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Protein

E3 SUMO-protein ligase SIZ1

Gene

SIZ1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as an E3 ligase mediating SUMO/Smt3 attachment to septins and PCNA. May be involved in chromosome maintenance.5 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 fingeri346 – 42378SP-RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  • chromosome segregation Source: SGD
  • DNA double-strand break attachment to nuclear envelope Source: SGD
  • negative regulation of protein ubiquitination Source: SGD
  • protein sumoylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29952-MONOMER.
ReactomeiR-SCE-3108214. SUMOylation of DNA damage response and repair proteins.
R-SCE-4615885. SUMOylation of DNA replication proteins.
R-SCE-5696395. Formation of Incision Complex in GG-NER.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase SIZ1 (EC:6.3.2.-)
Alternative name(s):
SAP and Miz-finger domain-containing protein 1
Ubiquitin-like protein ligase 1
Gene namesi
Name:SIZ1
Synonyms:ULL1
Ordered Locus Names:YDR409W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR409W.
SGDiS000002817. SIZ1.

Subcellular locationi

GO - Cellular componenti

  • cellular bud neck Source: UniProtKB-SubCell
  • nuclear chromatin Source: SGD
  • septin ring Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi361 – 3611C → S: Reduces E3 activity. 1 Publication
Mutagenesisi377 – 3771C → S: Strongly reduces E3 activity, but no effect on subcellular location. 3 Publications
Mutagenesisi400 – 4001C → S: Reduces E3 activity. 1 Publication
Mutagenesisi460 – 4601S → C: No effect on E3 activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 904904E3 SUMO-protein ligase SIZ1PRO_0000245783Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei132 – 1321PhosphoserineCombined sources
Modified residuei794 – 7941PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated in early M-phase.2 Publications
Autosumoylated upon ethanol stress.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ04195.

PTM databases

iPTMnetiQ04195.

Interactioni

Subunit structurei

Interacts with UBC9 and CDC3.2 Publications

Protein-protein interaction databases

BioGridi32469. 144 interactions.
DIPiDIP-1011N.
IntActiQ04195. 2 interactions.
MINTiMINT-597779.

Structurei

Secondary structure

1
904
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63Combined sources
Beta strandi16 – 183Combined sources
Helixi21 – 3414Combined sources
Helixi39 – 4810Combined sources
Helixi57 – 7014Combined sources
Helixi79 – 9416Combined sources
Helixi101 – 11010Combined sources
Beta strandi169 – 1724Combined sources
Beta strandi183 – 19614Combined sources
Beta strandi199 – 20911Combined sources
Helixi213 – 2208Combined sources
Beta strandi226 – 23611Combined sources
Helixi241 – 2433Combined sources
Beta strandi250 – 2567Combined sources
Helixi273 – 2753Combined sources
Helixi281 – 2833Combined sources
Beta strandi287 – 2893Combined sources
Beta strandi291 – 30212Combined sources
Beta strandi304 – 31310Combined sources
Helixi316 – 3249Combined sources
Helixi331 – 34313Combined sources
Beta strandi354 – 3607Combined sources
Turni362 – 3643Combined sources
Beta strandi365 – 3673Combined sources
Beta strandi369 – 3746Combined sources
Helixi385 – 39410Combined sources
Turni401 – 4033Combined sources
Helixi409 – 4113Combined sources
Beta strandi412 – 4154Combined sources
Helixi416 – 4227Combined sources
Beta strandi431 – 4355Combined sources
Beta strandi440 – 4423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RNNNMR-A1-111[»]
3I2DX-ray2.60A112-465[»]
ProteinModelPortaliQ04195.
SMRiQ04195. Positions 1-111, 159-444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04195.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 6835SAPPROSITE-ProRule annotationAdd
BLAST
Domaini162 – 314153PINITPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni794 – 904111Required for localization at the bud neckAdd
BLAST

Domaini

The SAP domain is required for nuclear targeting.
The SP-RING-type zinc finger mediates interaction with UBC9 and CDC3 and is required for E3 activity.

Sequence similaritiesi

Belongs to the PIAS family.Curated
Contains 1 PINIT domain.PROSITE-ProRule annotation
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 fingeri346 – 42378SP-RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00550000074410.
InParanoidiQ04195.
KOiK04706.
OrthoDBiEOG092C445R.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR023321. PINIT.
IPR003034. SAP_dom.
IPR027229. SIZ1/SIZ2/Pli1/Gei17.
IPR004181. Znf_MIZ.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10782:SF4. PTHR10782:SF4. 2 hits.
PfamiPF14324. PINIT. 1 hit.
PF02037. SAP. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04195-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MINLEDYWED ETPGPDREPT NELRNEVEET ITLMELLKVS ELKDICRSVS
60 70 80 90 100
FPVSGRKAVL QDLIRNFLQN ALVVGKSDPY RVQAVKFLIE RIRKNEPLPV
110 120 130 140 150
YKDLWNALRK GTPLSAITVR SMEGPPTVQQ QSPSVIRQSP TQRRKTSTTS
160 170 180 190 200
STSRAPPPTN PDASSSSSSF AVPTIHFKES PFYKIQRLIP ELVMNVEVTG
210 220 230 240 250
GRGMCSAKFK LSKADYNLLS NPNSKHRLYL FSGMINPLGS RGNEPIQFPF
260 270 280 290 300
PNELRCNNVQ IKDNIRGFKS KPGTAKPADL TPHLKPYTQQ NNVELIYAFT
310 320 330 340 350
TKEYKLFGYI VEMITPEQLL EKVLQHPKII KQATLLYLKK TLREDEEMGL
360 370 380 390 400
TTTSTIMSLQ CPISYTRMKY PSKSINCKHL QCFDALWFLH SQLQIPTWQC
410 420 430 440 450
PVCQIDIALE NLAISEFVDD ILQNCQKNVE QVELTSDGKW TAILEDDDDS
460 470 480 490 500
DSDSNDGSRS PEKGTSVSDH HCSSSHPSEP IIINLDSDDD EPNGNNPHVT
510 520 530 540 550
NNHDDSNRHS NDNNNNSIKN NDSHNKNNNN NNNNNNNNND NNNSIENNDS
560 570 580 590 600
NSNNKHDHGS RSNTPSHNHT KNLMNDNDDD DDDRLMAEIT SNHLKSTNTD
610 620 630 640 650
ILTEKGSSAP SRTLDPKSYN IVASETTTPV TNRVIPEYLG NSSSYIGKQL
660 670 680 690 700
PNILGKTPLN VTAVDNSSHL ISPDVSVSSP TPRNTASNAS SSALSTPPLI
710 720 730 740 750
RMSSLDPRGS TVPDKTIRPP INSNSYTASI SDSFVQPQES SVFPPREQNM
760 770 780 790 800
DMSFPSTVNS RFNDPRLNTT RFPDSTLRGA TILSNNGLDQ RNNSLPTTEA
810 820 830 840 850
ITRNDVGRQN STPVLPTLPQ NVPIRTNSNK SGLPLINNEN SVPNPPNTAT
860 870 880 890 900
IPLQKSRLIV NPFIPRRPYS NVLPQKRQLS NTSSTSPIMG TWKTQDYGKK

YNSG
Length:904
Mass (Da):100,796
Last modified:November 1, 1996 - v1
Checksum:iCBD581DFF23F7802
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32274 Genomic DNA. Translation: AAB64849.1.
L07952 Unassigned DNA. Translation: AAA16519.1.
BK006938 Genomic DNA. Translation: DAA12251.1.
PIRiS69691.
RefSeqiNP_010697.3. NM_001180717.3.

Genome annotation databases

EnsemblFungiiYDR409W; YDR409W; YDR409W.
GeneIDi852018.
KEGGisce:YDR409W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32274 Genomic DNA. Translation: AAB64849.1.
L07952 Unassigned DNA. Translation: AAA16519.1.
BK006938 Genomic DNA. Translation: DAA12251.1.
PIRiS69691.
RefSeqiNP_010697.3. NM_001180717.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RNNNMR-A1-111[»]
3I2DX-ray2.60A112-465[»]
ProteinModelPortaliQ04195.
SMRiQ04195. Positions 1-111, 159-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32469. 144 interactions.
DIPiDIP-1011N.
IntActiQ04195. 2 interactions.
MINTiMINT-597779.

PTM databases

iPTMnetiQ04195.

Proteomic databases

MaxQBiQ04195.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR409W; YDR409W; YDR409W.
GeneIDi852018.
KEGGisce:YDR409W.

Organism-specific databases

EuPathDBiFungiDB:YDR409W.
SGDiS000002817. SIZ1.

Phylogenomic databases

GeneTreeiENSGT00550000074410.
InParanoidiQ04195.
KOiK04706.
OrthoDBiEOG092C445R.

Enzyme and pathway databases

UniPathwayiUPA00886.
BioCyciYEAST:G3O-29952-MONOMER.
ReactomeiR-SCE-3108214. SUMOylation of DNA damage response and repair proteins.
R-SCE-4615885. SUMOylation of DNA replication proteins.
R-SCE-5696395. Formation of Incision Complex in GG-NER.

Miscellaneous databases

EvolutionaryTraceiQ04195.
PROiQ04195.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR023321. PINIT.
IPR003034. SAP_dom.
IPR027229. SIZ1/SIZ2/Pli1/Gei17.
IPR004181. Znf_MIZ.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10782:SF4. PTHR10782:SF4. 2 hits.
PfamiPF14324. PINIT. 1 hit.
PF02037. SAP. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSIZ1_YEAST
AccessioniPrimary (citable) accession number: Q04195
Secondary accession number(s): D6VT41, Q06762, Q7LIJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 149 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.