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P08243

- ASNS_HUMAN

UniProt

P08243 - ASNS_HUMAN

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Protein
Asparagine synthetase [glutamine-hydrolyzing]
Gene
ASNS, TS11
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Pathwayi

Sites

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

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. asparagine synthase (glutamine-hydrolyzing) activity Source: UniProtKB
  3. cofactor binding Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. L-asparagine biosynthetic process Source: UniProtKB-UniPathway
  2. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  3. asparagine biosynthetic process Source: UniProtKB
  4. cellular amino acid biosynthetic process Source: Reactome
  5. cellular nitrogen compound metabolic process Source: Reactome
  6. cellular protein metabolic process Source: Reactome
  7. cellular response to glucose starvation Source: UniProtKB
  8. cellular response to hormone stimulus Source: Ensembl
  9. endoplasmic reticulum unfolded protein response Source: Reactome
  10. glutamine metabolic process Source: UniProtKB-KW
  11. liver development Source: Ensembl
  12. negative regulation of apoptotic process Source: UniProtKB
  13. positive regulation of mitotic cell cycle Source: UniProtKB
  14. response to amino acid Source: Ensembl
  15. response to follicle-stimulating hormone Source: Ensembl
  16. response to light stimulus Source: Ensembl
  17. response to mechanical stimulus Source: Ensembl
  18. response to methotrexate Source: Ensembl
  19. response to toxic substance Source: Ensembl
  20. small molecule metabolic process Source: Reactome
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: Chromosome 7

Organism-specific databases

HGNCiHGNC:753. ASNS.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Asparagine synthetase deficiency (ASNSD) [MIM:615574]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By 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

ArrayExpressiP08243.
BgeeiP08243.
CleanExiHS_ASNS.
GenevestigatoriP08243.

Organism-specific databases

HPAiHPA004924.
HPA029318.

Interactioni

Protein-protein interaction databases

BioGridi106932. 43 interactions.
IntActiP08243. 5 interactions.
MINTiMINT-1371662.
STRINGi9606.ENSP00000175506.

Structurei

3D structure databases

ProteinModelPortaliP08243.
SMRiP08243. Positions 253-481.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 191190Glutamine amidotransferase type-2
Add
BLAST
Domaini213 – 536324Asparagine synthetase
Add
BLAST

Region

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

Sequence similaritiesi

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0367.
HOVERGENiHBG003103.
InParanoidiP08243.
KOiK01953.
OMAiWMPRWIE.
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]
PIRSFiPIRSF001589. Asn_synthetase_glu-h. 1 hit.
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. Align

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

MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL    50
AVVDPLFGMQ PIRVKKYPYL WLCYNGEIYN HKKMQQHFEF EYQTKVDGEI 100
ILHLYDKGGI EQTICMLDGV FAFVLLDTAN KKVFLGRDTY GVRPLFKAMT 150
EDGFLAVCSE AKGLVTLKHS ATPFLKVEPF LPGHYEVLDL KPNGKVASVE 200
MVKYHHCRDV PLHALYDNVE KLFPGFEIET VKNNLRILFN NAVKKRLMTD 250
RRIGCLLSGG LDSSLVAATL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR 300
KVADHIGSEH YEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK 350
YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLRELYLF 400
DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPEMRIPK NGIEKHLLRE 450
TFEDSNLIPK EILWRPKEAF SDGITSVKNS WFKILQEYVE HQVDDAMMAN 500
AAQKFPFNTP KTKEGYYYRQ VFERHYPGRA DWLSHYWMPK WINATDPSAR 550
TLTHYKSAVK A 561
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

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.
VSP_045817Add
BLAST
Alternative sequencei1 – 2121Missing in isoform 2.
VSP_045818Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti333 – 34311TYDITTVRASV → LMTLQQFVLRI in AAA36781. 1 Publication
Add
BLAST
Sequence conflicti353 – 3608RKNTDSVV → GRTQIAWL in AAA36781. 1 Publication
Sequence conflicti426 – 4261S → F1 Publication
Sequence conflicti426 – 4261S → F1 Publication
Sequence conflicti462 – 4621I → V in BAG63553. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. [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]
GeneIDi440.
KEGGihsa:440.
UCSCiuc003uot.4. human. [P08243-1]

Polymorphism databases

DMDMi13432102.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS55131.1. [P08243-3 ]
CCDS55132.1. [P08243-2 ]
CCDS5652.1. [P08243-1 ]
PIRi A27062. AJHUN1.
RefSeqi NP_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 ]
UniGenei Hs.489207.

3D structure databases

ProteinModelPortali P08243.
SMRi P08243. Positions 253-481.
ModBasei Search...

Protein-protein interaction databases

BioGridi 106932. 43 interactions.
IntActi P08243. 5 interactions.
MINTi MINT-1371662.
STRINGi 9606.ENSP00000175506.

Chemistry

BindingDBi P08243.
ChEMBLi CHEMBL3120.
DrugBanki DB00171. Adenosine triphosphate.
DB00174. L-Asparagine.
DB00128. L-Aspartic Acid.
DB00142. L-Glutamic Acid.
DB00130. L-Glutamine.

Protein family/group databases

MEROPSi C44.974.

PTM databases

PhosphoSitei P08243.

Polymorphism databases

DMDMi 13432102.

Proteomic databases

MaxQBi P08243.
PaxDbi P08243.
PeptideAtlasi P08243.
PRIDEi P08243.

Protocols and materials databases

DNASUi 440.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000175506 ; 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 ]
GeneIDi 440.
KEGGi hsa:440.
UCSCi uc003uot.4. human. [P08243-1 ]

Organism-specific databases

CTDi 440.
GeneCardsi GC07M097481.
HGNCi HGNC:753. ASNS.
HPAi HPA004924.
HPA029318.
MIMi 108370. gene.
615574. phenotype.
neXtProti NX_P08243.
Orphaneti 391376. Congenital microcephaly-severe encephalopathy-progressive cerebral atrophy syndrome.
PharmGKBi PA25052.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0367.
HOVERGENi HBG003103.
InParanoidi P08243.
KOi K01953.
OMAi WMPRWIE.
OrthoDBi EOG75MVVS.
PhylomeDBi P08243.
TreeFami TF300603.

Enzyme and pathway databases

UniPathwayi UPA00134 ; UER00195 .
BRENDAi 6.3.5.4. 2681.
Reactomei REACT_18355. ATF4 activates genes.
REACT_238. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

GenomeRNAii 440.
NextBioi 1843.
PROi P08243.
SOURCEi Search...

Gene expression databases

ArrayExpressi P08243.
Bgeei P08243.
CleanExi HS_ASNS.
Genevestigatori P08243.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProi IPR006426. 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 ]
Pfami PF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view ]
PIRSFi PIRSF001589. Asn_synthetase_glu-h. 1 hit.
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR01536. asn_synth_AEB. 1 hit.
PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 164 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

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