High mobility group protein HMG-I/HMG-Y

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P17096 (HMGA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 162. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
High mobility group protein HMG-I/HMG-Y
Short name=HMG-I(Y)

Alternative name(s):
High mobility group AT-hook protein 1
Short name=High mobility group protein A1
High mobility group protein R

Gene names

Name:	HMGA1
Synonyms:	HMGIY

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	107 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions.
Subunit structure	Interacts with HIPK2 By similarity. Interacts with HIV-1 pre-integration complex.
Subcellular location	Nucleus. Chromosome.
Post-translational modification	Constitutively phosphorylated on two or three sites. Hyperphosphorylated at early stages of apoptosis, followed by dephosphorylation and methylation, which coincides with chromatin condensation. Isoforms HMG-I and HMG-Y can be phosphorylated by HIPK2. Phosphorylation of HMG-I at Ser-36, Thr-53 and Thr-78 and of HMG-Y at Thr-42 and Thr-67 by HIPK2 modulates DNA-binding affinity. Ref.11 Ref.13 Ref.17 HMG-Y is not methylated. Ref.11 Ref.12 Ref.13 Ref.14 Methylation at Arg-58 is mutually exclusive with methylation at Arg-60. Ref.11 Ref.12 Ref.13 Ref.14
Involvement in disease	A chromosomal aberration involving HMGA1 is found in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24) with RAD51B.
Sequence similarities	Belongs to the HMGA family. Contains 3 A.T hook DNA-binding domains.
Mass spectrometry	Isoform HMG-I: Molecular mass is 11750±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl and 2 phosphate groups. Ref.13 Isoform HMG-I: Molecular mass is 11828±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl and 3 phosphate groups. Ref.13 Isoform HMG-I: Molecular mass is 11765±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl, 1 methyl and 2 phosphate groups. Ref.13 Isoform HMG-I: Molecular mass is 11844±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl, 1 methyl and 3 phosphate groups. Ref.13 Isoform HMG-I: Molecular mass is 11780±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl, 2 methyl and 2 phosphate groups. Ref.13 Isoform HMG-I: Molecular mass is 11858±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl, 2 methyl and 3 phosphate groups. Ref.13

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Domain	Repeat
Ligand	DNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA unwinding involved in replication Non-traceable author statement Ref.4. Source: UniProtKB base-excision repair Inferred from direct assay PubMed 19465398 PubMed 19465398. Source: UniProtKB establishment of integrated proviral latency Traceable author statement. Source: Reactome negative regulation of cell proliferation Inferred from mutant phenotype PubMed 16901784. Source: UniProtKB negative regulation of chromatin silencing Traceable author statement Ref.4. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from mutant phenotype PubMed 16901784. Source: UniProtKB nucleosome disassembly Traceable author statement Ref.4. Source: UniProtKB oncogene-induced senescence Inferred from direct assay PubMed 16901784. Source: UniProtKB positive regulation of cellular senescence Inferred from mutant phenotype PubMed 16901784. Source: UniProtKB protein complex assembly Traceable author statement Ref.4. Source: UniProtKB response to virus Inferred from expression pattern PubMed 17005673. Source: UniProtKB senescence-associated heterochromatin focus assembly Inferred from direct assay PubMed 16901784. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome senescence-associated heterochromatin focus Inferred from direct assay PubMed 16901784. Source: UniProtKB transcription factor complex Traceable author statement Ref.4. Source: UniProtKB
Molecular_function	5'-deoxyribose-5-phosphate lyase activity Inferred from direct assay PubMed 19465398 PubMed 19465398. Source: UniProtKB AT DNA binding Traceable author statement Ref.4. Source: UniProtKB DNA-(apurinic or apyrimidinic site) lyase activity Inferred from direct assay PubMed 19465398 PubMed 19465398. Source: UniProtKB ligand-dependent nuclear receptor transcription coactivator activity Inferred from mutant phenotype Ref.4. Source: UniProtKB peroxisome proliferator activated receptor binding Inferred from direct assay Ref.4. Source: UniProtKB retinoid X receptor binding Inferred from direct assay Ref.4. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from mutant phenotype Ref.4. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRMT6	Q96LA8	4	EBI-746854,EBI-912440

Alternative products

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

Isoform HMG-I (identifier: P17096-1) Also known as: HMGA1a; 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 HMG-Y (identifier: P17096-2) Also known as: HMGA1b; The sequence of this isoform differs from the canonical sequence as follows: 35-45: Missing.
Note: Contains a phosphothreonine at position 42.

Isoform HMG-R (identifier: P17096-3) Also known as: HMGA1c; The sequence of this isoform differs from the canonical sequence as follows: 66-107: NKGAAKTRKT...ISQESSEEEQ → KNWRRRKRRA...RIHTCPPGQG

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 107

106

High mobility group protein HMG-I/HMG-Y

PRO_0000206708

Regions

DNA binding

21 – 31

A.T hook 1 Ref.9

DNA binding

53 – 63

A.T hook 2 Ref.9

DNA binding

78 – 89

A.T hook 3 Ref.9

Region

53 – 77

Interaction with HIPK2 By similarity

Compositional bias

91 – 106

Glu-rich (acidic)

Amino acid modifications

Modified residue

N-acetylserine By similarity

Modified residue

N6-acetyllysine Ref.23

Modified residue

Asymmetric dimethylarginine; in isoform HMG-I; alternate Ref.11 Ref.13

Modified residue

Omega-N-methylarginine; in isoform HMG-I; alternate Ref.11 Ref.13

Modified residue

Symmetric dimethylarginine; in isoform HMG-I; alternate Ref.11 Ref.13

Modified residue

Phosphoserine; by HIPK2 and CDC2; in isoform HMG-I Ref.15 Ref.16 Ref.17 Ref.20 Ref.24 Ref.26

Modified residue

Phosphothreonine Ref.20

Modified residue

Phosphoserine Ref.20 Ref.26

Modified residue

Phosphoserine Ref.20

Modified residue

Phosphothreonine; by HIPK2 and CDC2; in isoform HMG-I and isoform HMG-Y Ref.16 Ref.17 Ref.20 Ref.24 Ref.26

Modified residue

Asymmetric dimethylarginine; by PRMT6; alternate Ref.14

Modified residue

Omega-N-methylarginine; by PRMT6; alternate Ref.14

Modified residue

Asymmetric dimethylarginine; by PRMT6; alternate Ref.14

Modified residue

Omega-N-methylarginine; by PRMT6; alternate Ref.14

Modified residue

Phosphothreonine; by HIPK2 and CDC2; in isoform HMG-I and isoform HMG-Y Ref.17

Modified residue

Phosphoserine; in isoform HMG-I and isoform HMG-Y Ref.13 Ref.15 Ref.18 Ref.22 Ref.24 Ref.26

Modified residue

102

Phosphoserine; by CK; in isoform HMG-I and isoform HMG-Y Ref.13 Ref.15 Ref.18 Ref.22 Ref.24 Ref.26

Modified residue

103

Phosphoserine; by CK; in isoform HMG-I and isoform HMG-Y Ref.13 Ref.15 Ref.18 Ref.22 Ref.24

Natural variations

Alternative sequence

35 – 45

Missing in isoform HMG-Y.

VSP_002182

Alternative sequence

66 – 107

NKGAA…SEEEQ → KNWRRRKRRASRRSPRRRSS DPCVPPAPHWRSSFLLGLDS FAPLPPPPPLPQAHHHHRLW PPPPSSTCALTTTLHSTPAA AGLPWAEWGAVFPWPQFPAP PAHPRIHTCPPGQG in isoform HMG-R.

VSP_018084

Experimental info

Mutagenesis

R → A: Does not affect methylation by PRMT6. Ref.14

Mutagenesis

R → A: Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-60. Ref.14

Mutagenesis

R → A: Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-58. Ref.14

Sequence conflict

107

Q → QQQ AA sequence Ref.8

Secondary structure

107

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform HMG-I (HMGA1a) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E9C4E3F2200914B8 Show »	FASTA	107	11,676
10 20 30 40 50 60 MSESSSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE VPTPKRPRGR 70 80 90 100 PKGSKNKGAA KTRKTTTTPG RKPRGRPKKL EKEEEEGISQ ESSEEEQ « Hide
Isoform HMG-Y (HMGA1b) [UniParc]. Checksum: B82DCAA29E6D18FD Show »	FASTA	96	10,679
10 20 30 40 50 60 MSESSSKSSQ PLASKQEKDG TEKRGRGRPR KQPPKEPSEV PTPKRPRGRP KGSKNKGAAK 70 80 90 TRKTTTTPGR KPRGRPKKLE KEEEEGISQE SSEEEQ « Hide
Isoform HMG-R (HMGA1c) [UniParc]. Checksum: 91E56E235C504AAA Show »	FASTA	179	19,694
10 20 30 40 50 60 MSESSSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE VPTPKRPRGR 70 80 90 100 110 120 PKGSKKNWRR RKRRASRRSP RRRSSDPCVP PAPHWRSSFL LGLDSFAPLP PPPPLPQAHH 130 140 150 160 170 HHRLWPPPPS STCALTTTLH STPAAAGLPW AEWGAVFPWP QFPAPPAHPR IHTCPPGQG « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of cDNAs coding for human HMG I and HMG Y proteins: both are capable of binding to the octamer sequence motif." Eckner R., Birnstiel M.L. Nucleic Acids Res. 17:5947-5959(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HMG-I AND HMG-Y).
[2]	"Alternative processing of mRNAs encoding mammalian chromosomal high-mobility-group proteins HMG-I and HMG-Y." Johnson K.R., Lehn D.A., Reeves R. Mol. Cell. Biol. 9:2114-2123(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HMG-I AND HMG-Y).
[3]	"Organization, inducible-expression and chromosome localization of the human HMG-I(Y) nonhistone protein gene." Friedmann M., Holth L.T., Zoghbi H.Y., Reeves R. Nucleic Acids Res. 21:4259-4267(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[4]	"Retinoid-dependent recruitment of a histone H1 displacement activity by retinoic acid receptor." Nagpal S., Ghosn C., DiSepio D., Molina Y., Sutter M., Klein E.S., Chandraratna R.A.S. J. Biol. Chem. 274:22563-22568(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HMG-R).
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORMS HMG-I AND HMG-Y). Tissue: B-cell, Mammary gland, Muscle, Pancreas and Uterus.
[7]	"The human chromosomal protein HMG I contains two identical palindrome amino acid sequences." Lund T., Dahl K.H., Mork E., Holtlund J., Laland S.G. Biochem. Biophys. Res. Commun. 146:725-730(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 4-107 (HMG-I).
[8]	"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." Karlson J.R., Mork E., Holtlund J., Laland S.G., Lund T. Biochem. Biophys. Res. Commun. 158:646-651(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 4-107 (HMG-Y).
[9]	"The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure." Reeves R., Nissen M.S. J. Biol. Chem. 265:8573-8582(1990) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING DOMAINS.
[10]	"Intragenic breakpoint within RAD51L1 in a t(6;14)(p21.3;q24) of a pulmonary chondroid hamartoma." Blank C., Schoenmakers E.F.P.M., Rogalla P., Huys E.H., van Rijk A.A., Drieschner N., Bullerdiek J. Cytogenet. Cell Genet. 95:17-19(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH RAD51B.
[11]	"During apoptosis of tumor cells HMGA1a protein undergoes methylation: identification of the modification site by mass spectrometry." Sgarra R., Diana F., Bellarosa C., Dekleva V., Rustighi A., Toller M., Manfioletti G., Giancotti V. Biochemistry 42:3575-3585(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, METHYLATION AT ARG-26, MASS SPECTROMETRY.
[12]	"Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a." Miranda T.B., Webb K.J., Edberg D.D., Reeves R., Clarke S. Biochem. Biophys. Res. Commun. 336:831-835(2005) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION BY PRMT6.
[13]	"Tandem mass spectrometry for the examination of the posttranslational modifications of high-mobility group A1 proteins: symmetric and asymmetric dimethylation of Arg25 in HMGA1a protein." Zou Y., Wang Y. Biochemistry 44:6293-6301(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, METHYLATION AT ARG-26, MASS SPECTROMETRY.
[14]	"Dynamics of human protein arginine methyltransferase 1(PRMT1) in vivo." Herrmann F., Lee J., Bedford M.T., Fackelmayer F.O. J. Biol. Chem. 280:38005-38010(2005) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-58 AND ARG-60 BY PRMT6, MUTAGENESIS OF ARG-26; ARG-58 AND ARG-60.
[15]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-99; SER-102 AND SER-103, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-53, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 (ISOFORM HMG-Y), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Homeodomain-interacting protein kinase-2 (HIPK2) phosphorylates HMGA1a at Ser-35, Thr-52, and Thr-77 and modulates its DNA binding affinity." Zhang Q., Wang Y. J. Proteome Res. 6:4711-4719(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-36; THR-53 AND THR-78 BY HIPK2 AND CDK1/CDC2.
[18]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[19]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: T-cell.
[20]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39; SER-44; SER-49 AND THR-53, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Liver.
[22]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[23]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-15, MASS SPECTROMETRY.
[24]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-53; SER-99; SER-102 AND SER-103, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-44; THR-53; SER-99 AND SER-102, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 (ISOFORM HMG-Y), MASS SPECTROMETRY.
[27]	"The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif." Huth J.R., Bewley C.A., Nissen M.S., Evans J.N., Reeves R., Gronenborn A.M., Clore G.M. Nat. Struct. Biol. 4:657-665(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 51-75 AND 80-89.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X14957 mRNA. Translation: CAA33080.1.
X14958 mRNA. Translation: CAA33081.1.
M23614 mRNA. Translation: AAA88072.1.
M23615 mRNA. Translation: AAA88073.1.
M23616 mRNA. Translation: AAA88074.1.
M23617 mRNA. Translation: AAA88075.1.
M23618 mRNA. Translation: AAA88076.1.
M23619 mRNA. Translation: AAA35998.1.
L17131 Genomic DNA. Translation: AAB00145.1.
AF176039 mRNA. Translation: AAD53889.1.
AL354740 Genomic DNA. Translation: CAI14991.1.
BC004924 mRNA. Translation: AAH04924.1.
BC008832 mRNA. Translation: AAH08832.1.
BC063434 mRNA. Translation: AAH63434.1.
BC067083 mRNA. Translation: AAH67083.1.
BC071864 mRNA. Translation: AAH71864.1.

IPI

IPI00177716.
IPI00179700.
IPI00746310.

PIR

A32794.

RefSeq

NP_002122.1. NM_002131.3.
NP_665906.1. NM_145899.2.
NP_665908.1. NM_145901.2.
NP_665909.1. NM_145902.2.
NP_665910.1. NM_145903.2.
NP_665912.1. NM_145905.2.

UniGene

Hs.518805.
Hs.703764.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EZD	NMR	-	A	51-75	[»]
2EZE	NMR	-	A	51-75	[»]
2EZF	NMR	-	A	80-89	[»]
2EZG	NMR	-	A	80-89	[»]

DisProt

DP00040.

ProteinModelPortal

P17096.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29687N.

IntAct

P17096. 38 interactions.

MINT

MINT-262941.

STRING

9606.ENSP00000308227.

PTM databases

PhosphoSite

P17096.

Polymorphism databases

DMDM

123377.

Proteomic databases

PaxDb

P17096.

PRIDE

P17096.

Protocols and materials databases

DNASU

3159.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000311487; ENSP00000308227; ENSG00000137309.
ENST00000327014; ENSP00000318322; ENSG00000137309.
ENST00000347617; ENSP00000288245; ENSG00000137309.
ENST00000357318; ENSP00000349871; ENSG00000137309.
ENST00000374116; ENSP00000363230; ENSG00000137309.
ENST00000401473; ENSP00000385693; ENSG00000137309.
ENST00000447654; ENSP00000399888; ENSG00000137309.

GeneID

3159.

KEGG

hsa:3159.

UCSC

uc003oit.3. human.

Organism-specific databases

CTD

3159.

GeneCards

GC06P034443.

HGNC

HGNC:5010. HMGA1.

HPA

CAB032200.

MIM

600701. gene.

neXtProt

NX_P17096.

PharmGKB

PA35094.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41800.

HOGENOM

HOG000076308.

HOVERGEN

HBG063451.

K09282.

OMA

EPSEAPN.

Enzyme and pathway databases

Pathway_Interaction_DB

il4_2pathway. IL4-mediated signaling events.

Reactome

REACT_116125. Disease.

SignaLink

P17096.

Gene expression databases

ArrayExpress

P17096.

Bgee

P17096.

CleanEx

HS_HMGA1.

Genevestigator

P17096.

GermOnline

ENSG00000137309. Homo sapiens.

Family and domain databases

InterPro

IPR020478. AT_hook-like.
IPR017956. AT_hook_DNA-bd_motif.
IPR000116. HMGI/HMGY.
IPR000637. HMGI/Y_DNA-bd_CS.
[Graphical view]

Pfam

PF02178. AT_hook. 3 hits.
[Graphical view]

PRINTS

PR00929. ATHOOK.
PR00930. HIGHMOBLTYIY.

SMART

SM00384. AT_hook. 3 hits.
[Graphical view]

PROSITE

PS00354. HMGI_Y. 3 hits.
[Graphical view]

ProtoNet

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Other

ChiTaRS

HMGA1. human.

GenomeRNAi

3159.

NextBio

12514.

SOURCE

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Entry information

Entry name

HMGA1_HUMAN

Accession

Primary (citable) accession number: P17096
Secondary accession number(s): P10910, Q5T6U9, Q9UKB0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 162 of the entry and version 3 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.

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents