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UniProtKB - P30520 (PURA2_HUMAN)

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Protein

Adenylosuccinate synthetase isozyme 2

Gene

ADSS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.

Catalytic activityi

GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Pathwayi: AMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes AMP from IMP.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Adenylosuccinate synthetase (purA), Adenylosuccinate synthetase, 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 (purB), 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei40Proton acceptorUniRule annotation1
Metal bindingi40MagnesiumUniRule annotation1
Binding sitei40SubstrateUniRule annotation1
Metal bindingi67Magnesium; via carbonyl oxygenUniRule annotation1
Active sitei68Proton donorUniRule annotation1
Binding sitei162IMPUniRule annotation1
Binding sitei176IMP; shared with dimeric partnerUniRule annotation1
Binding sitei255IMPUniRule annotation1
Binding sitei270IMPUniRule annotation1
Binding sitei334IMPUniRule annotation1
Binding sitei336GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi39 – 45GTP7
Nucleotide bindingi67 – 69GTP3
Nucleotide bindingi362 – 364GTP3
Nucleotide bindingi444 – 447GTP4

GO - Molecular functioni

  • adenylosuccinate synthase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • phosphate ion binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionLigase
Biological processPurine biosynthesis
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-73817 Purine ribonucleoside monophosphate biosynthesis
UniPathwayiUPA00075; UER00335

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate synthetase isozyme 2UniRule annotation (EC:6.3.4.4UniRule annotation)
Short name:
AMPSase 2UniRule annotation
Short name:
AdSS 2UniRule annotation
Alternative name(s):
Adenylosuccinate synthetase, acidic isozymeUniRule annotation
Adenylosuccinate synthetase, liver isozymeUniRule annotation
Short name:
L-type adenylosuccinate synthetaseUniRule annotation
IMP--aspartate ligase 2UniRule annotation
Gene namesi
Name:ADSSUniRule annotation
Synonyms:ADSS2UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000035687.9
HGNCiHGNC:292 ADSS
MIMi103060 gene
neXtProtiNX_P30520

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi159
OpenTargetsiENSG00000035687
PharmGKBiPA24601

Chemistry databases

ChEMBLiCHEMBL4875
DrugBankiDB00128 L-Aspartic Acid

Polymorphism and mutation databases

BioMutaiADSS
DMDMi21264498

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000951301 – 456Adenylosuccinate synthetase isozyme 2Add BLAST456

Proteomic databases

EPDiP30520
MaxQBiP30520
PaxDbiP30520
PeptideAtlasiP30520
PRIDEiP30520
ProteomicsDBi54711

PTM databases

iPTMnetiP30520
PhosphoSitePlusiP30520
SwissPalmiP30520

Expressioni

Gene expression databases

BgeeiENSG00000035687
CleanExiHS_ADSS
ExpressionAtlasiP30520 baseline and differential
GenevisibleiP30520 HS

Organism-specific databases

HPAiHPA024400

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Binary interactionsi

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

Protein-protein interaction databases

BioGridi106668, 45 interactors
IntActiP30520, 9 interactors
MINTiP30520
STRINGi9606.ENSP00000355493

Chemistry databases

BindingDBiP30520

Structurei

Secondary structure

1456
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 39Combined sources10
Helixi43 – 51Combined sources9
Beta strandi55 – 59Combined sources5
Beta strandi68 – 72Combined sources5
Beta strandi75 – 82Combined sources8
Helixi84 – 87Combined sources4
Beta strandi92 – 95Combined sources4
Beta strandi99 – 102Combined sources4
Helixi103 – 116Combined sources14
Helixi118 – 120Combined sources3
Helixi123 – 125Combined sources3
Beta strandi126 – 130Combined sources5
Beta strandi134 – 136Combined sources3
Helixi138 – 149Combined sources12
Helixi166 – 174Combined sources9
Helixi181 – 184Combined sources4
Helixi188 – 205Combined sources18
Helixi213 – 227Combined sources15
Helixi228 – 230Combined sources3
Helixi234 – 243Combined sources10
Beta strandi249 – 252Combined sources4
Helixi257 – 259Combined sources3
Turni261 – 263Combined sources3
Helixi277 – 283Combined sources7
Helixi287 – 289Combined sources3
Beta strandi290 – 307Combined sources18
Helixi316 – 324Combined sources9
Turni330 – 332Combined sources3
Beta strandi337 – 339Combined sources3
Helixi343 – 353Combined sources11
Beta strandi356 – 361Combined sources6
Helixi363 – 368Combined sources6
Beta strandi370 – 380Combined sources11
Beta strandi383 – 387Combined sources5
Helixi392 – 395Combined sources4
Beta strandi399 – 406Combined sources8
Helixi418 – 420Combined sources3
Helixi423 – 436Combined sources14
Beta strandi440 – 444Combined sources5
Beta strandi446 – 448Combined sources3
Beta strandi451 – 454Combined sources4

3D structure databases

ProteinModelPortaliP30520
SMRiP30520
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30520

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni40 – 43IMP bindingUniRule annotation4
Regioni65 – 68IMP bindingUniRule annotation4
Regioni330 – 336Substrate bindingUniRule annotation7

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG1355 Eukaryota
COG0104 LUCA
GeneTreeiENSGT00390000015553
HOGENOMiHOG000260959
HOVERGENiHBG053768
InParanoidiP30520
KOiK01939
OMAiGIAPFYS
OrthoDBiEOG091G1BIK
PhylomeDBiP30520
TreeFamiTF300486

Family and domain databases

CDDicd03108 AdSS, 1 hit
HAMAPiMF_00011 Adenylosucc_synth, 1 hit
MF_03127 Adenylosucc_synth_vert_acid, 1 hit
InterProiView protein in InterPro
IPR018220 Adenylosuccin_syn_GTP-bd
IPR033128 Adenylosuccin_syn_Lys_AS
IPR001114 Adenylosuccinate_synthetase
IPR027529 AdSS_2_vert
IPR027417 P-loop_NTPase
PANTHERiPTHR11846 PTHR11846, 1 hit
PfamiView protein in Pfam
PF00709 Adenylsucc_synt, 1 hit
SMARTiView protein in SMART
SM00788 Adenylsucc_synt, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00184 purA, 1 hit
PROSITEiView protein in PROSITE
PS01266 ADENYLOSUCCIN_SYN_1, 1 hit
PS00513 ADENYLOSUCCIN_SYN_2, 1 hit

Sequencei

Sequence statusi: Complete.

P30520-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFAETYPAA SSLPNGDCGR PRARPGGNRV TVVLGAQWGD EGKGKVVDLL 
        60         70         80         90        100
AQDADIVCRC QGGNNAGHTV VVDSVEYDFH LLPSGIINPN VTAFIGNGVV 
       110        120        130        140        150
IHLPGLFEEA EKNVQKGKGL EGWEKRLIIS DRAHIVFDFH QAADGIQEQQ 
       160        170        180        190        200
RQEQAGKNLG TTKKGIGPVY SSKAARSGLR MCDLVSDFDG FSERFKVLAN 
       210        220        230        240        250
QYKSIYPTLE IDIEGELQKL KGYMEKIKPM VRDGVYFLYE ALHGPPKKIL 
       260        270        280        290        300
VEGANAALLD IDFGTYPFVT SSNCTVGGVC TGLGMPPQNV GEVYGVVKAY 
       310        320        330        340        350
TTRVGIGAFP TEQDNEIGEL LQTRGREFGV TTGRKRRCGW LDLVLLKYAH 
       360        370        380        390        400
MINGFTALAL TKLDILDMFT EIKVGVAYKL DGEIIPHIPA NQEVLNKVEV 
       410        420        430        440        450
QYKTLPGWNT DISNARAFKE LPVNAQNYVR FIEDELQIPV KWIGVGKSRE 

SMIQLF
Length:456
Mass (Da):50,097
Last modified:May 27, 2002 - v3
Checksum:i23B7AAC58A238783
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24 – 25RP → A in CAA47123 (PubMed:1592113).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051881179L → F. Corresponds to variant dbSNP:rs12134870Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66503 Genomic DNA Translation: CAA47123.1
AL591594 Genomic DNA No translation available.
AL645465 Genomic DNA No translation available.
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.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPURA2_HUMAN
AccessioniPrimary (citable) accession number: P30520
Secondary accession number(s): B1AQM5, Q96EG7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 27, 2002
Last modified: July 18, 2018
This is version 185 of the entry and version 3 of the sequence. See 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

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