dbPTM

ARP19_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARP19_HUMAN
UniProt AC	P56211
Protein Name	cAMP-regulated phosphoprotein 19
Gene Name	ARPP19
Organism	Homo sapiens (Human).
Sequence Length	112
Subcellular Localization	Cytoplasm.
Protein Description	Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression..
Protein Sequence	MSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPSLVASKLAG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1 (in isoform 2)	Acetylation	-	8.48	-
2	Phosphorylation	------MSAEVPEAA ------CCCCCCCCC	32.89	25159151
2	Acetylation	------MSAEVPEAA ------CCCCCCCCC	32.89	19413330
6 (in isoform 2)	Phosphorylation	-	19.60	25849741
7 (in isoform 2)	Phosphorylation	-	63.14	25849741
10	Phosphorylation	AEVPEAASAEEQKEM CCCCCCCCHHHHHHH	43.17	25159151
22	Phosphorylation	KEMEDKVTSPEKAEE HHHHHHCCCHHHHHH	44.28	29255136
23	Phosphorylation	EMEDKVTSPEKAEEA HHHHHCCCHHHHHHH	33.77	29255136
26	Acetylation	DKVTSPEKAEEAKLK HHCCCHHHHHHHHHH	65.56	19608861
31	Acetylation	PEKAEEAKLKARYPH HHHHHHHHHHHHCCC	54.52	7709657
33	Acetylation	KAEEAKLKARYPHLG HHHHHHHHHHCCCCC	30.06	18604429
35	Methylation	EEAKLKARYPHLGQK HHHHHHHHCCCCCCC	43.88	-
36	Phosphorylation	EAKLKARYPHLGQKP HHHHHHHCCCCCCCC	10.40	-
42 (in isoform 2)	Ubiquitination	-	43.78	21890473
42	Acetylation	RYPHLGQKPGGSDFL HCCCCCCCCCCCHHH	43.78	23749302
42	Ubiquitination	RYPHLGQKPGGSDFL HCCCCCCCCCCCHHH	43.78	-
46	Phosphorylation	LGQKPGGSDFLRKRL CCCCCCCCHHHHHHH	30.98	25159151
58	Ubiquitination	KRLQKGQKYFDSGDY HHHHHCCCHHCCCCH	57.46	21890473
58 (in isoform 1)	Ubiquitination	-	57.46	21890473
58	Acetylation	KRLQKGQKYFDSGDY HHHHHCCCHHCCCCH	57.46	88691
59	Phosphorylation	RLQKGQKYFDSGDYN HHHHCCCHHCCCCHH	12.53	22167270
62	Phosphorylation	KGQKYFDSGDYNMAK HCCCHHCCCCHHHHH	24.54	19664994
65	Phosphorylation	KYFDSGDYNMAKAKM CHHCCCCHHHHHHHH	15.46	25463755
69	Ubiquitination	SGDYNMAKAKMKNKQ CCCHHHHHHHHCCCC	37.46	2189047
71	Ubiquitination	DYNMAKAKMKNKQLP CHHHHHHHHCCCCCC	50.10	-
79	Phosphorylation	MKNKQLPTAAPDKTE HCCCCCCCCCCCCCC	44.00	20068231
84	Acetylation	LPTAAPDKTEVTGDH CCCCCCCCCCCCCCC	45.59	25953088
85	Phosphorylation	PTAAPDKTEVTGDHI CCCCCCCCCCCCCCC	42.97	26074081
88	Phosphorylation	APDKTEVTGDHIPTP CCCCCCCCCCCCCCC	30.57	26074081
94	Phosphorylation	VTGDHIPTPQDLPQR CCCCCCCCCCCCCCC	32.74	26074081
94	O-linked_Glycosylation	VTGDHIPTPQDLPQR CCCCCCCCCCCCCCC	32.74	OGP
102	Ubiquitination	PQDLPQRKPSLVASK CCCCCCCCHHHHHHH	33.44	-
104	Phosphorylation	DLPQRKPSLVASKLA CCCCCCHHHHHHHHC	38.21	23401153
108	Phosphorylation	RKPSLVASKLAG--- CCHHHHHHHHCC---	22.26	23927012
109	Acetylation	KPSLVASKLAG---- CHHHHHHHHCC----	32.39	19608861

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
46	S	Phosphorylation	Kinase	MAST3	O60307	PSP
62	S	Phosphorylation	Kinase	MASTL	Q96GX5	PSP
104	S	Phosphorylation	Kinase	PKACA	P17612	PSP
104	S	Phosphorylation	Kinase	PKG1	Q13976	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
62	S	Phosphorylation		-
Phosphorylation at Ser-62 by GWL during mitosis is essential for interaction with PPP2R2D (PR55-delta) and subsequent inactivation of PP2A (By similarity).

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 ARP19_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049

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 ARP19_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-109, AND MASS SPECTROMETRY.	19608861 [Abstract]

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