PP14A_HUMAN - dbPTM
PP14A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP14A_HUMAN
UniProt AC Q96A00
Protein Name Protein phosphatase 1 regulatory subunit 14A
Gene Name PPP1R14A
Organism Homo sapiens (Human).
Sequence Length 147
Subcellular Localization Cytoplasm.
Protein Description Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction..
Protein Sequence MAAQRLGKRVLSKLQSPSRARGPGGSPGGLQKRHARVTVKYDRRELQRRLDVEKWIDGRLEELYRGMEADMPDEINIDELLELESEEERSRKIQGLLKSCGKPVEDFIQELLAKLQGLHRQPGLRQPSPSHDGSLSPLQDRARTAHP
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 Orthologous
Protein Cluster
5Methylation---MAAQRLGKRVLS
---CHHHHHHHHHHH
40.45115488467
12PhosphorylationRLGKRVLSKLQSPSR
HHHHHHHHHCCCCCC
28.5911287002
16PhosphorylationRVLSKLQSPSRARGP
HHHHHCCCCCCCCCC
34.9727422710
18PhosphorylationLSKLQSPSRARGPGG
HHHCCCCCCCCCCCC
43.7626434776
19MethylationSKLQSPSRARGPGGS
HHCCCCCCCCCCCCC
31.52115488477
21MethylationLQSPSRARGPGGSPG
CCCCCCCCCCCCCCC
51.2116287989
26PhosphorylationRARGPGGSPGGLQKR
CCCCCCCCCCCCCHH
26.7023401153
32MethylationGSPGGLQKRHARVTV
CCCCCCCHHCCEEEE
51.71116253377
32UbiquitinationGSPGGLQKRHARVTV
CCCCCCCHHCCEEEE
51.7132142685
38PhosphorylationQKRHARVTVKYDRRE
CHHCCEEEEEECHHH
13.0118835557
40MethylationRHARVTVKYDRRELQ
HCCEEEEEECHHHHH
31.8772605009
40UbiquitinationRHARVTVKYDRRELQ
HCCEEEEEECHHHHH
31.8733845483
64 (in isoform 2)Phosphorylation-14.3820068231
101PhosphorylationQGLLKSCGKPVEDFI
HHHHHHCCCCHHHHH
44.3832142685
107PhosphorylationCGKPVEDFIQELLAK
CCCCHHHHHHHHHHH
3.8232142685
109PhosphorylationKPVEDFIQELLAKLQ
CCHHHHHHHHHHHHC
34.9733259812
128PhosphorylationQPGLRQPSPSHDGSL
CCCCCCCCCCCCCCC
30.6023401153
130PhosphorylationGLRQPSPSHDGSLSP
CCCCCCCCCCCCCCH
38.2522617229
134PhosphorylationPSPSHDGSLSPLQDR
CCCCCCCCCCHHHHH
31.5628355574
136PhosphorylationPSHDGSLSPLQDRAR
CCCCCCCCHHHHHHH
25.8423401153

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
12SPhosphorylationKinaseDAPK3O43293
PSP
38TPhosphorylationKinasePRKCEQ02156
GPS
38TPhosphorylationKinasePKA_GROUP-PhosphoELM
38TPhosphorylationKinasePKC-Uniprot
38TPhosphorylationKinasePKG-FAMILY-GPS
38TPhosphorylationKinasePKA-FAMILY-GPS
38TPhosphorylationKinaseROCK2O75116
PSP
38TPhosphorylationKinasePKD1P98161
PhosphoELM
38TPhosphorylationKinasePRKCZQ05513
GPS
38TPhosphorylationKinasePRKD1Q15139
PSP
38TPhosphorylationKinasePRKCDQ05655
GPS
38TPhosphorylationKinasePRKCAP17252
GPS
38TPhosphorylationKinasePRKG1Q13976
GPS
38TPhosphorylationKinasePRKACAP17612
GPS
38TPhosphorylationKinaseILKQ13418
PSP
38TPhosphorylationKinaseDAPK3O43293
PSP
130SPhosphorylationKinaseCAMK2-FAMILY-GPS
130SPhosphorylationKinaseKCC2AQ9UQM7
PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PP14A_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 PP14A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
KPCA_HUMANPRKCAphysical
15003508
KPCE_HUMANPRKCEphysical
15003508
KPCL_HUMANPRKCHphysical
15003508
KPCZ_HUMANPRKCZphysical
15003508
KPCD1_HUMANPRKD1physical
15003508
KC1A_HUMANCSNK1A1physical
15003508
KC1E_HUMANCSNK1Ephysical
15003508
1433Z_HUMANYWHAZphysical
15003508
KC1D_HUMANCSNK1Dphysical
15003508
KC1G1_HUMANCSNK1G1physical
15003508
KC1G2_HUMANCSNK1G2physical
15003508
KC1G3_HUMANCSNK1G3physical
15003508

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 PP14A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-128; SER-134 ANDSER-136, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-128 AND SER-136,AND MASS SPECTROMETRY.

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