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Q91YI0

- ARLY_MOUSE

UniProt

Q91YI0 - ARLY_MOUSE

Protein

Argininosuccinate lyase

Gene

Asl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    2-(N(omega)-L-arginino)succinate = fumarate + L-arginine.

    Enzyme regulationi

    Enzyme activity is regulated by acetylation.By similarity

    Pathwayi

    GO - Molecular functioni

    1. argininosuccinate lyase activity Source: UniProtKB-EC

    GO - Biological processi

    1. ammonia assimilation cycle Source: MGI
    2. arginine biosynthetic process via ornithine Source: InterPro
    3. cellular amino acid metabolic process Source: MGI
    4. internal protein amino acid acetylation Source: UniProtKB
    5. locomotory behavior Source: MGI
    6. post-embryonic development Source: MGI
    7. urea cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesis, Urea cycle

    Enzyme and pathway databases

    UniPathwayiUPA00068; UER00114.
    UPA00158; UER00273.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Argininosuccinate lyase (EC:4.3.2.1)
    Short name:
    ASAL
    Alternative name(s):
    Arginosuccinase
    Gene namesi
    Name:Asl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:88084. Asl.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 464463Argininosuccinate lyasePRO_0000137714Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei7 – 71N6-acetyllysine1 Publication
    Modified residuei69 – 691N6-acetyllysineBy similarity
    Modified residuei288 – 2881N6-acetyllysineBy similarity

    Post-translational modificationi

    Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TCA) or with nicotinamide (NAM). Glucose increases acetylation by about a factor of 3 with decreasing enzyme activity. Acetylation on Lys-288 is decreased on the addition of extra amino acids resulting in activation of enzyme activity By similarity.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ91YI0.
    PaxDbiQ91YI0.
    PRIDEiQ91YI0.

    PTM databases

    PhosphoSiteiQ91YI0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ91YI0.
    BgeeiQ91YI0.
    CleanExiMM_ASL.
    GenevestigatoriQ91YI0.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    IntActiQ91YI0. 2 interactions.
    MINTiMINT-1869882.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91YI0.
    SMRiQ91YI0. Positions 6-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0165.
    GeneTreeiENSGT00390000014045.
    HOGENOMiHOG000242744.
    HOVERGENiHBG004281.
    InParanoidiQ91YI0.
    KOiK01755.
    OMAiKEGIFDA.
    OrthoDBiEOG7PS1FN.
    PhylomeDBiQ91YI0.
    TreeFamiTF300656.

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    HAMAPiMF_00006. Arg_succ_lyase.
    InterProiIPR029419. Arg_succ_lyase_C.
    IPR009049. Argininosuccinate_lyase.
    IPR024083. Fumarase/histidase_N.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    [Graphical view]
    PANTHERiPTHR11444. PTHR11444. 1 hit.
    PTHR11444:SF3. PTHR11444:SF3. 1 hit.
    PfamiPF14698. ASL_C2. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view]
    PRINTSiPR00149. FUMRATELYASE.
    SUPFAMiSSF48557. SSF48557. 1 hit.
    TIGRFAMsiTIGR00838. argH. 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.

    Q91YI0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASESGKLWG GRFVGAVDPI MEKFNSSISY DRHLWNVDVQ GSKAYSRGLE    50
    KAGLLTKAEM QQILQGLDKV AEEWAQGTFK LHPNDEDIHT ANERRLKELI 100
    GEAAGKLHTG RSRNDQVVTD LRLWMRQTCS KLSALLRVLI GTMVDRAEAE 150
    RDVLFPGYTH LQRAQPIRWS HWILSHAVAL TRDSERLLEV QKRINVLPLG 200
    SGAIAGNPLG VDRELLRAEL NFGAITLNSM DATSERDFVA EFLFWASLCM 250
    THLSRMAEDL ILYGTKEFSF VQLSDAYSTG SSLMPQKKNP DSLELIRSKA 300
    GRVFGRCAGL LMTLKGLPST YNKDLQEDKE AVFEVSDTMI AVLQVATGVI 350
    STLQIHRENM KQALSPDMLA TDLAYYLVRK GMPFRQAHEA SGKAVFMAET 400
    KGVALNLLSL QELQTISPLF SGDVSHVWDY SHSVEQYSAL GGTAKSSVEW 450
    QIRQVRALLQ AQEP 464
    Length:464
    Mass (Da):51,739
    Last modified:December 1, 2001 - v1
    Checksum:iA78ABC52A9285A59
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK076453 mRNA. Translation: BAC36348.1.
    AK140160 mRNA. Translation: BAE24262.1.
    AK148764 mRNA. Translation: BAE28659.1.
    AK168739 mRNA. Translation: BAE40580.1.
    BC016670 mRNA. Translation: AAH16670.1.
    CCDSiCCDS51655.1.
    RefSeqiNP_598529.1. NM_133768.4.
    XP_006504404.1. XM_006504341.1.
    UniGeneiMm.23869.

    Genome annotation databases

    EnsembliENSMUST00000159619; ENSMUSP00000123799; ENSMUSG00000025533.
    ENSMUST00000160129; ENSMUSP00000124579; ENSMUSG00000025533.
    ENSMUST00000161094; ENSMUSP00000124274; ENSMUSG00000025533.
    GeneIDi109900.
    KEGGimmu:109900.
    UCSCiuc008zty.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK076453 mRNA. Translation: BAC36348.1 .
    AK140160 mRNA. Translation: BAE24262.1 .
    AK148764 mRNA. Translation: BAE28659.1 .
    AK168739 mRNA. Translation: BAE40580.1 .
    BC016670 mRNA. Translation: AAH16670.1 .
    CCDSi CCDS51655.1.
    RefSeqi NP_598529.1. NM_133768.4.
    XP_006504404.1. XM_006504341.1.
    UniGenei Mm.23869.

    3D structure databases

    ProteinModelPortali Q91YI0.
    SMRi Q91YI0. Positions 6-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q91YI0. 2 interactions.
    MINTi MINT-1869882.

    PTM databases

    PhosphoSitei Q91YI0.

    Proteomic databases

    MaxQBi Q91YI0.
    PaxDbi Q91YI0.
    PRIDEi Q91YI0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000159619 ; ENSMUSP00000123799 ; ENSMUSG00000025533 .
    ENSMUST00000160129 ; ENSMUSP00000124579 ; ENSMUSG00000025533 .
    ENSMUST00000161094 ; ENSMUSP00000124274 ; ENSMUSG00000025533 .
    GeneIDi 109900.
    KEGGi mmu:109900.
    UCSCi uc008zty.1. mouse.

    Organism-specific databases

    CTDi 435.
    MGIi MGI:88084. Asl.

    Phylogenomic databases

    eggNOGi COG0165.
    GeneTreei ENSGT00390000014045.
    HOGENOMi HOG000242744.
    HOVERGENi HBG004281.
    InParanoidi Q91YI0.
    KOi K01755.
    OMAi KEGIFDA.
    OrthoDBi EOG7PS1FN.
    PhylomeDBi Q91YI0.
    TreeFami TF300656.

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00114 .
    UPA00158 ; UER00273 .

    Miscellaneous databases

    NextBioi 362969.
    PROi Q91YI0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q91YI0.
    Bgeei Q91YI0.
    CleanExi MM_ASL.
    Genevestigatori Q91YI0.

    Family and domain databases

    Gene3Di 1.10.275.10. 1 hit.
    HAMAPi MF_00006. Arg_succ_lyase.
    InterProi IPR029419. Arg_succ_lyase_C.
    IPR009049. Argininosuccinate_lyase.
    IPR024083. Fumarase/histidase_N.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    [Graphical view ]
    PANTHERi PTHR11444. PTHR11444. 1 hit.
    PTHR11444:SF3. PTHR11444:SF3. 1 hit.
    Pfami PF14698. ASL_C2. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00149. FUMRATELYASE.
    SUPFAMi SSF48557. SSF48557. 1 hit.
    TIGRFAMsi TIGR00838. argH. 1 hit.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
      Tissue: Corpora quadrigemina, Head, Liver and Sympathetic ganglion.
    2. "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].
    3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiARLY_MOUSE
    AccessioniPrimary (citable) accession number: Q91YI0
    Secondary accession number(s): Q3UFA2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 27, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 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