PEPD_HUMAN - dbPTM
PEPD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PEPD_HUMAN
UniProt AC P12955
Protein Name Xaa-Pro dipeptidase
Gene Name PEPD
Organism Homo sapiens (Human).
Sequence Length 493
Subcellular Localization
Protein Description 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..
Protein Sequence MAAATGPSFWLGNETLKVPLALFALNRQRLCERLRKNPAVQAGSIVVLQGGEETQRYCTDTGVLFRQESFFHWAFGVTEPGCYGVIDVDTGKSTLFVPRLPASHATWMGKIHSKEHFKEKYAVDDVQYVDEIASVLTSQKPSVLLTLRGVNTDSGSVCREASFDGISKFEVNNTILHPEIVECRVFKTDMELEVLRYTNKISSEAHREVMKAVKVGMKEYELESLFEHYCYSRGGMRHSSYTCICGSGENSAVLHYGHAGAPNDRTIQNGDMCLFDMGGEYYCFASDITCSFPANGKFTADQKAVYEAVLRSSRAVMGAMKPGVWWPDMHRLADRIHLEELAHMGILSGSVDAMVQAHLGAVFMPHGLGHFLGIDVHDVGGYPEGVERIDEPGLRSLRTARHLQPGMVLTVEPGIYFIDHLLDEALADPARASFLNREVLQRFRGFGGVRIEEDVVVTDSGIELLTCVPRTVEEIEACMAGCDKAFTPFSGPK
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
2Acetylation------MAAATGPSF
------CCCCCCCCC
13.0522223895
5Phosphorylation---MAAATGPSFWLG
---CCCCCCCCCCCC
44.9220068231
8PhosphorylationMAAATGPSFWLGNET
CCCCCCCCCCCCCCC
30.3320068231
15PhosphorylationSFWLGNETLKVPLAL
CCCCCCCCCHHCHHH
35.5620068231
17AcetylationWLGNETLKVPLALFA
CCCCCCCHHCHHHHH
49.5819816731
36UbiquitinationRLCERLRKNPAVQAG
HHHHHHHHCCCCCCC
72.3922053931
108SulfoxidationPASHATWMGKIHSKE
CCCCCCHHCCCCCHH
3.2130846556
110AcetylationSHATWMGKIHSKEHF
CCCCHHCCCCCHHHH
22.5723954790
110UbiquitinationSHATWMGKIHSKEHF
CCCCHHCCCCCHHHH
22.57-
113PhosphorylationTWMGKIHSKEHFKEK
CHHCCCCCHHHHHHH
43.1228348404
114UbiquitinationWMGKIHSKEHFKEKY
HHCCCCCHHHHHHHH
40.83-
120UbiquitinationSKEHFKEKYAVDDVQ
CHHHHHHHHCCCCHH
38.82-
128PhosphorylationYAVDDVQYVDEIASV
HCCCCHHHHHHHHHH
15.09-
142PhosphorylationVLTSQKPSVLLTLRG
HHHCCCCCEEEEECC
32.22-
156PhosphorylationGVNTDSGSVCREASF
CCCCCCCCCCCCCCC
23.2328857561
167PhosphorylationEASFDGISKFEVNNT
CCCCCCCCEEEECCE
36.508900231
188PhosphorylationVECRVFKTDMELEVL
EEEEEEECCHHHHHH
29.1616097034
190SulfoxidationCRVFKTDMELEVLRY
EEEEECCHHHHHHHH
8.4021406390
196MethylationDMELEVLRYTNKISS
CHHHHHHHHCCCCCH
41.21115486993
200UbiquitinationEVLRYTNKISSEAHR
HHHHHCCCCCHHHHH
35.84-
303UbiquitinationGKFTADQKAVYEAVL
CCCCCCHHHHHHHHH
40.1321906983
306PhosphorylationTADQKAVYEAVLRSS
CCCHHHHHHHHHHHC
11.7520068231
484UbiquitinationACMAGCDKAFTPFSG
HHHCCCCCCCCCCCC
49.85-
487PhosphorylationAGCDKAFTPFSGPK-
CCCCCCCCCCCCCC-
28.4327499020
490PhosphorylationDKAFTPFSGPK----
CCCCCCCCCCC----
56.2223403867
493AcetylationFTPFSGPK-------
CCCCCCCC-------
76.2190257

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 PEPD_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PEPD_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 PEPD_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OSTP_HUMANSPP1physical
21988832
ASSY_HUMANASS1physical
22863883
BCCIP_HUMANBCCIPphysical
22863883
CAN1_HUMANCAPN1physical
22863883
CASP7_HUMANCASP7physical
22863883
DLDH_HUMANDLDphysical
22863883
DPP3_HUMANDPP3physical
22863883
IF5A1_HUMANEIF5Aphysical
22863883
FTO_HUMANFTOphysical
22863883
GBP2_HUMANGBP2physical
22863883
GUAD_HUMANGDAphysical
22863883
PSF2_HUMANGINS2physical
22863883
GLSK_HUMANGLSphysical
22863883
GNS_HUMANGNSphysical
22863883
LDH6B_HUMANLDHAL6Bphysical
22863883
MVD1_HUMANMVDphysical
22863883
NDRG1_HUMANNDRG1physical
22863883
KS6A1_HUMANRPS6KA1physical
22863883
AATC_HUMANGOT1physical
26344197
CH10_HUMANHSPE1physical
26344197
PSMG4_HUMANPSMG4physical
26344197
TNG2_HUMANTANGO2physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
170100Prolidase deficiency (PD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PEPD_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 ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASSSPECTROMETRY.

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