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P08243 (ASNS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Asparagine synthetase [glutamine-hydrolyzing]

EC=6.3.5.4
Alternative name(s):
Cell cycle control protein TS11
Glutamine-dependent asparagine synthetase
Gene names
Name:ASNS
Synonyms:TS11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.

Pathway

Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.

Sequence similarities

Contains 1 asparagine synthetase domain.

Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Asparagine biosynthesis
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainGlutamine amidotransferase
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-asparagine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

asparagine biosynthetic process

Inferred by curator Ref.11. Source: UniProtKB

cellular amino acid biosynthetic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to glucose starvation

Inferred from direct assay PubMed 10085239. Source: UniProtKB

cellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

glutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

liver development

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 17409444. Source: UniProtKB

positive regulation of mitotic cell cycle

Inferred from direct assay Ref.10. Source: UniProtKB

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to follicle-stimulating hormone

Inferred from electronic annotation. Source: Ensembl

response to light stimulus

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to methotrexate

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

asparagine synthase (glutamine-hydrolyzing) activity

Inferred from direct assay PubMed 16023613Ref.11Ref.10Ref.1. Source: UniProtKB

cofactor binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P08243-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P08243-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P08243-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 561560Asparagine synthetase [glutamine-hydrolyzing]
PRO_0000056910

Regions

Domain2 – 191190Glutamine amidotransferase type-2
Domain213 – 536324Asparagine synthetase
Nucleotide binding363 – 3642ATP By similarity
Region49 – 535Glutamine binding By similarity
Region75 – 773Glutamine binding By similarity

Sites

Active site21For GATase activity Ref.11
Binding site971Glutamine By similarity
Binding site2561ATP; via carbonyl oxygen By similarity
Binding site2881ATP; via amide nitrogen and carbonyl oxygen By similarity
Site3651Important for beta-aspartyl-AMP intermediate formation By similarity

Amino acid modifications

Modified residue3851N6-acetyllysine Ref.13

Natural variations

Alternative sequence1 – 8383Missing in isoform 3.
VSP_045817
Alternative sequence1 – 2121Missing in isoform 2.
VSP_045818
Natural variant2101V → E. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
Corresponds to variant rs1049674 [ dbSNP | Ensembl ].
VAR_023443

Experimental info

Mutagenesis21C → A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected. Ref.12
Sequence conflict333 – 34311TYDITTVRASV → LMTLQQFVLRI in AAA36781. Ref.9
Sequence conflict353 – 3608RKNTDSVV → GRTQIAWL in AAA36781. Ref.9
Sequence conflict4261S → F Ref.1
Sequence conflict4261S → F Ref.2
Sequence conflict4621I → V in BAG63553. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 3E9B75E21D799FBE

FASTA56164,370
        10         20         30         40         50         60 
MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ 

        70         80         90        100        110        120 
PIRVKKYPYL WLCYNGEIYN HKKMQQHFEF EYQTKVDGEI ILHLYDKGGI EQTICMLDGV 

       130        140        150        160        170        180 
FAFVLLDTAN KKVFLGRDTY GVRPLFKAMT EDGFLAVCSE AKGLVTLKHS ATPFLKVEPF 

       190        200        210        220        230        240 
LPGHYEVLDL KPNGKVASVE MVKYHHCRDV PLHALYDNVE KLFPGFEIET VKNNLRILFN 

       250        260        270        280        290        300 
NAVKKRLMTD RRIGCLLSGG LDSSLVAATL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR 

       310        320        330        340        350        360 
KVADHIGSEH YEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV 

       370        380        390        400        410        420 
IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLRELYLF DVLRADRTTA AHGLELRVPF 

       430        440        450        460        470        480 
LDHRFSSYYL SLPPEMRIPK NGIEKHLLRE TFEDSNLIPK EILWRPKEAF SDGITSVKNS 

       490        500        510        520        530        540 
WFKILQEYVE HQVDDAMMAN AAQKFPFNTP KTKEGYYYRQ VFERHYPGRA DWLSHYWMPK 

       550        560 
WINATDPSAR TLTHYKSAVK A 

« Hide

Isoform 2 [UniParc].

Checksum: 7531F53E232D5AB0
Show »

FASTA54062,168
Isoform 3 [UniParc].

Checksum: F8AE4D4375F38522
Show »

FASTA47854,818

References

« Hide 'large scale' references
[1]"Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells."
Andrulis I.L., Chen J., Ray P.N.
Mol. Cell. Biol. 7:2435-2443(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular structure of the human asparagine synthetase gene."
Zhang Y.P., Lambert M.A., Cairney A.E., Wills D., Ray P.N., Andrulis I.L.
Genomics 4:259-265(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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] (ISOFORMS 2 AND 3), VARIANT GLU-210.
Tissue: Testis.
[5]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-210.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-210.
[7]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-210.
[8]"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] (ISOFORM 1), VARIANT GLU-210.
Tissue: Muscle.
[9]"Molecular cloning of a gene that is necessary for G1 progression in mammalian cells."
Greco A., Ittmann M., Basilico C.
Proc. Natl. Acad. Sci. U.S.A. 84:1565-1569(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-561 (ISOFORM 1).
[10]"Organization and expression of the cell cycle gene, ts11, that encodes asparagine synthetase."
Greco A., Gong S.S., Ittmann M., Basilico C.
Mol. Cell. Biol. 9:2350-2359(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-83.
[11]"Expression of human asparagine synthetase in Escherichia coli."
van Heeke G., Schuster S.M.
J. Biol. Chem. 264:5503-5509(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[12]"The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity."
van Heeke G., Schuster S.M.
J. Biol. Chem. 264:19475-19477(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-2.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27396 mRNA. Translation: AAA51789.1.
L35946 expand/collapse EMBL AC list , L35936, L35937, L35938, L35939, L35940, L35941, L35942, L35943, L35944, L35945 Genomic DNA. Translation: AAA52756.1.
BT007113 mRNA. Translation: AAP35777.1.
AK302189 mRNA. Translation: BAG63553.1.
AK316224 mRNA. Translation: BAH14595.1.
AC005326 Genomic DNA. No translation available.
AC079781 Genomic DNA. Translation: AAQ96856.1.
CH236949 Genomic DNA. Translation: EAL24115.1.
CH471091 Genomic DNA. Translation: EAW76730.1.
CH471091 Genomic DNA. Translation: EAW76723.1.
CH471091 Genomic DNA. Translation: EAW76731.1.
CH471091 Genomic DNA. Translation: EAW76732.1.
CH471091 Genomic DNA. Translation: EAW76733.1.
BC008723 mRNA. Translation: AAH08723.1.
BC014621 mRNA. Translation: AAH14621.1.
M15798 mRNA. Translation: AAA36781.1.
M27054 Genomic DNA. Translation: AAA63266.1.
PIRAJHUN1. A27062.
RefSeqNP_001171546.1. NM_001178075.1.
NP_001171547.1. NM_001178076.1.
NP_001171548.1. NM_001178077.1.
NP_001664.3. NM_001673.4.
NP_597680.2. NM_133436.3.
NP_899199.2. NM_183356.3.
UniGeneHs.489207.

3D structure databases

ProteinModelPortalP08243.
SMRP08243. Positions 2-531.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106932. 43 interactions.
IntActP08243. 5 interactions.
MINTMINT-1371662.
STRING9606.ENSP00000175506.

Chemistry

BindingDBP08243.
ChEMBLCHEMBL3120.
DrugBankDB00171. Adenosine triphosphate.
DB00174. L-Asparagine.
DB00128. L-Aspartic Acid.
DB00142. L-Glutamic Acid.
DB00130. L-Glutamine.

Protein family/group databases

MEROPSC44.974.

PTM databases

PhosphoSiteP08243.

Polymorphism databases

DMDM13432102.

Proteomic databases

PaxDbP08243.
PeptideAtlasP08243.
PRIDEP08243.

Protocols and materials databases

DNASU440.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000175506; ENSP00000175506; ENSG00000070669. [P08243-1]
ENST00000394308; ENSP00000377845; ENSG00000070669. [P08243-1]
ENST00000394309; ENSP00000377846; ENSG00000070669. [P08243-1]
ENST00000422745; ENSP00000414901; ENSG00000070669. [P08243-2]
ENST00000437628; ENSP00000414379; ENSG00000070669. [P08243-3]
ENST00000444334; ENSP00000406994; ENSG00000070669. [P08243-2]
ENST00000455086; ENSP00000408472; ENSG00000070669. [P08243-3]
GeneID440.
KEGGhsa:440.
UCSCuc003uot.4. human. [P08243-1]

Organism-specific databases

CTD440.
GeneCardsGC07M097481.
HGNCHGNC:753. ASNS.
HPAHPA004924.
HPA029318.
MIM108370. gene.
neXtProtNX_P08243.
PharmGKBPA25052.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0367.
HOVERGENHBG003103.
InParanoidP08243.
KOK01953.
OMAYGWIDAL.
OrthoDBEOG75MVVS.
PhylomeDBP08243.
TreeFamTF300603.

Enzyme and pathway databases

BRENDA6.3.5.4. 2681.
ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
UniPathwayUPA00134; UER00195.

Gene expression databases

ArrayExpressP08243.
BgeeP08243.
CleanExHS_ASNS.
GenevestigatorP08243.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
PIRSFPIRSF001589. Asn_synthetase_glu-h. 1 hit.
TIGRFAMsTIGR01536. asn_synth_AEB. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi440.
NextBio1843.
PROP08243.
SOURCESearch...

Entry information

Entry nameASNS_HUMAN
AccessionPrimary (citable) accession number: P08243
Secondary accession number(s): A4D1I8 expand/collapse secondary AC list , B4DXZ1, B7ZAA9, D6W5R3, E9PCI3, E9PCX6, P08184, Q15666, Q549T9, Q96HD0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 160 of the entry and version 4 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

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 7

Human chromosome 7: entries, gene names and cross-references to MIM