ENOF1_HUMAN - dbPTM
ENOF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENOF1_HUMAN
UniProt AC Q7L5Y1
Protein Name Mitochondrial enolase superfamily member 1
Gene Name ENOSF1
Organism Homo sapiens (Human).
Sequence Length 443
Subcellular Localization Mitochondrion .
Protein Description Plays a role in the catabolism of L-fucose, a sugar that is part of the carbohydrates that are attached to cellular glycoproteins. Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion. [PubMed: 24697329]
Protein Sequence MVRGRISRLSVRDVRFPTSLGGHGADAMHTDPDYSAAYVVIETDAEDGIKGCGITFTLGKGTEVVVCAVNALAHHVLNKDLKDIVGDFRGFYRQLTSDGQLRWIGPEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIDFRYITDVLTEEDALEILQKGQIGKKEREKQMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKHQYPDGEVWKKLLPAQEN
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
36UbiquitinationHTDPDYSAAYVVIET
CCCCCCCEEEEEEEE		9.15-
39UbiquitinationPDYSAAYVVIETDAE
CCCCEEEEEEEECCC		2.76-
41UbiquitinationYSAAYVVIETDAEDG
CCEEEEEEEECCCCC		3.17-
41UbiquitinationYSAAYVVIETDAEDG
CCEEEEEEEECCCCC		3.1729967540
62UbiquitinationTFTLGKGTEVVVCAV
EEEECCCCEEEEEHH		29.14-
76UbiquitinationVNALAHHVLNKDLKD
HHHHHHHHCCCCHHH		4.5321963094
82UbiquitinationHVLNKDLKDIVGDFR
HHCCCCHHHHHHHHH		56.3929967540
84UbiquitinationLNKDLKDIVGDFRGF
CCCCHHHHHHHHHHH		3.40-
85UbiquitinationNKDLKDIVGDFRGFY
CCCHHHHHHHHHHHH		9.6229967540
90UbiquitinationDIVGDFRGFYRQLTS
HHHHHHHHHHHHCCC		24.7521963094
92PhosphorylationVGDFRGFYRQLTSDG
HHHHHHHHHHCCCCC		10.5627134283
96PhosphorylationRGFYRQLTSDGQLRW
HHHHHHCCCCCCEEE		19.2127134283
97PhosphorylationGFYRQLTSDGQLRWI
HHHHHCCCCCCEEEE		48.6227134283
97UbiquitinationGFYRQLTSDGQLRWI
HHHHHCCCCCCEEEE		48.6221963094
111UbiquitinationIGPEKGVVHLATAAV
ECCCCCHHHHHHHHH		4.1121963094
132UbiquitinationLWAKQEGKPVWKLLV
HHHHHCCCCEEEEEE		35.3329967540
133UbiquitinationWAKQEGKPVWKLLVD
HHHHCCCCEEEEEEC		48.3229967540
148PhosphorylationMDPRMLVSCIDFRYI
CCHHHHHHHEEHHHH		11.0314702039
166UbiquitinationLTEEDALEILQKGQI
CCHHHHHHHHHHCCC		43.29-
170UbiquitinationDALEILQKGQIGKKE
HHHHHHHHCCCCHHH		49.7029967540
189UbiquitinationMLAQGYPAYTTSCAW
HHHCCCCCEECCCHH		13.0621963094
201UbiquitinationCAWLGYSDDTLKQLC
CHHCCCCHHHHHHHH		44.4221963094
206UbiquitinationYSDDTLKQLCAQALK
CCHHHHHHHHHHHHH		44.90-
210UbiquitinationTLKQLCAQALKDGWT
HHHHHHHHHHHHCCE		46.3521963094
215UbiquitinationCAQALKDGWTRFKVK
HHHHHHHCCEEEEEE		26.5221963094
222UbiquitinationGWTRFKVKVGADLQD
CCEEEEEEECCCCHH		35.2329967540
244UbiquitinationIRDMIGPEKTLMMDA
HHHHHCCCCEEEECH		54.1629967540
246PhosphorylationDMIGPEKTLMMDANQ
HHHCCCCEEEECHHH		20.44-
254UbiquitinationLMMDANQRWDVPEAV
EEECHHHCCCHHHHH		31.2229967540
255UbiquitinationMMDANQRWDVPEAVE
EECHHHCCCHHHHHH		10.9429967540
266UbiquitinationEAVEWMSKLAKFKPL
HHHHHHHHHHHCCCC		36.0429967540
269UbiquitinationEWMSKLAKFKPLWIE
HHHHHHHHCCCCEEC		65.44-
271UbiquitinationMSKLAKFKPLWIEEP
HHHHHHCCCCEECCC		38.1921963094
279PhosphorylationPLWIEEPTSPDDILG
CCEECCCCCCCCCCC		57.0526657352
280PhosphorylationLWIEEPTSPDDILGH
CEECCCCCCCCCCCC		36.7328857561
286UbiquitinationTSPDDILGHATISKA
CCCCCCCCCCHHHHH		14.5521963094
292UbiquitinationLGHATISKALVPLGI
CCCCHHHHHHHCCCC		41.7221963094
300PhosphorylationALVPLGIGIATGEQC
HHHCCCCCCCCCCHH		11.1527251275
307UbiquitinationGIATGEQCHNRVIFK
CCCCCCHHHHHHHHH		2.4021963094
314UbiquitinationCHNRVIFKQLLQAKA
HHHHHHHHHHHHHHH		28.9821963094
334UbiquitinationIDSCRLGSVNENLSV
CCCCCCCCCCCCHHH		26.7621963094
340PhosphorylationGSVNENLSVLLMAKK
CCCCCCHHHHHHHCC		23.4629759185
382UbiquitinationSVSASLENRVCEYVD
HCCHHHHHHHHHHHH		47.1521963094
387PhosphorylationLENRVCEYVDHLHEH
HHHHHHHHHHHHHHH		13.1718452278
396UbiquitinationDHLHEHFKYPVMIQR
HHHHHHCCCCEEEEE		51.0221963094
397PhosphorylationHLHEHFKYPVMIQRA
HHHHHCCCCEEEEEC		10.5025850435
403UbiquitinationKYPVMIQRASYMPPK
CCCEEEEECCCCCCC		17.9921963094
405PhosphorylationPVMIQRASYMPPKDP
CEEEEECCCCCCCCC		24.9322985185
406PhosphorylationVMIQRASYMPPKDPG
EEEEECCCCCCCCCC		16.8025850435
411UbiquitinationASYMPPKDPGYSTEM
CCCCCCCCCCCCCCC		47.8621963094
422PhosphorylationSTEMKEESVKKHQYP
CCCCCHHHHHHHCCC		40.0924702127
425UbiquitinationMKEESVKKHQYPDGE
CCHHHHHHHCCCCCH		33.5129967540
435UbiquitinationYPDGEVWKKLLPAQE
CCCCHHHHHHCCCCC		38.4229967540
436UbiquitinationPDGEVWKKLLPAQEN
CCCHHHHHHCCCCCC		39.2729967540
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 ENOF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENOF1_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 ENOF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ENOF1_HUMAN !!
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 ENOF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Enhancement of 5-fluorouracil sensitivity by an rTS signaling mimicin H630 colon cancer cells.";
Dolnick R., Wu Q., Angelino N.J., Stephanie L.V., Chow K.-C.,Sufrin J.R., Dolnick B.J.;
Cancer Res. 65:5917-5924(2005).
Cited for: PHOSPHORYLATION AT SER-148, AND SUMOYLATION.

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