PGAP1_HUMAN - dbPTM
PGAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGAP1_HUMAN
UniProt AC Q75T13
Protein Name GPI inositol-deacylase
Gene Name PGAP1
Organism Homo sapiens (Human).
Sequence Length 922
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Involved in inositol deacylation of GPI-anchored proteins. GPI inositol deacylation may important for efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi (By similarity)..
Protein Sequence MFLHSVNLWNLAFYVFMVFLATLGLWDVFFGFEENKCSMSYMFEYPEYQKIELPKKLAKRYPAYELYLYGEGSYAEEHKILPLTGIPVLFLPGNAGSYKQVRSIGSIALRKAEDIDFKYHFDFFSVNFNEELVALYGGSLQKQTKFVHECIKTILKLYKGQEFAPKSVAIIGHSMGGLVARALLTLKNFKHDLINLLITQATPHVAPVMPLDRFITDFYTTVNNYWILNARHINLTTLSVAGGFRDYQVRSGLTFLPKLSHHTSALSVVSSAVPKTWVSTDHLSIVWCKQLQLTTVRAFFDLIDADTKQITQNSKKKLSVLYHHFIRHPSKHFEENPAIISDLTGTSMWVLVKVSKWTYVAYNESEKIYFTFPLENHRKIYTHVYCQSTMLDTNSWIFACINSTSMCLQGVDLSWKAELLPTIKYLTLRLQDYPSLSHLVVYVPSVRGSKFVVDCEFFKKEKRYIQLPVTHLFSFGLSSRKVVLNTNGLYYNLELLNFGQIYQAFKINVVSKCSAVKEEITSIYRLHIPWSYEDSLTIAQAPSSTEISLKLHIAQPENNTHVALFKMYTSSDCRYEVTVKTSFSQILGQVVRFHGGALPAYVVSNILLAYRGQLYSLFSTGCCLEYATMLDKEAKPYKVDPFVIIIKFLLGYKWFKELWDVLLLPELDAVILTCQSMCFPLISLILFLFGTCTAYWSGLLSSASVRLLSSLWLALKRPSELPKDIKMISPDLPFLTIVLIIVSWTTCGALAILLSYLYYVFKVVHLQASLTTFKNSQPVNPKHSRRSEKKSNHHKDSSIHHLRLSANDAEDSLRMHSTVINLLTWIVLLSMPSLIYWLKNLRYYFKLNPDPCKPLAFILIPTMAILGNTYTVSIKSSKLLKTTSQFPLPLAVGVIAFGSAHLYRLPCFVFIPLLLHALCNFM
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
144PhosphorylationGGSLQKQTKFVHECI
CCCHHHHHHHHHHHH
33.22-
159UbiquitinationKTILKLYKGQEFAPK
HHHHHHHCCCCCCCC
65.6332142685
187UbiquitinationARALLTLKNFKHDLI
HHHHHHHCCCCHHHH
55.92-
308UbiquitinationDLIDADTKQITQNSK
HHHCCCCHHHHHCHH
40.00-
402N-linked_GlycosylationSWIFACINSTSMCLQ
CEEEEHHCCCCCCCC
38.84UniProtKB CARBOHYD
558N-linked_GlycosylationLHIAQPENNTHVALF
EEEECCCCCCEEEEE
66.44UniProtKB CARBOHYD
601PhosphorylationHGGALPAYVVSNILL
CCCCCCHHHHHHHHH
10.23-
610PhosphorylationVSNILLAYRGQLYSL
HHHHHHHHHHHHHHH
18.42-
637PhosphorylationLDKEAKPYKVDPFVI
HCCCCCCCCCCCHHH
23.96-
782UbiquitinationNSQPVNPKHSRRSEK
CCCCCCCCCCCCCCC
49.3529967540
797PhosphorylationKSNHHKDSSIHHLRL
CCCCCCCCCCEEEEC
35.6823312004
798PhosphorylationSNHHKDSSIHHLRLS
CCCCCCCCCEEEECC
35.7523312004
805PhosphorylationSIHHLRLSANDAEDS
CCEEEECCCCCHHHH
20.7025278378
812PhosphorylationSANDAEDSLRMHSTV
CCCCHHHHHHHHHHH
14.9125278378
830PhosphorylationLTWIVLLSMPSLIYW
HHHHHHHHHHHHHHH
25.20-
882PhosphorylationKSSKLLKTTSQFPLP
ECCCCCCCCCCCCCC
31.48-
883PhosphorylationSSKLLKTTSQFPLPL
CCCCCCCCCCCCCCC
20.95-
884PhosphorylationSKLLKTTSQFPLPLA
CCCCCCCCCCCCCCE
34.75-

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 PGAP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGAP1_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 PGAP1_HUMAN !!

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

Oops, there are no PPI records of PGAP1_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGAP1_HUMAN

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Related Literatures of Post-Translational Modification

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