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Protein

Adenylosuccinate lyase

Gene

ADSL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate.1 Publication

Catalytic activityi

N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.2 Publications
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.2 Publications

Enzyme regulationi

The enzyme reaction kinetics indicate cooperativity between subunits.2 Publications

Pathwayi: AMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes AMP from IMP.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Adenylosuccinate synthetase isozyme 2 (ADSS), Adenylosuccinate synthetase isozyme 2 (ADSS), Adenylosuccinate synthetase isozyme 1 (ADSSL1), Adenylosuccinate synthetase isozyme 2 (ADSS)
  2. Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase, Adenylosuccinate lyase, Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase, Adenylosuccinate lyase (ADSL)
This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from IMP, the pathway AMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Multifunctional protein ADE2 (PAICS)
  2. Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase, Adenylosuccinate lyase, Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase, Adenylosuccinate lyase (ADSL)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei159Proton donor/acceptor1 Publication1
Binding sitei241Substrate1
Active sitei289Proton donor/acceptor1 Publication1
Binding sitei303Substrate; shared with neighboring subunit1
Binding sitei329Substrate1
Binding sitei334Substrate1
Binding sitei338Substrate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:HS02059-MONOMER.
ZFISH:HS02059-MONOMER.
BRENDAi4.3.2.2. 2681.
ReactomeiR-HSA-73817. Purine ribonucleoside monophosphate biosynthesis.
SABIO-RKP30566.
UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate lyase1 Publication (EC:4.3.2.22 Publications)
Short name:
ADSL1 Publication
Short name:
ASL
Alternative name(s):
Adenylosuccinase1 Publication
Short name:
ASase
Gene namesi
Name:ADSL
Synonyms:AMPS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:291. ADSL.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Adenylosuccinase deficiency (ADSLD)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by the accumulation in the body fluids of succinylaminoimidazole-carboxamide riboside (SAICA-riboside) and succinyladenosine (S-Ado). Most children display marked psychomotor delay, often accompanied by epilepsy or autistic features, or both, although some patients may be less profoundly retarded. Occasionally, growth retardation and muscular wasting are also present.
See also OMIM:103050
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0169302A → V in ADSLD; severe. 1 PublicationCorresponds to variant rs143083947dbSNPEnsembl.1
Natural variantiVAR_0170783A → V in ADSLD; severe. 1 Publication1
Natural variantiVAR_01693126M → L in ADSLD; severe. 1 Publication1
Natural variantiVAR_00797272I → V in ADSLD; severe. 1 Publication1
Natural variantiVAR_017079100P → A in ADSLD; moderate. 1 PublicationCorresponds to variant rs119450942dbSNPEnsembl.1
Natural variantiVAR_017080114Y → H in ADSLD; severe; total loss of activity. 1 PublicationCorresponds to variant rs374259530dbSNPEnsembl.1
Natural variantiVAR_007973141R → W in ADSLD; severe. 2 PublicationsCorresponds to variant rs756210458dbSNPEnsembl.1
Natural variantiVAR_007974190R → Q in ADSLD; moderate. 2 PublicationsCorresponds to variant rs28941471dbSNPEnsembl.1
Natural variantiVAR_017081194R → C in ADSLD; severe; reduces protein stability. 2 Publications1
Natural variantiVAR_007975246K → E in ADSLD; moderate; strongly reduced catalytic activity. 2 PublicationsCorresponds to variant rs119450944dbSNPEnsembl.1
Natural variantiVAR_017082268D → N in ADSLD; severe; total loss of activity. 1 PublicationCorresponds to variant rs746501563dbSNPEnsembl.1
Natural variantiVAR_007976303R → C in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity. 3 PublicationsCorresponds to variant rs373458753dbSNPEnsembl.1
Natural variantiVAR_017083311L → V in ADSLD; severe; slightly reduced enzyme activity. 2 Publications1
Natural variantiVAR_017084318P → L in ADSLD; severe. Corresponds to variant rs202064195dbSNPEnsembl.1
Natural variantiVAR_017085364V → M in ADSLD; severe. 1 PublicationCorresponds to variant rs370851726dbSNPEnsembl.1
Natural variantiVAR_017086374R → W in ADSLD; severe. Corresponds to variant rs376533026dbSNPEnsembl.1
Natural variantiVAR_007977395S → R in ADSLD; severe. 2 Publications1
Natural variantiVAR_017087396R → C in ADSLD; severe; abolishes cooperativity and reduces enzyme activity. 1 PublicationCorresponds to variant rs755492501dbSNPEnsembl.1
Natural variantiVAR_017088396R → H in ADSLD; severe; abolishes cooperativity and reduces enzyme activity. 2 PublicationsCorresponds to variant rs763542069dbSNPEnsembl.1
Natural variantiVAR_017089422D → Y in ADSLD; moderate. 1 PublicationCorresponds to variant rs119450943dbSNPEnsembl.1
Natural variantiVAR_017090423L → V in ADSLD; moderate. 1
Natural variantiVAR_007978426R → H in ADSLD; severe; most frequent mutation. 5 PublicationsCorresponds to variant rs119450941dbSNPEnsembl.1
Natural variantiVAR_017091430D → N in ADSLD; mild. 1 PublicationCorresponds to variant rs554254383dbSNPEnsembl.1
Natural variantiVAR_000680438S → P in ADSLD; severe. 1 PublicationCorresponds to variant rs119450940dbSNPEnsembl.1
Natural variantiVAR_017092447S → P in ADSLD; severe. Corresponds to variant rs777821034dbSNPEnsembl.1
Natural variantiVAR_016932450T → S in ADSLD; moderate. 1 PublicationCorresponds to variant rs372895468dbSNPEnsembl.1
Natural variantiVAR_017093452R → P in ADSLD; severe. 1 Publication1

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

DisGeNETi158.
MalaCardsiADSL.
MIMi103050. phenotype.
OpenTargetsiENSG00000239900.
Orphaneti46. Adenylosuccinate lyase deficiency.
PharmGKBiPA24600.

Polymorphism and mutation databases

BioMutaiADSL.
DMDMi6686318.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001378922 – 484Adenylosuccinate lyaseAdd BLAST483

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei9PhosphoserineCombined sources1
Modified residuei15PhosphoserineCombined sources1
Modified residuei147N6-acetyllysineCombined sources1
Modified residuei295N6-acetyllysineCombined sources1
Cross-linki415Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP30566.
PaxDbiP30566.
PeptideAtlasiP30566.
PRIDEiP30566.

PTM databases

iPTMnetiP30566.
PhosphoSitePlusiP30566.
SwissPalmiP30566.

Expressioni

Tissue specificityi

Ubiquitously expressed. Both isoforms are produced by all tissues. Isoform 2 is 10-fold less abundant than isoform 1.

Gene expression databases

BgeeiENSG00000239900.
CleanExiHS_ADSL.
ExpressionAtlasiP30566. baseline and differential.
GenevisibleiP30566. HS.

Organism-specific databases

HPAiCAB019285.
HPA000525.

Interactioni

Subunit structurei

Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.2 Publications

Protein-protein interaction databases

BioGridi106667. 69 interactors.
IntActiP30566. 19 interactors.
STRINGi9606.ENSP00000216194.

Structurei

Secondary structure

1484
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 19Combined sources4
Helixi24 – 29Combined sources6
Helixi32 – 53Combined sources22
Helixi59 – 66Combined sources8
Beta strandi68 – 70Combined sources3
Helixi74 – 84Combined sources11
Helixi87 – 98Combined sources12
Turni100 – 102Combined sources3
Helixi103 – 105Combined sources3
Turni106 – 109Combined sources4
Helixi113 – 148Combined sources36
Turni149 – 151Combined sources3
Beta strandi153 – 158Combined sources6
Beta strandi161 – 167Combined sources7
Helixi168 – 192Combined sources25
Beta strandi201 – 204Combined sources4
Helixi206 – 211Combined sources6
Turni212 – 214Combined sources3
Helixi216 – 229Combined sources14
Beta strandi240 – 242Combined sources3
Helixi246 – 274Combined sources29
Beta strandi277 – 279Combined sources3
Helixi299 – 313Combined sources15
Helixi316 – 323Combined sources8
Helixi331 – 333Combined sources3
Helixi334 – 360Combined sources27
Helixi366 – 380Combined sources15
Helixi382 – 389Combined sources8
Turni391 – 393Combined sources3
Helixi396 – 416Combined sources21
Helixi423 – 429Combined sources7
Helixi431 – 433Combined sources3
Helixi434 – 437Combined sources4
Helixi440 – 443Combined sources4
Helixi446 – 449Combined sources4
Helixi453 – 463Combined sources11
Helixi465 – 469Combined sources5
Helixi470 – 472Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J91X-ray1.80A/B/C/D1-481[»]
2VD6X-ray2.00A/B/C/D1-481[»]
4FFXX-ray2.70A/B/C/D1-484[»]
4FLCX-ray2.60A/B/C/D1-484[»]
ProteinModelPortaliP30566.
SMRiP30566.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30566.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni20 – 21Substrate binding; shared with neighboring subunit2
Regioni85 – 87Substrate binding3
Regioni111 – 112Substrate binding2

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
GeneTreeiENSGT00390000013486.
HOGENOMiHOG000033915.
HOVERGENiHBG000214.
InParanoidiP30566.
KOiK01756.
PhylomeDBiP30566.
TreeFamiTF106385.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

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. AlignAdd to basket

Isoform 1 (identifier: P30566-1) [UniParc]FASTAAdd 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
MAAGGDHGSP DSYRSPLASR YASPEMCFVF SDRYKFRTWR QLWLWLAEAE
60 70 80 90 100
QTLGLPITDE QIQEMKSNLE NIDFKMAAEE EKRLRHDVMA HVHTFGHCCP
110 120 130 140 150
KAAGIIHLGA TSCYVGDNTD LIILRNALDL LLPKLARVIS RLADFAKERA
160 170 180 190 200
SLPTLGFTHF QPAQLTTVGK RCCLWIQDLC MDLQNLKRVR DDLRFRGVKG
210 220 230 240 250
TTGTQASFLQ LFEGDDHKVE QLDKMVTEKA GFKRAFIITG QTYTRKVDIE
260 270 280 290 300
VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR
310 320 330 340 350
SERCCSLARH LMTLVMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT
360 370 380 390 400
ILNTLQNISE GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQDCH
410 420 430 440 450
EKIRVLSQQA ASVVKQEGGD NDLIERIQVD AYFSPIHSQL DHLLDPSSFT
460 470 480
GRASQQVQRF LEEEVYPLLK PYESVMKVKA ELCL
Length:484
Mass (Da):54,889
Last modified:May 30, 2000 - v2
Checksum:i7AA3A0A2C681FD94
GO
Isoform 2 (identifier: P30566-2) [UniParc]FASTAAdd to basket
Also known as: Delta-ADSL

The sequence of this isoform differs from the canonical sequence as follows:
     398-456: Missing.

Note: Lacks enzymatic activity.
Show »
Length:425
Mass (Da):48,328
Checksum:i66356963E46FDA3D
GO

Sequence cautioni

The sequence AAC60603 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA46697 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0169302A → V in ADSLD; severe. 1 PublicationCorresponds to variant rs143083947dbSNPEnsembl.1
Natural variantiVAR_0170783A → V in ADSLD; severe. 1 Publication1
Natural variantiVAR_01693126M → L in ADSLD; severe. 1 Publication1
Natural variantiVAR_03788331S → N.Corresponds to variant rs5757921dbSNPEnsembl.1
Natural variantiVAR_00797272I → V in ADSLD; severe. 1 Publication1
Natural variantiVAR_017079100P → A in ADSLD; moderate. 1 PublicationCorresponds to variant rs119450942dbSNPEnsembl.1
Natural variantiVAR_017080114Y → H in ADSLD; severe; total loss of activity. 1 PublicationCorresponds to variant rs374259530dbSNPEnsembl.1
Natural variantiVAR_007973141R → W in ADSLD; severe. 2 PublicationsCorresponds to variant rs756210458dbSNPEnsembl.1
Natural variantiVAR_037884147K → M.Corresponds to variant rs11089991dbSNPEnsembl.1
Natural variantiVAR_007974190R → Q in ADSLD; moderate. 2 PublicationsCorresponds to variant rs28941471dbSNPEnsembl.1
Natural variantiVAR_017081194R → C in ADSLD; severe; reduces protein stability. 2 Publications1
Natural variantiVAR_007975246K → E in ADSLD; moderate; strongly reduced catalytic activity. 2 PublicationsCorresponds to variant rs119450944dbSNPEnsembl.1
Natural variantiVAR_017082268D → N in ADSLD; severe; total loss of activity. 1 PublicationCorresponds to variant rs746501563dbSNPEnsembl.1
Natural variantiVAR_007976303R → C in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity. 3 PublicationsCorresponds to variant rs373458753dbSNPEnsembl.1
Natural variantiVAR_017083311L → V in ADSLD; severe; slightly reduced enzyme activity. 2 Publications1
Natural variantiVAR_017084318P → L in ADSLD; severe. Corresponds to variant rs202064195dbSNPEnsembl.1
Natural variantiVAR_017085364V → M in ADSLD; severe. 1 PublicationCorresponds to variant rs370851726dbSNPEnsembl.1
Natural variantiVAR_017086374R → W in ADSLD; severe. Corresponds to variant rs376533026dbSNPEnsembl.1
Natural variantiVAR_007977395S → R in ADSLD; severe. 2 Publications1
Natural variantiVAR_017087396R → C in ADSLD; severe; abolishes cooperativity and reduces enzyme activity. 1 PublicationCorresponds to variant rs755492501dbSNPEnsembl.1
Natural variantiVAR_017088396R → H in ADSLD; severe; abolishes cooperativity and reduces enzyme activity. 2 PublicationsCorresponds to variant rs763542069dbSNPEnsembl.1
Natural variantiVAR_017089422D → Y in ADSLD; moderate. 1 PublicationCorresponds to variant rs119450943dbSNPEnsembl.1
Natural variantiVAR_017090423L → V in ADSLD; moderate. 1
Natural variantiVAR_007978426R → H in ADSLD; severe; most frequent mutation. 5 PublicationsCorresponds to variant rs119450941dbSNPEnsembl.1
Natural variantiVAR_017091430D → N in ADSLD; mild. 1 PublicationCorresponds to variant rs554254383dbSNPEnsembl.1
Natural variantiVAR_000680438S → P in ADSLD; severe. 1 PublicationCorresponds to variant rs119450940dbSNPEnsembl.1
Natural variantiVAR_017092447S → P in ADSLD; severe. Corresponds to variant rs777821034dbSNPEnsembl.1
Natural variantiVAR_016932450T → S in ADSLD; moderate. 1 PublicationCorresponds to variant rs372895468dbSNPEnsembl.1
Natural variantiVAR_017093452R → P in ADSLD; severe. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000318398 – 456Missing in isoform 2. 2 PublicationsAdd BLAST59

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65867 mRNA. Translation: CAA46696.1.
X65867 mRNA. Translation: CAA46697.1. Different initiation.
AF067853 mRNA. Translation: AAC21560.1.
AF067854 mRNA. Translation: AAC21561.1.
CR456368 mRNA. Translation: CAG30254.1.
AL022238 Genomic DNA. Translation: CAI18983.1.
AL022238 Genomic DNA. Translation: CAQ08930.1.
CH471095 Genomic DNA. Translation: EAW60375.1.
BC000253 mRNA. Translation: AAH00253.1.
S60710 mRNA. Translation: AAC60603.1. Different initiation.
CCDSiCCDS14001.1. [P30566-1]
CCDS46714.1. [P30566-2]
RefSeqiNP_000017.1. NM_000026.3. [P30566-1]
NP_001116850.1. NM_001123378.2. [P30566-2]
NP_001304852.1. NM_001317923.1.
UniGeneiHs.75527.

Genome annotation databases

EnsembliENST00000342312; ENSP00000341429; ENSG00000239900. [P30566-2]
ENST00000623063; ENSP00000485525; ENSG00000239900. [P30566-1]
GeneIDi158.
KEGGihsa:158.
UCSCiuc003ays.5. human. [P30566-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

ADSLdb

Adenylosuccinate lyase mutations database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65867 mRNA. Translation: CAA46696.1.
X65867 mRNA. Translation: CAA46697.1. Different initiation.
AF067853 mRNA. Translation: AAC21560.1.
AF067854 mRNA. Translation: AAC21561.1.
CR456368 mRNA. Translation: CAG30254.1.
AL022238 Genomic DNA. Translation: CAI18983.1.
AL022238 Genomic DNA. Translation: CAQ08930.1.
CH471095 Genomic DNA. Translation: EAW60375.1.
BC000253 mRNA. Translation: AAH00253.1.
S60710 mRNA. Translation: AAC60603.1. Different initiation.
CCDSiCCDS14001.1. [P30566-1]
CCDS46714.1. [P30566-2]
RefSeqiNP_000017.1. NM_000026.3. [P30566-1]
NP_001116850.1. NM_001123378.2. [P30566-2]
NP_001304852.1. NM_001317923.1.
UniGeneiHs.75527.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J91X-ray1.80A/B/C/D1-481[»]
2VD6X-ray2.00A/B/C/D1-481[»]
4FFXX-ray2.70A/B/C/D1-484[»]
4FLCX-ray2.60A/B/C/D1-484[»]
ProteinModelPortaliP30566.
SMRiP30566.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106667. 69 interactors.
IntActiP30566. 19 interactors.
STRINGi9606.ENSP00000216194.

PTM databases

iPTMnetiP30566.
PhosphoSitePlusiP30566.
SwissPalmiP30566.

Polymorphism and mutation databases

BioMutaiADSL.
DMDMi6686318.

Proteomic databases

EPDiP30566.
PaxDbiP30566.
PeptideAtlasiP30566.
PRIDEiP30566.

Protocols and materials databases

DNASUi158.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342312; ENSP00000341429; ENSG00000239900. [P30566-2]
ENST00000623063; ENSP00000485525; ENSG00000239900. [P30566-1]
GeneIDi158.
KEGGihsa:158.
UCSCiuc003ays.5. human. [P30566-1]

Organism-specific databases

CTDi158.
DisGeNETi158.
GeneCardsiADSL.
HGNCiHGNC:291. ADSL.
HPAiCAB019285.
HPA000525.
MalaCardsiADSL.
MIMi103050. phenotype.
608222. gene.
neXtProtiNX_P30566.
OpenTargetsiENSG00000239900.
Orphaneti46. Adenylosuccinate lyase deficiency.
PharmGKBiPA24600.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
GeneTreeiENSGT00390000013486.
HOGENOMiHOG000033915.
HOVERGENiHBG000214.
InParanoidiP30566.
KOiK01756.
PhylomeDBiP30566.
TreeFamiTF106385.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciMetaCyc:HS02059-MONOMER.
ZFISH:HS02059-MONOMER.
BRENDAi4.3.2.2. 2681.
ReactomeiR-HSA-73817. Purine ribonucleoside monophosphate biosynthesis.
SABIO-RKP30566.

Miscellaneous databases

EvolutionaryTraceiP30566.
GeneWikiiAdenylosuccinate_lyase.
GenomeRNAii158.
PROiP30566.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000239900.
CleanExiHS_ADSL.
ExpressionAtlasiP30566. baseline and differential.
GenevisibleiP30566. HS.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPUR8_HUMAN
AccessioniPrimary (citable) accession number: P30566
Secondary accession number(s): B0QY76, O75495, Q5TI34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 30, 2000
Last modified: November 30, 2016
This is version 185 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.