DCPS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DCPS_HUMAN
• UniProt AC: Q96C86
• Protein Name: m7GpppX diphosphatase
• Gene Name: DCPS
• Organism: Homo sapiens (Human).
• Sequence Length: 337
• Subcellular Localization: Cytoplasm. Nucleus. Predominantly localized in the nucleus. Nucleocytoplasmic shuttling protein that can transiently enter the cytoplasm in mammalian cells in a XPO1/CRM1-dependent manner.
• Protein Description: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP.3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP' target='_blank'> [PubMed: 22985415 May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP]
• Protein Sequence: MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS

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
2	Acetylation	------MADAAPQLG ------CCCCHHHHC	18.36	22223895
10	Ubiquitination	DAAPQLGKRKRELDV CCHHHHCCCHHHCCH	64.44	-
10	Acetylation	DAAPQLGKRKRELDV CCHHHHCCCHHHCCH	64.44	23954790
24	Phosphorylation	VEEAHAASTEEKEAG HHHHHHCCHHHHHCC	36.82	29255136
25	Phosphorylation	EEAHAASTEEKEAGV HHHHHCCHHHHHCCC	43.36	29255136
36	Phosphorylation	EAGVGNGTCAPVRLP HCCCCCCCEECEECC	14.97	-
45	Phosphorylation	APVRLPFSGFRLQKV ECEECCCCCCHHHHH	34.77	24719451
60	2-Hydroxyisobutyrylation	LRESARDKIIFLHGK HHHHHCCCEEEEECE	31.95	-
72	Phosphorylation	HGKVNEASGDGDGED ECEECCCCCCCCCCC	31.10	28450419
99	Phosphorylation	EQVAQLLTGSPELQL HHHHHHHHCCCCCEE	44.18	24275569
101	Phosphorylation	VAQLLTGSPELQLQF HHHHHHCCCCCEEEE	15.23	-
128	Acetylation	PRQLNDVKTTVVYPA HHHCCCCCEEEEECC	41.14	23954790
128	Ubiquitination	PRQLNDVKTTVVYPA HHHCCCCCEEEEECC	41.14	21906983
138	Ubiquitination	VVYPATEKHLQKYLR EEECCCHHHHHHHHH	45.31	21890473
138	Acetylation	VVYPATEKHLQKYLR EEECCCHHHHHHHHH	45.31	19608861
142	Acetylation	ATEKHLQKYLRQDLR CCHHHHHHHHHHHHH	53.24	19608861
142	Ubiquitination	ATEKHLQKYLRQDLR CCHHHHHHHHHHHHH	53.24	19608861
197	Phosphorylation	VFENPDPSDGFVLIP EECCCCCCCCEEEEC	58.72	26074081
329	Ubiquitination	RADDPLLKLLQEAQQ ECCCHHHHHHHHHHH	55.63	2190698

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
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:25043029

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DCPS_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 DCPS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GPC5_HUMAN	GPC5	physical	21988832
ACOC_HUMAN	ACO1	physical	22863883
ASNS_HUMAN	ASNS	physical	22863883
ECHM_HUMAN	ECHS1	physical	22863883
G3P_HUMAN	GAPDH	physical	22863883
PSF3_HUMAN	GINS3	physical	22863883
SLD5_HUMAN	GINS4	physical	22863883
GSHB_HUMAN	GSS	physical	22863883
GRP78_HUMAN	HSPA5	physical	22863883
MOES_HUMAN	MSN	physical	22863883
PDC10_HUMAN	PDCD10	physical	22863883
ODPA_HUMAN	PDHA1	physical	22863883
PUR4_HUMAN	PFAS	physical	22863883
IPP2_HUMAN	PPP1R2	physical	22863883
PPP5_HUMAN	PPP5C	physical	22863883
VINC_HUMAN	VCL	physical	22863883
XPO1_HUMAN	XPO1	physical	22863883
CAH14_HUMAN	CA14	physical	26186194
FLNB_HUMAN	FLNB	physical	26344197

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 ALA-2, 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-138 AND LYS-142, AND MASSSPECTROMETRY.
PubMed: 19608861