AADAT

Functionⁱ

Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).1 Publication

Catalytic activityⁱ

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.

L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate.

Cofactorⁱ

pyridoxal 5'-phosphate3 Publications

Activity regulationⁱ

Kynurenine transaminase activity is competitively inhibited by aminoadipate, asparagine, glutamate, histidine, cysteine, lysine, 3-hydroxy-kynurenine and phenylalanine.1 Publication

Kineticsⁱ

pH dependenceⁱ

Optimum pH is 7-9.1 Publication

Temperature dependenceⁱ

Optimum temperature is 50 degrees Celsius.1 Publication

Pathwayⁱ: L-lysine degradation via saccharopine pathway

This protein is involved in step 4 of the subpathway that synthesizes glutaryl-CoA from L-lysine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:

Alpha-aminoadipic semialdehyde synthase, mitochondrial (AASS)
Alpha-aminoadipic semialdehyde synthase, mitochondrial (AASS)
no protein annotated in this organism
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (AADAT)
no protein annotated in this organism
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (DLST), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (sucB)

This subpathway is part of the pathway L-lysine degradation via saccharopine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutaryl-CoA from L-lysine, the pathway L-lysine degradation via saccharopine pathway and in Amino-acid degradation.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	20	Substrate	1
Binding siteⁱ	74	Substrate	1
Binding siteⁱ	142	Substrate	1
Binding siteⁱ	202	Substrate	1
Binding siteⁱ	399	Substrate	1

GO - Molecular functionⁱ

2-aminoadipate transaminase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 18620547
kynurenine-oxoglutarate transaminase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 18620547
protein homodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 18620547
pyridoxal phosphate binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

2-oxoglutarate metabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 18620547
biosynthetic process Source: InterPro
glutamate metabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 18620547
kynurenine metabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 18620547
L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
lysine catabolic process Source: Reactome
tryptophan catabolic process Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Aminotransferase, Transferase
Ligand	Pyridoxal phosphate

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS03239-MONOMER
BRENDAⁱ	2.6.1.39 2681 2.6.1.7 2681
Reactomeⁱ	R-HSA-71064 Lysine catabolism R-HSA-71240 Tryptophan catabolism
SABIO-RKⁱ	Q8N5Z0
UniPathwayⁱ	UPA00868;UER00838

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial Short name: KAT/AadAT Alternative name(s): 2-aminoadipate aminotransferase 2-aminoadipate transaminase (EC:2.6.1.39) Alpha-aminoadipate aminotransferase Short name: AadAT Kynurenine aminotransferase II Kynurenine--oxoglutarate aminotransferase II Kynurenine--oxoglutarate transaminase 2 (EC:2.6.1.7) Kynurenine--oxoglutarate transaminase II
Gene namesⁱ	Name:AADAT Synonyms:KAT2
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 4

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000109576.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:17929 AADAT
MIMⁱ	611754 gene
neXtProtⁱ	NX_Q8N5Z0

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Organism-specific databases

DisGeNET More...DisGeNETⁱ	51166
Open Targets More...OpenTargetsⁱ	ENSG00000109576
PharmGKBⁱ	PA24364

Chemistry databases

ChEMBLⁱ	CHEMBL2046259
Drug and drug target database More...DrugBankⁱ	DB00142 L-Glutamic Acid DB00114 Pyridoxal Phosphate

Polymorphism and mutation databases

BioMutaⁱ	AADAT
DMDMⁱ	46395904

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 29	MitochondrionSequence analysisAdd BLAST		29
ChainⁱPRO_0000020602	30 – 425	Kynurenine/alpha-aminoadipate aminotransferase, mitochondrialAdd BLAST		396

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	69	N6-acetyllysineBy similarity	1
Modified residueⁱ	179	N6-acetyllysineBy similarity	1
Modified residueⁱ	263	N6-(pyridoxal phosphate)lysine; alternate	1
Modified residueⁱ	263	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	263	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	339	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	339	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	367	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	367	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	422	N6-acetyllysineBy similarity	1

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	Q8N5Z0
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q8N5Z0
PaxDbⁱ	Q8N5Z0
PeptideAtlas More...PeptideAtlasⁱ	Q8N5Z0
PRIDEⁱ	Q8N5Z0
ProteomicsDBⁱ	72114 72115 [Q8N5Z0-2]

PTM databases

iPTMnetⁱ	Q8N5Z0
PhosphoSitePlusⁱ	Q8N5Z0

Expressionⁱ

Tissue specificityⁱ

Higher expression in the liver. Also found in heart, brain, kidney, pancreas, prostate, testis and ovary.

Gene expression databases

Bgeeⁱ	ENSG00000109576 Expressed in 148 organ(s), highest expression level in right lobe of liver
CleanExⁱ	HS_AADAT
ExpressionAtlasⁱ	Q8N5Z0 baseline and differential
Genevisibleⁱ	Q8N5Z0 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA037502

HPAⁱ

HPA037502

Interactionⁱ

Subunit structureⁱ

Homodimer.3 Publications

GO - Molecular functionⁱ

protein homodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 18620547

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	119346, 2 interactors
STRINGⁱ	9606.ENSP00000226840

Chemistry databases

BindingDBⁱ	Q8N5Z0

BindingDBⁱ

Q8N5Z0

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 6	Combined sources	4
Helixⁱ	9 – 13	Combined sources	5
Helixⁱ	19 – 21	Combined sources	3
Helixⁱ	23 – 27	Combined sources	5
Helixⁱ	43 – 45	Combined sources	3
Beta strandⁱ	51 – 53	Combined sources	3
Turnⁱ	56 – 58	Combined sources	3
Beta strandⁱ	61 – 63	Combined sources	3
Helixⁱ	65 – 71	Combined sources	7
Helixⁱ	81 – 95	Combined sources	15
Turnⁱ	98 – 101	Combined sources	4
Helixⁱ	104 – 106	Combined sources	3
Beta strandⁱ	109 – 116	Combined sources	8
Helixⁱ	117 – 128	Combined sources	12
Beta strandⁱ	134 – 137	Combined sources	4
Helixⁱ	143 – 149	Combined sources	7
Helixⁱ	150 – 152	Combined sources	3
Beta strandⁱ	155 – 158	Combined sources	4
Helixⁱ	168 – 175	Combined sources	8
Helixⁱ	180 – 184	Combined sources	5
Helixⁱ	186 – 188	Combined sources	3
Beta strandⁱ	193 – 196	Combined sources	4
Turnⁱ	202 – 204	Combined sources	3
Helixⁱ	210 – 223	Combined sources	14
Beta strandⁱ	226 – 230	Combined sources	5
Turnⁱ	232 – 235	Combined sources	4
Beta strandⁱ	239 – 241	Combined sources	3
Helixⁱ	247 – 249	Combined sources	3
Beta strandⁱ	251 – 253	Combined sources	3
Beta strandⁱ	255 – 261	Combined sources	7
Turnⁱ	262 – 265	Combined sources	4
Turnⁱ	267 – 270	Combined sources	4
Beta strandⁱ	272 – 277	Combined sources	6
Helixⁱ	278 – 289	Combined sources	12
Turnⁱ	290 – 292	Combined sources	3
Beta strandⁱ	293 – 295	Combined sources	3
Helixⁱ	297 – 340	Combined sources	44
Turnⁱ	341 – 344	Combined sources	4
Beta strandⁱ	345 – 347	Combined sources	3
Beta strandⁱ	351 – 360	Combined sources	10
Helixⁱ	368 – 371	Combined sources	4
Turnⁱ	372 – 378	Combined sources	7
Beta strandⁱ	381 – 383	Combined sources	3
Helixⁱ	384 – 387	Combined sources	4
Beta strandⁱ	388 – 390	Combined sources	3
Beta strandⁱ	391 – 393	Combined sources	3
Beta strandⁱ	397 – 401	Combined sources	5
Turnⁱ	402 – 404	Combined sources	3
Helixⁱ	407 – 422	Combined sources	16

Show more details

3D structure databases

ProteinModelPortalⁱ	Q8N5Z0
SMRⁱ	Q8N5Z0
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q8N5Z0

EvolutionaryTraceⁱ

Q8N5Z0

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG0634 Eukaryota COG1167 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000004594
HOGENOMⁱ	HOG000223057
HOVERGENⁱ	HBG050429
InParanoidⁱ	Q8N5Z0
KEGG Orthology (KO) More...KOⁱ	K00825
OMAⁱ	MRLNFTY
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0B8J
PhylomeDBⁱ	Q8N5Z0
TreeFamⁱ	TF328598

Family and domain databases

Gene3Dⁱ	3.40.640.10, 1 hit
InterProⁱ	View protein in InterPro IPR004839 Aminotransferase_I/II IPR015424 PyrdxlP-dep_Trfase IPR015421 PyrdxlP-dep_Trfase_major
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00155 Aminotran_1_2, 1 hit
SUPFAMⁱ	SSF53383 SSF53383, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.ⁱShow all

Isoform 1 (identifier: Q8N5Z0-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNYARFITAA SAARNPSPIR TMTDILSRGP KSMISLAGGL PNPNMFPFKT 
        60         70         80         90        100
AVITVENGKT IQFGEEMMKR ALQYSPSAGI PELLSWLKQL QIKLHNPPTI 
       110        120        130        140        150
HYPPSQGQMD LCVTSGSQQG LCKVFEMIIN PGDNVLLDEP AYSGTLQSLH 
       160        170        180        190        200
PLGCNIINVA SDESGIVPDS LRDILSRWKP EDAKNPQKNT PKFLYTVPNG 
       210        220        230        240        250
NNPTGNSLTS ERKKEIYELA RKYDFLIIED DPYYFLQFNK FRVPTFLSMD 
       260        270        280        290        300
VDGRVIRADS FSKIISSGLR IGFLTGPKPL IERVILHIQV STLHPSTFNQ 
       310        320        330        340        350
LMISQLLHEW GEEGFMAHVD RVIDFYSNQK DAILAAADKW LTGLAEWHVP 
       360        370        380        390        400
AAGMFLWIKV KGINDVKELI EEKAVKMGVL MLPGNAFYVD SSAPSPYLRA 
       410        420 
SFSSASPEQM DVAFQVLAQL IKESL

Note: May be due to a competing donor splice site.

Length:425

Mass (Da):47,352

Last modified:April 13, 2004 - v2

Checksum:ⁱ448CCAAB2173A7BA

GO

Isoform 2 (identifier: Q8N5Z0-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
23-23: T → SEKRA

« Hide

        10         20         30         40         50
MNYARFITAA SAARNPSPIR TMSEKRADIL SRGPKSMISL AGGLPNPNMF 
        60         70         80         90        100
PFKTAVITVE NGKTIQFGEE MMKRALQYSP SAGIPELLSW LKQLQIKLHN 
       110        120        130        140        150
PPTIHYPPSQ GQMDLCVTSG SQQGLCKVFE MIINPGDNVL LDEPAYSGTL 
       160        170        180        190        200
QSLHPLGCNI INVASDESGI VPDSLRDILS RWKPEDAKNP QKNTPKFLYT 
       210        220        230        240        250
VPNGNNPTGN SLTSERKKEI YELARKYDFL IIEDDPYYFL QFNKFRVPTF 
       260        270        280        290        300
LSMDVDGRVI RADSFSKIIS SGLRIGFLTG PKPLIERVIL HIQVSTLHPS 
       310        320        330        340        350
TFNQLMISQL LHEWGEEGFM AHVDRVIDFY SNQKDAILAA ADKWLTGLAE 
       360        370        380        390        400
WHVPAAGMFL WIKVKGINDV KELIEEKAVK MGVLMLPGNA FYVDSSAPSP 
       410        420 
YLRASFSSAS PEQMDVAFQV LAQLIKESL

Show »

Length:429

Mass (Da):47,822

Checksum:ⁱ0C5A6E51F1BD6F53

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation
D6RFY7	D6RFY7_HUMAN	Kynurenine/alpha-aminoadipate amino... Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial	AADAT	209	Annotation score:
D6REB9	D6REB9_HUMAN	Kynurenine/alpha-aminoadipate amino... Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial	AADAT	220	Annotation score:
D6RC56	D6RC56_HUMAN	Kynurenine/alpha-aminoadipate amino... Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial	AADAT	180	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	103	P → Q in AAH31068 (PubMed:15489334).Curated		1
Sequence conflictⁱ	380	L → S in BAG51596 (PubMed:14702039).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_061005	243	V → I. Corresponds to variant dbSNP:rs56350236Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_009874	23	T → SEKRA in isoform 2. 1 Publication		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF097994 mRNA Translation: AAF04623.1 AF481738 mRNA Translation: AAM09683.1 AK055952 mRNA Translation: BAG51596.1 BC031068 mRNA Translation: AAH31068.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS3814.1 [Q8N5Z0-1] CCDS75209.1 [Q8N5Z0-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001273611.1, NM_001286682.1 [Q8N5Z0-2] NP_001273612.1, NM_001286683.1 [Q8N5Z0-1] NP_057312.1, NM_016228.3 [Q8N5Z0-1] NP_872603.1, NM_182662.1 [Q8N5Z0-1]
UniGeneⁱ	Hs.529735

Genome annotation databases

Ensemblⁱ	ENST00000337664; ENSP00000336808; ENSG00000109576 [Q8N5Z0-1] ENST00000353187; ENSP00000226840; ENSG00000109576 [Q8N5Z0-1] ENST00000509167; ENSP00000423190; ENSG00000109576 [Q8N5Z0-2] ENST00000515480; ENSP00000423341; ENSG00000109576 [Q8N5Z0-1]
GeneIDⁱ	51166
KEGGⁱ	hsa:51166
UCSC genome browser More...UCSCⁱ	uc003isr.4 human [Q8N5Z0-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q8N5Z0	Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (Fragment)		HUMAN		209	UniRef100_Q8N5Z0
Mitochondrial kynurenine/alpha-aminoadipate aminotransferase (Fragment)		MACMU		35
AADAT isoform 1 (Fragment)		PONAB		180
Aminoadipate aminotransferase, isoform CRA_b		HUMAN		425
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (Fragment)		HUMAN		180
+1

Protein	Similar proteins		Species	Score	Length	Source
Q8N5Z0	Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (Fragment)		HUMAN		209	UniRef90_Q8N5Z0
Mitochondrial kynurenine/alpha-aminoadipate aminotransferase (Fragment)		MACMU		35
AADAT isoform 1 (Fragment)		PONAB		180
Aminoadipate aminotransferase		RHIBE		435
Aminoadipate aminotransferase		AOTNA		429
+55

Protein	Similar proteins		Species	Score	Length	Source
Q8N5Z0	Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial		RAT		425	UniRef50_Q8N5Z0
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial		BOVIN		425
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial		MOUSE		425
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (Fragment)		HUMAN		209
Mitochondrial kynurenine/alpha-aminoadipate aminotransferase (Fragment)		MACMU		35
+322

Entry informationⁱ

Entry nameⁱ	AADAT_HUMAN
Accessionⁱ	Q8N5Z0Primary (citable) accession number: Q8N5Z0 Secondary accession number(s): B3KP84, Q9UL02
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
	Last sequence update:	April 13, 2004
	Last modified:	September 12, 2018
	This is version 147 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q8N5Z0 (AADAT_HUMAN)

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Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

pH dependencei

Temperature dependencei

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-lysine degradation via saccharopine pathway

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Mitochondrion

Mitochondrion

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Computationally mapped potential isoform sequencesi

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Kineticsⁱ

pH dependenceⁱ

Temperature dependenceⁱ

Pathwayⁱ: L-lysine degradation via saccharopine pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Computationally mapped potential isoform sequencesⁱ

Keywords - Coding sequence diversityⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ