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Q8R316 (HBP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
HMG box-containing protein 1
Alternative name(s):
HMG box transcription factor 1
High mobility group box transcription factor 1
Gene names
Name:Hbp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length516 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor that binds to the promoter region of target genes. Plays a role in the regulation of the cell cycle and of the Wnt pathway. Binds preferentially to the sequence 5'-TTCATTCATTCA-3'. Binding to the H1F0 promoter is enhanced by interaction with RB1. Disrupts the interaction between DNA and TCF4 By similarity. Ref.3

Subunit structure

Binds TCF4 By similarity. Binds RB1. Binds the second PAH repeat of SIN3A.

Subcellular location

Nucleus Ref.5.

Sequence similarities

Contains 1 AXH domain.

Contains 1 HMG box DNA-binding domain.

Sequence caution

The sequence BAC38611.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8R316-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8R316-2)

The sequence of this isoform differs from the canonical sequence as follows:
     465-516: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 516516HMG box-containing protein 1
PRO_0000048547

Regions

Domain203 – 345143AXH
DNA binding436 – 50469HMG box
Compositional bias156 – 1616Poly-Ser
Compositional bias197 – 2004Poly-Asp
Compositional bias394 – 43239Ser-rich

Natural variations

Alternative sequence465 – 51652Missing in isoform 2.
VSP_014657

Experimental info

Mutagenesis3701L → D: Strongly reduces Sin3A binding. Ref.5
Mutagenesis3731M → D: Strongly reduces Sin3A binding. Ref.5

Secondary structure

.......................... 516
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 2DC6D40FE41543B0

FASTA51657,645
        10         20         30         40         50         60 
MVWEVKTNQM PNAVQKLLLV MDKRAPGMSD SLELLQCNEN LPSSPGYNSC DEHMELDDLP 

        70         80         90        100        110        120 
ELQAVQSDPT QSAIYQLSSD VSHQEYPRSS WSQNTSDIPE NTHREDEVDW LTELANIATS 

       130        140        150        160        170        180 
PQSPLMQCSF YNRSSPVHII ATSKSLHSYA RPPPVSSSSK SGPAFPHDHW KEETPVRHER 

       190        200        210        220        230        240 
ANSESESGIF CMSSLSDDDD LGWCNSWPST IWHCFLKGTR LCFHKESNKE WQDVEDFARA 

       250        260        270        280        290        300 
ASCDNEEEIQ MGTHKGYGSD GLKLLSHEES VSFGESVLKL TFDPGTVEDG LLTVECKLDH 

       310        320        330        340        350        360 
PFYVKNKGWS SFYPSLTVVQ HGIPCCEIHI GDVCLPPGHP DAINFDDSGV FDTFKSYDFT 

       370        380        390        400        410        420 
PMDSSAVYVL SSMARQRRAS LSCGGGPGTG QEFSGSEFSK SCGSPGSSQL SSSSLYAKAV 

       430        440        450        460        470        480 
KSHSSGTVSA TSPNKCKRPM NAFMLFAKKY RVEYTQMYPG KDNRAISVIL GDRWKKMKNE 

       490        500        510 
ERRMYTLEAK ALAEEQKRLN PDCWKRKRTN SGSQQH 

« Hide

Isoform 2 [UniParc].

Checksum: B40F04F670C60E19
Show »

FASTA46451,433

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Skin and Testis.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary tumor.
[3]"The HMG-box transcription factor HBP1 is targeted by the pocket proteins and E1A."
Lavender P., Vandel L., Bannister A.J., Kouzarides T.
Oncogene 14:2721-2728(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RB1, FUNCTION.
[4]"Assignment of the 1H, 13C, and 15N resonances of the AXH domain of the transcription factor HBP1."
de Chiara C., Kelly G., Frenkiel T.A., Pastore A.
J. Biomol. NMR 28:411-412(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 208-345.
[5]"HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations."
Swanson K.A., Knoepfler P.S., Huang K., Kang R.S., Cowley S.M., Laherty C.D., Eisenman R.N., Radhakrishnan I.
Nat. Struct. Mol. Biol. 11:738-746(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 233-255, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-370 AND MET-373, INTERACTION WITH SIN3A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC026853 mRNA. Translation: AAH26853.1.
AK028674 mRNA. Translation: BAC26060.1.
AK082770 mRNA. Translation: BAC38611.1. Different initiation.
AK133127 mRNA. Translation: BAE21520.1.
RefSeqNP_694878.2. NM_153198.2.
NP_818774.2. NM_177993.3.
UniGeneMm.390461.
Mm.458534.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5RNMR-A358-380[»]
1V06NMR-A208-345[»]
ProteinModelPortalQ8R316.
SMRQ8R316. Positions 208-345, 427-505.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8R316.

Proteomic databases

PRIDEQ8R316.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID73389.
KEGGmmu:73389.

Organism-specific databases

CTD26959.
MGIMGI:894659. Hbp1.

Phylogenomic databases

eggNOGNOG149693.
HOGENOMHOG000065753.
HOVERGENHBG052810.
InParanoidQ8R316.
PhylomeDBQ8R316.

Gene expression databases

ArrayExpressQ8R316.
BgeeQ8R316.
CleanExMM_HBP1.
GenevestigatorQ8R316.

Family and domain databases

Gene3D1.10.30.10. 1 hit.
InterProIPR013723. Ataxin-1_HBP1.
IPR003652. Ataxin_AXH_dom.
IPR009071. HMG_box_dom.
[Graphical view]
PfamPF08517. AXH. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]
SMARTSM00536. AXH. 1 hit.
SM00398. HMG. 1 hit.
[Graphical view]
SUPFAMSSF102031. SSF102031. 1 hit.
SSF47095. SSF47095. 1 hit.
PROSITEPS51148. AXH. 1 hit.
PS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8R316.
NextBio338141.
PROQ8R316.
SOURCESearch...

Entry information

Entry nameHBP1_MOUSE
AccessionPrimary (citable) accession number: Q8R316
Secondary accession number(s): Q3V0I4, Q8BUS3, Q8C199
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: June 1, 2002
Last modified: June 11, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot