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Protein Page:
peptidase D (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
peptidase D Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen. Defects in PEPD are a cause of prolidase deficiency (PD). Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait. Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.13.9; Protease
Molecular Function: dipeptidase activity; manganese ion binding; aminopeptidase activity; metallocarboxypeptidase activity
Biological Process: amino acid metabolic process; collagen catabolic process; proteolysis
Reference #:  P12955 (UniProtKB)
Alt. Names/Synonyms: aminoacyl-L-proline hydrolase; Imidodipeptidase; MGC10905; PEPD; Peptidase D; PRD; Prolidase; Proline dipeptidase; X-Pro dipeptidase; Xaa-Pro dipeptidase
Gene Symbols: PEPD
Molecular weight: 54,548 Da
Basal Isoelectric point: 5.64  Predict pI for various phosphorylation states
Select Structure to View Below

peptidase D

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

► Hide Isoforms
 
0 2 K17-ac WLGNETLkVPLALFA
0 1 K17 WLGNETLKVPLALFA
0 1 K110-ac SHATWMGkIHSKEHF
0 1 K110 SHATWMGKIHSKEHF
0 1 K120 SKEHFKEKYAVDDVQ
0 2 Y128-p YAVDDVQyVDEIASV
0 1 S142 VLTSQKPSVLLTLRG
0 1 S167-p EASFDGIsKFEVNNT
0 1 K168 ASFDGIsKFEVNNTI
0 1 T188-p VECRVFKtDMELEVL
0 5 K303-ub GKFTADQkAVYEAVL
0 10 K484-ub ACMAGCDkAFtPFsG
0 1 T487-p AGCDkAFtPFsGPk_
0 1 S490-p DkAFtPFsGPk____
0 3 K493-ac FtPFsGPk_______
  peptidase D iso3  
K17 WLGNETLKVPLALFA
K17 WLGNETLKVPLALFA
- gap
- gap
- gap
- gap
S78-p VLTSQKPsVLLTLRG
S103 EASFDGISKFEVNNT
K104 ASFDGISKFEVNNTI
T124 VECRVFKTDMELEVL
K239 GKFTADQKAVYEAVL
K420 ACMAGCDKAFTPFSG
T423 AGCDKAFTPFSGPK_
S426 DKAFTPFSGPK____
K429 FTPFSGPK_______
  mouse

 
K17 SLGNETLKVPLALFA
K17-ub SLGNETLkVPLALFA
K110 SYATWMGKIHSKEYF
K110-ub SYATWMGkIHSKEYF
K120-ub SKEYFKEkYAVDDVQ
Y128 YAVDDVQYTDEIASV
S142 VLTSRNPSVLLTLRG
S167 EASFEGISkFNVNNT
K168-ub ASFEGISkFNVNNTI
T188 VECRVFKTDMELEVL
K303-ub GKFTEDQkAIYEAVL
K484-ub ACMAGCDkASVPFSG
V487 AGCDkASVPFSGQK_
S490 DkASVPFSGQK____
K493 SVPFSGQK_______
  rat

 
K17 SLGNETLKVPLALFA
K17 SLGNETLKVPLALFA
K110-ac SYATWMGkIHSKEHF
K110 SYATWMGKIHSKEHF
K120 SKEHFKEKYAVDDVQ
Y128 YAVDDVQYADEIASV
S142 VLTSRNPSVLLTLRG
S167-p EASFEGIsKFTVNNT
K168 ASFEGIsKFTVNNTI
T188 VECRVFKTDMELEVL
K303 GKFTDDQKAIYEAVL
K484-ub ACMAGCDkALAPSGP
A487 AGCDkALAPSGPK__
S489 CDkALAPSGPK____
K492 ALAPSGPK_______
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