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Protein

High mobility group protein 1

Gene

HMO1

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 is probably part of the rDNA transcription apparatus. Acts synergetically with the RPA49 subunit of RNA polymerase I during rDNA transcription. May participate in mutagenesis control.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi106 – 17974HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding, bending Source: SGD
  • double-stranded DNA binding Source: SGD
  • four-way junction DNA binding Source: SGD

GO - Biological processi

  • DNA packaging Source: SGD
  • dsDNA loop formation Source: SGD
  • regulation of ribosomal protein gene transcription from RNA polymerase II promoter Source: SGD
  • regulation of transcription from RNA polymerase I promoter Source: SGD
  • transcriptional start site selection at RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29763-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
High mobility group protein 1
Alternative name(s):
High spontaneous mutagenesis protein 2
Gene namesi
Name:HMO1
Synonyms:HSM2
Ordered Locus Names:YDR174W
ORF Names:YD9395.07
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR174W.
SGDiS000002581. HMO1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytosol Source: SGD
  • nucleolus Source: SGD
  • nucleus Source: SGD
  • rDNA heterochromatin Source: SGD
  • small-subunit processome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246High mobility group protein 1PRO_0000048564Add
BLAST

Proteomic databases

MaxQBiQ03973.
PeptideAtlasiQ03973.

PTM databases

iPTMnetiQ03973.

Interactioni

Subunit structurei

Interacts with FPR1. Interacts with an unidentified DNA helicase. Associates with rDNA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
C19orf57Q0VDD73EBI-33047,EBI-741210From a different organism.
CRN1Q064402EBI-33047,EBI-4950
EGD2P388792EBI-33047,EBI-6379
ELG1Q120502EBI-33047,EBI-32195
ENP1P383332EBI-33047,EBI-6482
EPL1P435722EBI-33047,EBI-22792
GCN2P154422EBI-33047,EBI-330
HCA4P204484EBI-33047,EBI-5612
HHF2P023093EBI-33047,EBI-8113
HHT2P618303EBI-33047,EBI-8098
HTA2P049124EBI-33047,EBI-8076
IFA38P382862EBI-33047,EBI-20857
IOC4Q042133EBI-33047,EBI-28077
LYS20P485704EBI-33047,EBI-8502
MSS51P323352EBI-33047,EBI-11318
NHP2P324953EBI-33047,EBI-12014
ORC6P388262EBI-33047,EBI-12588
RFA1P223364EBI-33047,EBI-14971
RFC1P386302EBI-33047,EBI-14985
RRP5Q050222EBI-33047,EBI-16011
SDO1Q079532EBI-33047,EBI-27124
SEC28P405092EBI-33047,EBI-4884
SGV1P232932EBI-33047,EBI-17078
SSB1P114843EBI-33047,EBI-8627
UTP22P532545EBI-33047,EBI-1878
YCR043CP253612EBI-33047,EBI-21909
YLR455WQ061883EBI-33047,EBI-35613
YRA1Q121593EBI-33047,EBI-29516

Protein-protein interaction databases

BioGridi32227. 291 interactions.
DIPiDIP-1687N.
IntActiQ03973. 111 interactions.
MINTiMINT-8285186.

Structurei

3D structure databases

ProteinModelPortaliQ03973.
SMRiQ03973. Positions 98-182.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi228 – 24114Poly-LysAdd
BLAST

Sequence similaritiesi

Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000001040.
InParanoidiQ03973.
OMAiPLTMYFA.
OrthoDBiEOG70KH25.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03973-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTDPSVKLK SAKDSLVSSL FELSKAANQT ASSIVDFYNA IGDDEEEKIE
60 70 80 90 100
AFTTLTESLQ TLTSGVNHLH GISSELVNPI DDDKDAIIAA PVKAVRRKIE
110 120 130 140 150
RDPNAPKKPL TVFFAYSAYV RQELREDRQK AGLPPLSSTE ITQEISKKWK
160 170 180 190 200
ELSDNEKEKW KQAYNVELEN YQREKSKYLE AKKNGTLPPA SLENGPTHAP
210 220 230 240
VPIPFSLQHA AEPPVEKRPH DDDGSSEKKK KKKKKDKKKD KSNSSI
Length:246
Mass (Da):27,544
Last modified:November 1, 1996 - v1
Checksum:i3D6DCD56A28B7D77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46727 Genomic DNA. Translation: CAA86679.1.
AY557680 Genomic DNA. Translation: AAS56006.1.
BK006938 Genomic DNA. Translation: DAA12016.1.
PIRiS49770.
RefSeqiNP_010459.1. NM_001180481.1.

Genome annotation databases

EnsemblFungiiYDR174W; YDR174W; YDR174W.
GeneIDi851754.
KEGGisce:YDR174W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46727 Genomic DNA. Translation: CAA86679.1.
AY557680 Genomic DNA. Translation: AAS56006.1.
BK006938 Genomic DNA. Translation: DAA12016.1.
PIRiS49770.
RefSeqiNP_010459.1. NM_001180481.1.

3D structure databases

ProteinModelPortaliQ03973.
SMRiQ03973. Positions 98-182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32227. 291 interactions.
DIPiDIP-1687N.
IntActiQ03973. 111 interactions.
MINTiMINT-8285186.

PTM databases

iPTMnetiQ03973.

Proteomic databases

MaxQBiQ03973.
PeptideAtlasiQ03973.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR174W; YDR174W; YDR174W.
GeneIDi851754.
KEGGisce:YDR174W.

Organism-specific databases

EuPathDBiFungiDB:YDR174W.
SGDiS000002581. HMO1.

Phylogenomic databases

HOGENOMiHOG000001040.
InParanoidiQ03973.
OMAiPLTMYFA.
OrthoDBiEOG70KH25.

Enzyme and pathway databases

BioCyciYEAST:G3O-29763-MONOMER.

Miscellaneous databases

NextBioi969516.
PROiQ03973.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Characterization of a high mobility group 1/2 homolog in yeast."
    Lu J., Kobayashi R., Brill S.J.
    J. Biol. Chem. 271:33678-33685(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 14-25; 51-84 AND 163-175, SUBCELLULAR LOCATION, DNA-BINDING.
  5. "Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase."
    Dolinski K.J., Heitman J.
    Genetics 151:935-944(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FPR1.
  6. "HSM2 (HMO1) gene participates in mutagenesis control in yeast Saccharomyces cerevisiae."
    Alekseev S.Y., Kovaltsova S.V., Fedorova I.V., Gracheva L.M., Evstukhina T.A., Peshekhonov V.T., Korolev V.G.
    DNA Repair 1:287-297(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Hmo1, an HMG-box protein, belongs to the yeast ribosomal DNA transcription system."
    Gadal O., Labarre S., Boschiero C., Thuriaux P.
    EMBO J. 21:5498-5507(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHMO1_YEAST
AccessioniPrimary (citable) accession number: Q03973
Secondary accession number(s): D6VSF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 137 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 19000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. 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.