PPB1_HUMAN - dbPTM
PPB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPB1_HUMAN
UniProt AC P05187
Protein Name Alkaline phosphatase, placental type
Gene Name ALPP
Organism Homo sapiens (Human).
Sequence Length 535
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor.
Protein Description
Protein Sequence MLGPCMLLLLLLLGLRLQLSLGIIPVEEENPDFWNREAAEALGAAKKLQPAQTAAKNLIIFLGDGMGVSTVTAARILKGQKKDKLGPEIPLAMDRFPYVALSKTYNVDKHVPDSGATATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGTYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYPDDYSQGGTRLDGKNLVQEWLAKRQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALRLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVLKDGARPDVTESESGSPEYRQQSAVPLDEETHAGEDVAVFARGPQAHLVHGVQEQTFIAHVMAFAACLEPYTACDLAPPAGTTDAAHPGRSVVPALLPLLAGTLLLLETATAP
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
46UbiquitinationAEALGAAKKLQPAQT
HHHHHHHHHCCHHHH		54.18-
46SuccinylationAEALGAAKKLQPAQT
HHHHHHHHHCCHHHH		54.1823954790
47UbiquitinationEALGAAKKLQPAQTA
HHHHHHHHCCHHHHH		47.86-
472-HydroxyisobutyrylationEALGAAKKLQPAQTA
HHHHHHHHCCHHHHH		47.86-
53PhosphorylationKKLQPAQTAAKNLII
HHCCHHHHHHHCEEE		30.59-
56UbiquitinationQPAQTAAKNLIIFLG
CHHHHHHHCEEEEEC		50.23-
84UbiquitinationLKGQKKDKLGPEIPL
HCCCCCCCCCCCCCC		65.31-
103AcetylationFPYVALSKTYNVDKH
CCEEEEECEEECCCC		56.7426051181
103UbiquitinationFPYVALSKTYNVDKH
CCEEEEECEEECCCC		56.74-
104PhosphorylationPYVALSKTYNVDKHV
CEEEEECEEECCCCC		19.5628152594
1092-HydroxyisobutyrylationSKTYNVDKHVPDSGA
ECEEECCCCCCCCCH		42.07-
109UbiquitinationSKTYNVDKHVPDSGA
ECEEECCCCCCCCCH		42.07-
109AcetylationSKTYNVDKHVPDSGA
ECEEECCCCCCCCCH		42.0726051181
114PhosphorylationVDKHVPDSGATATAY
CCCCCCCCCHHEEEH		25.0230266825
117PhosphorylationHVPDSGATATAYLCG
CCCCCCHHEEEHHHC		28.2430266825
119PhosphorylationPDSGATATAYLCGVK
CCCCHHEEEHHHCCC		16.1023663014
121PhosphorylationSGATATAYLCGVKGN
CCHHEEEHHHCCCCC		9.7330266825
126UbiquitinationTAYLCGVKGNFQTIG
EEHHHCCCCCCEEEC		33.16-
144N-linked_GlycosylationAARFNQCNTTRGNEV
HHHHHCCCCCCCCHH		34.4216815919
1632-HydroxyisobutyrylationNRAKKAGKSVGVVTT
HHHHHCCCCEEEEEE		46.99-
163UbiquitinationNRAKKAGKSVGVVTT
HHHHHCCCCEEEEEE		46.99-
177PhosphorylationTTRVQHASPAGTYAH
EEEEECCCCCCCEEE		17.1072265383
182PhosphorylationHASPAGTYAHTVNRN
CCCCCCCEEEECCCC		8.75110739419
191PhosphorylationHTVNRNWYSDADVPA
EECCCCCCCCCCCCH		10.5427642862
199PhosphorylationSDADVPASARQEGCQ
CCCCCCHHHHHHCHH		20.22110739425
232SulfoxidationGRKYMFRMGTPDPEY
CCEEEEECCCCCCCC		4.8528183972
234PhosphorylationKYMFRMGTPDPEYPD
EEEEECCCCCCCCCC		18.38110739431
239PhosphorylationMGTPDPEYPDDYSQG
CCCCCCCCCCCCCCC		19.83110739437
243PhosphorylationDPEYPDDYSQGGTRL
CCCCCCCCCCCCCCC		15.4174103173
244PhosphorylationPEYPDDYSQGGTRLD
CCCCCCCCCCCCCCC		29.37-
253UbiquitinationGGTRLDGKNLVQEWL
CCCCCCCHHHHHHHH		46.93-
262SuccinylationLVQEWLAKRQGARYV
HHHHHHHHHCCCCEE		42.9823954790
262UbiquitinationLVQEWLAKRQGARYV
HHHHHHHHHCCCCEE		42.98-
271N-linked_GlycosylationQGARYVWNRTELMQA
CCCCEEECHHHHHHH		30.8416815919
273PhosphorylationARYVWNRTELMQASL
CCEEECHHHHHHHHC		30.2020068231
279PhosphorylationRTELMQASLDPSVTH
HHHHHHHHCCHHHHH		19.2020068231
283PhosphorylationMQASLDPSVTHLMGL
HHHHCCHHHHHHHCC		39.0420068231
285PhosphorylationASLDPSVTHLMGLFE
HHCCHHHHHHHCCCC		17.4020068231
297SumoylationLFEPGDMKYEIHRDS
CCCCCCCCEEEECCC		44.4617000644
297SumoylationLFEPGDMKYEIHRDS
CCCCCCCCEEEECCC		44.46-
298PhosphorylationFEPGDMKYEIHRDST
CCCCCCCEEEECCCC		17.3027174698
304PhosphorylationKYEIHRDSTLDPSLM
CEEEECCCCCCHHHH		30.7227174698
305PhosphorylationYEIHRDSTLDPSLME
EEEECCCCCCHHHHH		39.2027174698
309PhosphorylationRDSTLDPSLMEMTEA
CCCCCCHHHHHHHHH		39.7627174698
314PhosphorylationDPSLMEMTEAALRLL
CHHHHHHHHHHHHHH		14.7920068231
322PhosphorylationEAALRLLSRNPRGFF
HHHHHHHHHCCCCEE		34.3025921289
367PhosphorylationIERAGQLTSEEDTLS
HHHHCCCCCCCCCEE		26.63110739455
368PhosphorylationERAGQLTSEEDTLSL
HHHCCCCCCCCCEEE		47.80110740537
372PhosphorylationQLTSEEDTLSLVTAD
CCCCCCCCEEEEECC		22.86110739465
377PhosphorylationEDTLSLVTADHSHVF
CCCEEEEECCCCCEE		31.49110740545
394PhosphorylationGGYPLRGSSIFGLAP
CCEECCCCCCCCCCC		17.5223663014
395PhosphorylationGYPLRGSSIFGLAPG
CEECCCCCCCCCCCC		25.4323663014
4032-HydroxyisobutyrylationIFGLAPGKARDRKAY
CCCCCCCCCCCCCCE		38.91-
403UbiquitinationIFGLAPGKARDRKAY
CCCCCCCCCCCCCCE		38.91-
408UbiquitinationPGKARDRKAYTVLLY
CCCCCCCCCEEEEEE		50.46-
410PhosphorylationKARDRKAYTVLLYGN
CCCCCCCEEEEEECC		10.6220068231
411PhosphorylationARDRKAYTVLLYGNG
CCCCCCEEEEEECCC		14.99110739483
415PhosphorylationKAYTVLLYGNGPGYV
CCEEEEEECCCCCEE		12.3720068231
421PhosphorylationLYGNGPGYVLKDGAR
EECCCCCEEECCCCC		13.0220068231
424UbiquitinationNGPGYVLKDGARPDV
CCCCEEECCCCCCCC		44.03-
432PhosphorylationDGARPDVTESESGSP
CCCCCCCCCCCCCCH		40.9723663014
434PhosphorylationARPDVTESESGSPEY
CCCCCCCCCCCCHHH		27.9123663014
436PhosphorylationPDVTESESGSPEYRQ
CCCCCCCCCCHHHHH		54.5823663014
438PhosphorylationVTESESGSPEYRQQS
CCCCCCCCHHHHHCC		24.6829116813
441PhosphorylationSESGSPEYRQQSAVP
CCCCCHHHHHCCCCC		19.67110739495
445PhosphorylationSPEYRQQSAVPLDEE
CHHHHHCCCCCCCCC		23.93110739501
453PhosphorylationAVPLDEETHAGEDVA
CCCCCCCCCCCCCEE		18.25110739507
506GPI-anchorAPPAGTTDAAHPGRS
CCCCCCCCCCCCCCC		41.412153284
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 PPB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPB1_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 PPB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KRA59_HUMANKRTAP5-9physical
25416956
KR412_HUMANKRTAP4-12physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
FBW1A_HUMANBTRCphysical
28049764
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 PPB1_HUMAN

loading...

Related Literatures of Post-Translational Modification
GPI-anchor
ReferencePubMed
"Site-specific mutations in the COOH-terminus of placental alkalinephosphatase: a single amino acid change converts aphosphatidylinositol-glycan-anchored protein to a secreted protein.";
Lowe M.E.;
J. Cell Biol. 116:799-807(1992).
Cited for: EFFECT OF MUTAGENESIS OF C-TERMINAL PEPTIDE ON GPI-ANCHORING.
"Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specificmutagenesis at Asp-484 of placental alkaline phosphatase.";
Micanovic R., Gerber L.D., Berger J., Kodukula K., Udenfriend S.;
Proc. Natl. Acad. Sci. U.S.A. 87:157-161(1990).
Cited for: GPI-ANCHOR AT ASP-506.
Phosphorylation
ReferencePubMed
"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-114, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory