GLTP_HUMAN - dbPTM
GLTP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLTP_HUMAN
UniProt AC Q9NZD2
Protein Name Glycolipid transfer protein
Gene Name GLTP
Organism Homo sapiens (Human).
Sequence Length 209
Subcellular Localization Cytoplasm .
Protein Description Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides..
Protein Sequence MALLAEHLLKPLPADKQIETGPFLEAVSHLPPFFDCLGSPVFTPIKADISGNITKIKAVYDTNPAKFRTLQNILEVEKEMYGAEWPKVGATLALMWLKRGLRFIQVFLQSICDGERDENHPNLIRVNATKAYEMALKKYHGWIVQKIFQAALYAAPYKSDFLKALSKGQNVTEEECLEKIRLFLVNYTATIDVIYEMYTQMNAELNYKV
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
2Acetylation------MALLAEHLL
------CCHHHHHHH
15.98-
55UbiquitinationDISGNITKIKAVYDT
CCCCCEEEEEEEEEC
38.11-
57UbiquitinationSGNITKIKAVYDTNP
CCCEEEEEEEEECCH
33.10-
66UbiquitinationVYDTNPAKFRTLQNI
EEECCHHHHHHHHHH
36.3121890473
69PhosphorylationTNPAKFRTLQNILEV
CCHHHHHHHHHHHHH
35.5120068231
91PhosphorylationEWPKVGATLALMWLK
CCCHHHHHHHHHHHH
13.4620068231
132PhosphorylationRVNATKAYEMALKKY
EECCHHHHHHHHHHH
14.0625907765
138UbiquitinationAYEMALKKYHGWIVQ
HHHHHHHHHHCHHHH
43.24-
139PhosphorylationYEMALKKYHGWIVQK
HHHHHHHHHCHHHHH
12.1825907765
158UbiquitinationALYAAPYKSDFLKAL
HHHHCCCCHHHHHHH
42.35-
167UbiquitinationDFLKALSKGQNVTEE
HHHHHHHCCCCCCHH
66.42-
179UbiquitinationTEEECLEKIRLFLVN
CHHHHHHHHHHHHHH
21.8521890473
195PhosphorylationTATIDVIYEMYTQMN
HCHHHHHHHHHHHHH
8.42-

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 GLTP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLTP_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 GLTP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CKLF5_HUMANCMTM5physical
25416956
STAR7_HUMANSTARD7physical
28514442
ASPC1_HUMANASPSCR1physical
28514442
SHKB1_HUMANSHKBP1physical
28514442
DCAM_HUMANAMD1physical
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 GLTP_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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