CNDP1_HUMAN - dbPTM
CNDP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNDP1_HUMAN
UniProt AC Q96KN2
Protein Name Beta-Ala-His dipeptidase
Gene Name CNDP1
Organism Homo sapiens (Human).
Sequence Length 507
Subcellular Localization Secreted.
Protein Description
Protein Sequence MDPKLGRMAASLLAVLLLLLERGMFSSPSPPPALLEKVFQYIDLHQDEFVQTLKEWVAIESDSVQPVPRFRQELFRMMAVAADTLQRLGARVASVDMGPQQLPDGQSLPIPPIILAELGSDPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEEAGSVALEELVEKEKDRFFSGVDYIVISDNLWISQRKPAITYGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVDSSGHILVPGIYDEVVPLTEEEINTYKAIHLDLEEYRNSSRVEKFLFDTKEEILMHLWRYPSLSIHGIEGAFDEPGTKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKRNSSNKMVVSMTLGLHPWIANIDDTQYLAAKRAIRTVFGTEPDMIRDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQNEKINRWNYIEGTKLFAAFFLEMAQLH
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
29O-linked_GlycosylationRGMFSSPSPPPALLE
CCCCCCCCCCHHHHH
52.57OGP
61PhosphorylationKEWVAIESDSVQPVP
HHHHCCCCCCCCCCH
29.1326074081
63PhosphorylationWVAIESDSVQPVPRF
HHCCCCCCCCCCHHH
31.7526074081
146O-linked_GlycosylationDRGDGWLTDPYVLTE
CCCCCCCCCCEEEEE
28.55OGP
219PhosphorylationKEKDRFFSGVDYIVI
HHHHCCCCCCCEEEE
34.88-
322N-linked_GlycosylationLDLEEYRNSSRVEKF
CCHHHHHCCHHHHHH
43.3616335952
346PhosphorylationMHLWRYPSLSIHGIE
HHHHHCCCCEECCCC
26.30-
363PhosphorylationFDEPGTKTVIPGRVI
CCCCCCEEEECCEEE
24.41-
382N-linked_GlycosylationIRLVPHMNVSAVEKQ
EEECCCCCHHHHHHH
22.8916335952
382N-linked_GlycosylationIRLVPHMNVSAVEKQ
EEECCCCCHHHHHHH
22.8916335952
425PhosphorylationWIANIDDTQYLAAKR
HHCCCCHHHHHHHHH
18.5024719451
427PhosphorylationANIDDTQYLAAKRAI
CCCCHHHHHHHHHHH
10.6224719451
440PhosphorylationAIRTVFGTEPDMIRD
HHHHHHCCCHHHCCC
32.64-

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 CNDP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNDP1_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 CNDP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
POTEF_HUMANPOTEFphysical
26186194
RAB3B_HUMANRAB3Bphysical
26186194
CNDP2_HUMANCNDP2physical
26186194
GDC_HUMANSLC25A16physical
26186194
CX7A2_HUMANCOX7A2physical
26186194
PIGM_HUMANPIGMphysical
26186194
ARF5_HUMANARF5physical
26186194
WRB_HUMANWRBphysical
26186194
MANEA_HUMANMANEAphysical
26186194
SCD5_HUMANSCD5physical
26186194
2B1F_HUMANHLA-DRB1physical
26186194
2B13_HUMANHLA-DRB1physical
26186194
2B1G_HUMANHLA-DRB1physical
26186194
POTEF_HUMANPOTEFphysical
28514442
CNDP2_HUMANCNDP2physical
28514442
MOT10_HUMANSLC16A10physical
28514442
RAB3B_HUMANRAB3Bphysical
28514442
MANEA_HUMANMANEAphysical
28514442
GDC_HUMANSLC25A16physical
28514442
CX7A2_HUMANCOX7A2physical
28514442
PIGM_HUMANPIGMphysical
28514442
ADT3_HUMANSLC25A6physical
28514442

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 CNDP1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-322 AND ASN-382, AND MASSSPECTROMETRY.

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