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Protein

Asparagine synthetase [glutamine-hydrolyzing]

Gene

ASNS

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

Functioni

Catalytic activityi

ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.1 Publication

Pathway:iL-asparagine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route).
Proteins known to be involved in this subpathway in this organism are:
  1. Asparagine synthetase [glutamine-hydrolyzing] (ASNS)
This subpathway is part of the pathway L-asparagine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route), the pathway L-asparagine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21For GATase activity2 Publications
Binding sitei97 – 971GlutamineBy similarity
Binding sitei256 – 2561ATP; via carbonyl oxygenBy similarity
Binding sitei288 – 2881ATP; via amide nitrogen and carbonyl oxygenBy similarity
Sitei365 – 3651Important for beta-aspartyl-AMP intermediate formationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi363 – 3642ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Asparagine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.5.4. 2681.
ReactomeiREACT_18355. ATF4 activates genes.
REACT_238. Amino acid synthesis and interconversion (transamination).
UniPathwayiUPA00134; UER00195.

Protein family/group databases

MEROPSiC44.974.

Names & Taxonomyi

Protein namesi
Recommended name:
Asparagine synthetase [glutamine-hydrolyzing] (EC:6.3.5.4)
Alternative name(s):
Cell cycle control protein TS11
Glutamine-dependent asparagine synthetase
Gene namesi
Name:ASNS
Synonyms:TS11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:753. ASNS.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Asparagine synthetase deficiency (ASNSD)1 Publication

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

Disease descriptionAn inborn error of asparagine biosynthesis that results in a severe neurologic disorder characterized by microcephaly, severely delayed psychomotor development, progressive encephalopathy, cortical atrophy, and seizure or hyperekplexic activity.

See also OMIM:615574
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61A → E in ASNSD; dramatic reduction in protein abundance. 1 Publication
VAR_070896
Natural varianti362 – 3621F → V in ASNSD; dramatic reduction in protein abundance. 1 Publication
VAR_070897
Natural varianti550 – 5501R → C in ASNSD; increases level of protein abundance. 1 Publication
VAR_070898

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21C → A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected. 1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi615574. phenotype.
Orphaneti391376. Congenital microcephaly-severe encephalopathy-progressive cerebral atrophy syndrome.
PharmGKBiPA25052.

Chemistry

DrugBankiDB00171. Adenosine triphosphate.
DB00174. L-Asparagine.
DB00128. L-Aspartic Acid.
DB00130. L-Glutamine.

Polymorphism and mutation databases

BioMutaiASNS.
DMDMi13432102.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 561560Asparagine synthetase [glutamine-hydrolyzing]PRO_0000056910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei385 – 3851N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP08243.
PaxDbiP08243.
PeptideAtlasiP08243.
PRIDEiP08243.

PTM databases

PhosphoSiteiP08243.

Expressioni

Gene expression databases

BgeeiP08243.
CleanExiHS_ASNS.
ExpressionAtlasiP08243. baseline and differential.
GenevisibleiP08243. HS.

Organism-specific databases

HPAiHPA004924.
HPA029318.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TRIM69Q86WT63EBI-722989,EBI-749955
WDR27A2RRH53EBI-722989,EBI-9476803

Protein-protein interaction databases

BioGridi106932. 44 interactions.
IntActiP08243. 7 interactions.
MINTiMINT-1371662.
STRINGi9606.ENSP00000175506.

Structurei

3D structure databases

ProteinModelPortaliP08243.
SMRiP08243. Positions 226-481.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 191190Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST
Domaini213 – 536324Asparagine synthetaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 535Glutamine bindingBy similarity
Regioni75 – 773Glutamine bindingBy similarity

Sequence similaritiesi

Contains 1 asparagine synthetase domain.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0367.
GeneTreeiENSGT00390000001994.
HOGENOMiHOG000027493.
HOVERGENiHBG003103.
InParanoidiP08243.
KOiK01953.
OMAiDWSGIYS.
OrthoDBiEOG75MVVS.
PhylomeDBiP08243.
TreeFamiTF300603.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProiIPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P08243-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL
60 70 80 90 100
AVVDPLFGMQ PIRVKKYPYL WLCYNGEIYN HKKMQQHFEF EYQTKVDGEI
110 120 130 140 150
ILHLYDKGGI EQTICMLDGV FAFVLLDTAN KKVFLGRDTY GVRPLFKAMT
160 170 180 190 200
EDGFLAVCSE AKGLVTLKHS ATPFLKVEPF LPGHYEVLDL KPNGKVASVE
210 220 230 240 250
MVKYHHCRDV PLHALYDNVE KLFPGFEIET VKNNLRILFN NAVKKRLMTD
260 270 280 290 300
RRIGCLLSGG LDSSLVAATL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR
310 320 330 340 350
KVADHIGSEH YEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK
360 370 380 390 400
YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLRELYLF
410 420 430 440 450
DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPEMRIPK NGIEKHLLRE
460 470 480 490 500
TFEDSNLIPK EILWRPKEAF SDGITSVKNS WFKILQEYVE HQVDDAMMAN
510 520 530 540 550
AAQKFPFNTP KTKEGYYYRQ VFERHYPGRA DWLSHYWMPK WINATDPSAR
560
TLTHYKSAVK A
Length:561
Mass (Da):64,370
Last modified:January 23, 2007 - v4
Checksum:i3E9B75E21D799FBE
GO
Isoform 2 (identifier: P08243-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.

Note: No experimental confirmation available.
Show »
Length:540
Mass (Da):62,168
Checksum:i7531F53E232D5AB0
GO
Isoform 3 (identifier: P08243-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: Missing.

Note: No experimental confirmation available.
Show »
Length:478
Mass (Da):54,818
Checksum:iF8AE4D4375F38522
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti333 – 34311TYDITTVRASV → LMTLQQFVLRI in AAA36781 (PubMed:3470743).CuratedAdd
BLAST
Sequence conflicti353 – 3608RKNTDSVV → GRTQIAWL in AAA36781 (PubMed:3470743).Curated
Sequence conflicti426 – 4261S → F (PubMed:2886907).Curated
Sequence conflicti426 – 4261S → F (PubMed:2565875).Curated
Sequence conflicti462 – 4621I → V in BAG63553 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61A → E in ASNSD; dramatic reduction in protein abundance. 1 Publication
VAR_070896
Natural varianti210 – 2101V → E.5 Publications
Corresponds to variant rs1049674 [ dbSNP | Ensembl ].
VAR_023443
Natural varianti362 – 3621F → V in ASNSD; dramatic reduction in protein abundance. 1 Publication
VAR_070897
Natural varianti550 – 5501R → C in ASNSD; increases level of protein abundance. 1 Publication
VAR_070898

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8383Missing in isoform 3. 1 PublicationVSP_045817Add
BLAST
Alternative sequencei1 – 2121Missing in isoform 2. 1 PublicationVSP_045818Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS55131.1. [P08243-3]
CCDS55132.1. [P08243-2]
CCDS5652.1. [P08243-1]
PIRiA27062. AJHUN1.
RefSeqiNP_001171546.1. NM_001178075.1. [P08243-2]
NP_001171547.1. NM_001178076.1. [P08243-3]
NP_001171548.1. NM_001178077.1. [P08243-3]
NP_001664.3. NM_001673.4. [P08243-1]
NP_597680.2. NM_133436.3. [P08243-1]
NP_899199.2. NM_183356.3. [P08243-1]
UniGeneiHs.489207.

Genome annotation databases

EnsembliENST00000175506; ENSP00000175506; ENSG00000070669.
ENST00000394308; ENSP00000377845; ENSG00000070669.
ENST00000394309; ENSP00000377846; ENSG00000070669.
ENST00000422745; ENSP00000414901; ENSG00000070669. [P08243-2]
ENST00000437628; ENSP00000414379; ENSG00000070669. [P08243-3]
ENST00000444334; ENSP00000406994; ENSG00000070669. [P08243-2]
ENST00000455086; ENSP00000408472; ENSG00000070669. [P08243-3]
GeneIDi440.
KEGGihsa:440.
UCSCiuc003uot.4. human. [P08243-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS55131.1. [P08243-3]
CCDS55132.1. [P08243-2]
CCDS5652.1. [P08243-1]
PIRiA27062. AJHUN1.
RefSeqiNP_001171546.1. NM_001178075.1. [P08243-2]
NP_001171547.1. NM_001178076.1. [P08243-3]
NP_001171548.1. NM_001178077.1. [P08243-3]
NP_001664.3. NM_001673.4. [P08243-1]
NP_597680.2. NM_133436.3. [P08243-1]
NP_899199.2. NM_183356.3. [P08243-1]
UniGeneiHs.489207.

3D structure databases

ProteinModelPortaliP08243.
SMRiP08243. Positions 226-481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106932. 44 interactions.
IntActiP08243. 7 interactions.
MINTiMINT-1371662.
STRINGi9606.ENSP00000175506.

Chemistry

BindingDBiP08243.
ChEMBLiCHEMBL3120.
DrugBankiDB00171. Adenosine triphosphate.
DB00174. L-Asparagine.
DB00128. L-Aspartic Acid.
DB00130. L-Glutamine.

Protein family/group databases

MEROPSiC44.974.

PTM databases

PhosphoSiteiP08243.

Polymorphism and mutation databases

BioMutaiASNS.
DMDMi13432102.

Proteomic databases

MaxQBiP08243.
PaxDbiP08243.
PeptideAtlasiP08243.
PRIDEiP08243.

Protocols and materials databases

DNASUi440.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000175506; ENSP00000175506; ENSG00000070669.
ENST00000394308; ENSP00000377845; ENSG00000070669.
ENST00000394309; ENSP00000377846; ENSG00000070669.
ENST00000422745; ENSP00000414901; ENSG00000070669. [P08243-2]
ENST00000437628; ENSP00000414379; ENSG00000070669. [P08243-3]
ENST00000444334; ENSP00000406994; ENSG00000070669. [P08243-2]
ENST00000455086; ENSP00000408472; ENSG00000070669. [P08243-3]
GeneIDi440.
KEGGihsa:440.
UCSCiuc003uot.4. human. [P08243-1]

Organism-specific databases

CTDi440.
GeneCardsiGC07M097481.
HGNCiHGNC:753. ASNS.
HPAiHPA004924.
HPA029318.
MIMi108370. gene.
615574. phenotype.
neXtProtiNX_P08243.
Orphaneti391376. Congenital microcephaly-severe encephalopathy-progressive cerebral atrophy syndrome.
PharmGKBiPA25052.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0367.
GeneTreeiENSGT00390000001994.
HOGENOMiHOG000027493.
HOVERGENiHBG003103.
InParanoidiP08243.
KOiK01953.
OMAiDWSGIYS.
OrthoDBiEOG75MVVS.
PhylomeDBiP08243.
TreeFamiTF300603.

Enzyme and pathway databases

UniPathwayiUPA00134; UER00195.
BRENDAi6.3.5.4. 2681.
ReactomeiREACT_18355. ATF4 activates genes.
REACT_238. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

GenomeRNAii440.
NextBioi1843.
PROiP08243.
SOURCEiSearch...

Gene expression databases

BgeeiP08243.
CleanExiHS_ASNS.
ExpressionAtlasiP08243. baseline and differential.
GenevisibleiP08243. HS.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProiIPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, CATALYTIC ACTIVITY, ACTIVE SITE.
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: VARIANTS ASNSD GLU-6; VAL-362 AND CYS-550, CHARACTERIZATION OF VARIANTS ASNSD GLU-6; VAL-362 AND CYS-550.

Entry informationi

Entry nameiASNS_HUMAN
AccessioniPrimary (citable) accession number: P08243
Secondary accession number(s): A4D1I8
, B4DXZ1, B7ZAA9, D6W5R3, E9PCI3, E9PCX6, P08184, Q15666, Q549T9, Q96HD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 174 of the entry and version 4 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

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