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Q8N142

- PURA1_HUMAN

UniProt

Q8N142 - PURA1_HUMAN

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Protein

Adenylosuccinate synthetase isozyme 1

Gene

ADSSL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Binds 1 magnesium ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei43 – 431Proton acceptorUniRule annotation
Metal bindingi43 – 431MagnesiumUniRule annotation
Binding sitei43 – 431SubstrateUniRule annotation
Metal bindingi70 – 701Magnesium; via carbonyl oxygenUniRule annotation
Active sitei71 – 711Proton donorUniRule annotation
Binding sitei163 – 1631IMPUniRule annotation
Binding sitei177 – 1771IMP; shared with dimeric partnerUniRule annotation
Binding sitei256 – 2561IMPUniRule annotation
Binding sitei271 – 2711IMPUniRule annotation
Binding sitei335 – 3351IMPUniRule annotation
Binding sitei337 – 3371GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 487GTPUniRule annotation
Nucleotide bindingi70 – 723GTPUniRule annotation
Nucleotide bindingi363 – 3653GTPUniRule annotation
Nucleotide bindingi445 – 4484GTPUniRule annotation

GO - Molecular functioni

  1. adenylosuccinate synthase activity Source: UniProtKB
  2. GTPase activity Source: Ensembl
  3. GTP binding Source: UniProtKB
  4. magnesium ion binding Source: UniProtKB-HAMAP
  5. phosphate ion binding Source: UniProtKB

GO - Biological processi

  1. 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
  2. AMP biosynthetic process Source: UniProtKB
  3. aspartate metabolic process Source: Ensembl
  4. cellular response to drug Source: Ensembl
  5. cellular response to electrical stimulus Source: Ensembl
  6. glutamine metabolic process Source: Ensembl
  7. immune system process Source: UniProtKB
  8. IMP metabolic process Source: Ensembl
  9. nucleobase-containing small molecule metabolic process Source: Reactome
  10. purine nucleobase metabolic process Source: Reactome
  11. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
  12. response to muscle activity Source: Ensembl
  13. response to starvation Source: Ensembl
  14. 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

BRENDAi6.3.4.4. 2681.
ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00075; UER00335.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate synthetase isozyme 1UniRule annotation (EC:6.3.4.4UniRule annotation)
Short name:
AMPSase 1UniRule annotation
Short name:
AdSS 1UniRule annotation
Alternative name(s):
Adenylosuccinate synthetase, basic isozymeUniRule annotation
Adenylosuccinate synthetase, muscle isozymeUniRule annotation
Short name:
M-type adenylosuccinate synthetaseUniRule annotation
IMP--aspartate ligase 1UniRule annotation
Gene namesi
Name:ADSSL1UniRule annotation
Synonyms:ADSS1UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:20093. ADSSL1.

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134974111.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457Adenylosuccinate synthetase isozyme 1PRO_0000095132Add
BLAST

Proteomic databases

MaxQBiQ8N142.
PaxDbiQ8N142.
PRIDEiQ8N142.

PTM databases

PhosphoSiteiQ8N142.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ8N142.
CleanExiHS_ADSSL1.
ExpressionAtlasiQ8N142. baseline and differential.
GenevestigatoriQ8N142.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

BioGridi125783. 2 interactions.
IntActiQ8N142. 3 interactions.
MINTiMINT-3319213.
STRINGi9606.ENSP00000333019.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GJOmodel-A27-457[»]
ProteinModelPortaliQ8N142.
SMRiQ8N142. Positions 27-457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 464IMP bindingUniRule annotation
Regioni68 – 714IMP bindingUniRule annotation
Regioni331 – 3377Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0104.
GeneTreeiENSGT00390000015553.
HOGENOMiHOG000260959.
HOVERGENiHBG053768.
InParanoidiQ8N142.
KOiK01939.
OMAiNGAVIHV.
OrthoDBiEOG7M6D76.
PhylomeDBiQ8N142.
TreeFamiTF300486.

Family and domain databases

HAMAPiMF_00011. Adenylosucc_synth.
MF_03126. Adenylosucc_synth_vert_basic.
InterProiIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027509. AdSS_1_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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8N142-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSGTRASNDR PPGAGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV
60 70 80 90 100
DLLATDADII SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN
110 120 130 140 150
GVVIHLPGLF EEAEKNEKKG LKDWEKRLII SDRAHLVFDF HQAVDGLQEV
160 170 180 190 200
QRQAQEGKNI GTTKKGIGPT YSSKAARTGL RICDLLSDFD EFSSRFKNLA
210 220 230 240 250
HQHQSMFPTL EIDIEGQLKR LKGFAERIRP MVRDGVYFMY EALHGPPKKI
260 270 280 290 300
LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA
310 320 330 340 350
YTTRVGIGAF PTEQINEIGG LLQTRGHEWG VTTGRKRRCG WLDLMILRYA
360 370 380 390 400
HMVNGFTALA LTKLDILDVL GEVKVGVSYK LNGKRIPYFP ANQEMLQKVE
410 420 430 440 450
VEYETLPGWK ADTTGARRWE DLPPQAQNYI RFVENHVGVA VKWVGVGKSR

ESMIQLF
Length:457
Mass (Da):50,208
Last modified:October 1, 2002 - v1
Checksum:i387341D49721B2EF
GO
Isoform 2 (identifier: Q8N142-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-64: MSGTRASNDR...TDADIISRCQ → MVGRSCGVAT...AGSLTPGGER

Note: No experimental confirmation available.

Show »
Length:500
Mass (Da):54,562
Checksum:i9C561192088BDAAF
GO

Sequence cautioni

The sequence AAH32039.1 differs from that shown. Reason: Frameshift at position 1.
The sequence CAD62614.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6464MSGTR…ISRCQ → MVGRSCGVATQRQGGGQRPT NLALTLSSSPAHSTALPWLP PRSLQLLSGHSVPAQPTPHL PSACGGPTRVTLGEERAWRS HGSNAGGHTCLPRRTAGAGS LTPGGER in isoform 2. 1 PublicationVSP_008421Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS9990.1. [Q8N142-1]
CCDS9991.1. [Q8N142-2]
RefSeqiNP_689541.1. NM_152328.3. [Q8N142-1]
NP_954634.1. NM_199165.1. [Q8N142-2]
UniGeneiHs.592327.

Genome annotation databases

EnsembliENST00000330877; ENSP00000331260; ENSG00000185100. [Q8N142-1]
ENST00000332972; ENSP00000333019; ENSG00000185100. [Q8N142-2]
GeneIDi122622.
KEGGihsa:122622.
UCSCiuc001ypd.3. human. [Q8N142-1]
uc001ype.3. human. [Q8N142-2]

Polymorphism databases

DMDMi37537958.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS9990.1. [Q8N142-1 ]
CCDS9991.1. [Q8N142-2 ]
RefSeqi NP_689541.1. NM_152328.3. [Q8N142-1 ]
NP_954634.1. NM_199165.1. [Q8N142-2 ]
UniGenei Hs.592327.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GJO model - A 27-457 [» ]
ProteinModelPortali Q8N142.
SMRi Q8N142. Positions 27-457.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125783. 2 interactions.
IntActi Q8N142. 3 interactions.
MINTi MINT-3319213.
STRINGi 9606.ENSP00000333019.

Chemistry

DrugBanki DB00128. L-Aspartic Acid.

PTM databases

PhosphoSitei Q8N142.

Polymorphism databases

DMDMi 37537958.

Proteomic databases

MaxQBi Q8N142.
PaxDbi Q8N142.
PRIDEi Q8N142.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330877 ; ENSP00000331260 ; ENSG00000185100 . [Q8N142-1 ]
ENST00000332972 ; ENSP00000333019 ; ENSG00000185100 . [Q8N142-2 ]
GeneIDi 122622.
KEGGi hsa:122622.
UCSCi uc001ypd.3. human. [Q8N142-1 ]
uc001ype.3. human. [Q8N142-2 ]

Organism-specific databases

CTDi 122622.
GeneCardsi GC14P105190.
HGNCi HGNC:20093. ADSSL1.
MIMi 612498. gene.
neXtProti NX_Q8N142.
PharmGKBi PA134974111.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0104.
GeneTreei ENSGT00390000015553.
HOGENOMi HOG000260959.
HOVERGENi HBG053768.
InParanoidi Q8N142.
KOi K01939.
OMAi NGAVIHV.
OrthoDBi EOG7M6D76.
PhylomeDBi Q8N142.
TreeFami TF300486.

Enzyme and pathway databases

UniPathwayi UPA00075 ; UER00335 .
BRENDAi 6.3.4.4. 2681.
Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

GenomeRNAii 122622.
NextBioi 80937.
PROi Q8N142.
SOURCEi Search...

Gene expression databases

Bgeei Q8N142.
CleanExi HS_ADSSL1.
ExpressionAtlasi Q8N142. baseline and differential.
Genevestigatori Q8N142.

Family and domain databases

HAMAPi MF_00011. Adenylosucc_synth.
MF_03126. Adenylosucc_synth_vert_basic.
InterProi IPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027509. AdSS_1_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. "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.
    , 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.

Entry informationi

Entry nameiPURA1_HUMAN
AccessioniPrimary (citable) accession number: Q8N142
Secondary accession number(s): Q86TT6, Q8N714
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 120 of the entry and version 1 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3