PIGN_HUMAN - dbPTM
PIGN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIGN_HUMAN
UniProt AC O95427
Protein Name GPI ethanolamine phosphate transferase 1
Gene Name PIGN
Organism Homo sapiens (Human).
Sequence Length 931
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor (By similarity). May act as suppressor of replication stress and chromosome missegregation..
Protein Sequence MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALYELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQFDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESMFTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSLCKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKPSHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYPLSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSLLLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLSTVLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMSTYLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLYLDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFVLVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTSISHYVIVMSMTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM
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
82PhosphorylationNIIMHEGSWGISHTR
HHHHCCCCCCCCCCC
21.1030177828
86PhosphorylationHEGSWGISHTRVPTE
CCCCCCCCCCCCCCC
18.1830177828
117UbiquitinationSAVAKGWKENPVEFD
HHHHCCCCCCCCCHH
57.17-
128N-linked_GlycosylationVEFDSLFNESKYTWS
CCHHHHCCCCCCCCC
58.90UniProtKB CARBOHYD
162UbiquitinationYTYSYDAKREDFGAQ
EEEEEECCCHHCCCC
54.12-
173UbiquitinationFGAQDATKLDTWVFD
CCCCCCHHCCCCCCC
46.19-
192N-linked_GlycosylationFFHHARNNQSLFSKI
HHHHHHCCCHHHHHC
27.54UniProtKB CARBOHYD
197PhosphorylationRNNQSLFSKINEEKI
HCCCHHHHHCCHHHH
37.6124719451
223PhosphorylationNGHAHRPSSRDYKHN
CCCCCCCCCHHHCCC
37.6522461510
224PhosphorylationGHAHRPSSRDYKHNI
CCCCCCCCHHHCCCC
31.6722461510
227PhosphorylationHRPSSRDYKHNIKKV
CCCCCHHHCCCCCCC
17.0322461510
307UbiquitinationQFDDAFLKEWRLENW
HCCHHHHHHHHHHCC
49.10-
350N-linked_GlycosylationILPVDYLNNTDLFKA
EEECCCCCCCCCCCC
43.03UniProtKB CARBOHYD
379UbiquitinationKVKMTQKKEVTLPFL
CCCCCCCCEEECCCC
47.82-
391UbiquitinationPFLFTPFKLLSDSKQ
CCCCCCHHHCCCCHH
50.12-
397UbiquitinationFKLLSDSKQFNILRK
HHHCCCCHHHHHHHH
64.99-
404MethylationKQFNILRKARSYIKH
HHHHHHHHHHHHHHC
44.71-
404TrimethylationKQFNILRKARSYIKH
HHHHHHHHHHHHHHC
44.71-
419PhosphorylationRKFDEVVSLCKELIH
CCHHHHHHHHHHHHH
32.9725690035
471UbiquitinationKSHSNLIKGVSKEVK
HHCCHHHHCCCCCCC
57.32-
591PhosphorylationLWTRAKMTSLSWTFF
HHHHHHHHHHHHHHH
26.3022210691
592PhosphorylationWTRAKMTSLSWTFFS
HHHHHHHHHHHHHHH
19.5322210691
596PhosphorylationKMTSLSWTFFSLLLA
HHHHHHHHHHHHHHH
16.0722210691
618PhosphorylationVGRKPDISLVMGAGL
CCCCCCHHHHHHHHH
23.4522210691
636PhosphorylationLLSLCVVTSLMKRKD
HHHHHHHHHHHHCCC
8.8522210691
637PhosphorylationLSLCVVTSLMKRKDS
HHHHHHHHHHHCCCC
18.1722210691
644PhosphorylationSLMKRKDSFIKEELL
HHHHCCCCCCCHHHH
31.7224719451
673PhosphorylationVVYSTQSSLLRKQGL
HHHHCHHHHHHHCCC
22.9324719451
823PhosphorylationYCFLTVFSPFMMGAL
HHHHHHHCHHHHHHH
16.9426074081
927UbiquitinationLRLCGKPKSHFM---
HHHCCCCHHHCC---
61.11-

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 PIGN_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIGN_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 PIGN_HUMAN !!

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

Oops, there are no PPI records of PIGN_HUMAN !!

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

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Related Literatures of Post-Translational Modification

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