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P30520 (PURA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Adenylosuccinate synthetase, liver isozyme
Short name=L-type adenylosuccinate synthetase
IMP--aspartate ligase 2
Gene names
Name:ADSS
Synonyms:ADSS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. HAMAP-Rule MF_03127

Catalytic activity

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP-Rule MF_03127

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_03127

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP-Rule MF_03127

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_03127

Subcellular location

Cytoplasm. Note: Partially associated with particulate fractions. HAMAP-Rule MF_03127

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' AMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

AMP biosynthetic process

Inferred from direct assay PubMed 2004783. Source: UniProtKB

GTP catabolic process

Inferred from electronic annotation. Source: Ensembl

IMP metabolic process

Inferred from electronic annotation. Source: Ensembl

aspartate metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

immune system process

Non-traceable author statement PubMed 15786719. Source: UniProtKB

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

purine nucleobase metabolic process

Traceable author statement. Source: Reactome

purine ribonucleoside monophosphate biosynthetic process

Traceable author statement. Source: Reactome

response to ammonium ion

Inferred from electronic annotation. Source: Ensembl

response to purine-containing compound

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionGTP binding

Non-traceable author statement PubMed 15786719Ref.1. Source: UniProtKB

adenylosuccinate synthase activity

Inferred from direct assay PubMed 2004783. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phosphate ion binding

Non-traceable author statement PubMed 15786719Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SMYD1Q8NB122EBI-1042898,EBI-8463848

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Adenylosuccinate synthetase isozyme 2 HAMAP-Rule MF_03127
PRO_0000095130

Regions

Nucleotide binding39 – 457GTP HAMAP-Rule MF_03127
Nucleotide binding67 – 693GTP HAMAP-Rule MF_03127
Nucleotide binding362 – 3643GTP HAMAP-Rule MF_03127
Nucleotide binding444 – 4474GTP HAMAP-Rule MF_03127
Region40 – 434IMP binding By similarity
Region65 – 684IMP binding By similarity
Region330 – 3367Substrate binding By similarity

Sites

Active site401Proton acceptor By similarity
Active site681Proton donor By similarity
Metal binding401Magnesium By similarity
Metal binding671Magnesium; via carbonyl oxygen By similarity
Binding site401Substrate By similarity
Binding site1621IMP By similarity
Binding site1761IMP; shared with dimeric partner By similarity
Binding site2551IMP By similarity
Binding site2701IMP By similarity
Binding site3341IMP By similarity
Binding site3361GTP By similarity

Natural variations

Natural variant1791L → F.
Corresponds to variant rs12134870 [ dbSNP | Ensembl ].
VAR_051881

Experimental info

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P30520 [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

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] [Europe PMC] [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 DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Eye.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Human adenylosuccinate synthetase isozyme 2 in complex with GDP."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 21-456 IN COMPLEX WITH GDP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66503 Genomic DNA. Translation: CAA47123.1.
AL591594, AL645465 Genomic DNA. Translation: CAI14037.1.
AL645465, AL591594 Genomic DNA. Translation: CAI15031.1.
CH471148 Genomic DNA. Translation: EAW77102.1.
BC012356 mRNA. Translation: AAH12356.1.
PIRS21166.
RefSeqNP_001117.2. NM_001126.3.
UniGeneHs.498313.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V40X-ray1.90A21-456[»]
ProteinModelPortalP30520.
SMRP30520. Positions 26-456.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106668. 24 interactions.
IntActP30520. 5 interactions.
MINTMINT-5004177.
STRING9606.ENSP00000355493.

Chemistry

BindingDBP30520.
ChEMBLCHEMBL4875.
DrugBankDB00128. L-Aspartic Acid.

PTM databases

PhosphoSiteP30520.

Polymorphism databases

DMDM21264498.

Proteomic databases

PaxDbP30520.
PeptideAtlasP30520.
PRIDEP30520.

Protocols and materials databases

DNASU159.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366535; ENSP00000355493; ENSG00000035687.
GeneID159.
KEGGhsa:159.
UCSCuc001iaj.3. human.

Organism-specific databases

CTD159.
GeneCardsGC01M244571.
HGNCHGNC:292. ADSS.
HPAHPA024400.
MIM103060. gene.
neXtProtNX_P30520.
PharmGKBPA24601.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHOG000260959.
HOVERGENHBG053768.
InParanoidP30520.
KOK01939.
OMAHIPANQE.
OrthoDBEOG7M6D76.
PhylomeDBP30520.
TreeFamTF300486.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00075; UER00335.

Gene expression databases

BgeeP30520.
CleanExHS_ADSS.
GenevestigatorP30520.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
MF_03127. Adenylosucc_synth_vert_acid.
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027529. AdSS_2_vert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11846. PTHR11846. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00184. purA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP30520.
GenomeRNAi159.
NextBio633.
PROP30520.
SOURCESearch...

Entry information

Entry namePURA2_HUMAN
AccessionPrimary (citable) accession number: P30520
Secondary accession number(s): B1AQM5, Q96EG7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 27, 2002
Last modified: April 16, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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