PR15A_HUMAN - dbPTM
PR15A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PR15A_HUMAN
UniProt AC O75807
Protein Name Protein phosphatase 1 regulatory subunit 15A
Gene Name PPP1R15A
Organism Homo sapiens (Human).
Sequence Length 674
Subcellular Localization Endoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side . Mitochondrion outer membrane
Peripheral membrane protein
Cytoplasmic side . Associates with membranes via an N-terminal amphipathic intramembrane region.
Protein Description Recruits the serine/threonine-protein phosphatase PP1 to dephosphorylate the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'..
Protein Sequence MAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLAIPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPGEEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVSPRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAAEKDGEAECPPCIPPPSAFLKAWVYWPGEDTEEEEDEEEDEDSDSGSDEEEGEAEASSSTPATGVFLKSWVYQPGEDTEEEEDEDSDTGSAEDEREAETSASTPPASAFLKAWVYRPGEDTEEEEDEDVDSEDKEDDSEAALGEAESDPHPSHPDQRAHFRGWGYRPGKETEEEEAAEDWGEAEPCPFRVAIYVPGEKPPPPWAPPRLPLRLQRRLKRPETPTHDPDPETPLKARKVRFSEKVTVHFLAVWAGPAQAARQGPWEQLARDRSRFARRITQAQEELSPCLTPAARARAWARLRNPPLAPIPALTQTLPSSSVPSSPVQTTPLSQAVATPSRSSAAAAAALDLSGRRG
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
118PhosphorylationLDDDDGMYGEREATS
CCCCCCCCCCEECCC		22.7422210691
132PhosphorylationSVPRGQGSQFADGQR
CCCCCCCCCCCCCCC		17.7823312004
143PhosphorylationDGQRAPLSPSLLIRT
CCCCCCCCHHHHHHH		16.0429255136
145PhosphorylationQRAPLSPSLLIRTLQ
CCCCCCHHHHHHHHC		32.2229978859
206PhosphorylationVKKEAHRTSTSALSP
HHHHHHHCCCCCCCC		26.8723312004
207PhosphorylationKKEAHRTSTSALSPG
HHHHHHCCCCCCCCC		21.9623312004
208PhosphorylationKEAHRTSTSALSPGS
HHHHHCCCCCCCCCC		19.8723312004
209PhosphorylationEAHRTSTSALSPGSK
HHHHCCCCCCCCCCC		27.2923312004
212PhosphorylationRTSTSALSPGSKPST
HCCCCCCCCCCCCCC		27.2523312004
215PhosphorylationTSALSPGSKPSTWVS
CCCCCCCCCCCCEEE		44.7923312004
218PhosphorylationLSPGSKPSTWVSCPG
CCCCCCCCCEEECCC		38.3423312004
219PhosphorylationSPGSKPSTWVSCPGE
CCCCCCCCEEECCCC		38.1123312004
222PhosphorylationSKPSTWVSCPGEEEN
CCCCCEEECCCCHHC		13.2223312004
232PhosphorylationGEEENQATEDKRTER
CCHHCCCCCCHHHHH		34.6523312004
237PhosphorylationQATEDKRTERSKGAR
CCCCCHHHHHHHCCC		41.3023312004
247PhosphorylationSKGARKTSVSPRSSG
HHCCCCCCCCCCCCC		24.51-
249PhosphorylationGARKTSVSPRSSGSD
CCCCCCCCCCCCCCC		17.86-
262PhosphorylationSDPRSWEYRSGEASE
CCCCCCCCCCCCCCH		12.1022817900
264PhosphorylationPRSWEYRSGEASEEK
CCCCCCCCCCCCHHH		39.8322817900
307PhosphorylationKSWWCQPSDEEEGEV
CCCCCCCCCCCCCCE		31.6025159151
388PhosphorylationATGVFLKSWVYQPGE
CCEEEEEEEEECCCC		24.7522468782
391PhosphorylationVFLKSWVYQPGEDTE
EEEEEEEECCCCCCC		11.6122468782
405PhosphorylationEEEEDEDSDTGSAED
CHHCCCCCCCCCHHH		34.7222468782
418PhosphorylationEDEREAETSASTPPA
HHHHHHHHCCCCCCH		36.3225850435
419PhosphorylationDEREAETSASTPPAS
HHHHHHHCCCCCCHH		16.2425850435
421PhosphorylationREAETSASTPPASAF
HHHHHCCCCCCHHHH		41.0125850435
422PhosphorylationEAETSASTPPASAFL
HHHHCCCCCCHHHHH		32.7725850435
426PhosphorylationSASTPPASAFLKAWV
CCCCCCHHHHHHHHE		25.9025850435
434PhosphorylationAFLKAWVYRPGEDTE
HHHHHHEECCCCCCC		10.6124092754
512PhosphorylationCPFRVAIYVPGEKPP
CCEEEEEEECCCCCC		7.2812016208
540PhosphorylationRRLKRPETPTHDPDP
HHHCCCCCCCCCCCC		35.8529255136
542PhosphorylationLKRPETPTHDPDPET
HCCCCCCCCCCCCCC		46.4629255136
549PhosphorylationTHDPDPETPLKARKV
CCCCCCCCCCCCCCC		39.0329255136
552UbiquitinationPDPETPLKARKVRFS
CCCCCCCCCCCCCCC		47.5529967540
631PhosphorylationLAPIPALTQTLPSSS
CCCCCCHHCCCCCCC		22.9323312004
633PhosphorylationPIPALTQTLPSSSVP
CCCCHHCCCCCCCCC		35.0923312004
636PhosphorylationALTQTLPSSSVPSSP
CHHCCCCCCCCCCCC		38.0623312004
637PhosphorylationLTQTLPSSSVPSSPV
HHCCCCCCCCCCCCC		33.1523312004
638PhosphorylationTQTLPSSSVPSSPVQ
HCCCCCCCCCCCCCC		42.2423312004
641PhosphorylationLPSSSVPSSPVQTTP
CCCCCCCCCCCCCCC		45.1523312004
642PhosphorylationPSSSVPSSPVQTTPL
CCCCCCCCCCCCCCH		24.0323312004
646PhosphorylationVPSSPVQTTPLSQAV
CCCCCCCCCCHHHHC		30.5223312004
647PhosphorylationPSSPVQTTPLSQAVA
CCCCCCCCCHHHHCC		12.7323312004
650PhosphorylationPVQTTPLSQAVATPS
CCCCCCHHHHCCCCC		19.8023312004
655PhosphorylationPLSQAVATPSRSSAA
CHHHHCCCCCHHHHH		18.3923312004
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

Oops, there are no upstream regulatory protein records of PR15A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PR15A_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 PR15A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BAG1_HUMANBAG1physical
12724406
HSP7C_HUMANHSPA8physical
12724406
PP1A_HUMANPPP1CAphysical
12724406
SNF5_HUMANSMARCB1physical
10490642
SNF5_HUMANSMARCB1physical
12016208
PP1A_HUMANPPP1CAphysical
12016208
PP1B_HUMANPPP1CBphysical
12016208
PP1G_HUMANPPP1CCphysical
12016208
IF2A_HUMANEIF2S1physical
12556489
TSN_HUMANTSNphysical
10434033
SMAD7_HUMANSMAD7physical
14718519
PKHA1_HUMANPLEKHA1physical
28514442
MINK1_HUMANMINK1physical
28514442
ZNF92_HUMANZNF92physical
28514442
RPP29_HUMANPOP4physical
28514442
MUM1_HUMANMUM1physical
28514442
BBX_HUMANBBXphysical
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 PR15A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-262 AND SER-264, ANDMASS SPECTROMETRY.

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