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P30520

- PURA2_HUMAN

UniProt

P30520 - PURA2_HUMAN

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Protein
Adenylosuccinate synthetase isozyme 2
Gene
ADSS, ADSS2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei40 – 401Proton acceptor By similarity
Metal bindingi40 – 401Magnesium By similarity
Binding sitei40 – 401Substrate By similarity
Metal bindingi67 – 671Magnesium; via carbonyl oxygen By similarity
Active sitei68 – 681Proton donor By similarity
Binding sitei162 – 1621IMP By similarity
Binding sitei176 – 1761IMP; shared with dimeric partner By similarity
Binding sitei255 – 2551IMP By similarity
Binding sitei270 – 2701IMP By similarity
Binding sitei334 – 3341IMP By similarity
Binding sitei336 – 3361GTP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 457GTPUniRule annotation
Nucleotide bindingi67 – 693GTPUniRule annotation
Nucleotide bindingi362 – 3643GTPUniRule annotation
Nucleotide bindingi444 – 4474GTPUniRule annotation

GO - Molecular functioni

  1. GTP binding Source: UniProtKB
  2. adenylosuccinate synthase activity Source: UniProtKB
  3. magnesium ion binding Source: UniProtKB-HAMAP
  4. phosphate ion binding Source: UniProtKB
  5. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
  2. AMP biosynthetic process Source: UniProtKB
  3. GTP catabolic process Source: Ensembl
  4. IMP metabolic process Source: Ensembl
  5. aspartate metabolic process Source: Ensembl
  6. cellular response to electrical stimulus Source: Ensembl
  7. immune system process Source: UniProtKB
  8. nucleobase-containing small molecule metabolic process Source: Reactome
  9. purine nucleobase metabolic process Source: Reactome
  10. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
  11. response to ammonium ion Source: Ensembl
  12. response to purine-containing compound Source: Ensembl
  13. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00075; UER00335.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate synthetase isozyme 2 (EC:6.3.4.4)
Short name:
AMPSase 2
Short name:
AdSS 2
Alternative name(s):
Adenylosuccinate synthetase, acidic isozyme
Adenylosuccinate synthetase, liver isozyme
Short name:
L-type adenylosuccinate synthetase
IMP--aspartate ligase 2
Gene namesi
Name:ADSS
Synonyms:ADSS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:292. ADSS.

Subcellular locationi

Cytoplasm
Note: Partially associated with particulate fractions.UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24601.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Adenylosuccinate synthetase isozyme 2UniRule annotation
PRO_0000095130Add
BLAST

Proteomic databases

MaxQBiP30520.
PaxDbiP30520.
PeptideAtlasiP30520.
PRIDEiP30520.

PTM databases

PhosphoSiteiP30520.

Expressioni

Gene expression databases

BgeeiP30520.
CleanExiHS_ADSS.
GenevestigatoriP30520.

Organism-specific databases

HPAiHPA024400.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
SMYD1Q8NB122EBI-1042898,EBI-8463848

Protein-protein interaction databases

BioGridi106668. 24 interactions.
IntActiP30520. 5 interactions.
MINTiMINT-5004177.
STRINGi9606.ENSP00000355493.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 3910
Helixi43 – 519
Beta strandi55 – 595
Beta strandi68 – 725
Beta strandi75 – 828
Helixi84 – 874
Beta strandi92 – 954
Beta strandi99 – 1024
Helixi103 – 11614
Helixi118 – 1203
Helixi123 – 1253
Beta strandi126 – 1305
Beta strandi134 – 1363
Helixi138 – 14912
Helixi166 – 1749
Helixi181 – 1844
Helixi188 – 20518
Helixi213 – 22715
Helixi228 – 2303
Helixi234 – 24310
Beta strandi249 – 2524
Helixi257 – 2593
Turni261 – 2633
Helixi277 – 2837
Helixi287 – 2893
Beta strandi290 – 30718
Helixi316 – 3249
Turni330 – 3323
Beta strandi337 – 3393
Helixi343 – 35311
Beta strandi356 – 3616
Helixi363 – 3686
Beta strandi370 – 38011
Beta strandi383 – 3875
Helixi392 – 3954
Beta strandi399 – 4068
Helixi418 – 4203
Helixi423 – 43614
Beta strandi440 – 4445
Beta strandi446 – 4483
Beta strandi451 – 4544

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V40X-ray1.90A21-456[»]
ProteinModelPortaliP30520.
SMRiP30520. Positions 26-456.

Miscellaneous databases

EvolutionaryTraceiP30520.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 434IMP binding By similarity
Regioni65 – 684IMP binding By similarity
Regioni330 – 3367Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0104.
HOGENOMiHOG000260959.
HOVERGENiHBG053768.
InParanoidiP30520.
KOiK01939.
OMAiNARAFKE.
OrthoDBiEOG7M6D76.
PhylomeDBiP30520.
TreeFamiTF300486.

Family and domain databases

HAMAPiMF_00011. Adenylosucc_synth.
MF_03127. Adenylosucc_synth_vert_acid.
InterProiIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027529. AdSS_2_vert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11846. PTHR11846. 1 hit.
PfamiPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTiSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00184. purA. 1 hit.
PROSITEiPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30520-1 [UniParc]FASTAAdd to Basket

« Hide

MAFAETYPAA SSLPNGDCGR PRARPGGNRV TVVLGAQWGD EGKGKVVDLL    50
AQDADIVCRC QGGNNAGHTV VVDSVEYDFH LLPSGIINPN VTAFIGNGVV 100
IHLPGLFEEA EKNVQKGKGL EGWEKRLIIS DRAHIVFDFH QAADGIQEQQ 150
RQEQAGKNLG TTKKGIGPVY SSKAARSGLR MCDLVSDFDG FSERFKVLAN 200
QYKSIYPTLE IDIEGELQKL KGYMEKIKPM VRDGVYFLYE ALHGPPKKIL 250
VEGANAALLD IDFGTYPFVT SSNCTVGGVC TGLGMPPQNV GEVYGVVKAY 300
TTRVGIGAFP TEQDNEIGEL LQTRGREFGV TTGRKRRCGW LDLVLLKYAH 350
MINGFTALAL TKLDILDMFT EIKVGVAYKL DGEIIPHIPA NQEVLNKVEV 400
QYKTLPGWNT DISNARAFKE LPVNAQNYVR FIEDELQIPV KWIGVGKSRE 450
SMIQLF 456
Length:456
Mass (Da):50,097
Last modified:May 27, 2002 - v3
Checksum:i23B7AAC58A238783
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti179 – 1791L → F.
Corresponds to variant rs12134870 [ dbSNP | Ensembl ].
VAR_051881

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 252RP → A in CAA47123. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1624.1.
PIRiS21166.
RefSeqiNP_001117.2. NM_001126.3.
UniGeneiHs.498313.

Genome annotation databases

EnsembliENST00000366535; ENSP00000355493; ENSG00000035687.
GeneIDi159.
KEGGihsa:159.
UCSCiuc001iaj.3. human.

Polymorphism databases

DMDMi21264498.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1624.1.
PIRi S21166.
RefSeqi NP_001117.2. NM_001126.3.
UniGenei Hs.498313.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V40 X-ray 1.90 A 21-456 [» ]
ProteinModelPortali P30520.
SMRi P30520. Positions 26-456.
ModBasei Search...

Protein-protein interaction databases

BioGridi 106668. 24 interactions.
IntActi P30520. 5 interactions.
MINTi MINT-5004177.
STRINGi 9606.ENSP00000355493.

Chemistry

BindingDBi P30520.
ChEMBLi CHEMBL4875.
DrugBanki DB00128. L-Aspartic Acid.

PTM databases

PhosphoSitei P30520.

Polymorphism databases

DMDMi 21264498.

Proteomic databases

MaxQBi P30520.
PaxDbi P30520.
PeptideAtlasi P30520.
PRIDEi P30520.

Protocols and materials databases

DNASUi 159.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366535 ; ENSP00000355493 ; ENSG00000035687 .
GeneIDi 159.
KEGGi hsa:159.
UCSCi uc001iaj.3. human.

Organism-specific databases

CTDi 159.
GeneCardsi GC01M244571.
HGNCi HGNC:292. ADSS.
HPAi HPA024400.
MIMi 103060. gene.
neXtProti NX_P30520.
PharmGKBi PA24601.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0104.
HOGENOMi HOG000260959.
HOVERGENi HBG053768.
InParanoidi P30520.
KOi K01939.
OMAi NARAFKE.
OrthoDBi EOG7M6D76.
PhylomeDBi P30520.
TreeFami TF300486.

Enzyme and pathway databases

UniPathwayi UPA00075 ; UER00335 .
Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

EvolutionaryTracei P30520.
GenomeRNAii 159.
NextBioi 633.
PROi P30520.
SOURCEi Search...

Gene expression databases

Bgeei P30520.
CleanExi HS_ADSS.
Genevestigatori P30520.

Family and domain databases

HAMAPi MF_00011. Adenylosucc_synth.
MF_03127. Adenylosucc_synth_vert_acid.
InterProi IPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027529. AdSS_2_vert.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR11846. PTHR11846. 1 hit.
Pfami PF00709. Adenylsucc_synt. 1 hit.
[Graphical view ]
SMARTi SM00788. Adenylsucc_synt. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00184. purA. 1 hit.
PROSITEi PS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiPURA2_HUMAN
AccessioniPrimary (citable) accession number: P30520
Secondary accession number(s): B1AQM5, Q96EG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 27, 2002
Last modified: September 3, 2014
This is version 148 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

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