FIG2_YEAST - dbPTM
FIG2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FIG2_YEAST
UniProt AC P25653
Protein Name Factor-induced gene 2 protein
Gene Name FIG2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1609
Subcellular Localization Secreted, cell wall . Membrane
Lipid-anchor, GPI-anchor . Periphery of the mating cells. Localized to the mating projection.
Protein Description Required for efficient mating. Plays a role in maintenance of cell wall integrity during mating. Important for mating cell projection shape and conjugation bridge diameter. Plays a role in cell fusion and nuclear migration..
Protein Sequence MNSFASLGLIYSVVNLLTRVEAQIVFYQNSSTSLPVPTLVSTSIADFHESSSTGEVQYSSSYSYVQPSIDSFTSSSFLTSFEAPTETSSSYAVSSSLITSDTFSSYSDIFDEETSSLISTSAASSEKASSTLSSTAQPHRTSHSSSSFELPVTAPSSSSLPSSTSLTFTSVNPSQSWTSFNSEKSSALSSTIDFTSSEISGSTSPKSLESFDTTGTITSSYSPSPSSKNSNQTSLLSPLEPLSSSSGDLILSSTIQATTNDQTSKTIPTLVDATSSLPPTLRSSSMAPTSGSDSISHNFTSPPSKTSGNYDVLTSNSIDPSLFTTTSEYSSTQLSSLNRASKSETVNFTASIASTPFGTDSATSLIDPISSVGSTASSFVGISTANFSTQGNSNYVPESTASGSSQYQDWSSSSLPLSQTTWVVINTTNTQGSVTSTTSPAYVSTATKTVDGVITEYVTWCPLTQTKSQAIGVSSSISSVPQASSFSGSSILSSNSSTLAASNNVPESTASGSSQYQDWSSSSLPLSQTTWVVINTTNTQGSVTSTTSPAYVSTATKTVDGVITEYVTWCPLTQTKSQAIGISSSTISATQTSKPSSILTLGISTLQLSDATFKGTETINTHLMTESTSITEPTYFSGTSDSFYLCTSEVNLASSLSSYPNFSSSEGSTATITNSTVTFGSTSKYPSTSVSNPTEASQHVSSSVNSLTDFTSNSTETIAVISNIHKTSSNKDYSLTTTQLKTSGMQTLVLSTVTTTVNGAATEYTTWCPASSIAYTTSISYKTLVLTTEVCSHSECTPTVITSVTATSSTIPLLSTSSSTVLSSTVSEGAKNPAASEVTINTQVSATSEATSTSTQVSATSATATASESSTTSQVSTASETISTLGTQNFTTTGSLLFPALSTEMINTTVVSRKTLIISTEVCSHSKCVPTVITEVVTSKGTPSNGHSSQTLQTEAVEVTLSSHQTVTMSTEVCSNSICTPTVITSVQMRSTPFPYLTSSTSSSSLASTKKSSLEASSEMSTFSVSTQSLPLAFTSSEKRSTTSVSQWSNTVLTNTIMSSSSNVISTNEKPSSTTSPYNFSSGYSLPSSSTPSQYSLSTATTTINGIKTVYTTWCPLAEKSTVAASSQSSRSVDRFVSSSKPSSSLSQTSIQYTLSTATTTISGLKTVYTTWCPLTSKSTLGATTQTSSTAKVRITSASSATSTSISLSTSTESESSSGYLSKGVCSGTECTQDVPTQSSSPASTLAYSPSVSTSSSSSFSTTTASTLTSTHTSVPLLPSSSSISASSPSSTSLLSTSLPSPAFTSSTLPTATAVSSSTFIASSLPLSSKSSLSLSPVSSSILMSQFSSSSSSSSSLASLPSLSISPTVDTVSVLQPTTSIATLTCTDSQCQQEVSTICNGSNCDDVTSTATTPPSTVTDTMTCTGSECQKTTSSSCDGYSCKVSETYKSSATISACSGEGCQASATSELNSQYVTMTSVITPSAITTTSVEVHSTESTISITTVKPVTYTSSDTNGELITITSSSQTVIPSVTTIITRTKVAITSAPKPTTTTYVEQRLSSSGIATSFVAAASSTWITTPIVSTYAGSASKFLCSKFFMIMVMVINFI
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
29N-linked_GlycosylationAQIVFYQNSSTSLPV
EEEEEEECCCCCCCC		26.92-
231N-linked_GlycosylationSPSSKNSNQTSLLSP
CCCCCCCCCCCCCCC		59.55-
298N-linked_GlycosylationGSDSISHNFTSPPSK
CCCCCCCCCCCCCCC		34.79-
347N-linked_GlycosylationASKSETVNFTASIAS
CCCCCCEEEEEEEEC		35.65-
386N-linked_GlycosylationFVGISTANFSTQGNS
CCCEEEEEEECCCCC		31.33-
426N-linked_GlycosylationQTTWVVINTTNTQGS
CCEEEEEECCCCCCC		29.28-
495N-linked_GlycosylationGSSILSSNSSTLAAS
CCCCCCCCCCCCEEC		36.28-
535N-linked_GlycosylationQTTWVVINTTNTQGS
CCEEEEEECCCCCCC		29.28-
596PhosphorylationATQTSKPSSILTLGI
CCCCCCCCCEEEEEE		33.4723607784
597PhosphorylationTQTSKPSSILTLGIS
CCCCCCCCEEEEEEE		30.0923607784
600PhosphorylationSKPSSILTLGISTLQ
CCCCCEEEEEEEEEE		22.6723607784
604PhosphorylationSILTLGISTLQLSDA
CEEEEEEEEEEECCC		22.6723607784
605PhosphorylationILTLGISTLQLSDAT
EEEEEEEEEEECCCE		19.3223607784
609PhosphorylationGISTLQLSDATFKGT
EEEEEEECCCEECCC		16.5523607784
612PhosphorylationTLQLSDATFKGTETI
EEEECCCEECCCCEE		30.7623607784
661N-linked_GlycosylationSSLSSYPNFSSSEGS
HHHHCCCCCCCCCCC		40.99-
674N-linked_GlycosylationGSTATITNSTVTFGS
CCCEEEECCEEEECC		31.65-
713N-linked_GlycosylationSLTDFTSNSTETIAV
HHHCCCCCCCCEEEE		50.31-
889N-linked_GlycosylationISTLGTQNFTTTGSL
HHCCCCCCCCCCCCE		35.75-
907N-linked_GlycosylationALSTEMINTTVVSRK
HHCCCCCCEEEECCC		28.52-
1079N-linked_GlycosylationSSTTSPYNFSSGYSL
CCCCCCCCCCCCCCC		33.44-
1187PhosphorylationTLGATTQTSSTAKVR
CCCCEECCCCCEEEE		23.6627017623
1188PhosphorylationLGATTQTSSTAKVRI
CCCEECCCCCEEEEE		18.8427017623
1190PhosphorylationATTQTSSTAKVRITS
CEECCCCCEEEEEEE		30.2027017623
1400N-linked_GlycosylationQEVSTICNGSNCDDV
HHHHHHCCCCCCCCC		53.75-
1588GPI-anchorPIVSTYAGSASKFLC
CCCCCCCCCHHHHHH		17.21-
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 FIG2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FIG2_YEAST !!
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 FIG2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FIG4_YEASTFIG4genetic
9456310
SAG1_YEASTSAG1genetic
19299340
AGA2_YEASTAGA2genetic
19299340
AGA1_YEASTAGA1genetic
19299340
AGA1_YEASTAGA1physical
19299340
PLMT_YEASTOPI3genetic
23891562
GET2_YEASTGET2genetic
23891562
INO4_YEASTINO4genetic
27708008
MTU1_YEASTSLM3genetic
27708008
MED5_YEASTNUT1genetic
27708008
MUP1_YEASTMUP1genetic
27708008
TBP7_YEASTYTA7genetic
27708008
KAPC_YEASTTPK3genetic
27708008
VRP1_YEASTVRP1genetic
27708008
ZRC1_YEASTZRC1genetic
27708008
NST1_YEASTNST1genetic
27708008
MDM12_YEASTMDM12genetic
27708008
MED1_YEASTMED1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FIG2_YEAST

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Related Literatures of Post-Translational Modification

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