AL1B1_HUMAN - dbPTM
AL1B1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AL1B1_HUMAN
UniProt AC P30837
Protein Name Aldehyde dehydrogenase X, mitochondrial
Gene Name ALDH1B1
Organism Homo sapiens (Human).
Sequence Length 517
Subcellular Localization Mitochondrion matrix.
Protein Description ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation..
Protein Sequence MLRFLAPRLLSLQGRTARYSSAAALPSPILNPDIPYNQLFINNEWQDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDRAVKAAREAFRLGSPWRRMDASERGRLLNLLADLVERDRVYLASLETLDNGKPFQESYALDLDEVIKVYRYFAGWADKWHGKTIPMDGQHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHVDVDKVAFTGSTEVGHLIQKAAGDSNLKRVTLELGGKSPSIVLADADMEHAVEQCHEALFFNMGQCCCAGSRTFVEESIYNEFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERVLGYIQLGQKEGAKLLCGGERFGERGFFIKPTVFGGVQDDMRIAKEEIFGPVQPLFKFKKIEEVVERANNTRYGLAAAVFTRDLDKAMYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLKAYTEVKTVTIKVPQKNS
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
11PhosphorylationFLAPRLLSLQGRTAR
CHHHHHHHCCCCCCC
24.2050564579
21PhosphorylationGRTARYSSAAALPSP
CCCCCCCCCCCCCCC
17.0046161947
27PhosphorylationSSAAALPSPILNPDI
CCCCCCCCCCCCCCC
25.9846161953
51AcetylationEWQDAVSKKTFPTVN
CHHHHHHCCCCCCCC
49.59-
52AcetylationWQDAVSKKTFPTVNP
HHHHHHCCCCCCCCC
48.14-
52UbiquitinationWQDAVSKKTFPTVNP
HHHHHHCCCCCCCCC
48.14-
52SuccinylationWQDAVSKKTFPTVNP
HHHHHHCCCCCCCCC
48.14-
52SuccinylationWQDAVSKKTFPTVNP
HHHHHHCCCCCCCCC
48.14-
52MalonylationWQDAVSKKTFPTVNP
HHHHHHCCCCCCCCC
48.1426320211
73MethylationGHVAEGDRADVDRAV
EECCCCCHHHHHHHH
43.47-
81SuccinylationADVDRAVKAAREAFR
HHHHHHHHHHHHHHH
35.03-
81SuccinylationADVDRAVKAAREAFR
HHHHHHHHHHHHHHH
35.03-
135PhosphorylationGKPFQESYALDLDEV
CCCCCCEECCCHHHH
15.4971731
155AcetylationYFAGWADKWHGKTIP
HHHCCCHHHCCEEEC
33.0923236377
202PhosphorylationKLAPALATGNTVVMK
EEEHHHHCCCEEEEE
31.6421406692
205PhosphorylationPALATGNTVVMKVAE
HHHHCCCEEEEEEHH
18.8021406692
214PhosphorylationVMKVAEQTPLSALYL
EEEEHHCCCHHHHHH
20.0826503514
217PhosphorylationVAEQTPLSALYLASL
EHHCCCHHHHHHHHH
19.89110743611
220PhosphorylationQTPLSALYLASLIKE
CCCHHHHHHHHHHHH
10.4326503514
223PhosphorylationLSALYLASLIKEAGF
HHHHHHHHHHHHHCC
28.2124719451
263PhosphorylationDKVAFTGSTEVGHLI
CEEEEECCHHHHHHH
20.5225690035
264PhosphorylationKVAFTGSTEVGHLIQ
EEEEECCHHHHHHHH
35.7125690035
272MalonylationEVGHLIQKAAGDSNL
HHHHHHHHHHCCCCC
32.9626320211
283PhosphorylationDSNLKRVTLELGGKS
CCCCCEEEEECCCCC
20.6720166139
330PhosphorylationSRTFVEESIYNEFLE
CCHHCHHHHHHHHHH
19.50110743619
332PhosphorylationTFVEESIYNEFLERT
HHCHHHHHHHHHHHH
20.23110743627
347UbiquitinationVEKAKQRKVGNPFEL
HHHHHHCCCCCCCCC
52.58-
364SuccinylationQQGPQVDKEQFERVL
CCCCCCCHHHHHHHH
55.34-
364SuccinylationQQGPQVDKEQFERVL
CCCCCCCHHHHHHHH
55.34-
364UbiquitinationQQGPQVDKEQFERVL
CCCCCCCHHHHHHHH
55.34-
364AcetylationQQGPQVDKEQFERVL
CCCCCCCHHHHHHHH
55.3423236377
373PhosphorylationQFERVLGYIQLGQKE
HHHHHHHHHHCCCCC
4.9428152594
379AcetylationGYIQLGQKEGAKLLC
HHHHCCCCCCCEEEE
57.2123236377
379MalonylationGYIQLGQKEGAKLLC
HHHHCCCCCCCEEEE
57.2126320211
383SuccinylationLGQKEGAKLLCGGER
CCCCCCCEEEECCCC
53.50-
383UbiquitinationLGQKEGAKLLCGGER
CCCCCCCEEEECCCC
53.50-
383AcetylationLGQKEGAKLLCGGER
CCCCCCCEEEECCCC
53.50-
383SuccinylationLGQKEGAKLLCGGER
CCCCCCCEEEECCCC
53.50-
383MalonylationLGQKEGAKLLCGGER
CCCCCCCEEEECCCC
53.5026320211
399AcetylationGERGFFIKPTVFGGV
CCCCCEECCEEECCC
29.4923236377
399SuccinylationGERGFFIKPTVFGGV
CCCCCEECCEEECCC
29.49-
399UbiquitinationGERGFFIKPTVFGGV
CCCCCEECCEEECCC
29.49-
399SuccinylationGERGFFIKPTVFGGV
CCCCCEECCEEECCC
29.4923954790
401PhosphorylationRGFFIKPTVFGGVQD
CCCEECCEEECCCCC
24.3846161959
414AcetylationQDDMRIAKEEIFGPV
CCCCHHHHHHHHCCC
54.21-
414UbiquitinationQDDMRIAKEEIFGPV
CCCCHHHHHHHHCCC
54.21-
414SuccinylationQDDMRIAKEEIFGPV
CCCCHHHHHHHHCCC
54.21-
414SuccinylationQDDMRIAKEEIFGPV
CCCCHHHHHHHHCCC
54.21-
426AcetylationGPVQPLFKFKKIEEV
CCCHHCCCCCCHHHH
65.0523236377
426UbiquitinationGPVQPLFKFKKIEEV
CCCHHCCCCCCHHHH
65.0521890473
426SuccinylationGPVQPLFKFKKIEEV
CCCHHCCCCCCHHHH
65.0523954790
426SuccinylationGPVQPLFKFKKIEEV
CCCHHCCCCCCHHHH
65.05-
429SuccinylationQPLFKFKKIEEVVER
HHCCCCCCHHHHHHH
59.4927452117
429AcetylationQPLFKFKKIEEVVER
HHCCCCCCHHHHHHH
59.4921339330
442PhosphorylationERANNTRYGLAAAVF
HHHHCCCCEEEEEHC
17.9128152594
500SuccinylationELGEDGLKAYTEVKT
EECCCHHHHEEEEEE
44.8923954790
500UbiquitinationELGEDGLKAYTEVKT
EECCCHHHHEEEEEE
44.89-

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 AL1B1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AL1B1_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 AL1B1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
QCR7_HUMANUQCRBphysical
22939629
FABPI_HUMANFABP2physical
21988832
FUMH_HUMANFHphysical
22863883
HEXB_HUMANHEXBphysical
22863883
PDC10_HUMANPDCD10physical
22863883
FEM1B_HUMANFEM1Bphysical
26186194
SUFU_HUMANSUFUphysical
26186194
DHRS4_HUMANDHRS4physical
26186194
ESTD_HUMANESDphysical
26344197
PDC6I_HUMANPDCD6IPphysical
26344197
PGM1_HUMANPGM1physical
26344197
SRP68_HUMANSRP68physical
26344197
STIP1_HUMANSTIP1physical
26344197
QCR2_HUMANUQCRC2physical
26344197
XPP1_HUMANXPNPEP1physical
26344197
FEM1B_HUMANFEM1Bphysical
28514442
DHRS4_HUMANDHRS4physical
28514442
SUFU_HUMANSUFUphysical
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 AL1B1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP