AL1L2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AL1L2_HUMAN
• UniProt AC: Q3SY69
• Protein Name: Mitochondrial 10-formyltetrahydrofolate dehydrogenase
• Gene Name: ALDH1L2
• Organism: Homo sapiens (Human).
• Sequence Length: 923
• Subcellular Localization: Mitochondrion .
• Protein Sequence: MLRRGSQALRRFSTGRVYFKNKLKLALIGQSLFGQEVYSHLRKEGHRVVGVFTVPDKDGKADPLALAAEKDGTPVFKLPKWRVKGKTIKEVAEAYRSVGAELNVLPFCTQFIPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVDALYNRFLFPEGIKAMVEAVQLIADGKAPRIPQPEEGATYEGIQKKENAEISWDQSAEVLHNWIRGHDKVPGAWTEINGQMVTFYGSTLLNSSVPPGEPLEIKGAKKPGLVTKNGLVLFGNDGKALTVRNLQFEDGKMIPASQYFSTGETSVVELTAEEVKVAETIKVIWAGILSNVPIIEDSTDFFKSGASSMDVARLVEEIRQKCGGLQLQNEDVYMATKFEGFIQKVVRKLRGEDQEVELVVDYISKEVNEIMVKMPYQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQNGDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTLEY

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
31	Phosphorylation	KLALIGQSLFGQEVY HHHHEEHHHHCHHHH	22.06	-
57	Acetylation	GVFTVPDKDGKADPL EEEEECCCCCCCCHH	63.41	66702447
57	Malonylation	GVFTVPDKDGKADPL EEEEECCCCCCCCHH	63.41	26320211
60	Succinylation	TVPDKDGKADPLALA EECCCCCCCCHHHHH	60.80	-
60	Acetylation	TVPDKDGKADPLALA EECCCCCCCCHHHHH	60.80	26051181
60	Malonylation	TVPDKDGKADPLALA EECCCCCCCCHHHHH	60.80	26320211
70	Malonylation	PLALAAEKDGTPVFK HHHHHCCCCCCCCCC	57.65	26320211
70	Acetylation	PLALAAEKDGTPVFK HHHHHCCCCCCCCCC	57.65	23236377
77	Acetylation	KDGTPVFKLPKWRVK CCCCCCCCCCCCEEC	65.20	19822193
89	Ubiquitination	RVKGKTIKEVAEAYR EECCCCHHHHHHHHH	51.90	-
89	Malonylation	RVKGKTIKEVAEAYR EECCCCHHHHHHHHH	51.90	26320211
109	Phosphorylation	LNVLPFCTQFIPMDI HCCCCCCCCCCCCCC	27.22	46161977
124	Phosphorylation	IDSPKHGSIIYHPSI CCCCCCCCEEECCCC	12.92	69003655
127	Phosphorylation	PKHGSIIYHPSILPR CCCCCEEECCCCCCC	13.15	69004527
209	Malonylation	VQLIADGKAPRIPQP HHHHHCCCCCCCCCC	56.62	26320211
222	Phosphorylation	QPEEGATYEGIQKKE CCCCCCCCCCCCHHH	16.18	-
227	Acetylation	ATYEGIQKKENAEIS CCCCCCCHHHCCCCC	61.20	23236377
270	Phosphorylation	MVTFYGSTLLNSSVP EEEEECCEECCCCCC	30.79	46161983
295	Malonylation	KKPGLVTKNGLVLFG CCCCEEECCCEEEEC	41.35	26320211
338	Phosphorylation	ETSVVELTAEEVKVA CCEEEEEEHHHHHHH	20.65	46161989
371	Phosphorylation	DSTDFFKSGASSMDV CCCHHHHCCCCHHHH	34.14	24670416
375	O-(pantetheine 4'-phosphoryl)serine	FFKSGASSMDVARLV HHHCCCCHHHHHHHH	20.61	-
375	Phosphorylation	FFKSGASSMDVARLV HHHCCCCHHHHHHHH	20.61	24670416
411	Malonylation	KFEGFIQKVVRKLRG HHHHHHHHHHHHHCC	37.57	26320211
484	Malonylation	ASLADVDKAVAAAKD CCHHHHHHHHHHHHH	44.61	26320211
490	Malonylation	DKAVAAAKDAFENGE HHHHHHHHHHHHCCC	44.88	26320211
550	Phosphorylation	HIGMSVQTFRYFAGW CCCCCHHHHHHHHHH	14.13	46161995
560	Malonylation	YFAGWCDKIQGSTIP HHHHHHHHCCCCEEC	33.52	26320211
623	Phosphorylation	VLKPAQVTPLTALKF EECCCCCCHHHHHHH	10.66	22210691
626	Phosphorylation	PAQVTPLTALKFAEL CCCCCHHHHHHHHHH	31.02	22210691
636	Malonylation	KFAELSVKAGFPKGV HHHHHHHHCCCCCCC	39.14	26320211
650	Phosphorylation	VINIIPGSGGIAGQR CEEECCCCCCCCCCC	28.61	-
670	Phosphorylation	DIRKLGFTGSTPIGK CHHHCCCCCCCHHHH	28.55	46162001
681	Succinylation	PIGKQIMKSCAVSNL HHHHHHHHHHHHCCC	43.97	-
681	Malonylation	PIGKQIMKSCAVSNL HHHHHHHHHHHHCCC	43.97	26320211
681	Succinylation	PIGKQIMKSCAVSNL HHHHHHHHHHHHCCC	43.97	-
754	Acetylation	RVVEEIKKMKIGDPL HHHHHHHHCCCCCCC	51.60	30586859
756	Malonylation	VEEIKKMKIGDPLDR HHHHHHCCCCCCCCC	53.03	26320211
765	Phosphorylation	GDPLDRSTDHGPQNH CCCCCCCCCCCCHHH	32.67	29460479
778	Malonylation	NHKAHLEKLLQYCET HHHHHHHHHHHHHHH	61.94	26320211
788	Succinylation	QYCETGVKEGATLVY HHHHHCCCCCCEEEE	52.34	-
788	Malonylation	QYCETGVKEGATLVY HHHHHCCCCCCEEEE	52.34	26320211
886	Malonylation	VFINTYNKTDVAAPF EEEEECCCCCCCCCC	35.37	26320211
886	Acetylation	VFINTYNKTDVAAPF EEEEECCCCCCCCCC	35.37	19608861
897	Malonylation	AAPFGGVKQSGFGKD CCCCCCCCCCCCCCC	41.86	26320211
903	Malonylation	VKQSGFGKDLGEEAL CCCCCCCCCCCHHHH	47.74	26320211
903	Acetylation	VKQSGFGKDLGEEAL CCCCCCCCCCCHHHH	47.74	19608861

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

Oops, there are no upstream regulatory protein records of AL1L2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AL1L2_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 AL1L2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYCB2_HUMAN	MYCBP2	physical	26186194
TTC5_HUMAN	TTC5	physical	26186194
TBA1A_HUMAN	TUBA1A	physical	26186194
SGT1_HUMAN	SUGT1	physical	26186194
WDR11_HUMAN	WDR11	physical	26186194
DPOLA_HUMAN	POLA1	physical	26186194
INT14_HUMAN	VWA9	physical	26186194
SGT1_HUMAN	SUGT1	physical	28514442
WDR11_HUMAN	WDR11	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-903, AND MASS SPECTROMETRY.
PubMed: 19608861