HMGA1

High mobility group AT-hook 1
Identifiers
Symbols	HMGA1; HMG-R; HMGA1A; HMGIY; MGC12816; MGC4242; MGC4854
External IDs	OMIM: 600701 MGI: 96160 HomoloGene: 32332 GeneCards: HMGA1 Gene
Gene Ontology Molecular function • DNA binding • AT DNA binding • sequence-specific DNA binding transcription factor activity • protein binding • transcription factor binding • enzyme binding • ligand-dependent nuclear receptor transcription coactivator activity • retinoic acid receptor binding • peroxisome proliferator activated receptor binding • retinoid X receptor binding Cellular component • chromatin • nucleus • nucleoplasm • transcription factor complex • chromosome • cytosol • cytosol Biological process • DNA unwinding involved in replication • nucleosome disassembly • loss of chromatin silencing • transcription, DNA-dependent • regulation of transcription, DNA-dependent • protein complex assembly • viral reproduction • provirus integration • provirus integration • initiation of viral infection • interspecies interaction between organisms • positive regulation of transcription, DNA-dependent Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3159	15361
Ensembl	ENSG00000137309	ENSMUSG00000046711
UniProt	P17096	Q3TE85
RefSeq (mRNA)	NM_002131.3	NM_001025427
RefSeq (protein)	NP_002122.1	NP_001020598
Location (UCSC)	Chr 6: 34.31 – 34.32 Mb	Chr 17: 27.28 – 27.29 Mb
PubMed search	[1]	[2]

High-mobility group protein HMG-I/HMG-Y is a protein that in humans is encoded by the HMGA1 gene.

This gene encodes a non-histone chromatin protein involved in many cellular processes, including regulation of inducible gene transcription, integration of retroviruses into chromosomes, and the metastatic progression of cancer cells. The encoded protein preferentially binds to the minor groove of A+T-rich regions in double-stranded DNA. It has little secondary structure in solution but assumes distinct conformations when bound to substrates such as DNA or other proteins. The encoded protein is frequently acetylated and is found in the nucleus. At least seven transcript variants encoding two different isoforms have been found for this gene.

Mice lacking their variant of HMGA1, i.e., Hmga1-/- mice, are diabetic and express low levels of the insulin receptor.

Interactions

HMGA1 has been shown to interact with CEBPB and Sp1 transcription factor.

See also

• HMGA
• AT-hook

Further reading

• Hui H, Perfetti R (2002). "Pancreas duodenum homeobox-1 regulates pancreas development during embryogenesis and islet cell function in adulthood.". Eur. J. Endocrinol. 146 (2): 129–41. doi:10.1530/eje.0.1460129. PMID 11834421. 
• Van Maele B, Debyser Z (2005). "HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins.". AIDS reviews 7 (1): 26–43. PMID 15875659. 
• Van Maele B, Busschots K, Vandekerckhove L, et al. (2006). "Cellular co-factors of HIV-1 integration.". Trends Biochem. Sci. 31 (2): 98–105. doi:10.1016/j.tibs.2005.12.002. PMID 16403635. 
• Reeves R, Nissen MS (1990). "The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure.". J. Biol. Chem. 265 (15): 8573–82. PMID 1692833. 
• Nissen MS, Langan TA, Reeves R (1991). "Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group I nonhistone chromatin protein.". J. Biol. Chem. 266 (30): 19945–52. PMID 1939057. 
• Eckner R, Birnstiel ML (1989). "Cloning of cDNAs coding for human HMG I and HMG Y proteins: both are capable of binding to the octamer sequence motif.". Nucleic Acids Res. 17 (15): 5947–59. doi:10.1093/nar/17.15.5947. PMC 318252. PMID 2505228. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=318252. 
• Johnson KR, Lehn DA, Reeves R (1989). "Alternative processing of mRNAs encoding mammalian chromosomal high-mobility-group proteins HMG-I and HMG-Y.". Mol. Cell. Biol. 9 (5): 2114–23. PMC 363005. PMID 2701943. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=363005. 
• Palvimo J, Linnala-Kankkunen A (1989). "Identification of sites on chromosomal protein HMG-I phosphorylated by casein kinase II.". FEBS Lett. 257 (1): 101–4. doi:10.1016/0014-5793(89)81796-X. PMID 2806554. 
• Karlson JR, Mørk E, Holtlund J, et al. (1989). "The amino acid sequence of the chromosomal protein HMG-Y, its relation to HMG-I and possible domains for the preferential binding of the proteins to stretches of A-T base pairs.". Biochem. Biophys. Res. Commun. 158 (3): 646–51. doi:10.1016/0006-291X(89)92770-8. PMID 2920035. 
• Lund T, Dahl KH, Mørk E, et al. (1987). "The human chromosomal protein HMG I contains two identical palindrome amino acid sequences.". Biochem. Biophys. Res. Commun. 146 (2): 725–30. doi:10.1016/0006-291X(87)90589-4. PMID 3619901. 
• Leger H, Sock E, Renner K, et al. (1995). "Functional interaction between the POU domain protein Tst-1/Oct-6 and the high-mobility-group protein HMG-I/Y.". Mol. Cell. Biol. 15 (7): 3738–47. PMC 230612. PMID 7791781. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230612. 
• John S, Reeves RB, Lin JX, et al. (1995). "Regulation of cell-type-specific interleukin-2 receptor alpha-chain gene expression: potential role of physical interactions between Elf-1, HMG-I(Y), and NF-kappa B family proteins.". Mol. Cell. Biol. 15 (3): 1786–96. PMC 230403. PMID 7862168. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230403. 
• Farnet CM, Bushman FD (1997). "HIV-1 cDNA integration: requirement of HMG I(Y) protein for function of preintegration complexes in vitro.". Cell 88 (4): 483–92. doi:10.1016/S0092-8674(00)81888-7. PMID 9038339. 
• Miller MD, Farnet CM, Bushman FD (1997). "Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition.". J. Virol. 71 (7): 5382–90. PMC 191777. PMID 9188609. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=191777. 
• Huth JR, Bewley CA, Nissen MS, et al. (1997). "The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif.". Nat. Struct. Biol. 4 (8): 657–65. doi:10.1038/nsb0897-657. PMID 9253416. 
• Currie RA (1998). "Functional interaction between the DNA binding subunit trimerization domain of NF-Y and the high mobility group protein HMG-I(Y).". J. Biol. Chem. 272 (49): 30880–8. doi:10.1074/jbc.272.49.30880. PMID 9388234. 
• Chin MT, Pellacani A, Wang H, et al. (1998). "Enhancement of serum-response factor-dependent transcription and DNA binding by the architectural transcription factor HMG-I(Y).". J. Biol. Chem. 273 (16): 9755–60. doi:10.1074/jbc.273.16.9755. PMID 9545312. 
• Chiappetta G, Tallini G, De Biasio MC, et al. (1998). "Detection of high mobility group I HMGI(Y) protein in the diagnosis of thyroid tumors: HMGI(Y) expression represents a potential diagnostic indicator of carcinoma.". Cancer Res. 58 (18): 4193–8. PMID 9751634. 

External links

• MeSH HMGA1+protein,+human

This article incorporates text from the United States National Library of Medicine, which is in the public domain.