dbPTM

PPR1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PPR1A_HUMAN
UniProt AC	Q13522
Protein Name	Protein phosphatase 1 regulatory subunit 1A
Gene Name	PPP1R1A
Organism	Homo sapiens (Human).
Sequence Length	171
Subcellular Localization
Protein Description	Inhibitor of protein-phosphatase 1. This protein may be important in hormonal control of glycogen metabolism. Hormones that elevate intracellular cAMP increase I-1 activity in many tissues. I-1 activation may impose cAMP control over proteins that are not directly phosphorylated by PKA. Following a rise in intracellular calcium, I-1 is inactivated by calcineurin (or PP2B). Does not inhibit type-2 phosphatases..
Protein Sequence	MEQDNSPRKIQFTVPLLEPHLDPEAAEQIRRRRPTPATLVLTSDQSSPEIDEDRIPNPHLKSTLAMSPRQRKKMTRITPTMKELQMMVEHHLGQQQQGEEPEGAAESTETQESRPPGIPDTEVESRLGTSGTAKKTAECIPKTHERGSKEPSTKEPSTHIPPLDSKGANSV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEQDNSPR -------CCCCCCCC	10.61	-
6	Phosphorylation	--MEQDNSPRKIQFT --CCCCCCCCEEEEE	34.08	22496350
35	Phosphorylation	QIRRRRPTPATLVLT HHHHHCCCCCEEEEC	24.60	10811908
38	Phosphorylation	RRRPTPATLVLTSDQ HHCCCCCEEEECCCC	20.71	28348404
42	Phosphorylation	TPATLVLTSDQSSPE CCCEEEECCCCCCCC	23.83	28348404
43	Phosphorylation	PATLVLTSDQSSPEI CCEEEECCCCCCCCC	29.50	28348404
46	Phosphorylation	LVLTSDQSSPEIDED EEECCCCCCCCCCCC	53.50	24719451
47	Phosphorylation	VLTSDQSSPEIDEDR EECCCCCCCCCCCCC	22.40	28348404
62	Phosphorylation	IPNPHLKSTLAMSPR CCCHHHHHHHCCCHH	34.71	26437602
67	Phosphorylation	LKSTLAMSPRQRKKM HHHHHCCCHHHHHHH	16.01	22617229
75	Phosphorylation	PRQRKKMTRITPTMK HHHHHHHHHCCCHHH	28.00	22817900
78	Phosphorylation	RKKMTRITPTMKELQ HHHHHHCCCHHHHHH	14.93	27251275
80	Phosphorylation	KMTRITPTMKELQMM HHHHCCCHHHHHHHH	32.02	22210691
143	Phosphorylation	TAECIPKTHERGSKE HHHCCCCCCCCCCCC	24.50	-
148	Phosphorylation	PKTHERGSKEPSTKE CCCCCCCCCCCCCCC	39.81	-

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
35	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
35	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
35	T	Phosphorylation	Kinase	PKA	-	Uniprot
67	S	Phosphorylation	Kinase	CDK5	Q02399	PSP
67	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
67	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
75	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
75	T	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
35	T	Phosphorylation		8611507
Phosphorylation of Thr-35 is required for activity.

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 PPR1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PR15A_HUMAN	PPP1R15A	physical	11564868
PP1A_RABIT	PPP1CA	physical	11564868
PP1B_RABIT	PPP1CB	physical	11564868
ACTA_HUMAN	ACTA2	physical	26186194
ACTS_HUMAN	ACTA1	physical	26186194
JMY_HUMAN	JMY	physical	26186194
ACTS_HUMAN	ACTA1	physical	28514442
JMY_HUMAN	JMY	physical	28514442
ACTA_HUMAN	ACTA2	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 PPR1A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Growth arrest and DNA damage-inducible protein GADD34 assembles anovel signaling complex containing protein phosphatase 1 and inhibitor1."; Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.; Mol. Cell. Biol. 21:6841-6850(2001). Cited for: INTERACTION WITH PPP1R15A, AND PHOSPHORYLATION AT THR-35.	11564868 [Abstract]