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Protein

Suppressor of mar1-1 protein

Gene

SUM1

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

DNA-binding protein that specifically binds the regulatory region of middle sporulation genes (MSE). Required for the repression of middle sporulation genes during vegetative growth. Represses expression via the recruitment of histone deacetylase HST1.1 Publication

GO - Molecular functioni

GO - Biological processi

  • chromatin silencing at silent mating-type cassette Source: SGD
  • negative regulation of transcription by competitive promoter binding Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter during mitosis Source: SGD
  • positive regulation of DNA-dependent DNA replication initiation Source: SGD
  • sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Sporulation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29869-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Suppressor of mar1-1 protein
Short name:
SUM1-1 protein
Gene namesi
Name:SUM1
Ordered Locus Names:YDR310C
ORF Names:D9740.19
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR310C.
SGDiS000002718. SUM1.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi988 – 9881T → I: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 10621061Suppressor of mar1-1 proteinPRO_0000072311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei378 – 3781PhosphoserineCombined sources
Modified residuei379 – 3791PhosphoserineCombined sources
Modified residuei628 – 6281PhosphoserineCombined sources
Modified residuei681 – 6811PhosphoserineCombined sources
Modified residuei697 – 6971PhosphothreonineCombined sources
Modified residuei712 – 7121Phosphoserine; by ATM or ATRCombined sources
Modified residuei738 – 7381PhosphoserineCombined sources
Modified residuei817 – 8171PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP46676.

PTM databases

iPTMnetiP46676.

Interactioni

Subunit structurei

Interacts with RFM1. This interaction is required to recruit HST1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HMT1P380742EBI-18547,EBI-8394

Protein-protein interaction databases

BioGridi32363. 227 interactions.
DIPiDIP-6438N.
IntActiP46676. 20 interactions.
MINTiMINT-2788081.

Structurei

3D structure databases

ProteinModelPortaliP46676.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi464 – 4674Poly-Asn
Compositional biasi514 – 52310Poly-Ala

Phylogenomic databases

HOGENOMiHOG000065939.
InParanoidiP46676.
KOiK12779.
OrthoDBiEOG7FJH8W.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46676-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSENTTAPSD NITNEQRLPS GPKDDVDTLA LTSAQNQANS LRKLDTDANA
60 70 80 90 100
KALPSITDIP VSDDSDIKRQ VGSGFGSNPL HIKDSEAFPH SSIEALKEGM
110 120 130 140 150
DKVTKQCNDL KTALLSKDTS LTDSVQDLFN SLKVLSHNQS VLENKLDDVM
160 170 180 190 200
KNQVNTDILV NNLNERLNKL STMLQNTSKV NHSNLLIENS SNNTSSQHNT
210 220 230 240 250
SSSRRGPGRP RKDASTSTMN KLVSNAASVN LKSASNQGAP FSPVNITLPT
260 270 280 290 300
AVVQTSKSKR YFVEPSTKQE SLLLSAPSSS RDDADMSLTS VPQRTNNENG
310 320 330 340 350
KERPSTANSS SITPTPVTPN NLIQIKRKRG RPPKKRTVET MISNSTDTID
360 370 380 390 400
KSDASNRIKN EIPINSLLPS SKFHQIPSSP SNPVSQPAPV RTSRSATQEI
410 420 430 440 450
DIKSLELASL ISTNGDPNAE DSNTTDTVHN NVEGKVNVEE NKTEKEKIIT
460 470 480 490 500
IKSSSENSGN NTTNNNNTDN VIKFSANSDI NSDIRRLMVN DQFSLSYDAS
510 520 530 540 550
GNITVKLPPV SSPAAATAAA AAAVTSEMNR QQRELDKRRD SREKMLVNMK
560 570 580 590 600
YNDRDKAKSF MESNKKLLKA MKEEERRKRM TSIIHDNHLN LNLNEISTRS
610 620 630 640 650
KIKSAEKPTT KGSSMSPKPR SASISGISDH QQEGYQPLEQ EKLVDIDNEG
660 670 680 690 700
SNANSDSLKM GLTISAADTV HKVGIQSMLN SGEEAITKEN AEYERKTPGD
710 720 730 740 750
EETTTFVPLE NSQPSDTIRK RTAGDDGALD QTENTSISPK KRRTEDHTKG
760 770 780 790 800
EEDEGERGVG NSGTLATVEN VSGDISADLS KGTSSIHNDT ESANDSSNGN
810 820 830 840 850
GNLGLGTESR NTLLTATPIE LICREGFFYR RDIPDVPITT GAYLEFKFKA
860 870 880 890 900
KEEELINSSI NEEDYAAKSK HEKMNAHFFK PDIQEETELA FEILSKTTLT
910 920 930 940 950
EKYVNSLEYF LMEFRWENKL VGLGLKLRES KRTWQRRKAL FALFEFWRDQ
960 970 980 990 1000
SRDKRRFHNY TILHAVKEME NYRIFINRSV SWFYNHITLL KMILYDLCDN
1010 1020 1030 1040 1050
VTTQWREWMF PHNETLPALG QDGINEDNLN ETIDNMLIFD FLDDGSENNQ
1060
VKYSRIIPPD IR
Length:1,062
Mass (Da):118,201
Last modified:October 1, 1996 - v2
Checksum:i08A43263CCCFC1C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 2020MSENT…QRLPS → MNRDFRL (PubMed:8754829).CuratedAdd
BLAST
Sequence conflicti30 – 301A → R in AAB38222 (PubMed:8754829).Curated
Sequence conflicti408 – 4081A → G in AAB38222 (PubMed:8754829).Curated
Sequence conflicti523 – 5231Missing in AAB38222 (PubMed:8754829).Curated
Sequence conflicti826 – 8261G → A in AAB38222 (PubMed:8754829).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34832 Genomic DNA. Translation: AAB38222.1.
U28374 Genomic DNA. Translation: AAB64746.1.
BK006938 Genomic DNA. Translation: DAA12149.1.
PIRiS61196.
RefSeqiNP_010596.1. NM_001180618.1.

Genome annotation databases

EnsemblFungiiYDR310C; YDR310C; YDR310C.
GeneIDi851905.
KEGGisce:YDR310C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34832 Genomic DNA. Translation: AAB38222.1.
U28374 Genomic DNA. Translation: AAB64746.1.
BK006938 Genomic DNA. Translation: DAA12149.1.
PIRiS61196.
RefSeqiNP_010596.1. NM_001180618.1.

3D structure databases

ProteinModelPortaliP46676.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32363. 227 interactions.
DIPiDIP-6438N.
IntActiP46676. 20 interactions.
MINTiMINT-2788081.

PTM databases

iPTMnetiP46676.

Proteomic databases

MaxQBiP46676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR310C; YDR310C; YDR310C.
GeneIDi851905.
KEGGisce:YDR310C.

Organism-specific databases

EuPathDBiFungiDB:YDR310C.
SGDiS000002718. SUM1.

Phylogenomic databases

HOGENOMiHOG000065939.
InParanoidiP46676.
KOiK12779.
OrthoDBiEOG7FJH8W.

Enzyme and pathway databases

BioCyciYEAST:G3O-29869-MONOMER.

Miscellaneous databases

PROiP46676.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SUM1-1, a dominant suppressor of SIR mutations in Saccharomyces cerevisiae, increases transcriptional silencing at telomeres and HM mating-type loci and decreases chromosome stability."
    Chi M.-H., Shore D.
    Mol. Cell. Biol. 16:4281-4294(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, MUTAGENESIS OF THR-988.
    Strain: ATCC 200060 / W303.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Sum1 and Hst1 repress middle sporulation-specific gene expression during mitosis in Saccharomyces cerevisiae."
    Xie J., Pierce M., Gailus-Durner V., Wagner M., Winter E., Vershon A.K.
    EMBO J. 18:6448-6454(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  5. "Rfm1, a novel tethering factor required to recruit the hst1 histone deacetylase for repression of middle sporulation genes."
    McCord R., Pierce M., Xie J., Wonkatal S., Mickel C., Vershon A.K.
    Mol. Cell. Biol. 23:2009-2016(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RFM1.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-697, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628; SER-681; THR-697; SER-738 AND THR-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378; SER-379; SER-628; THR-697; SER-712; SER-738 AND THR-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSUM1_YEAST
AccessioniPrimary (citable) accession number: P46676
Secondary accession number(s): D6VST9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 135 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. 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.