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P49040

- SUSY1_ARATH

UniProt

P49040 - SUSY1_ARATH

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Protein

Sucrose synthase 1

Gene

SUS1

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

Functioni

Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways.1 Publication

Catalytic activityi

NDP-glucose + D-fructose = NDP + sucrose.

Kineticsi

  1. KM=4.37 mM for D-fructose (synthetic reaction) at pH 9.42 Publications
  2. KM=0.04 mM for UDP-glucose (synthetic reaction) at pH 9.42 Publications
  3. KM=31.58 mM for sucrose (degradative reaction) at pH 62 Publications
  4. KM=53 mM for sucrose (degradative reaction) at pH 72 Publications
  5. KM=0.08 mM for UDP (degradative reaction) at pH 62 Publications
  6. KM=0.39 mM for UDP (degradative reaction) at pH 72 Publications
  7. KM=0.17 mM for ADP (degradative reaction) at pH 72 Publications

Vmax=11.14 µmol/min/mg enzyme for synthetic reaction at pH 9.42 Publications

Vmax=4.68 µmol/min/mg enzyme for degradative reaction at pH 62 Publications

Vmax=585 µmol/min/mg enzyme for degradative reaction at pH 72 Publications

pH dependencei

Optimum pH is 6.0-7.0 for degradative reaction and 7.0 (PubMed:22184213) or 9.0-9.5 (PubMed:17257168) for synthetic reaction.2 Publications

GO - Molecular functioni

  1. sucrose synthase activity Source: UniProtKB

GO - Biological processi

  1. biosynthetic process Source: InterPro
  2. response to cadmium ion Source: TAIR
  3. response to cold Source: UniProtKB
  4. response to flooding Source: TAIR
  5. response to glucose Source: UniProtKB
  6. response to hypoxia Source: UniProtKB
  7. response to mannitol Source: UniProtKB
  8. response to osmotic stress Source: TAIR
  9. response to sorbitol Source: UniProtKB
  10. response to sucrose Source: UniProtKB
  11. response to water deprivation Source: UniProtKB
  12. sucrose metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciARA:AT5G20830-MONOMER.
ARA:GQT-1272-MONOMER.
MetaCyc:AT5G20830-MONOMER.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
Sucrose synthase 1 (EC:2.4.1.13)
Short name:
AtSUS1
Alternative name(s):
Sucrose-UDP glucosyltransferase 1
Gene namesi
Name:SUS1
Ordered Locus Names:At5g20830
ORF Names:T1M15.230
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G20830.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: TAIR
  2. plasmodesma Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Biotechnological usei

A one-pot system for efficient enzymatic production of a wide range of glucosides couples the activities of two recombinant enzymes, UDP-glucose: curcumin glucosyltransferase from Catharanthus roseus (CaUGT2) and sucrose synthase from Arabidopsis thaliana (AtSUS1). UDP, a product inhibitor of UDP-glucosyltransferase, was removed from the system and used for regeneration of UDP-glucose by the second enzyme, AtSUS1. The productivity was increased several-fold and UDP-glucose initially added to the reaction mixture could be reduced to one-tenth of the normal level.1 Publication

Disruption phenotypei

No visible phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 808808Sucrose synthase 1PRO_0000204644Add
BLAST

Proteomic databases

PaxDbiP49040.
PRIDEiP49040.

Expressioni

Tissue specificityi

Expressed in the phloem of leaves and in roots. Detected in the whole plant but more precisely confined to the vasculature in cotyledons, mature leaves and siliques.4 Publications

Inductioni

By cold, drought and anaerobic stress. By sugar or osmoticum. By anoxia in the roots (at protein level). Up-regulated by NUC/IDD8.5 Publications

Gene expression databases

GenevestigatoriP49040.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi17481. 3 interactions.
STRINGi3702.AT5G20830.1-P.

Structurei

Secondary structure

1
808
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 4011Combined sources
Beta strandi43 – 475Combined sources
Helixi48 – 536Combined sources
Turni54 – 585Combined sources
Helixi61 – 633Combined sources
Turni64 – 685Combined sources
Helixi69 – 746Combined sources
Beta strandi76 – 816Combined sources
Beta strandi83 – 9311Combined sources
Beta strandi96 – 1038Combined sources
Beta strandi109 – 1124Combined sources
Helixi114 – 12613Combined sources
Beta strandi136 – 1383Combined sources
Helixi140 – 1434Combined sources
Helixi152 – 1543Combined sources
Helixi158 – 16912Combined sources
Turni170 – 1723Combined sources
Helixi174 – 18613Combined sources
Beta strandi192 – 1965Combined sources
Helixi203 – 21917Combined sources
Helixi226 – 23510Combined sources
Helixi246 – 26116Combined sources
Helixi265 – 27410Combined sources
Beta strandi280 – 2845Combined sources
Beta strandi292 – 2943Combined sources
Helixi303 – 32523Combined sources
Beta strandi333 – 3397Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi351 – 3555Combined sources
Beta strandi360 – 3678Combined sources
Beta strandi369 – 3713Combined sources
Beta strandi374 – 3763Combined sources
Turni382 – 3843Combined sources
Helixi386 – 3883Combined sources
Helixi389 – 40315Combined sources
Beta strandi409 – 4146Combined sources
Helixi415 – 42915Combined sources
Beta strandi433 – 4364Combined sources
Helixi441 – 4444Combined sources
Turni446 – 4516Combined sources
Helixi452 – 4598Combined sources
Helixi461 – 47414Combined sources
Beta strandi475 – 4817Combined sources
Helixi483 – 4875Combined sources
Beta strandi490 – 4923Combined sources
Helixi497 – 4993Combined sources
Beta strandi500 – 5045Combined sources
Turni505 – 5073Combined sources
Beta strandi508 – 5136Combined sources
Beta strandi521 – 5233Combined sources
Turni530 – 5323Combined sources
Turni539 – 5413Combined sources
Helixi544 – 5463Combined sources
Helixi547 – 5559Combined sources
Beta strandi563 – 5653Combined sources
Beta strandi570 – 5723Combined sources
Beta strandi574 – 5785Combined sources
Turni583 – 5864Combined sources
Helixi587 – 59610Combined sources
Helixi598 – 6036Combined sources
Beta strandi605 – 6095Combined sources
Helixi620 – 63516Combined sources
Beta strandi639 – 6457Combined sources
Helixi651 – 66313Combined sources
Beta strandi667 – 6704Combined sources
Beta strandi675 – 6773Combined sources
Helixi679 – 6868Combined sources
Beta strandi691 – 6977Combined sources
Helixi699 – 7024Combined sources
Turni705 – 7073Combined sources
Beta strandi710 – 7123Combined sources
Helixi717 – 73317Combined sources
Helixi736 – 75116Combined sources
Helixi755 – 77622Combined sources
Turni777 – 7793Combined sources
Helixi780 – 79314Combined sources
Helixi795 – 8017Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S27X-ray2.91A/B/C/D/E/F/G/H1-808[»]
3S28X-ray2.80A/B/C/D/E/F/G/H1-808[»]
3S29X-ray2.85A/B/C/D/E/F/G/H1-808[»]
ProteinModelPortaliP49040.
SMRiP49040. Positions 27-807.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49040.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni277 – 754478GT-B glycosyltransferaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0438.
HOGENOMiHOG000240125.
InParanoidiP49040.
KOiK00695.
OMAiYQNDKAS.
PhylomeDBiP49040.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
IPR000368. Sucrose_synth.
IPR012820. Sucrose_synthase_pln/cyn.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 1 hit.
PF00862. Sucrose_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02470. sucr_synth. 1 hit.

Sequencei

Sequence statusi: Complete.

P49040-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MANAERMITR VHSQRERLNE TLVSERNEVL ALLSRVEAKG KGILQQNQII
60 70 80 90 100
AEFEALPEQT RKKLEGGPFF DLLKSTQEAI VLPPWVALAV RPRPGVWEYL
110 120 130 140 150
RVNLHALVVE ELQPAEFLHF KEELVDGVKN GNFTLELDFE PFNASIPRPT
160 170 180 190 200
LHKYIGNGVD FLNRHLSAKL FHDKESLLPL LKFLRLHSHQ GKNLMLSEKI
210 220 230 240 250
QNLNTLQHTL RKAEEYLAEL KSETLYEEFE AKFEEIGLER GWGDNAERVL
260 270 280 290 300
DMIRLLLDLL EAPDPCTLET FLGRVPMVFN VVILSPHGYF AQDNVLGYPD
310 320 330 340 350
TGGQVVYILD QVRALEIEML QRIKQQGLNI KPRILILTRL LPDAVGTTCG
360 370 380 390 400
ERLERVYDSE YCDILRVPFR TEKGIVRKWI SRFEVWPYLE TYTEDAAVEL
410 420 430 440 450
SKELNGKPDL IIGNYSDGNL VASLLAHKLG VTQCTIAHAL EKTKYPDSDI
460 470 480 490 500
YWKKLDDKYH FSCQFTADIF AMNHTDFIIT STFQEIAGSK ETVGQYESHT
510 520 530 540 550
AFTLPGLYRV VHGIDVFDPK FNIVSPGADM SIYFPYTEEK RRLTKFHSEI
560 570 580 590 600
EELLYSDVEN KEHLCVLKDK KKPILFTMAR LDRVKNLSGL VEWYGKNTRL
610 620 630 640 650
RELANLVVVG GDRRKESKDN EEKAEMKKMY DLIEEYKLNG QFRWISSQMD
660 670 680 690 700
RVRNGELYRY ICDTKGAFVQ PALYEAFGLT VVEAMTCGLP TFATCKGGPA
710 720 730 740 750
EIIVHGKSGF HIDPYHGDQA ADTLADFFTK CKEDPSHWDE ISKGGLQRIE
760 770 780 790 800
EKYTWQIYSQ RLLTLTGVYG FWKHVSNLDR LEARRYLEMF YALKYRPLAQ

AVPLAQDD
Length:808
Mass (Da):92,998
Last modified:April 14, 2009 - v3
Checksum:iCDB56C6A57BD852E
GO

Sequence cautioni

The sequence BAD94975.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611R → Q in CAA50317. (PubMed:8220487)Curated
Sequence conflicti108 – 1081V → L in CAA50317. (PubMed:8220487)Curated
Sequence conflicti222 – 2221S → P in CAA50317. (PubMed:8220487)Curated
Sequence conflicti405 – 4051N → D in CAA50317. (PubMed:8220487)Curated
Sequence conflicti434 – 4341C → QC in CAA50317. (PubMed:8220487)Curated
Sequence conflicti609 – 6091V → I in CAA50317. (PubMed:8220487)Curated
Sequence conflicti751 – 7522EK → DE in CAA50317. (PubMed:8220487)Curated
Sequence conflicti799 – 8002Missing in CAA50317. (PubMed:8220487)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70990 Genomic DNA. Translation: CAA50317.1.
AF296832 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92894.1.
CP002688 Genomic DNA. Translation: AED92895.1.
AK316826 mRNA. Translation: BAH19538.1.
AK222090 mRNA. Translation: BAD94975.1. Different initiation.
RefSeqiNP_001031915.1. NM_001036838.1.
NP_197583.1. NM_122090.3.
UniGeneiAt.21918.

Genome annotation databases

EnsemblPlantsiAT5G20830.1; AT5G20830.1; AT5G20830.
AT5G20830.2; AT5G20830.2; AT5G20830.
GeneIDi832206.
KEGGiath:AT5G20830.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70990 Genomic DNA. Translation: CAA50317.1 .
AF296832 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92894.1 .
CP002688 Genomic DNA. Translation: AED92895.1 .
AK316826 mRNA. Translation: BAH19538.1 .
AK222090 mRNA. Translation: BAD94975.1 . Different initiation.
RefSeqi NP_001031915.1. NM_001036838.1.
NP_197583.1. NM_122090.3.
UniGenei At.21918.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3S27 X-ray 2.91 A/B/C/D/E/F/G/H 1-808 [» ]
3S28 X-ray 2.80 A/B/C/D/E/F/G/H 1-808 [» ]
3S29 X-ray 2.85 A/B/C/D/E/F/G/H 1-808 [» ]
ProteinModelPortali P49040.
SMRi P49040. Positions 27-807.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 17481. 3 interactions.
STRINGi 3702.AT5G20830.1-P.

Protein family/group databases

CAZyi GT4. Glycosyltransferase Family 4.

Proteomic databases

PaxDbi P49040.
PRIDEi P49040.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G20830.1 ; AT5G20830.1 ; AT5G20830 .
AT5G20830.2 ; AT5G20830.2 ; AT5G20830 .
GeneIDi 832206.
KEGGi ath:AT5G20830.

Organism-specific databases

TAIRi AT5G20830.

Phylogenomic databases

eggNOGi COG0438.
HOGENOMi HOG000240125.
InParanoidi P49040.
KOi K00695.
OMAi YQNDKAS.
PhylomeDBi P49040.

Enzyme and pathway databases

BioCyci ARA:AT5G20830-MONOMER.
ARA:GQT-1272-MONOMER.
MetaCyc:AT5G20830-MONOMER.

Miscellaneous databases

EvolutionaryTracei P49040.

Gene expression databases

Genevestigatori P49040.

Family and domain databases

InterProi IPR001296. Glyco_trans_1.
IPR000368. Sucrose_synth.
IPR012820. Sucrose_synthase_pln/cyn.
[Graphical view ]
Pfami PF00534. Glycos_transf_1. 1 hit.
PF00862. Sucrose_synth. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02470. sucr_synth. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of an Arabidopsis sucrose synthase gene indicates a role in metabolization of sucrose both during phloem loading and in sink organs."
    Martin T., Frommer W.B., Salanoubat M., Willmitzer L.
    Plant J. 4:367-377(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. C24.
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [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. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [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 (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 521-808.
    Strain: cv. Columbia.
  6. "Sugar/osmoticum levels modulate differential abscisic acid-independent expression of two stress-responsive sucrose synthase genes in Arabidopsis."
    Dejardin A., Sokolov L.N., Kleczkowski L.A.
    Biochem. J. 344:503-509(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. "Structure and expression profile of the sucrose synthase multigene family in Arabidopsis."
    Baud S., Vaultier M.N., Rochat C.
    J. Exp. Bot. 55:397-409(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, TISSUE SPECIFICITY, INDUCTION.
  8. "An efficient chemoenzymatic production of small molecule glucosides with in situ UDP-glucose recycling."
    Masada S., Kawase Y., Nagatoshi M., Oguchi Y., Terasaka K., Mizukami H.
    FEBS Lett. 581:2562-2566(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGY.
  9. Cited for: BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE.
  10. "Localization of sucrose synthase in developing seed and siliques of Arabidopsis thaliana reveals diverse roles for SUS during development."
    Fallahi H., Scofield G.N., Badger M.R., Chow W.S., Furbank R.T., Ruan Y.L.
    J. Exp. Bot. 59:3283-3295(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Modulation of sugar metabolism by an INDETERMINATE DOMAIN transcription factor contributes to photoperiodic flowering in Arabidopsis."
    Seo P.J., Ryu J., Kang S.K., Park C.M.
    Plant J. 65:418-429(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY NUC.
  12. "Sucrose synthase activity in the sus1/sus2/sus3/sus4 Arabidopsis mutant is sufficient to support normal cellulose and starch production."
    Baroja-Fernandez E., Munoz F.J., Li J., Bahaji A., Almagro G., Montero M., Etxeberria E., Hidalgo M., Sesma M.T., Pozueta-Romero J.
    Proc. Natl. Acad. Sci. U.S.A. 109:321-326(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  13. "The structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications."
    Zheng Y., Anderson S., Zhang Y., Garavito R.M.
    J. Biol. Chem. 286:36108-36118(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT, FUNCTION.

Entry informationi

Entry nameiSUSY1_ARATH
AccessioniPrimary (citable) accession number: P49040
Secondary accession number(s): B9DFM1, Q56WF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 14, 2009
Last modified: October 29, 2014
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3