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P04424

- ARLY_HUMAN

UniProt

P04424 - ARLY_HUMAN

Protein

Argininosuccinate lyase

Gene

ASL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      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: Reactome

    GO - Biological processi

    1. arginine biosynthetic process via ornithine Source: InterPro
    2. arginine catabolic process Source: ProtInc
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. internal protein amino acid acetylation Source: UniProtKB
    5. small molecule metabolic process Source: Reactome
    6. urea cycle Source: Reactome

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesis, Urea cycle

    Enzyme and pathway databases

    BioCyciMetaCyc:HS10034-MONOMER.
    ReactomeiREACT_847. Urea cycle.
    SABIO-RKP04424.
    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:746. ASL.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    Argininosuccinic aciduria (ARGINSA) [MIM:207900]: An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311D → N in ARGINSA. 1 Publication
    VAR_043106
    Natural varianti95 – 951R → C in ARGINSA. 1 Publication
    Corresponds to variant rs28940585 [ dbSNP | Ensembl ].
    VAR_000676
    Natural varianti111 – 1111R → W in ARGINSA. 1 Publication
    VAR_000677
    Natural varianti113 – 1131R → Q in ARGINSA. 1 Publication
    VAR_043107
    Natural varianti178 – 1781V → M in ARGINSA. 2 Publications
    Corresponds to variant rs28941473 [ dbSNP | Ensembl ].
    VAR_017572
    Natural varianti186 – 1861R → Q in ARGINSA. 1 Publication
    VAR_043108
    Natural varianti193 – 1931R → Q in ARGINSA. 1 Publication
    VAR_000678
    Natural varianti236 – 2361R → W in ARGINSA. 1 Publication
    VAR_043109
    Natural varianti286 – 2861Q → R in ARGINSA. 2 Publications
    Corresponds to variant rs28941472 [ dbSNP | Ensembl ].
    VAR_000679
    Natural varianti335 – 3351V → L in ARGINSA. 1 Publication
    VAR_043110
    Natural varianti379 – 3791R → C in ARGINSA. 1 Publication
    Corresponds to variant rs28940287 [ dbSNP | Ensembl ].
    VAR_017573
    Natural varianti382 – 3821M → R in ARGINSA. 1 Publication
    VAR_043111
    Natural varianti385 – 3851R → C in ARGINSA. 1 Publication
    Corresponds to variant rs28940286 [ dbSNP | Ensembl ].
    VAR_017574
    Natural varianti456 – 4561R → W in ARGINSA. 1 Publication
    VAR_043112

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi51 – 511K → N: 2-fold reduction in activity. 1 Publication
    Mutagenesisi89 – 891H → Q: 10-fold reduction in activity. 1 Publication
    Mutagenesisi288 – 2881K → R: Refractory to inhibition by TSA and NAM and by addition of extra amino acids. No effect on protein structure. 2 Publications

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi207900. phenotype.
    Orphaneti23. Argininosuccinic aciduria.
    PharmGKBiPA25046.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 464463Argininosuccinate lyasePRO_0000137712Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TSA) 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.1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP04424.
    PaxDbiP04424.
    PRIDEiP04424.

    PTM databases

    PhosphoSiteiP04424.

    Expressioni

    Gene expression databases

    ArrayExpressiP04424.
    BgeeiP04424.
    CleanExiHS_ASL.
    GenevestigatoriP04424.

    Organism-specific databases

    HPAiCAB003696.
    HPA016646.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi106927. 15 interactions.
    IntActiP04424. 5 interactions.
    STRINGi9606.ENSP00000307188.

    Structurei

    Secondary structure

    1
    464
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 257
    Helixi28 – 314
    Helixi32 – 343
    Helixi35 – 5117
    Helixi57 – 7620
    Helixi88 – 10013
    Helixi101 – 1066
    Turni107 – 1104
    Helixi113 – 15038
    Beta strandi154 – 1596
    Beta strandi162 – 1687
    Helixi169 – 19426
    Beta strandi195 – 1973
    Turni202 – 2054
    Helixi213 – 2197
    Beta strandi223 – 2253
    Helixi229 – 2324
    Helixi237 – 26428
    Turni266 – 2683
    Helixi291 – 31424
    Helixi323 – 3275
    Helixi328 – 35225
    Helixi357 – 3626
    Helixi366 – 3694
    Helixi370 – 37910
    Helixi384 – 40017
    Helixi405 – 4073
    Helixi410 – 4145
    Helixi423 – 4286
    Helixi430 – 4345
    Beta strandi442 – 4443
    Helixi445 – 46319

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AOSX-ray4.20A/B1-464[»]
    1K62X-ray2.65A/B1-464[»]
    ProteinModelPortaliP04424.
    SMRiP04424. Positions 6-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04424.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0165.
    HOGENOMiHOG000242744.
    HOVERGENiHBG004281.
    InParanoidiP04424.
    KOiK01755.
    OMAiDATTLME.
    OrthoDBiEOG7PS1FN.
    PhylomeDBiP04424.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P04424-1) [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

    MASESGKLWG GRFVGAVDPI MEKFNASIAY DRHLWEVDVQ GSKAYSRGLE    50
    KAGLLTKAEM DQILHGLDKV AEEWAQGTFK LNSNDEDIHT ANERRLKELI 100
    GATAGKLHTG RSRNDQVVTD LRLWMRQTCS TLSGLLWELI RTMVDRAEAE 150
    RDVLFPGYTH LQRAQPIRWS HWILSHAVAL TRDSERLLEV RKRINVLPLG 200
    SGAIAGNPLG VDRELLRAEL NFGAITLNSM DATSERDFVA EFLFWASLCM 250
    THLSRMAEDL ILYCTKEFSF VQLSDAYSTG SSLMPQKKNP DSLELIRSKA 300
    GRVFGRCAGL LMTLKGLPST YNKDLQEDKE AVFEVSDTMS AVLQVATGVI 350
    STLQIHQENM GQALSPDMLA TDLAYYLVRK GMPFRQAHEA SGKAVFMAET 400
    KGVALNQLSL QELQTISPLF SGDVICVWDY GHSVEQYGAL GGTARSSVDW 450
    QIRQVRALLQ AQQA 464
    Length:464
    Mass (Da):51,658
    Last modified:January 23, 2007 - v4
    Checksum:iF751625C1A581883
    GO
    Isoform 2 (identifier: P04424-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         307-326: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:444
    Mass (Da):49,509
    Checksum:i07114189995B2342
    GO
    Isoform 3 (identifier: P04424-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         176-201: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:438
    Mass (Da):48,733
    Checksum:iC05AA06470444AA4
    GO

    Sequence cautioni

    The sequence AAA51786.1 differs from that shown. Reason: Frameshift at positions 387 and 452.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti246 – 2461A → R in CAA68722. (PubMed:3391281)Curated
    Sequence conflicti246 – 2461A → R in AAA51786. (PubMed:3463959)Curated
    Sequence conflicti246 – 2461A → R in AAA51787. (PubMed:2644168)Curated
    Sequence conflicti246 – 2461A → R in AAA51788. 1 PublicationCurated
    Sequence conflicti246 – 2461A → R in AAL57276. 1 PublicationCurated
    Sequence conflicti431 – 4311G → R in CAA68722. (PubMed:3391281)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311D → N in ARGINSA. 1 Publication
    VAR_043106
    Natural varianti95 – 951R → C in ARGINSA. 1 Publication
    Corresponds to variant rs28940585 [ dbSNP | Ensembl ].
    VAR_000676
    Natural varianti111 – 1111R → W in ARGINSA. 1 Publication
    VAR_000677
    Natural varianti113 – 1131R → Q in ARGINSA. 1 Publication
    VAR_043107
    Natural varianti178 – 1781V → M in ARGINSA. 2 Publications
    Corresponds to variant rs28941473 [ dbSNP | Ensembl ].
    VAR_017572
    Natural varianti181 – 1811T → S in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036281
    Natural varianti186 – 1861R → Q in ARGINSA. 1 Publication
    VAR_043108
    Natural varianti193 – 1931R → Q in ARGINSA. 1 Publication
    VAR_000678
    Natural varianti200 – 2001G → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036282
    Natural varianti236 – 2361R → W in ARGINSA. 1 Publication
    VAR_043109
    Natural varianti286 – 2861Q → R in ARGINSA. 2 Publications
    Corresponds to variant rs28941472 [ dbSNP | Ensembl ].
    VAR_000679
    Natural varianti335 – 3351V → L in ARGINSA. 1 Publication
    VAR_043110
    Natural varianti379 – 3791R → C in ARGINSA. 1 Publication
    Corresponds to variant rs28940287 [ dbSNP | Ensembl ].
    VAR_017573
    Natural varianti382 – 3821M → R in ARGINSA. 1 Publication
    VAR_043111
    Natural varianti385 – 3851R → C in ARGINSA. 1 Publication
    Corresponds to variant rs28940286 [ dbSNP | Ensembl ].
    VAR_017574
    Natural varianti456 – 4561R → W in ARGINSA. 1 Publication
    VAR_043112

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei176 – 20126Missing in isoform 3. CuratedVSP_047255Add
    BLAST
    Alternative sequencei307 – 32620Missing in isoform 2. CuratedVSP_047256Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00753 mRNA. Translation: CAA68722.1.
    M14218 mRNA. Translation: AAA51786.1. Frameshift.
    J03058 mRNA. Translation: AAA51787.1.
    M57638 mRNA. Translation: AAA51788.1.
    AF376770 Genomic DNA. Translation: AAL57276.1.
    AC068533 Genomic DNA. No translation available.
    BC008195 mRNA. Translation: AAH08195.1.
    BC033146 mRNA. Translation: AAH33146.1.
    M21007, M21006 Genomic DNA. Translation: AAA35566.1.
    CCDSiCCDS47597.1. [P04424-2]
    CCDS47598.1. [P04424-3]
    CCDS5531.1. [P04424-1]
    PIRiA31658. WZHURS.
    RefSeqiNP_000039.2. NM_000048.3. [P04424-1]
    NP_001020114.1. NM_001024943.1. [P04424-1]
    NP_001020115.1. NM_001024944.1. [P04424-2]
    NP_001020117.1. NM_001024946.1. [P04424-3]
    UniGeneiHs.632015.

    Genome annotation databases

    EnsembliENST00000304874; ENSP00000307188; ENSG00000126522. [P04424-1]
    ENST00000380839; ENSP00000370219; ENSG00000126522. [P04424-3]
    ENST00000395331; ENSP00000378740; ENSG00000126522. [P04424-2]
    ENST00000395332; ENSP00000378741; ENSG00000126522. [P04424-1]
    GeneIDi435.
    KEGGihsa:435.
    UCSCiuc003tuo.3. human. [P04424-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00753 mRNA. Translation: CAA68722.1 .
    M14218 mRNA. Translation: AAA51786.1 . Frameshift.
    J03058 mRNA. Translation: AAA51787.1 .
    M57638 mRNA. Translation: AAA51788.1 .
    AF376770 Genomic DNA. Translation: AAL57276.1 .
    AC068533 Genomic DNA. No translation available.
    BC008195 mRNA. Translation: AAH08195.1 .
    BC033146 mRNA. Translation: AAH33146.1 .
    M21007 , M21006 Genomic DNA. Translation: AAA35566.1 .
    CCDSi CCDS47597.1. [P04424-2 ]
    CCDS47598.1. [P04424-3 ]
    CCDS5531.1. [P04424-1 ]
    PIRi A31658. WZHURS.
    RefSeqi NP_000039.2. NM_000048.3. [P04424-1 ]
    NP_001020114.1. NM_001024943.1. [P04424-1 ]
    NP_001020115.1. NM_001024944.1. [P04424-2 ]
    NP_001020117.1. NM_001024946.1. [P04424-3 ]
    UniGenei Hs.632015.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AOS X-ray 4.20 A/B 1-464 [» ]
    1K62 X-ray 2.65 A/B 1-464 [» ]
    ProteinModelPortali P04424.
    SMRi P04424. Positions 6-464.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106927. 15 interactions.
    IntActi P04424. 5 interactions.
    STRINGi 9606.ENSP00000307188.

    Chemistry

    DrugBanki DB00125. L-Arginine.

    PTM databases

    PhosphoSitei P04424.

    Proteomic databases

    MaxQBi P04424.
    PaxDbi P04424.
    PRIDEi P04424.

    Protocols and materials databases

    DNASUi 435.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304874 ; ENSP00000307188 ; ENSG00000126522 . [P04424-1 ]
    ENST00000380839 ; ENSP00000370219 ; ENSG00000126522 . [P04424-3 ]
    ENST00000395331 ; ENSP00000378740 ; ENSG00000126522 . [P04424-2 ]
    ENST00000395332 ; ENSP00000378741 ; ENSG00000126522 . [P04424-1 ]
    GeneIDi 435.
    KEGGi hsa:435.
    UCSCi uc003tuo.3. human. [P04424-1 ]

    Organism-specific databases

    CTDi 435.
    GeneCardsi GC07P065540.
    GeneReviewsi ASL.
    HGNCi HGNC:746. ASL.
    HPAi CAB003696.
    HPA016646.
    MIMi 207900. phenotype.
    608310. gene.
    neXtProti NX_P04424.
    Orphaneti 23. Argininosuccinic aciduria.
    PharmGKBi PA25046.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0165.
    HOGENOMi HOG000242744.
    HOVERGENi HBG004281.
    InParanoidi P04424.
    KOi K01755.
    OMAi DATTLME.
    OrthoDBi EOG7PS1FN.
    PhylomeDBi P04424.
    TreeFami TF300656.

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00114 .
    UPA00158 ; UER00273 .
    BioCyci MetaCyc:HS10034-MONOMER.
    Reactomei REACT_847. Urea cycle.
    SABIO-RK P04424.

    Miscellaneous databases

    ChiTaRSi asl. human.
    EvolutionaryTracei P04424.
    GenomeRNAii 435.
    NextBioi 1821.
    PROi P04424.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04424.
    Bgeei P04424.
    CleanExi HS_ASL.
    Genevestigatori P04424.

    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. "Isolation of cDNA clones of human argininosuccinate lyase and corrected amino acid sequence."
      Matuo S., Tatsuno M., Kobayashi K., Saheki T., Miyata T.
      FEBS Lett. 234:395-399(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Cloning and sequence analysis of cDNA for human argininosuccinate lyase."
      O'Brien W.E., McInnes R., Kalumuck K., Adcock M.
      Proc. Natl. Acad. Sci. U.S.A. 83:7211-7215(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "cDNA sequence, interspecies comparison, and gene mapping analysis of argininosuccinate lyase."
      Todd S., McGill J.R., McCombs J.L., Moore C.M., Weider I., Naylor S.L.
      Genomics 4:53-59(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Cloning and sequence analysis of cDNA for human argininosuccinate lyase."
      Matuo S.
      Kagoshima Daigaku Igaku Zasshi 40:147-160(1988)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Complete sequence of the human ASL gene."
      Linnebank M., Tschiedel E., Koch H.G.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Brain and Cervix.
    8. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-97 (ISOFORM 1/2/3).
    9. Cited for: ACETYLATION AT LYS-69 AND LYS-288, ENZYME REGULATION, MUTAGENESIS OF LYS-288, IDENTIFICATION BY MASS SPECTROMETRY.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Human argininosuccinate lyase: a structural basis for intragenic complementation."
      Turner M.A., Simpson A., McInnes R.R., Howell P.L.
      Proc. Natl. Acad. Sci. U.S.A. 94:9063-9068(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS).
      Tissue: Liver.
    12. "Three-dimensional structure of the argininosuccinate lyase frequently complementing allele Q286R."
      Sampaleanu L.M., Vallee F., Thompson G.D., Howell P.L.
      Biochemistry 40:15570-15580(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF VARIANT ARG-286.
    13. "Analysis of naturally occurring and site-directed mutations in the argininosuccinate lyase gene."
      Barbosa P., Cialkowski M., O'Brien W.E.
      J. Biol. Chem. 266:5286-5290(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARGINSA TRP-111; GLN-193 AND ARG-286, MUTAGENESIS.
    14. "Molecular analysis of human argininosuccinate lyase: mutant characterization and alternative splicing of the coding region."
      Walker D.C., McCloskey D.A., Simard L.R., McInnes R.R.
      Proc. Natl. Acad. Sci. U.S.A. 87:9625-9629(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARGINSA CYS-95.
    15. "Clinical, enzymatic, and molecular genetic characterization of a biochemical variant type of argininosuccinic aciduria: prenatal and postnatal diagnosis in five unrelated families."
      Kleijer W.J., Garritsen V.H., Linnebank M., Mooyer P., Huijmans J.G.M., Mustonen A., Simola K.O.J., Arslan-Kirchner M., Battini R., Briones P., Cardo E., Mandel H., Tschiedel E., Wanders R.J.A., Koch H.G.
      J. Inherit. Metab. Dis. 25:399-410(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARGINSA MET-178; CYS-379 AND CYS-385.
    16. Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-181 AND VAL-200.
    17. "Argininosuccinate lyase deficiency: mutational spectrum in Italian patients and identification of a novel ASL pseudogene."
      Trevisson E., Salviati L., Baldoin M.C., Toldo I., Casarin A., Sacconi S., Cesaro L., Basso G., Burlina A.B.
      Hum. Mutat. 28:694-702(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARGINSA ASN-31; GLN-113; MET-178; GLN-186; TRP-236; ARG-286; LEU-335; ARG-382 AND TRP-456.

    Entry informationi

    Entry nameiARLY_HUMAN
    AccessioniPrimary (citable) accession number: P04424
    Secondary accession number(s): E7EMI0
    , E9PE48, Q6LDS5, Q96HS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 172 of the entry and version 4 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 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3