P08243 (ASNS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	561 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Amino-acid biosynthesis Asparagine biosynthesis
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-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 response to glucose starvation Inferred from direct assay PubMed 10085239. Source: UniProtKB cellular response to hormone stimulus Inferred from electronic annotation. Source: Compara glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW liver development Inferred from electronic annotation. Source: Compara 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 stimulus Inferred from electronic annotation. Source: Compara response to follicle-stimulating hormone stimulus Inferred from electronic annotation. Source: Compara response to light stimulus Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to methotrexate Inferred from electronic annotation. Source: Compara response to toxin Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP 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: Compara
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 561	561	Asparagine synthetase [glutamine-hydrolyzing]		PRO_0000056910
Regions
	Domain	2 – 191	190	Glutamine amidotransferase type-2
	Domain	213 – 536	324	Asparagine synthetase
	Nucleotide binding	363 – 364	2	ATP By similarity
	Region	49 – 53	5	Glutamine binding By similarity
	Region	75 – 77	3	Glutamine binding By similarity
Sites
	Active site	2	1	For GATase activity Ref.11
	Binding site	97	1	Glutamine By similarity
	Binding site	256	1	ATP; via carbonyl oxygen By similarity
	Binding site	288	1	ATP; via amide nitrogen and carbonyl oxygen By similarity
	Site	365	1	Important for beta-aspartyl-AMP intermediate formation By similarity
Amino acid modifications
	Modified residue	385	1	N6-acetyllysine Ref.13
Natural variations
	Alternative sequence	1 – 83	83	Missing in isoform 3.		VSP_045817
	Alternative sequence	1 – 21	21	Missing in isoform 2.		VSP_045818
	Natural variant	210	1	V → E. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Corresponds to variant rs1049674 [ dbSNP | Ensembl ].		VAR_023443
Experimental info
	Mutagenesis	2	1	C → A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected. Ref.12
	Sequence conflict	333 – 343	11	TYDITTVRASV → LMTLQQFVLRI in AAA36781. Ref.9
	Sequence conflict	353 – 360	8	RKNTDSVV → GRTQIAWL in AAA36781. Ref.9
	Sequence conflict	426	1	S → F Ref.1
	Sequence conflict	426	1	S → F Ref.2
	Sequence conflict	462	1	I → V in BAG63553. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 3E9B75E21D799FBE	FASTA	561	64,370
	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
	Isoform 2 [UniParc]. Checksum: 7531F53E232D5AB0	FASTA	540	62,168
	10 20 30 40 50 60 MKIAHRGPDA FRFENVNGYT NCCFGFHRLA VVDPLFGMQP IRVKKYPYLW LCYNGEIYNH 70 80 90 100 110 120 KKMQQHFEFE YQTKVDGEII LHLYDKGGIE QTICMLDGVF AFVLLDTANK KVFLGRDTYG 130 140 150 160 170 180 VRPLFKAMTE DGFLAVCSEA KGLVTLKHSA TPFLKVEPFL PGHYEVLDLK PNGKVASVEM 190 200 210 220 230 240 VKYHHCRDVP LHALYDNVEK LFPGFEIETV KNNLRILFNN AVKKRLMTDR RIGCLLSGGL 250 260 270 280 290 300 DSSLVAATLL KQLKEAQVQY PLQTFAIGME DSPDLLAARK VADHIGSEHY EVLFNSEEGI 310 320 330 340 350 360 QALDEVIFSL ETYDITTVRA SVGMYLISKY IRKNTDSVVI FSGEGSDELT QGYIYFHKAP 370 380 390 400 410 420 SPEKAEEESE RLLRELYLFD VLRADRTTAA HGLELRVPFL DHRFSSYYLS LPPEMRIPKN 430 440 450 460 470 480 GIEKHLLRET FEDSNLIPKE ILWRPKEAFS DGITSVKNSW FKILQEYVEH QVDDAMMANA 490 500 510 520 530 540 AQKFPFNTPK TKEGYYYRQV FERHYPGRAD WLSHYWMPKW INATDPSART LTHYKSAVKA
	Isoform 3 [UniParc]. Checksum: F8AE4D4375F38522	FASTA	478	54,818
	10 20 30 40 50 60 MQQHFEFEYQ TKVDGEIILH LYDKGGIEQT ICMLDGVFAF VLLDTANKKV FLGRDTYGVR 70 80 90 100 110 120 PLFKAMTEDG FLAVCSEAKG LVTLKHSATP FLKVEPFLPG HYEVLDLKPN GKVASVEMVK 130 140 150 160 170 180 YHHCRDVPLH ALYDNVEKLF PGFEIETVKN NLRILFNNAV KKRLMTDRRI GCLLSGGLDS 190 200 210 220 230 240 SLVAATLLKQ LKEAQVQYPL QTFAIGMEDS PDLLAARKVA DHIGSEHYEV LFNSEEGIQA 250 260 270 280 290 300 LDEVIFSLET YDITTVRASV GMYLISKYIR KNTDSVVIFS GEGSDELTQG YIYFHKAPSP 310 320 330 340 350 360 EKAEEESERL LRELYLFDVL RADRTTAAHG LELRVPFLDH RFSSYYLSLP PEMRIPKNGI 370 380 390 400 410 420 EKHLLRETFE DSNLIPKEIL WRPKEAFSDG ITSVKNSWFK ILQEYVEHQV DDAMMANAAQ 430 440 450 460 470 KFPFNTPKTK EGYYYRQVFE RHYPGRADWL SHYWMPKWIN ATDPSARTLT HYKSAVKA

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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, MASS SPECTROMETRY.
[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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	M27396 mRNA. Translation: AAA51789.1. L35946 , 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.
IPI	IPI00554777. IPI00924906. IPI00925572.
PIR	AJHUN1. A27062.
RefSeq	NP_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.
UniGene	Hs.489207.
3D structure databases
ProteinModelPortal	P08243.
ModBase	Search...
Protein-protein interaction databases
IntAct	P08243. 5 interactions.
MINT	MINT-1371662.
STRING	9606.ENSP00000175506.
Protein family/group databases
MEROPS	C44.974.
PTM databases
PhosphoSite	P08243.
Polymorphism databases
DMDM	13432102.
Proteomic databases
PaxDb	P08243.
PeptideAtlas	P08243.
PRIDE	P08243.
Protocols and materials databases
DNASU	440.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000175506; ENSP00000175506; ENSG00000070669. ENST00000394308; ENSP00000377845; ENSG00000070669. ENST00000394309; ENSP00000377846; ENSG00000070669. ENST00000422745; ENSP00000414901; ENSG00000070669. ENST00000437628; ENSP00000414379; ENSG00000070669. ENST00000444334; ENSP00000406994; ENSG00000070669. ENST00000455086; ENSP00000408472; ENSG00000070669.
GeneID	440.
KEGG	hsa:440.
UCSC	uc003uot.4. human.
Organism-specific databases
CTD	440.
GeneCards	GC07M097481.
HGNC	HGNC:753. ASNS.
HPA	HPA029318.
MIM	108370. gene.
neXtProt	NX_P08243.
PharmGKB	PA25052.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0367.
HOVERGEN	HBG003103.
InParanoid	P08243.
KO	K01953.
OMA	VFERHYP.
OrthoDB	EOG4RV2R2.
PhylomeDB	P08243.
Enzyme and pathway databases
BRENDA	6.3.5.4. 2681.
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
UniPathway	UPA00134; UER00195.
Gene expression databases
ArrayExpress	P08243.
Bgee	P08243.
CleanEx	HS_ASNS.
Genevestigator	P08243.
GermOnline	ENSG00000070669. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
InterPro	IPR006426. Asn_synth_AEB. IPR001962. Asn_synthase. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF00733. Asn_synthase. 1 hit. PF13537. GATase_7. 1 hit. [Graphical view]
PIRSF	PIRSF001589. Asn_synthetase_glu-h. 1 hit.
TIGRFAMs	TIGR01536. asn_synth_AEB. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P08243.
ChEMBL	CHEMBL3120.
DrugBank	DB00171. Adenosine triphosphate. DB00174. L-Asparagine. DB00128. L-Aspartic Acid. DB00142. L-Glutamic Acid. DB00130. L-Glutamine.
GenomeRNAi	440.
NextBio	1843.
SOURCE	Search...

Entry information

Entry name

ASNS_HUMAN

Accession

Primary (citable) accession number: P08243
Secondary accession number(s): A4D1I8 , 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:	May 1, 2013
This is version 149 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.