KAT3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KAT3_HUMAN
• UniProt AC: Q6YP21
• Protein Name: Kynurenine--oxoglutarate transaminase 3
• Gene Name: KYAT3 {ECO:0000312|HGNC:HGNC:33238}
• Organism: Homo sapiens (Human).
• Sequence Length: 454
• Protein Description: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro) (By similarity)..
• Protein Sequence: MFLAQRSLCSLSGRAKFLKTISSSKILGFSTSAKMSLKFTNAKRIEGLDSNVWIEFTKLAADPSVVNLGQGFPDISPPTYVKEELSKIAAIDSLNQYTRGFGHPSLVKALSYLYEKLYQKQIDSNKEILVTVGAYGSLFNTIQALIDEGDEVILIVPFYDCYEPMVRMAGATPVFIPLRSKPVYGKRWSSSDWTLDPQELESKFNSKTKAIILNTPHNPLGKVYNREELQVIADLCIKYDTLCISDEVYEWLVYSGNKHLKIATFPGMWERTITIGSAGKTFSVTGWKLGWSIGPNHLIKHLQTVQQNTIYTCATPLQEALAQAFWIDIKRMDDPECYFNSLPKELEVKRDRMVRLLESVGLKPIVPDGGYFIIADVSLLDPDLSDMKNNEPYDYKFVKWMTKHKKLSAIPVSAFCNSETKSQFEKFVRFCFIKKDSTLDAAEEIIKAWSVQKS

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
2 (in isoform 3)	Acetylation	-	8.55	22814378
7	Phosphorylation	-MFLAQRSLCSLSGR -CCCHHHHHHHHCCH	22.96	25599653
10	Phosphorylation	LAQRSLCSLSGRAKF CHHHHHHHHCCHHHH	30.75	25599653
12	Phosphorylation	QRSLCSLSGRAKFLK HHHHHHHCCHHHHHH	15.22	18491316
22	Phosphorylation	AKFLKTISSSKILGF HHHHHHHCCCCCCCC	33.52	30631047
24	Phosphorylation	FLKTISSSKILGFST HHHHHCCCCCCCCCC	19.54	-
32	Phosphorylation	KILGFSTSAKMSLKF CCCCCCCCCCEEEEE	25.37	30631047
38	Methylation	TSAKMSLKFTNAKRI CCCCEEEEECCCCEE	42.72	-
74	Ubiquitination	NLGQGFPDISPPTYV ECCCCCCCCCCCHHH	52.30	21890473
74	Acetylation	NLGQGFPDISPPTYV ECCCCCCCCCCCHHH	52.30	19608861
74	Ubiquitination	NLGQGFPDISPPTYV ECCCCCCCCCCCHHH	52.30	19608861
76	Phosphorylation	GQGFPDISPPTYVKE CCCCCCCCCCHHHHH	32.01	26657352
79	Phosphorylation	FPDISPPTYVKEELS CCCCCCCHHHHHHHH	44.31	27251275
80	Phosphorylation	PDISPPTYVKEELSK CCCCCCHHHHHHHHH	18.46	27251275
82	Acetylation	ISPPTYVKEELSKIA CCCCHHHHHHHHHHH	34.75	19608861
82 (in isoform 1)	Ubiquitination	-	34.75	21890473
82	Ubiquitination	ISPPTYVKEELSKIA CCCCHHHHHHHHHHH	34.75	21906983
82 (in isoform 2)	Ubiquitination	-	34.75	21890473
86	Phosphorylation	TYVKEELSKIAAIDS HHHHHHHHHHHHHHH	25.87	24076635
87 (in isoform 2)	Ubiquitination	-	49.33	21890473
87 (in isoform 1)	Ubiquitination	-	49.33	21890473
87	Ubiquitination	YVKEELSKIAAIDSL HHHHHHHHHHHHHHH	49.33	21906983
93	Phosphorylation	SKIAAIDSLNQYTRG HHHHHHHHHHHHCCC	24.09	28857561
99	Methylation	DSLNQYTRGFGHPSL HHHHHHCCCCCCHHH	33.24	-
108 (in isoform 2)	Ubiquitination	-	49.23	21890473
108 (in isoform 1)	Ubiquitination	-	49.23	21890473
108	Ubiquitination	FGHPSLVKALSYLYE CCCHHHHHHHHHHHH	49.23	21890473
108	Acetylation	FGHPSLVKALSYLYE CCCHHHHHHHHHHHH	49.23	19608861
116	Succinylation	ALSYLYEKLYQKQID HHHHHHHHHHHHHCC	38.65	-
116	Succinylation	ALSYLYEKLYQKQID HHHHHHHHHHHHHCC	38.65	-
116	Acetylation	ALSYLYEKLYQKQID HHHHHHHHHHHHHCC	38.65	19608861
120 (in isoform 1)	Ubiquitination	-	35.35	21890473
120 (in isoform 2)	Ubiquitination	-	35.35	21890473
120	Ubiquitination	LYEKLYQKQIDSNKE HHHHHHHHHCCCCCC	35.35	21906983
189	Phosphorylation	PVYGKRWSSSDWTLD CCCCCCCCCCCCCCC	24.81	28450419
190	Phosphorylation	VYGKRWSSSDWTLDP CCCCCCCCCCCCCCH	25.92	28450419
191	Phosphorylation	YGKRWSSSDWTLDPQ CCCCCCCCCCCCCHH	31.48	28450419
194	Phosphorylation	RWSSSDWTLDPQELE CCCCCCCCCCHHHHH	26.69	28450419
203	Ubiquitination	DPQELESKFNSKTKA CHHHHHHHHCCCCEE	38.91	21906983
203 (in isoform 1)	Ubiquitination	-	38.91	21890473
215	Phosphorylation	TKAIILNTPHNPLGK CEEEEECCCCCCCCC	23.60	-
222	Ubiquitination	TPHNPLGKVYNREEL CCCCCCCCCCCHHHH	49.59	-
280	Other	ITIGSAGKTFSVTGW EEEECCCCEEEEEEE	46.22	-
280	N6-(pyridoxal phosphate)lysine	ITIGSAGKTFSVTGW EEEECCCCEEEEEEE	46.22	-
396	Ubiquitination	NNEPYDYKFVKWMTK CCCCCCHHHHHHHHH	40.56	-
396	Acetylation	NNEPYDYKFVKWMTK CCCCCCHHHHHHHHH	40.56	27452117
399	Ubiquitination	PYDYKFVKWMTKHKK CCCHHHHHHHHHCCC	34.09	-
399	Acetylation	PYDYKFVKWMTKHKK CCCHHHHHHHHHCCC	34.09	25953088
406	Ubiquitination	KWMTKHKKLSAIPVS HHHHHCCCCCCCCHH	47.60	-
413	Ubiquitination	KLSAIPVSAFCNSET CCCCCCHHHHCCCCC	15.41	21890473
421	Ubiquitination	AFCNSETKSQFEKFV HHCCCCCHHHHHHHH	37.90	-
434	Ubiquitination	FVRFCFIKKDSTLDA HHHHHHCCCCCHHHH	30.21	-
435	Ubiquitination	VRFCFIKKDSTLDAA HHHHHCCCCCHHHHH	52.69	-
437	Phosphorylation	FCFIKKDSTLDAAEE HHHCCCCCHHHHHHH	39.49	22210691
447 (in isoform 1)	Ubiquitination	-	49.84	21890473
447	Ubiquitination	DAAEEIIKAWSVQKS HHHHHHHHHHHHCCC	49.84	21890473
453	Ubiquitination	IKAWSVQKS------ HHHHHHCCC------	56.85	-

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

Oops, there are no upstream regulatory protein records of KAT3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KAT3_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 KAT3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MSS4_HUMAN	RABIF	physical	16169070
PGM1_HUMAN	PGM1	physical	26344197
PGM5_HUMAN	PGM5	physical	26344197

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.

Related Literatures of Post-Translational Modification

Acetylation

"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-108 AND LYS-116, AND MASSSPECTROMETRY.
PubMed: 19608861