GILT_HUMAN - dbPTM
GILT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GILT_HUMAN
UniProt AC P13284
Protein Name Gamma-interferon-inducible lysosomal thiol reductase
Gene Name IFI30
Organism Homo sapiens (Human).
Sequence Length 250
Subcellular Localization Secreted . Lysosome .
Protein Description Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II-restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds (By similarity). Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation (By similarity)..
Protein Sequence MTLSPLLLFLPPLLLLLDVPTAAVQASPLQALDFFGNGPPVNYKTGNLYLRGPLKKSNAPLVNVTLYYEALCGGCRAFLIRELFPTWLLVMEILNVTLVPYGNAQEQNVSGRWEFKCQHGEEECKFNKVEACVLDELDMELAFLTIVCMEEFEDMERSLPLCLQLYAPGLSPDTIMECAMGDRGMQLMHANAQRTDALQPPHEYVPWVTVNGKPLEDQTQLLTLVCQLYQGKKPDVCPSSTSSLRSVCFK
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
45PhosphorylationGPPVNYKTGNLYLRG
CCCCCCCCCCEEEEC
22.4218187866
63N-linked_GlycosylationKSNAPLVNVTLYYEA
CCCCCCEEEEHHHHH
28.83UniProtKB CARBOHYD
95N-linked_GlycosylationLLVMEILNVTLVPYG
HHHHHHHCCEEEECC
30.32UniProtKB CARBOHYD
108N-linked_GlycosylationYGNAQEQNVSGRWEF
CCCCCCCCCCCCEEE
29.21UniProtKB CARBOHYD
116AcetylationVSGRWEFKCQHGEEE
CCCCEEEEECCCCCC
22.8227178108

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 GILT_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GILT_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 GILT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR412_HUMANKRTAP4-12physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
ZO1_HUMANTJP1physical
26186194
F120A_HUMANFAM120Aphysical
26186194
L2GL2_HUMANLLGL2physical
26186194
DAPK1_HUMANDAPK1physical
26186194
TTC31_HUMANTTC31physical
26186194
MKLN1_HUMANMKLN1physical
26186194
ELP3_HUMANELP3physical
26186194
DEP1B_HUMANDEPDC1Bphysical
26186194
UBE3B_HUMANUBE3Bphysical
26186194
RT07_HUMANMRPS7physical
26186194
ZO2_HUMANTJP2physical
26186194
EOGT_HUMANEOGTphysical
26186194
TIMP3_HUMANTIMP3physical
26186194
PRC1_HUMANPRC1physical
26186194
TRI68_HUMANTRIM68physical
26186194
B9D1_HUMANB9D1physical
26186194
PDIA5_HUMANPDIA5physical
26186194
FBLN1_HUMANFBLN1physical
26186194
EGFL7_HUMANEGFL7physical
26186194
GTPB2_HUMANGTPBP2physical
26186194
F122B_HUMANFAM122Bphysical
26186194
BRCA1_HUMANBRCA1physical
26186194
SLX4I_HUMANSLX4IPphysical
26186194
B4GT1_HUMANB4GALT1physical
26186194
UBP46_HUMANUSP46physical
26186194
G3BP1_HUMANG3BP1physical
26344197
G3BP2_HUMANG3BP2physical
26344197
SNX12_HUMANSNX12physical
26344197
DAPK1_HUMANDAPK1physical
28514442
TTC31_HUMANTTC31physical
28514442
DEP1B_HUMANDEPDC1Bphysical
28514442
UBE3B_HUMANUBE3Bphysical
28514442
ZO1_HUMANTJP1physical
28514442
GTPB2_HUMANGTPBP2physical
28514442
ZO2_HUMANTJP2physical
28514442
BRCA1_HUMANBRCA1physical
28514442
F122B_HUMANFAM122Bphysical
28514442
F120A_HUMANFAM120Aphysical
28514442
L2GL2_HUMANLLGL2physical
28514442
PRC1_HUMANPRC1physical
28514442
SLX4I_HUMANSLX4IPphysical
28514442
EOGT_HUMANEOGTphysical
28514442
TRI68_HUMANTRIM68physical
28514442
UBP46_HUMANUSP46physical
28514442
TIMP3_HUMANTIMP3physical
28514442
RT07_HUMANMRPS7physical
28514442
NPTX1_HUMANNPTX1physical
28514442

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-45, AND MASSSPECTROMETRY.

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