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Protein Page:
PEDF (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PEDF a secreted neurotrophic protein that 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. The N-terminal (AA 44-121) exhibits neurite outgrowth-inducing activity. The C-terminal exposed loop (AA 382-418) is essential for serpin activity. Extracellular phosphorylation enhances antiangiogenic activity. Note: This description may include information from UniProtKB.
Protein type: Secreted; Secreted, signal peptide; Inhibitor protein
Cellular Component: extracellular matrix; extracellular space; extracellular region; melanosome
Molecular Function: serine-type endopeptidase inhibitor activity
Biological Process: cell proliferation; positive regulation of neurogenesis; negative regulation of angiogenesis; response to retinoic acid; short-term memory; negative regulation of inflammatory response; multicellular organismal development; response to glucocorticoid stimulus; regulation of proteolysis; kidney development; aging
Reference #:  P36955 (UniProtKB)
Alt. Names/Synonyms: Cell proliferation-inducing gene 35 protein; EPC-1; PEDF; PIG35; Pigment epithelium-derived factor; proliferation-inducing protein 35; serine (or cysteine) proteinase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 1; Serpin F1; serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 1; SERPINF1
Gene Symbols: SERPINF1
Molecular weight: 46,312 Da
Basal Isoelectric point: 5.97  Predict pI for various phosphorylation states
Select Structure to View Below

PEDF

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: S24‑p, S114‑p, S227‑p
carcinogenesis, altered: S24‑p, S114‑p, S227‑p
cell motility, altered: S24‑p, S114‑p, S227‑p
molecular association, regulation: S24‑p, S114‑p, S227‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
2 0 S24-p SSCQNPAsPPEEGSP
2 0 S114-p ALYYDLIsSPDIHGT
0 1 S152-p EKKLRIKssFVAPLE
0 1 S153-p KKLRIKssFVAPLEK
1 1 T226 TKFDSRKTsLEDFYL
3 1 S227-p KFDSRKTsLEDFYLD
0 1 T283-p FFLPLKVtQNLtLIE
0 1 T287-p LKVtQNLtLIEESLt
0 1 T294-p tLIEESLtsEFIHDI
0 1 S295-p LIEESLtsEFIHDID
0 2 K316-m1 QAVLTVPkLKLSYEG
  mouse

 
S24 GSSQNVPSSSEGSPV
T113 ALYYDLITNPDIHST
S151 ERKLRVKSSFVAPLE
S152 RKLRVKSSFVAPLEK
T225 TKFDSRKTTLQDFHL
T226 KFDSRKTTLQDFHLD
T282 FFLPLTVTQNLTMIE
T286 LTVTQNLTMIEESLT
T293 TMIEESLTSEFIHDI
S294 MIEESLTSEFIHDID
K315 QAVLTVPKLKLSFEG
  rat

 
D24 GSSQNVPDSSQDSPA
N114 ALYYDLINNPDIHST
S152 ERKLRVKSSFVAPLE
S153 RKLRVKSSFVAPLEK
T226-p TKFDSRKttLQDFHL
T227-p KFDSRKttLQDFHLD
T283 FFLPLTVTQNLTMIE
T287 LTVTQNLTMIEESLT
T294 TMIEESLTSEFVHDI
S295 MIEESLTSEFVHDID
K316 QAVLTVPKLKLSYEG
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