PHYD1_HUMAN - dbPTM
PHYD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHYD1_HUMAN
UniProt AC Q5SRE7
Protein Name Phytanoyl-CoA dioxygenase domain-containing protein 1
Gene Name PHYHD1
Organism Homo sapiens (Human).
Sequence Length 291
Subcellular Localization
Protein Description Isoform 1 has alpha-ketoglutarate-dependent dioxygenase activity. Does not show detectable activity towards fatty acid CoA thioesters. Is not expected to be active with phytanoyl CoA. Isoform 2 and isoform 3 probably lack enzyme activity..
Protein Sequence MACLSPSQLQKFQQDGFLVLEGFLSAEECVAMQQRIGEIVAEMDVPLHCRTEFSTQEEEQLRAQGSTDYFLSSGDKIRFFFEKGVFDEKGNFLVPPEKSINKIGHALHAHDPVFKSITHSFKVQTLARSLGLQMPVVVQSMYIFKQPHFGGEVSPHQDASFLYTEPLGRVLGVWIAVEDATLENGCLWFIPGSHTSGVSRRMVRAPVGSAPGTSFLGSEPARDNSLFVPTPVQRGALVLIHGEVVHKSKQNLSDRSRQAYTFHLMEASGTTWSPENWLQPTAELPFPQLYT
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
5Phosphorylation---MACLSPSQLQKF
---CCCCCHHHHHHH
23.5328348404
55PhosphorylationHCRTEFSTQEEEQLR
EEECCCCCHHHHHHH
45.3717525332
102AcetylationPPEKSINKIGHALHA
CCHHHHHHHHHHHHC
48.687460727
116PhosphorylationAHDPVFKSITHSFKV
CCCHHHHHHCHHHHH
22.6624719451
125PhosphorylationTHSFKVQTLARSLGL
CHHHHHHHHHHHCCC
25.93-
129PhosphorylationKVQTLARSLGLQMPV
HHHHHHHHCCCCCCE
22.60-
140PhosphorylationQMPVVVQSMYIFKQP
CCCEEEEEEEEEECC
11.27-
154PhosphorylationPHFGGEVSPHQDASF
CCCCCCCCCCCCCCE
16.6228857561
160PhosphorylationVSPHQDASFLYTEPL
CCCCCCCCEEECCCH
24.8728348404

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 PHYD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHYD1_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 PHYD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 PHYD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, AND MASSSPECTROMETRY.

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