PLMN_HUMAN - dbPTM
PLMN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLMN_HUMAN
UniProt AC P00747
Protein Name Plasminogen
Gene Name PLG
Organism Homo sapiens (Human).
Sequence Length 810
Subcellular Localization Secreted . Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface.
Protein Description Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells.; Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo..
Protein Sequence MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNN
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
16PhosphorylationLLLLFLKSGQGEPLD
HHHHHHHHCCCCCHH		38.2022210691
25PhosphorylationQGEPLDDYVNTQGAS
CCCCHHHHHCCCCHH		8.6822210691
28PhosphorylationPLDDYVNTQGASLFS
CHHHHHCCCCHHHEE		20.5222210691
28O-linked_GlycosylationPLDDYVNTQGASLFS
CHHHHHCCCCHHHEE		20.52OGP
32PhosphorylationYVNTQGASLFSVTKK
HHCCCCHHHEEECHH		36.4522210691
35PhosphorylationTQGASLFSVTKKQLG
CCCHHHEEECHHHHC		33.88-
45PhosphorylationKKQLGAGSIEECAAK
HHHHCCCCHHHHHHH		26.7127130503
66PhosphorylationFTCRAFQYHSKEQQC
CEEEEEEEECCCCEE		11.1228857561
68PhosphorylationCRAFQYHSKEQQCVI
EEEEEEECCCCEEEE		32.7127130503
82PhosphorylationIMAENRKSSIIIRMR
EEECCCCCEEEEEEC		24.4324275569
83PhosphorylationMAENRKSSIIIRMRD
EECCCCCEEEEEECE		22.3528857561
99PhosphorylationVLFEKKVYLSECKTG
EEEEEEEEEEECCCC		17.25-
111PhosphorylationKTGNGKNYRGTMSKT
CCCCCCCCCCCCCCC		17.57-
189PhosphorylationEEECMHCSGENYDGK
EHHHHCCCCCCCCCC		34.1727130503
200PhosphorylationYDGKISKTMSGLECQ
CCCCEECCCCCCEEE		15.13-
222PhosphorylationHAHGYIPSKFPNKNL
CCCCCCCCCCCCCCC		37.0524719451
263PhosphorylationLCDIPRCTTPPPSSG
ECCCCCCCCCCCCCC		43.5529632367
263O-linked_GlycosylationLCDIPRCTTPPPSSG
ECCCCCCCCCCCCCC		43.55OGP
264PhosphorylationCDIPRCTTPPPSSGP
CCCCCCCCCCCCCCC		37.1129632367
264O-linked_GlycosylationCDIPRCTTPPPSSGP
CCCCCCCCCCCCCCC		37.11OGP
268O-linked_GlycosylationRCTTPPPSSGPTYQC
CCCCCCCCCCCCCEE		54.429054441
268PhosphorylationRCTTPPPSSGPTYQC
CCCCCCCCCCCCCEE		54.4229632367
268O-linked_GlycosylationRCTTPPPSSGPTYQC
CCCCCCCCCCCCCEE		54.429054441
269O-linked_GlycosylationCTTPPPSSGPTYQCL
CCCCCCCCCCCCEEE		55.34OGP
269PhosphorylationCTTPPPSSGPTYQCL
CCCCCCCCCCCCEEE		55.3429632367
279PhosphorylationTYQCLKGTGENYRGN
CCEEEECCCCCCCCC		39.47-
308N-linked_GlycosylationAQTPHTHNRTPENFP
CCCCCCCCCCCCCCC		51.153356193
308N-linked_GlycosylationAQTPHTHNRTPENFP
CCCCCCCCCCCCCCC		51.1518780401
340PhosphorylationPWCHTTNSQVRWEYC
CCCCCCCCCEEEEEE		28.1428857561
346PhosphorylationNSQVRWEYCKIPSCD
CCCEEEEEECCCCCC		7.6524505115
351PhosphorylationWEYCKIPSCDSSPVS
EEEECCCCCCCCCCC		33.7524505115
354PhosphorylationCKIPSCDSSPVSTEQ
ECCCCCCCCCCCHHH		40.6524505115
355PhosphorylationKIPSCDSSPVSTEQL
CCCCCCCCCCCHHHH		18.9724505115
358O-linked_GlycosylationSCDSSPVSTEQLAPT
CCCCCCCCHHHHCCC		29.61OGP
358PhosphorylationSCDSSPVSTEQLAPT
CCCCCCCCHHHHCCC		29.6124505115
359O-linked_GlycosylationCDSSPVSTEQLAPTA
CCCCCCCHHHHCCCC		28.16OGP
359PhosphorylationCDSSPVSTEQLAPTA
CCCCCCCHHHHCCCC		28.1624505115
365O-linked_GlycosylationSTEQLAPTAPPELTP
CHHHHCCCCCCCCCC		46.30479158
365PhosphorylationSTEQLAPTAPPELTP
CHHHHCCCCCCCCCC		46.3024505115
365O-linked_GlycosylationSTEQLAPTAPPELTP
CHHHHCCCCCCCCCC		46.30479158
371O-linked_GlycosylationPTAPPELTPVVQDCY
CCCCCCCCCCCCEEE		16.63OGP
371PhosphorylationPTAPPELTPVVQDCY
CCCCCCCCCCCCEEE		16.6324505115
416NitrationHQKTPENYPNAGLTM
CCCCCCCCCCCCCCC		9.01-
422PhosphorylationNYPNAGLTMNYCRNP
CCCCCCCCCCCCCCC		11.49-
425PhosphorylationNAGLTMNYCRNPDAD
CCCCCCCCCCCCCCC		5.07-
425NitrationNAGLTMNYCRNPDAD
CCCCCCCCCCCCCCC		5.07-
457O-linked_GlycosylationNLKKCSGTEASVVAP
CCCCCCCCCCEEECC		16.45OGP
460O-linked_GlycosylationKCSGTEASVVAPPPV
CCCCCCCEEECCCCE		15.76OGP
477PhosphorylationLPDVETPSEEDCMFG
CCCCCCCCHHHCCCC		62.1226657352
544PhosphorylationDVGGPWCYTTNPRKL
CCCCCCEECCCCCHH		16.8422210691
545PhosphorylationVGGPWCYTTNPRKLY
CCCCCEECCCCCHHH		19.5722210691
564PhosphorylationVPQCAAPSFDCGKPQ
CCCCCCCCCCCCCCC		29.0522210691
597PhosphorylationHSWPWQVSLRTRFGM
CCCCCEEEEEEEECC		9.3128857561
662PhosphorylationSRLFLEPTRKDIALL
EEECCCCCHHHEEEE		40.76-
673PhosphorylationIALLKLSSPAVITDK
EEEEECCCCCEECCC		27.5824505115
678PhosphorylationLSSPAVITDKVIPAC
CCCCCEECCCCCCCC		24.14-
688PhosphorylationVIPACLPSPNYVVAD
CCCCCCCCCCEEEEC		16.9010233898
710O-linked_GlycosylationGWGETQGTFGAGLLK
CCCCCCCCCCCHHHH		14.74OGP
741PhosphorylationFLNGRVQSTELCAGH
HHCCCCCCCCCCCCH		22.4627130503
742O-linked_GlycosylationLNGRVQSTELCAGHL
HCCCCCCCCCCCCHH		18.84OGP
742PhosphorylationLNGRVQSTELCAGHL
HCCCCCCCCCCCCHH		18.8427130503
753PhosphorylationAGHLAGGTDSCQGDS
CCHHCCCCCCCCCCC		24.6624505115
755PhosphorylationHLAGGTDSCQGDSGG
HHCCCCCCCCCCCCC		14.2624505115
760PhosphorylationTDSCQGDSGGPLVCF
CCCCCCCCCCCEEEE		53.1028270605
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 PLMN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLMN_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
32Phosphorylation38 (6)K ⇒ Ers73015965
  • Childhood ear infection
27182965
28928442
35Phosphorylation38 (3)K ⇒ Ers73015965
  • Childhood ear infection
27182965
28928442
45Phosphorylation38 (7)K ⇒ Ers73015965
  • Childhood ear infection
27182965
28928442
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAI1_HUMANSERPINE1physical
11113116
IBP3_HUMANIGFBP3physical
9688635
S10AA_HUMANS100A10physical
11939791
CMGA_HUMANCHGAphysical
11342539
HMGB1_HUMANHMGB1physical
1909331
CO7_HUMANC7physical
7814888
TSP1_HUMANTHBS1physical
2522013
PAPP1_HUMANPAPPAphysical
7586586
KNG1_HUMANKNG1physical
9428707
CBPB2_HUMANCPB2physical
1939207
A2AP_HUMANSERPINF2physical
158022
SPRC_HUMANSPARCphysical
7982919
A2AP_HUMANSERPINF2physical
2437112
TF_HUMANF3physical
9490681
HSPB1_HUMANHSPB1physical
17206383
CH60_HUMANHSPD1physical
17206383
ACTB_HUMANACTBphysical
15746964
SMAD3_HUMANSMAD3physical
21988832
SMAD4_HUMANSMAD4physical
21988832
PRDX4_HUMANPRDX4physical
21988832
YTDC1_HUMANYTHDC1physical
21988832
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
217090Plasminogen deficiency (PLGD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLMN_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry.";
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
Proteomics 8:3833-3847(2008).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308, AND MASSSPECTROMETRY.
O-linked Glycosylation
ReferencePubMed
"Evidence for a novel O-linked sialylated trisaccharide on Ser-248 ofhuman plasminogen 2.";
Pirie-Shepherd S.R., Stevens R.D., Andon N.L., Enghild J.J.,Pizzo S.V.;
J. Biol. Chem. 272:7408-7411(1997).
Cited for: GLYCOSYLATION AT SER-268.
Phosphorylation
ReferencePubMed
"Serine-578 is a major phosphorylation locus in human plasmaplasminogen.";
Wang H., Prorok M., Bretthauer R.K., Castellino F.J.;
Biochemistry 36:8100-8106(1997).
Cited for: PHOSPHORYLATION AT SER-597.

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