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Protein Page:
HPGD (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
HPGD Prostaglandin inactivation. Contributes to the regulation of events that are under the control of prostaglandin levels. Catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4. Inhibits in vivo proliferation of colon cancer cells. Defects in HPGD are the cause of hypertrophic osteoarthropathy, primary, autosomal recessive, type 1 (PHOAR1). A disease characterized by digital clubbing, periostosis, acroosteolysis, painful joint enlargement, and variable features of pachydermia that include thickened facial skin and a thickened scalp. Other developmental anomalies include delayed closure of the cranial sutures and congenital heart disease. Defects in HPGD are the cause of cranioosteoarthropathy (COA). A form of osterarthropathy characterized by swelling of the joints, digital clubbing, hyperhidrosis, delayed closure of the fontanels, periostosis, and variable patent ductus arteriosus. Pachydermia is not a prominent feature. Defects in HPGD are a cause of isolated congenital nail clubbing (ICNC); also called clubbing of digits or hereditary acropachy. ICNC is a rare genodermatosis characterized by enlargement of the nail plate and terminal segments of the fingers and toes, resulting from proliferation of the connective tissues between the nail matrix and the distal phalanx. It is usually symmetrical and bilateral (in some cases unilateral). In nail clubbing usually the distal end of the nail matrix is relatively high compared to the proximal end, while the nail plate is complete but its dimensions and diameter more or less vary in comparison to normal. There may be different fingers and toes involved to varying degrees. Some fingers or toes are spared, but the thumbs are almost always involved. Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Oxidoreductase; EC 1.1.1.141
Cellular Component: basolateral plasma membrane; cytosol
Molecular Function: protein homodimerization activity; 15-hydroxyprostaglandin dehydrogenase (NAD+) activity; catalytic activity; NAD binding; prostaglandin E receptor activity
Biological Process: ovulation; lipoxygenase pathway; transforming growth factor beta receptor signaling pathway; cyclooxygenase pathway; arachidonic acid metabolic process; female pregnancy; parturition; prostaglandin metabolic process; negative regulation of cell cycle
Reference #:  P15428 (UniProtKB)
Alt. Names/Synonyms: 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostaglandin dehydrogenase [NAD+]; 15-PGDH; HPGD; hydroxyprostaglandin dehydrogenase 15-(NAD); NAD+-dependent 15-hydroxyprostaglandin dehydrogenase; PGDH; PGDH1; Prostaglandin dehydrogenase 1; SDR36C1; short chain dehydrogenase/reductase family 36C, member 1
Gene Symbols: HPGD
Molecular weight: 28,977 Da
Basal Isoelectric point: 5.56  Predict pI for various phosphorylation states
Select Structure to View Below

HPGD

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 Q69 QCDVADQQQLRDTFR
0 1 S110-p TLQINLVsVISGTYL
0 1 N173 ALAANLMNSGVRLNA
0 1 Y203-p KEENMGQyIEyKDHI
0 1 Y206-p NMGQyIEyKDHIKDM
0 1 K207 MGQyIEyKDHIKDMI
0 1 T246-p NGAIMKItTSKGIHF
0 1 K249 IMKItTSKGIHFQDy
0 2 Y256-p KGIHFQDyDttPFQA
0 1 T258-p IHFQDyDttPFQAKT
0 2 T259-p HFQDyDttPFQAKTQ
0 2 K264 DttPFQAKTQ_____
  mouse

 
K69-ub QCDVADQkQLRDTFR
S110 TLQINLVSVISGTYL
K173-ub AMAANLMkSGVRLNV
Y203 KEENMGQYIEYkDQI
Y206 NMGQYIEYkDQIKAM
K207-ub MGQYIEYkDQIKAMM
T246 NGAIMKITASkGIHF
K249-ub IMKITASkGIHFQDY
Y256 kGIHFQDYDIsPLLV
I258 IHFQDYDIsPLLVkA
S259-p HFQDYDIsPLLVkAP
K264-ub DIsPLLVkAPLTS__
  rat

 
K69 QCDVADQKQLRDTFR
S110 TLQINLVSVISGTYL
K173 AMAANLMKSGVRLNV
Y203 KEENMGQYIEYTDQI
Y206 NMGQYIEYTDQIKAM
T207 MGQYIEYTDQIKAMM
T246 NGAIMKITASKGIHF
K249 IMKITASKGIHFQDY
Y256 KGIHFQDYDLFPSFS
L258 IHFQDYDLFPSFSKA
F259 HFQDYDLFPSFSKAP
K264 DLFPSFSKAP_____
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