SERB_HUMAN - dbPTM
SERB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SERB_HUMAN
UniProt AC P78330
Protein Name Phosphoserine phosphatase
Gene Name PSPH
Organism Homo sapiens (Human).
Sequence Length 225
Subcellular Localization
Protein Description Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates..
Protein Sequence MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE
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
1Acetylation-------MVSHSELR
-------CCCHHHHH
6.6919413330
3Phosphorylation-----MVSHSELRKL
-----CCCHHHHHHH
21.7222210691
47SulfoxidationVEDAVSEMTRRAMGG
CHHHHHHHHHHHHCC
2.4830846556
52SulfoxidationSEMTRRAMGGAVPFK
HHHHHHHHCCCCCHH
4.8921406390
59MethylationMGGAVPFKAALTERL
HCCCCCHHHHHHHHH
27.04115975903
88PhosphorylationAEQPPHLTPGIRELV
HHCCCCCCHHHHHHH
19.21-
122AcetylationIVEHVASKLNIPATN
HHHHHHHHCCCCHHH
35.5025953088
138PhosphorylationFANRLKFYFNGEYAG
HHHCEEEEECCCCCC
8.4422817900
143PhosphorylationKFYFNGEYAGFDETQ
EEEECCCCCCCCCCC
17.2722817900
158UbiquitinationPTAESGGKGKVIKLL
CCCHHCCCCHHHHHH
60.1121906983

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 SERB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SERB_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 SERB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KPRA_HUMANPRPSAP1physical
17353931
SERB_HUMANPSPHphysical
12213811
SERB_HUMANPSPHphysical
25416956
FAD1_HUMANFLAD1physical
26344197
OGT1_HUMANOGTphysical
26344197
SERA_HUMANPHGDHphysical
26344197
TIM8B_HUMANTIMM8Bphysical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614023Phosphoserine phosphatase deficiency (PSPHD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SERB_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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