0924816145
81AcetylationKNDRRNRKFKEAERL
HHHHHHHHHHHHHHH		65.4226051181
83AcetylationDRRNRKFKEAERLFS
HHHHHHHHHHHHHHC		60.0826051181
90PhosphorylationKEAERLFSKSSVTSA
HHHHHHHCCCHHHHH		35.9024719451
91UbiquitinationEAERLFSKSSVTSAA
HHHHHHCCCHHHHHH		39.1432015554
91 (in isoform 3)Acetylation-39.14-
91AcetylationEAERLFSKSSVTSAA
HHHHHHCCCHHHHHH		39.1419608861
101PhosphorylationVTSAAAVSALAGVQD
HHHHHHHHHHHCCHH		16.91-
113UbiquitinationVQDQLIEKREPGSGT
CHHHHHHHCCCCCCC		55.8832015554
113 (in isoform 3)Ubiquitination-55.88-
113SumoylationVQDQLIEKREPGSGT
CHHHHHHHCCCCCCC		55.88-
113SumoylationVQDQLIEKREPGSGT
CHHHHHHHCCCCCCC		55.8825114211
118PhosphorylationIEKREPGSGTESDTS
HHHCCCCCCCCCCCC		53.9426503892
118 (in isoform 3)Phosphorylation-53.9421406692
120PhosphorylationKREPGSGTESDTSPD
HCCCCCCCCCCCCCC		33.7326503892
120 (in isoform 3)Phosphorylation-33.7321406692
122 (in isoform 3)Phosphorylation-46.1321406692
122PhosphorylationEPGSGTESDTSPDFH
CCCCCCCCCCCCCCC		46.1330278072
124PhosphorylationGSGTESDTSPDFHNQ
CCCCCCCCCCCCCCC		51.9830278072
124 (in isoform 3)Phosphorylation-51.9821406692
125PhosphorylationSGTESDTSPDFHNQE
CCCCCCCCCCCCCCC		27.7130278072
125 (in isoform 3)Phosphorylation-27.7121406692
136PhosphorylationHNQENEPSQEDPEDL
CCCCCCCCCCCHHHC		39.7717525332
136 (in isoform 3)Phosphorylation-39.7721406692
146PhosphorylationDPEDLDGSVQGVKPQ
CHHHCCCCCCCCCCC		15.7823927012
146 (in isoform 3)Phosphorylation-15.7821406692
151AcetylationDGSVQGVKPQKAASS
CCCCCCCCCCCCCCC		48.8623236377
160PhosphorylationQKAASSTSSGSHHSS
CCCCCCCCCCCCCCH		34.35-
167PhosphorylationSSGSHHSSHKKRKNK
CCCCCCCHHCCCCCC		34.66-
169AcetylationGSHHSSHKKRKNKNR
CCCCCHHCCCCCCCC		57.1130583989
178 (in isoform 2)Phosphorylation-22.3727732954
178 (in isoform 3)Phosphorylation-22.3724117733
180 (in isoform 2)Phosphorylation-37.3927732954
180 (in isoform 3)Phosphorylation-37.3924117733
182AcetylationNRHRIDLKLNKKPRA
CCCCCCCCCCCCCCC		46.3925953088
185 (in isoform 2)Phosphorylation-74.6827732954
185UbiquitinationRIDLKLNKKPRADY-
CCCCCCCCCCCCCC-		74.6824816145
195UbiquitinationRADY-----------
CCCC-----------		24816145
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 EAF6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EAF6_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 EAF6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LMBL2_HUMANL3MBTL2physical
16189514
JADE1_HUMANJADE1physical
22144582
PKHF2_HUMANPLEKHF2physical
25416956
KAT7_HUMANKAT7physical
28514442
JADE2_HUMANJADE2physical
28514442
KAT5_HUMANKAT5physical
28514442
JADE3_HUMANJADE3physical
28514442
ING4_HUMANING4physical
28514442
JADE1_HUMANJADE1physical
28514442
ING5_HUMANING5physical
28514442
BRPF3_HUMANBRPF3physical
28514442
KAT6B_HUMANKAT6Bphysical
28514442
BRPF1_HUMANBRPF1physical
28514442
MO4L1_HUMANMORF4L1physical
28514442
ING3_HUMANING3physical
28514442
JAZF1_HUMANJAZF1physical
28514442
EPC1_HUMANEPC1physical
28514442
MRGBP_HUMANMRGBPphysical
28514442
DAPK3_HUMANDAPK3physical
28514442
KAT6A_HUMANKAT6Aphysical
28514442
EP400_HUMANEP400physical
28514442
YETS4_HUMANYEATS4physical
28514442
EPC2_HUMANEPC2physical
28514442
RUVB1_HUMANRUVBL1physical
28514442
RUVB2_HUMANRUVBL2physical
28514442
SESD1_HUMANSESTD1physical
28514442
MBTD1_HUMANMBTD1physical
28514442
TRRAP_HUMANTRRAPphysical
28514442
MO4L2_HUMANMORF4L2physical
28514442
DMAP1_HUMANDMAP1physical
28514442
BRD8_HUMANBRD8physical
28514442
VPS72_HUMANVPS72physical
28514442
KIF23_HUMANKIF23physical
28514442
IMA7_HUMANKPNA6physical
28514442
TPD52_HUMANTPD52physical
28514442
KBTB6_HUMANKBTBD6physical
28514442
UBP7_HUMANUSP7physical
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 EAF6_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-69; LYS-74 AND LYS-91, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; THR-120 ANDSER-122, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND MASSSPECTROMETRY.
"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-136, AND MASSSPECTROMETRY.

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