COLI_HUMAN - dbPTM
COLI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COLI_HUMAN
UniProt AC P01189
Protein Name Pro-opiomelanocortin
Gene Name POMC
Organism Homo sapiens (Human).
Sequence Length 267
Subcellular Localization Secreted . Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms.
Protein Description Corticotropin: Stimulates the adrenal glands to release cortisol.; Melanocyte-stimulating hormone alpha: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; Melanocyte-stimulating hormone beta: Increases the pigmentation of skin by increasing melanin production in melanocytes.; Beta-endorphin: Endogenous orexigenic opiate.; Met-enkephalin: Endogenous opiate..
Protein Sequence MPRSCCSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLLECIRACKPDLSAETPMFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNSSSSGSSGAGQKREDVSAGEDCGPLPEGGPEPRSDGAKPGPREGKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAEAFPLEFKRELTGQRLREGDGPDGPADDGAGAQADLEHSLLVAAEKKDEGPYRMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE
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
55PhosphorylationRACKPDLSAETPMFP
HHHCCCCCCCCCCCC
31.2929691806
58PhosphorylationKPDLSAETPMFPGNG
CCCCCCCCCCCCCCC
21.5529691806
71O-linked_GlycosylationNGDEQPLTENPRKYV
CCCCCCCCCCCCHHH
40.166267033
87Phenylalanine amideGHFRWDRFGRRNSSS
EEECCCCCCCCCCCC
9.17-
87AmidationGHFRWDRFGRRNSSS
EEECCCCCCCCCCCC
9.17-
91N-linked_GlycosylationWDRFGRRNSSSSGSS
CCCCCCCCCCCCCCC
44.906945581
92PhosphorylationDRFGRRNSSSSGSSG
CCCCCCCCCCCCCCC
29.77-
95PhosphorylationGRRNSSSSGSSGAGQ
CCCCCCCCCCCCCCC
44.64-
97PhosphorylationRNSSSSGSSGAGQKR
CCCCCCCCCCCCCCC
27.78-
108PhosphorylationGQKREDVSAGEDCGP
CCCCCCCCCCCCCCC
42.7629691806
125PhosphorylationEGGPEPRSDGAKPGP
CCCCCCCCCCCCCCC
51.6229691806
134AmidationGAKPGPREGKRSYSM
CCCCCCCCCCCCCCC
72.676272808
134Glutamic acid 1-amideGAKPGPREGKRSYSM
CCCCCCCCCCCCCCC
72.67-
138PhosphorylationGPREGKRSYSMEHFR
CCCCCCCCCCCCCCC
25.6629691806
138AcetylationGPREGKRSYSMEHFR
CCCCCCCCCCCCCCC
25.66-
140PhosphorylationREGKRSYSMEHFRWG
CCCCCCCCCCCCCCC
20.9529691806
150Valine amideHFRWGKPVGKKRRPV
CCCCCCCCCCCCCCE
23.34-
150AmidationHFRWGKPVGKKRRPV
CCCCCCCCCCCCCCE
23.34-
168PhosphorylationPNGAEDESAEAFPLE
CCCCCCCCCCCCCCH
43.6729691806
230PhosphorylationMEHFRWGSPPKDKRY
CCCCCCCCCCCCCCC
30.9427251275

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 COLI_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COLI_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 COLI_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MC4R_HUMANMC4Rphysical
11101306
MC4R_HUMANMC4Rphysical
9058374
MC5R_HUMANMC5Rphysical
9058374
MC3R_HUMANMC3Rphysical
9058374
MSHR_HUMANMC1Rphysical
9058374
A4_HUMANAPPphysical
21832049
TTL_HUMANTTLphysical
28514442
E2F4_HUMANE2F4physical
28514442
UBR4_HUMANUBR4physical
28514442
KLH15_HUMANKLHL15physical
28514442
DCAM_HUMANAMD1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
601665Obesity (OBESITY)
609734Pro-opiomelanocortinin deficiency (POMCD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COLI_HUMAN

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Related Literatures of Post-Translational Modification
Amidation
ReferencePubMed
"Alpha-amidated peptides derived from pro-opiomelanocortin in normalhuman pituitary.";
Fenger M., Johnsen A.H.;
Biochem. J. 250:781-788(1988).
Cited for: PROTEOLYTIC PROCESSING.
O-linked Glycosylation
ReferencePubMed
"Primary structure of the major human pituitary pro-opiomelanocortinNH2-terminal glycopeptide. Evidence for an aldosterone-stimulatingactivity.";
Seidah N.G., Rochemont J., Hamelin J., Lis M., Chretien M.;
J. Biol. Chem. 256:7977-7984(1981).
Cited for: PROTEIN SEQUENCE OF 27-102.
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND MASSSPECTROMETRY.

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