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Protein

HMG box-containing protein 1

Gene

HBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 TCF4.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi434 – 50269HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. RNA binding Source: InterPro

GO - Biological processi

  1. cell cycle arrest Source: UniProtKB
  2. positive regulation of potassium ion transport Source: Ensembl
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
  5. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
HMG box-containing protein 1
Alternative name(s):
HMG box transcription factor 1
High mobility group box transcription factor 1
Gene namesi
Name:HBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:23200. HBP1.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134901346.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 514514HMG box-containing protein 1PRO_0000048546Add
BLAST

Proteomic databases

MaxQBiO60381.
PaxDbiO60381.
PRIDEiO60381.

PTM databases

PhosphoSiteiO60381.

Expressioni

Gene expression databases

BgeeiO60381.
CleanExiHS_HBP1.
ExpressionAtlasiO60381. baseline and differential.
GenevestigatoriO60381.

Organism-specific databases

HPAiCAB032824.
HPA020225.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
RB1P064002EBI-954175,EBI-491274

Protein-protein interaction databases

BioGridi117927. 18 interactions.
IntActiO60381. 7 interactions.
MINTiMINT-1185770.
STRINGi9606.ENSP00000222574.

Structurei

Secondary structure

1
514
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi220 – 2278Combined sources
Helixi234 – 2407Combined sources
Turni253 – 2608Combined sources
Beta strandi262 – 27211Combined sources
Beta strandi275 – 2839Combined sources
Helixi287 – 2893Combined sources
Beta strandi292 – 2976Combined sources
Beta strandi301 – 3044Combined sources
Turni305 – 3073Combined sources
Beta strandi308 – 3136Combined sources
Helixi314 – 3218Combined sources
Helixi440 – 4478Combined sources
Helixi449 – 4557Combined sources
Helixi461 – 47414Combined sources
Helixi477 – 49721Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E6ONMR-A424-503[»]
3QVEX-ray2.04A/B/C206-342[»]
ProteinModelPortaliO60381.
SMRiO60381. Positions 208-345, 425-503.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60381.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini203 – 345143AXHPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi156 – 1616Poly-Ser
Compositional biasi197 – 2004Poly-Asp

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG149693.
GeneTreeiENSGT00390000011239.
HOVERGENiHBG052810.
InParanoidiO60381.
OMAiPSTAWHC.
OrthoDBiEOG7VX8VK.
PhylomeDBiO60381.
TreeFamiTF105381.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR013723. Ataxin-1_HBP1.
IPR003652. Ataxin_AXH_dom.
IPR009071. HMG_box_dom.
[Graphical view]
PfamiPF08517. AXH. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00536. AXH. 1 hit.
SM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF102031. SSF102031. 1 hit.
SSF47095. SSF47095. 1 hit.
PROSITEiPS51148. AXH. 1 hit.
PS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O60381-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVWEVKTNQM PNAVQKLLLV MDKRASGMND SLELLQCNEN LPSSPGYNSC
60 70 80 90 100
DEHMELDDLP ELQAVQSDPT QSGMYQLSSD VSHQEYPRSS WNQNTSDIPE
110 120 130 140 150
TTYRENEVDW LTELANIATS PQSPLMQCSF YNRSSPVHII ATSKSLHSYA
160 170 180 190 200
RPPPVSSSSK SEPAFPHHHW KEETPVRHER ANSESESGIF CMSSLSDDDD
210 220 230 240 250
LGWCNSWPST VWHCFLKGTR LCFHKGSNKE WQDVEDFARA EGCDNEEDLQ
260 270 280 290 300
MGIHKGYGSD GLKLLSHEES VSFGESVLKL TFDPGTVEDG LLTVECKLDH
310 320 330 340 350
PFYVKNKGWS SFYPSLTVVQ HGIPCCEVHI GDVCLPPGHP DAINFDDSGV
360 370 380 390 400
FDTFKSYDFT PMDSSAVYVL SSMARQRRAS LSCGGPGGQD FARSGFSKNC
410 420 430 440 450
GSPGSSQLSS NSLYAKAVKN HSSGTVSATS PNKCKRPMNA FMLFAKKYRV
460 470 480 490 500
EYTQMYPGKD NRAISVILGD RWKKMKNEER RMYTLEAKAL AEEQKRLNPD
510
CWKRKRTNSG SQQH
Length:514
Mass (Da):57,645
Last modified:July 19, 2005 - v2
Checksum:i2AFADC995F73A031
GO
Isoform 2 (identifier: O60381-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     463-514: Missing.

Note: No experimental confirmation available.

Show »
Length:462
Mass (Da):51,433
Checksum:iF2972041A89482BC
GO
Isoform 3 (identifier: O60381-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     510-514: GSQQH → VCFNK

Show »
Length:514
Mass (Da):57,699
Checksum:i2838539245C3A031
GO

Sequence cautioni

The sequence BAB85059.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1271Q → L in AAH22329 (PubMed:15489334).Curated
Sequence conflicti348 – 3481S → P in AAH22329 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei463 – 51452Missing in isoform 2. 1 PublicationVSP_014655Add
BLAST
Alternative sequencei510 – 5145GSQQH → VCFNK in isoform 3. 1 PublicationVSP_014656

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182038 mRNA. Translation: AAD56225.1.
AK074353 mRNA. Translation: BAB85059.1. Different initiation.
AK122785 mRNA. Translation: BAG53729.1.
AC004492 Genomic DNA. Translation: AAC08317.1.
CH471070 Genomic DNA. Translation: EAW83392.1.
BC017069 mRNA. Translation: AAH17069.1.
BC022329 mRNA. Translation: AAH22329.1.
CCDSiCCDS5741.1. [O60381-1]
RefSeqiNP_001231191.1. NM_001244262.1.
NP_036389.2. NM_012257.3. [O60381-1]
XP_005250323.1. XM_005250266.2. [O60381-1]
XP_005250324.1. XM_005250267.2. [O60381-1]
UniGeneiHs.162032.

Genome annotation databases

EnsembliENST00000222574; ENSP00000222574; ENSG00000105856. [O60381-1]
ENST00000468410; ENSP00000420500; ENSG00000105856. [O60381-1]
ENST00000485846; ENSP00000418738; ENSG00000105856. [O60381-1]
GeneIDi26959.
KEGGihsa:26959.
UCSCiuc003vdy.3. human. [O60381-1]
uc003veb.1. human. [O60381-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182038 mRNA. Translation: AAD56225.1.
AK074353 mRNA. Translation: BAB85059.1. Different initiation.
AK122785 mRNA. Translation: BAG53729.1.
AC004492 Genomic DNA. Translation: AAC08317.1.
CH471070 Genomic DNA. Translation: EAW83392.1.
BC017069 mRNA. Translation: AAH17069.1.
BC022329 mRNA. Translation: AAH22329.1.
CCDSiCCDS5741.1. [O60381-1]
RefSeqiNP_001231191.1. NM_001244262.1.
NP_036389.2. NM_012257.3. [O60381-1]
XP_005250323.1. XM_005250266.2. [O60381-1]
XP_005250324.1. XM_005250267.2. [O60381-1]
UniGeneiHs.162032.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E6ONMR-A424-503[»]
3QVEX-ray2.04A/B/C206-342[»]
ProteinModelPortaliO60381.
SMRiO60381. Positions 208-345, 425-503.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117927. 18 interactions.
IntActiO60381. 7 interactions.
MINTiMINT-1185770.
STRINGi9606.ENSP00000222574.

PTM databases

PhosphoSiteiO60381.

Proteomic databases

MaxQBiO60381.
PaxDbiO60381.
PRIDEiO60381.

Protocols and materials databases

DNASUi26959.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000222574; ENSP00000222574; ENSG00000105856. [O60381-1]
ENST00000468410; ENSP00000420500; ENSG00000105856. [O60381-1]
ENST00000485846; ENSP00000418738; ENSG00000105856. [O60381-1]
GeneIDi26959.
KEGGihsa:26959.
UCSCiuc003vdy.3. human. [O60381-1]
uc003veb.1. human. [O60381-3]

Organism-specific databases

CTDi26959.
GeneCardsiGC07P106809.
HGNCiHGNC:23200. HBP1.
HPAiCAB032824.
HPA020225.
neXtProtiNX_O60381.
PharmGKBiPA134901346.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG149693.
GeneTreeiENSGT00390000011239.
HOVERGENiHBG052810.
InParanoidiO60381.
OMAiPSTAWHC.
OrthoDBiEOG7VX8VK.
PhylomeDBiO60381.
TreeFamiTF105381.

Miscellaneous databases

ChiTaRSiHBP1. human.
EvolutionaryTraceiO60381.
GeneWikiiHBP1.
GenomeRNAii26959.
NextBioi49416.
PROiO60381.

Gene expression databases

BgeeiO60381.
CleanExiHS_HBP1.
ExpressionAtlasiO60381. baseline and differential.
GenevestigatoriO60381.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR013723. Ataxin-1_HBP1.
IPR003652. Ataxin_AXH_dom.
IPR009071. HMG_box_dom.
[Graphical view]
PfamiPF08517. AXH. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00536. AXH. 1 hit.
SM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF102031. SSF102031. 1 hit.
SSF47095. SSF47095. 1 hit.
PROSITEiPS51148. AXH. 1 hit.
PS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Involvement of retinoblastoma protein and HBP1 in histone H1(0) gene expression."
    Lemercier C., Duncliffe K., Boibessot I., Zhang H., Verdel A., Angelov D., Khochbin S.
    Mol. Cell. Biol. 20:6627-6637(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH RB1.
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-514 (ISOFORM 2).
    Tissue: Hepatoma and Testis.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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).
    Tissue: Brain and Uterus.
  6. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Negative regulation of the Wnt-beta-catenin pathway by the transcriptional repressor HBP1."
    Sampson E.M., Haque Z.K., Ku M.-C., Tevosian S.G., Albanese C., Pestell R.G., Paulson K.E., Yee A.S.
    EMBO J. 20:4500-4511(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TCF4.
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Solution structure of the HMG box domain from human HMG-box transcription factor 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 422-503.

Entry informationi

Entry nameiHBP1_HUMAN
AccessioniPrimary (citable) accession number: O60381
Secondary accession number(s): B3KVB7
, Q8TBM1, Q8TE93, Q96AJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: March 4, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.