Skip Header

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

Adenylosuccinate synthetase isozyme 2

Gene

ADSS

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

Catalytic activityi

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(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 isozyme 1 (ADSSL1), Adenylosuccinate synthetase isozyme 2 (ADSS), Adenylosuccinate synthetase isozyme 2 (ADSS), Adenylosuccinate synthetase isozyme 2 (ADSS)
  2. Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase, Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase, 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
  • magnesium ion binding Source: UniProtKB-HAMAP
  • phosphate ion binding Source: UniProtKB

GO - Biological processi

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

BioCyciZFISH:HS00510-MONOMER.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:292. ADSS.

Subcellular locationi

  • Cytoplasm

  • Note: Partially associated with particulate fractions.

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • plasma membrane Source: HPA
Complete GO annotation...

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.

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. 43 interactors.
IntActiP30520. 6 interactors.
MINTiMINT-5004177.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V40X-ray1.90A21-456[»]
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.
OMAiYAIEISG.
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.
InterProiIPR018220. Adenylosuccin_syn_GTP-bd.
IPR033128. Adenylosuccin_syn_Lys_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

        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 rs12134870dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V40X-ray1.90A21-456[»]
ProteinModelPortaliP30520.
SMRiP30520.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106668. 43 interactors.
IntActiP30520. 6 interactors.
MINTiMINT-5004177.
STRINGi9606.ENSP00000355493.

Chemistry databases

BindingDBiP30520.
ChEMBLiCHEMBL4875.
DrugBankiDB00128. L-Aspartic Acid.

PTM databases

iPTMnetiP30520.
PhosphoSitePlusiP30520.
SwissPalmiP30520.

Polymorphism and mutation databases

BioMutaiADSS.
DMDMi21264498.

Proteomic databases

EPDiP30520.
MaxQBiP30520.
PaxDbiP30520.
PeptideAtlasiP30520.
PRIDEiP30520.

Protocols and materials databases

DNASUi159.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366535; ENSP00000355493; ENSG00000035687.
GeneIDi159.
KEGGihsa:159.
UCSCiuc001iaj.4. human.

Organism-specific databases

CTDi159.
DisGeNETi159.
GeneCardsiADSS.
HGNCiHGNC:292. ADSS.
HPAiHPA024400.
MIMi103060. gene.
neXtProtiNX_P30520.
OpenTargetsiENSG00000035687.
PharmGKBiPA24601.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00075; UER00335.
BioCyciZFISH:HS00510-MONOMER.
ReactomeiR-HSA-73817. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

ChiTaRSiADSS. human.
EvolutionaryTraceiP30520.
GenomeRNAii159.
PROiP30520.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000035687.
CleanExiHS_ADSS.
ExpressionAtlasiP30520. baseline and differential.
GenevisibleiP30520. HS.

Family and domain databases

CDDicd03108. AdSS. 1 hit.
HAMAPiMF_00011. Adenylosucc_synth. 1 hit.
MF_03127. Adenylosucc_synth_vert_acid. 1 hit.
InterProiIPR018220. Adenylosuccin_syn_GTP-bd.
IPR033128. Adenylosuccin_syn_Lys_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]
ProtoNetiSearch...

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: November 2, 2016
This is version 172 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.