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P04424

- ARLY_HUMAN

UniProt

P04424 - ARLY_HUMAN

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Protein

Argininosuccinate lyase

Gene

ASL

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

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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication

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

BgeeiP04424.
CleanExiHS_ASL.
ExpressionAtlasiP04424. baseline.
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.
GeneTreeiENSGT00390000014045.
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

        10         20         30         40         50
MASESGKLWG GRFVGAVDPI MEKFNASIAY DRHLWEVDVQ GSKAYSRGLE
60 70 80 90 100
KAGLLTKAEM DQILHGLDKV AEEWAQGTFK LNSNDEDIHT ANERRLKELI
110 120 130 140 150
GATAGKLHTG RSRNDQVVTD LRLWMRQTCS TLSGLLWELI RTMVDRAEAE
160 170 180 190 200
RDVLFPGYTH LQRAQPIRWS HWILSHAVAL TRDSERLLEV RKRINVLPLG
210 220 230 240 250
SGAIAGNPLG VDRELLRAEL NFGAITLNSM DATSERDFVA EFLFWASLCM
260 270 280 290 300
THLSRMAEDL ILYCTKEFSF VQLSDAYSTG SSLMPQKKNP DSLELIRSKA
310 320 330 340 350
GRVFGRCAGL LMTLKGLPST YNKDLQEDKE AVFEVSDTMS AVLQVATGVI
360 370 380 390 400
STLQIHQENM GQALSPDMLA TDLAYYLVRK GMPFRQAHEA SGKAVFMAET
410 420 430 440 450
KGVALNQLSL QELQTISPLF SGDVICVWDY GHSVEQYGAL GGTARSSVDW
460
QIRQVRALLQ AQQA
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.
GeneTreei ENSGT00390000014045.
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

Bgeei P04424.
CleanExi HS_ASL.
ExpressionAtlasi P04424. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 173 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

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