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Searching in 'World-2DPAGE Repository [0014]' for entry matching: P09606




World-2DPAGE Repository (0014):  P09606

P09606


General information about the entry
View entry in simple text format
Entry nameGLNA_RAT
Primary accession numberP09606
integrated into World-2DPAGE Repository (0014) on October 13, 2008 (release 1)
2D Annotations were last modified onJune 1, 2011 (version 3)
General Annotations were last modified on November 25, 2011 (version 2)
Name and origin of the protein
DescriptionRecName: Full=Glutamine synthetase; Short=GS; EC=6.3.1.2; AltName: Full=Glutamate decarboxylase; EC=4.1.1.15; AltName: Full=Glutamate--ammonia ligase;.
Gene nameName=Glul
Synonyms=Glns
Annotated speciesRattus norvegicus (Rat) [TaxID: 10116]
TaxonomyEukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
References
[1]   2D-PAGE GEL CHARACTERIZATION
DOI=10.1002/pmic.200900680;
Maurya D.K., Sundaram C.S., Bhargava P.
''Proteome profile of whole cerebellum of the mature rat''
Proteomics 10(23):4311-4319 (2010)
2D PAGE maps for identified proteins
How to interpret a protein

RAT_CEREBELLUM_21D {Proteome of 21 days old rat cerebellum}
Rattus norvegicus (Rat)
Tissue: Cerebellum
RAT_CEREBELLUM_21D
  map experimental info 		 
RAT_CEREBELLUM_21D

MAP LOCATIONS:
pI=6.49; Mw=44000  [identification data]

IDENTIFICATION: SPOT 2937: SeqCov=42%. MascotPMF=149 [1].
MAPPING (identification):
SPOT 2937: Peptide mass fingerprinting [1]; Tandem mass spectrometry [1].

Copyright
Data from Dr. Purnima Bhargava, Centre for Cellular and Molecular Biology, India
Cross-references
PRIDE10017.
UniProtKB/Swiss-ProtP09606; GLNA_RAT.



2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 2011_11
Entry nameGLNA_RAT
Primary accession numberP09606
Secondary accession number(s) Q6P7Q9
Sequence was last modified on January 23, 2007 (version 3)
Annotations were last modified on November 16, 2011 (version 105)
Name and origin of the protein
DescriptionRecName: Full=Glutamine synthetase; Short=GS; EC=6.3.1.2; AltName: Full=Glutamate decarboxylase; EC=4.1.1.15; AltName: Full=Glutamate--ammonia ligase;
Gene nameName=Glul
Synonyms=Glns
Encoded onName=Glul; Synonyms=Glns
KeywordsAcetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Lyase; Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLX07921; CAA30754.1; -; mRNA
EMBLM29599; AAA65096.1; -; Genomic_DNA
EMBLM29595; AAA65096.1; JOINED; Genomic_DNA
EMBLM29596; AAA65096.1; JOINED; Genomic_DNA
EMBLM29597; AAA65096.1; JOINED; Genomic_DNA
EMBLM29598; AAA65096.1; JOINED; Genomic_DNA
EMBLM29579; AAA65095.1; -; mRNA
EMBLM91652; AAC42038.1; -; mRNA
EMBLBC061559; AAH61559.1; -; mRNA
EMBLBC072694; AAH72694.1; -; mRNA
IPIIPI00324020; -; .
PIRS01242; AJRTQ; .
RefSeqNP_058769.4; NM_017073.3; .
UniGeneRn.2204; -; .
ProteinModelPortalP09606; -; .
SMRP09606; 3-372; .
IntActP09606; 1; .
PhosphoSiteP09606; -; .
World-2DPAGE0004:P09606; -; .
PRIDEP09606; -; .
GeneID24957; -; .
KEGGrno:24957; -; .
CTD2752; -; .
RGD2710; Glul; .
eggNOGmaNOG04435; -; .
HOVERGENHBG005847; -; .
PhylomeDBP09606; -; .
NextBio604985; -; .
GenevestigatorP09606; -; .
GOGO:0043679; C:axon terminus; IDA:RGD; .
GOGO:0005792; C:microsome; IDA:RGD; .
GOGO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell; .
GOGO:0043204; C:perikaryon; IDA:RGD; .
GOGO:0043234; C:protein complex; IDA:RGD; .
GOGO:0005791; C:rough endoplasmic reticulum; IDA:RGD; .
GOGO:0005625; C:soluble fraction; IDA:RGD; .
GOGO:0019717; C:synaptosome; IDA:RGD; .
GOGO:0005524; F:ATP binding; IDA:RGD; .
GOGO:0045503; F:dynein light chain binding; IPI:RGD; .
GOGO:0016595; F:glutamate binding; IDA:RGD; .
GOGO:0004351; F:glutamate decarboxylase activity; IEA:EC; .
GOGO:0004356; F:glutamate-ammonia ligase activity; IDA:RGD; .
GOGO:0000287; F:magnesium ion binding; IDA:RGD; .
GOGO:0030145; F:manganese ion binding; IDA:RGD; .
GOGO:0019676; P:ammonia assimilation cycle; IDA:RGD; .
GOGO:0006542; P:glutamine biosynthetic process; IDA:RGD; .
GOGO:0042133; P:neurotransmitter metabolic process; TAS:RGD; .
GOGO:0050679; P:positive regulation of epithelial cell proliferation; IMP:RGD; .
GOGO:0032024; P:positive regulation of insulin secretion; IMP:RGD; .
GOGO:0051968; P:positive regulation of synaptic transmission; glutamatergic; IMP:RGD
GOGO:0051260; P:protein homooligomerization; IDA:RGD; .
InterProIPR008147; Gln_synt_beta; .
InterProIPR014746; Gln_synth/guanido_kin_cat_dom; .
InterProIPR008146; Gln_synth_cat_dom; .
Gene3DG3DSA:3.30.590.10; ATP-gua_Ptrans; 1; .
Gene3DG3DSA:3.10.20.70; G3DSA:3.10.20.70; 1; .
KOK01915; -; .
PfamPF00120; Gln-synt_C; 1; .
PfamPF03951; Gln-synt_N; 1; .
SUPFAMSSF54368; Gln_synt_beta; 1; .
PROSITEPS00180; GLNA_1; 1; .
PROSITEPS00181; GLNA_ATP; 1; .


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