CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014720
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 SUMO-protein ligase SIZ1 
Protein Synonyms/Alias
  
Gene Name
 SIZ1 
Gene Synonyms/Alias
 At5g60410; At5g60420; MUF9.5; MUF9.70 
Created Date
 July 27, 2013 
Organism
 Arabidopsis thaliana (Mouse-ear cress) 
NCBI Taxa ID
 3702 
Lysine Modification
Position
Peptide
Type
References
100DTSNLKVKGEPEDPFsumoylation[1, 2, 3]
479CPSAVDIKRKMEMLPsumoylation[3]
488KMEMLPVKQEGYSDGsumoylation[1, 2, 3]
Reference
 [1] The PHD domain of plant PIAS proteins mediates sumoylation of bromodomain GTE proteins.
 Garcia-Dominguez M, March-Diaz R, Reyes JC.
 J Biol Chem. 2008 Aug 1;283(31):21469-77. [PMID: 18502747]
 [2] Specific domain structures control abscisic acid-, salicylic acid-, and stress-mediated SIZ1 phenotypes.
 Cheong MS, Park HC, Hong MJ, Lee J, Choi W, Jin JB, Bohnert HJ, Lee SY, Bressan RA, Yun DJ.
 Plant Physiol. 2009 Dec;151(4):1930-42. [PMID: 19837819]
 [3] Proteomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in Arabidopsis.
 Miller MJ, Barrett-Wilt GA, Hua Z, Vierstra RD.
 Proc Natl Acad Sci U S A. 2010 Sep 21;107(38):16512-7. [PMID: 20813957] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 11 45 SAP.
 ZN_FING 112 168 PHD-type.
 ZN_FING 348 425 SP-RING-type.
 CROSSLNK 100 100 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 488 488 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Flowering; Isopeptide bond; Ligase; Metal-binding; Nucleus; Plant defense; Reference proteome; Stress response; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 884 AA 
Protein Sequence
MDLEANCKEK LSYFRIKELK DVLTQLGLSK QGKKQELVDR ILTLLSDEQA ARLLSKKNTV 60
AKEAVAKLVD DTYRKMQVSG ASDLASKGQV SSDTSNLKVK GEPEDPFQPE IKVRCVCGNS 120
LETDSMIQCE DPRCHVWQHV GCVILPDKPM DGNPPLPESF YCEICRLTRA DPFWVTVAHP 180
LSPVRLTATT IPNDGASTMQ SVERTFQITR ADKDLLAKPE YDVQAWCMLL NDKVLFRMQW 240
PQYADLQVNG VPVRAINRPG GQLLGVNGRD DGPIITSCIR DGVNRISLSG GDVRIFCFGV 300
RLVKRRTLQQ VLNLIPEEGK GETFEDALAR VRRCIGGGGG DDNADSDSDI EVVADFFGVN 360
LRCPMSGSRI KVAGRFLPCV HMGCFDLDVF VELNQRSRKW QCPICLKNYS VEHVIVDPYF 420
NRITSKMKHC DEEVTEIEVK PDGSWRVKFK RESERRELGE LSQWHAPDGS LCPSAVDIKR 480
KMEMLPVKQE GYSDGPAPLK LGIRKNRNGI WEVSKPNTNG LSSSNRQEKV GYQEKNIIPM 540
SSSATGSGRD GDDASVNQDA IGTFDFVANG MELDSISMNV DSGYNFPDRN QSGEGGNNEV 600
IVLSDSDDEN DLVITPGPAY SGCQTDGGLT FPLNPPGIIN SYNEDPHSIA GGSSGLGLFN 660
DDDEFDTPLW SFPSETPEAP GFQLFRSDAD VSGGLVGLHH HSPLNCSPEI NGGYTMAPET 720
SMASVPVVPG STGRSEANDG LVDNPLAFGR DDPSLQIFLP TKPDASAQSG FKNQADMSNG 780
LRSEDWISLR LGDSASGNHG DPATTNGINS SHQMSTREGS MDTTTETASL LLGMNDSRQD 840
KAKKQRSDNP FSFPRQKRSN NEQDHQTRHR SLNKICIILC AGKN 884 
Gene Ontology
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:TAIR.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0019789; F:SUMO ligase activity; IDA:TAIR.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051301; P:cell division; IMP:TAIR.
 GO:0016049; P:cell growth; IMP:TAIR.
 GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
 GO:0006952; P:defense response; IEA:UniProtKB-KW.
 GO:0010247; P:detection of phosphate ion; IDA:TAIR.
 GO:0048589; P:developmental growth; IMP:UniProtKB.
 GO:0009908; P:flower development; IEA:UniProtKB-KW.
 GO:0010286; P:heat acclimation; IMP:UniProtKB.
 GO:0009910; P:negative regulation of flower development; IMP:TAIR.
 GO:0010113; P:negative regulation of systemic acquired resistance; IMP:UniProtKB.
 GO:0016925; P:protein sumoylation; IDA:UniProtKB.
 GO:0009787; P:regulation of abscisic acid mediated signaling pathway; IMP:TAIR.
 GO:0040008; P:regulation of growth; IMP:TAIR.
 GO:0090352; P:regulation of nitrate assimilation; IMP:TAIR.
 GO:2000070; P:regulation of response to water deprivation; IMP:TAIR.
 GO:0010337; P:regulation of salicylic acid metabolic process; IMP:TAIR.
 GO:0050826; P:response to freezing; IMP:TAIR.
 GO:0009414; P:response to water deprivation; IMP:UniProtKB. 
Interpro
 IPR003034; SAP_dom.
 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. 
Pfam
 PF00628; PHD
 PF02037; SAP
 PF02891; zf-MIZ 
SMART
 SM00249; PHD
 SM00513; SAP 
PROSITE
 PS50800; SAP
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2
 PS51044; ZF_SP_RING 
PRINTS