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Q91YI0

- ARLY_MOUSE

UniProt

Q91YI0 - ARLY_MOUSE

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Protein

Argininosuccinate lyase

Gene

Asl

Organism
Mus musculus (Mouse)
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: 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
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Urea cycle

Enzyme and pathway databases

ReactomeiREACT_246679. Urea cycle.
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

BgeeiQ91YI0.
CleanExiMM_ASL.
ExpressionAtlasiQ91YI0. baseline and differential.
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

        10         20         30         40         50
MASESGKLWG GRFVGAVDPI MEKFNSSISY DRHLWNVDVQ GSKAYSRGLE
60 70 80 90 100
KAGLLTKAEM QQILQGLDKV AEEWAQGTFK LHPNDEDIHT ANERRLKELI
110 120 130 140 150
GEAAGKLHTG RSRNDQVVTD LRLWMRQTCS KLSALLRVLI GTMVDRAEAE
160 170 180 190 200
RDVLFPGYTH LQRAQPIRWS HWILSHAVAL TRDSERLLEV QKRINVLPLG
210 220 230 240 250
SGAIAGNPLG VDRELLRAEL NFGAITLNSM DATSERDFVA EFLFWASLCM
260 270 280 290 300
THLSRMAEDL ILYGTKEFSF VQLSDAYSTG SSLMPQKKNP DSLELIRSKA
310 320 330 340 350
GRVFGRCAGL LMTLKGLPST YNKDLQEDKE AVFEVSDTMI AVLQVATGVI
360 370 380 390 400
STLQIHRENM KQALSPDMLA TDLAYYLVRK GMPFRQAHEA SGKAVFMAET
410 420 430 440 450
KGVALNLLSL QELQTISPLF SGDVSHVWDY SHSVEQYSAL GGTAKSSVEW
460
QIRQVRALLQ AQEP
Length:464
Mass (Da):51,739
Last modified:December 1, 2001 - v1
Checksum:iA78ABC52A9285A59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 .
Reactomei REACT_246679. Urea cycle.

Miscellaneous databases

NextBioi 362969.
PROi Q91YI0.
SOURCEi Search...

Gene expression databases

Bgeei Q91YI0.
CleanExi MM_ASL.
ExpressionAtlasi Q91YI0. baseline and differential.
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: November 26, 2014
This is version 112 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