Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P30566

- PUR8_HUMAN

UniProt

P30566 - PUR8_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Adenylosuccinate lyase

Gene

ADSL

Organism
Homo sapiens (Human)
Status
Reviewed - 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.

Catalytic activityi

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

Enzyme regulationi

The enzyme reaction kinetics indicate cooperativity between subunits.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei159 – 1591Proton donor/acceptor1 Publication
Binding sitei241 – 2411Substrate
Active sitei289 – 2891Proton donor/acceptor1 Publication
Binding sitei303 – 3031Substrate; shared with neighboring subunit
Binding sitei329 – 3291Substrate
Binding sitei334 – 3341Substrate
Binding sitei338 – 3381Substrate

GO - Molecular functioni

  1. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Source: UniProtKB-EC
  2. N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Source: UniProtKB

GO - Biological processi

  1. 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
  2. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  3. aerobic respiration Source: Ensembl
  4. AMP biosynthetic process Source: UniProtKB
  5. metabolic process Source: GOC
  6. nucleobase-containing small molecule metabolic process Source: Reactome
  7. protein tetramerization Source: UniProtKB
  8. purine nucleobase metabolic process Source: Reactome
  9. purine nucleotide biosynthetic process Source: UniProtKB
  10. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
  11. response to hypoxia Source: Ensembl
  12. response to muscle activity Source: Ensembl
  13. response to nutrient Source: Ensembl
  14. response to starvation Source: Ensembl
  15. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:HS02059-MONOMER.
ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
SABIO-RKP30566.
UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate lyase (EC:4.3.2.2)
Short name:
ASL
Alternative name(s):
Adenylosuccinase
Short name:
ASase
Gene namesi
Name:ADSL
Synonyms:AMPS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:291. ADSL.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Adenylosuccinase deficiency (ADSL deficiency) [MIM:103050]: An 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.7 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21A → V in ADSL deficiency; severe.
Corresponds to variant rs143083947 [ dbSNP | Ensembl ].
VAR_016930
Natural varianti3 – 31A → V in ADSL deficiency; severe. 1 Publication
VAR_017078
Natural varianti26 – 261M → L in ADSL deficiency; severe.
VAR_016931
Natural varianti72 – 721I → V in ADSL deficiency; severe. 1 Publication
VAR_007972
Natural varianti100 – 1001P → A in ADSL deficiency; moderate. 1 Publication
VAR_017079
Natural varianti114 – 1141Y → H in ADSL deficiency; severe. Total loss of activity. 1 Publication
VAR_017080
Natural varianti141 – 1411R → W in ADSL deficiency; severe. 1 Publication
VAR_007973
Natural varianti190 – 1901R → Q in ADSL deficiency; moderate. 2 Publications
Corresponds to variant rs28941471 [ dbSNP | Ensembl ].
VAR_007974
Natural varianti194 – 1941R → C in ADSL deficiency; severe. Reduces protein stability. 1 Publication
VAR_017081
Natural varianti246 – 2461K → E in ADSL deficiency; moderate. Strongly reduced catalytic activity. 1 Publication
VAR_007975
Natural varianti268 – 2681D → N in ADSL deficiency; severe. Total loss of activity. 1 Publication
VAR_017082
Natural varianti303 – 3031R → C in ADSL deficiency; mild. Strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR. Abolishes cooperativity. 1 Publication
VAR_007976
Natural varianti311 – 3111L → V in ADSL deficiency; severe. Slightly reduced enzyme activity. 1 Publication
VAR_017083
Natural varianti318 – 3181P → L in ADSL deficiency; severe.
VAR_017084
Natural varianti364 – 3641V → M in ADSL deficiency; severe. 1 Publication
VAR_017085
Natural varianti374 – 3741R → W in ADSL deficiency; severe.
VAR_017086
Natural varianti395 – 3951S → R in ADSL deficiency; severe. 1 Publication
VAR_007977
Natural varianti396 – 3961R → C in ADSL deficiency; severe. Abolishes cooperativity and reduces enzyme activity.
VAR_017087
Natural varianti396 – 3961R → H in ADSL deficiency; severe. Abolishes cooperativity and reduces enzyme activity. 1 Publication
VAR_017088
Natural varianti422 – 4221D → Y in ADSL deficiency; moderate. 1 Publication
VAR_017089
Natural varianti423 – 4231L → V in ADSL deficiency; moderate.
VAR_017090
Natural varianti426 – 4261R → H in ADSL deficiency; severe. Most frequent mutation. 4 Publications
VAR_007978
Natural varianti430 – 4301D → N in ADSL deficiency; mild. 1 Publication
VAR_017091
Natural varianti438 – 4381S → P in ADSL deficiency; severe. 1 Publication
VAR_000680
Natural varianti447 – 4471S → P in ADSL deficiency; severe.
VAR_017092
Natural varianti450 – 4501T → S in ADSL deficiency; moderate.
VAR_016932
Natural varianti452 – 4521R → P in ADSL deficiency; severe. 1 Publication
VAR_017093

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

MIMi103050. phenotype.
Orphaneti46. Adenylosuccinate lyase deficiency.
PharmGKBiPA24600.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 484483Adenylosuccinate lyasePRO_0000137892Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei147 – 1471N6-acetyllysine1 Publication
Modified residuei295 – 2951N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP30566.
PaxDbiP30566.
PeptideAtlasiP30566.
PRIDEiP30566.

PTM databases

PhosphoSiteiP30566.

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

BgeeiP30566.
CleanExiHS_ADSL.
ExpressionAtlasiP30566. baseline and differential.
GenevestigatoriP30566.

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. 34 interactions.
IntActiP30566. 4 interactions.
STRINGi9606.ENSP00000216194.

Structurei

Secondary structure

1
484
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 194Combined sources
Helixi24 – 296Combined sources
Helixi32 – 5322Combined sources
Helixi59 – 668Combined sources
Beta strandi68 – 703Combined sources
Helixi74 – 8411Combined sources
Helixi87 – 9812Combined sources
Turni100 – 1023Combined sources
Helixi103 – 1053Combined sources
Turni106 – 1094Combined sources
Helixi113 – 14836Combined sources
Turni149 – 1513Combined sources
Beta strandi153 – 1586Combined sources
Beta strandi161 – 1677Combined sources
Helixi168 – 19225Combined sources
Beta strandi201 – 2044Combined sources
Helixi206 – 2116Combined sources
Turni212 – 2143Combined sources
Helixi216 – 22914Combined sources
Beta strandi240 – 2423Combined sources
Helixi246 – 27429Combined sources
Beta strandi277 – 2793Combined sources
Helixi299 – 31315Combined sources
Helixi316 – 3238Combined sources
Helixi331 – 3333Combined sources
Helixi334 – 36027Combined sources
Helixi366 – 38015Combined sources
Helixi382 – 3898Combined sources
Helixi396 – 41621Combined sources
Helixi423 – 4297Combined sources
Helixi431 – 4333Combined sources
Helixi434 – 4374Combined sources
Helixi440 – 4434Combined sources
Helixi446 – 4494Combined sources
Helixi453 – 46311Combined sources
Helixi465 – 4695Combined sources
Helixi470 – 4723Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 5-474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30566.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 212Substrate binding; shared with neighboring subunit
Regioni85 – 873Substrate binding
Regioni111 – 1122Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0015.
GeneTreeiENSGT00390000013486.
HOGENOMiHOG000033915.
HOVERGENiHBG000214.
InParanoidiP30566.
KOiK01756.
OrthoDBiEOG7GQXVD.
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. Align

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 AAC60603.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA46697.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21A → V in ADSL deficiency; severe.
Corresponds to variant rs143083947 [ dbSNP | Ensembl ].
VAR_016930
Natural varianti3 – 31A → V in ADSL deficiency; severe. 1 Publication
VAR_017078
Natural varianti26 – 261M → L in ADSL deficiency; severe.
VAR_016931
Natural varianti31 – 311S → N.
Corresponds to variant rs5757921 [ dbSNP | Ensembl ].
VAR_037883
Natural varianti72 – 721I → V in ADSL deficiency; severe. 1 Publication
VAR_007972
Natural varianti100 – 1001P → A in ADSL deficiency; moderate. 1 Publication
VAR_017079
Natural varianti114 – 1141Y → H in ADSL deficiency; severe. Total loss of activity. 1 Publication
VAR_017080
Natural varianti141 – 1411R → W in ADSL deficiency; severe. 1 Publication
VAR_007973
Natural varianti147 – 1471K → M.
Corresponds to variant rs11089991 [ dbSNP | Ensembl ].
VAR_037884
Natural varianti190 – 1901R → Q in ADSL deficiency; moderate. 2 Publications
Corresponds to variant rs28941471 [ dbSNP | Ensembl ].
VAR_007974
Natural varianti194 – 1941R → C in ADSL deficiency; severe. Reduces protein stability. 1 Publication
VAR_017081
Natural varianti246 – 2461K → E in ADSL deficiency; moderate. Strongly reduced catalytic activity. 1 Publication
VAR_007975
Natural varianti268 – 2681D → N in ADSL deficiency; severe. Total loss of activity. 1 Publication
VAR_017082
Natural varianti303 – 3031R → C in ADSL deficiency; mild. Strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR. Abolishes cooperativity. 1 Publication
VAR_007976
Natural varianti311 – 3111L → V in ADSL deficiency; severe. Slightly reduced enzyme activity. 1 Publication
VAR_017083
Natural varianti318 – 3181P → L in ADSL deficiency; severe.
VAR_017084
Natural varianti364 – 3641V → M in ADSL deficiency; severe. 1 Publication
VAR_017085
Natural varianti374 – 3741R → W in ADSL deficiency; severe.
VAR_017086
Natural varianti395 – 3951S → R in ADSL deficiency; severe. 1 Publication
VAR_007977
Natural varianti396 – 3961R → C in ADSL deficiency; severe. Abolishes cooperativity and reduces enzyme activity.
VAR_017087
Natural varianti396 – 3961R → H in ADSL deficiency; severe. Abolishes cooperativity and reduces enzyme activity. 1 Publication
VAR_017088
Natural varianti422 – 4221D → Y in ADSL deficiency; moderate. 1 Publication
VAR_017089
Natural varianti423 – 4231L → V in ADSL deficiency; moderate.
VAR_017090
Natural varianti426 – 4261R → H in ADSL deficiency; severe. Most frequent mutation. 4 Publications
VAR_007978
Natural varianti430 – 4301D → N in ADSL deficiency; mild. 1 Publication
VAR_017091
Natural varianti438 – 4381S → P in ADSL deficiency; severe. 1 Publication
VAR_000680
Natural varianti447 – 4471S → P in ADSL deficiency; severe.
VAR_017092
Natural varianti450 – 4501T → S in ADSL deficiency; moderate.
VAR_016932
Natural varianti452 – 4521R → P in ADSL deficiency; severe. 1 Publication
VAR_017093

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei398 – 45659Missing in isoform 2. 2 PublicationsVSP_000318Add
BLAST

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_000026.2. [P30566-1]
NP_001116850.1. NM_001123378.1. [P30566-2]
UniGeneiHs.75527.

Genome annotation databases

EnsembliENST00000342312; ENSP00000341429; ENSG00000239900. [P30566-2]
ENST00000623063; ENSP00000485525; ENSG00000239900. [P30566-1]
GeneIDi158.
KEGGihsa:158.
UCSCiuc003ayp.4. human. [P30566-1]
uc003ays.4. human. [P30566-2]

Polymorphism databases

DMDMi6686318.

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.
CCDSi CCDS14001.1. [P30566-1 ]
CCDS46714.1. [P30566-2 ]
RefSeqi NP_000017.1. NM_000026.2. [P30566-1 ]
NP_001116850.1. NM_001123378.1. [P30566-2 ]
UniGenei Hs.75527.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2J91 X-ray 1.80 A/B/C/D 1-481 [» ]
2VD6 X-ray 2.00 A/B/C/D 1-481 [» ]
4FFX X-ray 2.70 A/B/C/D 1-484 [» ]
4FLC X-ray 2.60 A/B/C/D 1-484 [» ]
ProteinModelPortali P30566.
SMRi P30566. Positions 5-474.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106667. 34 interactions.
IntActi P30566. 4 interactions.
STRINGi 9606.ENSP00000216194.

PTM databases

PhosphoSitei P30566.

Polymorphism databases

DMDMi 6686318.

Proteomic databases

MaxQBi P30566.
PaxDbi P30566.
PeptideAtlasi P30566.
PRIDEi P30566.

Protocols and materials databases

DNASUi 158.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000342312 ; ENSP00000341429 ; ENSG00000239900 . [P30566-2 ]
ENST00000623063 ; ENSP00000485525 ; ENSG00000239900 . [P30566-1 ]
GeneIDi 158.
KEGGi hsa:158.
UCSCi uc003ayp.4. human. [P30566-1 ]
uc003ays.4. human. [P30566-2 ]

Organism-specific databases

CTDi 158.
GeneCardsi GC22P040742.
HGNCi HGNC:291. ADSL.
HPAi CAB019285.
HPA000525.
MIMi 103050. phenotype.
608222. gene.
neXtProti NX_P30566.
Orphaneti 46. Adenylosuccinate lyase deficiency.
PharmGKBi PA24600.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0015.
GeneTreei ENSGT00390000013486.
HOGENOMi HOG000033915.
HOVERGENi HBG000214.
InParanoidi P30566.
KOi K01756.
OrthoDBi EOG7GQXVD.
PhylomeDBi P30566.
TreeFami TF106385.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00132 .
UPA00075 ; UER00336 .
BioCyci MetaCyc:HS02059-MONOMER.
Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.
SABIO-RK P30566.

Miscellaneous databases

EvolutionaryTracei P30566.
GeneWikii Adenylosuccinate_lyase.
GenomeRNAii 158.
NextBioi 629.
PROi P30566.
SOURCEi Search...

Gene expression databases

Bgeei P30566.
CleanExi HS_ADSL.
ExpressionAtlasi P30566. baseline and differential.
Genevestigatori P30566.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
InterProi IPR019468. 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 ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SMARTi SM00998. ADSL_C. 1 hit.
[Graphical view ]
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00928. purB. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mapping of the human adenylosuccinate lyase (ADSL) gene to chromosome 22q13.1-->q13.2."
    Fon E.A., Demczuk S., Delattre O., Thomas G., Rouleau G.A.
    Cytogenet. Cell Genet. 64:201-203(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Human adenylosuccinate lyase (ADSL), cloning and characterization of full-length cDNA and its isoform, gene structure and molecular basis for ADSL deficiency in six patients."
    Kmoch S., Hartmannova H., Stiburkova B., Krijt J., Zikanova M., Sebesta I.
    Hum. Mol. Genet. 9:1501-1513(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS ADSL DEFICIENCY VAL-3; HIS-114; GLN-190; CYS-194; ASN-268; HIS-426 AND ASN-430.
    Tissue: Skeletal muscle.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Eye.
  7. "A mutation in adenylosuccinate lyase associated with mental retardation and autistic features."
    Stone R.L., Aimi J., Barshop B.A., Jaeken J., van den Berghe G., Zalkin H., Dixon J.E.
    Nat. Genet. 1:59-63(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-484 (ISOFORM 1), VARIANT ADSL DEFICIENCY PRO-438.
  8. Bienvenut W.V., Ramsay A., Leung H.Y.
    Submitted (JUN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-20 AND 235-245, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  9. "Expression, purification, and characterization of stable, recombinant human adenylosuccinate lyase."
    Lee P., Colman R.F.
    Protein Expr. Purif. 51:227-234(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBUNIT.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147 AND LYS-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Human adenylosuccinate lyase in complex with its substrate N6-(1,2-dicarboxyethyl)-AMP, and its products AMP and fumarate."
    Structural genomics consortium (SGC)
    Submitted (SEP-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE; FUMARATE AND AMP.
  14. "Structural and biochemical characterization of human adenylosuccinate lyase (ADSL) and the R303C ADSL deficiency-associated mutation."
    Ray S.P., Deaton M.K., Capodagli G.C., Calkins L.A., Sawle L., Ghosh K., Patterson D., Pegan S.D.
    Biochemistry 51:6701-6713(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF WILD-TYPE AND VARIANT ADSL DEFICIENCY CYS-303, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT ADSL DEFICIENCY CYS-303, ACTIVE SITE, ENZYME REGULATION, SUBUNIT.
  15. Cited for: VARIANT ADSL DEFICIENCY HIS-426.
  16. "Identification of new mutations in the adenylosuccinate lyase gene associated with impaired enzyme activity in lymphocytes and red blood cells."
    Verginelli D., Luckow B., Crifo C., Salerno C., Gross M.
    Biochim. Biophys. Acta 1406:81-84(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ADSL DEFICIENCY ALA-100 AND TYR-422.
  17. "Mutation analysis in adenylosuccinate lyase deficiency: eight novel mutations in the re-evaluated full ADSL coding sequence."
    Marie S., Cuppens H., Heuterspreute M., Jaspers M., Tola E.Z., Gu X.X., Legius E., Vincent M.-F., Jaeken J., Cassiman J.-J., van den Berghe G.
    Hum. Mutat. 13:197-202(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ADSL DEFICIENCY VAL-72; TRP-141; GLN-190; GLU-246; CYS-303; ARG-395 AND HIS-426.
  18. "Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency."
    Race V., Marie S., Vincent M.-F., Van den Berghe G.
    Hum. Mol. Genet. 9:2159-2165(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS ADSL DEFICIENCY VAL-2; LEU-26; TRP-141; CYS-303; ARG-395; HIS-426 AND SER-450.
  19. "Screening for adenylosuccinate lyase deficiency: clinical, biochemical and molecular findings in four patients."
    Castro M., Perez-Cerda C., Merinero B., Garcia M.J., Bernar J., Gil Nagel A., Torres J., Bermudez M., Garavito P., Marie S., Vincent F., Van den Berghe G., Ugarte M.
    Neuropediatrics 33:186-189(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ADSL DEFICIENCY VAL-311; MET-364; HIS-396 AND PRO-452.
  20. "Intrafamilial variability in the phenotypic expression of adenylosuccinate lyase deficiency: a report on three patients."
    Edery P., Chabrier S., Ceballos-Picot I., Marie S., Vincent M.-F., Tardieu M.
    Am. J. Med. Genet. A 120:185-190(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ADSL DEFICIENCY HIS-426.
  21. "Biochemical and biophysical analysis of five disease-associated human adenylosuccinate lyase mutants."
    Ariyananda Lde Z., Lee P., Antonopoulos C., Colman R.F.
    Biochemistry 48:5291-5302(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS ADSL DEFICIENCY CYS-194; GLU-246; VAL-311; CYS-396 AND HIS-396, ENZYME REGULATION.

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 26, 2014
This is version 163 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

External Data

Dasty 3