O60381 (HBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1 Ref.6 Ref.7
Subunit structure	Binds the second PAH repeat of SIN3A By similarity. Binds TCF4 and RB1.
Subcellular location	Nucleus Ref.6.
Sequence similarities	Contains 1 AXH domain. Contains 1 HMG box DNA-binding domain.
Sequence caution	The sequence BAB85059.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Wnt signaling pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Repressor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW cell cycle arrest Non-traceable author statement PubMed 9030690. Source: UniProtKB positive regulation of potassium ion transport Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O60381-1)

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: O60381-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: O60381-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 514

514

HMG box-containing protein 1

PRO_0000048546

Regions

Domain

203 – 345

143

AXH

DNA binding

434 – 502

69

HMG box

Compositional bias

156 – 161

6

Poly-Ser

Compositional bias

197 – 200

4

Poly-Asp

Natural variations

Alternative sequence

463 – 514

52

Missing in isoform 2.

VSP_014655

Alternative sequence

510 – 514

5

GSQQH → VCFNK in isoform 3.

VSP_014656

Experimental info

Sequence conflict

127

1

Q → L in AAH22329. Ref.5

Sequence conflict

348

1

S → P in AAH22329. Ref.5

Secondary structure

1

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514

Helix Strand Turn

Details...

Beta strand

220 – 227

8

Helix

234 – 240

7

Turn

253 – 260

8

Beta strand

262 – 272

11

Beta strand

275 – 283

9

Helix

287 – 289

3

Beta strand

292 – 297

6

Beta strand

301 – 304

4

Turn

305 – 307

3

Beta strand

308 – 313

6

Helix

314 – 321

8

Helix

440 – 447

8

Helix

449 – 455

7

Helix

461 – 474

14

Helix

477 – 497

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 19, 2005. Version 2. Checksum: 2AFADC995F73A031	FASTA	514	57,645
	10 20 30 40 50 60 MVWEVKTNQM PNAVQKLLLV MDKRASGMND SLELLQCNEN LPSSPGYNSC DEHMELDDLP 70 80 90 100 110 120 ELQAVQSDPT QSGMYQLSSD VSHQEYPRSS WNQNTSDIPE TTYRENEVDW LTELANIATS 130 140 150 160 170 180 PQSPLMQCSF YNRSSPVHII ATSKSLHSYA RPPPVSSSSK SEPAFPHHHW KEETPVRHER 190 200 210 220 230 240 ANSESESGIF CMSSLSDDDD LGWCNSWPST VWHCFLKGTR LCFHKGSNKE WQDVEDFARA 250 260 270 280 290 300 EGCDNEEDLQ MGIHKGYGSD GLKLLSHEES VSFGESVLKL TFDPGTVEDG LLTVECKLDH 310 320 330 340 350 360 PFYVKNKGWS SFYPSLTVVQ HGIPCCEVHI GDVCLPPGHP DAINFDDSGV FDTFKSYDFT 370 380 390 400 410 420 PMDSSAVYVL SSMARQRRAS LSCGGPGGQD FARSGFSKNC GSPGSSQLSS NSLYAKAVKN 430 440 450 460 470 480 HSSGTVSATS PNKCKRPMNA FMLFAKKYRV EYTQMYPGKD NRAISVILGD RWKKMKNEER 490 500 510 RMYTLEAKAL AEEQKRLNPD CWKRKRTNSG SQQH
	Isoform 2 [UniParc]. Checksum: F2972041A89482BC	FASTA	462	51,433
	10 20 30 40 50 60 MVWEVKTNQM PNAVQKLLLV MDKRASGMND SLELLQCNEN LPSSPGYNSC DEHMELDDLP 70 80 90 100 110 120 ELQAVQSDPT QSGMYQLSSD VSHQEYPRSS WNQNTSDIPE TTYRENEVDW LTELANIATS 130 140 150 160 170 180 PQSPLMQCSF YNRSSPVHII ATSKSLHSYA RPPPVSSSSK SEPAFPHHHW KEETPVRHER 190 200 210 220 230 240 ANSESESGIF CMSSLSDDDD LGWCNSWPST VWHCFLKGTR LCFHKGSNKE WQDVEDFARA 250 260 270 280 290 300 EGCDNEEDLQ MGIHKGYGSD GLKLLSHEES VSFGESVLKL TFDPGTVEDG LLTVECKLDH 310 320 330 340 350 360 PFYVKNKGWS SFYPSLTVVQ HGIPCCEVHI GDVCLPPGHP DAINFDDSGV FDTFKSYDFT 370 380 390 400 410 420 PMDSSAVYVL SSMARQRRAS LSCGGPGGQD FARSGFSKNC GSPGSSQLSS NSLYAKAVKN 430 440 450 460 HSSGTVSATS PNKCKRPMNA FMLFAKKYRV EYTQMYPGKD NR
	Isoform 3 [UniParc]. Checksum: 2838539245C3A031	FASTA	514	57,699
	10 20 30 40 50 60 MVWEVKTNQM PNAVQKLLLV MDKRASGMND SLELLQCNEN LPSSPGYNSC DEHMELDDLP 70 80 90 100 110 120 ELQAVQSDPT QSGMYQLSSD VSHQEYPRSS WNQNTSDIPE TTYRENEVDW LTELANIATS 130 140 150 160 170 180 PQSPLMQCSF YNRSSPVHII ATSKSLHSYA RPPPVSSSSK SEPAFPHHHW KEETPVRHER 190 200 210 220 230 240 ANSESESGIF CMSSLSDDDD LGWCNSWPST VWHCFLKGTR LCFHKGSNKE WQDVEDFARA 250 260 270 280 290 300 EGCDNEEDLQ MGIHKGYGSD GLKLLSHEES VSFGESVLKL TFDPGTVEDG LLTVECKLDH 310 320 330 340 350 360 PFYVKNKGWS SFYPSLTVVQ HGIPCCEVHI GDVCLPPGHP DAINFDDSGV FDTFKSYDFT 370 380 390 400 410 420 PMDSSAVYVL SSMARQRRAS LSCGGPGGQD FARSGFSKNC GSPGSSQLSS NSLYAKAVKN 430 440 450 460 470 480 HSSGTVSATS PNKCKRPMNA FMLFAKKYRV EYTQMYPGKD NRAISVILGD RWKKMKNEER 490 500 510 RMYTLEAKAL AEEQKRLNPD CWKRKRTNSV CFNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"Human HMG box transcription factor HBP1: a role in hCD2 LCR function." Zhuma T., Tyrrell R., Sekkali B., Skavdis G., Saveliev A., Tolaini M., Roderick K., Norton T., Smerdon S., Sedgwick S., Festenstein R., Kioussis D. EMBO J. 18:6396-6406(1999) [PubMed] [Europe PMC] [Abstract] 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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00099615.
IPI00550468.
IPI00607765.

RefSeq

NP_001231191.1. NM_001244262.1.
NP_036389.2. NM_012257.3.

UniGene

Hs.162032.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E6O	NMR	-	A	424-503	[»]
3QVE	X-ray	2.04	A/B/C	206-342	[»]

ProteinModelPortal

O60381.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60381. 5 interactions.

MINT

MINT-1185770.

STRING

9606.ENSP00000222574.

PTM databases

PhosphoSite

O60381.

Proteomic databases

PaxDb

O60381.

PRIDE

O60381.

Protocols and materials databases

DNASU

26959.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000222574; ENSP00000222574; ENSG00000105856.
ENST00000468410; ENSP00000420500; ENSG00000105856.
ENST00000485846; ENSP00000418738; ENSG00000105856.

GeneID

26959.

KEGG

hsa:26959.

UCSC

uc003vdy.3. human.
uc003veb.1. human.

Organism-specific databases

CTD

26959.

GeneCards

GC07P106809.

HGNC

HGNC:23200. HBP1.

HPA

CAB032824.
HPA020225.

neXtProt

NX_O60381.

PharmGKB

PA134901346.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG149693.

HOVERGEN

HBG052810.

InParanoid

O60381.

OMA

CCEIHIG.

OrthoDB

EOG4KKZ36.

PhylomeDB

O60381.

Enzyme and pathway databases

Pathway_Interaction_DB

p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Gene expression databases

ArrayExpress

O60381.

Bgee

O60381.

CleanEx

HS_HBP1.

Genevestigator

O60381.

GermOnline

ENSG00000105856. Homo sapiens.

Family and domain databases

Gene3D

1.10.30.10. 1 hit.

InterPro

IPR013723. Ataxin-1_HBP1.
IPR003652. Ataxin_AXH_dom.
IPR009071. HMG_box_dom.
[Graphical view]

Pfam

PF08517. AXH. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]

SMART

SM00536. AXH. 1 hit.
SM00398. HMG. 1 hit.
[Graphical view]

SUPFAM

SSF102031. Ataxin-1_HBP1. 1 hit.
SSF47095. HMG-box. 1 hit.

PROSITE

PS51148. AXH. 1 hit.
PS50118. HMG_BOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HBP1. human.

EvolutionaryTrace

O60381.

GenomeRNAi

26959.

NextBio

49416.

Entry information

Entry name

HBP1_HUMAN

Accession

Primary (citable) accession number: O60381
Secondary accession number(s): B3KVB7 , Q8TBM1, Q8TE93, Q96AJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.