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Protein

Cellulose synthase A catalytic subunit 1 [UDP-forming]

Gene

CESA1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the primary cell wall formation. Required during embryogenesis for cell elongation, orientation of cell expansion and complex cell wall formations, such as interdigitated pattern of epidermal pavement cells, stomatal guard cells and trichomes. Plays a role in lateral roots formation, but seems not necessary for the development of tip-growing cells such as root hairs. The presence of each protein CESA1 and CESA6 is critical for cell expansion after germination.10 Publications

Catalytic activityi

UDP-glucose + (1,4-beta-D-glucosyl)(n) = UDP + (1,4-beta-D-glucosyl)(n+1).

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Pathwayi: plant cellulose biosynthesis

This protein is involved in the pathway plant cellulose biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway plant cellulose biosynthesis and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi39 – 391Zinc 1By similarity
Metal bindingi42 – 421Zinc 1By similarity
Metal bindingi58 – 581Zinc 2By similarity
Metal bindingi61 – 611Zinc 2By similarity
Metal bindingi66 – 661Zinc 1By similarity
Metal bindingi69 – 691Zinc 1By similarity
Metal bindingi81 – 811Zinc 2By similarity
Metal bindingi84 – 841Zinc 2By similarity
Active sitei395 – 3951Sequence analysis
Binding sitei561 – 5611SubstrateSequence analysis
Binding sitei563 – 5631SubstrateSequence analysis
Active sitei780 – 7801Sequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri39 – 8547RING-type; degenerateAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cellulose biosynthetic process Source: TAIR
  • cell wall organization Source: UniProtKB-KW
  • hyperosmotic salinity response Source: TAIR
  • plant-type primary cell wall biogenesis Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation, Cellulose biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-2361.
UniPathwayiUPA00695.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.
TCDBi4.D.3.1.4. the glycan glucosyl transferase (opgh) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellulose synthase A catalytic subunit 1 [UDP-forming] (EC:2.4.1.12)
Short name:
AtCesA1
Alternative name(s):
Protein RADIALLY SWOLLEN 1
Short name:
AtRSW1
Gene namesi
Name:CESA1
Synonyms:RSW1
Ordered Locus Names:At4g32410
ORF Names:F8B4.110
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G32410.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 270270CytoplasmicSequence analysisAdd
BLAST
Transmembranei271 – 29121HelicalSequence analysisAdd
BLAST
Topological domaini292 – 2998ExtracellularSequence analysis
Transmembranei300 – 32021HelicalSequence analysisAdd
BLAST
Topological domaini321 – 856536CytoplasmicSequence analysisAdd
BLAST
Transmembranei857 – 87721HelicalSequence analysisAdd
BLAST
Topological domaini878 – 88912ExtracellularSequence analysisAdd
BLAST
Transmembranei890 – 91021HelicalSequence analysisAdd
BLAST
Topological domaini911 – 92515CytoplasmicSequence analysisAdd
BLAST
Transmembranei926 – 94621HelicalSequence analysisAdd
BLAST
Topological domaini947 – 97630ExtracellularSequence analysisAdd
BLAST
Transmembranei977 – 99721HelicalSequence analysisAdd
BLAST
Topological domaini998 – 100811CytoplasmicSequence analysisAdd
BLAST
Transmembranei1009 – 102921HelicalSequence analysisAdd
BLAST
Topological domaini1030 – 10389ExtracellularSequence analysis
Transmembranei1039 – 105921HelicalSequence analysisAdd
BLAST
Topological domaini1060 – 108122CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endosome Source: TAIR
  • Golgi apparatus Source: TAIR
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: TAIR
  • trans-Golgi network Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi549 – 5491A → V in rsw1-1; temperature-sensitive disassembly of cellulose synthase complexes ('rosettes') and altered cellulose crystallinity, accumulation of noncrystalline beta-1,4-glucan, normal below 21 degrees Celsius but not above 30 degrees Celsius, accumulation of starch in roots, constitutive and high expression of vegetative storage proteins (VSP) and widespread morphological abnormalities. 5 Publications
Mutagenesisi631 – 6311G → S in rsw1-2; abnormal embryos, very short and stout plants, reduced crystalline cellulose deposition in cell walls, and restricted intercellular spaces due to increased cell junction thickness. 1 Publication
Mutagenesisi779 – 7791E → K in rsw1-45; abnormal embryos, short and stout plants, and reduced crystalline cellulose deposition in cell walls. 1 Publication
Mutagenesisi780 – 7801D → N in rsw1-20; abnormal embryos, short and stout plants, reduced crystalline cellulose deposition in cell walls, and restricted intercellular spaces due to increased cell junction thickness. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10811081Cellulose synthase A catalytic subunit 1 [UDP-forming]PRO_0000166367Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Glycosylationi953 – 9531N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

PaxDbiO48946.
PRIDEiO48946.

PTM databases

iPTMnetiO48946.
SwissPalmiO48946.

Expressioni

Tissue specificityi

Expressed in germinating seeds, seedlings, roots, stems, shoots leaves and flowers, but not in mature flowers.4 Publications

Developmental stagei

Expressed throughout the embryo during all steps of embryogenesis, and decrease toward the bent-cotyledon stage. Higher levels in tissues undergoing primary cell wall formation, and drop of expression when secondary wall synthesis takes place. High levels in developing seedlings and elongating stems, with a decrease at later growth stages.2 Publications

Gene expression databases

ExpressionAtlasiO48946. baseline and differential.
GenevisibleiO48946. AT.

Interactioni

Subunit structurei

Interacts with CESA3 and CESA6. Assembly with CESA3 and CESA6 is required for functional complex in primary cell wall cellulose synthesis.2 Publications

Protein-protein interaction databases

BioGridi14662. 9 interactions.
DIPiDIP-59354N.
STRINGi3702.AT4G32410.1.

Structurei

3D structure databases

ProteinModelPortaliO48946.
SMRiO48946. Positions 27-97.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili449 – 47628Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri39 – 8547RING-type; degenerateAdd
BLAST

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IIG9. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiO48946.
KOiK10999.
OMAiNEFNYTQ.
PhylomeDBiO48946.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR005150. Cellulose_synth.
IPR027934. CES_Znf_RING.
IPR029044. Nucleotide-diphossugar_trans.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF03552. Cellulose_synt. 1 hit.
PF14569. zf-UDP. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 2 hits.

Sequencei

Sequence statusi: Complete.

O48946-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEASAGLVAG SYRRNELVRI RHESDGGTKP LKNMNGQICQ ICGDDVGLAE
60 70 80 90 100
TGDVFVACNE CAFPVCRPCY EYERKDGTQC CPQCKTRFRR HRGSPRVEGD
110 120 130 140 150
EDEDDVDDIE NEFNYAQGAN KARHQRHGEE FSSSSRHESQ PIPLLTHGHT
160 170 180 190 200
VSGEIRTPDT QSVRTTSGPL GPSDRNAISS PYIDPRQPVP VRIVDPSKDL
210 220 230 240 250
NSYGLGNVDW KERVEGWKLK QEKNMLQMTG KYHEGKGGEI EGTGSNGEEL
260 270 280 290 300
QMADDTRLPM SRVVPIPSSR LTPYRVVIIL RLIILCFFLQ YRTTHPVKNA
310 320 330 340 350
YPLWLTSVIC EIWFAFSWLL DQFPKWYPIN RETYLDRLAI RYDRDGEPSQ
360 370 380 390 400
LVPVDVFVST VDPLKEPPLV TANTVLSILS VDYPVDKVAC YVSDDGSAML
410 420 430 440 450
TFESLSETAE FAKKWVPFCK KFNIEPRAPE FYFAQKIDYL KDKIQPSFVK
460 470 480 490 500
ERRAMKREYE EFKVRINALV AKAQKIPEEG WTMQDGTPWP GNNTRDHPGM
510 520 530 540 550
IQVFLGHSGG LDTDGNELPR LIYVSREKRP GFQHHKKAGA MNALIRVSAV
560 570 580 590 600
LTNGAYLLNV DCDHYFNNSK AIKEAMCFMM DPAIGKKCCY VQFPQRFDGI
610 620 630 640 650
DLHDRYANRN IVFFDINMKG LDGIQGPVYV GTGCCFNRQA LYGYDPVLTE
660 670 680 690 700
EDLEPNIIVK SCCGSRKKGK SSKKYNYEKR RGINRSDSNA PLFNMEDIDE
710 720 730 740 750
GFEGYDDERS ILMSQRSVEK RFGQSPVFIA ATFMEQGGIP PTTNPATLLK
760 770 780 790 800
EAIHVISCGY EDKTEWGKEI GWIYGSVTED ILTGFKMHAR GWISIYCNPP
810 820 830 840 850
RPAFKGSAPI NLSDRLNQVL RWALGSIEIL LSRHCPIWYG YHGRLRLLER
860 870 880 890 900
IAYINTIVYP ITSIPLIAYC ILPAFCLITD RFIIPEISNY ASIWFILLFI
910 920 930 940 950
SIAVTGILEL RWSGVSIEDW WRNEQFWVIG GTSAHLFAVF QGLLKVLAGI
960 970 980 990 1000
DTNFTVTSKA TDEDGDFAEL YIFKWTALLI PPTTVLLVNL IGIVAGVSYA
1010 1020 1030 1040 1050
VNSGYQSWGP LFGKLFFALW VIAHLYPFLK GLLGRQNRTP TIVIVWSVLL
1060 1070 1080
ASIFSLLWVR INPFVDANPN ANNFNGKGGV F
Length:1,081
Mass (Da):122,237
Last modified:June 1, 1998 - v1
Checksum:iBDEB5D9DEE334D59
GO

Sequence cautioni

The sequence BAD95078.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027172 Genomic DNA. Translation: AAC39334.1.
AL034567 Genomic DNA. Translation: CAA22568.1.
AL161581 Genomic DNA. Translation: CAB79958.1.
CP002687 Genomic DNA. Translation: AEE86053.1.
BT008654 mRNA. Translation: AAP40467.1.
AK222115 mRNA. Translation: BAD95078.1. Different initiation.
AK226243 mRNA. Translation: BAE98406.1.
PIRiT05351.
RefSeqiNP_194967.1. NM_119393.2.
UniGeneiAt.21246.

Genome annotation databases

EnsemblPlantsiAT4G32410.1; AT4G32410.1; AT4G32410.
GeneIDi829376.
GrameneiAT4G32410.1; AT4G32410.1; AT4G32410.
KEGGiath:AT4G32410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027172 Genomic DNA. Translation: AAC39334.1.
AL034567 Genomic DNA. Translation: CAA22568.1.
AL161581 Genomic DNA. Translation: CAB79958.1.
CP002687 Genomic DNA. Translation: AEE86053.1.
BT008654 mRNA. Translation: AAP40467.1.
AK222115 mRNA. Translation: BAD95078.1. Different initiation.
AK226243 mRNA. Translation: BAE98406.1.
PIRiT05351.
RefSeqiNP_194967.1. NM_119393.2.
UniGeneiAt.21246.

3D structure databases

ProteinModelPortaliO48946.
SMRiO48946. Positions 27-97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14662. 9 interactions.
DIPiDIP-59354N.
STRINGi3702.AT4G32410.1.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.
TCDBi4.D.3.1.4. the glycan glucosyl transferase (opgh) family.

PTM databases

iPTMnetiO48946.
SwissPalmiO48946.

Proteomic databases

PaxDbiO48946.
PRIDEiO48946.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G32410.1; AT4G32410.1; AT4G32410.
GeneIDi829376.
GrameneiAT4G32410.1; AT4G32410.1; AT4G32410.
KEGGiath:AT4G32410.

Organism-specific databases

TAIRiAT4G32410.

Phylogenomic databases

eggNOGiENOG410IIG9. Eukaryota.
COG1215. LUCA.
HOGENOMiHOG000241942.
InParanoidiO48946.
KOiK10999.
OMAiNEFNYTQ.
PhylomeDBiO48946.

Enzyme and pathway databases

UniPathwayiUPA00695.
BioCyciMetaCyc:MONOMER-2361.

Miscellaneous databases

PROiO48946.

Gene expression databases

ExpressionAtlasiO48946. baseline and differential.
GenevisibleiO48946. AT.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR005150. Cellulose_synth.
IPR027934. CES_Znf_RING.
IPR029044. Nucleotide-diphossugar_trans.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF03552. Cellulose_synt. 1 hit.
PF14569. zf-UDP. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ALA-549.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. Cited for: GENE FAMILY, NOMENCLATURE.
  7. "Fractionation of carbohydrates in Arabidopsis root cell walls shows that three radial swelling loci are specifically involved in cellulose production."
    Peng L., Hocart C.H., Redmond J.W., Williamson R.E.
    Planta 211:406-414(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ALA-549.
  8. "PROCUSTE1 encodes a cellulose synthase required for normal cell elongation specifically in roots and dark-grown hypocotyls of Arabidopsis."
    Fagard M., Desnos T., Desprez T., Goubet F., Refregier G., Mouille G., McCann M., Rayon C., Vernhettes S., Hoefte H.
    Plant Cell 12:2409-2423(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  9. "Modifications of cellulose synthase confer resistance to isoxaben and thiazolidinone herbicides in Arabidopsis Ixr1 mutants."
    Scheible W.-R., Eshed R., Richmond T., Delmer D., Somerville C.
    Proc. Natl. Acad. Sci. U.S.A. 98:10079-10084(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  10. "Morphology of rsw1, a cellulose-deficient mutant of Arabidopsis thaliana."
    Williamson R.E., Burn J.E., Birch R., Baskin T.I., Arioli T., Betzner A.S., Cork A.
    Protoplasma 215:116-127(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ALA-549.
  11. "Wall architecture in the cellulose-deficient rsw1 mutant of Arabidopsis thaliana: microfibrils but not microtubules lose their transverse alignment before microfibrils become unrecognizable in the mitotic and elongation zones of roots."
    Sugimoto K., Williamson R.E., Wasteneys G.O.
    Protoplasma 215:172-183(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ALA-549.
  12. "Alpha-glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis."
    Gillmor C.S., Poindexter P., Lorieau J., Palcic M.M., Somerville C.
    J. Cell Biol. 156:1003-1013(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-631.
  13. "The Arabidopsis mutant cev1 links cell wall signaling to jasmonate and ethylene responses."
    Ellis C., Karafyllidis I., Wasternack C., Turner J.G.
    Plant Cell 14:1557-1566(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ALA-549.
  14. "Functional analysis of the cellulose synthase genes CesA1, CesA2, and CesA3 in Arabidopsis."
    Burn J.E., Hocart C.H., Birch R.J., Cork A.C., Williamson R.E.
    Plant Physiol. 129:797-807(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  15. "Genetic complexity of cellulose synthase A gene function in Arabidopsis embryogenesis."
    Beeckman T., Przemeck G.K.H., Stamatiou G., Lau R., Terryn N., De Rycke R., Inze D., Berleth T.
    Plant Physiol. 130:1883-1893(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLU-779 AND ASP-780.
  16. "Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database."
    Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
    Plant Cell 16:2394-2405(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Genetic evidence for three unique components in primary cell-wall cellulose synthase complexes in Arabidopsis."
    Persson S., Paredez A., Carroll A., Palsdottir H., Doblin M., Poindexter P., Khitrov N., Auer M., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 104:15566-15571(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  18. "Organization of cellulose synthase complexes involved in primary cell wall synthesis in Arabidopsis thaliana."
    Desprez T., Juraniec M., Crowell E.F., Jouy H., Pochylova Z., Parcy F., Hoefte H., Gonneau M., Vernhettes S.
    Proc. Natl. Acad. Sci. U.S.A. 104:15572-15577(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CESA3 AND CESA6.
  19. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCESA1_ARATH
AccessioniPrimary (citable) accession number: O48946
Secondary accession number(s): Q0WWU2, Q56WC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.