AL1L1_HUMAN - dbPTM
AL1L1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AL1L1_HUMAN
UniProt AC O75891
Protein Name Cytosolic 10-formyltetrahydrofolate dehydrogenase
Gene Name ALDH1L1
Organism Homo sapiens (Human).
Sequence Length 902
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGDALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLEDGKMILASNFFKGAASSVLELTEAELVTAEAVRSVWQRILPKVLEVEDSTDFFKSGAASVDVVRLVEEVKELCDGLELENEDVYMASTFGDFIQLLVRKLRGDDEEGECSIDYVEMAVNKRTVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTFEY
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 Orthologous
Protein Cluster
5 (in isoform 3)Phosphorylation-6.0221955146
9PhosphorylationKIAVIGQSLFGQEVY
EEEEEECHHHCCEEE		22.0624275569
10 (in isoform 3)Phosphorylation-4.2621955146
35AcetylationGVFTVPDKDGKADPL
EEEEEECCCCCCCCC		63.4123236377
35SuccinylationGVFTVPDKDGKADPL
EEEEEECCCCCCCCC		63.4123954790
35MalonylationGVFTVPDKDGKADPL
EEEEEECCCCCCCCC		63.4126320211
38SuccinylationTVPDKDGKADPLGLE
EEECCCCCCCCCCCC		60.80-
38SuccinylationTVPDKDGKADPLGLE
EEECCCCCCCCCCCC		60.80-
57PhosphorylationGVPVFKYSRWRAKGQ
CCEEEEEHHHCCCCC		26.4263651425
105PhosphorylationPRHGSIIYHPSLLPR
CCCCCEEECCCCCCC		13.1546161971
112MethylationYHPSLLPRHRGASAI
ECCCCCCCCCCCCEE		31.91-
187MethylationVRLIAEGKAPRLPQP
HHHHHCCCCCCCCCC		46.88-
200PhosphorylationQPEEGATYEGIQKKE
CCCCCCCCCCCCCCE		16.1830815049
205MalonylationATYEGIQKKETAKIN
CCCCCCCCCEEECCC		51.1326320211
344PhosphorylationKVLEVEDSTDFFKSG
HHCEEECCCCHHHHC		19.1728857561
345PhosphorylationVLEVEDSTDFFKSGA
HCEEECCCCHHHHCC		49.5028857561
350PhosphorylationDSTDFFKSGAASVDV
CCCCHHHHCCCCHHH		28.6226437602
354O-(pantetheine 4'-phosphoryl)serineFFKSGAASVDVVRLV
HHHHCCCCHHHHHHH		20.51-
354PhosphorylationFFKSGAASVDVVRLV
HHHHCCCCHHHHHHH		20.5128258704
405PhosphorylationDDEEGECSIDYVEMA
CCCCCCEECEEEEEC		17.7546161965
408PhosphorylationEGECSIDYVEMAVNK
CCCEECEEEEECCCC		9.1769006549
507AcetylationQEELATIEALDAGAV
HHHHHHHHHHHHCHH		38.5319413330
539MalonylationYFAGWCDKIQGSTIP
HHHHHHHHCCCCEEC		33.5226320211
602PhosphorylationVIKPAQVTPLTALKF
EECCCCCCCHHHHHH		10.6622210691
605PhosphorylationPAQVTPLTALKFAEL
CCCCCCHHHHHHHHH		31.0222210691
608AcetylationVTPLTALKFAELTLK
CCCHHHHHHHHHHHH		39.8119413330
613PhosphorylationALKFAELTLKAGIPK
HHHHHHHHHHCCCCC		20.0972550353
618AcetylationELTLKAGIPKGVVNV
HHHHHCCCCCCCEEE		3.6819413330
629PhosphorylationVVNVLPGSGSLVGQR
CEEECCCCCCCCCCC		24.2225307156
631PhosphorylationNVLPGSGSLVGQRLS
EECCCCCCCCCCCCC		22.9128258704
641PhosphorylationGQRLSDHPDVRKIGF
CCCCCCCCCCCCCCE		46.9427251275
651PhosphorylationRKIGFTGSTEVGKHI
CCCCEECCHHHHHHH		20.5224275569
660AcetylationEVGKHIMKSCAISNV
HHHHHHHHHHHCCCC		41.60160755
660SuccinylationEVGKHIMKSCAISNV
HHHHHHHHHHHCCCC		41.60-
662S-nitrosylationGKHIMKSCAISNVKK
HHHHHHHHHCCCCEE		3.0424105792
665PhosphorylationIMKSCAISNVKKVSL
HHHHHHCCCCEEEEE		19.6224076635
668AcetylationSCAISNVKKVSLELG
HHHCCCCEEEEEECC		52.2724888333
767SuccinylationEYCQHGVKEGATLVC
HHHHCCCCCCCEEEE		55.83-
767SuccinylationEYCQHGVKEGATLVC
HHHHCCCCCCCEEEE		55.83-
825PhosphorylationGDLDAVLSRANATEF
CCHHHHHHHCCCCHH		23.8124275569
830PhosphorylationVLSRANATEFGLASG
HHHHCCCCHHCCCCC		31.4922985185
836PhosphorylationATEFGLASGVFTRDI
CCHHCCCCCCEECCH		40.3022985185
840PhosphorylationGLASGVFTRDINKAL
CCCCCCEECCHHHHH		25.6522985185
848PhosphorylationRDINKALYVSDKLQA
CCHHHHHEECCCCCC		11.6369004561
876AcetylationAAPFGGFKQSGFGKD
CCCCCCCCCCCCCCC		46.9920167786
882AcetylationFKQSGFGKDLGEAAL
CCCCCCCCCHHHHHH		47.7420167786
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 AL1L1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AL1L1_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 AL1L1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AL1L2_HUMANALDH1L2physical
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
DB00116Tetrahydrofolic acid
Regulatory Network of AL1L1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-613, AND MASSSPECTROMETRY.

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