FGF2_HUMAN - dbPTM
FGF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FGF2_HUMAN
UniProt AC P09038
Protein Name Fibroblast growth factor 2
Gene Name FGF2
Organism Homo sapiens (Human).
Sequence Length 288
Subcellular Localization Secreted. Nucleus. Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism. Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane. Binding of exogenous FGF2 to FGFR facilitates endocytosis
Protein Description Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4. [PubMed: 8663044 Also acts as an integrin ligand which is required for FGF2 signaling]
Protein Sequence MVGVGGGDVEDVTPRPGGCQISGRGARGCNGIPGAAAWEAALPRRRPRRHPSVNPRSRAAGSPRTRGRRTEERPSGSRLGDRGRGRALPGGRLGGRGRGRAPERVGGRGRGRGTAAPRAAPAARGSRPGPAGTMAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS
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
13PhosphorylationGGDVEDVTPRPGGCQ
CCCHHHCCCCCCCCE		26.3824850871
62PhosphorylationPRSRAAGSPRTRGRR
HHHHHCCCCCCCCCC		13.3926853621
65PhosphorylationRAAGSPRTRGRRTEE
HHCCCCCCCCCCCCC		40.64-
73PhosphorylationRGRRTEERPSGSRLG
CCCCCCCCCCCCCCC		25.182541433
82DimethylationSGSRLGDRGRGRALP
CCCCCCCCCCCCCCC		34.60-
82MethylationSGSRLGDRGRGRALP
CCCCCCCCCCCCCCC		34.60-
84DimethylationSRLGDRGRGRALPGG
CCCCCCCCCCCCCCC		32.11-
84MethylationSRLGDRGRGRALPGG
CCCCCCCCCCCCCCC		32.11-
86MethylationLGDRGRGRALPGGRL
CCCCCCCCCCCCCCC		31.43-
86DimethylationLGDRGRGRALPGGRL
CCCCCCCCCCCCCCC		31.43-
96DimethylationPGGRLGGRGRGRAPE
CCCCCCCCCCCCCCC		29.82-
96MethylationPGGRLGGRGRGRAPE
CCCCCCCCCCCCCCC		29.82-
98DimethylationGRLGGRGRGRAPERV
CCCCCCCCCCCCCCC		30.02-
98MethylationGRLGGRGRGRAPERV
CCCCCCCCCCCCCCC		30.02-
108DimethylationAPERVGGRGRGRGTA
CCCCCCCCCCCCCCC		26.21-
108MethylationAPERVGGRGRGRGTA
CCCCCCCCCCCCCCC		26.21-
110DimethylationERVGGRGRGRGTAAP
CCCCCCCCCCCCCCC		30.21-
110MethylationERVGGRGRGRGTAAP
CCCCCCCCCCCCCCC		30.21-
112DimethylationVGGRGRGRGTAAPRA
CCCCCCCCCCCCCCC		37.62-
112MethylationVGGRGRGRGTAAPRA
CCCCCCCCCCCCCCC		37.62-
118MethylationGRGTAAPRAAPAARG
CCCCCCCCCCCCCCC		38.36-
121PhosphorylationTAAPRAAPAARGSRP
CCCCCCCCCCCCCCC		26.012541433
124MethylationPRAAPAARGSRPGPA
CCCCCCCCCCCCCCC		45.81-
138PhosphorylationAGTMAAGSITTLPAL
CCCCCCCEEEEECCC		16.43-
141PhosphorylationMAAGSITTLPALPED
CCCCEEEEECCCCCC		29.13-
168AcetylationDPKRLYCKNGGFFLR
CCCCEEECCCCEEEE		45.108958573
168MalonylationDPKRLYCKNGGFFLR
CCCCEEECCCCEEEE		45.1026320211
194MalonylationEKSDPHIKLQLQAEE
ECCCCCEEEEEEEHH		27.4426320211
206PhosphorylationAEERGVVSIKGVCAN
EHHHCCEEEEEEECC		19.042541433
208MalonylationERGVVSIKGVCANRY
HHCCEEEEEEECCCE		37.4732601280
215PhosphorylationKGVCANRYLAMKEDG
EEEECCCEEEECCCC		9.9128302677
219MalonylationANRYLAMKEDGRLLA
CCCEEEECCCCCEEE		47.2326320211
228SumoylationDGRLLASKCVTDECF
CCCEEEEEEECCCCE		27.4125114211
228UbiquitinationDGRLLASKCVTDECF
CCCEEEEEEECCCCE		27.4129967540
242PhosphorylationFFFERLESNNYNTYR
EEHHCHHHCCCCCCC		34.6629116813
245PhosphorylationERLESNNYNTYRSRK
HCHHHCCCCCCCCCC		17.0929116813
247PhosphorylationLESNNYNTYRSRKYT
HHHCCCCCCCCCCCC		15.2226657352
248PhosphorylationESNNYNTYRSRKYTS
HHCCCCCCCCCCCCE		11.7129116813
250PhosphorylationNNYNTYRSRKYTSWY
CCCCCCCCCCCCEEE		23.7810657989
253PhosphorylationNTYRSRKYTSWYVAL
CCCCCCCCCEEEEEE		12.6126657352
254PhosphorylationTYRSRKYTSWYVALK
CCCCCCCCEEEEEEH		18.8029116813
255PhosphorylationYRSRKYTSWYVALKR
CCCCCCCEEEEEEHH		17.2029116813
257PhosphorylationSRKYTSWYVALKRTG
CCCCCEEEEEEHHCC		3.9026657352
261AcetylationTSWYVALKRTGQYKL
CEEEEEEHHCCCCCC		37.878958573
267AcetylationLKRTGQYKLGSKTGP
EHHCCCCCCCCCCCC		38.1883623
267UbiquitinationLKRTGQYKLGSKTGP
EHHCCCCCCCCCCCC		38.1829967540
271AcetylationGQYKLGSKTGPGQKA
CCCCCCCCCCCCCEE		56.5683627
271UbiquitinationGQYKLGSKTGPGQKA
CCCCCCCCCCCCCEE		56.5629967540
277AcetylationSKTGPGQKAILFLPM
CCCCCCCEEEEEEEC		43.228958573
285PhosphorylationAILFLPMSAKS----
EEEEEECCCCC----		30.5229396449
288PhosphorylationFLPMSAKS-------
EEECCCCC-------		45.2122199227
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
73SPhosphorylationKinaseKPCAP17252
PhosphoELM
121TPhosphorylationKinasePKA_GROUP-PhosphoELM
206SPhosphorylationKinasePRKCAP04409
GPS
215YPhosphorylationKinaseTECP42680
Uniprot
254TPhosphorylationKinasePRKACAP36887
GPS
254TPhosphorylationKinasePKA-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FGF2_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 FGF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SDC1_HUMANSDC1physical
16982797
SDC2_HUMANSDC2physical
16982797
SDC4_HUMANSDC4physical
16982797
RS19_HUMANRPS19physical
11716516
TSP1_HUMANTHBS1physical
17996481
FGFR1_HUMANFGFR1physical
9174056
KAPCA_HUMANPRKACAphysical
26056081
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00686Pentosan Polysulfate
DB00877Sirolimus
DB00364Sucralfate
Regulatory Network of FGF2_HUMAN

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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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