FAH2B_HUMAN - dbPTM
FAH2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FAH2B_HUMAN
UniProt AC Q6P2I3
Protein Name Fumarylacetoacetate hydrolase domain-containing protein 2B
Gene Name FAHD2B
Organism Homo sapiens (Human).
Sequence Length 314
Subcellular Localization
Protein Description May have hydrolase activity..
Protein Sequence MLVSGRRRLLTALLQAQKWPFQPSRDMRLVQFRAPHLVGPHLGLETGNGGGVINLNAFDPTLPKTMTQFLEQGEATLSVARRALAAQLPVLPWSEVTFLAPVTWPDKVVCVGMNYVDHCKEQNVPVPKEPIIFSKFASSIVGPYDEVVLPPQSQEVDWEVELAVVIGKKGKHIKATDAMAHVAGFTVAHDVSARDWLTRRNGKQWLLGKTFDTFCPLGPALVTKDSVADPHNLKICCRVNGEVVQSSNTNQMVFKTEDLIAWVSQFVTFYPGDVILTGTPPGVGVFRKPPVFLKKGDEVQCEIEELGVIINKVV
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
120AcetylationMNYVDHCKEQNVPVP
CCCCHHHHHCCCCCC		59.9425038526
120UbiquitinationMNYVDHCKEQNVPVP
CCCCHHHHHCCCCCC		59.94-
128UbiquitinationEQNVPVPKEPIIFSK
HCCCCCCCCCCEEEC		76.10-
128AcetylationEQNVPVPKEPIIFSK
HCCCCCCCCCCEEEC		76.1025038526
128SuccinylationEQNVPVPKEPIIFSK
HCCCCCCCCCCEEEC		76.1023954790
134PhosphorylationPKEPIIFSKFASSIV
CCCCCEEECCCHHCC		19.2224719451
174MalonylationGKKGKHIKATDAMAH
CCCCCCCEEHHHHHH		44.9826320211
192PhosphorylationFTVAHDVSARDWLTR
CEEECCCCHHHHHHH		24.5222210691
203MalonylationWLTRRNGKQWLLGKT
HHHHCCCCEEEECCE		41.6826320211
203UbiquitinationWLTRRNGKQWLLGKT
HHHHCCCCEEEECCE		41.68-
203AcetylationWLTRRNGKQWLLGKT
HHHHCCCCEEEECCE		41.6823236377
209UbiquitinationGKQWLLGKTFDTFCP
CCEEEECCEECCCCC		46.09-
213PhosphorylationLLGKTFDTFCPLGPA
EECCEECCCCCCCCE		23.9720068231
223PhosphorylationPLGPALVTKDSVADP
CCCCEEECCCCCCCC		29.9520068231
224AcetylationLGPALVTKDSVADPH
CCCEEECCCCCCCCC		40.2925038526
224UbiquitinationLGPALVTKDSVADPH
CCCEEECCCCCCCCC		40.29-
234MalonylationVADPHNLKICCRVNG
CCCCCCCEEEEEECC		38.7326320211
234UbiquitinationVADPHNLKICCRVNG
CCCCCCCEEEEEECC		38.73-
234AcetylationVADPHNLKICCRVNG
CCCCCCCEEEEEECC		38.7323749302
288UbiquitinationPGVGVFRKPPVFLKK
CCCCCCCCCCEECCC		42.06-
295UbiquitinationKPPVFLKKGDEVQCE
CCCEECCCCCEEEEE		73.98-
312UbiquitinationELGVIINKVV-----
ECEEEEEECC-----		33.69-
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 FAH2B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FAH2B_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 FAH2B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FAH2B_HUMAN !!
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 FAH2B_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-203 AND LYS-234, AND MASSSPECTROMETRY.

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