AMD_HUMAN - dbPTM
AMD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMD_HUMAN
UniProt AC P19021
Protein Name Peptidyl-glycine alpha-amidating monooxygenase
Gene Name PAM
Organism Homo sapiens (Human).
Sequence Length 973
Subcellular Localization Isoform 1: Membrane
Single-pass type I membrane protein.
Isoform 2: Membrane
Single-pass type I membrane protein.
Isoform 3: Secreted. Secreted from secretory granules.
Isoform 4: Secreted. Secreted from 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 MAGRVPSLLVLLVFPSSCLAFRSPLSVFKRFKETTRPFSNECLGTTRPVVPIDSSDFALDIRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNNKDCSGVSLHLTRLPQPLIAGMYLMMSVDTVIPAGEKVVNSDISCHYKNYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPPEANIPIPVKSDMVMMHEHHKETEYKDKIPLLQQPKREEEEVLDQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESESDLVAEIANVVQKKDLGRSDAREGAEHERGNAILVRDRIHKFHRLVSTLRPPESRVFSLQQPPPGEGTWEPEHTGDFHMEEALDWPGVYLLPGQVSGVALDPKNNLVIFHRGDHVWDGNSFDSKFVYQQIGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALHQVFKLDPNNKEGPVLILGRSMQPGSDQNHFCQPTDVAVDPGTGAIYVSDGYCNSRIVQFSPSGKFITQWGEESSGSSPLPGQFTVPHSLALVPLLGQLCVADRENGRIQCFKTDTKEFVREIKHSSFGRNVFAISYIPGLLFAVNGKPHFGDQEPVQGFVMNFSNGEIIDIFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTEKLEHRSVKKAGIEVQEIKEAEAVVETKMENKPTSSELQKMQEKQKLIKEPGSGVPVVLITTLLVIPVVVLLAIAIFIRWKKSRAFGDSEHKLETSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKEDDGSESEEEYSAPLPALAPSSS
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
35O-linked_GlycosylationFKRFKETTRPFSNEC
HHHHHHCCCCCCCCC		37.12OGP
45O-linked_GlycosylationFSNECLGTTRPVVPI
CCCCCCCCCCCEEEC		13.49OGP
46O-linked_GlycosylationSNECLGTTRPVVPID
CCCCCCCCCCEEECC		31.04OGP
69 (in isoform 5)Ubiquitination-53.74-
69UbiquitinationRMPGVTPKQSDTYFC
ECCCCCCCCCCCEEE		53.74-
93 (in isoform 2)Ubiquitination-29.8221890473
93UbiquitinationEAFVIDFKPRASMDT
CEEEEECCCCCCCCC		29.8221906983
93 (in isoform 3)Ubiquitination-29.8221890473
93 (in isoform 4)Ubiquitination-29.8221906983
172PhosphorylationQVHYGDISAFRDNNK
EEEECCHHHCCCCCC		26.5424719451
278UbiquitinationPVGHPVDVSFGDLLA
CCCCCCCCCHHHHEE		5.3421890473
328PhosphorylationKHAVSFMTCTQNVAP
HHHHCEEECCCCCCC		15.4725332170
340PhosphorylationVAPDMFRTIPPEANI
CCCCHHCCCCCCCCC		26.9425332170
392PhosphorylationLDQGDFYSLLSKLLG
HCHHHHHHHHHHHHC		23.8724719451
396UbiquitinationDFYSLLSKLLGERED
HHHHHHHHHHCCCCC		47.93-
409UbiquitinationEDVVHVHKYNPTEKA
CCEEEEEECCCCCCC		45.7121906983
409 (in isoform 3)Ubiquitination-45.7121890473
409 (in isoform 4)Ubiquitination-45.7121906983
413O-linked_GlycosylationHVHKYNPTEKAESES
EEEECCCCCCCCCHH		46.6255830559
415 (in isoform 3)Ubiquitination-60.9921890473
415 (in isoform 4)Ubiquitination-60.9921906983
415UbiquitinationHKYNPTEKAESESDL
EECCCCCCCCCHHHH		60.9921906983
418PhosphorylationNPTEKAESESDLVAE
CCCCCCCCHHHHHHH		47.4629507054
418O-linked_GlycosylationNPTEKAESESDLVAE
CCCCCCCCHHHHHHH		47.46OGP
432 (in isoform 4)Ubiquitination-36.3221906983
432UbiquitinationEIANVVQKKDLGRSD
HHHHHHHHHHCCCCC		36.3221906983
432 (in isoform 3)Ubiquitination-36.3221890473
466O-linked_GlycosylationHKFHRLVSTLRPPES
HHHHHHHHCCCCCHH		26.7355831067
467O-linked_GlycosylationKFHRLVSTLRPPESR
HHHHHHHCCCCCHHC		21.2155831069
473O-linked_GlycosylationSTLRPPESRVFSLQQ
HCCCCCHHCEEEECC		39.2555831071
503 (in isoform 2)Ubiquitination-57.4821890473
609 (in isoform 2)Ubiquitination-49.4921890473
610UbiquitinationFKLDPNNKEGPVLIL
EECCCCCCCCCEEEE		71.3521906983
610 (in isoform 4)Ubiquitination-71.3521906983
610 (in isoform 3)Ubiquitination-71.3521890473
620PhosphorylationPVLILGRSMQPGSDQ
CEEEEECCCCCCCCC		21.70-
648PhosphorylationGTGAIYVSDGYCNSR
CCCEEEEECCCCCCE		14.35-
651PhosphorylationAIYVSDGYCNSRIVQ
EEEEECCCCCCEEEE		8.0819060867
712UbiquitinationNGRIQCFKTDTKEFV
CCCEEEEECCHHHHH		53.79-
712 (in isoform 2)Ubiquitination-53.7921890473
716UbiquitinationQCFKTDTKEFVREIK
EEEECCHHHHHHHHH		52.5521906983
716 (in isoform 4)Ubiquitination-52.5521906983
716 (in isoform 3)Ubiquitination-52.5521890473
735PhosphorylationGRNVFAISYIPGLLF
CCCEEEEEECCCCEE		17.3622210691
736PhosphorylationRNVFAISYIPGLLFA
CCEEEEEECCCCEEE		12.6722210691
762N-linked_GlycosylationPVQGFVMNFSNGEII
CCCEEEEECCCCCEE		31.71UniProtKB CARBOHYD
794 (in isoform 2)Ubiquitination-10.0621890473
809 (in isoform 2)Ubiquitination-28.1921890473
819 (in isoform 4)Ubiquitination-50.0921906983
819UbiquitinationLEHRSVKKAGIEVQE
HHCCCHHHCCCCHHH		50.0921906983
819 (in isoform 3)Ubiquitination-50.0921890473
836PhosphorylationEAEAVVETKMENKPT
HHHHHHHHHHCCCCC		24.8719651622
843O-linked_GlycosylationTKMENKPTSSELQKM
HHHCCCCCHHHHHHH		46.63OGP
848 (in isoform 3)Ubiquitination-34.8121890473
875 (in isoform 4)Sulfation-1.858144680
892PhosphorylationIFIRWKKSRAFGDSE
HHHHHHHHHCCCCCC		25.7222985185
892 (in isoform 5)Phosphorylation-25.72-
893 (in isoform 3)Sulfation-42.708144680
899 (in isoform 5)Phosphorylation-50.1926657352
901UbiquitinationAFGDSEHKLETSSGR
CCCCCCCEEEECCCC		43.9221906983
916 (in isoform 1)Ubiquitination-45.7221890473
916UbiquitinationVLGRFRGKGSGGLNL
EEECCCCCCCCCCCC		45.722189047
917 (in isoform 5)Ubiquitination-34.05-
917UbiquitinationLGRFRGKGSGGLNLG
EECCCCCCCCCCCCH		34.0521890473
918PhosphorylationGRFRGKGSGGLNLGN
ECCCCCCCCCCCCHH		32.9225159151
929PhosphorylationNLGNFFASRKGYSRK
CCHHHHHCCCCCCCC		29.3925159151
934PhosphorylationFASRKGYSRKGFDRL
HHCCCCCCCCCCCCC		35.868530412
942PhosphorylationRKGFDRLSTEGSDQE
CCCCCCCCCCCCCCC		25.8825159151
943PhosphorylationKGFDRLSTEGSDQEK
CCCCCCCCCCCCCCC		49.2925159151
946PhosphorylationDRLSTEGSDQEKEDD
CCCCCCCCCCCCCCC		29.8628355574
955PhosphorylationQEKEDDGSESEEEYS
CCCCCCCCCCHHHHC		44.9725159151
957PhosphorylationKEDDGSESEEEYSAP
CCCCCCCCHHHHCCC		52.5925159151
961SulfationGSESEEEYSAPLPAL
CCCCHHHHCCCCCCC		17.26-
961PhosphorylationGSESEEEYSAPLPAL
CCCCHHHHCCCCCCC		17.2621406692
962PhosphorylationSESEEEYSAPLPALA
CCCHHHHCCCCCCCC		27.0421406692
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
929SPhosphorylationKinasePKC-FAMILY-GPS
929SPhosphorylationKinasePKC_GROUP-PhosphoELM
934SPhosphorylationKinasePKC-FAMILY-GPS
934SPhosphorylationKinasePKC_GROUP-PhosphoELM
946SPhosphorylationKinaseUHMK1Q8TAS1
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMD_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 AMD_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TSC1_HUMANTSC1physical
14559897
TSC2_HUMANTSC2physical
14559897
RASF9_HUMANRASSF9physical
9837933
KALRN_HUMANKALRNphysical
9139723
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 AMD_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-929, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-955 AND SER-957, ANDMASS SPECTROMETRY.
Sulfation
ReferencePubMed
"Alternative splicing governs sulfation of tyrosine or oligosaccharideon peptidylglycine alpha-amidating monooxygenase.";
Yun H.Y., Keutmann H.T., Eipper B.A.;
J. Biol. Chem. 269:10946-10955(1994).
Cited for: SULFATION AT TYR-961.

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