Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Fibroblast growth factor 2  

UniProtKB / Swiss-Prot ID :  FGF2_HUMAN

Gene Name (Synonyms) : 
FGF2, FGFB  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. Note=Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism. Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane. 

Protein Function :  Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. 

Protein Sequence MVGVGGGDVEDVTPRPGGCQISGRGARGCNGIPGAAAWEAALPRRRPRRHPSVNPRSRAAGSPRTRGRRT...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEEEEECCCEEEEECCCCCEEEEECCCCCEEEEEEEECCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
825-methylarginineRLGDRGRGR
CCCEEEEEC
34.60HPRD
Link
82N2,N2-dimethylarginineRLGDRGRGR
CCCEEEEEC
34.60Phosphositeplus
Link
845-methylarginineGDRGRGRAL
CEEEEECCC
32.11HPRD
Link
84N2,N2-dimethylarginineGDRGRGRAL
CEEEEECCC
32.11Phosphositeplus
Link
865-methylarginineRGRGRALPG
EEEECCCCC
31.43HPRD
Link
86N2,N2-dimethylarginineRGRGRALPG
EEEECCCCC
31.43Phosphositeplus
Link
965-methylarginineRLGGRGRGR
EECCCCCCC
29.82HPRD
Link
96N2,N2-dimethylarginineRLGGRGRGR
EECCCCCCC
29.82Phosphositeplus
Link
985-methylarginineGGRGRGRAP
CCCCCCCCE
30.02HPRD
Link
98N2,N2-dimethylarginineGGRGRGRAP
CCCCCCCCE
30.02Phosphositeplus
Link
1085-methylarginineRVGGRGRGR
EEEEECCCC
26.21HPRD
Link
108N2,N2-dimethylarginineRVGGRGRGR
EEEEECCCC
26.21Phosphositeplus
Link
1105-methylarginineGGRGRGRGT
EEECCCCHH
30.21HPRD
Link
110N2,N2-dimethylarginineGGRGRGRGT
EEECCCCHH
30.21Phosphositeplus
Link
1125-methylarginineRGRGRGTAA
ECCCCHHHH
37.62HPRD
Link
112N2,N2-dimethylarginineRGRGRGTAA
ECCCCHHHH
37.62Phosphositeplus
Link
168N6-acetyllysineRLYCKNGGF
45.10Phosphositeplus
Link-
206PhosphoserineRGVVSIKGV
19.04Phosphositeplus
Link-
206Phosphoserine (PKC_alpha)RGVVSIKGV
19.04PhosphoELM
Link-
215Phosphotyrosine; by TEC.CANRYLAMK
9.91UniProtKB
Link-
250PhosphoserineNTYRSRKYT
23.78Phosphositeplus
Link-
254PhosphothreonineSRKYTSWYV
18.80Phosphositeplus
Link-
254Phosphothreonine (PKA_group)SRKYTSWYV
18.80PhosphoELM
Link-
261N6-acetyllysineYVALKRTGQ
37.87Phosphositeplus
Link-
267N6-acetyllysineTGQYKLGSK
38.18Phosphositeplus
Link-
271N6-acetyllysineKLGSKTGPG
56.56Phosphositeplus
Link-
277N6-acetyllysineGPGQKAILF
43.22Phosphositeplus
Link-
285PhosphoserineFLPMSAKS
30.52Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
FGFR2_HUMANphysical interaction
physical interaction
DIP:6035EDIP11121055
10950949
FGFR1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
DIP:6046EDIP10574979
10950949
7730326
1722683
FGFR4_HUMANphysical interactionDIP:8297EDIP7680645
FGFR1_HUMANdirect interaction
direct interaction
EBI-1028412
EBI-1030022
intact10490103
11030354
CD44_HUMANin vivoHPRD:00622HPRD7532176
CSK22_HUMANin vitro
in vivo
HPRD:00622HPRD7735329
CSK21_HUMANin vitroHPRD:00622HPRD12145206
SDC3_HUMANin vitroHPRD:00622HPRD16982797
8344959
NRP1_HUMANin vitroHPRD:00622HPRD15695515
FGF2_HUMANin vitroHPRD:00622HPRD9558385
FGFR3_HUMANin vivoHPRD:00622HPRD10574949
KS6A3_HUMANin vitroHPRD:00622HPRD15879597
SDC2_HUMANin vitroHPRD:00622HPRD16982797
SDC1_HUMANin vitroHPRD:00622HPRD16982797
FGF4_HUMANENSP00000264498STRING
FGF20_HUMANENSP00000264498STRING
GSLG1_HUMANENSP00000264498STRING
FGF22_HUMANENSP00000264498STRING
ONCM_HUMANENSP00000264498STRING
MMP2_HUMANENSP00000264498STRING
TGFB1_HUMANENSP00000264498STRING
SCF_HUMANENSP00000264498STRING
FGF6_HUMANENSP00000264498STRING
FGF23_HUMANENSP00000264498STRING
EGR1_HUMANENSP00000264498STRING
CXCR4_HUMANENSP00000264498STRING
INS_HUMANENSP00000264498STRING
INS_HUMANENSP00000264498STRING
SDC1_HUMANENSP00000264498STRING
IL6_HUMANENSP00000264498STRING
TSP1_HUMANENSP00000264498STRING
VWF_HUMANENSP00000264498STRING
IL1A_HUMANENSP00000264498STRING
VGFR2_HUMANENSP00000264498STRING
FGF10_HUMANENSP00000264498STRING
INHBE_HUMANENSP00000264498STRING
FGF18_HUMANENSP00000264498STRING
CD44_HUMANENSP00000264498STRING
FGFR4_HUMANENSP00000264498STRING
FGF19_HUMANENSP00000264498STRING
TGFA_HUMANENSP00000264498STRING
FOS_HUMANENSP00000264498STRING
FGF5_HUMANENSP00000264498STRING
VEGFA_HUMANENSP00000264498STRING
BDNF_HUMANENSP00000264498STRING
FGF3_HUMANENSP00000264498STRING
ANGI_HUMANENSP00000264498STRING
FGF1_HUMANENSP00000264498STRING
FGFR2_HUMANENSP00000264498STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00686Pentosan Polysulfate
DB00877Sirolimus
DB00364Sucralfate
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 isessential for unconventional secretion.";
Ebert A.D., Laussmann M., Wegehingel S., Kaderali L., Erfle H.,Reichert J., Lechner J., Beer H.D., Pepperkok R., Nickel W.;
Traffic 11:813-826(2010).
Cited for: PHOSPHORYLATION AT TYR-215, INTERACTION WITH TEC, AND SUBCELLULARLOCATION.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures