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P54822

- PUR8_MOUSE

UniProt

P54822 - PUR8_MOUSE

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Protein

Adenylosuccinate lyase

Gene

Adsl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate.By similarity

Catalytic activityi

N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei159 – 1591Proton donor/acceptorBy similarity
Binding sitei241 – 2411SubstrateBy similarity
Active sitei289 – 2891Proton donor/acceptorBy similarity
Binding sitei303 – 3031Substrate; shared with neighboring subunitBy similarity
Binding sitei329 – 3291SubstrateBy similarity
Binding sitei334 – 3341SubstrateBy similarity
Binding sitei338 – 3381SubstrateBy similarity

GO - Molecular functioni

  1. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Source: UniProtKB-EC
  2. N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Source: MGI

GO - Biological processi

  1. 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
  2. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  3. aerobic respiration Source: Ensembl
  4. AMP biosynthetic process Source: MGI
  5. protein tetramerization Source: Ensembl
  6. response to hypoxia Source: Ensembl
  7. response to muscle activity Source: Ensembl
  8. response to nutrient Source: Ensembl
  9. response to starvation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

ReactomeiREACT_263184. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate lyase (EC:4.3.2.2)
Short name:
ASL
Alternative name(s):
Adenylosuccinase
Short name:
ASase
Gene namesi
Name:Adsl
Synonyms:Adl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:103202. Adsl.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 484483Adenylosuccinate lyasePRO_0000137894Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei147 – 1471N6-acetyllysineBy similarity
Modified residuei295 – 2951N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP54822.
PaxDbiP54822.
PRIDEiP54822.

PTM databases

PhosphoSiteiP54822.

Expressioni

Gene expression databases

BgeeiP54822.
CleanExiMM_ADSL.
ExpressionAtlasiP54822. baseline and differential.
GenevestigatoriP54822.

Interactioni

Subunit structurei

Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site (By similarity).By similarity

Protein-protein interaction databases

BioGridi198009. 1 interaction.
IntActiP54822. 3 interactions.
MINTiMINT-4109237.
STRINGi10090.ENSMUSP00000023043.

Structurei

3D structure databases

ProteinModelPortaliP54822.
SMRiP54822. Positions 5-472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 212Substrate binding; shared with neighboring subunitBy similarity
Regioni85 – 873Substrate bindingBy similarity
Regioni111 – 1122Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0015.
GeneTreeiENSGT00390000013486.
HOGENOMiHOG000033915.
HOVERGENiHBG000214.
InParanoidiP54822.
KOiK01756.
OMAiMAHVHAY.
OrthoDBiEOG7GQXVD.
TreeFamiTF106385.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54822-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAASGDPGSA ESYRSPLAAR YASREMCFLF SDRYKFQTWR QLWLWLAEAE
60 70 80 90 100
QTLGLPITDE QIQEMKSNLN NIDFQMAAEE EKRLRHDVMA HVHTFGHCCP
110 120 130 140 150
KAAGIIHLGA TSCYVGDNTD LIILRNAFDL LLPKLARVIS RLADFAKDRA
160 170 180 190 200
DLPTLGFTHF QPAQLTTVGK RCCLWIQDLC MDLQNLKRVR DELRFRGVKG
210 220 230 240 250
TTGTQASFLQ LFEGDHQKVE QLDKMVTEKA GFKRAFIITG QTYTRKVDIE
260 270 280 290 300
VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR
310 320 330 340 350
SERCCSLARH LMALTMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT
360 370 380 390 400
ILNTLQNISE GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQDCH
410 420 430 440 450
EKIRVLSQQA AAVVKQEGGD NDLIERIRAD AYFSPIHSQL EHLLDPSSFT
460 470 480
GRAPQQVHRF LEEEVRPLLK PYGNEMAVKA ELCL
Length:484
Mass (Da):54,866
Last modified:July 27, 2011 - v2
Checksum:i9F11689AD41D1453
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1802LC → SV in AAB60684. (PubMed:8530047)Curated
Sequence conflicti192 – 1932EL → DV in AAB60684. (PubMed:8530047)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20225 mRNA. Translation: AAB60684.1.
AK049372 mRNA. Translation: BAC33717.1.
AK051111 mRNA. Translation: BAC34529.1.
AK152092 mRNA. Translation: BAE30940.1.
AK168906 mRNA. Translation: BAE40720.1.
AK171725 mRNA. Translation: BAE42633.1.
CH466550 Genomic DNA. Translation: EDL04592.1.
BC020187 mRNA. Translation: AAH20187.1.
CCDSiCCDS27664.1.
RefSeqiNP_033764.2. NM_009634.6.
UniGeneiMm.38151.

Genome annotation databases

EnsembliENSMUST00000023043; ENSMUSP00000023043; ENSMUSG00000022407.
GeneIDi11564.
KEGGimmu:11564.
UCSCiuc007wvz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20225 mRNA. Translation: AAB60684.1 .
AK049372 mRNA. Translation: BAC33717.1 .
AK051111 mRNA. Translation: BAC34529.1 .
AK152092 mRNA. Translation: BAE30940.1 .
AK168906 mRNA. Translation: BAE40720.1 .
AK171725 mRNA. Translation: BAE42633.1 .
CH466550 Genomic DNA. Translation: EDL04592.1 .
BC020187 mRNA. Translation: AAH20187.1 .
CCDSi CCDS27664.1.
RefSeqi NP_033764.2. NM_009634.6.
UniGenei Mm.38151.

3D structure databases

ProteinModelPortali P54822.
SMRi P54822. Positions 5-472.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198009. 1 interaction.
IntActi P54822. 3 interactions.
MINTi MINT-4109237.
STRINGi 10090.ENSMUSP00000023043.

PTM databases

PhosphoSitei P54822.

Proteomic databases

MaxQBi P54822.
PaxDbi P54822.
PRIDEi P54822.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023043 ; ENSMUSP00000023043 ; ENSMUSG00000022407 .
GeneIDi 11564.
KEGGi mmu:11564.
UCSCi uc007wvz.1. mouse.

Organism-specific databases

CTDi 158.
MGIi MGI:103202. Adsl.

Phylogenomic databases

eggNOGi COG0015.
GeneTreei ENSGT00390000013486.
HOGENOMi HOG000033915.
HOVERGENi HBG000214.
InParanoidi P54822.
KOi K01756.
OMAi MAHVHAY.
OrthoDBi EOG7GQXVD.
TreeFami TF106385.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00132 .
UPA00075 ; UER00336 .
Reactomei REACT_263184. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

NextBioi 279062.
PROi P54822.
SOURCEi Search...

Gene expression databases

Bgeei P54822.
CleanExi MM_ADSL.
ExpressionAtlasi P54822. baseline and differential.
Genevestigatori P54822.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
InterProi IPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SMARTi SM00998. ADSL_C. 1 hit.
[Graphical view ]
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00928. purB. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the cDNA and the gene encoding murine adenylosuccinate lyase."
    Wong L.J., O'Brien W.E.
    Genomics 28:341-343(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129.
    Tissue: Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Kidney and Spleen.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Strain: FVB/N.
    Tissue: Salivary gland.

Entry informationi

Entry nameiPUR8_MOUSE
AccessioniPrimary (citable) accession number: P54822
Secondary accession number(s): Q8VCD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3