PPBT_HUMAN - dbPTM
PPBT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPBT_HUMAN
UniProt AC P05186
Protein Name Alkaline phosphatase, tissue-nonspecific isozyme
Gene Name ALPL
Organism Homo sapiens (Human).
Sequence Length 524
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor .
Protein Description This isozyme may play a role in skeletal mineralization..
Protein Sequence MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF
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
4 (in isoform 2)Phosphorylation-18.70-
48PhosphorylationLELQKLNTNVAKNVI
HHHHHCCCHHHHHHH
41.3246162759
100PhosphorylationPFVALSKTYNTNAQV
CEEEEECEECCCCCC
20.7323663014
101PhosphorylationFVALSKTYNTNAQVP
EEEEECEECCCCCCC
24.5923663014
103PhosphorylationALSKTYNTNAQVPDS
EEECEECCCCCCCCC
22.8623663014
110PhosphorylationTNAQVPDSAGTATAY
CCCCCCCCCCCCEEE
23.6425463755
113PhosphorylationQVPDSAGTATAYLCG
CCCCCCCCCEEEEEE
22.1325463755
115PhosphorylationPDSAGTATAYLCGVK
CCCCCCCEEEEEEEE
18.7023663014
117PhosphorylationSAGTATAYLCGVKAN
CCCCCEEEEEEEECC
9.7323663014
131PhosphorylationNEGTVGVSAATERSR
CCCCCCEEEECCHHH
13.2721712546
140N-linked_GlycosylationATERSRCNTTQGNEV
ECCHHHCCCCCCCHH
45.08UniProtKB CARBOHYD
149PhosphorylationTQGNEVTSILRWAKD
CCCCHHHHHHHHHHH
25.4624719451
160PhosphorylationWAKDAGKSVGIVTTT
HHHHCCCEEEEEEEC
25.3446162753
230N-linked_GlycosylationRKYMYPKNKTDVEYE
CCCCCCCCCCCCCCC
48.21UniProtKB CARBOHYD
232O-linked_GlycosylationYMYPKNKTDVEYESD
CCCCCCCCCCCCCCC
55.4630059200
236PhosphorylationKNKTDVEYESDEKAR
CCCCCCCCCCCHHHC
22.1526657352
271N-linked_GlycosylationKHSHFIWNRTELLTL
CCCCEEECCCEEEEC
35.86UniProtKB CARBOHYD
303N-linked_GlycosylationQYELNRNNVTDPSLS
CEEHHCCCCCCCHHH
34.52UniProtKB CARBOHYD
308PhosphorylationRNNVTDPSLSEMVVV
CCCCCCCHHHHHHHH
47.5428387310
310PhosphorylationNVTDPSLSEMVVVAI
CCCCCHHHHHHHHHH
28.1628387310
394PhosphorylationGYTPRGNSIFGLAPM
CCCCCCCCCCCCCCC
23.3228555341
415PhosphorylationKPFTAILYGNGPGYK
CCEEEEECCCCCCCE
11.4825367160
430N-linked_GlycosylationVVGGERENVSMVDYA
EECCCCCEEEEEECC
37.0719159218
501GPI-anchorLGHCAPASSAGSLAA
CCCCCCCCHHHHHHH
21.47-

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 PPBT_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPBT_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 PPBT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EF1A1_HUMANEEF1A1physical
16014383
LOX5_HUMANALOX5physical
26210919
SPCS2_HUMANSPCS2physical
28514442
SC11C_HUMANSEC11Cphysical
28514442

Drug and Disease Associations
Kegg Disease
H00213 Hypophosphatasia
OMIM Disease
146300Hypophosphatasia (HOPS)
241510Hypophosphatasia childhood type (HOPSC)
241500Hypophosphatasia infantile type (HOPSI)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PPBT_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-430, AND MASSSPECTROMETRY.

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