NCEH1_HUMAN - dbPTM
NCEH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCEH1_HUMAN
UniProt AC Q6PIU2
Protein Name Neutral cholesterol ester hydrolase 1
Gene Name NCEH1
Organism Homo sapiens (Human).
Sequence Length 408
Subcellular Localization Membrane
Single-pass type II membrane protein . Microsome.
Protein Description Hydrolyzes 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor. May be responsible for cholesterol ester hydrolysis in macrophages, thereby contributing to the development of atherosclerosis. Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds. May contribute to cancer pathogenesis by promoting tumor cell migration..
Protein Sequence MRSSCVLLTALVALAAYYVYIPLPGSVSDPWKLMLLDATFRGAQQVSNLIHYLGLSHHLLALNFIIVSFGKKSAWSSAQVKVTDTDFDGVEVRVFEGPPKPEEPLKRSVVYIHGGGWALASAKIRYYDELCTAMAEELNAVIVSIEYRLVPKVYFPEQIHDVVRATKYFLKPEVLQKYMVDPGRICISGDSAGGNLAAALGQQFTQDASLKNKLKLQALIYPVLQALDFNTPSYQQNVNTPILPRYVMVKYWVDYFKGNYDFVQAMIVNNHTSLDVEEAAAVRARLNWTSLLPASFTKNYKPVVQTTGNARIVQELPQLLDARSAPLIADQAVLQLLPKTYILTCEHDVLRDDGIMYAKRLESAGVEVTLDHFEDGFHGCMIFTSWPTNFSVGIRTRNSYIKWLDQNL
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
39PhosphorylationKLMLLDATFRGAQQV
HHHHHHCCHHCHHHH		17.3320068231
85PhosphorylationAQVKVTDTDFDGVEV
CEEEEECCCCCCCEE		29.24110753309
1062-HydroxyisobutyrylationPKPEEPLKRSVVYIH
CCCCCCCCCEEEEEE		54.03-
117PhosphorylationVYIHGGGWALASAKI
EEEECCCHHHHHHEH		7.44-
132UbiquitinationRYYDELCTAMAEELN
HHHHHHHHHHHHHHC		31.90-
144PhosphorylationELNAVIVSIEYRLVP
HHCCEEEEEEEEECC		9.8924043423
147PhosphorylationAVIVSIEYRLVPKVY
CEEEEEEEEECCCCC		13.9424043423
1522-HydroxyisobutyrylationIEYRLVPKVYFPEQI
EEEEECCCCCCHHHH		41.93-
154PhosphorylationYRLVPKVYFPEQIHD
EEECCCCCCHHHHHH		21.3929759185
166PhosphorylationIHDVVRATKYFLKPE
HHHHHHHHHHHCCHH		18.7329759185
168PhosphorylationDVVRATKYFLKPEVL
HHHHHHHHHCCHHHH		15.1320068231
176PhosphorylationFLKPEVLQKYMVDPG
HCCHHHHHHHCCCCC		39.75-
200PhosphorylationGGNLAAALGQQFTQD
HHHHHHHHCCCCCCC		5.6620068231
240PhosphorylationSYQQNVNTPILPRYV
CHHCCCCCCCCCHHH		13.86110753315
270N-linked_GlycosylationVQAMIVNNHTSLDVE
EEEEEECCCCCCCHH		28.99UniProtKB CARBOHYD
272PhosphorylationAMIVNNHTSLDVEEA
EEEECCCCCCCHHHH		32.86-
287N-linked_GlycosylationAAVRARLNWTSLLPA
HHHHHHCCHHHHCCC		34.1319159218
295PhosphorylationWTSLLPASFTKNYKP
HHHHCCCHHCCCCCC		31.3568707747
297PhosphorylationSLLPASFTKNYKPVV
HHCCCHHCCCCCCEE		18.8468707753
319N-linked_GlycosylationIVQELPQLLDARSAP
HHHHHHHHHCCCCCC		4.3919159218
333UbiquitinationPLIADQAVLQLLPKT
CCCCCHHHHHHCCCE		2.66-
3592-HydroxyisobutyrylationDDGIMYAKRLESAGV
CCCEEEEEEHHHCCC		39.77-
389N-linked_GlycosylationIFTSWPTNFSVGIRT
EEECCCCCEEEEEEC		24.10UniProtKB CARBOHYD
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 NCEH1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCEH1_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 NCEH1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UD3A2_HUMANUGT3A2physical
28514442
NRN1_HUMANNRN1physical
28514442
LRRC3_HUMANLRRC3physical
28514442
TM231_HUMANTMEM231physical
28514442
SIA10_HUMANST3GAL6physical
28514442
CANT1_HUMANCANT1physical
28514442
AMGO1_HUMANAMIGO1physical
28514442
ALG9_HUMANALG9physical
28514442
LMF2_HUMANLMF2physical
28514442
BT2A2_HUMANBTN2A2physical
28514442
GLBL2_HUMANGLB1L2physical
28514442
CGT_HUMANUGT8physical
28514442
POMT1_HUMANPOMT1physical
28514442
C1QRF_HUMANC1QL1physical
28514442
E2AK3_HUMANEIF2AK3physical
28514442
IPRI_HUMANITPRIPphysical
28514442
FA69A_HUMANFAM69Aphysical
28514442
TMTC3_HUMANTMTC3physical
28514442
CALX_HUMANCANXphysical
28514442
CD151_HUMANCD151physical
28514442
GALT7_HUMANGALNT7physical
28514442
CCPG1_HUMANCCPG1physical
28514442
ITA7_HUMANITGA7physical
28514442
HYAL2_HUMANHYAL2physical
28514442
SCRB1_HUMANSCARB1physical
28514442
SIA7C_HUMANST6GALNAC3physical
28514442
PGAP1_HUMANPGAP1physical
28514442
MTFP1_HUMANMTFP1physical
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 NCEH1_HUMAN

loading...

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-287, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory