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P00966 (ASSY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Argininosuccinate synthase

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Name:ASS1
Synonyms:ASS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is indirectly involved in the control of blood pressure By similarity. HAMAP-Rule MF_00005

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP-Rule MF_00005

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00005

Nitrogen metabolism; urea cycle; (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline: step 1/1. HAMAP-Rule MF_00005

Subunit structure

Homotetramer. Interacts with NMRAL1. Ref.9 Ref.12

Involvement in disease

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. Ref.3 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
Urea cycle
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

arginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

argininosuccinate metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to amine stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to ammonium ion

Inferred from electronic annotation. Source: Ensembl

cellular response to cAMP

Inferred from electronic annotation. Source: Ensembl

cellular response to dexamethasone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to glucagon stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to interferon-gamma

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

cellular response to oleic acid

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

diaphragm development

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

midgut development

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to growth hormone

Inferred from electronic annotation. Source: Ensembl

response to mycotoxin

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

urea cycle

Traceable author statement. Source: Reactome

   Cellular_componentcell body fiber

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

lysosome

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

perikaryon

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

argininosuccinate synthase activity

Inferred from experiment. Source: Reactome

toxic substance binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARAFP103984EBI-536842,EBI-365961

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 412412Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148554

Regions

Nucleotide binding10 – 189ATP By similarity
Nucleotide binding115 – 1239ATP By similarity

Sites

Binding site361ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site871Citrulline
Binding site921Citrulline
Binding site1191Aspartate
Binding site1231Aspartate
Binding site1231Citrulline
Binding site1241Aspartate
Binding site1271Citrulline
Binding site1801Citrulline
Binding site1891Citrulline
Binding site2701Citrulline
Binding site2821Citrulline

Amino acid modifications

Modified residue1801Phosphoserine Ref.10
Modified residue2191Phosphothreonine Ref.10

Natural variations

Natural variant141G → S in CTLN1. Ref.14 Ref.20
VAR_000681
Natural variant181S → L in CTLN1. Ref.15
VAR_000682
Natural variant191C → R in CTLN1. Ref.19
VAR_015891
Natural variant401Q → L in CTLN1. Ref.20
VAR_058337
Natural variant651S → I.
Corresponds to variant rs2229556 [ dbSNP | Ensembl ].
VAR_050427
Natural variant691V → A in CTLN1. Ref.18
VAR_016013
Natural variant791S → P in CTLN1.
VAR_058338
Natural variant861R → C in CTLN1. Ref.15
VAR_000683
Natural variant861R → H in CTLN1. Ref.19
VAR_015892
Natural variant951R → S in CTLN1. Ref.19
VAR_015893
Natural variant961P → H in CTLN1.
VAR_058339
Natural variant961P → S in CTLN1. Ref.19
VAR_015894
Natural variant1081R → L in CTLN1. Ref.3 Ref.18
Corresponds to variant rs35269064 [ dbSNP | Ensembl ].
VAR_016014
Natural variant1171G → D in CTLN1. Ref.18 Ref.19
VAR_015896
Natural variant1171G → S in CTLN1. Ref.19
VAR_015895
Natural variant1181A → T in CTLN1. Ref.16
VAR_000684
Natural variant1191T → I in CTLN1. Ref.18
VAR_016015
Natural variant1241D → N in CTLN1. Ref.21
VAR_058340
Natural variant1271R → Q in CTLN1. Ref.20
VAR_058341
Natural variant1271R → W in CTLN1; severe clinical course.
VAR_058342
Natural variant1571R → C in CTLN1. Ref.19
VAR_015897
Natural variant1571R → H in CTLN1. Ref.14 Ref.21
VAR_000685
Natural variant1601L → P in CTLN1.
VAR_058343
Natural variant1791W → R in CTLN1; mild. Ref.3 Ref.19 Ref.20
Corresponds to variant rs121908646 [ dbSNP | Ensembl ].
VAR_015898
Natural variant1801S → N in CTLN1. Ref.14
VAR_000686
Natural variant1901Y → D in CTLN1. Ref.20
VAR_058344
Natural variant1911E → K in CTLN1. Ref.19
VAR_015899
Natural variant1911E → Q in CTLN1.
VAR_058345
Natural variant1921A → V in CTLN1. Ref.16
VAR_000687
Natural variant2021A → E in CTLN1.
VAR_058346
Natural variant2061L → P in CTLN1.
VAR_058347
Natural variant2631V → M in CTLN1; mild clinical course. Ref.20
Corresponds to variant rs192838388 [ dbSNP | Ensembl ].
VAR_058348
Natural variant2651R → C in CTLN1; severe clinical course.
VAR_058349
Natural variant2651R → H in CTLN1. Ref.19
VAR_015900
Natural variant2691V → M in CTLN1. Ref.19 Ref.20
VAR_015901
Natural variant2701E → Q in CTLN1. Ref.18 Ref.21
VAR_016007
Natural variant2721R → C in CTLN1. Ref.16 Ref.19
VAR_000688
Natural variant2771K → T in CTLN1.
VAR_058350
Natural variant2791R → Q in CTLN1. Ref.21
VAR_016008
Natural variant2801G → R in CTLN1. Ref.16
VAR_000689
Natural variant2831E → K in CTLN1. Ref.19 Ref.21
VAR_015902
Natural variant2841T → I in CTLN1; mild clinical course.
VAR_058351
Natural variant2911Y → S in CTLN1.
VAR_058352
Natural variant2961D → G in CTLN1.
VAR_058353
Natural variant3021M → V in CTLN1.
VAR_058354
Natural variant3041R → W in CTLN1. Ref.14 Ref.16 Ref.19
VAR_000690
Natural variant3071R → C in CTLN1.
Corresponds to variant rs183276875 [ dbSNP | Ensembl ].
VAR_058355
Natural variant3101K → Q in CTLN1. Ref.19
VAR_016009
Natural variant3101K → R in CTLN1.
VAR_015903
Natural variant3241G → S in CTLN1. Ref.14 Ref.19 Ref.20 Ref.21
VAR_000691
Natural variant3241G → V in CTLN1.
VAR_058356
Natural variant3411S → F in CTLN1.
VAR_058357
Natural variant3451V → G in CTLN1.
VAR_058358
Natural variant3471G → R in CTLN1; severe clinical course.
VAR_058359
Natural variant3591Y → D in CTLN1; mild clinical course.
VAR_058360
Natural variant3621G → V in CTLN1; mild. Ref.3 Ref.19 Ref.20
VAR_015904
Natural variant3631R → G in CTLN1. Ref.21
VAR_016010
Natural variant3631R → L in CTLN1. Ref.16
VAR_000692
Natural variant3631R → Q in CTLN1. Ref.19
VAR_016011
Natural variant3631R → W in CTLN1. Ref.14 Ref.19
VAR_000693
Natural variant3891T → I in CTLN1. Ref.19
VAR_016012
Natural variant3901G → R in CTLN1. Ref.3 Ref.14 Ref.18 Ref.19 Ref.21
VAR_000694

Experimental info

Sequence conflict325 – 3273FWH → LRP in CAA25771. Ref.1
Sequence conflict325 – 3273FWH → LRP in AAA51783. Ref.2

Secondary structure

..................................................................... 412
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00966 [UniParc].

Last modified April 3, 2002. Version 2.
Checksum: 47CAD2373AE47E47

FASTA41246,530
        10         20         30         40         50         60 
MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF 

        70         80         90        100        110        120 
IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR KQVEIAQREG AKYVSHGATG 

       130        140        150        160        170        180 
KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS 

       190        200        210        220        230        240 
MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD 

       250        260        270        280        290        300 
GTTHQTSLEL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF 

       310        320        330        340        350        360 
TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ VSVLKGQVYI 

       370        380        390        400        410 
LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK EYHRLQSKVT AK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Structure of human argininosuccinate synthetase."
Karlberg T., Collins R., van den Berg S., Flores A., Hammarstrom M., Hogbom M., Holmberg Schiavone L., Uppenberg J.
Acta Crystallogr. D 64:279-286(2008) [PubMed] [Europe PMC] [Abstract]
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]"Phenotype and genotype heterogeneity in Mediterranean citrullinemia."
Vilaseca M.A., Kobayashi K., Briones P., Lambruschini N., Campistol J., Tabata A., Alomar A., Rodes M., Lluch M., Saheki T.
Mol. Genet. Metab. 74:396-398(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CTLN1 ALA-69; LEU-108; ASP-117; ILE-119; GLN-270 AND ARG-390.
[19]"Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients."
Gao H.-Z., Kobayashi K., Tabata A., Tsuge H., Iijima M., Yasuda T., Kalkanoglu H.S., Dursun A., Tokatli A., Coskun T., Trefz F.K., Skladal D., Mandel H., Seidel J., Kodama S., Shirane S., Ichida T., Makino S. expand/collapse author list , Yoshino M., Kang J.-H., Mizuguchi M., Barshop B.A., Fuchinoue S., Seneca S., Zeesman S., Knerr I., Rodes M., Wasant P., Yoshida I., De Meirleir L., Abdul-Jalil M., Begum L., Horiuchi M., Katunuma N., Nakagawa S., Saheki T.
Hum. Mutat. 22:24-34(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01630 mRNA. Translation: CAA25771.1.
L00084 expand/collapse EMBL AC list , 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.
PIRAJHURS. A01195.
RefSeqNP_000041.2. NM_000050.4.
NP_446464.1. NM_054012.3.
XP_005272257.1. XM_005272200.1.
UniGeneHs.160786.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NZ2X-ray2.40A1-412[»]
ProteinModelPortalP00966.
SMRP00966. Positions 4-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106937. 37 interactions.
IntActP00966. 13 interactions.
MINTMINT-5000467.
STRING9606.ENSP00000253004.

Chemistry

DrugBankDB00171. Adenosine triphosphate.
DB00125. L-Arginine.
DB00128. L-Aspartic Acid.
DB00155. L-Citrulline.

PTM databases

PhosphoSiteP00966.

Polymorphism databases

DMDM20141195.

Proteomic databases

PaxDbP00966.
PRIDEP00966.

Protocols and materials databases

DNASU445.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000352480; ENSP00000253004; ENSG00000130707.
ENST00000372393; ENSP00000361469; ENSG00000130707.
ENST00000372394; ENSP00000361471; ENSG00000130707.
GeneID445.
KEGGhsa:445.
UCSCuc004bzm.3. human.

Organism-specific databases

CTD445.
GeneCardsGC09P133320.
H-InvDBHIX0025782.
HGNCHGNC:758. ASS1.
HPAHPA020896.
HPA020934.
MIM215700. phenotype.
603470. gene.
neXtProtNX_P00966.
Orphanet247546. Acute neonatal citrullinemia type I.
247573. Adult-onset citrullinemia type I.
PharmGKBPA162376926.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
HOVERGENHBG001717.
InParanoidP00966.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG7PVWPB.
PhylomeDBP00966.
TreeFamTF300736.

Enzyme and pathway databases

BioCycMetaCyc:HS05425-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP00966.
UniPathwayUPA00068; UER00113.
UPA00158; UER00272.

Gene expression databases

ArrayExpressP00966.
BgeeP00966.
CleanExHS_ASS1.
GenevestigatorP00966.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00005. Arg_succ_synth_type1.
InterProIPR001518. 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]
PfamPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR00032. argG. 1 hit.
PROSITEPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00966.
GeneWikiArgininosuccinate_synthetase_1.
GenomeRNAi445.
NextBio1871.
PROP00966.
SOURCESearch...

Entry information

Entry nameASSY_HUMAN
AccessionPrimary (citable) accession number: P00966
Secondary accession number(s): Q6LDL2, Q86UZ0, Q96GT4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 3, 2002
Last modified: March 19, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM