C1TM_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: C1TM_MOUSE
• UniProt AC: Q3V3R1
• Protein Name: Monofunctional C1-tetrahydrofolate synthase, mitochondrial
• Gene Name: Mthfd1l
• Organism: Mus musculus (Mouse).
• Sequence Length: 977
• Subcellular Localization: Mitochondrion.
• Protein Description: May provide the missing metabolic reaction required to link the mitochondria and the cytoplasm in the mammalian model of one-carbon folate metabolism in embryonic an transformed cells complementing thus the enzymatic activities of MTHFD2..
• Protein Sequence: MSVRLPLLLRQLGRQQLPSGPACRLRELCRSGSRSSSSGGGDPEGLRGRRLQDGQTFSSHGPGNPEAPGMDSIVRDVIHNSKEVLSLLQEKNPAFKPVLVVIQAGDDNLMKDMNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLTLQISEDSLSNKVLNALKPEKDVDGVTDINLGKLVRGDAPECFVSPLAKAAVELVEKSGITLDGKKVLVVGAHGPLEAALQWLFQRKGSMTMSCPWATPQLPDKLREADIVVLGSPKPEEIPAVWIPSGTTILNCFHDFLSGKLSGGSPGVPVDKLIAEESVSLLAAALRIQNMVSSGRRWLREQQHRRWRLHCLKLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVQLSLLERLKDQTDGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLKVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHESTQTDKALYNRLVPLVNGVREFSEIQLSRLKKLGIHKTDPSTLTEEEVRKFARLNIDPATITWQRVLDTNDRFLRKITIGQGSTEKGYSRQAQFDIAVASEIMAVLALTDSLTDMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYHWSAGGKGSVDLARAVREAANKRSRFQFLYDVQLPIVEKIRVIAQTVYGAKDIELSPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHEPDKKGVPRDFTLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVKGLF

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
129	Glutathionylation	GLDITHICLPPDSGE CCCCEEEECCCCCCC	3.47	24333276
160	Phosphorylation	HGLTLQISEDSLSNK CCEEEEECCHHHCHH	23.53	26824392
188	Succinylation	VTDINLGKLVRGDAP CEECCCCHHHCCCCC	47.15	-
188	Acetylation	VTDINLGKLVRGDAP CEECCCCHHHCCCCC	47.15	23806337
188	Succinylation	VTDINLGKLVRGDAP CEECCCCHHHCCCCC	47.15	23806337
220	Acetylation	SGITLDGKKVLVVGA HCCEECCEEEEEEEC	39.10	19847613
249	S-palmitoylation	KGSMTMSCPWATPQL CCCCEEECCCCCCCC	1.96	28680068
300	Phosphorylation	DFLSGKLSGGSPGVP HHHCCCCCCCCCCCC	44.59	26745281
303	Phosphorylation	SGKLSGGSPGVPVDK CCCCCCCCCCCCHHH	23.23	26745281
351	Acetylation	RWRLHCLKLQPLSPV HHHHEEEECEECCCC	50.93	23806337
356	Phosphorylation	CLKLQPLSPVPSDIE EEECEECCCCCCCCE	30.45	24453211
360	Phosphorylation	QPLSPVPSDIEISRG EECCCCCCCCEECCC	51.99	23984901
365	Phosphorylation	VPSDIEISRGQTPKA CCCCCEECCCCCHHH	19.98	23984901
369	Phosphorylation	IEISRGQTPKAVDVL CEECCCCCHHHHHHH	29.58	23984901
585	Acetylation	TNDRFLRKITIGQGS CCCCCEEEEEECCCC	46.47	23806337
585	Succinylation	TNDRFLRKITIGQGS CCCCCEEEEEECCCC	46.47	23806337
592	Phosphorylation	KITIGQGSTEKGYSR EEEECCCCCCCCCCC	26.04	29514104
595	Acetylation	IGQGSTEKGYSRQAQ ECCCCCCCCCCCHHH	64.34	23806337
595	Succinylation	IGQGSTEKGYSRQAQ ECCCCCCCCCCCHHH	64.34	-
595	Succinylation	IGQGSTEKGYSRQAQ ECCCCCCCCCCCHHH	64.34	23806337
726	Ubiquitination	MEKFFNIKCRASGLV CHHCCCCCCCCCCCC	20.83	-
754	Phosphorylation	KMHGGGPSVTAGVPL HHCCCCCCCCCCCCC	35.06	25619855
756	Phosphorylation	HGGGPSVTAGVPLKK CCCCCCCCCCCCCCC	23.25	25619855
805	Phosphorylation	LNVFKTDTRAEIDLV EEECCCCCHHHHHHH	36.69	-
813	Glutathionylation	RAEIDLVCELAKRAG HHHHHHHHHHHHHCC	4.63	24333276
852	Phosphorylation	REAANKRSRFQFLYD HHHHHHCCCCCHHHC	38.77	22802335

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

Oops, there are no upstream regulatory protein records of C1TM_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of C1TM_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of C1TM_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of C1TM_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.