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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)DescriptionActionsGraphical viewLength
Zinc fingeri346 – 423SP-RING-typePROSITE-ProRule annotationAdd BLAST78

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-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
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)DescriptionActionsGraphical viewLength
Mutagenesisi361C → S: Reduces E3 activity. 1 Publication1
Mutagenesisi377C → S: Strongly reduces E3 activity, but no effect on subcellular location. 3 Publications1
Mutagenesisi400C → S: Reduces E3 activity. 1 Publication1
Mutagenesisi460S → C: No effect on E3 activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002457831 – 904E3 SUMO-protein ligase SIZ1Add BLAST904

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei132PhosphoserineCombined sources1
Modified residuei794PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ04195.
PRIDEiQ04195.

PTM databases

iPTMnetiQ04195.

Interactioni

Subunit structurei

Interacts with UBC9 and CDC3.2 Publications

Protein-protein interaction databases

BioGridi32469. 145 interactors.
DIPiDIP-1011N.
IntActiQ04195. 2 interactors.
MINTiMINT-597779.

Structurei

Secondary structure

1904
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Beta strandi16 – 18Combined sources3
Helixi21 – 34Combined sources14
Helixi39 – 48Combined sources10
Helixi57 – 70Combined sources14
Helixi79 – 94Combined sources16
Helixi101 – 110Combined sources10
Beta strandi169 – 172Combined sources4
Beta strandi183 – 196Combined sources14
Beta strandi199 – 209Combined sources11
Helixi213 – 220Combined sources8
Beta strandi226 – 236Combined sources11
Helixi241 – 243Combined sources3
Beta strandi250 – 256Combined sources7
Beta strandi269 – 271Combined sources3
Helixi273 – 275Combined sources3
Helixi281 – 283Combined sources3
Beta strandi287 – 289Combined sources3
Beta strandi291 – 302Combined sources12
Beta strandi304 – 313Combined sources10
Helixi316 – 324Combined sources9
Helixi331 – 343Combined sources13
Beta strandi354 – 360Combined sources7
Turni362 – 364Combined sources3
Beta strandi365 – 367Combined sources3
Beta strandi369 – 374Combined sources6
Helixi385 – 394Combined sources10
Turni401 – 403Combined sources3
Helixi409 – 411Combined sources3
Beta strandi412 – 415Combined sources4
Helixi416 – 422Combined sources7
Beta strandi431 – 435Combined sources5
Beta strandi440 – 442Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RNNNMR-A1-111[»]
3I2DX-ray2.60A112-465[»]
5JNEX-ray2.85A/E167-445[»]
A/E453-559[»]
ProteinModelPortaliQ04195.
SMRiQ04195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04195.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 68SAPPROSITE-ProRule annotationAdd BLAST35
Domaini162 – 314PINITPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni794 – 904Required for localization at the bud neckAdd BLAST111

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)DescriptionActionsGraphical viewLength
Zinc fingeri346 – 423SP-RING-typePROSITE-ProRule annotationAdd BLAST78

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RNNNMR-A1-111[»]
3I2DX-ray2.60A112-465[»]
5JNEX-ray2.85A/E167-445[»]
A/E453-559[»]
ProteinModelPortaliQ04195.
SMRiQ04195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32469. 145 interactors.
DIPiDIP-1011N.
IntActiQ04195. 2 interactors.
MINTiMINT-597779.

PTM databases

iPTMnetiQ04195.

Proteomic databases

MaxQBiQ04195.
PRIDEiQ04195.

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-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
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: November 30, 2016
This is version 126 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.