PEDF_HUMAN - dbPTM
PEDF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PEDF_HUMAN
UniProt AC P36955
Protein Name Pigment epithelium-derived factor
Gene Name SERPINF1
Organism Homo sapiens (Human).
Sequence Length 418
Subcellular Localization Secreted . Melanosome . Enriched in stage I melanosomes.
Protein Description Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity..
Protein Sequence MQALVLLLCIGALLGHSSCQNPASPPEEGSPDPDSTGALVEEEDPFFKVPVNKLAAAVSNFGYDLYRVRSSTSPTTNVLLSPLSVATALSALSLGAEQRTESIIHRALYYDLISSPDIHGTYKELLDTVTAPQKNLKSASRIVFEKKLRIKSSFVAPLEKSYGTRPRVLTGNPRLDLQEINNWVQAQMKGKLARSTKEIPDEISILLLGVAHFKGQWVTKFDSRKTSLEDFYLDEERTVRVPMMSDPKAVLRYGLDSDLSCKIAQLPLTGSMSIIFFLPLKVTQNLTLIEESLTSEFIHDIDRELKTVQAVLTVPKLKLSYEGEVTKSLQEMKLQSLFDSPDFSKITGKPIKLTQVEHRAGFEWNEDGAGTTPSPGLQPAHLTFPLDYHLNQPFIFVLRDTDTGALLFIGKILDPRGP
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
20Pyrrolidone_carboxylic_acidLLGHSSCQNPASPPE
HHCCCCCCCCCCCCC
61.97-
20Pyrrolidone_carboxylic_acidLLGHSSCQNPASPPE
HHCCCCCCCCCCCCC
61.9712737624
20Pyrrolidone_carboxylic_acidLLGHSSCQNPASPPE
HHCCCCCCCCCCCCC
61.9712737624
24PhosphorylationSSCQNPASPPEEGSP
CCCCCCCCCCCCCCC
42.0926657352
24O-linked_GlycosylationSSCQNPASPPEEGSP
CCCCCCCCCCCCCCC
42.09OGP
30O-linked_GlycosylationASPPEEGSPDPDSTG
CCCCCCCCCCCCCCC
29.43OGP
30PhosphorylationASPPEEGSPDPDSTG
CCCCCCCCCCCCCCC
29.4326657352
35PhosphorylationEGSPDPDSTGALVEE
CCCCCCCCCCCCCCC
33.8426657352
36O-linked_GlycosylationGSPDPDSTGALVEEE
CCCCCCCCCCCCCCC
33.58OGP
36PhosphorylationGSPDPDSTGALVEEE
CCCCCCCCCCCCCCC
33.5826657352
114PhosphorylationALYYDLISSPDIHGT
HHHHHHHCCCCCCCC
43.0222817900
152PhosphorylationEKKLRIKSSFVAPLE
EEEHHCCEEEEECCH
27.00-
153PhosphorylationKKLRIKSSFVAPLEK
EEHHCCEEEEECCHH
20.81-
227PhosphorylationKFDSRKTSLEDFYLD
CCCCCCCCHHHHCCC
32.5621082442
283PhosphorylationFFLPLKVTQNLTLIE
EEEEEEECCCEEHHH
15.34-
285N-linked_GlycosylationLPLKVTQNLTLIEES
EEEEECCCEEHHHHH
26.1511562499
285N-linked_GlycosylationLPLKVTQNLTLIEES
EEEEECCCEEHHHHH
26.1511562499
287PhosphorylationLKVTQNLTLIEESLT
EEECCCEEHHHHHHH
32.99-
294PhosphorylationTLIEESLTSEFIHDI
EHHHHHHHHHHHHHH
35.17-
295PhosphorylationLIEESLTSEFIHDID
HHHHHHHHHHHHHHH
35.48-
313PhosphorylationKTVQAVLTVPKLKLS
CHHHHHEECCCCCCE
28.3224719451
316MethylationQAVLTVPKLKLSYEG
HHHEECCCCCCEECC
54.65-
372O-linked_GlycosylationNEDGAGTTPSPGLQP
CCCCCCCCCCCCCCC
22.35OGP
374O-linked_GlycosylationDGAGTTPSPGLQPAH
CCCCCCCCCCCCCCE
29.52OGP

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
24SPhosphorylationKinaseCSNK2A1P68400
GPS
24SPhosphorylationKinaseCK2-FAMILY-GPS
24SPhosphorylationKinaseCK2-Uniprot
114SPhosphorylationKinaseCSNK2A1P68400
GPS
114SPhosphorylationKinaseCK2-FAMILY-GPS
114SPhosphorylationKinaseCK2-Uniprot
227SPhosphorylationKinasePRKACAP17612
GPS
227SPhosphorylationKinasePKA-FAMILY-GPS
227SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PEDF_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 PEDF_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLPL2_HUMANPNPLA2physical
18191271
EPMIP_HUMANEPM2AIP1physical
25416956
LMBL2_HUMANL3MBTL2physical
28514442
KLHL8_HUMANKLHL8physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
GRP78_HUMANHSPA5physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613982Osteogenesis imperfecta 6 (OI6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PEDF_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Crystal structure of human PEDF, a potent anti-angiogenic and neuritegrowth-promoting factor.";
Simonovic M., Gettins P.G.W., Volz K.;
Proc. Natl. Acad. Sci. U.S.A. 98:11131-11135(2001).
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 21-418, AND GLYCOSYLATION ATASN-285.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-285, AND MASSSPECTROMETRY.
"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-285, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Extracellular phosphorylation converts pigment epithelium-derivedfactor from a neurotrophic to an antiangiogenic factor.";
Maik-Rachline G., Shaltiel S., Seger R.;
Blood 105:670-678(2005).
Cited for: PHOSPHORYLATION AT SER-24; SER-114 AND SER-227.

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