PP1R7_HUMAN - dbPTM
PP1R7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP1R7_HUMAN
UniProt AC Q15435
Protein Name Protein phosphatase 1 regulatory subunit 7
Gene Name PPP1R7
Organism Homo sapiens (Human).
Sequence Length 360
Subcellular Localization Nucleus.
Protein Description Regulatory subunit of protein phosphatase 1..
Protein Sequence MAAERGAGQQQSQEMMEVDRRVESEESGDEEGKKHSSGIVADLSEQSLKDGEERGEEDPEEEHELPVDMETINLDRDAEDVDLNHYRIGKIEGFEVLKKVKTLCLRQNLIKCIENLEELQSLRELDLYDNQIKKIENLEALTELEILDISFNLLRNIEGVDKLTRLKKLFLVNNKISKIENLSNLHQLQMLELGSNRIRAIENIDTLTNLESLFLGKNKITKLQNLDALTNLTVLSMQSNRLTKIEGLQNLVNLRELYLSHNGIEVIEGLENNNKLTMLDIASNRIKKIENISHLTELQEFWMNDNLLESWSDLDELKGARSLETVYLERNPLQKDPQYRRKVMLALPSVRQIDATFVRF
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------MAAERGAGQ
------CCCCCCCCH		20.3119413330
12 (in isoform 4)Phosphorylation-24.6226657352
12 (in isoform 2)Phosphorylation-24.6226657352
12PhosphorylationRGAGQQQSQEMMEVD
CCCCHHHHHHHHHHH		24.6225159151
15SulfoxidationGQQQSQEMMEVDRRV
CHHHHHHHHHHHHHH		1.8421406390
24PhosphorylationEVDRRVESEESGDEE
HHHHHHHHCCCCCCC		43.7529255136
27PhosphorylationRRVESEESGDEEGKK
HHHHHCCCCCCCCCC		47.7129255136
31UbiquitinationSEESGDEEGKKHSSG
HCCCCCCCCCCCCCC		79.60-
34AcetylationSGDEEGKKHSSGIVA
CCCCCCCCCCCCCEE		60.6230591473
36PhosphorylationDEEGKKHSSGIVADL
CCCCCCCCCCCEEEC		38.8629255136
37PhosphorylationEEGKKHSSGIVADLS
CCCCCCCCCCEEECC		32.0529255136
39UbiquitinationGKKHSSGIVADLSEQ
CCCCCCCCEEECCHH		2.20-
40UbiquitinationKKHSSGIVADLSEQS
CCCCCCCEEECCHHH		3.75-
42UbiquitinationHSSGIVADLSEQSLK
CCCCCEEECCHHHCC		39.5721890473
44PhosphorylationSGIVADLSEQSLKDG
CCCEEECCHHHCCCC		33.8529255136
47 (in isoform 2)Ubiquitination-33.0821890473
47 (in isoform 4)Ubiquitination-33.0821890473
47PhosphorylationVADLSEQSLKDGEER
EEECCHHHCCCCHHC		33.0829255136
49UbiquitinationDLSEQSLKDGEERGE
ECCHHHCCCCHHCCC		69.78-
54MethylationSLKDGEERGEEDPEE
HCCCCHHCCCCCCCC		54.22115488517
58 (in isoform 2)Ubiquitination-52.1621890473
58 (in isoform 4)Ubiquitination-52.1621890473
76MethylationMETINLDRDAEDVDL
HHEECCCCCHHHCCC		48.48115488509
90 (in isoform 3)Ubiquitination-34.9021890473
90UbiquitinationLNHYRIGKIEGFEVL
CCCCEECEEHHHHHH		34.9021906983
90 (in isoform 1)Ubiquitination-34.9021890473
90 (in isoform 4)Ubiquitination-34.9021890473
90 (in isoform 2)Ubiquitination-34.9021890473
982-HydroxyisobutyrylationIEGFEVLKKVKTLCL
EHHHHHHHHHHHHHH		61.77-
98UbiquitinationIEGFEVLKKVKTLCL
EHHHHHHHHHHHHHH		61.77-
99UbiquitinationEGFEVLKKVKTLCLR
HHHHHHHHHHHHHHH		44.81-
101 (in isoform 3)Ubiquitination-44.6621890473
101UbiquitinationFEVLKKVKTLCLRQN
HHHHHHHHHHHHHHH		44.6621890473
101 (in isoform 1)Ubiquitination-44.6621890473
109UbiquitinationTLCLRQNLIKCIENL
HHHHHHHHHHHHHCH		2.7521890473
111UbiquitinationCLRQNLIKCIENLEE
HHHHHHHHHHHCHHH		32.12-
112GlutathionylationLRQNLIKCIENLEEL
HHHHHHHHHHCHHHH		3.6022555962
116UbiquitinationLIKCIENLEELQSLR
HHHHHHCHHHHHHHH		3.3421890473
119UbiquitinationCIENLEELQSLRELD
HHHCHHHHHHHHHHC		2.8321890473
119 (in isoform 2)Ubiquitination-2.8321890473
119 (in isoform 4)Ubiquitination-2.8321890473
125 (in isoform 2)Ubiquitination-4.4321890473
125 (in isoform 4)Ubiquitination-4.4321890473
132 (in isoform 2)Ubiquitination-6.5121890473
132 (in isoform 4)Ubiquitination-6.5121890473
133AcetylationDLYDNQIKKIENLEA
CCCHHHHHHHHCHHH		37.6223236377
133 (in isoform 1)Ubiquitination-37.6221890473
133 (in isoform 3)Ubiquitination-37.6221890473
133UbiquitinationDLYDNQIKKIENLEA
CCCHHHHHHHHCHHH		37.6221906983
135 (in isoform 2)Ubiquitination-3.4421890473
135 (in isoform 4)Ubiquitination-3.4421890473
158UbiquitinationFNLLRNIEGVDKLTR
HHHHHCCCCHHHHHH		57.6321890473
162 (in isoform 3)Ubiquitination-49.7221890473
162 (in isoform 1)Ubiquitination-49.7221890473
162UbiquitinationRNIEGVDKLTRLKKL
HCCCCHHHHHHHHHH		49.7221906983
163UbiquitinationNIEGVDKLTRLKKLF
CCCCHHHHHHHHHHH		2.6621890473
167UbiquitinationVDKLTRLKKLFLVNN
HHHHHHHHHHHHHCC		44.11-
168UbiquitinationDKLTRLKKLFLVNNK
HHHHHHHHHHHHCCC		49.4121890473
168 (in isoform 1)Ubiquitination-49.4121890473
168 (in isoform 3)Ubiquitination-49.4121890473
174 (in isoform 4)Ubiquitination-35.2421890473
174 (in isoform 2)Ubiquitination-35.2421890473
175 (in isoform 1)Ubiquitination-43.0621890473
175UbiquitinationKLFLVNNKISKIENL
HHHHHCCCCHHHHHC		43.0621890473
175AcetylationKLFLVNNKISKIENL
HHHHHCCCCHHHHHC		43.0625953088
175 (in isoform 3)Ubiquitination-43.0621890473
178 (in isoform 3)Ubiquitination-58.4721890473
178 (in isoform 1)Ubiquitination-58.4721890473
178UbiquitinationLVNNKISKIENLSNL
HHCCCCHHHHHCCCH		58.4721890473
179 (in isoform 4)Ubiquitination-3.2021890473
179 (in isoform 2)Ubiquitination-3.2021890473
185UbiquitinationKIENLSNLHQLQMLE
HHHHCCCHHHHHHHH		2.1521890473
190SulfoxidationSNLHQLQMLELGSNR
CCHHHHHHHHHCCCH		4.2230846556
201 (in isoform 4)Ubiquitination-2.7521890473
201 (in isoform 2)Ubiquitination-2.7521890473
217 (in isoform 1)Ubiquitination-58.1621890473
217UbiquitinationLESLFLGKNKITKLQ
HHHHHCCCCCCHHHC		58.1621890473
217 (in isoform 3)Ubiquitination-58.1621890473
219UbiquitinationSLFLGKNKITKLQNL
HHHCCCCCCHHHCCH		56.06-
221PhosphorylationFLGKNKITKLQNLDA
HCCCCCCHHHCCHHH		27.5828270605
222 (in isoform 1)Ubiquitination-52.1021890473
222UbiquitinationLGKNKITKLQNLDAL
CCCCCCHHHCCHHHH		52.1021890473
222 (in isoform 3)Ubiquitination-52.1021890473
230PhosphorylationLQNLDALTNLTVLSM
HCCHHHHHCCHHHHC		29.8728270605
233PhosphorylationLDALTNLTVLSMQSN
HHHHHCCHHHHCCCC		22.8228270605
236PhosphorylationLTNLTVLSMQSNRLT
HHCCHHHHCCCCCCC		15.5028270605
239PhosphorylationLTVLSMQSNRLTKIE
CHHHHCCCCCCCHHH		18.4428270605
243PhosphorylationSMQSNRLTKIEGLQN
HCCCCCCCHHHHHHH		27.0928270605
244 (in isoform 1)Ubiquitination-43.2721890473
244 (in isoform 3)Ubiquitination-43.2721890473
244UbiquitinationMQSNRLTKIEGLQNL
CCCCCCCHHHHHHHH		43.2721890473
277PhosphorylationLENNNKLTMLDIASN
CCCCCCEEEHHHHHH		19.80-
278SulfoxidationENNNKLTMLDIASNR
CCCCCEEEHHHHHHH		4.6021406390
322PhosphorylationDELKGARSLETVYLE
HHHCCCCCCCEEEEC		29.9825693802
325PhosphorylationKGARSLETVYLERNP
CCCCCCCEEEECCCC		21.5323186163
327PhosphorylationARSLETVYLERNPLQ
CCCCCEEEECCCCCC		15.40-
335UbiquitinationLERNPLQKDPQYRRK
ECCCCCCCCHHHHHH		78.16-
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
24SPhosphorylationKinasePLK1P53350
PSP
27SPhosphorylationKinasePLK1P53350
PSP
44SPhosphorylationKinasePLK1P53350
PSP
47SPhosphorylationKinasePLK1P53350
PSP
277TPhosphorylationKinasePLK1P53350
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PP1R7_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 PP1R7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HNRPF_HUMANHNRNPFphysical
22863883
HPBP1_HUMANHSPBP1physical
22863883
PPME1_HUMANPPME1physical
22863883
RPR1B_HUMANRPRD1Bphysical
22863883
TTL12_HUMANTTLL12physical
22863883
ZPR1_HUMANZPR1physical
22863883
USBP1_HUMANUSHBP1physical
25416956
PP1G_HUMANPPP1CCphysical
26186194
PP1A_HUMANPPP1CAphysical
26186194
IPP2_HUMANPPP1R2physical
26344197
UBP7_HUMANUSP7physical
26344197
VPS29_HUMANVPS29physical
26344197
UBX2A_HUMANUBXN2Aphysical
26389662
PP1G_HUMANPPP1CCphysical
28514442
PP1A_HUMANPPP1CAphysical
28514442
CT027_HUMANC20orf27physical
27173435
PP1RB_HUMANPPP1R11physical
27173435
PDRG1_HUMANPDRG1physical
27173435
WDR92_HUMANWDR92physical
27173435
WBP11_HUMANWBP11physical
27173435
SH24A_HUMANSH2D4Aphysical
27173435
RPAP3_HUMANRPAP3physical
27173435
PIHD1_HUMANPIH1D1physical
27173435
CC85C_HUMANCCDC85Cphysical
27173435
GYS1_HUMANGYS1physical
27173435
IASPP_HUMANPPP1R13Lphysical
27173435
PP1RA_HUMANPPP1R10physical
27173435
ASPP2_HUMANTP53BP2physical
27173435
PACS1_HUMANPACS1physical
27173435
TILB_HUMANLRRC6physical
27173435
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 PP1R7_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-24 AND SER-27, AND MASS SPECTROMETRY.
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-24 AND SER-27, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, AND MASSSPECTROMETRY.

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