HMGA1: Difference between revisions

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Latest revision as of 00:22, 27 October 2017

High-mobility group protein HMG-I/HMG-Y is a protein that in humans is encoded by the HMGA1 gene.^[1]^[2]

Function

This gene encodes a non-histone chromatin protein involved in many cellular processes, including regulation of inducible gene transcription, DNA replication, heterochromatin organization, integration of retroviruses into chromosomes, and the metastatic progression of cancer cells.

HMGA1 proteins are quite small (~10-12 kDa) and basic molecules, and consist of three AT-hooks with the RGRP (Arg-Gly-Arg-Pro) core motif, a novel cross-linking domain located between the second and third AT-hook, and a C-terminal acidic tail characteristic for the HMG family comprising HMGA, HMGB and HMGN proteins.

HMGA1-GFP fusion proteins are highly dynamic in vivo (determined using FRAP analysis), but in contrast also show nanomolar affinity to AT-rich DNA in vitro (determined biochemically), which might be explained due to the extensive post-transcriptional modifications in vivo. HMGA1 preferentially binds to the minor groove of AT-rich regions in double-stranded DNA using its AT-hooks. It has little secondary structure in solution but assumes distinct conformations when bound to substrates such as DNA or other proteins. HMGA1 proteins have high amounts of diverse posttranslational modifications and are located mainly in the nucleus, especially in heterochromatin, but also in mitochondria and the cytoplasm.

Recently it has been shown that HMGA1 proteins, HMGA1a and HMGA1b, can cross-link DNA fibers in vitro and can induce chromatin clustering in vivo suggesting a structural role of HMGA1 proteins in heterochromatin organization.^[3]

At least seven transcript variants encoding two different isoforms (HMGA1a, HMGA1b) have been found for this gene.^[4] The splice variant HMGA1c with only two AT hooks and no acidic tail is in discussion to be a real member of the HMGA family.

Mice lacking their variant of HMGA1, i.e., Hmga1-/- mice, are diabetic, show a cardiac hypertrophy and express low levels of the insulin receptor.^[5]

Interactions

HMGA1 has been shown to interact with CEBPB^[6] and Sp1 transcription factor.^[6]

References

↑ Friedmann M, Holth LT, Zoghbi HY, Reeves R (Sep 1993). "Organization, inducible-expression and chromosome localization of the human HMG-I(Y) nonhistone protein gene". Nucleic Acids Research. 21 (18): 4259–67. doi:10.1093/nar/21.18.4259. PMC 310059. PMID 8414980.
↑ Reeves R, Beckerbauer L (May 2001). "HMGI/Y proteins: flexible regulators of transcription and chromatin structure". Biochimica et Biophysica Acta. 1519 (1–2): 13–29. doi:10.1016/S0167-4781(01)00215-9. PMID 11406267.
↑ Vogel B, Löschberger A, Sauer M, Hock R (Sep 2011). "Cross-linking of DNA through HMGA1 suggests a DNA scaffold". Nucleic Acids Research. 39 (16): 7124–33. doi:10.1093/nar/gkr396. PMC 3167630. PMID 21596776.
↑ "Entrez Gene: HMGA1 high mobility group AT-hook 1".
↑ Semple RK (2009). "From bending DNA to diabetes: the curious case of HMGA1". Journal of Biology. 8 (7): 64. doi:10.1186/jbiol164. PMC 2736670. PMID 19664187.
↑ ^6.0 ^6.1 Foti D, Iuliano R, Chiefari E, Brunetti A (Apr 2003). "A nucleoprotein complex containing Sp1, C/EBP beta, and HMGI-Y controls human insulin receptor gene transcription". Molecular and Cellular Biology. 23 (8): 2720–32. doi:10.1128/MCB.23.8.2720-2732.2003. PMC 152545. PMID 12665574.

Hui H, Perfetti R (Feb 2002). "Pancreas duodenum homeobox-1 regulates pancreas development during embryogenesis and islet cell function in adulthood". European Journal of Endocrinology / European Federation of Endocrine Societies. 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, Christ F, Debyser Z (Feb 2006). "Cellular co-factors of HIV-1 integration". Trends in Biochemical Sciences. 31 (2): 98–105. doi:10.1016/j.tibs.2005.12.002. PMID 16403635.
Reeves R, Nissen MS (May 1990). "The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure". The Journal of Biological Chemistry. 265 (15): 8573–82. PMID 1692833.
Nissen MS, Langan TA, Reeves R (Oct 1991). "Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group I nonhistone chromatin protein". The Journal of Biological Chemistry. 266 (30): 19945–52. PMID 1939057.
Eckner R, Birnstiel ML (Aug 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 Research. 17 (15): 5947–59. doi:10.1093/nar/17.15.5947. PMC 318252. PMID 2505228.
Johnson KR, Lehn DA, Reeves R (May 1989). "Alternative processing of mRNAs encoding mammalian chromosomal high-mobility-group proteins HMG-I and HMG-Y". Molecular and Cellular Biology. 9 (5): 2114–23. doi:10.1128/mcb.9.5.2114. PMC 363005. PMID 2701943.
Palvimo J, Linnala-Kankkunen A (Oct 1989). "Identification of sites on chromosomal protein HMG-I phosphorylated by casein kinase II". FEBS Letters. 257 (1): 101–4. doi:10.1016/0014-5793(89)81796-X. PMID 2806554.
Karlson JR, Mørk E, Holtlund J, Laland SG, Lund T (Feb 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". Biochemical and Biophysical Research Communications. 158 (3): 646–51. doi:10.1016/0006-291X(89)92770-8. PMID 2920035.
Lund T, Dahl KH, Mørk E, Holtlund J, Laland SG (Jul 1987). "The human chromosomal protein HMG I contains two identical palindrome amino acid sequences". Biochemical and Biophysical Research Communications. 146 (2): 725–30. doi:10.1016/0006-291X(87)90589-4. PMID 3619901.
Leger H, Sock E, Renner K, Grummt F, Wegner M (Jul 1995). "Functional interaction between the POU domain protein Tst-1/Oct-6 and the high-mobility-group protein HMG-I/Y". Molecular and Cellular Biology. 15 (7): 3738–47. doi:10.1128/mcb.15.7.3738. PMC 230612. PMID 7791781.
John S, Reeves RB, Lin JX, Child R, Leiden JM, Thompson CB, Leonard WJ (Mar 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". Molecular and Cellular Biology. 15 (3): 1786–96. doi:10.1128/mcb.15.3.1786. PMC 230403. PMID 7862168.
Farnet CM, Bushman FD (Feb 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 (Jul 1997). "Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition". Journal of Virology. 71 (7): 5382–90. PMC 191777. PMID 9188609.
Huth JR, Bewley CA, Nissen MS, Evans JN, Reeves R, Gronenborn AM, Clore GM (Aug 1997). "The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif". Nature Structural Biology. 4 (8): 657–65. doi:10.1038/nsb0897-657. PMID 9253416.
Currie RA (Dec 1997). "Functional interaction between the DNA binding subunit trimerization domain of NF-Y and the high mobility group protein HMG-I(Y)". The Journal of Biological Chemistry. 272 (49): 30880–8. doi:10.1074/jbc.272.49.30880. PMID 9388234.
Chin MT, Pellacani A, Wang H, Lin SS, Jain MK, Perrella MA, Lee ME (Apr 1998). "Enhancement of serum-response factor-dependent transcription and DNA binding by the architectural transcription factor HMG-I(Y)". The Journal of Biological Chemistry. 273 (16): 9755–60. doi:10.1074/jbc.273.16.9755. PMID 9545312.
Chiappetta G, Tallini G, De Biasio MC, Manfioletti G, Martinez-Tello FJ, Pentimalli F, de Nigris F, Mastro A, Botti G, Fedele M, Berger N, Santoro M, Giancotti V, Fusco A (Sep 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 Research. 58 (18): 4193–8. PMID 9751634.
Vogel B, Löschberger A, Sauer M, Hock R (Sep 2011). "Cross-linking of DNA through HMGA1 suggests a DNA scaffold". Nucleic Acids Research. 39 (16): 7124–33. doi:10.1093/nar/gkr396. PMC 3167630. PMID 21596776.

External links

HMGA1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

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

[pmid8414980-1] Friedmann M, Holth LT, Zoghbi HY, Reeves R (Sep 1993). "Organization, inducible-expression and chromosome localization of the human HMG-I(Y) nonhistone protein gene". Nucleic Acids Research. 21 (18): 4259–67. doi:10.1093/nar/21.18.4259. PMC 310059. PMID 8414980.

[pmid11406267-2] Reeves R, Beckerbauer L (May 2001). "HMGI/Y proteins: flexible regulators of transcription and chromatin structure". Biochimica et Biophysica Acta. 1519 (1–2): 13–29. doi:10.1016/S0167-4781(01)00215-9. PMID 11406267.

[3] Vogel B, Löschberger A, Sauer M, Hock R (Sep 2011). "Cross-linking of DNA through HMGA1 suggests a DNA scaffold". Nucleic Acids Research. 39 (16): 7124–33. doi:10.1093/nar/gkr396. PMC 3167630. PMID 21596776.

[entrez-4] "Entrez Gene: HMGA1 high mobility group AT-hook 1".

[5] Semple RK (2009). "From bending DNA to diabetes: the curious case of HMGA1". Journal of Biology. 8 (7): 64. doi:10.1186/jbiol164. PMC 2736670. PMID 19664187.

[pmid12665574-6] 6.0 ^6.1 Foti D, Iuliano R, Chiefari E, Brunetti A (Apr 2003). "A nucleoprotein complex containing Sp1, C/EBP beta, and HMGI-Y controls human insulin receptor gene transcription". Molecular and Cellular Biology. 23 (8): 2720–32. doi:10.1128/MCB.23.8.2720-2732.2003. PMC 152545. PMID 12665574.

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@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+'''High-mobility group protein HMG-I/HMG-Y''' is a [[protein]] that in humans is encoded by the ''HMGA1'' [[gene]].<ref name="pmid8414980">{{cite journal | vauthors = Friedmann M, Holth LT, Zoghbi HY, Reeves R | title = Organization, inducible-expression and chromosome localization of the human HMG-I(Y) nonhistone protein gene | journal = Nucleic Acids Research | volume = 21 | issue = 18 | pages = 4259–67 | date = Sep 1993 | pmid = 8414980 | pmc = 310059 | doi = 10.1093/nar/21.18.4259 }}</ref><ref name="pmid11406267">{{cite journal | vauthors = Reeves R, Beckerbauer L | title = HMGI/Y proteins: flexible regulators of transcription and chromatin structure | journal = Biochimica et Biophysica Acta | volume = 1519 | issue = 1-2 | pages = 13–29 | date = May 2001 | pmid = 11406267 | pmc =  | doi = 10.1016/S0167-4781(01)00215-9 }}</ref>
-| update_page = yes
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+== Function ==
-{{GNF_Protein_box
- | image =
- | image_source =
- | PDB =
- | Name = High mobility group AT-hook 1
- | HGNCid = 5010
- | Symbol = HMGA1
- | AltSymbols =; HMG-R; HMGIY; MGC12816; MGC4242; MGC4854
- | OMIM = 600701
- | ECnumber =
- | Homologene = 32332
- | MGIid = 96160
- | GeneAtlas_image1 = PBB_GE_HMGA1_206074_s_at_tn.png
- | GeneAtlas_image2 = PBB_GE_HMGA1_210457_x_at_tn.png
- | Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003680 |text = AT DNA binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0030374 |text = ligand-dependent nuclear receptor transcription coactivator activity}} {{GNF_GO|id=GO:0042975 |text = peroxisome proliferator activated receptor binding}} {{GNF_GO|id=GO:0046965 |text = retinoid X receptor binding}}
- | Component = {{GNF_GO|id=GO:0000785 |text = chromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}} {{GNF_GO|id=GO:0005694 |text = chromosome}}
- | Process = {{GNF_GO|id=GO:0006268 |text = DNA unwinding during replication}} {{GNF_GO|id=GO:0006337 |text = nucleosome disassembly}} {{GNF_GO|id=GO:0006345 |text = loss of chromatin silencing}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0007001 |text = chromosome organization and biogenesis (sensu Eukaryota)}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 3159
-    | Hs_Ensembl = ENSG00000137309
-    | Hs_RefseqProtein = NP_002122
-    | Hs_RefseqmRNA = NM_002131
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 6
-    | Hs_GenLoc_start = 34312628
-    | Hs_GenLoc_end = 34321986
-    | Hs_Uniprot = P17096
-    | Mm_EntrezGene = 15361
-    | Mm_Ensembl = ENSMUSG00000046711
-    | Mm_RefseqmRNA = NM_001025427
-    | Mm_RefseqProtein = NP_001020598
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 17
-    | Mm_GenLoc_start = 27284171
-    | Mm_GenLoc_end = 27291260
-    | Mm_Uniprot = Q3TE85
-  }}
-}}
-'''High mobility group AT-hook 1''', also known as '''HMGA1''', is a human [[gene]].
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+This gene encodes a non-histone chromatin protein involved in many cellular processes, including regulation of inducible gene transcription, DNA replication, [[heterochromatin]] organization,  [[retroviral integration|integration]] of retroviruses into chromosomes, and the metastatic progression of cancer cells.
-{{PBB_Summary
-| section_title =
-| summary_text = This gene encodes a non-histone protein involved in many cellular processes, including regulation of inducible gene transcription, [[retroviral integration|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.<ref name="entrez">{{cite web | title = Entrez Gene: HMGA1 high mobility group AT-hook 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3159| accessdate = }}</ref>
-}}
-==See also==
+HMGA1 proteins are quite small (~10-12 kDa) and basic molecules, and consist of three [[AT-hook]]s with the RGRP (Arg-Gly-Arg-Pro) core  [[sequence motif|motif]], a novel [[cross-link]]ing domain located between the second and third AT-hook, and a [[C-terminal]] acidic tail characteristic for the [[high mobility group|HMG]] family comprising HMGA, HMGB and HMGN proteins.
+HMGA1-GFP fusion proteins are highly dynamic in vivo (determined using [[fluorescence recovery after photobleaching|FRAP]] analysis), but in contrast also show nanomolar affinity to AT-rich DNA in vitro (determined biochemically), which might be explained due to the extensive [[post-transcriptional modification]]s in vivo. HMGA1 preferentially binds to the minor groove of AT-rich regions in double-stranded DNA using its AT-hooks. It has little secondary structure in solution but assumes distinct conformations when bound to substrates such as DNA or other proteins. HMGA1 proteins have high amounts of diverse [[posttranslational modification]]s and are located mainly in the nucleus, especially in heterochromatin, but also in mitochondria and the cytoplasm.
+Recently it has been shown that HMGA1 proteins, HMGA1a and HMGA1b, can cross-link DNA fibers ''in vitro'' and can induce chromatin clustering ''in vivo'' suggesting a structural role of HMGA1 proteins in heterochromatin organization.<ref>{{cite journal | vauthors = Vogel B, Löschberger A, Sauer M, Hock R | title = Cross-linking of DNA through HMGA1 suggests a DNA scaffold | journal = Nucleic Acids Research | volume = 39 | issue = 16 | pages = 7124–33 | date = Sep 2011 | pmid = 21596776 | pmc = 3167630 | doi = 10.1093/nar/gkr396 }}</ref>
+At least seven transcript variants encoding two different isoforms (HMGA1a, HMGA1b) have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: HMGA1 high mobility group AT-hook 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3159| accessdate = }}</ref> The splice variant HMGA1c with only two AT hooks and no acidic tail is in discussion to be a real member of the HMGA family.
+Mice lacking their variant of ''HMGA1'', i.e., ''Hmga1-/-'' mice, are [[diabetic]], show a cardiac hypertrophy and express low levels of the [[insulin receptor]].<ref>{{cite journal | vauthors = Semple RK | title = From bending DNA to diabetes: the curious case of HMGA1 | journal = Journal of Biology | volume = 8 | issue = 7 | pages = 64 | year = 2009 | pmid = 19664187 | pmc = 2736670 | doi = 10.1186/jbiol164 | url = http://jbiol.com/content/8/7/64 }}</ref>
+== Interactions ==
+HMGA1 has been shown to [[Protein-protein interaction|interact]] with [[CEBPB]]<ref name=pmid12665574>{{cite journal | vauthors = Foti D, Iuliano R, Chiefari E, Brunetti A | title = A nucleoprotein complex containing Sp1, C/EBP beta, and HMGI-Y controls human insulin receptor gene transcription | journal = Molecular and Cellular Biology | volume = 23 | issue = 8 | pages = 2720–32 | date = Apr 2003 | pmid = 12665574 | pmc = 152545 | doi = 10.1128/MCB.23.8.2720-2732.2003 }}</ref> and [[Sp1 transcription factor]].<ref name=pmid12665574/>
+== See also ==
 * [[HMGA]]
+* [[AT-hook]]
-==References==
+== References ==
-{{reflist|2}}
+{{reflist|33em}}
-==Further reading==
+== Further reading ==
-{{refbegin | 2}}
+{{refbegin|33em}}
-{{PBB_Further_reading
+* {{cite journal | vauthors = Hui H, Perfetti R | title = Pancreas duodenum homeobox-1 regulates pancreas development during embryogenesis and islet cell function in adulthood | journal = European Journal of Endocrinology / European Federation of Endocrine Societies | volume = 146 | issue = 2 | pages = 129–41 | date = Feb 2002 | pmid = 11834421 | doi = 10.1530/eje.0.1460129 }}
-| citations =
+* {{cite journal | vauthors = Van Maele B, Debyser Z | title = HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins | journal = AIDS Reviews | volume = 7 | issue = 1 | pages = 26–43 | year = 2005 | pmid = 15875659 | doi =  }}
-*{{cite journal  | author=Reeves R, Beckerbauer L |title=HMGI/Y proteins: flexible regulators of transcription and chromatin structure. |journal=Biochim. Biophys. Acta |volume=1519 |issue= 1-2 |pages= 13-29 |year= 2001 |pmid= 11406267 |doi=  }}
+* {{cite journal | vauthors = Van Maele B, Busschots K, Vandekerckhove L, Christ F, Debyser Z | title = Cellular co-factors of HIV-1 integration | journal = Trends in Biochemical Sciences | volume = 31 | issue = 2 | pages = 98–105 | date = Feb 2006 | pmid = 16403635 | doi = 10.1016/j.tibs.2005.12.002 }}
-*{{cite journal  | author=Hui H, Perfetti R |title=Pancreas duodenum homeobox-1 regulates pancreas development during embryogenesis and islet cell function in adulthood. |journal=Eur. J. Endocrinol. |volume=146 |issue= 2 |pages= 129-41 |year= 2002 |pmid= 11834421 |doi=  }}
+* {{cite journal | vauthors = Reeves R, Nissen MS | title = The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure | journal = The Journal of Biological Chemistry | volume = 265 | issue = 15 | pages = 8573–82 | date = May 1990 | pmid = 1692833 | doi =  }}
-*{{cite journal  | author=Van Maele B, Debyser Z |title=[[HIV-1 integration]]: an interplay between HIV-1 integrase, cellular and viral proteins. |journal=AIDS reviews |volume=7 |issue= 1 |pages= 26-43 |year= 2005 |pmid= 15875659 |doi=  }}
+* {{cite journal | vauthors = Nissen MS, Langan TA, Reeves R | title = Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group I nonhistone chromatin protein | journal = The Journal of Biological Chemistry | volume = 266 | issue = 30 | pages = 19945–52 | date = Oct 1991 | pmid = 1939057 | doi =  }}
-*{{cite journal  | author=Van Maele B, Busschots K, Vandekerckhove L, ''et al.'' |title=Cellular co-factors of HIV-1 integration. |journal=Trends Biochem. Sci. |volume=31 |issue= 2 |pages= 98-105 |year= 2006 |pmid= 16403635 |doi= 10.1016/j.tibs.2005.12.002 }}
+* {{cite journal | vauthors = Eckner R, Birnstiel ML | title = Cloning of cDNAs coding for human HMG I and HMG Y proteins: both are capable of binding to the octamer sequence motif | journal = Nucleic Acids Research | volume = 17 | issue = 15 | pages = 5947–59 | date = Aug 1989 | pmid = 2505228 | pmc = 318252 | doi = 10.1093/nar/17.15.5947 }}
-*{{cite journal  | author=Reeves R, Nissen MS |title=The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure. |journal=J. Biol. Chem. |volume=265 |issue= 15 |pages= 8573-82 |year= 1990 |pmid= 1692833 |doi=  }}
+* {{cite journal | vauthors = Johnson KR, Lehn DA, Reeves R | title = Alternative processing of mRNAs encoding mammalian chromosomal high-mobility-group proteins HMG-I and HMG-Y | journal = Molecular and Cellular Biology | volume = 9 | issue = 5 | pages = 2114–23 | date = May 1989 | pmid = 2701943 | pmc = 363005 | doi =  10.1128/mcb.9.5.2114}}
-*{{cite journal  | author=Nissen MS, Langan TA, Reeves R |title=Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group I nonhistone chromatin protein. |journal=J. Biol. Chem. |volume=266 |issue= 30 |pages= 19945-52 |year= 1991 |pmid= 1939057 |doi=  }}
+* {{cite journal | vauthors = Palvimo J, Linnala-Kankkunen A | title = Identification of sites on chromosomal protein HMG-I phosphorylated by casein kinase II | journal = FEBS Letters | volume = 257 | issue = 1 | pages = 101–4 | date = Oct 1989 | pmid = 2806554 | doi = 10.1016/0014-5793(89)81796-X }}
-*{{cite journal  | author=Eckner R, Birnstiel ML |title=Cloning of cDNAs coding for human HMG I and HMG Y proteins: both are capable of binding to the octamer sequence motif. |journal=Nucleic Acids Res. |volume=17 |issue= 15 |pages= 5947-59 |year= 1989 |pmid= 2505228 |doi=  }}
+* {{cite journal | vauthors = Karlson JR, Mørk E, Holtlund J, Laland SG, Lund T | title = 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 | journal = Biochemical and Biophysical Research Communications | volume = 158 | issue = 3 | pages = 646–51 | date = Feb 1989 | pmid = 2920035 | doi = 10.1016/0006-291X(89)92770-8 }}
-*{{cite journal  | author=Johnson KR, Lehn DA, Reeves R |title=Alternative processing of mRNAs encoding mammalian chromosomal high-mobility-group proteins HMG-I and HMG-Y. |journal=Mol. Cell. Biol. |volume=9 |issue= 5 |pages= 2114-23 |year= 1989 |pmid= 2701943 |doi=  }}
+* {{cite journal | vauthors = Lund T, Dahl KH, Mørk E, Holtlund J, Laland SG | title = The human chromosomal protein HMG I contains two identical palindrome amino acid sequences | journal = Biochemical and Biophysical Research Communications | volume = 146 | issue = 2 | pages = 725–30 | date = Jul 1987 | pmid = 3619901 | doi = 10.1016/0006-291X(87)90589-4 }}
-*{{cite journal  | author=Palvimo J, Linnala-Kankkunen A |title=Identification of sites on chromosomal protein HMG-I phosphorylated by casein kinase II. |journal=FEBS Lett. |volume=257 |issue= 1 |pages= 101-4 |year= 1989 |pmid= 2806554 |doi=  }}
+* {{cite journal | vauthors = Leger H, Sock E, Renner K, Grummt F, Wegner M | title = Functional interaction between the POU domain protein Tst-1/Oct-6 and the high-mobility-group protein HMG-I/Y | journal = Molecular and Cellular Biology | volume = 15 | issue = 7 | pages = 3738–47 | date = Jul 1995 | pmid = 7791781 | pmc = 230612 | doi =  10.1128/mcb.15.7.3738}}
-*{{cite journal  | author=Karlson JR, Mørk E, Holtlund J, ''et al.'' |title=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. |journal=Biochem. Biophys. Res. Commun. |volume=158 |issue= 3 |pages= 646-51 |year= 1989 |pmid= 2920035 |doi=  }}
+* {{cite journal | vauthors = John S, Reeves RB, Lin JX, Child R, Leiden JM, Thompson CB, Leonard WJ | title = 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 | journal = Molecular and Cellular Biology | volume = 15 | issue = 3 | pages = 1786–96 | date = Mar 1995 | pmid = 7862168 | pmc = 230403 | doi =  10.1128/mcb.15.3.1786}}
-*{{cite journal  | author=Lund T, Dahl KH, Mørk E, ''et al.'' |title=The human chromosomal protein HMG I contains two identical palindrome amino acid sequences. |journal=Biochem. Biophys. Res. Commun. |volume=146 |issue= 2 |pages= 725-30 |year= 1987 |pmid= 3619901 |doi=  }}
+* {{cite journal | vauthors = Farnet CM, Bushman FD | title = HIV-1 cDNA integration: requirement of HMG I(Y) protein for function of preintegration complexes in vitro | journal = Cell | volume = 88 | issue = 4 | pages = 483–92 | date = Feb 1997 | pmid = 9038339 | doi = 10.1016/S0092-8674(00)81888-7 }}
-*{{cite journal  | author=Leger H, Sock E, Renner K, ''et al.'' |title=Functional interaction between the POU domain protein Tst-1/Oct-6 and the high-mobility-group protein HMG-I/Y. |journal=Mol. Cell. Biol. |volume=15 |issue= 7 |pages= 3738-47 |year= 1995 |pmid= 7791781 |doi=  }}
+* {{cite journal | vauthors = Miller MD, Farnet CM, Bushman FD | title = Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition | journal = Journal of Virology | volume = 71 | issue = 7 | pages = 5382–90 | date = Jul 1997 | pmid = 9188609 | pmc = 191777 | doi =  }}
-*{{cite journal  | author=John S, Reeves RB, Lin JX, ''et al.'' |title=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. |journal=Mol. Cell. Biol. |volume=15 |issue= 3 |pages= 1786-96 |year= 1995 |pmid= 7862168 |doi=  }}
+* {{cite journal | vauthors = Huth JR, Bewley CA, Nissen MS, Evans JN, Reeves R, Gronenborn AM, Clore GM | title = The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif | journal = Nature Structural Biology | volume = 4 | issue = 8 | pages = 657–65 | date = Aug 1997 | pmid = 9253416 | doi = 10.1038/nsb0897-657 }}
-*{{cite journal  | author=Friedmann M, Holth LT, Zoghbi HY, Reeves R |title=Organization, inducible-expression and chromosome localization of the human HMG-I(Y) nonhistone protein gene. |journal=Nucleic Acids Res. |volume=21 |issue= 18 |pages= 4259-67 |year= 1993 |pmid= 8414980 |doi=  }}
+* {{cite journal | vauthors = Currie RA | title = Functional interaction between the DNA binding subunit trimerization domain of NF-Y and the high mobility group protein HMG-I(Y) | journal = The Journal of Biological Chemistry | volume = 272 | issue = 49 | pages = 30880–8 | date = Dec 1997 | pmid = 9388234 | doi = 10.1074/jbc.272.49.30880 }}
-*{{cite journal  | author=Farnet CM, Bushman FD |title=HIV-1 cDNA integration: requirement of HMG I(Y) protein for function of preintegration complexes in vitro. |journal=Cell |volume=88 |issue= 4 |pages= 483-92 |year= 1997 |pmid= 9038339 |doi=  }}
+* {{cite journal | vauthors = Chin MT, Pellacani A, Wang H, Lin SS, Jain MK, Perrella MA, Lee ME | title = Enhancement of serum-response factor-dependent transcription and DNA binding by the architectural transcription factor HMG-I(Y) | journal = The Journal of Biological Chemistry | volume = 273 | issue = 16 | pages = 9755–60 | date = Apr 1998 | pmid = 9545312 | doi = 10.1074/jbc.273.16.9755 }}
-*{{cite journal  | author=Miller MD, Farnet CM, Bushman FD |title=Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition. |journal=J. Virol. |volume=71 |issue= 7 |pages= 5382-90 |year= 1997 |pmid= 9188609 |doi=  }}
+* {{cite journal | vauthors = Chiappetta G, Tallini G, De Biasio MC, Manfioletti G, Martinez-Tello FJ, Pentimalli F, de Nigris F, Mastro A, Botti G, Fedele M, Berger N, Santoro M, Giancotti V, Fusco A | title = 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 | journal = Cancer Research | volume = 58 | issue = 18 | pages = 4193–8 | date = Sep 1998 | pmid = 9751634 | doi =  }}
-*{{cite journal  | author=Huth JR, Bewley CA, Nissen MS, ''et al.'' |title=The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif. |journal=Nat. Struct. Biol. |volume=4 |issue= 8 |pages= 657-65 |year= 1997 |pmid= 9253416 |doi=  }}
+* {{cite journal | vauthors = Vogel B, Löschberger A, Sauer M, Hock R | title = Cross-linking of DNA through HMGA1 suggests a DNA scaffold | journal = Nucleic Acids Research | volume = 39 | issue = 16 | pages = 7124–33 | date = Sep 2011 | pmid = 21596776 | pmc = 3167630 | doi = 10.1093/nar/gkr396 }}
-*{{cite journal  | author=Currie RA |title=Functional interaction between the DNA binding subunit trimerization domain of NF-Y and the high mobility group protein HMG-I(Y). |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 30880-8 |year= 1998 |pmid= 9388234 |doi=  }}
-*{{cite journal  | author=Chin MT, Pellacani A, Wang H, ''et al.'' |title=Enhancement of serum-response factor-dependent transcription and DNA binding by the architectural transcription factor HMG-I(Y). |journal=J. Biol. Chem. |volume=273 |issue= 16 |pages= 9755-60 |year= 1998 |pmid= 9545312 |doi=  }}
-*{{cite journal  | author=Chiappetta G, Tallini G, De Biasio MC, ''et al.'' |title=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. |journal=Cancer Res. |volume=58 |issue= 18 |pages= 4193-8 |year= 1998 |pmid= 9751634 |doi=  }}
-}}
 {{refend}}
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 * {{MeshName|HMGA1+protein,+human}}
+{{NLM content}}
+{{Transcription factors|g0}}
-{{protein-stub}}
-{{NLM content}}
-{{Transcription factors}}
 [[Category:Transcription factors]]
-{{WikiDoc Sources}}

HMGA1: Difference between revisions

Latest revision as of 00:22, 27 October 2017

Contents

Function

Interactions

See also

References

Further reading

External links

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