FURIN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FURIN_HUMAN
• UniProt AC: P09958
• Protein Name: Furin
• Gene Name: FURIN
• Organism: Homo sapiens (Human).
• Sequence Length: 794
• Subcellular Localization: Golgi apparatus, trans-Golgi network membrane ; Single-pass type I membrane protein . Cell membrane ; Single-pass type I membrane protein . Secreted . Endosome membrane ; Single-pass type I membrane protein . Shuttles between the trans-Golgi network
• Protein Description: Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.; (Microbial infection) Probably cleaves and activates anthrax and diphtheria toxins.; (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin..
• Protein Sequence: MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPEVVAGLSCAFIVLVFVTVFLVLQLRSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL

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
123	Phosphorylation	PKFPQQWYLSGVTQR CCCCHHCCCCCCCHH	6.15	-
253	Phosphorylation	HIHIYSASWGPEDDG EEEEEECCCCCCCCC	26.99	-
387	N-linked_Glycosylation	LTLEANKNLTWRDMQ EEHHHHCCCCHHHCE	42.37	UniProtKB CARBOHYD
440	N-linked_Glycosylation	AMVALAQNWTTVAPQ HHHHHHCCCCCCCCC	32.24	UniProtKB CARBOHYD
553	N-linked_Glycosylation	EWVLEIENTSEANNY CEEEEEECCCCCCCC	55.34	UniProtKB CARBOHYD
625	Phosphorylation	FAPQVLDTHYSTEND CCCHHHCCCCCCCCC	20.67	24275569
629	Phosphorylation	VLDTHYSTENDVETI HHCCCCCCCCCHHHH	31.48	24275569
743	Phosphorylation	LQLRSGFSFRGVKVY HHHHCCCCCCCEEEE	19.98	24719451
748	Ubiquitination	GFSFRGVKVYTMDRG CCCCCCEEEEEECCC	32.14	21890473
750	Phosphorylation	SFRGVKVYTMDRGLI CCCCEEEEEECCCEE	7.22	25072903
751	Phosphorylation	FRGVKVYTMDRGLIS CCCEEEEEECCCEEC	18.64	25072903
758	Phosphorylation	TMDRGLISYKGLPPE EECCCEECCCCCCHH	26.32	25072903
759	Phosphorylation	MDRGLISYKGLPPEA ECCCEECCCCCCHHH	11.33	25072903
771	S-palmitoylation	PEAWQEECPSDSEED HHHHHHHCCCCCCCC	3.73	30610172
773	Phosphorylation	AWQEECPSDSEEDEG HHHHHCCCCCCCCCC	66.48	23927012
775	Phosphorylation	QEECPSDSEEDEGRG HHHCCCCCCCCCCCC	47.42	23927012
785	Phosphorylation	DEGRGERTAFIKDQS CCCCCCCCEEECCCC	22.93	29514088
789	Acetylation	GERTAFIKDQSAL-- CCCCEEECCCCCC--	43.17	20167786
789	Ubiquitination	GERTAFIKDQSAL-- CCCCEEECCCCCC--	43.17	-

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
773	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
773	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
773	S	Phosphorylation	Kinase	CK2	-	Uniprot
775	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
775	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
775	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FURIN_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 FURIN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FLNA_MOUSE	Flna	physical	9412467
AP2M1_HUMAN	AP2M1	physical	10593987
PACS1_HUMAN	PACS1	physical	9695949
ENV_HV1H2	env	physical	8940009
MMP14_HUMAN	MMP14	physical	8804434

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Intracellular trafficking of furin is modulated by thephosphorylation state of a casein kinase II site in its cytoplasmictail.";
Jones B.G., Thomas L., Molloy S.S., Thulin C.D., Fry M.D., Walsh K.A.,Thomas G.;
EMBO J. 14:5869-5883(1995).
Cited for: PHOSPHORYLATION AT SER-773 AND SER-775.
PubMed: 8846780