AK1BA_HUMAN - dbPTM
AK1BA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AK1BA_HUMAN
UniProt AC O60218
Protein Name Aldo-keto reductase family 1 member B10
Gene Name AKR1B10
Organism Homo sapiens (Human).
Sequence Length 316
Subcellular Localization Lysosome . Secreted . Secreted through a lysosome-mediated non-classical pathway.
Protein Description Acts as all-trans-retinaldehyde reductase. Can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). May be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs..
Protein Sequence MATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWRACNVLQSSHLEDYPFNAEY
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
8PhosphorylationMATFVELSTKAKMPI
CCCEEECCCCCCCCE		17.8522617229
9PhosphorylationATFVELSTKAKMPIV
CCEEECCCCCCCCEE		47.8728857561
10UbiquitinationTFVELSTKAKMPIVG
CEEECCCCCCCCEEE		42.5133845483
12UbiquitinationVELSTKAKMPIVGLG
EECCCCCCCCEEEEE		46.9233845483
20PhosphorylationMPIVGLGTWKSPLGK
CCEEEEECCCCCCHH		34.4626657352
22UbiquitinationIVGLGTWKSPLGKVK
EEEEECCCCCCHHHH		41.8733845483
23PhosphorylationVGLGTWKSPLGKVKE
EEEECCCCCCHHHHH		19.5422617229
27UbiquitinationTWKSPLGKVKEAVKV
CCCCCCHHHHHHHHH		58.7933845483
27AcetylationTWKSPLGKVKEAVKV
CCCCCCHHHHHHHHH		58.7919608861
33UbiquitinationGKVKEAVKVAIDAGY
HHHHHHHHHHHHCCC		32.7533845483
40PhosphorylationKVAIDAGYRHIDCAY
HHHHHCCCCEEEEEE		10.7611906237
47PhosphorylationYRHIDCAYVYQNEHE
CCEEEEEEEECCHHH		13.1626356563
49PhosphorylationHIDCAYVYQNEHEVG
EEEEEEEECCHHHHH		7.9226356563
62UbiquitinationVGEAIQEKIQEKAVK
HHHHHHHHHHHHCCC		33.0633845483
66UbiquitinationIQEKIQEKAVKREDL
HHHHHHHHCCCHHHH		41.9533845483
69AcetylationKIQEKAVKREDLFIV
HHHHHCCCHHHHEEE		55.7319608861
70MethylationIQEKAVKREDLFIVS
HHHHCCCHHHHEEEE		35.74-
78UbiquitinationEDLFIVSKLWPTFFE
HHHEEEECCHHHHHH		43.6133845483
95UbiquitinationLVRKAFEKTLKDLKL
HHHHHHHHHHHHHCH		53.3433845483
95AcetylationLVRKAFEKTLKDLKL
HHHHHHHHHHHHHCH		53.3419608861
101UbiquitinationEKTLKDLKLSYLDVY
HHHHHHHCHHHEEEE		45.5833845483
103PhosphorylationTLKDLKLSYLDVYLI
HHHHHCHHHEEEEEE		23.2828857561
117UbiquitinationIHWPQGFKSGDDLFP
ECCCCCCCCCCCCCC		61.4233845483
118PhosphorylationHWPQGFKSGDDLFPK
CCCCCCCCCCCCCCC		45.2326657352
125AcetylationSGDDLFPKDDKGNAI
CCCCCCCCCCCCCCC		71.8319608861
125UbiquitinationSGDDLFPKDDKGNAI
CCCCCCCCCCCCCCC		71.8333845483
128UbiquitinationDLFPKDDKGNAIGGK
CCCCCCCCCCCCCCC		65.2933845483
135UbiquitinationKGNAIGGKATFLDAW
CCCCCCCCHHHHHHH		38.7533845483
137PhosphorylationNAIGGKATFLDAWEA
CCCCCCHHHHHHHHH		28.37120161391
156UbiquitinationVDEGLVKALGVSNFS
HHHHHHHHHCCCCCC		11.3222817900
163PhosphorylationALGVSNFSHFQIEKL
HHCCCCCCHHHHHHH		27.8728857561
169UbiquitinationFSHFQIEKLLNKPGL
CCHHHHHHHHCCCCC		60.9633845483
173UbiquitinationQIEKLLNKPGLKYKP
HHHHHHCCCCCCCCC		40.1933845483
177UbiquitinationLLNKPGLKYKPVTNQ
HHCCCCCCCCCCCCC		58.08-
179AcetylationNKPGLKYKPVTNQVE
CCCCCCCCCCCCCEE		31.2719608861
179UbiquitinationNKPGLKYKPVTNQVE
CCCCCCCCCCCCCEE		31.2733845483
183UbiquitinationLKYKPVTNQVECHPY
CCCCCCCCCEECCCC		44.1022817900
190PhosphorylationNQVECHPYLTQEKLI
CCEECCCCCCHHHHH		9.94-
195UbiquitinationHPYLTQEKLIQYCHS
CCCCCHHHHHHHHHH		40.8633845483
199PhosphorylationTQEKLIQYCHSKGIT
CHHHHHHHHHHCCCE		5.78-
206PhosphorylationYCHSKGITVTAYSPL
HHHHCCCEEEEECCC		22.0720071362
211PhosphorylationGITVTAYSPLGSPDR
CCEEEEECCCCCCCC		15.93-
215PhosphorylationTAYSPLGSPDRPWAK
EEECCCCCCCCCCCC		31.1728857561
222AcetylationSPDRPWAKPEDPSLL
CCCCCCCCCCCHHHH		45.1026051181
222UbiquitinationSPDRPWAKPEDPSLL
CCCCCCCCCCCHHHH		45.1033845483
224UbiquitinationDRPWAKPEDPSLLED
CCCCCCCCCHHHHCC		80.1527667366
227PhosphorylationWAKPEDPSLLEDPKI
CCCCCCHHHHCCHHH		58.8926657352
243UbiquitinationEIAAKHKKTAAQVLI
HHHHHCCCCHHHHHH		43.0233845483
244PhosphorylationIAAKHKKTAAQVLIR
HHHHCCCCHHHHHHH		31.8430257219
263AcetylationRNVIVIPKSVTPARI
CCEEEEECCCCHHHH		46.5719608861
263UbiquitinationRNVIVIPKSVTPARI
CCEEEEECCCCHHHH		46.5733845483
280UbiquitinationNIQVFDFKLSDEEMA
EEEEEEEECCHHHHH		49.2633845483
282PhosphorylationQVFDFKLSDEEMATI
EEEEEECCHHHHHHH		43.4968744639
288PhosphorylationLSDEEMATILSFNRN
CCHHHHHHHHHCCCC		22.5720068231
291PhosphorylationEEMATILSFNRNWRA
HHHHHHHHCCCCHHH		19.3420068231
310PhosphorylationQSSHLEDYPFNAEY-
HCCCCCCCCCCCCC-		10.5955101
316PhosphorylationDYPFNAEY-------
CCCCCCCC-------		22.8018083107
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 AK1BA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AK1BA_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 AK1BA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACACA_HUMANACACAphysical
18056116
AK1BF_HUMANAKR1B15physical
26186194
POTEF_HUMANPOTEFphysical
26186194
PCBP3_HUMANPCBP3physical
26186194
AK1BF_HUMANAKR1B15physical
28514442
POTEF_HUMANPOTEFphysical
28514442
PCBP3_HUMANPCBP3physical
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 AK1BA_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-27; LYS-69; LYS-95; LYS-125;LYS-179 AND LYS-263, AND MASS SPECTROMETRY.

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