dbPTM

DENR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DENR_HUMAN
UniProt AC	O43583
Protein Name	Density-regulated protein
Gene Name	DENR
Organism	Homo sapiens (Human).
Sequence Length	198
Subcellular Localization
Protein Description	May be involved in the translation of target mRNAs by scanning and recognition of the initiation codon. Involved in translation initiation; promotes recruitmnet of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Plays a role in the modulation of the translational profile of a subset of cancer-related mRNAs when recruited to the translational initiation complex by the oncogene MCTS1..
Protein Sequence	MAADISESSGADCKGDPRNSAKLDADYPLRVLYCGVCSLPTEYCEYMPDVAKCRQWLEKNFPNEFAKLTVENSPKQEAGISEGQGTAGEEEEKKKQKRGGRGQIKQKKKTVPQKVTIAKIPRAKKKYVTRVCGLATFEIDLKEAQRFFAQKFSCGASVTGEDEIIIQGDFTDDIIDVIQEKWPEVDDDSIEDLGEVKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAADISESS ------CCCCCCCCC	17.53	22223895
6	Phosphorylation	--MAADISESSGADC --CCCCCCCCCCCCC	31.79	30108239
8	Phosphorylation	MAADISESSGADCKG CCCCCCCCCCCCCCC	27.55	29507054
9	Phosphorylation	AADISESSGADCKGD CCCCCCCCCCCCCCC	33.67	25849741
14	Ubiquitination	ESSGADCKGDPRNSA CCCCCCCCCCCCCCC	67.88	-
20	Phosphorylation	CKGDPRNSAKLDADY CCCCCCCCCCCCCCC	28.23	25159151
22	Acetylation	GDPRNSAKLDADYPL CCCCCCCCCCCCCCC	46.88	25953088
22	Ubiquitination	GDPRNSAKLDADYPL CCCCCCCCCCCCCCC	46.88	-
27	Phosphorylation	SAKLDADYPLRVLYC CCCCCCCCCCEEEEE	13.09	20068231
59	Acetylation	KCRQWLEKNFPNEFA HHHHHHHHHCCCHHH	62.81	25953088
59	Ubiquitination	KCRQWLEKNFPNEFA HHHHHHHHHCCCHHH	62.81	21890473
69	Phosphorylation	PNEFAKLTVENSPKQ CCHHHHEEEECCCCH	25.68	22167270
73	Phosphorylation	AKLTVENSPKQEAGI HHEEEECCCCHHCCC	21.70	29255136
75	Ubiquitination	LTVENSPKQEAGISE EEEECCCCHHCCCCC	61.67	-
81	Phosphorylation	PKQEAGISEGQGTAG CCHHCCCCCCCCCCC	34.45	25159151
86	Phosphorylation	GISEGQGTAGEEEEK CCCCCCCCCCHHHHH	24.49	23401153
107	Ubiquitination	GRGQIKQKKKTVPQK CCCHHCCCCCCCCCC	51.76	-
119	2-Hydroxyisobutyrylation	PQKVTIAKIPRAKKK CCCEEEEECCCCCHH	49.76	-
189	Phosphorylation	WPEVDDDSIEDLGEV CCCCCCCCCHHHHCC	34.57	27251275
197	Ubiquitination	IEDLGEVKK------ CHHHHCCCC------	48.76	-
197	2-Hydroxyisobutyrylation	IEDLGEVKK------ CHHHHCCCC------	48.76	-

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 DENR_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DENR_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 DENR_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCTS1_HUMAN	MCTS1	physical	22939629
DMAP1_HUMAN	DMAP1	physical	22939629
NLRX1_HUMAN	NLRX1	physical	22939629
XRCC4_HUMAN	XRCC4	physical	22939629
HMGB3_HUMAN	HMGB3	physical	22863883
ROA2_HUMAN	HNRNPA2B1	physical	22863883
HNRPD_HUMAN	HNRNPD	physical	22863883
PP1B_HUMAN	PPP1CB	physical	22863883
RL10_HUMAN	RPL10	physical	22863883
UBXN1_HUMAN	UBXN1	physical	22863883
EIF2D_HUMAN	EIF2D	physical	26344197
MCTS1_HUMAN	MCTS1	physical	28514442
DOC11_HUMAN	DOCK11	physical	28514442
NTM1A_HUMAN	NTMT1	physical	28514442
RBCC1_HUMAN	RB1CC1	physical	28514442
ATG13_HUMAN	ATG13	physical	28514442
CSN5_HUMAN	COPS5	physical	28514442
DHTK1_HUMAN	DHTKD1	physical	28514442
NSUN4_HUMAN	NSUN4	physical	28514442
CSN2_HUMAN	COPS2	physical	28514442
AMZ2_HUMAN	AMZ2	physical	28514442
PDLI5_HUMAN	PDLIM5	physical	28514442
CSN7A_HUMAN	COPS7A	physical	28514442
TALDO_HUMAN	TALDO1	physical	28514442
CSN4_HUMAN	COPS4	physical	28514442
VDAC2_HUMAN	VDAC2	physical	28514442
CSN6_HUMAN	COPS6	physical	28514442
BTBD1_HUMAN	BTBD1	physical	28514442
CSN7B_HUMAN	COPS7B	physical	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 DENR_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-69; SER-73 AND THR-86, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-69; SER-73 AND THR-86, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-73, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69 AND SER-73, AND MASSSPECTROMETRY.	17287340 [Abstract]