PHP14_HUMAN - dbPTM
PHP14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHP14_HUMAN
UniProt AC Q9NRX4
Protein Name 14 kDa phosphohistidine phosphatase {ECO:0000303|PubMed:12383260}
Gene Name PHPT1
Organism Homo sapiens (Human).
Sequence Length 125
Subcellular Localization Cytoplasm.
Protein Description Exhibits phosphohistidine phosphatase activity..
Protein Sequence MAVADLALIPDVDIDSDGVFKYVLIRVHSAPRSGAPAAESKEIVRGYKWAEYHADIYDKVSGDMQKQGCDCECLGGGRISHQSQDKKIHVYGYSMAYGPAQHAISTEKIKAKYPDYEVTWANDGY
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------MAVADLALI
------CCCCCEEEC
12.7619413330
16PhosphorylationIPDVDIDSDGVFKYV
CCCCEECCCCEEEEE
36.2820068231
22PhosphorylationDSDGVFKYVLIRVHS
CCCCEEEEEEEEEEC
6.7729514088
29PhosphorylationYVLIRVHSAPRSGAP
EEEEEEECCCCCCCC
36.7929514088
33PhosphorylationRVHSAPRSGAPAAES
EEECCCCCCCCCHHH
37.9428985074
40PhosphorylationSGAPAAESKEIVRGY
CCCCCHHHHHHHHCC
30.7528857561
412-HydroxyisobutyrylationGAPAAESKEIVRGYK
CCCCHHHHHHHHCCC
42.86-
41AcetylationGAPAAESKEIVRGYK
CCCCHHHHHHHHCCC
42.8626822725
41UbiquitinationGAPAAESKEIVRGYK
CCCCHHHHHHHHCCC
42.86-
482-HydroxyisobutyrylationKEIVRGYKWAEYHAD
HHHHHCCCHHHHHHH
42.63-
57PhosphorylationAEYHADIYDKVSGDM
HHHHHHHHHHHCCCH
15.4027642862
59UbiquitinationYHADIYDKVSGDMQK
HHHHHHHHHCCCHHH
22.7121890473
59UbiquitinationYHADIYDKVSGDMQK
HHHHHHHHHCCCHHH
22.7121890473
66UbiquitinationKVSGDMQKQGCDCEC
HHCCCHHHCCCCCEE
41.86-
862-HydroxyisobutyrylationISHQSQDKKIHVYGY
CCCCCCCCCEEEEEE
46.09-
91PhosphorylationQDKKIHVYGYSMAYG
CCCCEEEEEEEECCC
9.0028152594
93PhosphorylationKKIHVYGYSMAYGPA
CCEEEEEEEECCCCH
4.2421082442
94PhosphorylationKIHVYGYSMAYGPAQ
CEEEEEEEECCCCHH
7.8028152594
95SulfoxidationIHVYGYSMAYGPAQH
EEEEEEEECCCCHHH
2.2228465586
97PhosphorylationVYGYSMAYGPAQHAI
EEEEEECCCCHHHCC
18.2628152594
105PhosphorylationGPAQHAISTEKIKAK
CCHHHCCCHHHHHHH
31.1524719451
106PhosphorylationPAQHAISTEKIKAKY
CHHHCCCHHHHHHHC
34.8724719451
112UbiquitinationSTEKIKAKYPDYEVT
CHHHHHHHCCCCEEE
52.92-
113PhosphorylationTEKIKAKYPDYEVTW
HHHHHHHCCCCEEEE
13.2428152594
116PhosphorylationIKAKYPDYEVTWAND
HHHHCCCCEEEECCC
14.0628152594
119PhosphorylationKYPDYEVTWANDGY-
HCCCCEEEECCCCC-
13.6128152594
125PhosphorylationVTWANDGY-------
EEECCCCC-------
20.4628152594

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 PHP14_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHP14_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 PHP14_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNM3L_HUMANDNMT3Lphysical
16189514
PTMS_HUMANPTMSphysical
22939629
PSME1_HUMANPSME1physical
22939629
RANB3_HUMANRANBP3physical
22939629
ZPR1_HUMANZPR1physical
22939629
GDPP1_HUMANGDPGP1physical
26344197
PTPA_HUMANPPP2R4physical
26344197
TPPC4_HUMANTRAPPC4physical
26344197

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 PHP14_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-116 AND TYR-125, ANDMASS SPECTROMETRY.

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