SIZ2_YEAST
ID SIZ2_YEAST Reviewed; 726 AA.
AC Q12216; D6W2L3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=E3 SUMO-protein ligase SIZ2;
DE EC=2.3.2.-;
DE AltName: Full=E3 SUMO-protein transferase SIZ2 {ECO:0000305};
DE AltName: Full=SAP and Miz-finger domain-containing protein 2;
GN Name=NFI1; Synonyms=SIZ2; OrderedLocusNames=YOR156C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RA De Virgilio C., Pringle J.R.;
RT "S. cerevisiae two-hybrid interactor with the C-terminus of Cdc12p.";
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1678;
RX PubMed=9046089;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<73::aid-yea52>3.0.co;2-m;
RA Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B.,
RA Martin R.P.;
RT "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae
RT chromosome XV.";
RL Yeast 13:73-83(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11587849; DOI=10.1016/s0378-1119(01)00662-x;
RA Takahashi Y., Toh-e A., Kikuchi Y.;
RT "A novel factor required for the SUMO1/Smt3 conjugation of yeast septins.";
RL Gene 275:223-231(2001).
RN [6]
RP FUNCTION.
RX PubMed=11333221; DOI=10.1093/genetics/158.1.95;
RA Strunnikov A.V., Aravind L., Koonin E.V.;
RT "Saccharomyces cerevisiae SMT4 encodes an evolutionarily conserved protease
RT with a role in chromosome condensation regulation.";
RL Genetics 158:95-107(2001).
RN [7]
RP FUNCTION.
RX PubMed=12761287; DOI=10.1093/jb/mvg054;
RA Takahashi Y., Toh-e A., Kikuchi Y.;
RT "Comparative analysis of yeast PIAS-type SUMO ligases in vivo and in
RT vitro.";
RL J. Biochem. 133:415-422(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15166219; DOI=10.1074/jbc.m404173200;
RA Zhou W., Ryan J.J., Zhou H.;
RT "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.
RT Induction of protein sumoylation by cellular stresses.";
RL J. Biol. Chem. 279:32262-32268(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: May act as an E3 ligase mediating SUMO/Smt3 attachment to
CC septins. May be involved in chromosome maintenance.
CC {ECO:0000269|PubMed:11333221, ECO:0000269|PubMed:12761287}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with CDC12.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11587849}.
CC -!- PTM: Autosumoylated upon ethanol stress. {ECO:0000269|PubMed:15166219}.
CC -!- MISCELLANEOUS: Present with 3170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PIAS family. {ECO:0000305}.
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DR EMBL; U33152; AAA86121.1; -; Genomic_DNA.
DR EMBL; U55020; AAC49642.1; -; Genomic_DNA.
DR EMBL; Z75064; CAA99362.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10929.1; -; Genomic_DNA.
DR PIR; S67044; S67044.
DR RefSeq; NP_014799.1; NM_001183575.1.
DR PDB; 6U75; X-ray; 2.63 A; A/B=154-420.
DR PDBsum; 6U75; -.
DR AlphaFoldDB; Q12216; -.
DR SMR; Q12216; -.
DR BioGRID; 34552; 227.
DR DIP; DIP-5775N; -.
DR IntAct; Q12216; 13.
DR MINT; Q12216; -.
DR STRING; 4932.YOR156C; -.
DR iPTMnet; Q12216; -.
DR PaxDb; Q12216; -.
DR PRIDE; Q12216; -.
DR EnsemblFungi; YOR156C_mRNA; YOR156C; YOR156C.
DR GeneID; 854327; -.
DR KEGG; sce:YOR156C; -.
DR SGD; S000005682; NFI1.
DR VEuPathDB; FungiDB:YOR156C; -.
DR eggNOG; KOG2169; Eukaryota.
DR GeneTree; ENSGT01030000234539; -.
DR HOGENOM; CLU_014307_0_0_1; -.
DR InParanoid; Q12216; -.
DR OMA; ECKVREQ; -.
DR BioCyc; YEAST:G3O-33673-MON; -.
DR Reactome; R-SCE-3232118; SUMOylation of transcription factors.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR UniPathway; UPA00886; -.
DR PRO; PR:Q12216; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12216; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:1990683; P:DNA double-strand break attachment to nuclear envelope; IGI:SGD.
DR GO; GO:0016925; P:protein sumoylation; IDA:SGD.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.60.120.780; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..726
FT /note="E3 SUMO-protein ligase SIZ2"
FT /id="PRO_0000218985"
FT DOMAIN 43..77
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 139..291
FT /note="PINIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00799"
FT ZN_FING 323..408
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 507..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:6U75"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:6U75"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 281..290
FT /evidence="ECO:0007829|PDB:6U75"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:6U75"
FT HELIX 308..319
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:6U75"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:6U75"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:6U75"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:6U75"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:6U75"
FT HELIX 393..400
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:6U75"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:6U75"
SQ SEQUENCE 726 AA; 81178 MW; 74F0F839C5E74BAB CRC64;
MASVMSNNNN NNNNNNASYM FTNPLSNTGG GLINEIKDAI NEMEQLKVLE LKQICKSLDL
SITGKKAVLQ DRIKQFLRKS CDIGHIDPWR PKAIKILIAK VRINSSLPKY STLWETLKTG
AFKHPVASGQ LPVTALQSTA LPPYSQQQAL AYSFTSPFYK PIVQIPDANK KLKQSAGRGC
TKMKFKVSKS NHDLLKSNKS YKLYLFSGFS IPFIYETVGH EAIDFPYPCE LVFNGTKLED
NVKGLKKQNG TGNPANLTPY LKVPTEMNHL DLHYLNIDKE YSISCFIVEV FSPEALLGKI
LKRPKIIKQA TTAYIKRTLN EQDDDDIITT STVLSLQCPI SCTRMKYPAK TDQCKHIQCF
DALWFLHSQS QVPTWQCPIC QHPIKFDQLK ISEFVDNIIQ NCNEDVEQVE ISVDGSWKPI
HNSSAVITDT VNQNHSVKNE NQGTVKQEQD YDSRNAFDTN LRNGSNHNEP EIISLDSSDD
EAFIPASKSF PTHVNPRNDQ LRADIFPSES EGSSDYNPNH TSTPKGSPTM DQDNYQDAFQ
MRSFLNQGAT TNINDTPTNN SSINSFVTAT NGDSRIFYNR GPSTPLLPAV LQNLTNQTEA
QRNPYGPNYN TTAQDRNLLG IEGDLPPIPP VDPNSEAETE LPTRTTSAAH LPPYIHVSTS
GHGDDGKIRK RRHSNVSIYI PKNPYATLMK RRPQANHAIM NKTLAQTNDF NTSAQDNSEV
VDLTSD
