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P00966

- ASSY_HUMAN

UniProt

P00966 - ASSY_HUMAN

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Protein
Argininosuccinate synthase
Gene
ASS1, ASS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei87 – 871Citrulline
Binding sitei92 – 921Citrulline
Binding sitei119 – 1191Aspartate
Binding sitei123 – 1231Aspartate
Binding sitei123 – 1231Citrulline
Binding sitei124 – 1241Aspartate
Binding sitei127 – 1271Citrulline
Binding sitei180 – 1801Citrulline
Binding sitei189 – 1891Citrulline
Binding sitei270 – 2701Citrulline
Binding sitei282 – 2821Citrulline

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. amino acid binding Source: BHF-UCL
  3. argininosuccinate synthase activity Source: BHF-UCL
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. arginine biosynthetic process Source: UniProtKB-UniPathway
  2. argininosuccinate metabolic process Source: BHF-UCL
  3. aspartate metabolic process Source: BHF-UCL
  4. cellular nitrogen compound metabolic process Source: Reactome
  5. cellular response to laminar fluid shear stress Source: BHF-UCL
  6. citrulline metabolic process Source: BHF-UCL
  7. negative regulation of leukocyte cell-cell adhesion Source: BHF-UCL
  8. positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
  9. small molecule metabolic process Source: Reactome
  10. urea cycle Source: BHF-UCL
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.
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: Chromosome 9

Organism-specific databases

HGNCiHGNC:758. ASS1.

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

Citrullinemia 1 (CTLN1) [MIM:215700]: The 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.9 Publications
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 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.
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412Argininosuccinate synthaseUniRule annotation
PRO_0000148554Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801Phosphoserine1 Publication
Modified residuei219 – 2191Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP00966.
PaxDbiP00966.
PRIDEiP00966.

PTM databases

PhosphoSiteiP00966.

Expressioni

Gene expression databases

ArrayExpressiP00966.
BgeeiP00966.
CleanExiHS_ASS1.
GenevestigatoriP00966.

Organism-specific databases

HPAiHPA020896.
HPA020934.

Interactioni

Subunit structurei

Homotetramer. Interacts with NMRAL1.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi106937. 39 interactions.
IntActiP00966. 13 interactions.
MINTiMINT-5000467.
STRINGi9606.ENSP00000253004.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NZ2X-ray2.40A1-412[»]
ProteinModelPortaliP00966.
SMRiP00966. Positions 4-407.

Miscellaneous databases

EvolutionaryTraceiP00966.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0137.
HOGENOMiHOG000230093.
HOVERGENiHBG001717.
InParanoidiP00966.
KOiK01940.
OMAiQGDYEPA.
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

MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK    50
ALKLGAKKVF IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR 100
KQVEIAQREG AKYVSHGATG KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF 150
YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS MDENLMHISY EAGILENPKN 200
QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD GTTHQTSLEL 250
FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF 300
TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ 350
VSVLKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK 400
EYHRLQSKVT AK 412
Length:412
Mass (Da):46,530
Last modified:April 3, 2002 - v2
Checksum:i47CAD2373AE47E47
GO

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 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.
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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti325 – 3273FWH → LRP in CAA25771. 1 Publication
Sequence conflicti325 – 3273FWH → LRP in AAA51783. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005272200.1.
UniGeneiHs.160786.

Genome annotation databases

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

Polymorphism databases

DMDMi20141195.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6933.1.
PIRi A01195. AJHURS.
RefSeqi NP_000041.2. NM_000050.4.
NP_446464.1. NM_054012.3.
XP_005272257.1. XM_005272200.1.
UniGenei Hs.160786.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NZ2 X-ray 2.40 A 1-412 [» ]
ProteinModelPortali P00966.
SMRi P00966. Positions 4-407.
ModBasei Search...

Protein-protein interaction databases

BioGridi 106937. 39 interactions.
IntActi P00966. 13 interactions.
MINTi MINT-5000467.
STRINGi 9606.ENSP00000253004.

Chemistry

DrugBanki DB00171. Adenosine triphosphate.
DB00125. L-Arginine.
DB00128. L-Aspartic Acid.
DB00155. L-Citrulline.

PTM databases

PhosphoSitei P00966.

Polymorphism databases

DMDMi 20141195.

Proteomic databases

MaxQBi P00966.
PaxDbi P00966.
PRIDEi P00966.

Protocols and materials databases

DNASUi 445.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000352480 ; ENSP00000253004 ; ENSG00000130707 .
ENST00000372393 ; ENSP00000361469 ; ENSG00000130707 .
ENST00000372394 ; ENSP00000361471 ; ENSG00000130707 .
GeneIDi 445.
KEGGi hsa:445.
UCSCi uc004bzm.3. human.

Organism-specific databases

CTDi 445.
GeneCardsi GC09P133320.
GeneReviewsi ASS1.
H-InvDB HIX0025782.
HGNCi HGNC:758. ASS1.
HPAi HPA020896.
HPA020934.
MIMi 215700. phenotype.
603470. gene.
neXtProti NX_P00966.
Orphaneti 247546. Acute neonatal citrullinemia type I.
247573. Adult-onset citrullinemia type I.
PharmGKBi PA162376926.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0137.
HOGENOMi HOG000230093.
HOVERGENi HBG001717.
InParanoidi P00966.
KOi K01940.
OMAi QGDYEPA.
OrthoDBi EOG7PVWPB.
PhylomeDBi P00966.
TreeFami TF300736.

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00113 .
UPA00158 ; UER00272 .
BioCyci MetaCyc:HS05425-MONOMER.
Reactomei REACT_847. Urea cycle.
SABIO-RK P00966.

Miscellaneous databases

EvolutionaryTracei P00966.
GeneWikii Argininosuccinate_synthetase_1.
GenomeRNAii 445.
NextBioi 1871.
PROi P00966.
SOURCEi Search...

Gene expression databases

ArrayExpressi P00966.
Bgeei P00966.
CleanExi HS_ASS1.
Genevestigatori P00966.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPi MF_00005. Arg_succ_synth_type1.
InterProi 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.
[Graphical view ]
Pfami PF00764. Arginosuc_synth. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00032. argG. 1 hit.
PROSITEi PS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH CITRULLINE AND ASPARTATE, SUBUNIT.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. Cited for: VARIANTS CTLN1 ALA-69; LEU-108; ASP-117; ILE-119; GLN-270 AND ARG-390.
  19. 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.
  20. "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.
  21. "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.

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: September 3, 2014
This is version 168 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

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