Q680Q4 (SIZ1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 SUMO-protein ligase SIZ1
EC=6.3.2.-

Gene names

Name:	SIZ1
Ordered Locus Names:	At5g60410, At5g60420
ORF Names:	MUF9.5, MUF9.70

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	884 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E3 SUMO protein ligase involved in regulation processes. Mediates SUMO/ attachment to PHR1, a MYB transcriptional activator controlling the phosphate deficiency responses. 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. Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
Pathway	Protein modification; protein sumoylation.
Subunit structure	Interacts (via PHD domain) with SCE1, GTE3 and GTE5. Ref.14
Subcellular location	Nucleus speckle Ref.7.
Tissue specificity	Ubiquitous. Ref.11
Domain	The PHD-type zinc finger mediates interaction with SCE1, GTE3 and GTE5 and is required for E3 activity. Ref.14
Post-translational modification	Autosumoylated at Lys-100 and Lys-488. Ref.14
Disruption phenotype	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. Ref.9 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16
Sequence similarities	Belongs to the PIAS family. Contains 1 PHD-type zinc finger. Contains 1 SAP domain. Contains 1 SP-RING-type zinc finger.

Ontologies

Keywords
Biological process	Flowering Plant defense Stress response Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell division Inferred from mutant phenotype. Source: TAIR cell growth Inferred from mutant phenotype. Source: TAIR cellular response to phosphate starvation Inferred from mutant phenotype. Source: TAIR defense response Inferred from electronic annotation. Source: UniProtKB-KW detection of phosphate ion Inferred from direct assay. Source: TAIR developmental growth Inferred from mutant phenotype Ref.11. Source: UniProtKB flower development Inferred from electronic annotation. Source: UniProtKB-KW heat acclimation Inferred from mutant phenotype Ref.9. Source: UniProtKB negative regulation of flower development Inferred from mutant phenotype Ref.15. Source: TAIR negative regulation of systemic acquired resistance Inferred from mutant phenotype Ref.12. Source: UniProtKB protein sumoylation Inferred from direct assay Ref.15Ref.14. Source: UniProtKB regulation of abscisic acid mediated signaling pathway Inferred from mutant phenotype Ref.16. Source: TAIR regulation of growth Inferred from mutant phenotype Ref.11. Source: TAIR regulation of nitrate assimilation Inferred from mutant phenotype. Source: TAIR regulation of response to water deprivation Inferred from mutant phenotype Ref.11. Source: TAIR regulation of salicylic acid metabolic process Inferred from mutant phenotype. Source: TAIR response to freezing Inferred from mutant phenotype Ref.10. Source: TAIR response to water deprivation Inferred from mutant phenotype Ref.11. Source: UniProtKB
Cellular component	nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	SUMO ligase activity Inferred from direct assay Ref.15Ref.14. Source: UniProtKB nucleic acid binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.14. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q680Q4-1)

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.

Note: No experimental confirmation available.

Isoform 2 (identifier: Q680Q4-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q680Q4-3)

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

Isoform 4 (identifier: Q680Q4-4)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 884

884

E3 SUMO-protein ligase SIZ1

PRO_0000218984

Regions

Domain

11 – 45

35

SAP

Zinc finger

112 – 168

57

PHD-type

Zinc finger

348 – 425

78

SP-RING-type

Compositional bias

336 – 340

5

Poly-Gly

Amino acid modifications

Cross-link

100

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.14

Cross-link

488

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.14

Natural variations

Alternative sequence

828 – 832

5

ASLLL → GLFPV in isoform 2.

VSP_015483

Alternative sequence

833 – 884

52

Missing in isoform 2.

VSP_015484

Alternative sequence

860 – 884

25

NNEQD…CAGKN → VRPRMYLSIDSDSETMNRII RQDTGV in isoform 4.

VSP_015485

Alternative sequence

860 – 873

14

NNEQD…HRSLN → VRPRMYLSIDSDSE in isoform 3.

VSP_015486

Alternative sequence

874 – 884

11

Missing in isoform 3.

VSP_015487

Experimental info

Mutagenesis

100

1

K → R: Strongly reduces autosumoylation; when associated with R-488. Ref.14

Mutagenesis

488

1

K → R: Strongly reduces autosumoylation; when associated with R-100. Ref.14

Sequence conflict

335

1

I → S in BAD94301. Ref.5

Sequence conflict

335

1

I → S in BAD43867. Ref.5

Sequence conflict

436

1

E → D in BAD43867. Ref.5

Sequence conflict

785

1

D → G in BAD43867. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

884

Helix Strand Turn

Details...

Beta strand

106 – 108

3

Beta strand

126 – 128

3

Turn

132 – 134

3

Beta strand

137 – 139

3

Helix

140 – 143

4

Turn

148 – 150

3

Helix

163 – 167

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 5E44EA57FE896113	FASTA	884	97,034
	10 20 30 40 50 60 MDLEANCKEK LSYFRIKELK DVLTQLGLSK QGKKQELVDR ILTLLSDEQA ARLLSKKNTV 70 80 90 100 110 120 AKEAVAKLVD DTYRKMQVSG ASDLASKGQV SSDTSNLKVK GEPEDPFQPE IKVRCVCGNS 130 140 150 160 170 180 LETDSMIQCE DPRCHVWQHV GCVILPDKPM DGNPPLPESF YCEICRLTRA DPFWVTVAHP 190 200 210 220 230 240 LSPVRLTATT IPNDGASTMQ SVERTFQITR ADKDLLAKPE YDVQAWCMLL NDKVLFRMQW 250 260 270 280 290 300 PQYADLQVNG VPVRAINRPG GQLLGVNGRD DGPIITSCIR DGVNRISLSG GDVRIFCFGV 310 320 330 340 350 360 RLVKRRTLQQ VLNLIPEEGK GETFEDALAR VRRCIGGGGG DDNADSDSDI EVVADFFGVN 370 380 390 400 410 420 LRCPMSGSRI KVAGRFLPCV HMGCFDLDVF VELNQRSRKW QCPICLKNYS VEHVIVDPYF 430 440 450 460 470 480 NRITSKMKHC DEEVTEIEVK PDGSWRVKFK RESERRELGE LSQWHAPDGS LCPSAVDIKR 490 500 510 520 530 540 KMEMLPVKQE GYSDGPAPLK LGIRKNRNGI WEVSKPNTNG LSSSNRQEKV GYQEKNIIPM 550 560 570 580 590 600 SSSATGSGRD GDDASVNQDA IGTFDFVANG MELDSISMNV DSGYNFPDRN QSGEGGNNEV 610 620 630 640 650 660 IVLSDSDDEN DLVITPGPAY SGCQTDGGLT FPLNPPGIIN SYNEDPHSIA GGSSGLGLFN 670 680 690 700 710 720 DDDEFDTPLW SFPSETPEAP GFQLFRSDAD VSGGLVGLHH HSPLNCSPEI NGGYTMAPET 730 740 750 760 770 780 SMASVPVVPG STGRSEANDG LVDNPLAFGR DDPSLQIFLP TKPDASAQSG FKNQADMSNG 790 800 810 820 830 840 LRSEDWISLR LGDSASGNHG DPATTNGINS SHQMSTREGS MDTTTETASL LLGMNDSRQD 850 860 870 880 KAKKQRSDNP FSFPRQKRSN NEQDHQTRHR SLNKICIILC AGKN
	Isoform 2 [UniParc]. Checksum: 8C5DD47141D7E92F	FASTA	832	90,970
	10 20 30 40 50 60 MDLEANCKEK LSYFRIKELK DVLTQLGLSK QGKKQELVDR ILTLLSDEQA ARLLSKKNTV 70 80 90 100 110 120 AKEAVAKLVD DTYRKMQVSG ASDLASKGQV SSDTSNLKVK GEPEDPFQPE IKVRCVCGNS 130 140 150 160 170 180 LETDSMIQCE DPRCHVWQHV GCVILPDKPM DGNPPLPESF YCEICRLTRA DPFWVTVAHP 190 200 210 220 230 240 LSPVRLTATT IPNDGASTMQ SVERTFQITR ADKDLLAKPE YDVQAWCMLL NDKVLFRMQW 250 260 270 280 290 300 PQYADLQVNG VPVRAINRPG GQLLGVNGRD DGPIITSCIR DGVNRISLSG GDVRIFCFGV 310 320 330 340 350 360 RLVKRRTLQQ VLNLIPEEGK GETFEDALAR VRRCIGGGGG DDNADSDSDI EVVADFFGVN 370 380 390 400 410 420 LRCPMSGSRI KVAGRFLPCV HMGCFDLDVF VELNQRSRKW QCPICLKNYS VEHVIVDPYF 430 440 450 460 470 480 NRITSKMKHC DEEVTEIEVK PDGSWRVKFK RESERRELGE LSQWHAPDGS LCPSAVDIKR 490 500 510 520 530 540 KMEMLPVKQE GYSDGPAPLK LGIRKNRNGI WEVSKPNTNG LSSSNRQEKV GYQEKNIIPM 550 560 570 580 590 600 SSSATGSGRD GDDASVNQDA IGTFDFVANG MELDSISMNV DSGYNFPDRN QSGEGGNNEV 610 620 630 640 650 660 IVLSDSDDEN DLVITPGPAY SGCQTDGGLT FPLNPPGIIN SYNEDPHSIA GGSSGLGLFN 670 680 690 700 710 720 DDDEFDTPLW SFPSETPEAP GFQLFRSDAD VSGGLVGLHH HSPLNCSPEI NGGYTMAPET 730 740 750 760 770 780 SMASVPVVPG STGRSEANDG LVDNPLAFGR DDPSLQIFLP TKPDASAQSG FKNQADMSNG 790 800 810 820 830 LRSEDWISLR LGDSASGNHG DPATTNGINS SHQMSTREGS MDTTTETGLF PV
	Isoform 3 [UniParc]. Checksum: 0C9BD3F7F66AA3ED	FASTA	873	95,795
	10 20 30 40 50 60 MDLEANCKEK LSYFRIKELK DVLTQLGLSK QGKKQELVDR ILTLLSDEQA ARLLSKKNTV 70 80 90 100 110 120 AKEAVAKLVD DTYRKMQVSG ASDLASKGQV SSDTSNLKVK GEPEDPFQPE IKVRCVCGNS 130 140 150 160 170 180 LETDSMIQCE DPRCHVWQHV GCVILPDKPM DGNPPLPESF YCEICRLTRA DPFWVTVAHP 190 200 210 220 230 240 LSPVRLTATT IPNDGASTMQ SVERTFQITR ADKDLLAKPE YDVQAWCMLL NDKVLFRMQW 250 260 270 280 290 300 PQYADLQVNG VPVRAINRPG GQLLGVNGRD DGPIITSCIR DGVNRISLSG GDVRIFCFGV 310 320 330 340 350 360 RLVKRRTLQQ VLNLIPEEGK GETFEDALAR VRRCIGGGGG DDNADSDSDI EVVADFFGVN 370 380 390 400 410 420 LRCPMSGSRI KVAGRFLPCV HMGCFDLDVF VELNQRSRKW QCPICLKNYS VEHVIVDPYF 430 440 450 460 470 480 NRITSKMKHC DEEVTEIEVK PDGSWRVKFK RESERRELGE LSQWHAPDGS LCPSAVDIKR 490 500 510 520 530 540 KMEMLPVKQE GYSDGPAPLK LGIRKNRNGI WEVSKPNTNG LSSSNRQEKV GYQEKNIIPM 550 560 570 580 590 600 SSSATGSGRD GDDASVNQDA IGTFDFVANG MELDSISMNV DSGYNFPDRN QSGEGGNNEV 610 620 630 640 650 660 IVLSDSDDEN DLVITPGPAY SGCQTDGGLT FPLNPPGIIN SYNEDPHSIA GGSSGLGLFN 670 680 690 700 710 720 DDDEFDTPLW SFPSETPEAP GFQLFRSDAD VSGGLVGLHH HSPLNCSPEI NGGYTMAPET 730 740 750 760 770 780 SMASVPVVPG STGRSEANDG LVDNPLAFGR DDPSLQIFLP TKPDASAQSG FKNQADMSNG 790 800 810 820 830 840 LRSEDWISLR LGDSASGNHG DPATTNGINS SHQMSTREGS MDTTTETASL LLGMNDSRQD 850 860 870 KAKKQRSDNP FSFPRQKRSV RPRMYLSIDS DSE
	Isoform 4 [UniParc]. Checksum: CBD103E9A048FD1D	FASTA	885	97,181
	10 20 30 40 50 60 MDLEANCKEK LSYFRIKELK DVLTQLGLSK QGKKQELVDR ILTLLSDEQA ARLLSKKNTV 70 80 90 100 110 120 AKEAVAKLVD DTYRKMQVSG ASDLASKGQV SSDTSNLKVK GEPEDPFQPE IKVRCVCGNS 130 140 150 160 170 180 LETDSMIQCE DPRCHVWQHV GCVILPDKPM DGNPPLPESF YCEICRLTRA DPFWVTVAHP 190 200 210 220 230 240 LSPVRLTATT IPNDGASTMQ SVERTFQITR ADKDLLAKPE YDVQAWCMLL NDKVLFRMQW 250 260 270 280 290 300 PQYADLQVNG VPVRAINRPG GQLLGVNGRD DGPIITSCIR DGVNRISLSG GDVRIFCFGV 310 320 330 340 350 360 RLVKRRTLQQ VLNLIPEEGK GETFEDALAR VRRCIGGGGG DDNADSDSDI EVVADFFGVN 370 380 390 400 410 420 LRCPMSGSRI KVAGRFLPCV HMGCFDLDVF VELNQRSRKW QCPICLKNYS VEHVIVDPYF 430 440 450 460 470 480 NRITSKMKHC DEEVTEIEVK PDGSWRVKFK RESERRELGE LSQWHAPDGS LCPSAVDIKR 490 500 510 520 530 540 KMEMLPVKQE GYSDGPAPLK LGIRKNRNGI WEVSKPNTNG LSSSNRQEKV GYQEKNIIPM 550 560 570 580 590 600 SSSATGSGRD GDDASVNQDA IGTFDFVANG MELDSISMNV DSGYNFPDRN QSGEGGNNEV 610 620 630 640 650 660 IVLSDSDDEN DLVITPGPAY SGCQTDGGLT FPLNPPGIIN SYNEDPHSIA GGSSGLGLFN 670 680 690 700 710 720 DDDEFDTPLW SFPSETPEAP GFQLFRSDAD VSGGLVGLHH HSPLNCSPEI NGGYTMAPET 730 740 750 760 770 780 SMASVPVVPG STGRSEANDG LVDNPLAFGR DDPSLQIFLP TKPDASAQSG FKNQADMSNG 790 800 810 820 830 840 LRSEDWISLR LGDSASGNHG DPATTNGINS SHQMSTREGS MDTTTETASL LLGMNDSRQD 850 860 870 880 KAKKQRSDNP FSFPRQKRSV RPRMYLSIDS DSETMNRIIR QDTGV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9679202] [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: 14593172] [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: 19423640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: cv. Columbia.
[7]	"The Arabidopsis SUMO E3 ligase SIZ1 controls phosphate deficiency responses." Miura K., Rus A., Sharkhuu A., Yokoi S., Karthikeyan A.S., Raghothama K.G., Baek D., Koo Y.D., Jin J.B., Bressan R.A., Yun D.-J., Hasegawa P.M. Proc. Natl. Acad. Sci. U.S.A. 102:7760-7765(2005) [PubMed: 15894620] [Abstract] Cited for: IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION.
[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: 17041025] [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: 17416732] [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: 17905899] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[12]	"Salicylic acid-mediated innate immunity in Arabidopsis is regulated by SIZ1 SUMO E3 ligase." Lee J., Nam J., Park H.C., Na G., Miura K., Jin J.B., Yoo C.Y., Baek D., Kim D.H., Jeong J.C., Kim D., Lee S.Y., Salt D.E., Mengiste T., Gong Q., Ma S., Bohnert H.J., Kwak S.S. , Bressan R.A., Hasegawa P.M., Yun D.J. Plant J. 49:79-90(2007) [PubMed: 17163880] [Abstract] 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: 17644626] [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: 18502747] [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: 18069938] [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: 19276109] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00541361.
IPI00548950.
IPI00651114.
IPI00651122.

RefSeq

NP_001032108.1. NM_001037031.1.
NP_001032109.2. NM_001037032.2.
NP_001119465.1. NM_001125993.1.
NP_200849.2. NM_125434.3.
NP_974969.1. NM_203240.2.

UniGene

At.43746.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WEW	NMR	-	A	104-168	[»]

ProteinModelPortal

Q680Q4.

SMR

Q680Q4. Positions 2-95, 104-168, 358-427.

ModBase

Search...

Protein-protein interaction databases

STRING

Q680Q4.

Proteomic databases

PRIDE

Q680Q4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G60410.4; AT5G60410.4; AT5G60410.

GeneID

836163.

GenomeReviews

Gene locus AT5G60410 in contig BA000015_GR.

KEGG

ath:AT5G60410.

Organism-specific databases

TAIR

At5g60410.

Phylogenomic databases

eggNOG

KOG2169.

GeneTree

EPGT00050000003846.

HOGENOM

HBG597472.

InParanoid

Q680Q4.

OMA

GRSEAND.

PhylomeDB

Q680Q4.

ProtClustDB

CLSN2680574.

Gene expression databases

Genevestigator

Q680Q4.

Family and domain databases

InterPro

IPR003034. SAP_DNA-bd.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR004181. Znf_MIZ.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Gene3D

G3DSA:1.10.720.30. G3DSA:1.10.720.30. 1 hit.
G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.

Pfam

PF00628. PHD. 1 hit.
PF02037. SAP. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]

SMART

SM00249. PHD. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS50800. SAP. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. False negative.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SIZ1_ARATH

Accession

Primary (citable) accession number: Q680Q4
Secondary accession number(s): B9DG12 , Q56YS2, Q56ZS1, Q67ZL3, Q9FKK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	August 30, 2005
Last modified:	January 25, 2012
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program