PHT14_ARATH - dbPTM
PHT14_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHT14_ARATH
UniProt AC Q96303
Protein Name Inorganic phosphate transporter 1-4
Gene Name PHT1-4
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 534
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description High-affinity transporter for external inorganic phosphate. Acts as a H(+):phosphate symporter in both low- and high-Pi conditions. Confers sensitivity to arsenate..
Protein Sequence MAREQLQVLNALDVAKTQWYHFTAIIIAGMGFFTDAYDLFCISLVTKLLGRIYYHVEGAQKPGTLPPNVAAAVNGVAFCGTLAGQLFFGWLGDKLGRKKVYGMTLMVMVLCSIASGLSFGHEPKAVMATLCFFRFWLGFGIGGDYPLSATIMSEYANKKTRGAFVSAVFAMQGFGIMAGGIFAIIISSAFEAKFPSPAYADDALGSTIPQADLVWRIILMAGAIPAAMTYYSRSKMPETARYTALVAKDAKQAASDMSKVLQVEIEPEQQKLEEISKEKSKAFGLFSKEFMSRHGLHLLGTTSTWFLLDIAFYSQNLFQKDIFSAIGWIPPAQSMNAIQEVFKIARAQTLIALCSTVPGYWFTVAFIDVIGRFAIQMMGFFFMTVFMFALAIPYNHWTHKENRIGFVIMYSLTFFFANFGPNATTFVVPAEIFPARFRSTCHGISAASGKLGAMVGAFGFLYLAQNPDKDKTDAGYPPGIGVRNSLIVLGVVNFLGILFTFLVPESKGKSLEEMSGENEDNENSNNDSRTVPIV
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
104PhosphorylationRKKVYGMTLMVMVLC
CCCHHHHHHHHHHHH
13.8224243849
112PhosphorylationLMVMVLCSIASGLSF
HHHHHHHHHHHCCCC
19.6124243849
129PhosphorylationEPKAVMATLCFFRFW
CHHHHHHHHHHHHHH
13.1319880383
255PhosphorylationKDAKQAASDMSKVLQ
HHHHHHHHHHHHHHC
36.5419688752
258PhosphorylationKQAASDMSKVLQVEI
HHHHHHHHHHHCEEC
25.3017317660
276PhosphorylationQQKLEEISKEKSKAF
HHHHHHHHHHHHHHH
37.7317317660
440PhosphorylationFPARFRSTCHGISAA
CCHHHHHHHHHHHHH
12.3119880383
524PhosphorylationENEDNENSNNDSRTV
CCCCCCCCCCCCCCC
30.7219880383
528PhosphorylationNENSNNDSRTVPIV-
CCCCCCCCCCCCCC-
31.7917317660

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 PHT14_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHT14_ARATH !!

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 PHT14_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHT11_ARATHPHT1;1physical
25754174
PHT14_ARATHPHT1;4physical
25754174

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHT14_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND MASSSPECTROMETRY.
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis.";
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.;
J. Proteome Res. 7:2458-2470(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND MASSSPECTROMETRY.
"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database.";
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
Plant Cell 16:2394-2405(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, SUBCELLULARLOCATION, AND MASS SPECTROMETRY.

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