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UniProtKB/Swiss-Prot entry P30520


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PURA2_HUMAN
Primary accession number P30520
Secondary accession number Q96EG7
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on May 27, 2002 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 90)
Name and origin of the protein
Protein name Adenylosuccinate synthetase isozyme 2
Synonyms AdSS 2
EC 6.3.4.4
Adenylosuccinate synthetase, acidic isozyme
IMP--aspartate ligase 2
AMPSase 2
Gene name
Name: ADSS
Synonyms: ADSS2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
DOI=10.1016/0014-5793(92)80465-S; PubMed=1592113 [NCBI, ExPASy, EBI, Israel, Japan]
Powell S.M., Zalkin H., Dixon J.E.;
"Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase.";
FEBS Lett. 303:4-10(1992).
[2]
SEQUENCE REVISION.
Stone R.L.;
Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X66503; CAA47123.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012356; AAH12356.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S21166; S21166.
RefSeq NP_001117.2; -.
UniGene Hs.498313
3D structure databases
PDB
2V40; X-ray; 1.90 A; A=21-456.[ExPASy / RCSB / EBI]
PDBsum 2V40; -.
ModBase P30520.
Protein-protein interaction databases
IntAct P30520; -.
PTM databases
PhosphoSite P30520; -.
Enzyme and pathway databases
Reactome REACT_1698; Nucleotide metabolism.
Organism-specific databases
H-InvDB HIX0001748; -.
HGNC HGNC:292; ADSS.
GenAtlas ADSS.
MIM 103060; gene. [NCBI / EBI]
PharmGKB PA24601; -.
GeneCards P30520.
Gene expression databases
ArrayExpress P30520; -.
CleanEx HS_ADSS; -.
GermOnline ENSG00000035687; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004019; Molecular function: adenylosuccinate synthase activity (inferred from direct assay from UniProtKB).
GO:0005525; Molecular function: GTP binding (non-traceable author statement from UniProtKB).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042301; Molecular function: phosphate binding (non-traceable author statement from UniProtKB).
GO:0006167; Biological process: AMP biosynthetic process (inferred from direct assay from UniProtKB).
GO:0002376; Biological process: immune system process (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001114; AdlSucc_Synth.
Graphical view of domain structure.
PANTHER PTHR11846; Asucc_synthtase; 1.
Pfam PF00709; Adenylsucc_synt; 1.
Pfam graphical view of domain structure.
ProDom PD001188; Asucc_synthtase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00788; Adenylsucc_synt; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00184; purA; 1.
PROSITE PS01266; ADENYLOSUCCIN_SYN_1; 1.
PS00513; ADENYLOSUCCIN_SYN_2; 1.
BLOCKS P30520.
ProtoNet P30520.
Proteomic databases
PeptideAtlas P30520; -.
Genome annotation databases
Ensembl ENSG00000035687; Homo sapiens. [Contig view]
GeneID 159; -.
KEGG hsa:159; -.
Phylogenomic databases
HOGENOM P30520; -.
HOVERGEN P30520; -.
Other
DrugBank DB00128; L-Aspartic Acid.
NextBio 633; -.
SOURCE ADSS; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   456  456     Adenylosuccinate synthetase isozyme 2. PRO_0000095130
NP_BIND   39    45  7     GTP (Potential). 
ACT_SITE   173   173        By similarity. 
ACT_SITE   180   180        By similarity. 
METAL   40    40        Magnesium (By similarity). 
METAL   67    67        Magnesium; via carbonyl oxygen (By similarity). 
CONFLICT   24    25        RP -> A (in Ref. 1; CAA47123). 
STRAND   30    39  10      
HELIX   43    51  9      
STRAND   55    59  5      
STRAND   68    72  5      
STRAND   75    82  8      
HELIX   84    87  4      
STRAND   92    95  4      
STRAND   99   102  4      
HELIX   103   116  14      
HELIX   118   120  3      
HELIX   123   125  3      
STRAND   126   130  5      
STRAND   134   136  3      
HELIX   138   149  12      
HELIX   166   174  9      
HELIX   181   184  4      
HELIX   188   205  18      
HELIX   213   227  15      
HELIX   228   230  3      
HELIX   234   243  10      
STRAND   249   252  4      
HELIX   257   259  3      
TURN   261   263  3      
HELIX   277   283  7      
HELIX   287   289  3      
STRAND   290   307  18      
HELIX   316   324  9      
TURN   330   332  3      
STRAND   337   339  3      
HELIX   343   353  11      
STRAND   356   361  6      
HELIX   363   368  6      
STRAND   370   380  11      
STRAND   383   387  5      
HELIX   392   395  4      
STRAND   399   406  8      
HELIX   418   420  3      
HELIX   423   436  14      
STRAND   440   444  5      
STRAND   446   448  3      
STRAND   451   454  4      
Sequence information
Length: 456 AA [This is the length of the unprocessed precursor] Molecular weight: 50097 Da [This is the MW of the unprocessed precursor] CRC64: 23B7AAC58A238783 [This is a checksum on the sequence]
        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 

P30520 in FASTA format

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