A16A1_HUMAN - dbPTM
A16A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID A16A1_HUMAN
UniProt AC Q8IZ83
Protein Name Aldehyde dehydrogenase family 16 member A1
Gene Name ALDH16A1
Organism Homo sapiens (Human).
Sequence Length 802
Subcellular Localization
Protein Description
Protein Sequence MAATRAGPRAREIFTSLEYGPVPESHACALAWLDTQDRCLGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAPLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGPGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARGAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRPSGTPARLSCLSKNLNYDTFGLAVPSTLPAGPEIGPSPAPPYGLFVGGRFQAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQGAELKAAEAEVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPVWASRGCPRAWDQEAEGAGPELGLRVARTKALWLPMGD
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
5Methylation---MAATRAGPRARE
---CCCCCCCHHHHH		32.59-
15PhosphorylationPRAREIFTSLEYGPV
HHHHHHHHCCCCCCC		37.7624719451
16PhosphorylationRAREIFTSLEYGPVP
HHHHHHHCCCCCCCC		14.4128348404
19PhosphorylationEIFTSLEYGPVPESH
HHHHCCCCCCCCHHH		31.8330804103
25PhosphorylationEYGPVPESHACALAW
CCCCCCHHHHEEEHH		15.4346161905
47UbiquitinationLGHYVNGKWLKPEHR
HHHHHCCEECCHHHC		44.12-
50AcetylationYVNGKWLKPEHRNSV
HHCCEECCHHHCCCC		47.4419608861
50UbiquitinationYVNGKWLKPEHRNSV
HHCCEECCHHHCCCC		47.4419608861
62UbiquitinationNSVPCQDPITGENLA
CCCCCCCCCCCCHHH		10.5221890473
85UbiquitinationDVAAAVEAARMAFKG
HHHHHHHHHHHHHCC		8.1827667366
91 (in isoform 2)Ubiquitination-50.3521890473
91UbiquitinationEAARMAFKGWSAHPG
HHHHHHHCCCCCCCC		50.3521890473
91 (in isoform 1)Ubiquitination-50.3521890473
91UbiquitinationEAARMAFKGWSAHPG
HHHHHHHCCCCCCCC		50.3521890473
114AcetylationRLAEVIQKHQRLLWT
HHHHHHHHHHHHHHH		30.4926822725
114UbiquitinationRLAEVIQKHQRLLWT
HHHHHHHHHHHHHHH		30.4933845483
121PhosphorylationKHQRLLWTLESLVTG
HHHHHHHHHHHHHHC		22.1819413330
124PhosphorylationRLLWTLESLVTGRAV
HHHHHHHHHHHCCCH		31.1172550343
127PhosphorylationWTLESLVTGRAVREV
HHHHHHHHCCCHHHH		26.6624719451
216UbiquitinationLLAQLAGELGPFPGI
HHHHHHHHHCCCCCH		44.9722505724
245UbiquitinationASQPGIRKVAFCGAP
HCCCCCCEEEECCCC		35.6729901268
275PhosphorylationELGLALGTESLLLLT
HHHHHHCCCEEEEEE		24.2123401153
277PhosphorylationGLALGTESLLLLTDT
HHHHCCCEEEEEECC		24.9323401153
282PhosphorylationTESLLLLTDTADVDS
CCEEEEEECCCCHHH		31.1323401153
284PhosphorylationSLLLLTDTADVDSAV
EEEEEECCCCHHHHH		21.3723401153
289PhosphorylationTDTADVDSAVEGVVD
ECCCCHHHHHHCHHH		33.7823401153
332PhosphorylationERMGRLRSGRGLDGA
HHHCHHHCCCCCCCC		37.1228270605
342SulfoxidationGLDGAVDMGARGAAA
CCCCCCCCCHHHHHH		3.4830846556
362UbiquitinationRFVREAQSQGAQVFQ
HHHHHHHHCCCEEEE		37.3121890473
362UbiquitinationRFVREAQSQGAQVFQ
HHHHHHHHCCCEEEE		37.3121963094
375PhosphorylationFQAGDVPSERPFYPP
EECCCCCCCCCCCCC		46.1930631047
384UbiquitinationRPFYPPTLVSNLPPA
CCCCCCCHHCCCCCC		4.9821963094
413 (in isoform 1)Ubiquitination-42.7921890473
413UbiquitinationASPFRTAKEALLVAN
ECCCCCHHHHHHEEC		42.7921963094
422PhosphorylationALLVANGTPRGGSAS
HHHEECCCCCCCCHH		15.0426714015
424MethylationLVANGTPRGGSASVW
HEECCCCCCCCHHHH		63.04-
448UbiquitinationLGYGLQVGTVWINAH
HCCCCEEECEEEECC		11.1121963094
468UbiquitinationSVPTGGCKESGCSWH
CCCCCCCCCCCCCCC		59.18-
470UbiquitinationPTGGCKESGCSWHGG
CCCCCCCCCCCCCCC		30.5121963094
482PhosphorylationHGGPDGLYEYLRPSG
CCCCCCHHHHHCCCC		14.2022817900
488O-linked_GlycosylationLYEYLRPSGTPARLS
HHHHHCCCCCCHHHH		49.1929351928
488PhosphorylationLYEYLRPSGTPARLS
HHHHHCCCCCCHHHH		49.1925627689
490PhosphorylationEYLRPSGTPARLSCL
HHHCCCCCCHHHHHH		20.3625627689
499UbiquitinationARLSCLSKNLNYDTF
HHHHHHHCCCCCCCC		53.1321963094
513UbiquitinationFGLAVPSTLPAGPEI
CCEECCCCCCCCCCC		30.5921890473
513UbiquitinationFGLAVPSTLPAGPEI
CCEECCCCCCCCCCC		30.5921890473
535MethylationYGLFVGGRFQAPGAR
CCEEECCEECCCCCC		17.99-
535UbiquitinationYGLFVGGRFQAPGAR
CCEEECCEECCCCCC		17.9921890473
543PhosphorylationFQAPGARSSRPIRDS
ECCCCCCCCCCCCCC		30.1126657352
544PhosphorylationQAPGARSSRPIRDSS
CCCCCCCCCCCCCCC		36.2026657352
550PhosphorylationSSRPIRDSSGNLHGY
CCCCCCCCCCCEEEE		30.2326657352
551PhosphorylationSRPIRDSSGNLHGYV
CCCCCCCCCCEEEEE		35.6728270605
557PhosphorylationSSGNLHGYVAEGGAK
CCCCEEEEEECCCCC		5.9223312004
564UbiquitinationYVAEGGAKDIRGAVE
EEECCCCCCHHHHHH		57.8921963094
564 (in isoform 1)Ubiquitination-57.8921890473
567MethylationEGGAKDIRGAVEAAH
CCCCCCHHHHHHHHH		36.83-
567UbiquitinationEGGAKDIRGAVEAAH
CCCCCCHHHHHHHHH		36.8322817900
584PhosphorylationFPGWAGQSPGARAAL
CCCCCCCCHHHHHHH		25.12110754377
589UbiquitinationGQSPGARAALLWALA
CCCHHHHHHHHHHHH		11.2622817900
618AcetylationERQGAELKAAEAEVE
HHCCCHHHHHHHHHH		36.7420167786
618 (in isoform 1)Ubiquitination-36.7421890473
618UbiquitinationERQGAELKAAEAEVE
HHCCCHHHHHHHHHH		36.7422817900
743UbiquitinationHQDVQAMWYFGSAQG
CHHHHHHHHHCCCCC		6.5822505724
751O-linked_GlycosylationYFGSAQGSQFVEWAS
HHCCCCCHHHHHHHH		14.36OGP
765UbiquitinationSAGNLKPVWASRGCP
HCCCCCCEEHHCCCC		6.7922505724
794UbiquitinationGLRVARTKALWLPMG
HHHHEEEEEEEEECC		35.6122505724
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 A16A1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of A16A1_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 A16A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DEOC_HUMANDERAphysical
22863883
FUBP2_HUMANKHSRPphysical
22863883
MEA1_HUMANMEA1physical
22863883
PURB_HUMANPURBphysical
22863883
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 A16A1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-50, AND MASS SPECTROMETRY.

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