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Reviewed, UniProtKB/Swiss-Prot P30520 (PURA2_HUMAN)

Last modified June 16, 2009. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Adenylosuccinate synthetase isozyme 2
      Short name=AMPSase 2
      Short name=AdSS 2
    EC=6.3.4.4
Alternative name(s):
    Adenylosuccinate synthetase, acidic isozyme
    IMP--aspartate ligase 2
Gene names
Name: ADSS
Synonyms: ADSS2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis.

Catalytic activity

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm. Note: Partially associated with particulate fractions.

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

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Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processAMP biosynthetic process Ref.1

Inferred from direct assay. Source: UniProtKB

immune system process

Non-traceable author statement. Source: UniProtKB

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding Ref.1

Non-traceable author statement. Source: UniProtKB

adenylosuccinate synthase activity Ref.1

Inferred from direct assay. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphate binding Ref.1

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Adenylosuccinate synthetase isozyme 2
PRO_0000095130

Regions

Nucleotide binding39 – 457GTP Potential

Sites

Active site1731 By similarity
Active site1801 By similarity
Metal binding401Magnesium By similarity
Metal binding671Magnesium; via carbonyl oxygen By similarity

Natural variations

Natural variant1791L → F: dbSNP rs12134870.
VAR_051881

Experimental info

Sequence conflict24 – 252RP → A in CAA47123. Ref.1

Secondary structure

1 ............................................................................... 456
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P30520-1 [UniParc].

Last modified May 27, 2002. Version 3.
Checksum: 23B7AAC58A238783

FASTA45650,097
        10         20         30         40         50         60 
MAFAETYPAA SSLPNGDCGR PRARPGGNRV TVVLGAQWGD EGKGKVVDLL AQDADIVCRC 

        70         80         90        100        110        120 
QGGNNAGHTV VVDSVEYDFH LLPSGIINPN VTAFIGNGVV IHLPGLFEEA EKNVQKGKGL 

       130        140        150        160        170        180 
EGWEKRLIIS DRAHIVFDFH QAADGIQEQQ RQEQAGKNLG TTKKGIGPVY SSKAARSGLR 

       190        200        210        220        230        240 
MCDLVSDFDG FSERFKVLAN QYKSIYPTLE IDIEGELQKL KGYMEKIKPM VRDGVYFLYE 

       250        260        270        280        290        300 
ALHGPPKKIL VEGANAALLD IDFGTYPFVT SSNCTVGGVC TGLGMPPQNV GEVYGVVKAY 

       310        320        330        340        350        360 
TTRVGIGAFP TEQDNEIGEL LQTRGREFGV TTGRKRRCGW LDLVLLKYAH MINGFTALAL 

       370        380        390        400        410        420 
TKLDILDMFT EIKVGVAYKL DGEIIPHIPA NQEVLNKVEV QYKTLPGWNT DISNARAFKE 

       430        440        450 
LPVNAQNYVR FIEDELQIPV KWIGVGKSRE SMIQLF

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase."
Powell S.M., Zalkin H., Dixon J.E.
FEBS Lett. 303:4-10(1992) [PubMed: 1592113] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[2]Stone R.L.
Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[4]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X66503 Genomic DNA. Translation: CAA47123.1.
BC012356 mRNA. Translation: AAH12356.1.
IPIIPI00026833.
PIRS21166.
RefSeqNP_001117.2.
UniGeneHs.498313

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2V40X-ray1.90A21-456[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP30520. 2 interactions.

PTM databases

PhosphoSiteP30520.

Proteomic databases

PeptideAtlasP30520.
PRIDEP30520.

Genome annotation databases

EnsemblENSG00000035687. Homo sapiens. [Contig view]
GeneID159.
KEGGhsa:159.

Organism-specific databases

GeneCardsGC01M242638.
H-InvDBHIX0001748.
HGNCHGNC:292. ADSS.
MIM103060. gene.
PharmGKBPA24601.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP30520.
HOVERGENP30520.
OMAP30520. YVLGIIK.

Enzyme and pathway databases

BRENDA6.3.4.4. 247.
ReactomeREACT_1698. Nucleotide metabolism.

Gene expression databases

ArrayExpressP30520.
BgeeP30520.
CleanExHS_ADSS.
GermOnlineENSG00000035687. Homo sapiens.

Family and domain databases

InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
PANTHERPTHR11846. Asucc_synthtase. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
ProDomPD001188. Asucc_synthtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
TIGRFAMsTIGR00184. purA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00128. L-Aspartic Acid.
NextBio633.
SOURCESearch...

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Entry information

Entry namePURA2_HUMAN
AccessionPrimary (citable) accession number: P30520
Secondary accession number(s): Q96EG7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 27, 2002
Last modified: June 16, 2009
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents