DPY30_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DPY30_HUMAN
• UniProt AC: Q9C005
• Protein Name: Protein dpy-30 homolog
• Gene Name: DPY30
• Organism: Homo sapiens (Human).
• Sequence Length: 99
• Subcellular Localization: Nucleus . Golgi apparatus, trans-Golgi network . Associated with chromatin at regions enriched in histone H3 trimethylated at 'Lys-4. Highly enriched in gene promoter regions and 5' UTRs, but not in downstream regions of genes or 3' UTRs (By similari
• Protein Description: As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport..
• Protein Sequence: MEPEQMLEGQTQVAENPHSEYGLTDNVERIVENEKINAEKSSKQKVDLQSLPTRAYLDQTVVPILLQGLAVLAKERPPNPIEFLASYLLKNKAQFEDRN

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
1	Acetylation	-------MEPEQMLE -------CCHHHHHC	20.48	22814378
11	Phosphorylation	EQMLEGQTQVAENPH HHHHCCCCCCCCCCC	35.55	18491316
19	Phosphorylation	QVAENPHSEYGLTDN CCCCCCCCCCCCCCC	33.50	25159151
21	Phosphorylation	AENPHSEYGLTDNVE CCCCCCCCCCCCCHH	22.05	21406692
24	Phosphorylation	PHSEYGLTDNVERIV CCCCCCCCCCHHHHH	22.59	21406692
35	Acetylation	ERIVENEKINAEKSS HHHHHHHCCCCCHHC	53.49	19608861
35	Ubiquitination	ERIVENEKINAEKSS HHHHHHHCCCCCHHC	53.49	2190698
35	Sumoylation	ERIVENEKINAEKSS HHHHHHHCCCCCHHC	53.49	28112733
40	Acetylation	NEKINAEKSSKQKVD HHCCCCCHHCCCCCC	58.58	23749302
41	Phosphorylation	EKINAEKSSKQKVDL HCCCCCHHCCCCCCH	33.98	26714015
42	Phosphorylation	KINAEKSSKQKVDLQ CCCCCHHCCCCCCHH	50.61	26714015
45	Ubiquitination	AEKSSKQKVDLQSLP CCHHCCCCCCHHHCC	41.26	-
50	Phosphorylation	KQKVDLQSLPTRAYL CCCCCHHHCCCHHHC	43.54	22210691
56	Phosphorylation	QSLPTRAYLDQTVVP HHCCCHHHCCCCHHH	13.92	22210691
86	Phosphorylation	NPIEFLASYLLKNKA CHHHHHHHHHHHCHH	20.61	24719451
87	Phosphorylation	PIEFLASYLLKNKAQ HHHHHHHHHHHCHHH	15.50	24719451
90	Ubiquitination	FLASYLLKNKAQFED HHHHHHHHCHHHHCC	54.53	-
90	Acetylation	FLASYLLKNKAQFED HHHHHHHHCHHHHCC	54.53	26051181
92	2-Hydroxyisobutyrylation	ASYLLKNKAQFEDRN HHHHHHCHHHHCCCC	41.81	-
92	Acetylation	ASYLLKNKAQFEDRN HHHHHHCHHHHCCCC	41.81	27452117

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of DPY30_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DPY30_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DPY30_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DYDC1_HUMAN	DYDC1	physical	16189514
DPY30_HUMAN	DPY30	physical	16189514
DPY30_HUMAN	DPY30	physical	19481096
BIG1_HUMAN	ARFGEF1	physical	20668708
ASH2L_HUMAN	ASH2L	physical	22231628
PNPT1_HUMAN	PNPT1	physical	22939629
NU153_HUMAN	NUP153	physical	22939629
SETD7_HUMAN	SETD7	physical	22939629
LRRF1_HUMAN	LRRFIP1	physical	22939629
HCFC1_HUMAN	HCFC1	physical	22939629
LAMB1_HUMAN	LAMB1	physical	22939629
MEA1_HUMAN	MEA1	physical	22939629
HDAC2_HUMAN	HDAC2	physical	22939629
DPY30_HUMAN	DPY30	physical	25416956
SMD1_HUMAN	SNRPD1	physical	26344197
PRC2B_HUMAN	PRRC2B	physical	21516116
ASH2L_HUMAN	ASH2L	physical	21516116

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-35, AND MASS SPECTROMETRY.
PubMed: 19608861