BAAT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BAAT_HUMAN
• UniProt AC: Q14032
• Protein Name: Bile acid-CoA:amino acid N-acyltransferase {ECO:0000303|PubMed:8034703}
• Gene Name: BAAT
• Organism: Homo sapiens (Human).
• Sequence Length: 418
• Subcellular Localization: Cytoplasm .
• Protein Description: Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs..
• Protein Sequence: MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDLNHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVASAPKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASLLASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQIGLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFETTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGAGHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL

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
35	Phosphorylation	QMVSFQASLEDENGD EEEEEEEEEECCCCC	22.85	28787133
125	Phosphorylation	VASAPKASLTLERWY ECCCCCCEEEEEEEE	28.19	-
132	Phosphorylation	SLTLERWYVAPGVTR EEEEEEEEECCCCEE	7.92	-
138	Phosphorylation	WYVAPGVTRIKVREG EEECCCCEEEEEEEC	32.37	-
196	Phosphorylation	LALAYHNYEDLPRKP HHHHHCCCCCCCCCC	9.48	-
210	Phosphorylation	PEVTDLEYFEEAANF CCCCCHHHHHHHHHH	24.48	-
307	Phosphorylation	ETTQVGASQYLFPIE CCCCCCCEEEEEEEH	17.27	24275569
309	Phosphorylation	TQVGASQYLFPIEEA CCCCCEEEEEEEHHC	14.07	24275569
334	Acetylation	GDKTINSKAHAEQAI CCCEECCHHHHHHHH	39.44	20167786
345	Acetylation	EQAIGQLKRHGKNNW HHHHHHHHHHCCCCE	34.17	24885297
345	Ubiquitination	EQAIGQLKRHGKNNW HHHHHHHHHHCCCCE	34.17	33845483
416	Phosphorylation	HLIPDVTSQL----- HCCCCHHCCC-----	29.36	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of BAAT_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BAAT_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of BAAT_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STAU1_HUMAN	STAU1	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 607748: Familial hypercholanemia (FHCA)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00145: Glycine