AMD_RAT - dbPTM
AMD_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMD_RAT
UniProt AC P14925
Protein Name Peptidyl-glycine alpha-amidating monooxygenase
Gene Name Pam
Organism Rattus norvegicus (Rat).
Sequence Length 976
Subcellular Localization Cytoplasmic vesicle, secretory vesicle membrane
Single-pass membrane protein. Secretory granules.
Protein Description Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity..
Protein Sequence MAGRARSGLLLLLLGLLALQSSCLAFRSPLSVFKRFKETTRSFSNECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTRVPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPAEANIPIPVKPDMVMMHGHHKEAENKEKSALMQQPKQGEEEVLEQGDFYSLLSKLLGEREDVHVHKYNPTEKTESGSDLVAEIANVVQKKDLGRSDAREGAEHEEWGNAILVRDRIHRFHQLESTLRPAESRAFSFQQPGEGPWEPEPSGDFHVEEELDWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSKFVYQQRGLGPIEEDTILVIDPNNAEILQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSMQPGSDQNHFCQPTDVAVEPSTGAVFVSDGYCNSRIVQFSPSGKFVTQWGEESSGSSPRPGQFSVPHSLALVPHLDQLCVADRENGRIQCFKTDTKEFVREIKHASFGRNVFAISYIPGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTEKMEHRSVKKAGIEVQEIKEAEAVVEPKVENKPTSSELQKMQEKQKLSTEPGSGVSVVLITTLLVIPVLVLLAIVMFIRWKKSRAFGDHDRKLESSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRVSTEGSDQEKDEDDGTESEEEYSAPLPKPAPSS
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
765N-linked_GlycosylationPVQGFVMNFSSGEII
CCCEEEEECCCCCEE
28.482211657
774 (in isoform 3)Sulfation-4.71-
792 (in isoform 4)Sulfation-51.20-
814AcetylationWKFTLTEKMEHRSVK
EEEEECHHHCCCCHH
44.3322902405
846PhosphorylationPKVENKPTSSELQKM
CCCCCCCCHHHHHHH
46.6328432305
847PhosphorylationKVENKPTSSELQKMQ
CCCCCCCHHHHHHHH
30.2728432305
848PhosphorylationVENKPTSSELQKMQE
CCCCCCHHHHHHHHH
44.8228432305
904UbiquitinationAFGDHDRKLESSSGR
CCCCCCCCCCCCCCC
63.76-
921PhosphorylationGRFRGKGSGGLNLGN
ECCCCCCCCCCCCHH
32.9227097102
932PhosphorylationNLGNFFASRKGYSRK
CCHHHHHCCCCCCCC
29.3927097102
937PhosphorylationFASRKGYSRKGFDRV
HHCCCCCCCCCCCCC
35.8610409666
945PhosphorylationRKGFDRVSTEGSDQE
CCCCCCCCCCCCCCC
22.9522673903
946PhosphorylationKGFDRVSTEGSDQEK
CCCCCCCCCCCCCCC
41.3220374556
949PhosphorylationDRVSTEGSDQEKDED
CCCCCCCCCCCCCCC
29.8610574929
959PhosphorylationEKDEDDGTESEEEYS
CCCCCCCCCCHHHCC
43.2522673903
961PhosphorylationDEDDGTESEEEYSAP
CCCCCCCCHHHCCCC
50.5822673903
965SulfationGTESEEEYSAPLPKP
CCCCHHHCCCCCCCC
17.26-

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
937SPhosphorylationKinasePRKCAP05696
GPS
946TPhosphorylationKinaseCSNK2A1P19139
GPS
949SPhosphorylationKinaseCSNK2A1P19139
GPS
949SPhosphorylationKinaseUHMK1Q63285
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMD_RAT !!

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 AMD_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
16098968

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMD_RAT

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Purification and characterization of functional recombinant alpha-amidating enzyme secreted from mammalian cells.";
Beaudry G.A., Mehta N.M., Ray M.L., Bertelsen A.H.;
J. Biol. Chem. 265:17694-17699(1990).
Cited for: PROTEIN SEQUENCE OF 26-42, AND GLYCOSYLATION AT ASN-765.

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