PTPA_HUMAN - dbPTM
PTPA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPA_HUMAN
UniProt AC Q15257
Protein Name Serine/threonine-protein phosphatase 2A activator
Gene Name PTPA {ECO:0000312|HGNC:HGNC:9308}
Organism Homo sapiens (Human).
Sequence Length 358
Subcellular Localization Cytoplasm . Nucleus .
Protein Description PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A..
Protein Sequence MAEGERQPPPDSSEEAPPATQNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFEYRVSEMWNEVHEEKEQAAKQSVSCDECIPLPRAGHCAPSEAIEKLVALLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDEEAENLVATVVPTHLAAAVPEVAVYLKESVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQIAIVFKVFNRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPYLEPRHFVDEKAVNENHKDYMFLECILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIHPVTSG
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
2Acetylation------MAEGERQPP
------CCCCCCCCC		33.2419413330
12PhosphorylationERQPPPDSSEEAPPA
CCCCCCCCCCCCCCC		45.4825159151
13PhosphorylationRQPPPDSSEEAPPAT
CCCCCCCCCCCCCCC		47.0025159151
27 (in isoform 1)Ubiquitination-53.2621906983
27 (in isoform 2)Ubiquitination-53.2621906983
27 (in isoform 3)Ubiquitination-53.2621906983
27 (in isoform 4)Ubiquitination-53.2621906983
27UbiquitinationTQNFIIPKKEIHTVP
CCCCEEEHHHCCCCC		53.2621906983
28UbiquitinationQNFIIPKKEIHTVPD
CCCEEEHHHCCCCCC		57.45-
36SulfoxidationEIHTVPDMGKWKRSQ
HCCCCCCCCCCHHHH		4.9430846556
38UbiquitinationHTVPDMGKWKRSQAY
CCCCCCCCCHHHHHH		42.79-
42 (in isoform 3)Phosphorylation-18.5530622161
54 (in isoform 3)Phosphorylation-23.7930622161
62AcetylationLNEGVKGKKLTFEYR
CCCCCCCCEEEEEEE		38.6019608861
63UbiquitinationNEGVKGKKLTFEYRV
CCCCCCCEEEEEEEH		62.52-
88PhosphorylationKEQAAKQSVSCDECI
HHHHHHHCCCCCCCC		18.4528555341
90PhosphorylationQAAKQSVSCDECIPL
HHHHHCCCCCCCCCC		22.5424719451
111AcetylationAPSEAIEKLVALLNT
CCHHHHHHHHHHHHH		41.99-
118PhosphorylationKLVALLNTLDRWIDE
HHHHHHHHHHHHHHC		29.97-
121MethylationALLNTLDRWIDETPP
HHHHHHHHHHHCCCC		35.05115488599
126PhosphorylationLDRWIDETPPVDQPS
HHHHHHCCCCCCCCC		29.1920068231
133PhosphorylationTPPVDQPSRFGNKAY
CCCCCCCCCCCCCHH		34.3120068231
138UbiquitinationQPSRFGNKAYRTWYA
CCCCCCCCHHHHHHH		47.37-
138AcetylationQPSRFGNKAYRTWYA
CCCCCCCCHHHHHHH		47.3725953088
141MethylationRFGNKAYRTWYAKLD
CCCCCHHHHHHHHCH		24.52115488593
186PhosphorylationGNSTRIDYGTGHEAA
CCCCEECCCCCHHHH		17.7628270605
188PhosphorylationSTRIDYGTGHEAAFA
CCEECCCCCHHHHHH		29.1828270605
200 (in isoform 4)Ubiquitination-5.6321906983
213 (in isoform 3)Ubiquitination-3.4821906983
223PhosphorylationVFKVFNRYLEVMRKL
HHHHHHHHHHHHHHH		14.3318083107
242 (in isoform 2)Ubiquitination-49.9321906983
254AcetylationLDDFQFLPFIWGSSQ
CCCCCCCHHHCCCCC		21.7019608861
260AcetylationLPFIWGSSQLIDHPY
CHHHCCCCCCCCCCC		25.6819608861
267AcetylationSQLIDHPYLEPRHFV
CCCCCCCCCCCCCCC		21.9319608861
273AcetylationPYLEPRHFVDEKAVN
CCCCCCCCCCHHHCC		8.6019608861
277UbiquitinationPRHFVDEKAVNENHK
CCCCCCHHHCCCCCC		53.852190698
277 (in isoform 1)Ubiquitination-53.8521906983
296AcetylationLECILFITEMKTGPF
HHHHHHHHHCCCCCC		23.7719608861
302AcetylationITEMKTGPFAEHSNQ
HHHCCCCCCHHHCCC		30.4219608861
321AcetylationSAVPSWSKVNQGLIR
ECCCCHHHHCHHHHH		38.6625953088
321UbiquitinationSAVPSWSKVNQGLIR
ECCCCHHHHCHHHHH		38.66-
331UbiquitinationQGLIRMYKAECLEKF
HHHHHHHHHHHHHHC		28.5019608861
331AcetylationQGLIRMYKAECLEKF
HHHHHHHHHHHHHHC		28.5023749302
331MalonylationQGLIRMYKAECLEKF
HHHHHHHHHHHHHHC		28.5026320211
337UbiquitinationYKAECLEKFPVIQHF
HHHHHHHHCCEEEEE		41.8619608861
337AcetylationYKAECLEKFPVIQHF
HHHHHHHHCCEEEEE		41.8623749302
345AcetylationFPVIQHFKFGSLLPI
CCEEEEEECCCEEEC		46.8425953088
345UbiquitinationFPVIQHFKFGSLLPI
CCEEEEEECCCEEEC		46.84-
356PhosphorylationLLPIHPVTSG-----
EEECCCCCCC-----		31.9828555341
357PhosphorylationLPIHPVTSG------
EECCCCCCC------		42.6228348404
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
-KUbiquitinationE3 ubiquitin ligaseMPGP29372
PMID:25207814
-KUbiquitinationE3 ubiquitin ligaseUBE3AQ05086
PMID:31160454
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPA_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 PTPA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTPA2_YEASTRRD2physical
12952889
CCNG1_HUMANCCNG1physical
8887688
P2R3A_HUMANPPP2R3Aphysical
18397887
H2AX_HUMANH2AFXphysical
16310392
H2A1_YEASTHTA1physical
16310392
CP17A_HUMANCYP17A1physical
12444089
HDAC4_HUMANHDAC4physical
18045992
TCPE_HUMANCCT5physical
19156129
TCPQ_HUMANCCT8physical
19156129
TCPB_HUMANCCT2physical
19156129
TCPD_HUMANCCT4physical
19156129
TCPH_HUMANCCT7physical
19156129
TCPG_HUMANCCT3physical
19156129
TCPA_HUMANTCP1physical
19156129
PP4C_HUMANPPP4Cphysical
19156129
PP2AA_HUMANPPP2CAphysical
19156129
MPCP_HUMANSLC25A3physical
19156129
TCPZ_HUMANCCT6Aphysical
19156129
MLRS_HUMANMYLPFphysical
19156129
MYCD_HUMANMYOCDphysical
19156129
MYH9_HUMANMYH9physical
19156129
PP2AA_HUMANPPP2CAphysical
19818709
MDM2_HUMANMDM2physical
22525275
PP2AA_HUMANPPP2CAphysical
22379092
AURKB_HUMANAURKBphysical
20593489
CYLD_HUMANCYLDphysical
20593489
STK26_HUMANSTK26physical
18782753
AKT1_HUMANAKT1physical
17505062
MP2K3_HUMANMAP2K3physical
17438131
TRI18_HUMANMID1physical
17438131
AKT1_HUMANAKT1physical
14645548
CAV1_HUMANCAV1physical
14645548
RGAP1_HUMANRACGAP1physical
18201571
A4_HUMANAPPphysical
21832049
IEX1_HUMANIER3physical
16456541
TAU_HUMANMAPTphysical
12435421
KPCB_HUMANPRKCBphysical
8749392
4EBP1_HUMANEIF4EBP1physical
18337751
AMOT_HUMANAMOTphysical
25416956
F110C_HUMANFAM110Cphysical
19698782
TBA1A_HUMANTUBA1Aphysical
19698782
PP4R2_HUMANPPP4R2physical
26186194
ANXA3_HUMANANXA3physical
26344197
BRNP1_HUMANBRINP1physical
26496610
CCNE1_HUMANCCNE1physical
28137908
PP4R2_HUMANPPP4R2physical
28514442
TF_HUMANF3physical
27599717
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 PTPA_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-62 AND LYS-337, AND MASSSPECTROMETRY.

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