PPR18_HUMAN - dbPTM
PPR18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPR18_HUMAN
UniProt AC Q6NYC8
Protein Name Phostensin
Gene Name PPP1R18
Organism Homo sapiens (Human).
Sequence Length 613
Subcellular Localization Isoform 1: Cytoplasm, cytoskeleton .
Isoform 4: Cytoplasm, cytoskeleton .
Protein Description Isoform 1: May target protein phosphatase 1 to F-actin cytoskeleton.; Isoform 4: May target protein phosphatase 1 to F-actin cytoskeleton..
Protein Sequence MATIPDWKLQLLARRRQEEASVRGREKAERERLSQMPAWKRGLLERRRAKLGLSPGEPSPVLGTVEAGPPDPDESAVLLEAIGPVHQNRFIRQERQQQQQQQQRSEELLAERKPGPLEARERRPSPGEMRDQSPKGRESREERLSPRETRERRLGIGGAQELSLRPLEARDWRQSPGEVGDRSSRLSEAWKWRLSPGETPERSLRLAESREQSPRRKEVESRLSPGESAYQKLGLTEAHKWRPDSRESQEQSLVQLEATEWRLRSGEERQDYSEECGRKEEWPVPGVAPKETAELSETLTREAQGNSSAGVEAAEQRPVEDGERGMKPTEGWKWTLNSGKAREWTPRDIEAQTQKPEPPESAEKLLESPGVEAGEGEAEKEEAGAQGRPLRALQNCCSVPSPLPPEDAGTGGLRQQEEEAVELQPPPPAPLSPPPPAPTAPQPPGDPLMSRLFYGVKAGPGVGAPRRSGHTFTVNPRRSVPPATPATPTSPATVDAAVPGAGKKRYPTAEEILVLGGYLRLSRSCLAKGSPERHHKQLKISFSETALETTYQYPSESSVLEELGPEPEVPSAPNPPAAQPDDEEDEEELLLLQPELQGGLRTKALIVDESCRR
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
21PhosphorylationRRRQEEASVRGREKA
HHHHHHHHHHHHHHH		18.67-
23MethylationRQEEASVRGREKAER
HHHHHHHHHHHHHHH		35.6482797691
40AcetylationLSQMPAWKRGLLERR
HHCCHHHHHHHHHHH		38.4026051181
41MethylationSQMPAWKRGLLERRR
HCCHHHHHHHHHHHH		30.23115387127
54PhosphorylationRRAKLGLSPGEPSPV
HHHHCCCCCCCCCCC		29.1225159151
59PhosphorylationGLSPGEPSPVLGTVE
CCCCCCCCCCCCEEE		24.2821712546
64PhosphorylationEPSPVLGTVEAGPPD
CCCCCCCEEECCCCC		15.8324732914
75PhosphorylationGPPDPDESAVLLEAI
CCCCCCHHHHHHHHH		30.9324732914
125PhosphorylationEARERRPSPGEMRDQ
CHHHCCCCCCCCCCC		43.6629255136
133PhosphorylationPGEMRDQSPKGRESR
CCCCCCCCCCCCCCH		32.6323401153
139PhosphorylationQSPKGRESREERLSP
CCCCCCCCHHHHCCH		43.5624732914
145PhosphorylationESREERLSPRETRER
CCHHHHCCHHHHHHH		28.2923401153
163PhosphorylationIGGAQELSLRPLEAR
CCCCCCCCCCCCCCC		22.9120068231
175PhosphorylationEARDWRQSPGEVGDR
CCCCHHCCCCCCCCC		26.7129255136
183PhosphorylationPGEVGDRSSRLSEAW
CCCCCCCHHHHHHHH		25.2622199227
184PhosphorylationGEVGDRSSRLSEAWK
CCCCCCHHHHHHHHH		37.8322199227
187PhosphorylationGDRSSRLSEAWKWRL
CCCHHHHHHHHHCCC		24.9425159151
195PhosphorylationEAWKWRLSPGETPER
HHHHCCCCCCCCHHH		23.4522167270
199PhosphorylationWRLSPGETPERSLRL
CCCCCCCCHHHHHHH		36.0429255136
203O-linked_GlycosylationPGETPERSLRLAESR
CCCCHHHHHHHHHHH		19.0423301498
203PhosphorylationPGETPERSLRLAESR
CCCCHHHHHHHHHHH		19.0418212344
209PhosphorylationRSLRLAESREQSPRR
HHHHHHHHHCCCCCH		35.1925159151
213PhosphorylationLAESREQSPRRKEVE
HHHHHCCCCCHHHHH		18.6728355574
221PhosphorylationPRRKEVESRLSPGES
CCHHHHHHHCCCCHH		43.6323927012
224PhosphorylationKEVESRLSPGESAYQ
HHHHHHCCCCHHHHH		29.7429255136
228PhosphorylationSRLSPGESAYQKLGL
HHCCCCHHHHHHHCC		37.8923927012
230PhosphorylationLSPGESAYQKLGLTE
CCCCHHHHHHHCCCH		18.5625159151
245PhosphorylationAHKWRPDSRESQEQS
HHCCCCCCHHHHHHH		40.4028348404
248PhosphorylationWRPDSRESQEQSLVQ
CCCCCHHHHHHHHHH		37.6027251275
265PhosphorylationATEWRLRSGEERQDY
HHHHHHHCCCHHCCH		55.9728857561
272PhosphorylationSGEERQDYSEECGRK
CCCHHCCHHHHCCCC		15.0528796482
273PhosphorylationGEERQDYSEECGRKE
CCHHCCHHHHCCCCC		34.9028796482
296PhosphorylationPKETAELSETLTREA
CHHHHHHHHHHHHHH		21.7529255136
298PhosphorylationETAELSETLTREAQG
HHHHHHHHHHHHHCC		30.0129255136
300PhosphorylationAELSETLTREAQGNS
HHHHHHHHHHHCCCC		33.6129255136
307PhosphorylationTREAQGNSSAGVEAA
HHHHCCCCCCCCHHH		28.5229978859
308PhosphorylationREAQGNSSAGVEAAE
HHHCCCCCCCCHHHH		32.8025159151
335PhosphorylationPTEGWKWTLNSGKAR
CCCCCEEECCCCCCC		16.6023403867
338PhosphorylationGWKWTLNSGKAREWT
CCEEECCCCCCCCCC		44.7923312004
353PhosphorylationPRDIEAQTQKPEPPE
HHHHHHHHCCCCCCH		45.6826074081
355AcetylationDIEAQTQKPEPPESA
HHHHHHCCCCCCHHH		55.5326051181
361PhosphorylationQKPEPPESAEKLLES
CCCCCCHHHHHHHHC		47.7222199227
368PhosphorylationSAEKLLESPGVEAGE
HHHHHHHCCCCCCCC		27.2429255136
398PhosphorylationRALQNCCSVPSPLPP
HHHHHHCCCCCCCCH		38.9829255136
401PhosphorylationQNCCSVPSPLPPEDA
HHHCCCCCCCCHHHC		36.5929255136
410PhosphorylationLPPEDAGTGGLRQQE
CCHHHCCCCCCCHHH		29.7827080861
432PhosphorylationPPPPAPLSPPPPAPT
CCCCCCCCCCCCCCC		34.0128355574
439PhosphorylationSPPPPAPTAPQPPGD
CCCCCCCCCCCCCCC		53.7428102081
450PhosphorylationPPGDPLMSRLFYGVK
CCCCCCHHHHHHCCC		33.2522199227
454PhosphorylationPLMSRLFYGVKAGPG
CCHHHHHHCCCCCCC		26.12-
457UbiquitinationSRLFYGVKAGPGVGA
HHHHHCCCCCCCCCC		43.17-
457AcetylationSRLFYGVKAGPGVGA
HHHHHCCCCCCCCCC		43.1725953088
466MethylationGPGVGAPRRSGHTFT
CCCCCCCCCCCCCEE		44.88115387135
468PhosphorylationGVGAPRRSGHTFTVN
CCCCCCCCCCCEEEC		35.8828857561
471PhosphorylationAPRRSGHTFTVNPRR
CCCCCCCCEEECCCC		25.2429449344
473PhosphorylationRRSGHTFTVNPRRSV
CCCCCCEEECCCCCC		22.1129449344
479PhosphorylationFTVNPRRSVPPATPA
EEECCCCCCCCCCCC		40.0123403867
484PhosphorylationRRSVPPATPATPTSP
CCCCCCCCCCCCCCC		21.1626055452
487PhosphorylationVPPATPATPTSPATV
CCCCCCCCCCCCCCC		28.4426055452
489PhosphorylationPATPATPTSPATVDA
CCCCCCCCCCCCCCC		42.8829255136
490PhosphorylationATPATPTSPATVDAA
CCCCCCCCCCCCCCC		17.4629255136
493PhosphorylationATPTSPATVDAAVPG
CCCCCCCCCCCCCCC		23.4629255136
508PhosphorylationAGKKRYPTAEEILVL
CCCCCCCCHHHHHHH		37.45-
522PhosphorylationLGGYLRLSRSCLAKG
HCHHHHHHHHHHHCC		18.7327251275
524O-linked_GlycosylationGYLRLSRSCLAKGSP
HHHHHHHHHHHCCCH		15.3123301498
524PhosphorylationGYLRLSRSCLAKGSP
HHHHHHHHHHHCCCH		15.3123403867
530PhosphorylationRSCLAKGSPERHHKQ
HHHHHCCCHHHHHCE		23.9223401153
557O-linked_GlycosylationTYQYPSESSVLEELG
HCCCCCHHHHHHHHC		30.0423301498
603UbiquitinationLQGGLRTKALIVDES
HCCCCCCCEEEEEHH		34.46-
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 PPR18_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPR18_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 PPR18_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FAM9B_HUMANFAM9Bphysical
25416956
SPERT_HUMANSPERTphysical
25416956
CCD57_HUMANCCDC57physical
25416956
GELS_HUMANGSNphysical
26186194
PP1B_HUMANPPP1CBphysical
26186194
OGA_HUMANMGEA5physical
26186194
DOCK7_HUMANDOCK7physical
26186194
RAIN_HUMANRASIP1physical
26186194
PCBP3_HUMANPCBP3physical
26186194
TRI27_HUMANTRIM27physical
21516116
RAIN_HUMANRASIP1physical
28514442
PP1B_HUMANPPP1CBphysical
28514442
PCBP3_HUMANPCBP3physical
28514442
GELS_HUMANGSNphysical
28514442
OGA_HUMANMGEA5physical
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 PPR18_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-368, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-175; SER-195;THR-199 AND SER-224, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-224 ANDSER-368, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, 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-125; SER-133; SER-145;SER-265; SER-368 AND SER-530, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND MASSSPECTROMETRY.

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