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Q8N142 (PURA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenylosuccinate synthetase isozyme 1

Short name=AMPSase 1
Short name=AdSS 1
EC=6.3.4.4
Alternative name(s):
Adenylosuccinate synthetase, basic isozyme
Adenylosuccinate synthetase, muscle isozyme
Short name=M-type adenylosuccinate synthetase
IMP--aspartate ligase 1
Gene names
Name:ADSSL1
Synonyms:ADSS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP By similarity. HAMAP-Rule MF_03126

Catalytic activity

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP-Rule MF_03126

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_03126

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP-Rule MF_03126

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_03126

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Predominantly expressed in skeletal muscle and heart, as well as in several hematopoietic cell lines and solid tumors. Ref.1

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Sequence caution

The sequence AAH32039.1 differs from that shown. Reason: Frameshift at position 1.

The sequence CAD62614.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   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 Ref.1. Source: UniProtKB

IMP metabolic process

Inferred from electronic annotation. Source: Ensembl

aspartate metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to drug

Inferred from electronic annotation. Source: Ensembl

cellular response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

glutamine metabolic process

Inferred from electronic annotation. Source: Ensembl

immune system process

Non-traceable author statement Ref.1. 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 muscle activity

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionGTP binding

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

GTPase activity

Inferred from electronic annotation. Source: Ensembl

adenylosuccinate synthase activity

Inferred from direct assay Ref.1. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phosphate ion binding

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

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N142-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8N142-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-64: MSGTRASNDR...TDADIISRCQ → MVGRSCGVAT...AGSLTPGGER
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Adenylosuccinate synthetase isozyme 1 HAMAP-Rule MF_03126
PRO_0000095132

Regions

Nucleotide binding42 – 487GTP By similarity
Nucleotide binding70 – 723GTP By similarity
Nucleotide binding363 – 3653GTP By similarity
Nucleotide binding445 – 4484GTP By similarity
Region43 – 464IMP binding By similarity
Region68 – 714IMP binding By similarity
Region331 – 3377Substrate binding By similarity

Sites

Active site431Proton acceptor By similarity
Active site711Proton donor By similarity
Metal binding431Magnesium By similarity
Metal binding701Magnesium; via carbonyl oxygen By similarity
Binding site431Substrate By similarity
Binding site1631IMP By similarity
Binding site1771IMP; shared with dimeric partner By similarity
Binding site2561IMP By similarity
Binding site2711IMP By similarity
Binding site3351IMP By similarity
Binding site3371GTP By similarity

Natural variations

Alternative sequence1 – 6464MSGTR…ISRCQ → MVGRSCGVATQRQGGGQRPT NLALTLSSSPAHSTALPWLP PRSLQLLSGHSVPAQPTPHL PSACGGPTRVTLGEERAWRS HGSNAGGHTCLPRRTAGAGS LTPGGER in isoform 2.
VSP_008421

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 387341D49721B2EF

FASTA45750,208
        10         20         30         40         50         60 
MSGTRASNDR PPGAGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV DLLATDADII 

        70         80         90        100        110        120 
SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN GVVIHLPGLF EEAEKNEKKG 

       130        140        150        160        170        180 
LKDWEKRLII SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTKKGIGPT YSSKAARTGL 

       190        200        210        220        230        240 
RICDLLSDFD EFSSRFKNLA HQHQSMFPTL EIDIEGQLKR LKGFAERIRP MVRDGVYFMY 

       250        260        270        280        290        300 
EALHGPPKKI LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA 

       310        320        330        340        350        360 
YTTRVGIGAF PTEQINEIGG LLQTRGHEWG VTTGRKRRCG WLDLMILRYA HMVNGFTALA 

       370        380        390        400        410        420 
LTKLDILDVL GEVKVGVSYK LNGKRIPYFP ANQEMLQKVE VEYETLPGWK ADTTGARRWE 

       430        440        450 
DLPPQAQNYI RFVENHVGVA VKWVGVGKSR ESMIQLF 

« Hide

Isoform 2 [UniParc].

Checksum: 9C561192088BDAAF
Show »

FASTA50054,562

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells."
Sun H., Li N., Wang X., Chen T., Shi L., Zhang L., Wang J., Wan T., Cao X.
Mol. Cell. Biochem. 269:85-94(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Bone marrow stroma.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Heart.
[3]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[4]"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] (ISOFORMS 1 AND 2).
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY037159 mRNA. Translation: AAK67646.1.
AK095921 mRNA. Translation: BAC04649.1.
BX248286 mRNA. Translation: CAD62614.1. Different initiation.
BC032039 mRNA. Translation: AAH32039.1. Frameshift.
BC047904 mRNA. Translation: AAH47904.1.
RefSeqNP_689541.1. NM_152328.3.
NP_954634.1. NM_199165.1.
UniGeneHs.592327.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GJOmodel-A27-457[»]
ProteinModelPortalQ8N142.
SMRQ8N142. Positions 27-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125783. 2 interactions.
IntActQ8N142. 3 interactions.
MINTMINT-3319213.
STRING9606.ENSP00000333019.

Chemistry

DrugBankDB00128. L-Aspartic Acid.

PTM databases

PhosphoSiteQ8N142.

Polymorphism databases

DMDM37537958.

Proteomic databases

PaxDbQ8N142.
PRIDEQ8N142.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330877; ENSP00000331260; ENSG00000185100. [Q8N142-1]
ENST00000332972; ENSP00000333019; ENSG00000185100. [Q8N142-2]
GeneID122622.
KEGGhsa:122622.
UCSCuc001ypd.3. human. [Q8N142-1]
uc001ype.3. human. [Q8N142-2]

Organism-specific databases

CTD122622.
GeneCardsGC14P105190.
HGNCHGNC:20093. ADSSL1.
MIM612498. gene.
neXtProtNX_Q8N142.
PharmGKBPA134974111.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHOG000260959.
HOVERGENHBG053768.
KOK01939.
OMAILLRHPY.
OrthoDBEOG7M6D76.
PhylomeDBQ8N142.
TreeFamTF300486.

Enzyme and pathway databases

BRENDA6.3.4.4. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00075; UER00335.

Gene expression databases

ArrayExpressQ8N142.
BgeeQ8N142.
CleanExHS_ADSSL1.
GenevestigatorQ8N142.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
MF_03126. Adenylosucc_synth_vert_basic.
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027509. AdSS_1_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

GenomeRNAi122622.
NextBio80937.
PROQ8N142.
SOURCESearch...

Entry information

Entry namePURA1_HUMAN
AccessionPrimary (citable) accession number: Q8N142
Secondary accession number(s): Q86TT6, Q8N714
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 115 of the entry and version 1 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 chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM