AL3B1_HUMAN - dbPTM
AL3B1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AL3B1_HUMAN
UniProt AC P43353
Protein Name Aldehyde dehydrogenase family 3 member B1
Gene Name ALDH3B1
Organism Homo sapiens (Human).
Sequence Length 468
Subcellular Localization Cell membrane
Lipid-anchor . Primarily in the plasma membrane as well as in some punctate structures in the cytoplasm.
Protein Description Oxidizes medium and long chain saturated and unsaturated aldehydes. Metabolizes also benzaldehyde. Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde. May not metabolize short chain aldehydes. May use both NADP(+) and NAD(+) as cofactors. May have a protective role against the cytotoxicity induced by lipid peroxidation..
Protein Sequence MDPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRACLLRSPGMEKLNALRYPPQSPRRLRMLLVAMEAQGCSCTLL
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
1Acetylation-------MDPLGDTL
-------CCCHHHHH		12.3522814378
41UbiquitinationGRFLQENKQLLHDAL
HHHHHHHHHHHHHHH		41.3821890473
41 (in isoform 1)Ubiquitination-41.3821890473
41UbiquitinationGRFLQENKQLLHDAL
HHHHHHHHHHHHHHH		41.3821890473
41 (in isoform 2)Ubiquitination-41.3821890473
89UbiquitinationMKDERVPKNLATQLD
HCCCCCCCCHHHHHH		62.8321890473
89 (in isoform 1)Ubiquitination-62.8321890473
89UbiquitinationMKDERVPKNLATQLD
HCCCCCCCCHHHHHH		62.8321890473
93PhosphorylationRVPKNLATQLDSAFI
CCCCCHHHHHHHHHH		32.6030631047
97PhosphorylationNLATQLDSAFIRKEP
CHHHHHHHHHHCCCC		33.4030631047
183PhosphorylationLLEHRFDYIFFTGSP
HHHEECCEEEEECCC		9.2768707961
187PhosphorylationRFDYIFFTGSPRVGK
ECCEEEEECCCCHHH		26.4668707967
189PhosphorylationDYIFFTGSPRVGKIV
CEEEEECCCCHHHHH		13.3868707973
202UbiquitinationIVMTAAAKHLTPVTL
HHHHHHHHHCCCEEE		34.13-
205PhosphorylationTAAAKHLTPVTLELG
HHHHHHCCCEEEEEC		18.5546162035
208PhosphorylationAKHLTPVTLELGGKN
HHHCCCEEEEECCCC		18.73-
214UbiquitinationVTLELGGKNPCYVDD
EEEEECCCCCEECCC		56.79-
252 (in isoform 2)Ubiquitination-4.5621890473
279PhosphorylationYGDDPQSSPNLGRII
HCCCCCCCCCHHHHC		16.7421815630
289 (in isoform 1)Ubiquitination-48.9021890473
289UbiquitinationLGRIINQKQFQRLRA
HHHHCCHHHHHHHHH		48.90-
323 (in isoform 2)Ubiquitination-32.0221890473
338 (in isoform 2)Ubiquitination-17.7521890473
360UbiquitinationEFINRREKPLALYAF
HHHHHCCCCEEEEEE		43.4521906983
360 (in isoform 1)Ubiquitination-43.4521890473
368PhosphorylationPLALYAFSNSSQVVK
CEEEEEECCCHHHHH		27.8618187866
375UbiquitinationSNSSQVVKRVLTQTS
CCCHHHHHHHHHCCC		37.6221890473
375UbiquitinationSNSSQVVKRVLTQTS
CCCHHHHHHHHHCCC		37.6221890473
375 (in isoform 1)Ubiquitination-37.6221890473
400 (in isoform 2)Ubiquitination-3.2021890473
432PhosphorylationHRACLLRSPGMEKLN
CCCHHHCCCCHHHHH		26.2730576142
437UbiquitinationLRSPGMEKLNALRYP
HCCCCHHHHHHCCCC		37.8421890473
437 (in isoform 1)Ubiquitination-37.8421890473
437UbiquitinationLRSPGMEKLNALRYP
HCCCCHHHHHHCCCC		37.8421890473
443PhosphorylationEKLNALRYPPQSPRR
HHHHHCCCCCCCHHH		21.8030576142
447PhosphorylationALRYPPQSPRRLRML
HCCCCCCCHHHHHHH		26.5830576142
463S-palmitoylationVAMEAQGCSCTLL--
HHHHHCCCCEEEC--		1.6923721920
464PhosphorylationAMEAQGCSCTLL---
HHHHCCCCEEEC---		19.5750564585
465GeranylgeranylationMEAQGCSCTLL----
HHHCCCCEEEC----		3.4623721920
465MethylationMEAQGCSCTLL----
HHHCCCCEEEC----		3.46-
465GeranylgeranylationMEAQGCSCTLL----
HHHCCCCEEEC----		3.4623721920
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 AL3B1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AL3B1_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 AL3B1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K1H1_HUMANKRT31physical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
K1C40_HUMANKRT40physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
WDR73_HUMANWDR73physical
26186194
TRI65_HUMANTRIM65physical
26186194
TAF9_HUMANTAF9physical
26186194
HS71L_HUMANHSPA1Lphysical
26186194
OBSL1_HUMANOBSL1physical
26186194
TBB1_HUMANTUBB1physical
26186194
RN123_HUMANRNF123physical
26186194
LACRT_HUMANLACRTphysical
26186194
APOL2_HUMANAPOL2physical
26186194
LIRA3_HUMANLILRA3physical
26186194
BAG5_HUMANBAG5physical
26186194
T22D3_HUMANTSC22D3physical
26186194
CHIT1_HUMANCHIT1physical
28514442
FMN2_HUMANFMN2physical
28514442
WDR73_HUMANWDR73physical
28514442
SELT_HUMANSELTphysical
28514442
UBA6_HUMANUBA6physical
28514442
IREB2_HUMANIREB2physical
28514442
NU155_HUMANNUP155physical
28514442
SYTC2_HUMANTARSL2physical
28514442
OBSL1_HUMANOBSL1physical
28514442
P55G_HUMANPIK3R3physical
28514442
DMWD_HUMANDMWDphysical
28514442
UBP32_HUMANUSP32physical
28514442
PPM1A_HUMANPPM1Aphysical
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 AL3B1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND MASSSPECTROMETRY.

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