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P15104

- GLNA_HUMAN

UniProt

P15104 - GLNA_HUMAN

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Protein

Glutamine synthetase

Gene

GLUL

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

Functioni

This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity). Essential for proliferation of fetal skin fibroblasts.By similarity1 Publication

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.
L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Protein has several cofactor binding sites:
  • biotinBy similarityNote: Biotin.By similarity
  • Mg2+By similarity, Mn2+By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-ammonia ligase activity Source: Reactome
  3. glutamate binding Source: Ensembl
  4. glutamate decarboxylase activity Source: UniProtKB-EC
  5. identical protein binding Source: IntAct
  6. magnesium ion binding Source: Ensembl
  7. manganese ion binding Source: Ensembl

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. cellular amino acid biosynthetic process Source: Reactome
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. cellular response to starvation Source: Ensembl
  5. glutamate catabolic process Source: BHF-UCL
  6. glutamine biosynthetic process Source: BHF-UCL
  7. neurotransmitter uptake Source: Reactome
  8. positive regulation of epithelial cell proliferation Source: Ensembl
  9. positive regulation of insulin secretion Source: Ensembl
  10. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
  11. protein homooligomerization Source: Ensembl
  12. response to glucose Source: Ensembl
  13. small molecule metabolic process Source: Reactome
  14. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Lyase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06066-MONOMER.
ReactomeiREACT_13639. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
REACT_238. Amino acid synthesis and interconversion (transamination).
SABIO-RKP15104.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase (EC:6.3.1.2)
Short name:
GS
Alternative name(s):
Glutamate decarboxylase (EC:4.1.1.15)
Glutamate--ammonia ligase
Gene namesi
Name:GLUL
Synonyms:GLNS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:4341. GLUL.

Subcellular locationi

Cytoplasm. Mitochondrion By similarity

GO - Cellular componenti

  1. axon terminus Source: Ensembl
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. glial cell projection Source: Ensembl
  6. mitochondrion Source: UniProtKB-KW
  7. nucleus Source: UniProt
  8. perikaryon Source: Ensembl
  9. protein complex Source: Ensembl
  10. rough endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Congenital systemic glutamine deficiency (CSGD) [MIM:610015]: Rare developmental disorder with severe brain malformation resulting in multi-organ failure and neonatal death. Glutamine is largely absent from affected patients serum, urine and cerebrospinal fluid.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti324 – 3241R → C in CSGD; reduced glutamine synthetase activity. 1 Publication
VAR_026560
Natural varianti341 – 3411R → C in CSGD; suggests reduced glutamine synthetase activity. 1 Publication
VAR_026561

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi610015. phenotype.
Orphaneti71278. Congenital brain dysgenesis due to glutamine synthetase deficiency.
PharmGKBiPA28743.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 373372Glutamine synthetasePRO_0000153139Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei104 – 1041PhosphotyrosineBy similarity

Post-translational modificationi

Ubiquitinated by ZNRF1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP15104.
PaxDbiP15104.
PeptideAtlasiP15104.
PRIDEiP15104.

2D gel databases

REPRODUCTION-2DPAGEIPI00010130.
UCD-2DPAGEP15104.

PTM databases

PhosphoSiteiP15104.

Expressioni

Developmental stagei

Expressed during early fetal stages.1 Publication

Inductioni

By glucocorticoids. Vitamin D and the Wnt signaling pathway inhibit its expression and activity.1 Publication

Gene expression databases

BgeeiP15104.
CleanExiHS_GLUL.
ExpressionAtlasiP15104. baseline and differential.
GenevestigatoriP15104.

Organism-specific databases

HPAiCAB008636.
HPA007316.
HPA007571.

Interactioni

Subunit structurei

Homooctamer and homotetramer. Interacts with PALMD (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-746653,EBI-746653

Protein-protein interaction databases

BioGridi109014. 27 interactions.
DIPiDIP-308N.
IntActiP15104. 19 interactions.
MINTiMINT-1183856.
STRINGi9606.ENSP00000307900.

Structurei

Secondary structure

1
373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84Combined sources
Helixi11 – 188Combined sources
Beta strandi26 – 338Combined sources
Beta strandi40 – 4910Combined sources
Helixi54 – 563Combined sources
Beta strandi60 – 634Combined sources
Turni64 – 685Combined sources
Beta strandi69 – 713Combined sources
Helixi72 – 743Combined sources
Beta strandi76 – 8611Combined sources
Turni88 – 903Combined sources
Beta strandi95 – 1028Combined sources
Beta strandi106 – 1083Combined sources
Helixi114 – 12310Combined sources
Helixi124 – 1274Combined sources
Beta strandi130 – 14011Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi158 – 1603Combined sources
Turni167 – 1693Combined sources
Helixi173 – 18614Combined sources
Beta strandi190 – 1956Combined sources
Beta strandi201 – 21010Combined sources
Helixi213 – 23220Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi251 – 2577Combined sources
Helixi259 – 2624Combined sources
Turni264 – 2663Combined sources
Helixi267 – 27812Combined sources
Helixi281 – 2877Combined sources
Turni290 – 2956Combined sources
Helixi296 – 2983Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi321 – 3255Combined sources
Helixi327 – 3326Combined sources
Beta strandi337 – 3393Combined sources
Helixi348 – 35912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OJWX-ray2.05A/B/C/D/E5-365[»]
2QC8X-ray2.60A/B/C/D/E/F/G/H/I/J5-365[»]
ProteinModelPortaliP15104.
SMRiP15104. Positions 10-365.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15104.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0174.
GeneTreeiENSGT00390000010047.
HOGENOMiHOG000061500.
HOVERGENiHBG005847.
InParanoidiP15104.
KOiK01915.
OMAiRIPRNVG.
OrthoDBiEOG7CZK5G.
PhylomeDBiP15104.
TreeFamiTF300491.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15104-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE
60 70 80 90 100
PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE
110 120 130 140 150
VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP
160 170 180 190 200
SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA
210 220 230 240 250
QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA
260 270 280 290 300
GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL
310 320 330 340 350
TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS
360 370
VTEALIRTCL LNETGDEPFQ YKN
Length:373
Mass (Da):42,064
Last modified:January 23, 2007 - v4
Checksum:i45390C100924FAF3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71S → Y in AAH31964. (PubMed:15489334)Curated
Sequence conflicti154 – 1541F → L in CAD97626. (PubMed:17974005)Curated
Sequence conflicti155 – 1551P → T in AAH31964. (PubMed:15489334)Curated
Sequence conflicti314 – 3141A → G in CAA68457. (PubMed:2888076)Curated
Sequence conflicti322 – 3232SI → RL in CAA42495. (PubMed:1681907)Curated
Sequence conflicti347 – 3471D → E in CAA42495. (PubMed:1681907)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti324 – 3241R → C in CSGD; reduced glutamine synthetase activity. 1 Publication
VAR_026560
Natural varianti341 – 3411R → C in CSGD; suggests reduced glutamine synthetase activity. 1 Publication
VAR_026561

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00387 mRNA. Translation: CAA68457.1.
X59834 mRNA. Translation: CAA42495.1.
S70290 mRNA. Translation: AAB30693.1.
AY486122 mRNA. Translation: AAS57904.1.
AY486123 Genomic DNA. Translation: AAS57905.1.
BX537384 mRNA. Translation: CAD97626.1.
AL139344 Genomic DNA. Translation: CAI19842.1.
BC010037 mRNA. Translation: AAH10037.1.
BC011700 mRNA. Translation: AAH11700.1.
BC011852 mRNA. Translation: AAH11852.1.
BC018992 mRNA. Translation: AAH18992.1.
BC031964 mRNA. Translation: AAH31964.1.
BC051726 mRNA. Translation: AAH51726.1.
CCDSiCCDS1344.1.
PIRiS18455. AJHUQ.
RefSeqiNP_001028216.1. NM_001033044.2.
NP_001028228.1. NM_001033056.2.
NP_002056.2. NM_002065.5.
XP_006711341.1. XM_006711278.1.
UniGeneiHs.518525.

Genome annotation databases

EnsembliENST00000311223; ENSP00000307900; ENSG00000135821.
ENST00000331872; ENSP00000356537; ENSG00000135821.
ENST00000339526; ENSP00000344958; ENSG00000135821.
ENST00000417584; ENSP00000398320; ENSG00000135821.
GeneIDi2752.
KEGGihsa:2752.
UCSCiuc001gpa.2. human.

Cross-referencesi

Web resourcesi

Wikipedia

Glutamine synthetase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00387 mRNA. Translation: CAA68457.1 .
X59834 mRNA. Translation: CAA42495.1 .
S70290 mRNA. Translation: AAB30693.1 .
AY486122 mRNA. Translation: AAS57904.1 .
AY486123 Genomic DNA. Translation: AAS57905.1 .
BX537384 mRNA. Translation: CAD97626.1 .
AL139344 Genomic DNA. Translation: CAI19842.1 .
BC010037 mRNA. Translation: AAH10037.1 .
BC011700 mRNA. Translation: AAH11700.1 .
BC011852 mRNA. Translation: AAH11852.1 .
BC018992 mRNA. Translation: AAH18992.1 .
BC031964 mRNA. Translation: AAH31964.1 .
BC051726 mRNA. Translation: AAH51726.1 .
CCDSi CCDS1344.1.
PIRi S18455. AJHUQ.
RefSeqi NP_001028216.1. NM_001033044.2.
NP_001028228.1. NM_001033056.2.
NP_002056.2. NM_002065.5.
XP_006711341.1. XM_006711278.1.
UniGenei Hs.518525.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OJW X-ray 2.05 A/B/C/D/E 5-365 [» ]
2QC8 X-ray 2.60 A/B/C/D/E/F/G/H/I/J 5-365 [» ]
ProteinModelPortali P15104.
SMRi P15104. Positions 10-365.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109014. 27 interactions.
DIPi DIP-308N.
IntActi P15104. 19 interactions.
MINTi MINT-1183856.
STRINGi 9606.ENSP00000307900.

Chemistry

BindingDBi P15104.
ChEMBLi CHEMBL4612.
DrugBanki DB01212. Ceftriaxone.
DB01119. Diazoxide.
DB00130. L-Glutamine.
DB00134. L-Methionine.
DB00082. Pegvisomant.

PTM databases

PhosphoSitei P15104.

2D gel databases

REPRODUCTION-2DPAGE IPI00010130.
UCD-2DPAGE P15104.

Proteomic databases

MaxQBi P15104.
PaxDbi P15104.
PeptideAtlasi P15104.
PRIDEi P15104.

Protocols and materials databases

DNASUi 2752.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311223 ; ENSP00000307900 ; ENSG00000135821 .
ENST00000331872 ; ENSP00000356537 ; ENSG00000135821 .
ENST00000339526 ; ENSP00000344958 ; ENSG00000135821 .
ENST00000417584 ; ENSP00000398320 ; ENSG00000135821 .
GeneIDi 2752.
KEGGi hsa:2752.
UCSCi uc001gpa.2. human.

Organism-specific databases

CTDi 2752.
GeneCardsi GC01M182350.
HGNCi HGNC:4341. GLUL.
HPAi CAB008636.
HPA007316.
HPA007571.
MIMi 138290. gene.
610015. phenotype.
neXtProti NX_P15104.
Orphaneti 71278. Congenital brain dysgenesis due to glutamine synthetase deficiency.
PharmGKBi PA28743.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0174.
GeneTreei ENSGT00390000010047.
HOGENOMi HOG000061500.
HOVERGENi HBG005847.
InParanoidi P15104.
KOi K01915.
OMAi RIPRNVG.
OrthoDBi EOG7CZK5G.
PhylomeDBi P15104.
TreeFami TF300491.

Enzyme and pathway databases

BioCyci MetaCyc:HS06066-MONOMER.
Reactomei REACT_13639. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
REACT_238. Amino acid synthesis and interconversion (transamination).
SABIO-RK P15104.

Miscellaneous databases

ChiTaRSi GLUL. human.
EvolutionaryTracei P15104.
GenomeRNAii 2752.
NextBioi 10840.
PROi P15104.
SOURCEi Search...

Gene expression databases

Bgeei P15104.
CleanExi HS_GLUL.
ExpressionAtlasi P15104. baseline and differential.
Genevestigatori P15104.

Family and domain databases

Gene3Di 3.30.590.10. 1 hit.
InterProi IPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view ]
Pfami PF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view ]
SUPFAMi SSF54368. SSF54368. 1 hit.
PROSITEi PS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "Overexpression of glutamine synthetase in human primary liver cancer."
    Christa L., Simon M.T., Flinois J.P., Gebhardt R., Brechot C., Lasserre C.
    Gastroenterology 106:1312-1320(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  4. Haberle J., Koch H.G.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Retina.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain, Colon, Eye, Muscle and Testis.
  8. "Glutamine synthetase isolated from human brain: octameric structure and homology of partial primary structure with human liver glutamine synthetase."
    Boksha I.S., Schonfeld H.J., Langen H., Muller F., Tereshkina E.B., Burbaeva G.S.H.
    Biochemistry (Mosc.) 67:1012-1020(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain.
  9. "Glutamine synthetase is essential for proliferation of fetal skin fibroblasts."
    Vermeulen T., Goerg B., Vogl T., Wolf M., Varga G., Toutain A., Paul R., Schliess F., Haeussinger D., Haeberle J.
    Arch. Biochem. Biophys. 478:96-102(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  10. "Wnt and steroid pathways control glutamate signalling by regulating glutamine synthetase activity in osteoblastic cells."
    Olkku A., Mahonen A.
    Bone 43:483-493(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: VARIANTS CSGD CYS-324 AND CYS-341, CHARACTERIZATION OF VARIANTS CSGD CYS-324 AND CYS-341.

Entry informationi

Entry nameiGLNA_HUMAN
AccessioniPrimary (citable) accession number: P15104
Secondary accession number(s): Q499Y9
, Q5T9Z1, Q7Z3W4, Q8IZ17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: November 26, 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3