UniProtKB - Q9UDR5 (AASS_HUMAN)

BLAST

>sp|Q9UDR5|AASS_HUMAN Alpha-aminoadipic semialdehyde synthase, mitochondrial OS=Homo sapiens OX=9606 GN=AASS PE=1 SV=1
MLQVHRTGLGRLGVSLSKGLHHKAVLAVRREDVNAWERRAPLAPKHIKGITNLGYKVLIQ
PSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEKLMSRKTYAFFSHTIKAQEANM
GLLDEILKQEIRLIDYEKMVDHRGVRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFM
HIGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQAIFNELPC
EYVEPHELKEVSQTGDLRKVYGTVLSRHHHLVRKTDAVYDPAEYDKHPERYISRFNTDIA
PYTTCLINGIYWEQNTPRLLTRQDAQSLLAPGKFSPAGVEGCPALPHKLVAICDISADTG
GSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEATECFGDMLY
PYVEEMILSDATQPLESQNFSPVVRDAVITSNGTLPDKYKYIQTLRESRERAQSLSMGTR
RKVLVLGSGYISEPVLEYLSRDGNIEITVGSDMKNQIEQLGKKYNINPVSMDICKQEEKL
GFLVAKQDLVISLLPYVLHPLVAKACITNKVNMVTASYITPALKELEKSVEDAGITIIGE
LGLDPGLDHMLAMETIDKAKEVGATIESYISYCGGLPAPEHSNNPLRYKFSWSPVGVLMN
VMQSATYLLDGKVVNVAGGISFLDAVTSMDFFPGLNLEGYPNRDSTKYAEIYGISSAHTL
LRGTLRYKGYMKALNGFVKLGLINREALPAFRPEANPLTWKQLLCDLVGISPSSEHDVLK
EAVLKKLGGDNTQLEAAEWLGLLGDEQVPQAESILDALSKHLVMKLSYGPEEKDMIVMRD
SFGIRHPSGHLEHKTIDLVAYGDINGFSAMAKTVGLPTAMAAKMLLDGEIGAKGLMGPFS
KEIYGPILERIKAEGIIYTTQSTIKP

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History
Entry version 152 (12 Sep 2018)
Sequence version 1 (01 May 2000)
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Protein

Alpha-aminoadipic semialdehyde synthase, mitochondrial

Gene

AASS

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-ketoglutarate reductase and saccharopine dehydrogenase activity, respectively.

Catalytic activityⁱ

N₆-(L-1,3-dicarboxypropyl)-L-lysine + NADP⁺ + H₂O = L-lysine + 2-oxoglutarate + NADPH.

N₆-(L-1,3-dicarboxypropyl)-L-lysine + NAD⁺ + H₂O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH.

Pathwayⁱ: L-lysine degradation via saccharopine pathway

This protein is involved in step 1 and 2 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	604	SaccharopineBy similarity	1
Binding siteⁱ	653	NADP; via amide nitrogenBy similarity	1
Binding siteⁱ	703	SaccharopineBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	488 – 491	NADPBy similarity		4
Nucleotide bindingⁱ	603 – 605	NADPBy similarity		3

GO - Molecular functionⁱ

saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity
Source: Reactome
Inferred from experimentⁱ
- 6434529
saccharopine dehydrogenase (NADP+, L-lysine-forming) activity
Source: Reactome
Inferred from experimentⁱ
- 6434529
saccharopine dehydrogenase activity Source: GO_Central

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

generation of precursor metabolites and energy Source: GO_Central
L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
lysine biosynthetic process via aminoadipic acid Source: GO_Central
lysine catabolic process Source: Reactome
protein tetramerization
Source: UniProtKB
Traceable author statementⁱ
- 10567240

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Multifunctional enzyme, Oxidoreductase
Ligand	NAD, NADP

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS00244-MONOMER
Reactomeⁱ	R-HSA-71064 Lysine catabolism
SABIO-RKⁱ	Q9UDR5
UniPathwayⁱ	UPA00868;UER00835 UPA00868;UER00836

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Alpha-aminoadipic semialdehyde synthase, mitochondrial Alternative name(s): LKR/SDH Including the following 2 domains: Lysine ketoglutarate reductase (EC:1.5.1.8) Short name: LKR Short name: LOR Saccharopine dehydrogenase (EC:1.5.1.9) Short name: SDH
Gene namesⁱ	Name:AASS
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 7

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000008311.14
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:17366 AASS
MIMⁱ	605113 gene
neXtProtⁱ	NX_Q9UDR5

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Hyperlysinemia, 1 (HYPLYS1)1 Publication

The disease is caused by mutations affecting the gene represented in this entry. In hyperlysinemia 1, both enzymatic functions of AASS are defective and patients have increased serum lysine and possibly increased saccharopine. Some individuals, however, retain significant amounts of lysine-ketoglutarate reductase and present with saccharopinuria, a metabolic condition with few, if any, clinical manifestations.1 Publication

Disease descriptionAn autosomal recessive metabolic condition with variable clinical features. Some patients present with non-specific seizures, hypotonia, or mildly delayed psychomotor development, and increased serum lysine and pipecolic acid on laboratory analysis. However, about half of the probands are reported to be asymptomatic, and hyperlysinemia is generally considered to be a benign metabolic variant.

2,4-dienoyl-CoA reductase deficiency (DECRD)1 Publication

The protein represented in this entry is involved in disease pathogenesis. A selective decrease in mitochondrial NADP(H) levels due to NADK2 mutations causes a deficiency of NADPH-dependent mitochondrial enzymes, such as DECR1 and AASS.1 Publication

Disease descriptionA rare, autosomal recessive, inborn error of polyunsaturated fatty acids and lysine metabolism, resulting in mitochondrial dysfunction. Affected individuals have a severe encephalopathy with neurologic and metabolic abnormalities beginning in early infancy. Laboratory studies show increased C10:2 carnitine levels and hyperlysinemia.

Organism-specific databases

DisGeNET More...DisGeNETⁱ	10157
MalaCards human disease database More...MalaCardsⁱ	AASS
MIMⁱ	238700 phenotype 616034 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000008311
Orphanetⁱ	2203 Hyperlysinemia 3124 Saccharopinuria
PharmGKBⁱ	PA24369

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB00142 L-Glutamic Acid DB04207 N-(5-Amino-5-Carboxypentyl)Glutamic Acid DB00157 NADH DB02338 Nadph Dihydro-Nicotinamide-Adenine-Dinucleotidephosphate

DrugBankⁱ

DB00142 L-Glutamic Acid
DB04207 N-(5-Amino-5-Carboxypentyl)Glutamic Acid
DB00157 NADH
DB02338 Nadph Dihydro-Nicotinamide-Adenine-Dinucleotidephosphate

Polymorphism and mutation databases

BioMutaⁱ	AASS
DMDMⁱ	46396032

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 32	MitochondrionBy similarityAdd BLAST		32
ChainⁱPRO_0000001052	33 – 926	Alpha-aminoadipic semialdehyde synthase, mitochondrialAdd BLAST		894

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	48	N6-acetyllysineBy similarity	1
Modified residueⁱ	56	N6-acetyllysineBy similarity	1
Modified residueⁱ	93	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	93	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	128	N6-acetyllysineBy similarity	1
Modified residueⁱ	138	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	138	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	274	N6-succinyllysineBy similarity	1
Modified residueⁱ	286	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	286	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	333	N6-succinyllysineBy similarity	1
Modified residueⁱ	458	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	458	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	523	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	523	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	535	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	535	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	584	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	584	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	707	N6-acetyllysineBy similarity	1
Modified residueⁱ	732	N6-succinyllysineBy similarity	1
Modified residueⁱ	739	N6-acetyllysineBy similarity	1
Modified residueⁱ	761	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	761	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	780	N6-acetyllysineBy similarity	1

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	Q9UDR5
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9UDR5
PaxDbⁱ	Q9UDR5
PeptideAtlas More...PeptideAtlasⁱ	Q9UDR5
PRIDEⁱ	Q9UDR5
ProteomicsDBⁱ	84114

PTM databases

CarbonylDBⁱ	Q9UDR5
iPTMnetⁱ	Q9UDR5
PhosphoSitePlusⁱ	Q9UDR5

Expressionⁱ

Tissue specificityⁱ

Expressed in all 16 tissues examined with highest expression in the liver.

Inductionⁱ

Induced by starvation.By similarity

Gene expression databases

Bgeeⁱ	ENSG00000008311 Expressed in 200 organ(s), highest expression level in right ovary
CleanExⁱ	HS_AASS
ExpressionAtlasⁱ	Q9UDR5 baseline and differential
Genevisibleⁱ	Q9UDR5 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA020637 HPA020728 HPA020734

HPAⁱ

HPA020637
HPA020728
HPA020734

Interactionⁱ

Subunit structureⁱ

Homodimer.By similarity

Protein-protein interaction databases

BioGridⁱ	115459, 12 interactors
IntActⁱ	Q9UDR5, 6 interactors
Molecular INTeraction database More...MINTⁱ	Q9UDR5
STRINGⁱ	9606.ENSP00000377040

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	483 – 486	Combined sources	4
Helixⁱ	492 – 499	Combined sources	8
Beta strandⁱ	500 – 503	Combined sources	4
Beta strandⁱ	507 – 512	Combined sources	6
Helixⁱ	514 – 523	Combined sources	10
Beta strandⁱ	527 – 530	Combined sources	4
Turnⁱ	533 – 535	Combined sources	3
Helixⁱ	537 – 545	Combined sources	9
Beta strandⁱ	548 – 552	Combined sources	5
Helixⁱ	556 – 558	Combined sources	3
Helixⁱ	559 – 569	Combined sources	11
Beta strandⁱ	572 – 577	Combined sources	6
Helixⁱ	581 – 584	Combined sources	4
Helixⁱ	587 – 593	Combined sources	7
Beta strandⁱ	596 – 598	Combined sources	3
Turnⁱ	603 – 606	Combined sources	4
Helixⁱ	607 – 620	Combined sources	14
Turnⁱ	621 – 623	Combined sources	3
Beta strandⁱ	625 – 637	Combined sources	13
Helixⁱ	639 – 641	Combined sources	3
Beta strandⁱ	650 – 652	Combined sources	3
Helixⁱ	655 – 660	Combined sources	6
Beta strandⁱ	665 – 669	Combined sources	5
Beta strandⁱ	672 – 676	Combined sources	5
Helixⁱ	679 – 685	Combined sources	7
Beta strandⁱ	687 – 689	Combined sources	3
Beta strandⁱ	697 – 701	Combined sources	5
Beta strandⁱ	703 – 705	Combined sources	3
Helixⁱ	708 – 712	Combined sources	5
Beta strandⁱ	718 – 727	Combined sources	10
Helixⁱ	730 – 740	Combined sources	11
Helixⁱ	760 – 768	Combined sources	9
Helixⁱ	775 – 785	Combined sources	11
Turnⁱ	787 – 789	Combined sources	3
Helixⁱ	791 – 800	Combined sources	10
Turnⁱ	801 – 803	Combined sources	3
Helixⁱ	814 – 825	Combined sources	12
Beta strandⁱ	834 – 845	Combined sources	12
Beta strandⁱ	851 – 861	Combined sources	11
Beta strandⁱ	864 – 866	Combined sources	3
Helixⁱ	869 – 886	Combined sources	18
Beta strandⁱ	894 – 896	Combined sources	3
Helixⁱ	901 – 910	Combined sources	10
Turnⁱ	911 – 915	Combined sources	5
Beta strandⁱ	917 – 924	Combined sources	8

Show more details

3D structure databases

ProteinModelPortalⁱ	Q9UDR5
SMRⁱ	Q9UDR5
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	33 – 455	Lysine-ketoglutarate reductaseAdd BLAST	423
Regionⁱ	477 – 926	Saccharopine dehydrogenaseAdd BLAST	450
Regionⁱ	577 – 578	Saccharopine bindingBy similarity	2
Regionⁱ	724 – 726	Saccharopine bindingBy similarity	3

Sequence similaritiesⁱ

In the N-terminal section; belongs to the AlaDH/PNT family.Curated

In the C-terminal section; belongs to the saccharopine dehydrogenase family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG0172 Eukaryota COG1748 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000013249
HOGENOMⁱ	HOG000252920
HOVERGENⁱ	HBG048688
InParanoidⁱ	Q9UDR5
KEGG Orthology (KO) More...KOⁱ	K14157
OMAⁱ	IHDKEYV
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G03D7
PhylomeDBⁱ	Q9UDR5
TreeFamⁱ	TF105728

Family and domain databases

InterProⁱ	View protein in InterPro IPR007886 AlaDH/PNT_N IPR007698 AlaDH/PNT_NAD(H)-bd IPR036291 NAD(P)-bd_dom_sf IPR032095 Sacchrp_dh_C IPR005097 Sacchrp_dh_NADP
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF05222 AlaDh_PNT_N, 1 hit PF16653 Sacchrp_dh_C, 1 hit PF03435 Sacchrp_dh_NADP, 1 hit
SMARTⁱ	View protein in SMART SM01002 AlaDh_PNT_C, 1 hit SM01003 AlaDh_PNT_N, 1 hit
SUPFAMⁱ	SSF51735 SSF51735, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show all Align All

Q9UDR5-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MLQVHRTGLG RLGVSLSKGL HHKAVLAVRR EDVNAWERRA PLAPKHIKGI 
        60         70         80         90        100
TNLGYKVLIQ PSNRRAIHDK DYVKAGGILQ EDISEACLIL GVKRPPEEKL 
       110        120        130        140        150
MSRKTYAFFS HTIKAQEANM GLLDEILKQE IRLIDYEKMV DHRGVRVVAF 
       160        170        180        190        200
GQWAGVAGMI NILHGMGLRL LALGHHTPFM HIGMAHNYRN SSQAVQAVRD 
       210        220        230        240        250
AGYEISLGLM PKSIGPLTFV FTGTGNVSKG AQAIFNELPC EYVEPHELKE 
       260        270        280        290        300
VSQTGDLRKV YGTVLSRHHH LVRKTDAVYD PAEYDKHPER YISRFNTDIA 
       310        320        330        340        350
PYTTCLINGI YWEQNTPRLL TRQDAQSLLA PGKFSPAGVE GCPALPHKLV 
       360        370        380        390        400
AICDISADTG GSIEFMTECT TIEHPFCMYD ADQHIIHDSV EGSGILMCSI 
       410        420        430        440        450
DNLPAQLPIE ATECFGDMLY PYVEEMILSD ATQPLESQNF SPVVRDAVIT 
       460        470        480        490        500
SNGTLPDKYK YIQTLRESRE RAQSLSMGTR RKVLVLGSGY ISEPVLEYLS 
       510        520        530        540        550
RDGNIEITVG SDMKNQIEQL GKKYNINPVS MDICKQEEKL GFLVAKQDLV 
       560        570        580        590        600
ISLLPYVLHP LVAKACITNK VNMVTASYIT PALKELEKSV EDAGITIIGE 
       610        620        630        640        650
LGLDPGLDHM LAMETIDKAK EVGATIESYI SYCGGLPAPE HSNNPLRYKF 
       660        670        680        690        700
SWSPVGVLMN VMQSATYLLD GKVVNVAGGI SFLDAVTSMD FFPGLNLEGY 
       710        720        730        740        750
PNRDSTKYAE IYGISSAHTL LRGTLRYKGY MKALNGFVKL GLINREALPA 
       760        770        780        790        800
FRPEANPLTW KQLLCDLVGI SPSSEHDVLK EAVLKKLGGD NTQLEAAEWL 
       810        820        830        840        850
GLLGDEQVPQ AESILDALSK HLVMKLSYGP EEKDMIVMRD SFGIRHPSGH 
       860        870        880        890        900
LEHKTIDLVA YGDINGFSAM AKTVGLPTAM AAKMLLDGEI GAKGLMGPFS 
       910        920 
KEIYGPILER IKAEGIIYTT QSTIKP

Length:926

Mass (Da):102,132

Last modified:May 1, 2000 - v1

Checksum:ⁱCB4194014351A18D

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

F8WAH1	F8WAH1_HUMAN	Alpha-aminoadipic semialdehyde synt... Alpha-aminoadipic semialdehyde synthase, mitochondrial	AASS	732	Annotation score:
F8WE53	F8WE53_HUMAN	Alpha-aminoadipic semialdehyde synt... Alpha-aminoadipic semialdehyde synthase, mitochondrial	AASS	511	Annotation score:
H7C0C6	H7C0C6_HUMAN	Alpha-aminoadipic semialdehyde synt... Alpha-aminoadipic semialdehyde synthase, mitochondrial	AASS	21	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	589	S → C in CAA07619 (Ref. 2) Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF229180 mRNA Translation: AAF44328.1 AJ007714 mRNA Translation: CAA07619.2 AC006020 Genomic DNA Translation: AAF03526.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS5783.1
NCBI Reference Sequences More...RefSeqⁱ	NP_005754.2, NM_005763.3
UniGeneⁱ	Hs.156738

Genome annotation databases

Ensemblⁱ	ENST00000393376; ENSP00000377040; ENSG00000008311 ENST00000417368; ENSP00000403768; ENSG00000008311
GeneIDⁱ	10157
KEGGⁱ	hsa:10157
UCSC genome browser More...UCSCⁱ	uc003vka.4 human

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9UDR5	Aminoadipate-semialdehyde synthase, isoform CRA_a		HUMAN		926	UniRef100_Q9UDR5

Protein	Similar proteins		Species	Score	Length	Source
Q9UDR5	Alpha-aminoadipic semialdehyde synthase, mitochondrial		BOVIN		926	UniRef90_Q9UDR5
Aminoadipate-semialdehyde synthase, isoform CRA_a		HUMAN		926
Uncharacterized protein		FELCA		977
alpha-aminoadipic semialdehyde synthase, mitochondrial isoform X1		Enhydra lutris kenyoni		935
Alpha-aminoadipic semialdehyde synthase, mitochondrial		PTEAL		932
+123

Protein	Similar proteins		Species	Score	Length	Source
Q9UDR5	Alpha-aminoadipic semialdehyde synthase, mitochondrial		BOVIN		926	UniRef50_Q9UDR5
Aminoadipate-semialdehyde synthase, isoform CRA_a		HUMAN		926
Uncharacterized protein		FELCA		977
alpha-aminoadipic semialdehyde synthase, mitochondrial isoform X1		Enhydra lutris kenyoni		935
Alpha-aminoadipic semialdehyde synthase, mitochondrial		PTEAL		932
+412

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF229180 mRNA Translation: AAF44328.1 AJ007714 mRNA Translation: CAA07619.2 AC006020 Genomic DNA Translation: AAF03526.1
CCDSⁱ	CCDS5783.1
RefSeqⁱ	NP_005754.2, NM_005763.3
UniGeneⁱ	Hs.156738

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5L76	X-ray	2.57	A	455-926	[»]
	5L78	X-ray	2.68	A/B	455-926	[»]
	5O1N	X-ray	2.28	A	455-926	[»]
	5O1O	X-ray	2.48	A/B	455-926	[»]
	5O1P	X-ray	1.90	A	455-926	[»]
ProteinModelPortalⁱ	Q9UDR5
SMRⁱ	Q9UDR5
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	115459, 12 interactors
IntActⁱ	Q9UDR5, 6 interactors
MINTⁱ	Q9UDR5
STRINGⁱ	9606.ENSP00000377040

Chemistry databases

DrugBankⁱ	DB00142 L-Glutamic Acid DB04207 N-(5-Amino-5-Carboxypentyl)Glutamic Acid DB00157 NADH DB02338 Nadph Dihydro-Nicotinamide-Adenine-Dinucleotidephosphate

DrugBankⁱ

DB00142 L-Glutamic Acid
DB04207 N-(5-Amino-5-Carboxypentyl)Glutamic Acid
DB00157 NADH
DB02338 Nadph Dihydro-Nicotinamide-Adenine-Dinucleotidephosphate

PTM databases

CarbonylDBⁱ	Q9UDR5
iPTMnetⁱ	Q9UDR5
PhosphoSitePlusⁱ	Q9UDR5

Polymorphism and mutation databases

BioMutaⁱ	AASS
DMDMⁱ	46396032

Proteomic databases

EPDⁱ	Q9UDR5
MaxQBⁱ	Q9UDR5
PaxDbⁱ	Q9UDR5
PeptideAtlasⁱ	Q9UDR5
PRIDEⁱ	Q9UDR5
ProteomicsDBⁱ	84114

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000393376; ENSP00000377040; ENSG00000008311 ENST00000417368; ENSP00000403768; ENSG00000008311
GeneIDⁱ	10157
KEGGⁱ	hsa:10157
UCSCⁱ	uc003vka.4 human

Organism-specific databases

CTDⁱ	10157
DisGeNETⁱ	10157
EuPathDBⁱ	HostDB:ENSG00000008311.14
GeneCardsⁱ	AASS
HGNCⁱ	HGNC:17366 AASS
HPAⁱ	HPA020637 HPA020728 HPA020734
MalaCardsⁱ	AASS
MIMⁱ	238700 phenotype 605113 gene 616034 phenotype
neXtProtⁱ	NX_Q9UDR5
OpenTargetsⁱ	ENSG00000008311
Orphanetⁱ	2203 Hyperlysinemia 3124 Saccharopinuria
PharmGKBⁱ	PA24369
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0172 Eukaryota COG1748 LUCA
GeneTreeⁱ	ENSGT00390000013249
HOGENOMⁱ	HOG000252920
HOVERGENⁱ	HBG048688
InParanoidⁱ	Q9UDR5
KOⁱ	K14157
OMAⁱ	IHDKEYV
OrthoDBⁱ	EOG091G03D7
PhylomeDBⁱ	Q9UDR5
TreeFamⁱ	TF105728

Enzyme and pathway databases

UniPathwayⁱ	UPA00868;UER00835 UPA00868;UER00836
BioCycⁱ	MetaCyc:HS00244-MONOMER
Reactomeⁱ	R-HSA-71064 Lysine catabolism
SABIO-RKⁱ	Q9UDR5

Miscellaneous databases

ChiTaRSⁱ	AASS human
GeneWikiⁱ	AASS
GenomeRNAiⁱ	10157
Protein Ontology More...PROⁱ	PR:Q9UDR5
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000008311 Expressed in 200 organ(s), highest expression level in right ovary
CleanExⁱ	HS_AASS
ExpressionAtlasⁱ	Q9UDR5 baseline and differential
Genevisibleⁱ	Q9UDR5 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR007886 AlaDH/PNT_N IPR007698 AlaDH/PNT_NAD(H)-bd IPR036291 NAD(P)-bd_dom_sf IPR032095 Sacchrp_dh_C IPR005097 Sacchrp_dh_NADP
Pfamⁱ	View protein in Pfam PF05222 AlaDh_PNT_N, 1 hit PF16653 Sacchrp_dh_C, 1 hit PF03435 Sacchrp_dh_NADP, 1 hit
SMARTⁱ	View protein in SMART SM01002 AlaDh_PNT_C, 1 hit SM01003 AlaDh_PNT_N, 1 hit
SUPFAMⁱ	SSF51735 SSF51735, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	AASS_HUMAN
Accessionⁱ	Q9UDR5Primary (citable) accession number: Q9UDR5 Secondary accession number(s): O95462
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
	Last sequence update:	May 1, 2000
	Last modified:	September 12, 2018
	This is version 152 of the entry and version 1 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

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human chromosome 7
Human chromosome 7: entries, gene names and cross-references to MIM

UniProtKB

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UniRef

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Supporting data

UniProtKB - Q9UDR5 (AASS_HUMAN)

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Alpha-aminoadipic semialdehyde synthase, mitochondrial

AASS

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<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 <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

Regions

<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

Other locations

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

Protein-protein interaction 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

<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

Region

<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

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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

Documents

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Functionⁱ

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

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ