PIGT_HUMAN - dbPTM
PIGT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIGT_HUMAN
UniProt AC Q969N2
Protein Name GPI transamidase component PIG-T
Gene Name PIGT
Organism Homo sapiens (Human).
Sequence Length 578
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein .
Protein Description Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates..
Protein Sequence MAAAMPLALLVLLLLGPGGWCLAEPPRDSLREELVITPLPSGDVAATFQFRTRWDSELQREGVSHYRLFPKALGQLISKYSLRELHLSFTQGFWRTRYWGPPFLQAPSGAELWVWFQDTVTDVDKSWKELSNVLSGIFCASLNFIDSTNTVTPTASFKPLGLANDTDHYFLRYAVLPREVVCTENLTPWKKLLPCSSKAGLSVLLKADRLFHTSYHSQAVHIRPVCRNARCTSISWELRQTLSVVFDAFITGQGKKDWSLFRMFSRTLTEPCPLASESRVYVDITTYNQDNETLEVHPPPTTTYQDVILGTRKTYAIYDLLDTAMINNSRNLNIQLKWKRPPENEAPPVPFLHAQRYVSGYGLQKGELSTLLYNTHPYRAFPVLLLDTVPWYLRLYVHTLTITSKGKENKPSYIHYQPAQDRLQPHLLEMLIQLPANSVTKVSIQFERALLKWTEYTPDPNHGFYVSPSVLSALVPSMVAAKPVDWEESPLFNSLFPVSDGSNYFVRLYTEPLLVNLPTPDFSMPYNVICLTCTVVAVCYGSFYNLLTRTFHIEEPRTGGLAKRLANLIRRARGVPPL
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
78PhosphorylationKALGQLISKYSLREL
HHHHHHHHHHCCCHH		33.8524719451
81PhosphorylationGQLISKYSLRELHLS
HHHHHHHCCCHHHCC		25.3724719451
88UbiquitinationSLRELHLSFTQGFWR
CCCHHHCCCCCCCCC		18.5929967540
89UbiquitinationLRELHLSFTQGFWRT
CCHHHCCCCCCCCCC		8.1229967540
96UbiquitinationFTQGFWRTRYWGPPF
CCCCCCCCCCCCCCC		20.7829967540
103UbiquitinationTRYWGPPFLQAPSGA
CCCCCCCCCCCCCCC		9.9421890473
104UbiquitinationRYWGPPFLQAPSGAE
CCCCCCCCCCCCCCE		5.3821963094
134UbiquitinationWKELSNVLSGIFCAS
HHHHHHHHHHHHHHC		4.5529967540
135UbiquitinationKELSNVLSGIFCASL
HHHHHHHHHHHHHCC		26.0929967540
142UbiquitinationSGIFCASLNFIDSTN
HHHHHHCCCEECCCC		3.0129967540
150UbiquitinationNFIDSTNTVTPTASF
CEECCCCCCCCCCCC		26.3321963094
156PhosphorylationNTVTPTASFKPLGLA
CCCCCCCCCCCCCCC		35.9624719451
164N-linked_GlycosylationFKPLGLANDTDHYFL
CCCCCCCCCCCCEEE		58.7319159218
171 (in isoform 2)Ubiquitination-3.0121890473
190UbiquitinationTENLTPWKKLLPCSS
CCCCCCHHHHCCCCC		34.4429967540
191UbiquitinationENLTPWKKLLPCSSK
CCCCCHHHHCCCCCH		51.9229967540
198UbiquitinationKLLPCSSKAGLSVLL
HHCCCCCHHHHHHHH		30.1329967540
206UbiquitinationAGLSVLLKADRLFHT
HHHHHHHHHHHHCCC		44.0421963094
235PhosphorylationNARCTSISWELRQTL
CCCCCCCCCHHHHHH		17.7924719451
237UbiquitinationRCTSISWELRQTLSV
CCCCCCCHHHHHHHH		27.5529967540
241PhosphorylationISWELRQTLSVVFDA
CCCHHHHHHHHEEEE		17.9920068231
243PhosphorylationWELRQTLSVVFDAFI
CHHHHHHHHEEEEEH		21.4420068231
251PhosphorylationVVFDAFITGQGKKDW
HEEEEEHHCCCCCCC		19.5920068231
259PhosphorylationGQGKKDWSLFRMFSR
CCCCCCCHHHHHHHC		27.9720068231
263 (in isoform 4)Ubiquitination-2.5421890473
263UbiquitinationKDWSLFRMFSRTLTE
CCCHHHHHHHCCCCC		2.5421890473
283UbiquitinationSESRVYVDITTYNQD
CCCEEEEEEEEECCC		18.1529967540
291N-linked_GlycosylationITTYNQDNETLEVHP
EEEECCCCCEEEECC		34.09UniProtKB CARBOHYD
301O-linked_GlycosylationLEVHPPPTTTYQDVI
EEECCCCCCCCCCEE		37.23OGP
308UbiquitinationTTTYQDVILGTRKTY
CCCCCCEECCCCCEE		3.8529967540
309UbiquitinationTTYQDVILGTRKTYA
CCCCCEECCCCCEEH		6.0321890473
309UbiquitinationTTYQDVILGTRKTYA
CCCCCEECCCCCEEH		6.0321890473
327N-linked_GlycosylationLLDTAMINNSRNLNI
HHHHHHHCCCCCEEE		27.60UniProtKB CARBOHYD
339UbiquitinationLNIQLKWKRPPENEA
EEEEEEECCCCCCCC		54.1429967540
354UbiquitinationPPVPFLHAQRYVSGY
CCCCEEEEEEECCCC		9.5529967540
365UbiquitinationVSGYGLQKGELSTLL
CCCCCCCCCCCCHHE		60.4423000965
365 (in isoform 1)Ubiquitination-60.4421890473
405UbiquitinationHTLTITSKGKENKPS
EEEEEEECCCCCCCC		66.41-
410UbiquitinationTSKGKENKPSYIHYQ
EECCCCCCCCEECCC		36.1129967540
509PhosphorylationSNYFVRLYTEPLLVN
CCEEEEEECCCEEEC		9.86-
510PhosphorylationNYFVRLYTEPLLVNL
CEEEEEECCCEEECC		35.40-
563UbiquitinationPRTGGLAKRLANLIR
CCCCCHHHHHHHHHH		53.65-
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 PIGT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIGT_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 PIGT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GPAA1_HUMANGPAA1physical
11483512
PIGU_HUMANPIGUphysical
22939629
ERLEC_HUMANERLEC1physical
26344197
UBP54_HUMANUSP54physical
28514442
TNIP1_HUMANTNIP1physical
28514442
CE85L_HUMANCEP85Lphysical
28514442
HXC9_HUMANHOXC9physical
28514442
RMD5B_HUMANRMND5Bphysical
28514442
ZMY19_HUMANZMYND19physical
28514442
ARMC8_HUMANARMC8physical
28514442
PIGS_HUMANPIGSphysical
28514442
MKLN1_HUMANMKLN1physical
28514442
RMD5A_HUMANRMND5Aphysical
28514442
GID8_HUMANGID8physical
28514442
MAEA_HUMANMAEAphysical
28514442
RBP10_HUMANRANBP10physical
28514442
GID4_HUMANGID4physical
28514442
ZN609_HUMANZNF609physical
28514442
EGFL7_HUMANEGFL7physical
28514442
RANB9_HUMANRANBP9physical
28514442
N42L2_HUMANN4BP2L2physical
28514442
WDR26_HUMANWDR26physical
28514442
ANR40_HUMANANKRD40physical
28514442
BORA_HUMANBORAphysical
28514442
PIGU_HUMANPIGUphysical
28514442
STOM_HUMANSTOMphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615398Multiple congenital anomalies-hypotonia-seizures syndrome 3 (MCAHS3)
615399Paroxysmal nocturnal hemoglobinuria 2 (PNH2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIGT_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-164, AND MASSSPECTROMETRY.

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