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Q12680

- GLT1_YEAST

UniProt

Q12680 - GLT1_YEAST

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Protein

Glutamate synthase [NADH]

Gene

GLT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate.2 Publications

Catalytic activityi

2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by homocysteine sulfonamide.1 Publication

Kineticsi

  1. KM=280 µM for L-glutamine2 Publications
  2. KM=40 µM for 2-oxoglutarate2 Publications
  3. KM=7 µM for NADH2 Publications

pH dependencei

Optimum pH is 7-7.5. Active from pH 6 to 9.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541For GATase activityBy similarity
Metal bindingi1185 – 11851Iron-sulfur (3Fe-4S)By similarity
Metal bindingi1191 – 11911Iron-sulfur (3Fe-4S)By similarity
Metal bindingi1196 – 11961Iron-sulfur (3Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1132 – 118958FMNBy similarityAdd
BLAST
Nucleotide bindingi1928 – 194215NADSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. 3 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. flavin adenine dinucleotide binding Source: InterPro
  3. FMN binding Source: InterPro
  4. glutamate synthase (NADH) activity Source: SGD
  5. iron ion binding Source: InterPro

GO - Biological processi

  1. ammonia assimilation cycle Source: SGD
  2. glutamate biosynthetic process Source: SGD
  3. L-glutamate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Glutamate biosynthesis

Keywords - Ligandi

3Fe-4S, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13146.
YEAST:YDL171C-MONOMER.
SABIO-RKQ12680.
UniPathwayiUPA00045.
UPA00634; UER00690.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate synthase [NADH] (EC:1.4.1.14)
Alternative name(s):
NADH-GOGAT
Gene namesi
Name:GLT1
Ordered Locus Names:YDL171C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL171c.
SGDiS000002330. GLT1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 53531 PublicationPRO_0000011612Add
BLAST
Chaini54 – 21452092Glutamate synthase [NADH]PRO_0000011613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2070 – 20701Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein, Zymogen

Proteomic databases

MaxQBiQ12680.
PaxDbiQ12680.
PeptideAtlasiQ12680.
PRIDEiQ12680.

Expressioni

Gene expression databases

GenevestigatoriQ12680.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi31894. 56 interactions.
DIPiDIP-6490N.
IntActiQ12680. 34 interactions.
MINTiMINT-647261.

Structurei

3D structure databases

ProteinModelPortaliQ12680.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 455402Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1551 – 160050Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the glutamate synthase family.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0493.
GeneTreeiENSGT00500000044896.
HOGENOMiHOG000031559.
InParanoidiQ12680.
KOiK00264.
OMAiMMPADLP.
OrthoDBiEOG7TN012.

Family and domain databases

Gene3Di2.160.20.60. 1 hit.
3.20.20.70. 2 hits.
3.40.50.720. 2 hits.
3.60.20.10. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR028261. DPD_II.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR002489. Glu_synth_asu_C.
IPR006982. Glu_synth_centr_N.
IPR012220. Glu_synth_euk.
IPR002932. Glu_synthdom.
IPR006005. Glut_synth_ssu1.
IPR009051. Helical_ferredxn.
IPR016040. NAD(P)-bd_dom.
IPR029055. Ntn_hydrolases_N.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF14691. Fer4_20. 1 hit.
PF00310. GATase_2. 1 hit.
PF04898. Glu_syn_central. 1 hit.
PF01645. Glu_synthase. 1 hit.
PF01493. GXGXG. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000187. GOGAT. 1 hit.
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF56235. SSF56235. 1 hit.
SSF69336. SSF69336. 1 hit.
TIGRFAMsiTIGR01317. GOGAT_sm_gam. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q12680-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPVLKSDNFD PLEEAYEGGT IQNYNDEHHL HKSWANVIPD KRGLYDPDYE
60 70 80 90 100
HDACGVGFVA NKHGEQSHKI VTDARYLLVN MTHRGAVSSD GNGDGAGILL
110 120 130 140 150
GIPHEFMKRE FKLDLDLDIP EMGKYAVGNV FFKKNEKNNK KNLIKCQKIF
160 170 180 190 200
EDLAASFNLS VLGWRNVPVD STILGDVALS REPTILQPLL VPLYDEKQPE
210 220 230 240 250
FNETKFRTQL YLLRKEASLQ IGLENWFYVC SLNNTTIVYK GQLTPAQVYN
260 270 280 290 300
YYPDLTNAHF KSHMALVHSR FSTNTFPSWD RAQPLRWLAH NGEINTLRGN
310 320 330 340 350
KNWMRSREGV MNSATFKDEL DKLYPIIEEG GSDSAALDNV LELLTINGTL
360 370 380 390 400
SLPEAVMMMV PEAYHKDMDS DLKAWYDWAA CLMEPWDGPA LLTFTDGRYC
410 420 430 440 450
GAILDRNGLR PCRYYITSDD RVICASEVGV IPIENSLVVQ KGKLKPGDLF
460 470 480 490 500
LVDTQLGEMV DTKKLKSQIS KRQDFKSWLS KVIKLDDLLS KTANLVPKEF
510 520 530 540 550
ISQDSLSLKV QSDPRLLANG YTFEQVTFLL TPMALTGKEA LGSMGNDAPL
560 570 580 590 600
ACLNENPVLL YDYFRQLFAQ VTNPPIDPIR EANVMSLECY VGPQGNLLEM
610 620 630 640 650
HSSQCDRLLL KSPILHWNEF QALKNIEAAY PSWSVAEIDI TFDKSEGLLG
660 670 680 690 700
YTDTIDKITK LASEAIDDGK KILIITDRKM GANRVSISSL IAISCIHHHL
710 720 730 740 750
IRNKQRSQVA LILETGEARE IHHFCVLLGY GCDGVYPYLA METLVRMNRE
760 770 780 790 800
GLLRNVNNDN DTLEEGQILE NYKHAIDAGI LKVMSKMGIS TLASYKGAQI
810 820 830 840 850
FEALGLDNSI VDLCFTGTSS RIRGVTFEYL AQDAFSLHER GYPSRQTISK
860 870 880 890 900
SVNLPESGEY HFRDGGYKHV NEPTAIASLQ DTVRNKNDVS WQLYVKKEME
910 920 930 940 950
AIRDCTLRGL LELDFENSVS IPLEQVEPWT EIARRFASGA MSYGSISMEA
960 970 980 990 1000
HSTLAIAMNR LGAKSNCGEG GEDAERSAVQ ENGDTMRSAI KQVASARFGV
1010 1020 1030 1040 1050
TSYYLSDADE IQIKIAQGAK PGEGGELPAH KVSKDIAKTR HSTPNVGLIS
1060 1070 1080 1090 1100
PPPHHDIYSI EDLKQLIYDL KCANPRAGIS VKLVSEVGVG IVASGVAKAK
1110 1120 1130 1140 1150
ADHILVSGHD GGTGAARWTS VKYAGLPWEL GLAETHQTLV LNDLRRNVVV
1160 1170 1180 1190 1200
QTDGQLRTGF DIAVAVLLGA ESFTLATVPL IAMGCVMLRR CHLNSCAVGI
1210 1220 1230 1240 1250
ATQDPYLRSK FKGQPEHVIN FFYYLIQDLR QIMAKLGFRT IDEMVGHSEK
1260 1270 1280 1290 1300
LKKRDDVNAK AINIDLSPIL TPAHVIRPGV PTKFTKKQDH KLHTRLDNKL
1310 1320 1330 1340 1350
IDEAEVTLDR GLPVNIDASI INTDRALGST LSYRVSKKFG EDGLPKDTVV
1360 1370 1380 1390 1400
VNIEGSAGQS FGAFLASGIT FILNGDANDY VGKGLSGGII VIKPPKDSKF
1410 1420 1430 1440 1450
KSDENVIVGN TCFYGATSGT AFISGSAGER FGVRNSGATI VVERIKGNNA
1460 1470 1480 1490 1500
FEYMTGGRAI VLSQMESLNA FSGATGGIAY CLTSDYDDFV GKINKDTVEL
1510 1520 1530 1540 1550
ESLCDPVEIA FVKNLIQEHW NYTQSDLAAR ILGNFNHYLK DFVKVIPTDY
1560 1570 1580 1590 1600
KKVLLKEKAE AAKAKAKATS EYLKKFRSNQ EVDDEVNTLL IANQKAKEQE
1610 1620 1630 1640 1650
KKKSITISNK ATLKEPKVVD LEDAVPDSKQ LEKNSERIEK TRGFMIHKRR
1660 1670 1680 1690 1700
HETHRDPRTR VNDWKEFTNP ITKKDAKYQT ARCMDCGTPF CLSDTGCPLS
1710 1720 1730 1740 1750
NIIPKFNELL FKNQWKLALD KLLETNNFPE FTGRVCPAPC EGACTLGIIE
1760 1770 1780 1790 1800
DPVGIKSVER IIIDNAFKEG WIKPCPPSTR TGFTVGVIGS GPAGLACADM
1810 1820 1830 1840 1850
LNRAGHTVTV YERSDRCGGL LMYGIPNMKL DKAIVQRRID LLSAEGIDFV
1860 1870 1880 1890 1900
TNTEIGKTIS MDELKNKHNA VVYAIGSTIP RDLPIKGREL KNIDFAMQLL
1910 1920 1930 1940 1950
ESNTKALLNK DLEIIREKIQ GKKVIVVGGG DTGNDCLGTS VRHGAASVLN
1960 1970 1980 1990 2000
FELLPEPPVE RAKDNPWPQW PRVMRVDYGH AEVKEHYGRD PREYCILSKE
2010 2020 2030 2040 2050
FIGNDEGEVT AIRTVRVEWK KSQSGVWQMV EIPNSEEIFE ADIILLSMGF
2060 2070 2080 2090 2100
VGPELINGND NEVKKTRRGT IATLDDSSYS IDGGKTFACG DCRRGQSLIV
2110 2120 2130 2140
WAIQEGRKCA ASVDKFLMDG TTYLPSNGGI VQRDYKLLKE LASQV
Length:2,145
Mass (Da):238,102
Last modified:September 5, 2006 - v2
Checksum:i78184877D2167A0D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1738NVPVDSTI → TSRRFYY in CAA61505. (PubMed:8923741)Curated
Sequence conflicti450 – 4523FLV → IPS in CAA61505. (PubMed:8923741)Curated
Sequence conflicti1753 – 17531V → L in CAA61505. (PubMed:8923741)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89221 Genomic DNA. Translation: CAA61505.1.
Z67750 Genomic DNA. Translation: CAA91574.1.
Z74219 Genomic DNA. Translation: CAA98745.1.
BK006938 Genomic DNA. Translation: DAA11690.1.
PIRiS61041.
RefSeqiNP_010110.1. NM_001180231.1.

Genome annotation databases

EnsemblFungiiYDL171C; YDL171C; YDL171C.
GeneIDi851383.
KEGGisce:YDL171C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89221 Genomic DNA. Translation: CAA61505.1 .
Z67750 Genomic DNA. Translation: CAA91574.1 .
Z74219 Genomic DNA. Translation: CAA98745.1 .
BK006938 Genomic DNA. Translation: DAA11690.1 .
PIRi S61041.
RefSeqi NP_010110.1. NM_001180231.1.

3D structure databases

ProteinModelPortali Q12680.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31894. 56 interactions.
DIPi DIP-6490N.
IntActi Q12680. 34 interactions.
MINTi MINT-647261.

Proteomic databases

MaxQBi Q12680.
PaxDbi Q12680.
PeptideAtlasi Q12680.
PRIDEi Q12680.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL171C ; YDL171C ; YDL171C .
GeneIDi 851383.
KEGGi sce:YDL171C.

Organism-specific databases

CYGDi YDL171c.
SGDi S000002330. GLT1.

Phylogenomic databases

eggNOGi COG0493.
GeneTreei ENSGT00500000044896.
HOGENOMi HOG000031559.
InParanoidi Q12680.
KOi K00264.
OMAi MMPADLP.
OrthoDBi EOG7TN012.

Enzyme and pathway databases

UniPathwayi UPA00045 .
UPA00634 ; UER00690 .
BioCyci MetaCyc:MONOMER-13146.
YEAST:YDL171C-MONOMER.
SABIO-RK Q12680.

Miscellaneous databases

NextBioi 968525.
PROi Q12680.

Gene expression databases

Genevestigatori Q12680.

Family and domain databases

Gene3Di 2.160.20.60. 1 hit.
3.20.20.70. 2 hits.
3.40.50.720. 2 hits.
3.60.20.10. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR028261. DPD_II.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR002489. Glu_synth_asu_C.
IPR006982. Glu_synth_centr_N.
IPR012220. Glu_synth_euk.
IPR002932. Glu_synthdom.
IPR006005. Glut_synth_ssu1.
IPR009051. Helical_ferredxn.
IPR016040. NAD(P)-bd_dom.
IPR029055. Ntn_hydrolases_N.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view ]
Pfami PF14691. Fer4_20. 1 hit.
PF00310. GATase_2. 1 hit.
PF04898. Glu_syn_central. 1 hit.
PF01645. Glu_synthase. 1 hit.
PF01493. GXGXG. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000187. GOGAT. 1 hit.
SUPFAMi SSF46548. SSF46548. 1 hit.
SSF56235. SSF56235. 1 hit.
SSF69336. SSF69336. 1 hit.
TIGRFAMsi TIGR01317. GOGAT_sm_gam. 1 hit.
PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the GLT1 gene from Saccharomyces cerevisiae reveals the domain structure of yeast glutamate synthase."
    Filetici P., Martegani M.P., Valenzuela L., Gonzalez A., Ballario P.
    Yeast 12:1359-1366(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96744 / CN36.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Saccharomyces cerevisiae has a single glutamate synthase gene coding for a plant-like high-molecular-weight polypeptide."
    Cogoni C., Valenzuela L., Gonzalez-Halphen D., Olivera H., Macino G., Ballario P., Gonzalez A.
    J. Bacteriol. 177:792-798(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 54-61, SUBUNIT.
    Strain: ATCC 96744 / CN36.
  5. "Glutamate synthase: properties of the reduced nicotinamide adenine dinucleotide-dependent enzyme from Saccharomyces cerevisiae."
    Roon R.J., Even H.L., Larimore F.
    J. Bacteriol. 118:89-95(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
  6. "Inhibition of homocysteine sulfonamide of glutamate synthase purified from Saccharomyces cerevisiae."
    Masters D.S. Jr., Meister A.
    J. Biol. Chem. 257:8711-8715(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2070, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGLT1_YEAST
AccessioniPrimary (citable) accession number: Q12680
Secondary accession number(s): D6VRI0, Q12290
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 5, 2006
Last modified: November 26, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 18900 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3