dbPTM

MTHFS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MTHFS_HUMAN
UniProt AC	P49914
Protein Name	5-formyltetrahydrofolate cyclo-ligase
Gene Name	MTHFS
Organism	Homo sapiens (Human).
Sequence Length	203
Subcellular Localization	Cytoplasm.
Protein Description	Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to yield 5,10-methenyltetrahydrofolate..
Protein Sequence	MAAAAVSSAKRSLRGELKQRLRAMSAEERLRQSRVLSQKVIAHSEYQKSKRISIFLSMQDEIETEEIIKDIFQRGKICFIPRYRFQSNHMDMVRIESPEEISLLPKTSWNIPQPGEGDVREEALSTGGLDLIFMPGLGFDKHGNRLGRGKGYYDAYLKRCLQHQEVKPYTLALAFKEQICLQVPVNENDMKVDEVLYEDSSTA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAAVSSA ------CHHHHHHHH	13.05	22814378
4 (in isoform 2)	Phosphorylation	-	10.00	-
7	Phosphorylation	-MAAAAVSSAKRSLR -CHHHHHHHHHHHHH	21.61	29255136
8	Phosphorylation	MAAAAVSSAKRSLRG CHHHHHHHHHHHHHH	31.07	29255136
10	Acetylation	AAAVSSAKRSLRGEL HHHHHHHHHHHHHHH	44.46	18585117
10	Sumoylation	AAAVSSAKRSLRGEL HHHHHHHHHHHHHHH	44.46	-
10	Ubiquitination	AAAVSSAKRSLRGEL HHHHHHHHHHHHHHH	44.46	22053931
10	Sumoylation	AAAVSSAKRSLRGEL HHHHHHHHHHHHHHH	44.46	-
18	Acetylation	RSLRGELKQRLRAMS HHHHHHHHHHHHHCC	29.12	25953088
37	Phosphorylation	LRQSRVLSQKVIAHS HHHHHHHCHHHHHCH	25.71	20068231
39	Ubiquitination	QSRVLSQKVIAHSEY HHHHHCHHHHHCHHH	32.03	29967540
44	Phosphorylation	SQKVIAHSEYQKSKR CHHHHHCHHHHHHHC	29.04	20068231
46	Phosphorylation	KVIAHSEYQKSKRIS HHHHCHHHHHHHCEE	25.02	20068231
48	Ubiquitination	IAHSEYQKSKRISIF HHCHHHHHHHCEEEE	57.98	29967540
49	Phosphorylation	AHSEYQKSKRISIFL HCHHHHHHHCEEEEE	16.19	20068231
76	Ubiquitination	KDIFQRGKICFIPRY HHHHHCCCEEEEECC	38.19	-
83	Phosphorylation	KICFIPRYRFQSNHM CEEEEECCCCCCCCC	15.49	28857561
84	Ubiquitination	ICFIPRYRFQSNHMD EEEEECCCCCCCCCC	25.14	29967540
87	Phosphorylation	IPRYRFQSNHMDMVR EECCCCCCCCCCEEE	26.45	26330541
93	Ubiquitination	QSNHMDMVRIESPEE CCCCCCEEEECCHHH	4.93	33845483
97	Phosphorylation	MDMVRIESPEEISLL CCEEEECCHHHHCCC	34.93	26471730
101	Ubiquitination	RIESPEEISLLPKTS EECCHHHHCCCCCCC	3.16	29967540
102	Phosphorylation	IESPEEISLLPKTSW ECCHHHHCCCCCCCC	27.42	27251275
107	Phosphorylation	EISLLPKTSWNIPQP HHCCCCCCCCCCCCC	36.71	24275569
108	Phosphorylation	ISLLPKTSWNIPQPG HCCCCCCCCCCCCCC	25.01	26471730
141	Ubiquitination	MPGLGFDKHGNRLGR CCCCCCCCCCCCCCC	51.67	29967540
150	Ubiquitination	GNRLGRGKGYYDAYL CCCCCCCCCHHHHHH	42.24	33845483
150	Acetylation	GNRLGRGKGYYDAYL CCCCCCCCCHHHHHH	42.24	25825284
150	Malonylation	GNRLGRGKGYYDAYL CCCCCCCCCHHHHHH	42.24	26320211
152	Phosphorylation	RLGRGKGYYDAYLKR CCCCCCCHHHHHHHH	11.14	29496907
156	Phosphorylation	GKGYYDAYLKRCLQH CCCHHHHHHHHHHHC	15.17	29496907
158	Ubiquitination	GYYDAYLKRCLQHQE CHHHHHHHHHHHCCC	28.52	29967540
158	Methylation	GYYDAYLKRCLQHQE CHHHHHHHHHHHCCC	28.52	6568017
197	Phosphorylation	MKVDEVLYEDSSTA- CCCCEEEECCCCCC-	23.90	-

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 MTHFS_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MTHFS_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 MTHFS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
T22D4_HUMAN	TSC22D4	physical	16189514
PLCL2_HUMAN	PLCL2	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.

Regulatory Network of MTHFS_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]