HACD3_HUMAN - dbPTM
HACD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HACD3_HUMAN
UniProt AC Q9P035
Protein Name Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 {ECO:0000305}
Gene Name HACD3 {ECO:0000303|PubMed:18554506, ECO:0000312|HGNC:HGNC:24175}
Organism Homo sapiens (Human).
Sequence Length 362
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May be involved in Rac1-signaling pathways leading to the modulation of gene expression. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization. [PubMed: 25687571]
Protein Sequence MENQVLTPHVYWAQRHRELYLRVELSDVQNPAISITENVLHFKAQGHGAKGDNVYEFHLEFLDLVKPEPVYKLTQRQVNITVQKKVSQWWERLTKQEKRPLFLAPDFDRWLDESDAEMELRAKEEERLNKLRLESEGSPETLTNLRKGYLFMYNLVQFLGFSWIFVNLTVRFCILGKESFYDTFHTVADMMYFCQMLAVVETINAAIGVTTSPVLPSLIQLLGRNFILFIIFGTMEEMQNKAVVFFVFYLWSAIEIFRYSFYMLTCIDMDWKVLTWLRYTLWIPLYPLGCLAEAVSVIQSIPIFNETGRFSFTLPYPVKIKVRFSFFLQIYLIMIFLGLYINFRHLYKQRRRRYGQKKKKIH
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
1Acetylation-------MENQVLTP
-------CCCCCCCC		11.1525944712
7Phosphorylation-MENQVLTPHVYWAQ
-CCCCCCCCCHHHHH		16.7027422710
11PhosphorylationQVLTPHVYWAQRHRE
CCCCCCHHHHHHHHE		7.6226074081
15MethylationPHVYWAQRHRELYLR
CCHHHHHHHHEEEEE		24.08115489605
26PhosphorylationLYLRVELSDVQNPAI
EEEEEEEHHCCCCCE		23.41-
43UbiquitinationTENVLHFKAQGHGAK
ECCEEEEEECCCCCC		29.1121890473
43AcetylationTENVLHFKAQGHGAK
ECCEEEEEECCCCCC		29.1125953088
43UbiquitinationTENVLHFKAQGHGAK
ECCEEEEEECCCCCC		29.1121890473
72AcetylationVKPEPVYKLTQRQVN
CCCCCEEEEEECEEE		45.347665255
75UbiquitinationEPVYKLTQRQVNITV
CCEEEEEECEEEEEH		44.22-
84AcetylationQVNITVQKKVSQWWE
EEEEEHHHHHHHHHH		51.2925953088
842-HydroxyisobutyrylationQVNITVQKKVSQWWE
EEEEEHHHHHHHHHH		51.29-
85MalonylationVNITVQKKVSQWWER
EEEEHHHHHHHHHHH		29.9926320211
852-HydroxyisobutyrylationVNITVQKKVSQWWER
EEEEHHHHHHHHHHH		29.99-
85UbiquitinationVNITVQKKVSQWWER
EEEEHHHHHHHHHHH		29.99-
92MethylationKVSQWWERLTKQEKR
HHHHHHHHHHHHCCC		33.66115489621
98AcetylationERLTKQEKRPLFLAP
HHHHHHCCCCCEECC		57.7425953088
98UbiquitinationERLTKQEKRPLFLAP
HHHHHHCCCCCEECC		57.7421890473
99MethylationRLTKQEKRPLFLAPD
HHHHHCCCCCEECCC		32.19115489613
114PhosphorylationFDRWLDESDAEMELR
HHHHCCCCHHHHHHH		41.6119664994
130UbiquitinationKEEERLNKLRLESEG
HHHHHHHHHHHCCCC		39.312190698
135PhosphorylationLNKLRLESEGSPETL
HHHHHHCCCCCHHHH		52.4230266825
138PhosphorylationLRLESEGSPETLTNL
HHHCCCCCHHHHHHH		18.6030266825
141PhosphorylationESEGSPETLTNLRKG
CCCCCHHHHHHHHHH		42.1223403867
143PhosphorylationEGSPETLTNLRKGYL
CCCHHHHHHHHHHHH		39.3628176443
259PhosphorylationSAIEIFRYSFYMLTC
HHHHHHHHHHHHHHH		7.7423401153
260PhosphorylationAIEIFRYSFYMLTCI
HHHHHHHHHHHHHHH		12.9723401153
262PhosphorylationEIFRYSFYMLTCIDM
HHHHHHHHHHHHHCC		5.8123401153
264UbiquitinationFRYSFYMLTCIDMDW
HHHHHHHHHHHCCCH		2.1121890473
265PhosphorylationRYSFYMLTCIDMDWK
HHHHHHHHHHCCCHH		7.2923401153
313PhosphorylationETGRFSFTLPYPVKI
CCCCEEEECCCCEEE		26.1428152594
316PhosphorylationRFSFTLPYPVKIKVR
CEEEECCCCEEEEEH		24.6228152594
319UbiquitinationFTLPYPVKIKVRFSF
EECCCCEEEEEHHHH		32.1021890473
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 HACD3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HACD3_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 HACD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AT2A2_HUMANATP2A2physical
25036637
PEX19_HUMANPEX19physical
25036637
AT2B1_HUMANATP2B1physical
25036637
BZW2_HUMANBZW2physical
25036637
FANCI_HUMANFANCIphysical
25036637
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 HACD3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.

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