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Protein

Argininosuccinate synthase

Gene

ASS1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues.By similarity

Catalytic activityi

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate.By similarity

Pathwayi: L-arginine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.By similarity
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Argininosuccinate synthase (ASS1)
  3. Argininosuccinate lyase (ASL)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: urea cycle

This protein is involved in step 1 of the subpathway that synthesizes (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline.By similarity
Proteins known to be involved in this subpathway in this organism are:
  1. Argininosuccinate synthase (ASS1)
This subpathway is part of the pathway urea cycle, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline, the pathway urea cycle and in Nitrogen metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei36ATP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei87CitrullineBy similarity1
Binding sitei92CitrullineBy similarity1
Binding sitei119AspartateBy similarity1
Binding sitei123AspartateBy similarity1
Binding sitei123CitrullineBy similarity1
Binding sitei124AspartateBy similarity1
Binding sitei127CitrullineBy similarity1
Binding sitei180CitrullineBy similarity1
Binding sitei189CitrullineBy similarity1
Binding sitei270CitrullineBy similarity1
Binding sitei282CitrullineBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 18ATPBy similarity9
Nucleotide bindingi115 – 123ATPBy similarity9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processAmino-acid biosynthesis, Arginine biosynthesis, Urea cycle
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-70635 Urea cycle
SABIO-RKiP14568
UniPathwayiUPA00068; UER00113
UPA00158; UER00272

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate synthaseCurated (EC:6.3.4.5By similarity)
Alternative name(s):
Citrulline--aspartate ligase
Gene namesi
Name:ASS1By similarity
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 11

Organism-specific databases

VGNCiVGNC:26224 ASS1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Defects in ASS1 are the cause of a bovine form of citrullinemia.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001485531 – 412Argininosuccinate synthaseAdd BLAST412

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei87PhosphotyrosineBy similarity1
Modified residuei112N6-acetyllysineBy similarity1
Modified residuei113PhosphotyrosineBy similarity1
Modified residuei165N6-acetyllysine; by CLOCKBy similarity1
Modified residuei176N6-acetyllysine; by CLOCKBy similarity1
Modified residuei180PhosphoserineBy similarity1
Modified residuei219PhosphoserineBy similarity1

Post-translational modificationi

Acetylated by CLOCK in a circadian manner which negatively regulates its enzyme activity. Deacetylated by histone deacetylases.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP14568
PeptideAtlasiP14568
PRIDEiP14568

PTM databases

iPTMnetiP14568

Expressioni

Gene expression databases

BgeeiENSBTAG00000020747

Interactioni

Subunit structurei

Homotetramer. Interacts with NMRAL1. Interacts with CLOCK; in a circadian manner.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000027649

Structurei

3D structure databases

ProteinModelPortaliP14568
SMRiP14568
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1706 Eukaryota
COG0137 LUCA
GeneTreeiENSGT00390000004524
HOGENOMiHOG000230093
HOVERGENiHBG001717
InParanoidiP14568
KOiK01940
OMAiGVGRIDM
OrthoDBiEOG091G0AIR
TreeFamiTF300736

Family and domain databases

CDDicd01999 Argininosuccinate_Synthase, 1 hit
Gene3Di3.40.50.620, 1 hit
3.90.1260.10, 1 hit
HAMAPiMF_00005 Arg_succ_synth_type1, 1 hit
InterProiView protein in InterPro
IPR001518 Arginosuc_synth
IPR018223 Arginosuc_synth_CS
IPR023434 Arginosuc_synth_type_1_subfam
IPR024074 AS_cat/multimer_dom_body
IPR014729 Rossmann-like_a/b/a_fold
PANTHERiPTHR11587 PTHR11587, 1 hit
PfamiView protein in Pfam
PF00764 Arginosuc_synth, 1 hit
TIGRFAMsiTIGR00032 argG, 1 hit
PROSITEiView protein in PROSITE
PS00564 ARGININOSUCCIN_SYN_1, 1 hit
PS00565 ARGININOSUCCIN_SYN_2, 1 hit

Sequencei

Sequence statusi: Complete.

P14568-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK
60 70 80 90 100
ALKLGAKKVF IEDISKEFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR
110 120 130 140 150
KQVEIAQREG AKYVSHGATG KGNDQIRFEL TCYSLAPQIK VIAPWRMPEF
160 170 180 190 200
YNRFQGRNDL MEYAKQHGIP VPVTPKNPWS MDENLMHISY EAGILENPKN
210 220 230 240 250
QAPPGLYTKT QDPAKAPNSP DMLEIEFKKG VPVKVTNVGD GTTHSTALEL
260 270 280 290 300
FLYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF
310 320 330 340 350
TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ
360 370 380 390 400
VSVFKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPVDATG FININSLRLK
410
EYHRLQNKVT AK
Length:412
Mass (Da):46,417
Last modified:January 1, 1990 - v1
Checksum:i6F74C7F445EE0D86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26198 mRNA Translation: AAA30388.1
BC102474 mRNA Translation: AAI02475.1
PIRiA33986 AJBORS
RefSeqiNP_776317.1, NM_173892.4
UniGeneiBt.1370

Genome annotation databases

EnsembliENSBTAT00000027649; ENSBTAP00000027649; ENSBTAG00000020747
GeneIDi280726
KEGGibta:280726

Similar proteinsi

Entry informationi

Entry nameiASSY_BOVIN
AccessioniPrimary (citable) accession number: P14568
Secondary accession number(s): Q3T0A7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: March 28, 2018
This is version 141 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health