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Protein

E3 SUMO-protein ligase SIZ1

Gene

SIZ1

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

Functioni

E3 SUMO protein ligase involved in regulation processes. Mediates SUMO/ attachment to PHR1, a MYB transcriptional activator controlling the phosphate deficiency responses (PubMed:15894620). Functions as an upstream negative regulator of salicylic acid (SA) accumulation and subsequent SA-mediated systemic acquired resistance (SAR) signaling. Probably not involved in jasmonic acid (JA)-mediated defense response. Participates in abiotic stress-induced sumoylation. Controls heat shock-induced SUMO1 and SUMO2 conjugation and facilitates basal thermotolerance. Involved in freezing tolerance by mediating sumoylation of ICE1, a transcription activator of the cold signaling regulator CBF3/DREB1A. Acts as positive regulator of drought stress tolerance. Acts as floral repressor that promotes FLC expression by repressing FLD activity through sumoylation. Acts as negative regulator of abscisic acid (ABA) signaling through ABI5 sumoylation. Mediates sumoylation of SCE1, GTE3 and GTE5.9 Publications

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri112 – 16857PHD-typeAdd
BLAST
Zinc fingeri348 – 42578SP-RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • SUMO transferase activity Source: TAIR
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell division Source: TAIR
  • cell growth Source: TAIR
  • cellular response to extracellular stimulus Source: InterPro
  • cellular response to phosphate starvation Source: TAIR
  • defense response Source: UniProtKB-KW
  • detection of phosphate ion Source: TAIR
  • developmental growth Source: UniProtKB
  • embryo sac development Source: TAIR
  • flower development Source: UniProtKB-KW
  • heat acclimation Source: UniProtKB
  • negative regulation of flower development Source: TAIR
  • negative regulation of systemic acquired resistance Source: UniProtKB
  • plant ovule development Source: TAIR
  • pollen tube guidance Source: TAIR
  • protein sumoylation Source: UniProtKB
  • regulation of abscisic acid-activated signaling pathway Source: TAIR
  • regulation of growth Source: TAIR
  • regulation of nitrate assimilation Source: TAIR
  • regulation of response to water deprivation Source: TAIR
  • regulation of salicylic acid metabolic process Source: TAIR
  • response to freezing Source: TAIR
  • response to water deprivation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Flowering, Plant defense, Stress response, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-ATH-3108214. SUMOylation of DNA damage response and repair proteins.
R-ATH-4615885. SUMOylation of DNA replication proteins.
R-ATH-5696395. Formation of Incision Complex in GG-NER.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase SIZ11 Publication (EC:6.3.2.-Curated)
Gene namesi
Name:SIZ11 Publication
Ordered Locus Names:At5g60410Imported
ORF Names:MUF9.5Imported, MUF9.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G60410.

Subcellular locationi

GO - Cellular componenti

  • nuclear speck Source: UniProtKB-SubCell
  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Dwarf phenotype. Heat-sensitive phenotype. Early flowering under short day. Elevated level of salicylic acid (SA), increased expression of pathogenesis-related (PR) genes and increased resistance to the bacterial pathogen P.syringae. ABA hypersensitivity during seed germination primary root growth. Exaggerated prototypical Pi-starvation responses, including increased root-shoot mass ratio and greater anthocyanin accumulation (PubMed:15894620).7 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001K → R: Strongly reduces autosumoylation; when associated with R-488. 1 Publication
Mutagenesisi488 – 4881K → R: Strongly reduces autosumoylation; when associated with R-100. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 884884E3 SUMO-protein ligase SIZ1PRO_0000218984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki100 – 100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki488 – 488Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Autosumoylated at Lys-100 and Lys-488.

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiQ680Q4.
PRIDEiQ680Q4.

PTM databases

iPTMnetiQ680Q4.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

ExpressionAtlasiQ680Q4. baseline and differential.
GenevisibleiQ680Q4. AT.

Interactioni

Subunit structurei

Interacts (via PHD domain) with SCE1, GTE3 and GTE5.1 Publication

Protein-protein interaction databases

BioGridi21407. 10 interactions.
STRINGi3702.AT5G60410.2.

Structurei

Secondary structure

1
884
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi106 – 1083Combined sources
Beta strandi126 – 1283Combined sources
Turni132 – 1343Combined sources
Beta strandi137 – 1393Combined sources
Helixi140 – 1434Combined sources
Turni148 – 1503Combined sources
Helixi163 – 1675Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEWNMR-A104-168[»]
ProteinModelPortaliQ680Q4.
SMRiQ680Q4. Positions 2-95, 104-168, 359-445.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ680Q4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 4535SAPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi336 – 3405Poly-Gly

Domaini

The PHD-type zinc finger mediates interaction with SCE1, GTE3 and GTE5 and is required for E3 activity.1 Publication

Sequence similaritiesi

Belongs to the PIAS family.Curated
Contains 1 PHD-type zinc finger.Curated
Contains 1 SAP domain.PROSITE-ProRule annotation
Contains 1 SP-RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri112 – 16857PHD-typeAdd
BLAST
Zinc fingeri348 – 42578SP-RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2169. Eukaryota.
ENOG410XQ2E. LUCA.
HOGENOMiHOG000029457.
InParanoidiQ680Q4.
OMAiQWHAPDG.
PhylomeDBiQ680Q4.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR003034. SAP_dom.
IPR031141. SIZ1_plant.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR004181. Znf_MIZ.
IPR001965. Znf_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10782:SF34. PTHR10782:SF34. 2 hits.
PfamiPF02037. SAP. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50800. SAP. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q680Q4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDLEANCKEK LSYFRIKELK DVLTQLGLSK QGKKQELVDR ILTLLSDEQA
60 70 80 90 100
ARLLSKKNTV AKEAVAKLVD DTYRKMQVSG ASDLASKGQV SSDTSNLKVK
110 120 130 140 150
GEPEDPFQPE IKVRCVCGNS LETDSMIQCE DPRCHVWQHV GCVILPDKPM
160 170 180 190 200
DGNPPLPESF YCEICRLTRA DPFWVTVAHP LSPVRLTATT IPNDGASTMQ
210 220 230 240 250
SVERTFQITR ADKDLLAKPE YDVQAWCMLL NDKVLFRMQW PQYADLQVNG
260 270 280 290 300
VPVRAINRPG GQLLGVNGRD DGPIITSCIR DGVNRISLSG GDVRIFCFGV
310 320 330 340 350
RLVKRRTLQQ VLNLIPEEGK GETFEDALAR VRRCIGGGGG DDNADSDSDI
360 370 380 390 400
EVVADFFGVN LRCPMSGSRI KVAGRFLPCV HMGCFDLDVF VELNQRSRKW
410 420 430 440 450
QCPICLKNYS VEHVIVDPYF NRITSKMKHC DEEVTEIEVK PDGSWRVKFK
460 470 480 490 500
RESERRELGE LSQWHAPDGS LCPSAVDIKR KMEMLPVKQE GYSDGPAPLK
510 520 530 540 550
LGIRKNRNGI WEVSKPNTNG LSSSNRQEKV GYQEKNIIPM SSSATGSGRD
560 570 580 590 600
GDDASVNQDA IGTFDFVANG MELDSISMNV DSGYNFPDRN QSGEGGNNEV
610 620 630 640 650
IVLSDSDDEN DLVITPGPAY SGCQTDGGLT FPLNPPGIIN SYNEDPHSIA
660 670 680 690 700
GGSSGLGLFN DDDEFDTPLW SFPSETPEAP GFQLFRSDAD VSGGLVGLHH
710 720 730 740 750
HSPLNCSPEI NGGYTMAPET SMASVPVVPG STGRSEANDG LVDNPLAFGR
760 770 780 790 800
DDPSLQIFLP TKPDASAQSG FKNQADMSNG LRSEDWISLR LGDSASGNHG
810 820 830 840 850
DPATTNGINS SHQMSTREGS MDTTTETASL LLGMNDSRQD KAKKQRSDNP
860 870 880
FSFPRQKRSN NEQDHQTRHR SLNKICIILC AGKN
Note: No experimental confirmation available.
Length:884
Mass (Da):97,034
Last modified:August 30, 2005 - v2
Checksum:i5E44EA57FE896113
GO
Isoform 2 (identifier: Q680Q4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     828-832: ASLLL → GLFPV
     833-884: Missing.

Note: No experimental confirmation available.
Show »
Length:832
Mass (Da):90,970
Checksum:i8C5DD47141D7E92F
GO
Isoform 3 (identifier: Q680Q4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     860-873: NNEQDHQTRHRSLN → VRPRMYLSIDSDSE
     874-884: Missing.

Show »
Length:873
Mass (Da):95,795
Checksum:i0C9BD3F7F66AA3ED
GO
Isoform 4 (identifier: Q680Q4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     860-884: NNEQDHQTRHRSLNKICIILCAGKN → VRPRMYLSIDSDSETMNRIIRQDTGV

Note: No experimental confirmation available.
Show »
Length:885
Mass (Da):97,181
Checksum:iCBD103E9A048FD1D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti335 – 3351I → S in BAD94301 (Ref. 5) Curated
Sequence conflicti335 – 3351I → S in BAD43867 (Ref. 5) Curated
Sequence conflicti436 – 4361E → D in BAD43867 (Ref. 5) Curated
Sequence conflicti785 – 7851D → G in BAD43867 (Ref. 5) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei828 – 8325ASLLL → GLFPV in isoform 2. 2 PublicationsVSP_015483
Alternative sequencei833 – 88452Missing in isoform 2. 2 PublicationsVSP_015484Add
BLAST
Alternative sequencei860 – 88425NNEQD…CAGKN → VRPRMYLSIDSDSETMNRII RQDTGV in isoform 4. 1 PublicationVSP_015485Add
BLAST
Alternative sequencei860 – 87314NNEQD…HRSLN → VRPRMYLSIDSDSE in isoform 3. 3 PublicationsVSP_015486Add
BLAST
Alternative sequencei874 – 88411Missing in isoform 3. 3 PublicationsVSP_015487Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY700572 mRNA. Translation: AAU00414.1.
AB011483 Genomic DNA. Translation: BAB08225.1.
CP002688 Genomic DNA. Translation: AED97324.1.
CP002688 Genomic DNA. Translation: AED97325.1.
CP002688 Genomic DNA. Translation: AED97326.1.
CP002688 Genomic DNA. Translation: AED97327.1.
CP002688 Genomic DNA. Translation: AED97328.1.
AY139752 mRNA. Translation: AAM98074.1.
BT004542 mRNA. Translation: AAO42788.1.
AK175813 mRNA. Translation: BAD43576.1.
AK221190 mRNA. Translation: BAD95283.1.
AK220973 mRNA. Translation: BAD94544.1.
AK221249 mRNA. Translation: BAD93882.1.
AK221292 mRNA. Translation: BAD94016.1.
AK220890 mRNA. Translation: BAD94301.1.
AK176104 mRNA. Translation: BAD43867.1.
AK316983 mRNA. Translation: BAH19679.1.
RefSeqiNP_001032108.1. NM_001037031.1. [Q680Q4-2]
NP_001032109.2. NM_001037032.2. [Q680Q4-1]
NP_001119465.1. NM_001125993.1. [Q680Q4-4]
NP_200849.2. NM_125434.3. [Q680Q4-3]
NP_974969.1. NM_203240.2. [Q680Q4-4]
UniGeneiAt.43746.

Genome annotation databases

EnsemblPlantsiAT5G60410.4; AT5G60410.4; AT5G60410. [Q680Q4-1]
GeneIDi836163.
KEGGiath:AT5G60410.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY700572 mRNA. Translation: AAU00414.1.
AB011483 Genomic DNA. Translation: BAB08225.1.
CP002688 Genomic DNA. Translation: AED97324.1.
CP002688 Genomic DNA. Translation: AED97325.1.
CP002688 Genomic DNA. Translation: AED97326.1.
CP002688 Genomic DNA. Translation: AED97327.1.
CP002688 Genomic DNA. Translation: AED97328.1.
AY139752 mRNA. Translation: AAM98074.1.
BT004542 mRNA. Translation: AAO42788.1.
AK175813 mRNA. Translation: BAD43576.1.
AK221190 mRNA. Translation: BAD95283.1.
AK220973 mRNA. Translation: BAD94544.1.
AK221249 mRNA. Translation: BAD93882.1.
AK221292 mRNA. Translation: BAD94016.1.
AK220890 mRNA. Translation: BAD94301.1.
AK176104 mRNA. Translation: BAD43867.1.
AK316983 mRNA. Translation: BAH19679.1.
RefSeqiNP_001032108.1. NM_001037031.1. [Q680Q4-2]
NP_001032109.2. NM_001037032.2. [Q680Q4-1]
NP_001119465.1. NM_001125993.1. [Q680Q4-4]
NP_200849.2. NM_125434.3. [Q680Q4-3]
NP_974969.1. NM_203240.2. [Q680Q4-4]
UniGeneiAt.43746.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEWNMR-A104-168[»]
ProteinModelPortaliQ680Q4.
SMRiQ680Q4. Positions 2-95, 104-168, 359-445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21407. 10 interactions.
STRINGi3702.AT5G60410.2.

PTM databases

iPTMnetiQ680Q4.

Proteomic databases

PaxDbiQ680Q4.
PRIDEiQ680Q4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G60410.4; AT5G60410.4; AT5G60410. [Q680Q4-1]
GeneIDi836163.
KEGGiath:AT5G60410.

Organism-specific databases

TAIRiAT5G60410.

Phylogenomic databases

eggNOGiKOG2169. Eukaryota.
ENOG410XQ2E. LUCA.
HOGENOMiHOG000029457.
InParanoidiQ680Q4.
OMAiQWHAPDG.
PhylomeDBiQ680Q4.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiR-ATH-3108214. SUMOylation of DNA damage response and repair proteins.
R-ATH-4615885. SUMOylation of DNA replication proteins.
R-ATH-5696395. Formation of Incision Complex in GG-NER.

Miscellaneous databases

EvolutionaryTraceiQ680Q4.
PROiQ680Q4.

Gene expression databases

ExpressionAtlasiQ680Q4. baseline and differential.
GenevisibleiQ680Q4. AT.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR003034. SAP_dom.
IPR031141. SIZ1_plant.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR004181. Znf_MIZ.
IPR001965. Znf_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10782:SF34. PTHR10782:SF34. 2 hits.
PfamiPF02037. SAP. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50800. SAP. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Arabidopsis thaliana SUMO E3 ligase."
    Ouyang J., Chua N.-H.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones."
    Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 5:131-145(1998) [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] (ISOFORM 3).
    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] (ISOFORMS 1; 2; 3 AND 4).
    Strain: cv. Columbia.
  6. "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] (ISOFORM 2).
    Strain: cv. Columbia.
  7. Cited for: IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  8. "Solution structure of PHD domain in DNA-binding family protein AAM98074."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 104-168.
  9. "SIZ1 small ubiquitin-like modifier E3 ligase facilitates basal thermotolerance in Arabidopsis independent of salicylic acid."
    Yoo C.Y., Miura K., Jin J.B., Lee J., Park H.C., Salt D.E., Yun D.J., Bressan R.A., Hasegawa P.M.
    Plant Physiol. 142:1548-1558(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "SIZ1-mediated sumoylation of ICE1 controls CBF3/DREB1A expression and freezing tolerance in Arabidopsis."
    Miura K., Jin J.B., Lee J., Yoo C.Y., Stirm V., Miura T., Ashworth E.N., Bressan R.A., Yun D.J., Hasegawa P.M.
    Plant Cell 19:1403-1414(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The Arabidopsis E3 SUMO ligase SIZ1 regulates plant growth and drought responses."
    Catala R., Ouyang J., Abreu I.A., Hu Y., Seo H., Zhang X., Chua N.H.
    Plant Cell 19:2952-2966(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  12. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  13. "Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and SUMO2 to nuclear proteins is essential."
    Saracco S.A., Miller M.J., Kurepa J., Vierstra R.D.
    Plant Physiol. 145:119-134(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  14. "The PHD domain of plant PIAS proteins mediates sumoylation of bromodomain GTE proteins."
    Garcia-Dominguez M., March-Diaz R., Reyes J.C.
    J. Biol. Chem. 283:21469-21477(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOSUMOYLATION AT LYS-100 AND LYS-488, INTERACTION WITH SCE1; GTE3 AND GTE5, DOMAIN, MUTAGENESIS OF LYS-100 AND LYS-488.
  15. "The SUMO E3 ligase, AtSIZ1, regulates flowering by controlling a salicylic acid-mediated floral promotion pathway and through affects on FLC chromatin structure."
    Jin J.B., Jin Y.H., Lee J., Miura K., Yoo C.Y., Kim W.Y., Van Oosten M., Hyun Y., Somers D.E., Lee I., Yun D.J., Bressan R.A., Hasegawa P.M.
    Plant J. 53:530-540(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  16. "Sumoylation of ABI5 by the Arabidopsis SUMO E3 ligase SIZ1 negatively regulates abscisic acid signaling."
    Miura K., Lee J., Jin J.B., Yoo C.Y., Miura T., Hasegawa P.M.
    Proc. Natl. Acad. Sci. U.S.A. 106:5418-5423(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiSIZ1_ARATH
AccessioniPrimary (citable) accession number: Q680Q4
Secondary accession number(s): B9DG12
, Q56YS2, Q56ZS1, Q67ZL3, Q9FKK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: July 6, 2016
This is version 118 of the entry and version 2 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.