FCL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FCL_HUMAN
• UniProt AC: Q13630
• Protein Name: GDP-L-fucose synthase
• Gene Name: TSTA3
• Organism: Homo sapiens (Human).
• Sequence Length: 321
• Protein Description: Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction..
• Protein Sequence: MGEPQGSMRILVTGGSGLVGKAIQKVVADGAGLPGEDWVFVSSKDADLTDTAQTRALFEKVQPTHVIHLAAMVGGLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAVIPTNVFGPHDNFNIEDGHVLPGLIHKVHLAKSSGSALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNEVEPIILSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFTPFKQAVKETCAWFTDNYEQARK

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
7	Phosphorylation	-MGEPQGSMRILVTG -CCCCCCCEEEEEEC	10.31	24719451
13	Phosphorylation	GSMRILVTGGSGLVG CCEEEEEECCCCHHH	32.17	20068231
16	Phosphorylation	RILVTGGSGLVGKAI EEEEECCCCHHHHHH	30.23	20860994
21	Ubiquitination	GGSGLVGKAIQKVVA CCCCHHHHHHHHHHH	34.53	21906983
25	Ubiquitination	LVGKAIQKVVADGAG HHHHHHHHHHHCCCC	32.34	-
42	Phosphorylation	GEDWVFVSSKDADLT CCCEEEEECCCCCCC	21.87	28348404
43	Phosphorylation	EDWVFVSSKDADLTD CCEEEEECCCCCCCC	29.29	28348404
44	Ubiquitination	DWVFVSSKDADLTDT CEEEEECCCCCCCCH	49.80	21906983
81	Acetylation	GGLFRNIKYNLDFWR HHHHHHHCCCHHHHH	31.47	26051181
82	Phosphorylation	GLFRNIKYNLDFWRK HHHHHHCCCHHHHHH	19.70	27251275
89	Ubiquitination	YNLDFWRKNVHMNDN CCHHHHHHCCCCCCC	54.65	-
111	Phosphorylation	VGARKVVSCLSTCIF HCHHHHHHHHHHCCC	16.60	30622161
114	Phosphorylation	RKVVSCLSTCIFPDK HHHHHHHHHCCCCCC	26.09	30622161
115	Phosphorylation	KVVSCLSTCIFPDKT HHHHHHHHCCCCCCC	9.18	30622161
147	Acetylation	NFGYSYAKRMIDVQN CCCHHHHHHHHHCCC	33.98	23954790
200	Phosphorylation	HKVHLAKSSGSALTV EEEEEHHCCCCCEEE	34.03	20068231
201	Phosphorylation	KVHLAKSSGSALTVW EEEEHHCCCCCEEEE	35.74	20068231
203	Phosphorylation	HLAKSSGSALTVWGT EEHHCCCCCEEEECC	23.27	25693802
206	Phosphorylation	KSSGSALTVWGTGNP HCCCCCEEEECCCCC	17.58	25693802
287	Phosphorylation	FKKTASNSKLRTYLP EEEEECCCCCHHCCC	30.48	-
306	Ubiquitination	TPFKQAVKETCAWFT CCHHHHHHHHHHHHH	50.77	-
316	Phosphorylation	CAWFTDNYEQARK-- HHHHHCCHHHHHC--	16.54	20068231

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FCL_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 FCL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBBP7_HUMAN	RBBP7	physical	22863883
PCBP3_HUMAN	PCBP3	physical	26186194
ARFP1_HUMAN	ARFIP1	physical	26344197
G6PD_HUMAN	G6PD	physical	26344197
GALE_HUMAN	GALE	physical	26344197
HNRH1_HUMAN	HNRNPH1	physical	26344197
KDM3A_HUMAN	KDM3A	physical	26344197
NTM1A_HUMAN	NTMT1	physical	26344197
MSS4_HUMAN	RABIF	physical	26344197
SC31A_HUMAN	SEC31A	physical	26344197
XPO1_HUMAN	XPO1	physical	26344197
PCBP3_HUMAN	PCBP3	physical	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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147, AND MASS SPECTROMETRY.
PubMed: 19608861