Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

General negative regulator of transcription subunit 4

Gene

MOT2

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 component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri33 – 7846RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri229 – 25628C3H1-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • deadenylation-independent decapping of nuclear-transcribed mRNA Source: SGD
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  • proteasomal protein catabolic process Source: SGD
  • protein polyubiquitination Source: SGD
  • protein ubiquitination Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-30242-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
General negative regulator of transcription subunit 4
Alternative name(s):
Modulator of transcription 2
Gene namesi
Name:MOT2
Synonyms:CCL1, NOT4, SIG1, SSF1
Ordered Locus Names:YER068W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER068W.
SGDiS000000870. MOT2.

Subcellular locationi

GO - Cellular componenti

  • CCR4-NOT core complex Source: SGD
  • cytoplasm Source: SGD
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 587587General negative regulator of transcription subunit 4PRO_0000081681Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei310 – 3101PhosphothreonineCombined sources
Modified residuei312 – 3121PhosphoserineCombined sources
Modified residuei326 – 3261PhosphothreonineCombined sources
Modified residuei360 – 3601PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP34909.
PeptideAtlasiP34909.

PTM databases

iPTMnetiP34909.

Interactioni

Subunit structurei

Forms a NOT protein complex that comprises NOT1, NOT2, NOT3, NOT4 and NOT5. Subunit of the 1.0 MDa CCR4-NOT core complex that contains CCR4, CAF1, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In the complex interacts with NOT1. The core complex probably is part of a less characterized 1.9 MDa CCR4-NOT complex.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CAF40P538295EBI-12174,EBI-28306
CCR4P313844EBI-12174,EBI-4396
CDC39P256554EBI-12174,EBI-12139
POP2P390083EBI-12174,EBI-13629

Protein-protein interaction databases

BioGridi36811. 175 interactions.
DIPiDIP-2255N.
IntActiP34909. 23 interactions.
MINTiMINT-617490.

Structurei

Secondary structure

1
587
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni34 – 363Combined sources
Turni42 – 465Combined sources
Helixi58 – 669Combined sources
Beta strandi68 – 703Combined sources
Turni75 – 773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5AIEX-ray2.80A30-83[»]
5AJDX-ray3.62B/D/F/H/J/L418-477[»]
ProteinModelPortaliP34909.
SMRiP34909. Positions 30-82, 132-236, 420-469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini137 – 22892RRMPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili94 – 12835Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 C3H1-type zinc finger.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri33 – 7846RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri229 – 25628C3H1-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00390000000068.
HOGENOMiHOG000248860.
InParanoidiP34909.
KOiK10643.
OMAiEEDYCPL.
OrthoDBiEOG7FNCKC.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
IPR000571. Znf_CCCH.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P34909-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMNPHVQENL QAIHNALSNF DTSFLSEDEE DYCPLCIEPM DITDKNFFPC
60 70 80 90 100
PCGYQICQFC YNNIRQNPEL NGRCPACRRK YDDENVRYVT LSPEELKMER
110 120 130 140 150
AKLARKEKER KHREKERKEN EYTNRKHLSG TRVIQKNLVY VVGINPPVPY
160 170 180 190 200
EEVAPTLKSE KYFGQYGKIN KIVVNRKTPH SNNTTSEHYH HHSPGYGVYI
210 220 230 240 250
TFGSKDDAAR CIAQVDGTYM DGRLIKAAYG TTKYCSSYLR GLPCPNPNCM
260 270 280 290 300
FLHEPGEEAD SFNKRELHNK QQAQQQSGGT AFTRSGIHNN ISTSTAGSNT
310 320 330 340 350
NLLSENFTGT PSPAAMRAQL HHDSHTNAGT PVLTPAPVPA GSNPWGVTQS
360 370 380 390 400
ATPVTSINLS KNSSSINLPT LNDSLGHHTT PTTENTITST TTTTNTNATS
410 420 430 440 450
HSHGSKKKQS LAAEEYKDPY DALGNAVDFL DARLHSLSNY QKRPISIKSN
460 470 480 490 500
IIDEETYKKY PSLFSWDKIE ASKKSDNTLA NKLVEILAIK PIDYTASVVQ
510 520 530 540 550
FLQSVNVGVN DNITITDNTK TPTQPIRLQT VSQQIQPPLN VSTPPPGIFG
560 570 580
PQHKVPIQQQ QMGDTSSRNS SDLLNQLING RKIIAGN
Length:587
Mass (Da):65,354
Last modified:February 1, 1994 - v1
Checksum:i8847084BD9BF48B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96736 Genomic DNA. Translation: AAC37413.1.
L26309 Unassigned DNA. Translation: AAB00326.1.
U18813 Genomic DNA. Translation: AAB64604.1.
BK006939 Genomic DNA. Translation: DAA07727.1.
PIRiA56015.
RefSeqiNP_010991.3. NM_001178959.3.

Genome annotation databases

EnsemblFungiiYER068W; YER068W; YER068W.
GeneIDi856799.
KEGGisce:YER068W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96736 Genomic DNA. Translation: AAC37413.1.
L26309 Unassigned DNA. Translation: AAB00326.1.
U18813 Genomic DNA. Translation: AAB64604.1.
BK006939 Genomic DNA. Translation: DAA07727.1.
PIRiA56015.
RefSeqiNP_010991.3. NM_001178959.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5AIEX-ray2.80A30-83[»]
5AJDX-ray3.62B/D/F/H/J/L418-477[»]
ProteinModelPortaliP34909.
SMRiP34909. Positions 30-82, 132-236, 420-469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36811. 175 interactions.
DIPiDIP-2255N.
IntActiP34909. 23 interactions.
MINTiMINT-617490.

PTM databases

iPTMnetiP34909.

Proteomic databases

MaxQBiP34909.
PeptideAtlasiP34909.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER068W; YER068W; YER068W.
GeneIDi856799.
KEGGisce:YER068W.

Organism-specific databases

EuPathDBiFungiDB:YER068W.
SGDiS000000870. MOT2.

Phylogenomic databases

GeneTreeiENSGT00390000000068.
HOGENOMiHOG000248860.
InParanoidiP34909.
KOiK10643.
OMAiEEDYCPL.
OrthoDBiEOG7FNCKC.

Enzyme and pathway databases

BioCyciYEAST:G3O-30242-MONOMER.

Miscellaneous databases

NextBioi983041.
PROiP34909.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
IPR000571. Znf_CCCH.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of SIG1, a Saccharomyces cerevisiae gene involved in negative regulation of G-protein-mediated signal transduction."
    Leberer E., Dignard D., Harcus D., Whiteway M., Thomas D.Y.
    EMBO J. 13:3050-3064(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "MOT2 encodes a negative regulator of gene expression that affects basal expression of pheromone-responsive genes in Saccharomyces cerevisiae."
    Cade R.M., Errede B.
    Mol. Cell. Biol. 14:3139-3149(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "The yeast MOT2 gene encodes a putative zinc finger protein that serves as a global negative regulator affecting expression of several categories of genes, including mating-pheromone-responsive genes."
    Irie K., Yamaguchi K., Kawase K., Matsumoto K.
    Mol. Cell. Biol. 14:3150-3157(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "NOT1(CDC39), NOT2(CDC36), NOT3, and NOT4 encode a global-negative regulator of transcription that differentially affects TATA-element utilization."
    Collart M.A., Struhl K.
    Genes Dev. 8:525-537(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "The NOT proteins are part of the CCR4 transcriptional complex and affect gene expression both positively and negatively."
    Liu H.Y., Badarinarayana V., Audino D.C., Rappsilber J., Mann M., Denis C.L.
    EMBO J. 17:1096-1106(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CCR4-NOT CORE COMPLEX, FUNCTION OF THE CCR4-NOT CORE COMPLEX IN TRANSCRIPTIONAL REGULATION.
  8. "The CCR4 and CAF1 proteins of the CCR4-NOT complex are physically and functionally separated from NOT2, NOT4, and NOT5."
    Bai Y., Salvadore C., Chiang Y.C., Collart M.A., Liu H.Y., Denis C.L.
    Mol. Cell. Biol. 19:6642-6651(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOT1.
  9. "Purification and characterization of the 1.0 MDa CCR4-NOT complex identifies two novel components of the complex."
    Chen J., Rappsilber J., Chiang Y.C., Russell P., Mann M., Denis C.L.
    J. Mol. Biol. 314:683-694(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CCR4-NOT CORE COMPLEX.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "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-310 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 THR-310; SER-312; THR-326 AND SER-360, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNOT4_YEAST
AccessioniPrimary (citable) accession number: P34909
Secondary accession number(s): D3DLX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 11, 2016
This is version 165 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 4280 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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