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Protein

Argininosuccinate synthase

Gene

ASS1

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

Functioni

Is indirectly involved in the control of blood pressure.By similarity

Catalytic activityi

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

Pathway:iL-arginine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.
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.

Pathway:iurea cycle

This protein is involved in step 1 of the subpathway that synthesizes (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361ATP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei87 – 871Citrulline1 Publication
Binding sitei92 – 921Citrulline1 Publication
Binding sitei119 – 1191Aspartate1 Publication
Binding sitei123 – 1231Aspartate1 Publication
Binding sitei123 – 1231Citrulline1 Publication
Binding sitei124 – 1241Aspartate1 Publication
Binding sitei127 – 1271Citrulline1 Publication
Binding sitei180 – 1801Citrulline1 Publication
Binding sitei189 – 1891Citrulline1 Publication
Binding sitei270 – 2701Citrulline1 Publication
Binding sitei282 – 2821Citrulline1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189ATPBy similarity
Nucleotide bindingi115 – 1239ATPBy similarity

GO - Molecular functioni

  • amino acid binding Source: BHF-UCL
  • argininosuccinate synthase activity Source: BHF-UCL
  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • poly(A) RNA binding Source: UniProtKB
  • toxic substance binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Urea cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS05425-MONOMER.
BRENDAi6.3.4.5. 2681.
ReactomeiREACT_847. Urea cycle.
SABIO-RKP00966.
UniPathwayiUPA00068; UER00113.
UPA00158; UER00272.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate synthase (EC:6.3.4.5)
Alternative name(s):
Citrulline--aspartate ligase
Gene namesi
Name:ASS1
Synonyms:ASS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:758. ASS1.

Subcellular locationi

GO - Cellular componenti

  • cell body fiber Source: Ensembl
  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • endoplasmic reticulum Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • lysosome Source: Ensembl
  • mitochondrial outer membrane Source: Ensembl
  • nucleus Source: Ensembl
  • perikaryon Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Citrullinemia 1 (CTLN1)9 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionThe classic form of citrullinemia, an autosomal recessive disease characterized primarily by elevated serum and urine citrulline levels. Ammonia intoxication is another manifestation. It is a disorder of the urea cycle, usually manifesting in the first few days of life. Affected infants appear normal at birth, but as ammonia builds up in the body they present symptoms such as lethargy, poor feeding, vomiting, seizures and loss of consciousness. Less commonly, a milder form can develop later in childhood or adulthood.

See also OMIM:215700
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141G → S in CTLN1. 2 Publications
VAR_000681
Natural varianti18 – 181S → L in CTLN1. 1 Publication
VAR_000682
Natural varianti19 – 191C → R in CTLN1. 1 Publication
VAR_015891
Natural varianti40 – 401Q → L in CTLN1. 1 Publication
VAR_058337
Natural varianti69 – 691V → A in CTLN1. 1 Publication
VAR_016013
Natural varianti79 – 791S → P in CTLN1.
VAR_058338
Natural varianti86 – 861R → C in CTLN1. 1 Publication
VAR_000683
Natural varianti86 – 861R → H in CTLN1. 1 Publication
VAR_015892
Natural varianti95 – 951R → S in CTLN1. 1 Publication
VAR_015893
Natural varianti96 – 961P → H in CTLN1.
VAR_058339
Natural varianti96 – 961P → S in CTLN1. 1 Publication
VAR_015894
Natural varianti108 – 1081R → L in CTLN1. 2 Publications
Corresponds to variant rs35269064 [ dbSNP | Ensembl ].
VAR_016014
Natural varianti117 – 1171G → D in CTLN1. 2 Publications
VAR_015896
Natural varianti117 – 1171G → S in CTLN1. 1 Publication
VAR_015895
Natural varianti118 – 1181A → T in CTLN1. 1 Publication
VAR_000684
Natural varianti119 – 1191T → I in CTLN1. 1 Publication
VAR_016015
Natural varianti124 – 1241D → N in CTLN1. 1 Publication
VAR_058340
Natural varianti127 – 1271R → Q in CTLN1. 1 Publication
VAR_058341
Natural varianti127 – 1271R → W in CTLN1; severe clinical course.
VAR_058342
Natural varianti141 – 1411V → G in CTLN1. 1 Publication
VAR_072792
Natural varianti157 – 1571R → C in CTLN1. 1 Publication
VAR_015897
Natural varianti157 – 1571R → H in CTLN1. 2 Publications
VAR_000685
Natural varianti160 – 1601L → P in CTLN1.
VAR_058343
Natural varianti179 – 1791W → R in CTLN1; mild. 3 Publications
Corresponds to variant rs121908646 [ dbSNP | Ensembl ].
VAR_015898
Natural varianti180 – 1801S → N in CTLN1. 1 Publication
VAR_000686
Natural varianti190 – 1901Y → D in CTLN1. 1 Publication
VAR_058344
Natural varianti191 – 1911E → K in CTLN1. 1 Publication
VAR_015899
Natural varianti191 – 1911E → Q in CTLN1.
VAR_058345
Natural varianti192 – 1921A → V in CTLN1. 1 Publication
VAR_000687
Natural varianti202 – 2021A → E in CTLN1.
VAR_058346
Natural varianti206 – 2061L → P in CTLN1.
VAR_058347
Natural varianti263 – 2631V → M in CTLN1; mild clinical course. 1 Publication
Corresponds to variant rs192838388 [ dbSNP | Ensembl ].
VAR_058348
Natural varianti265 – 2651R → C in CTLN1; severe clinical course. 1 Publication
VAR_058349
Natural varianti265 – 2651R → H in CTLN1. 1 Publication
VAR_015900
Natural varianti269 – 2691V → M in CTLN1. 2 Publications
VAR_015901
Natural varianti270 – 2701E → Q in CTLN1. 2 Publications
VAR_016007
Natural varianti272 – 2721R → C in CTLN1. 2 Publications
VAR_000688
Natural varianti277 – 2771K → T in CTLN1.
VAR_058350
Natural varianti279 – 2791R → Q in CTLN1. 1 Publication
VAR_016008
Natural varianti280 – 2801G → R in CTLN1. 1 Publication
VAR_000689
Natural varianti283 – 2831E → K in CTLN1. 2 Publications
VAR_015902
Natural varianti284 – 2841T → I in CTLN1; mild clinical course.
VAR_058351
Natural varianti291 – 2911Y → S in CTLN1.
VAR_058352
Natural varianti296 – 2961D → G in CTLN1.
VAR_058353
Natural varianti302 – 3021M → V in CTLN1.
VAR_058354
Natural varianti304 – 3041R → W in CTLN1. 3 Publications
VAR_000690
Natural varianti307 – 3071R → C in CTLN1.
Corresponds to variant rs183276875 [ dbSNP | Ensembl ].
VAR_058355
Natural varianti310 – 3101K → Q in CTLN1. 1 Publication
VAR_016009
Natural varianti310 – 3101K → R in CTLN1.
VAR_015903
Natural varianti324 – 3241G → S in CTLN1. 4 Publications
VAR_000691
Natural varianti324 – 3241G → V in CTLN1.
VAR_058356
Natural varianti341 – 3411S → F in CTLN1.
VAR_058357
Natural varianti345 – 3451V → G in CTLN1.
VAR_058358
Natural varianti347 – 3471G → R in CTLN1; severe clinical course.
VAR_058359
Natural varianti359 – 3591Y → D in CTLN1; mild clinical course.
VAR_058360
Natural varianti362 – 3621G → V in CTLN1; mild. 3 Publications
VAR_015904
Natural varianti363 – 3631R → G in CTLN1. 1 Publication
VAR_016010
Natural varianti363 – 3631R → L in CTLN1. 1 Publication
VAR_000692
Natural varianti363 – 3631R → Q in CTLN1. 1 Publication
VAR_016011
Natural varianti363 – 3631R → W in CTLN1. 2 Publications
VAR_000693
Natural varianti389 – 3891T → I in CTLN1. 1 Publication
VAR_016012
Natural varianti390 – 3901G → R in CTLN1. 5 Publications
VAR_000694

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi215700. phenotype.
Orphaneti247546. Acute neonatal citrullinemia type I.
247573. Adult-onset citrullinemia type I.
PharmGKBiPA162376926.

Chemistry

DrugBankiDB00171. Adenosine triphosphate.
DB00125. L-Arginine.
DB00128. L-Aspartic Acid.
DB00155. L-Citrulline.

Polymorphism and mutation databases

BioMutaiASS1.
DMDMi20141195.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412Argininosuccinate synthasePRO_0000148554Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131Phosphotyrosine1 Publication
Modified residuei180 – 1801Phosphoserine1 Publication
Modified residuei219 – 2191Phosphothreonine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP00966.
PaxDbiP00966.
PRIDEiP00966.

PTM databases

PhosphoSiteiP00966.

Expressioni

Gene expression databases

BgeeiP00966.
CleanExiHS_ASS1.
ExpressionAtlasiP00966. baseline and differential.
GenevisibleiP00966. HS.

Organism-specific databases

HPAiHPA020896.
HPA020934.

Interactioni

Subunit structurei

Homotetramer. Interacts with NMRAL1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-536842,EBI-536842
ARAFP103984EBI-536842,EBI-365961

Protein-protein interaction databases

BioGridi106937. 41 interactions.
DIPiDIP-34055N.
IntActiP00966. 13 interactions.
MINTiMINT-5000467.
STRINGi9606.ENSP00000253004.

Structurei

Secondary structure

1
412
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Helixi15 – 2612Combined sources
Beta strandi29 – 3911Combined sources
Helixi44 – 5411Combined sources
Beta strandi57 – 637Combined sources
Helixi65 – 717Combined sources
Helixi73 – 786Combined sources
Turni84 – 863Combined sources
Turni90 – 934Combined sources
Helixi94 – 10916Combined sources
Beta strandi112 – 1154Combined sources
Helixi124 – 13512Combined sources
Beta strandi140 – 1423Combined sources
Helixi144 – 1463Combined sources
Helixi148 – 1514Combined sources
Helixi158 – 1669Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi188 – 1903Combined sources
Helixi193 – 1964Combined sources
Helixi204 – 2063Combined sources
Turni213 – 2153Combined sources
Beta strandi221 – 2288Combined sources
Beta strandi231 – 2377Combined sources
Turni238 – 2403Combined sources
Helixi247 – 26115Combined sources
Beta strandi265 – 2717Combined sources
Beta strandi277 – 2837Combined sources
Helixi285 – 30117Combined sources
Helixi304 – 32320Combined sources
Beta strandi326 – 3283Combined sources
Helixi329 – 34113Combined sources
Turni342 – 3443Combined sources
Beta strandi347 – 3548Combined sources
Beta strandi357 – 3648Combined sources
Helixi372 – 3754Combined sources
Helixi385 – 40420Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NZ2X-ray2.40A1-412[»]
ProteinModelPortaliP00966.
SMRiP00966. Positions 4-407.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00966.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0137.
GeneTreeiENSGT00390000004524.
HOGENOMiHOG000230093.
HOVERGENiHBG001717.
InParanoidiP00966.
KOiK01940.
OMAiIYNGYWW.
OrthoDBiEOG7PVWPB.
PhylomeDBiP00966.
TreeFamiTF300736.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00005. Arg_succ_synth_type1.
InterProiIPR001518. 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.
[Graphical view]
PfamiPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00032. argG. 1 hit.
PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00966-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK
60 70 80 90 100
ALKLGAKKVF IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR
110 120 130 140 150
KQVEIAQREG AKYVSHGATG KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF
160 170 180 190 200
YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS MDENLMHISY EAGILENPKN
210 220 230 240 250
QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD GTTHQTSLEL
260 270 280 290 300
FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF
310 320 330 340 350
TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ
360 370 380 390 400
VSVLKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK
410
EYHRLQSKVT AK
Length:412
Mass (Da):46,530
Last modified:April 3, 2002 - v2
Checksum:i47CAD2373AE47E47
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti325 – 3273FWH → LRP in CAA25771 (PubMed:6194510).Curated
Sequence conflicti325 – 3273FWH → LRP in AAA51783 (PubMed:6321498).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141G → S in CTLN1. 2 Publications
VAR_000681
Natural varianti18 – 181S → L in CTLN1. 1 Publication
VAR_000682
Natural varianti19 – 191C → R in CTLN1. 1 Publication
VAR_015891
Natural varianti40 – 401Q → L in CTLN1. 1 Publication
VAR_058337
Natural varianti65 – 651S → I.
Corresponds to variant rs2229556 [ dbSNP | Ensembl ].
VAR_050427
Natural varianti69 – 691V → A in CTLN1. 1 Publication
VAR_016013
Natural varianti79 – 791S → P in CTLN1.
VAR_058338
Natural varianti86 – 861R → C in CTLN1. 1 Publication
VAR_000683
Natural varianti86 – 861R → H in CTLN1. 1 Publication
VAR_015892
Natural varianti95 – 951R → S in CTLN1. 1 Publication
VAR_015893
Natural varianti96 – 961P → H in CTLN1.
VAR_058339
Natural varianti96 – 961P → S in CTLN1. 1 Publication
VAR_015894
Natural varianti108 – 1081R → L in CTLN1. 2 Publications
Corresponds to variant rs35269064 [ dbSNP | Ensembl ].
VAR_016014
Natural varianti117 – 1171G → D in CTLN1. 2 Publications
VAR_015896
Natural varianti117 – 1171G → S in CTLN1. 1 Publication
VAR_015895
Natural varianti118 – 1181A → T in CTLN1. 1 Publication
VAR_000684
Natural varianti119 – 1191T → I in CTLN1. 1 Publication
VAR_016015
Natural varianti124 – 1241D → N in CTLN1. 1 Publication
VAR_058340
Natural varianti127 – 1271R → Q in CTLN1. 1 Publication
VAR_058341
Natural varianti127 – 1271R → W in CTLN1; severe clinical course.
VAR_058342
Natural varianti141 – 1411V → G in CTLN1. 1 Publication
VAR_072792
Natural varianti157 – 1571R → C in CTLN1. 1 Publication
VAR_015897
Natural varianti157 – 1571R → H in CTLN1. 2 Publications
VAR_000685
Natural varianti160 – 1601L → P in CTLN1.
VAR_058343
Natural varianti179 – 1791W → R in CTLN1; mild. 3 Publications
Corresponds to variant rs121908646 [ dbSNP | Ensembl ].
VAR_015898
Natural varianti180 – 1801S → N in CTLN1. 1 Publication
VAR_000686
Natural varianti190 – 1901Y → D in CTLN1. 1 Publication
VAR_058344
Natural varianti191 – 1911E → K in CTLN1. 1 Publication
VAR_015899
Natural varianti191 – 1911E → Q in CTLN1.
VAR_058345
Natural varianti192 – 1921A → V in CTLN1. 1 Publication
VAR_000687
Natural varianti202 – 2021A → E in CTLN1.
VAR_058346
Natural varianti206 – 2061L → P in CTLN1.
VAR_058347
Natural varianti263 – 2631V → M in CTLN1; mild clinical course. 1 Publication
Corresponds to variant rs192838388 [ dbSNP | Ensembl ].
VAR_058348
Natural varianti265 – 2651R → C in CTLN1; severe clinical course. 1 Publication
VAR_058349
Natural varianti265 – 2651R → H in CTLN1. 1 Publication
VAR_015900
Natural varianti269 – 2691V → M in CTLN1. 2 Publications
VAR_015901
Natural varianti270 – 2701E → Q in CTLN1. 2 Publications
VAR_016007
Natural varianti272 – 2721R → C in CTLN1. 2 Publications
VAR_000688
Natural varianti277 – 2771K → T in CTLN1.
VAR_058350
Natural varianti279 – 2791R → Q in CTLN1. 1 Publication
VAR_016008
Natural varianti280 – 2801G → R in CTLN1. 1 Publication
VAR_000689
Natural varianti283 – 2831E → K in CTLN1. 2 Publications
VAR_015902
Natural varianti284 – 2841T → I in CTLN1; mild clinical course.
VAR_058351
Natural varianti291 – 2911Y → S in CTLN1.
VAR_058352
Natural varianti296 – 2961D → G in CTLN1.
VAR_058353
Natural varianti302 – 3021M → V in CTLN1.
VAR_058354
Natural varianti304 – 3041R → W in CTLN1. 3 Publications
VAR_000690
Natural varianti307 – 3071R → C in CTLN1.
Corresponds to variant rs183276875 [ dbSNP | Ensembl ].
VAR_058355
Natural varianti310 – 3101K → Q in CTLN1. 1 Publication
VAR_016009
Natural varianti310 – 3101K → R in CTLN1.
VAR_015903
Natural varianti324 – 3241G → S in CTLN1. 4 Publications
VAR_000691
Natural varianti324 – 3241G → V in CTLN1.
VAR_058356
Natural varianti341 – 3411S → F in CTLN1.
VAR_058357
Natural varianti345 – 3451V → G in CTLN1.
VAR_058358
Natural varianti347 – 3471G → R in CTLN1; severe clinical course.
VAR_058359
Natural varianti359 – 3591Y → D in CTLN1; mild clinical course.
VAR_058360
Natural varianti362 – 3621G → V in CTLN1; mild. 3 Publications
VAR_015904
Natural varianti363 – 3631R → G in CTLN1. 1 Publication
VAR_016010
Natural varianti363 – 3631R → L in CTLN1. 1 Publication
VAR_000692
Natural varianti363 – 3631R → Q in CTLN1. 1 Publication
VAR_016011
Natural varianti363 – 3631R → W in CTLN1. 2 Publications
VAR_000693
Natural varianti389 – 3891T → I in CTLN1. 1 Publication
VAR_016012
Natural varianti390 – 3901G → R in CTLN1. 5 Publications
VAR_000694

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01630 mRNA. Translation: CAA25771.1.
L00084
, L00079, L00080, L00081, L00082, L00083 Genomic DNA. Translation: AAA51783.1.
AY034076 Genomic DNA. Translation: AAK67487.1.
AK027126 mRNA. No translation available.
BC009243 mRNA. Translation: AAH09243.1.
BC021676 mRNA. Translation: AAH21676.1.
M34903 Genomic DNA. Translation: AAA51782.1.
CCDSiCCDS6933.1.
PIRiA01195. AJHURS.
RefSeqiNP_000041.2. NM_000050.4.
NP_446464.1. NM_054012.3.
XP_005272257.1. XM_005272200.2.
UniGeneiHs.160786.

Genome annotation databases

EnsembliENST00000352480; ENSP00000253004; ENSG00000130707.
ENST00000372393; ENSP00000361469; ENSG00000130707.
ENST00000372394; ENSP00000361471; ENSG00000130707.
GeneIDi445.
KEGGihsa:445.
UCSCiuc004bzm.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01630 mRNA. Translation: CAA25771.1.
L00084
, L00079, L00080, L00081, L00082, L00083 Genomic DNA. Translation: AAA51783.1.
AY034076 Genomic DNA. Translation: AAK67487.1.
AK027126 mRNA. No translation available.
BC009243 mRNA. Translation: AAH09243.1.
BC021676 mRNA. Translation: AAH21676.1.
M34903 Genomic DNA. Translation: AAA51782.1.
CCDSiCCDS6933.1.
PIRiA01195. AJHURS.
RefSeqiNP_000041.2. NM_000050.4.
NP_446464.1. NM_054012.3.
XP_005272257.1. XM_005272200.2.
UniGeneiHs.160786.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NZ2X-ray2.40A1-412[»]
ProteinModelPortaliP00966.
SMRiP00966. Positions 4-407.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106937. 41 interactions.
DIPiDIP-34055N.
IntActiP00966. 13 interactions.
MINTiMINT-5000467.
STRINGi9606.ENSP00000253004.

Chemistry

DrugBankiDB00171. Adenosine triphosphate.
DB00125. L-Arginine.
DB00128. L-Aspartic Acid.
DB00155. L-Citrulline.

PTM databases

PhosphoSiteiP00966.

Polymorphism and mutation databases

BioMutaiASS1.
DMDMi20141195.

Proteomic databases

MaxQBiP00966.
PaxDbiP00966.
PRIDEiP00966.

Protocols and materials databases

DNASUi445.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000352480; ENSP00000253004; ENSG00000130707.
ENST00000372393; ENSP00000361469; ENSG00000130707.
ENST00000372394; ENSP00000361471; ENSG00000130707.
GeneIDi445.
KEGGihsa:445.
UCSCiuc004bzm.3. human.

Organism-specific databases

CTDi445.
GeneCardsiGC09P133320.
GeneReviewsiASS1.
H-InvDBHIX0025782.
HGNCiHGNC:758. ASS1.
HPAiHPA020896.
HPA020934.
MIMi215700. phenotype.
603470. gene.
neXtProtiNX_P00966.
Orphaneti247546. Acute neonatal citrullinemia type I.
247573. Adult-onset citrullinemia type I.
PharmGKBiPA162376926.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0137.
GeneTreeiENSGT00390000004524.
HOGENOMiHOG000230093.
HOVERGENiHBG001717.
InParanoidiP00966.
KOiK01940.
OMAiIYNGYWW.
OrthoDBiEOG7PVWPB.
PhylomeDBiP00966.
TreeFamiTF300736.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.
UPA00158; UER00272.
BioCyciMetaCyc:HS05425-MONOMER.
BRENDAi6.3.4.5. 2681.
ReactomeiREACT_847. Urea cycle.
SABIO-RKP00966.

Miscellaneous databases

EvolutionaryTraceiP00966.
GeneWikiiArgininosuccinate_synthetase_1.
GenomeRNAii445.
NextBioi1871.
PROiP00966.
SOURCEiSearch...

Gene expression databases

BgeeiP00966.
CleanExiHS_ASS1.
ExpressionAtlasiP00966. baseline and differential.
GenevisibleiP00966. HS.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00005. Arg_succ_synth_type1.
InterProiIPR001518. 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.
[Graphical view]
PfamiPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00032. argG. 1 hit.
PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence for human argininosuccinate synthetase cDNA."
    Bock H.-G.O., Su T.-S., O'Brien W.E., Beaudet A.L.
    Nucleic Acids Res. 11:6505-6512(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular structures of human argininosuccinate synthetase pseudogenes. Evolutionary and mechanistic implications."
    Freytag S.O., Bock H.-G.O., Beaudet A.L., O'Brien W.E.
    J. Biol. Chem. 259:3160-3166(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Structure of the human argininosuccinate synthetase gene and an improved system for molecular diagnostics in patients with classical and mild citrullinemia."
    Haeberle J., Pauli S., Linnebank M., Kleijer W.J., Bakker H.D., Wanders R.J.A., Harms E., Koch H.G.
    Hum. Genet. 110:327-333(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CTLN1 LEU-108; ARG-179; VAL-362 AND ARG-390.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Small intestine.
  5. "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].
    Tissue: Kidney and Muscle.
  6. "Structure of the 5' end region of the human argininosuccinate synthetase gene."
    Jinno Y., Nomiyama H., Matuo S., Shimada K., Matsuda I., Saheki T.
    J. Inherit. Metab. Dis. 8:157-159(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
  7. "Identification of essential arginine residue(s) for Mg-ATP binding of human argininosuccinate synthetase."
    Isashiki Y., Noda T., Kobayashi K., Sase M., Saheki T., Titani K.
    Protein Seq. Data Anal. 2:283-287(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 148-161.
  8. "A two-dimensional gel database of human colon carcinoma proteins."
    Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
    Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 200-209.
    Tissue: Colon carcinoma.
  9. "Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein."
    Zheng X., Dai X., Zhao Y., Chen Q., Lu F., Yao D., Yu Q., Liu X., Zhang C., Gu X., Luo M.
    Proc. Natl. Acad. Sci. U.S.A. 104:8809-8814(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NMRAL1.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180 AND THR-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-113 AND THR-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH CITRULLINE AND ASPARTATE, SUBUNIT.
  14. "Mutations and polymorphisms in the human argininosuccinate synthetase (ASS1) gene."
    Engel K., Hoehne W., Haeberle J.
    Hum. Mutat. 30:300-307(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  15. "Heterogeneity of mutations in argininosuccinate synthetase causing human citrullinemia."
    Kobayashi K., Jackson M.J., Tick D.B., O'Brien W.E., Beaudet A.L.
    J. Biol. Chem. 265:11361-11367(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CTLN1 SER-14; HIS-157; ASN-180; TRP-304; SER-324; TRP-363 AND ARG-390.
  16. "Additional mutations in argininosuccinate synthetase causing citrullinemia."
    Kobayashi K., Rosenbloom C., Beaudet A.L., O'Brien W.E.
    Mol. Biol. Med. 8:95-100(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CTLN1 LEU-18 AND CYS-86.
  17. "Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia."
    Kobayashi K., Shaheen N., Terazono H., Saheki T.
    Am. J. Hum. Genet. 55:1103-1112(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CTLN1 THR-118; VAL-192; CYS-272; ARG-280; TRP-304 AND LEU-363.
  18. "Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells."
    Shaheen N., Kobayashi K., Terazono H., Fukushige T., Horiuchi M., Saheki T.
    Enzyme Protein 48:251-264(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF SOME CTLN1 VARIANTS.
  19. Cited for: VARIANTS CTLN1 ALA-69; LEU-108; ASP-117; ILE-119; GLN-270 AND ARG-390.
  20. Cited for: VARIANTS CTLN1 ARG-19; HIS-86; SER-95; SER-96; ASP-117; SER-117; CYS-157; ARG-179; LYS-191; HIS-265; MET-269; CYS-272; LYS-283; TRP-304; GLN-310; SER-324; VAL-362; GLN-363; TRP-363; ILE-389 AND ARG-390.
  21. "Mild citrullinemia in Caucasians is an allelic variant of argininosuccinate synthetase deficiency (citrullinemia type 1)."
    Haeberle J., Pauli S., Schmidt E., Schulze-Eilfing B., Berning C., Koch H.G.
    Mol. Genet. Metab. 80:302-306(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CTLN1 SER-14; LEU-40; GLN-127; ARG-179; ASP-190; MET-263; MET-269; SER-324 AND VAL-362.
  22. "Prenatal diagnosis of citrullinemia and argininosuccinic aciduria: evidence for a transmission ratio distortion in citrullinemia."
    Kleijer W.J., Garritsen V.H., van der Sterre M.L., Berning C., Haeberle J., Huijmans J.G.M.
    Prenat. Diagn. 26:242-247(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CTLN1 ASN-124; HIS-157; GLN-270; GLN-279; LYS-283; SER-324; GLY-363 AND ARG-390.
  23. "Functional analysis of novel splicing and missense mutations identified in the ASS1 gene in classical citrullinemia patients."
    Kimani J.K., Wei T., Chol K., Li Y., Yu P., Ye S., Huang X., Qi M.
    Clin. Chim. Acta 438:323-329(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CTLN1 GLY-141 AND CYS-265.

Entry informationi

Entry nameiASSY_HUMAN
AccessioniPrimary (citable) accession number: P00966
Secondary accession number(s): Q6LDL2, Q86UZ0, Q96GT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 3, 2002
Last modified: July 22, 2015
This is version 179 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.