FABPL_HUMAN - dbPTM
FABPL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FABPL_HUMAN
UniProt AC P07148
Protein Name Fatty acid-binding protein, liver
Gene Name FABP1
Organism Homo sapiens (Human).
Sequence Length 127
Subcellular Localization Cytoplasm.
Protein Description Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes. [PubMed: 25732850 Binds cholesterol]
Protein Sequence MSFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTVVQLEGDNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI
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-------MSFSGKYQ
-------CCCCCCCC
9.123838309
11PhosphorylationSGKYQLQSQENFEAF
CCCCCCCCHHHHHHH
48.3220166139
31SuccinylationLPEELIQKGKDIKGV
CCHHHHHCCCCCCCH
62.02-
31SuccinylationLPEELIQKGKDIKGV
CCHHHHHCCCCCCCH
62.02-
33AcetylationEELIQKGKDIKGVSE
HHHHHCCCCCCCHHH
64.4120167786
36SuccinylationIQKGKDIKGVSEIVQ
HHCCCCCCCHHHHHH
64.49-
36SuccinylationIQKGKDIKGVSEIVQ
HHCCCCCCCHHHHHH
64.49-
39PhosphorylationGKDIKGVSEIVQNGK
CCCCCCHHHHHHCCC
30.21-
46AcetylationSEIVQNGKHFKFTIT
HHHHHCCCEEEEEEE
54.1120167786
46SuccinylationSEIVQNGKHFKFTIT
HHHHHCCCEEEEEEE
54.11-
46SuccinylationSEIVQNGKHFKFTIT
HHHHHCCCEEEEEEE
54.11-
49AcetylationVQNGKHFKFTITAGS
HHCCCEEEEEEECCC
41.1227178108
51PhosphorylationNGKHFKFTITAGSKV
CCCEEEEEEECCCEE
20.2928857561
53PhosphorylationKHFKFTITAGSKVIQ
CEEEEEEECCCEEEC
23.1620166139
56PhosphorylationKFTITAGSKVIQNEF
EEEEECCCEEECCEE
22.6828857561
57SuccinylationFTITAGSKVIQNEFT
EEEECCCEEECCEEE
42.30-
57SuccinylationFTITAGSKVIQNEFT
EEEECCCEEECCEEE
42.30-
64PhosphorylationKVIQNEFTVGEECEL
EEECCEEECCCEEEE
22.7928857561
78SuccinylationLETMTGEKVKTVVQL
EEECCCCEEEEEEEE
50.83-
78SuccinylationLETMTGEKVKTVVQL
EEECCCCEEEEEEEE
50.83-
81PhosphorylationMTGEKVKTVVQLEGD
CCCCEEEEEEEEECC
28.9722798277
90SuccinylationVQLEGDNKLVTTFKN
EEEECCCCEEEEECC
49.42-
90SuccinylationVQLEGDNKLVTTFKN
EEEECCCCEEEEECC
49.42-
100PhosphorylationTTFKNIKSVTELNGD
EEECCCCCHHEECCC
30.4028258704
121SuccinylationTLGDIVFKRISKRI-
CHHHHHHHHHHHCC-
37.62-
121AcetylationTLGDIVFKRISKRI-
CHHHHHHHHHHHCC-
37.62156649
121SuccinylationTLGDIVFKRISKRI-
CHHHHHHHHHHHCC-
37.62-

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 FABPL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FABPL_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 FABPL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FLNA_HUMANFLNAphysical
25416956
GNA1_HUMANGNPNAT1physical
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
DB02659Cholic Acid
Regulatory Network of FABPL_HUMAN

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Related Literatures of Post-Translational Modification

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