SETD7_HUMAN - dbPTM
SETD7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SETD7_HUMAN
UniProt AC Q8WTS6
Protein Name Histone-lysine N-methyltransferase SETD7
Gene Name SETD7
Organism Homo sapiens (Human).
Sequence Length 366
Subcellular Localization Nucleus. Chromosome .
Protein Description Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation..
Protein Sequence MDSDDEMVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESERVYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAPEWYQVELKAFQATQQK
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
3Phosphorylation-----MDSDDEMVEE
-----CCCHHHHHHH
45.7425849741
45UbiquitinationGNFVHGEKNGRGKFF
CCEECCEECCCEEEE
70.10-
85PhosphorylationDGGVLQGTYVDGELN
CCCEEEEEEECCCCC
13.8622468782
86PhosphorylationGGVLQGTYVDGELNG
CCEEEEEEECCCCCC
11.9022468782
111UbiquitinationLIFKGQYKDNIRHGV
EEEEEECCCCCCEEE
36.09-
152MethylationAYVYPDERTALYGKF
EEECCCCCCEEEEEE
32.45115916529
158UbiquitinationERTALYGKFIDGEMI
CCCEEEEEECCCEEE
26.11-
224PhosphorylationYVAESLISSAGEGLF
HHHHHHHHHCCCCCC
21.3028348404
225PhosphorylationVAESLISSAGEGLFS
HHHHHHHHCCCCCCC
33.0428348404
232PhosphorylationSAGEGLFSKVAVGPN
HCCCCCCCEEEECCC
31.1224719451
305PhosphorylationSFTPNCIYDMFVHPR
CCCCCCEEEECCCCC
11.98-
332PhosphorylationVEADEELTVAYGYDH
EECCCEEEEEECCCC
13.3321712546
335PhosphorylationDEELTVAYGYDHSPP
CCEEEEEECCCCCCC
16.3321712546
337PhosphorylationELTVAYGYDHSPPGK
EEEEEECCCCCCCCC
9.6021712546
340PhosphorylationVAYGYDHSPPGKSGP
EEECCCCCCCCCCCC
29.8625159151
345PhosphorylationDHSPPGKSGPEAPEW
CCCCCCCCCCCCCCE
66.5525159151
358UbiquitinationEWYQVELKAFQATQQ
CEEEEHHHHHHHHHC
33.38-

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 SETD7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SETD7_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 SETD7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LMBL1_HUMANL3MBTL1physical
18408754
DNMT1_HUMANDNMT1physical
19282482
TF65_HUMANRELAphysical
19262565
TF65_HUMANRELAphysical
19864627
P53_HUMANTP53physical
17108971
TF65_HUMANRELAphysical
18650421
TAF10_HUMANTAF10physical
16415881
H31_HUMANHIST1H3Aphysical
16415881
ESR1_HUMANESR1physical
18471979
H31_HUMANHIST1H3Aphysical
11779497
P53_HUMANTP53physical
15525938
H31_HUMANHIST1H3Aphysical
15525938
TAF10_HUMANTAF10physical
15099517
TBP_HUMANTBPphysical
15099517
TAF7_HUMANTAF7physical
15099517
TAF6_HUMANTAF6physical
15099517
E2F1_HUMANE2F1physical
20603083
SIR1_HUMANSIRT1physical
21245319
DNMT1_HUMANDNMT1physical
21151116
MYPT1_HUMANPPP1R12Aphysical
21115810
E2F1_HUMANE2F1physical
21320024
H31T_HUMANHIST3H3physical
21273441
ANDR_HUMANARphysical
21273441
TF65_HUMANRELAphysical
21131967
STAT3_HUMANSTAT3physical
21098664
H33_HUMANH3F3Aphysical
17166833
SMCA4_HUMANSMARCA4physical
22403242
H31_HUMANHIST1H3Aphysical
22403242
MYOD1_HUMANMYOD1physical
21859860
E2F1_HUMANE2F1physical
22836579
P53_HUMANTP53physical
21988832
STEA3_HUMANSTEAP3physical
21988832
SOX2_HUMANSOX2physical
25042802
H31T_HUMANHIST3H3physical
25042802
KLF4_HUMANKLF4physical
25042802
ESR1_HUMANESR1physical
24101509
SETD7_HUMANSETD7physical
24101509
SMAD7_HUMANSMAD7physical
27292644
RN111_HUMANRNF111physical
27292644
SMUF1_HUMANSMURF1physical
27292644
SMUF2_HUMANSMURF2physical
27292644

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SETD7_HUMAN

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Related Literatures of Post-Translational Modification

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