PFL2_SCHPO - dbPTM
PFL2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PFL2_SCHPO
UniProt AC Q8TFG9
Protein Name Putative GPI-anchored protein pfl2 {ECO:0000305}
Gene Name pfl2 {ECO:0000303|PubMed:23236291}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1036
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor .
Protein Description May be involved in agglutination during conjugation or other aspects of colony formation (By similarity). Induces flocculation when overexpressed. [PubMed: 23236291]
Protein Sequence MKFFTASTLFLLAAQSLNSGVSASLSDPANTPTILADDIVHGYTPATYLSSVPTLLKRATTSYNYNTSSASSSSLTSSSAASSSLTSSSSLASSSTNSTTSASPTSSSLTSSSATSSSLASSSTTSSSLASSSITSSSLASSSITSSSLASSSTTSSSLASSSTNSTTSATPTSSATSSSLSSTAASNSATSSSLASSSLNSTTSATATSSSLSSTAASNSATSSSLASSSLNSTTSATATSSSISSTVSSSTPLTSSNSTTAATSASATSSSAQYNTSSLLPSSTPSSTPLSSANSTTATSASSTPLTSVNSTTTTSASSTPLSSVSSANSTTATSTSSTPLSSVNSTTATSASSTPLTSVNSTTATSASSTPLTSVNSTSATSASSTPLTSANSTTSTSVSSTAPSYNTSSVLPTSSVSSTPLSSANSTTATSASSTPLSSVNSTTATSASSTPLSSVNSTTATSASSTPLTSVNSTTATSASSTPLTSVNSTSATSASSTPLTSANSTTSTSVSSTAPSYNTSSVLPTSSVSSTPLSSANSTTATSASSTPLTSVNSTTATSASSTPFGNSTITSSASGSTGEFTNTNSGNGDVSGSVTTPTSTPLSNSTVAPTSTFTSSGFNTTSGLPTSSASTPLSNSTVAPTSTFTSSGFNTTSGLPTSSASTPSSNSSIVPTSTFTSSGFNTTSGLPTSSASTPLSNSTVAPTSTFTSSGFNTTSGLPTSSVSTPLSNSSAYPSSGSSTFSRLSSTLTSSIIPTETFGSTSGSATGTRPTGSSSQGSVVPTTSTGSSVTSTGTGTTTGVTEVTETSTFETTEIITSTIEPTTASGTGGGNPTAAPTNEPTVTTGTETTEGTATYTEPTTFTSTFSFTTTIIGGTTTIIPVNPGNPSSSVSAPPTTSFTPGPGGSGYPSYSNTTQGMNTTSIWNSSNSTIVSNVTATITGNVTITTGDLTTIDPTTFTSTYLSSGFQTVSNTTATSGSDDDVKTASTSSSTSYTSSSSSSSSTTSAASSKASVSMGLNGLMIAAVILLVA
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
66N-linked_GlycosylationATTSYNYNTSSASSS
HCCCCCCCCCCCCCC
-
97N-linked_GlycosylationSLASSSTNSTTSASP
HHCCCCCCCCCCCCC
-
165N-linked_GlycosylationSLASSSTNSTTSATP
HHCCCCCCCCCCCCC
-
201N-linked_GlycosylationSLASSSLNSTTSATA
HHHHHHCCCCCCCEE
-
233N-linked_GlycosylationSLASSSLNSTTSATA
HHCHHHCCCCCCCEE
-
259N-linked_GlycosylationSTPLTSSNSTTAATS
CCCCCCCCCCCCCCC
-
277N-linked_GlycosylationTSSSAQYNTSSLLPS
CCCCCCCCCCCCCCC
-
296N-linked_GlycosylationSTPLSSANSTTATSA
CCCCCCCCCCCCCCC
-
312N-linked_GlycosylationSTPLTSVNSTTTTSA
CCCCEEECCCCCCCC
-
331N-linked_GlycosylationLSSVSSANSTTATST
CCCCCCCCCCCCCCC
-
347N-linked_GlycosylationSTPLSSVNSTTATSA
CCCCCCCCCCCCCCC
-
363N-linked_GlycosylationSTPLTSVNSTTATSA
CCCCEEECCCCCCCC
-
379N-linked_GlycosylationSTPLTSVNSTSATSA
CCCCEEECCCCCCCC
-
395N-linked_GlycosylationSTPLTSANSTTSTSV
CCCCCCCCCCCCCEE
-
410N-linked_GlycosylationSSTAPSYNTSSVLPT
CCCCCCCCCCCCCCC
-
429N-linked_GlycosylationSTPLSSANSTTATSA
CCCCCCCCCCCCCCC
-
445N-linked_GlycosylationSTPLSSVNSTTATSA
CCCCCCCCCCCCCCC
-
461N-linked_GlycosylationSTPLSSVNSTTATSA
CCCCCCCCCCCCCCC
-
477N-linked_GlycosylationSTPLTSVNSTTATSA
CCCCEEECCCCCCCC
-
493N-linked_GlycosylationSTPLTSVNSTSATSA
CCCCEEECCCCCCCC
-
509N-linked_GlycosylationSTPLTSANSTTSTSV
CCCCCCCCCCCCCEE
-
524N-linked_GlycosylationSSTAPSYNTSSVLPT
CCCCCCCCCCCCCCC
-
543N-linked_GlycosylationSTPLSSANSTTATSA
CCCCCCCCCCCCCCC
-
559N-linked_GlycosylationSTPLTSVNSTTATSA
CCCCEEECCCCCCCC
-
573N-linked_GlycosylationASSTPFGNSTITSSA
CCCCCCCCCEEEECC
-
611N-linked_GlycosylationPTSTPLSNSTVAPTS
CCCCCCCCCCCCCCC
-
626N-linked_GlycosylationTFTSSGFNTTSGLPT
EECCCCCCCCCCCCC
-
642N-linked_GlycosylationSASTPLSNSTVAPTS
CCCCCCCCCCCCCCC
-
657N-linked_GlycosylationTFTSSGFNTTSGLPT
EECCCCCCCCCCCCC
-
673N-linked_GlycosylationSASTPSSNSSIVPTS
CCCCCCCCCCCCCCC
-
688N-linked_GlycosylationTFTSSGFNTTSGLPT
EECCCCCCCCCCCCC
-
704N-linked_GlycosylationSASTPLSNSTVAPTS
CCCCCCCCCCCCCCC
-
719N-linked_GlycosylationTFTSSGFNTTSGLPT
EECCCCCCCCCCCCC
-
735N-linked_GlycosylationSVSTPLSNSSAYPSS
CCCCCCCCCCCCCCC
-
918N-linked_GlycosylationSGYPSYSNTTQGMNT
CCCCCCCCCCCCCCC
-
924N-linked_GlycosylationSNTTQGMNTTSIWNS
CCCCCCCCCCEEEEC
-
930N-linked_GlycosylationMNTTSIWNSSNSTIV
CCCCEEEECCCCEEE
-
933N-linked_GlycosylationTSIWNSSNSTIVSNV
CEEEECCCCEEEECE
-
939N-linked_GlycosylationSNSTIVSNVTATITG
CCCEEEECEEEEEEC
-
947N-linked_GlycosylationVTATITGNVTITTGD
EEEEEECCEEEECCC
-
977N-linked_GlycosylationSGFQTVSNTTATSGS
CCEEEEECCCCCCCC
-
1011GPI-anchorSSSSSTTSAASSKAS
CCCCCCCCCCCCCCH
-

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 PFL2_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PFL2_SCHPO !!

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 PFL2_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PFL2_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PFL2_SCHPO

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Related Literatures of Post-Translational Modification

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