OFUT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: OFUT1_HUMAN
• UniProt AC: Q9H488
• Protein Name: GDP-fucose protein O-fucosyltransferase 1
• Gene Name: POFUT1
• Organism: Homo sapiens (Human).
• Sequence Length: 388
• Subcellular Localization: Endoplasmic reticulum .
• Protein Description: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs)..
• Protein Sequence: MGAAAWARPLSVSFLLLLLPLPGMPAGSWDPAGYLLYCPCMGRFGNQADHFLGSLAFAKLLNRTLAVPPWIEYQHHKPPFTNLHVSYQKYFKLEPLQAYHRVISLEDFMEKLAPTHWPPEKRVAYCFEVAAQRSPDKKTCPMKEGNPFGPFWDQFHVSFNKSELFTGISFSASYREQWSQRFSPKEHPVLALPGAPAQFPVLEEHRPLQKYMVWSDEMVKTGEAQIHAHLVRPYVGIHLRIGSDWKNACAMLKDGTAGSHFMASPQCVGYSRSTAAPLTMTMCLPDLKEIQRAVKLWVRSLDAQSVYVATDSESYVPELQQLFKGKVKVVSLKPEVAQVDLYILGQADHFIGNCVSSFTAFVKRERDLQGRPSSFFGMDRPPKLRDEF

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
62	N-linked_Glycosylation	LAFAKLLNRTLAVPP HHHHHHHHCCCCCCC	45.38	28334865
87	Phosphorylation	FTNLHVSYQKYFKLE CCEEEEEEEHHCCCC	14.13	-
92	Ubiquitination	VSYQKYFKLEPLQAY EEEEHHCCCCHHHHH	49.18	-
104	Phosphorylation	QAYHRVISLEDFMEK HHHCEEEEHHHHHHH	23.89	21712546
160	N-linked_Glycosylation	DQFHVSFNKSELFTG HHEEEEECHHHHCEE	39.16	19159218
162	Phosphorylation	FHVSFNKSELFTGIS EEEEECHHHHCEECE	40.41	23663014
166	Phosphorylation	FNKSELFTGISFSAS ECHHHHCEECEEEEH	46.35	23663014
169	Phosphorylation	SELFTGISFSASYRE HHHCEECEEEEHHHH	17.94	23663014
171	Phosphorylation	LFTGISFSASYREQW HCEECEEEEHHHHHH	14.98	23663014
173	Phosphorylation	TGISFSASYREQWSQ EECEEEEHHHHHHHH	24.43	23663014
174	Phosphorylation	GISFSASYREQWSQR ECEEEEHHHHHHHHH	20.20	23663014
179	Phosphorylation	ASYREQWSQRFSPKE EHHHHHHHHHCCCCC	15.92	23663014
183	Phosphorylation	EQWSQRFSPKEHPVL HHHHHHCCCCCCCEE	36.93	24719451
211	Phosphorylation	EHRPLQKYMVWSDEM CCCCCCEEEEECHHH	5.50	22817900
246	Ubiquitination	LRIGSDWKNACAMLK EEECCCHHHHHHHCC	39.39	-
253	Acetylation	KNACAMLKDGTAGSH HHHHHHCCCCCCCCC	40.81	26051181
256	Phosphorylation	CAMLKDGTAGSHFMA HHHCCCCCCCCCEEC	37.67	21406692
259	Phosphorylation	LKDGTAGSHFMASPQ CCCCCCCCCEECCCH	15.87	21406692
264	Phosphorylation	AGSHFMASPQCVGYS CCCCEECCCHHCCCC	12.06	21406692
270	Phosphorylation	ASPQCVGYSRSTAAP CCCHHCCCCCCCCCC	4.78	21406692
271	Phosphorylation	SPQCVGYSRSTAAPL CCHHCCCCCCCCCCC	17.52	21406692
283	Glutathionylation	APLTMTMCLPDLKEI CCCEEEEECCCHHHH	3.52	22555962
295	Ubiquitination	KEIQRAVKLWVRSLD HHHHHHHHHHHHCCC	35.33	-
310	Phosphorylation	AQSVYVATDSESYVP CCEEEEEECCHHHHH	29.98	-
324	Ubiquitination	PELQQLFKGKVKVVS HHHHHHHCCCCEEEE	67.43	22817900
324 (in isoform 1)	Ubiquitination	-	67.43	21906983
326	Ubiquitination	LQQLFKGKVKVVSLK HHHHHCCCCEEEECC	39.20	22817900
328	Ubiquitination	QLFKGKVKVVSLKPE HHHCCCCEEEECCCC	40.17	22817900
378	Sulfoxidation	RPSSFFGMDRPPKLR CCCHHCCCCCCCCCC	3.14	21406390

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of OFUT1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of OFUT1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of OFUT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THIM_HUMAN	ACAA2	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 615327: Dowling-Degos disease 2 (DDD2)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-160, AND MASSSPECTROMETRY.
PubMed: 19159218