PHS2_HUMAN - dbPTM
PHS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHS2_HUMAN
UniProt AC Q9H0N5
Protein Name Pterin-4-alpha-carbinolamine dehydratase 2
Gene Name PCBD2
Organism Homo sapiens (Human).
Sequence Length 130
Subcellular Localization
Protein Description Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2 (By similarity).; Regulates the dimerization of homeodomain protein HNF-1-alpha and enhances its transcriptional activity..
Protein Sequence MAAVLGALGATRRLLAALRGQSLGLAAMSSGTHRLTAEERNQAILDLKAAGWSELSERDAIYKEFSFHNFNQAFGFMSRVALQAEKMNHHPEWFNVYNKVQITLTSHDCGELTKKDVKLAKFIEKAAASV
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
11PhosphorylationVLGALGATRRLLAAL
HHHHHHHHHHHHHHH
17.9621406692
86AcetylationRVALQAEKMNHHPEW
HHHHHHHHCCCCCHH
48.2825953088
106PhosphorylationKVQITLTSHDCGELT
HHEEEEEECCCCCCC
22.0528509920
113PhosphorylationSHDCGELTKKDVKLA
ECCCCCCCHHHHHHH
31.5728509920
114AcetylationHDCGELTKKDVKLAK
CCCCCCCHHHHHHHH
60.65-
114SuccinylationHDCGELTKKDVKLAK
CCCCCCCHHHHHHHH
60.65-
114SuccinylationHDCGELTKKDVKLAK
CCCCCCCHHHHHHHH
60.65-
118AcetylationELTKKDVKLAKFIEK
CCCHHHHHHHHHHHH
53.51-
118SuccinylationELTKKDVKLAKFIEK
CCCHHHHHHHHHHHH
53.51-
118SuccinylationELTKKDVKLAKFIEK
CCCHHHHHHHHHHHH
53.51-
121AcetylationKKDVKLAKFIEKAAA
HHHHHHHHHHHHHHH
58.2625953088
125AcetylationKLAKFIEKAAASV--
HHHHHHHHHHHCC--
38.2127178108
125SuccinylationKLAKFIEKAAASV--
HHHHHHHHHHHCC--
38.21-
125SuccinylationKLAKFIEKAAASV--
HHHHHHHHHHHCC--
38.21-

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 PHS2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHS2_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 PHS2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASCC2_HUMANASCC2physical
20211142
MED30_HUMANMED30physical
20211142
TF2LY_HUMANTGIF2LYphysical
20211142
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 PHS2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND MASS SPECTROMETRY.

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