FAAA_HUMAN - dbPTM
FAAA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FAAA_HUMAN
UniProt AC P16930
Protein Name Fumarylacetoacetase
Gene Name FAH
Organism Homo sapiens (Human).
Sequence Length 419
Subcellular Localization
Protein Description
Protein Sequence MSFIPVAEDSDFPIHNLPYGVFSTRGDPRPRIGVAIGDQILDLSIIKHLFTGPVLSKHQDVFNQPTLNSFMGLGQAAWKEARVFLQNLLSVSQARLRDDTELRKCAFISQASATMHLPATIGDYTDFYSSRQHATNVGIMFRDKENALMPNWLHLPVGYHGRASSVVVSGTPIRRPMGQMKPDDSKPPVYGACKLLDMELEMAFFVGPGNRLGEPIPISKAHEHIFGMVLMNDWSARDIQKWEYVPLGPFLGKSFGTTVSPWVVPMDALMPFAVPNPKQDPRPLPYLCHDEPYTFDINLSVNLKGEGMSQAATICKSNFKYMYWTMLQQLTHHSVNGCNLRPGDLLASGTISGPEPENFGSMLELSWKGTKPIDLGNGQTRKFLLDGDEVIITGYCQGDGYRIGFGQCAGKVLPALLPS
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
2Phosphorylation------MSFIPVAED
------CCCCCCCCC
31.7024043423
2Acetylation------MSFIPVAED
------CCCCCCCCC
31.7025944712
10PhosphorylationFIPVAEDSDFPIHNL
CCCCCCCCCCCCCCC
32.4324043423
19PhosphorylationFPIHNLPYGVFSTRG
CCCCCCCCCEEECCC
29.1424043423
23PhosphorylationNLPYGVFSTRGDPRP
CCCCCEEECCCCCCC
18.1324043423
24PhosphorylationLPYGVFSTRGDPRPR
CCCCEEECCCCCCCC
27.4924043423
44PhosphorylationGDQILDLSIIKHLFT
CCCHHHHHHHHHHHH
23.1824719451
57AcetylationFTGPVLSKHQDVFNQ
HHCCCHHCCHHHHCC
40.9225953088
79AcetylationGLGQAAWKEARVFLQ
HHHHHHHHHHHHHHH
36.4525953088
90PhosphorylationVFLQNLLSVSQARLR
HHHHHHHHHHHHHCC
23.9228857561
92PhosphorylationLQNLLSVSQARLRDD
HHHHHHHHHHHCCCC
18.1028857561
128PhosphorylationIGDYTDFYSSRQHAT
CCCCHHHHHCCCCCC
14.46-
144UbiquitinationVGIMFRDKENALMPN
EEEEEECCCCCCCCC
48.92-
164PhosphorylationVGYHGRASSVVVSGT
CCCCCCCCEEEEECC
23.4628857561
165PhosphorylationGYHGRASSVVVSGTP
CCCCCCCEEEEECCC
20.2528857561
219PhosphorylationLGEPIPISKAHEHIF
CCCCEECHHHHHHHH
20.5921406692
241UbiquitinationWSARDIQKWEYVPLG
CCHHHHCCCEEEECC
42.1821890473
241UbiquitinationWSARDIQKWEYVPLG
CCHHHHCCCEEEECC
42.1821890473
241AcetylationWSARDIQKWEYVPLG
CCHHHHCCCEEEECC
42.1820167786
244PhosphorylationRDIQKWEYVPLGPFL
HHHCCCEEEECCCCC
13.27-
308SulfoxidationVNLKGEGMSQAATIC
EEECCCCCCHHHHHH
2.0330846556
309PhosphorylationNLKGEGMSQAATICK
EECCCCCCHHHHHHH
27.7628857561
313PhosphorylationEGMSQAATICKSNFK
CCCCHHHHHHHHHHH
29.8929255136
370PhosphorylationLELSWKGTKPIDLGN
EEEEECCCCCEECCC
29.89-
371UbiquitinationELSWKGTKPIDLGNG
EEEECCCCCEECCCC
48.95-
395PhosphorylationDEVIITGYCQGDGYR
CEEEEEEECCCCCCE
3.497550234
411UbiquitinationGFGQCAGKVLPALLP
CCCCCCCCCHHHHCC
23.29-
419PhosphorylationVLPALLPS-------
CHHHHCCC-------
53.4728102081

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 FAAA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FAAA_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 FAAA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KRA59_HUMANKRTAP5-9physical
25416956
ITF2_HUMANTCF4physical
25416956
SRTD1_HUMANSERTAD1physical
25416956
ATL4_HUMANADAMTSL4physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
PGM1_HUMANPGM1physical
26344197
DHSO_HUMANSORDphysical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
276700Tyrosinemia 1 (TYRSN1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FAAA_HUMAN

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Related Literatures of Post-Translational Modification

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