P17096 (HMGA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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)

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. Phosphorylated upon DNA damage, probably by ATM or ATR. 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.12 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 HMG-Y is not methylated. Ref.11 Ref.13 Ref.14 Ref.15 Methylation at Arg-58 is mutually exclusive with methylation at Arg-60.
Involvement in disease	Note=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.12 Isoform HMG-I: Molecular mass is 11828±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl and 3 phosphate groups. Ref.12 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.12 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.12 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.12 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.12

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. Source: UniProtKB initiation of viral infection Traceable author statement. Source: Reactome interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell proliferation Inferred from mutant phenotype. Source: UniProtKB negative regulation of chromatin silencing Traceable author statement Ref.4. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from mutant phenotype. Source: UniProtKB nucleosome disassembly Traceable author statement Ref.4. Source: UniProtKB oncogene-induced senescence Inferred from direct assay. Source: UniProtKB positive regulation of cellular senescence Inferred from mutant phenotype. Source: UniProtKB protein complex assembly Traceable author statement Ref.4. Source: UniProtKB provirus integration Traceable author statement. Source: Reactome response to virus Inferred from expression pattern. Source: UniProtKB senescence-associated heterochromatin focus assembly Inferred from direct assay. 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. Source: UniProtKB transcription factor complex Traceable author statement Ref.4. Source: UniProtKB
Molecular function	5'-deoxyribose-5-phosphate lyase activity Inferred from direct assay. Source: UniProtKB AT DNA binding Traceable author statement Ref.4. Source: UniProtKB DNA-(apurinic or apyrimidinic site) lyase activity Inferred from direct assay. Source: UniProtKB enzyme binding Inferred from physical interaction Ref.13. 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 protein binding Inferred from physical interaction. Source: IntAct 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.

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

1

1

Removed

Chain

2 – 107

106

High mobility group protein HMG-I/HMG-Y

PRO_0000206708

Regions

DNA binding

21 – 31

11

A.T hook 1 Ref.9

DNA binding

53 – 63

11

A.T hook 2 Ref.9

DNA binding

78 – 89

12

A.T hook 3 Ref.9

Region

53 – 77

25

Interaction with HIPK2 By similarity

Compositional bias

91 – 106

16

Glu-rich (acidic)

Amino acid modifications

Modified residue

2

1

N-acetylserine By similarity

Modified residue

15

1

N6-acetyllysine Ref.27

Modified residue

26

1

Asymmetric dimethylarginine; in isoform HMG-I; alternate Ref.11 Ref.14

Modified residue

26

1

Omega-N-methylarginine; in isoform HMG-I; alternate Ref.11 Ref.14

Modified residue

26

1

Symmetric dimethylarginine; in isoform HMG-I; alternate Ref.11 Ref.14

Modified residue

36

1

Phosphoserine; by HIPK2 and CDC2; in isoform HMG-I Ref.17 Ref.18 Ref.19 Ref.22 Ref.24

Modified residue

39

1

Phosphothreonine Ref.22 Ref.24

Modified residue

44

1

Phosphoserine Ref.20 Ref.22

Modified residue

49

1

Phosphoserine Ref.22

Modified residue

53

1

Phosphothreonine; by HIPK2 and CDC2; in isoform HMG-I and isoform HMG-Y Ref.18 Ref.19 Ref.22 Ref.24

Modified residue

58

1

Asymmetric dimethylarginine; by PRMT6; alternate Ref.15

Modified residue

58

1

Omega-N-methylarginine; by PRMT6; alternate Ref.15

Modified residue

60

1

Asymmetric dimethylarginine; by PRMT6; alternate Ref.15

Modified residue

60

1

Omega-N-methylarginine; by PRMT6; alternate Ref.15

Modified residue

78

1

Phosphothreonine; by HIPK2 and CDC2; in isoform HMG-I and isoform HMG-Y Ref.19

Modified residue

99

1

Phosphoserine; in isoform HMG-I and isoform HMG-Y Ref.12 Ref.14 Ref.16 Ref.17 Ref.20 Ref.22 Ref.26

Modified residue

102

1

Phosphoserine; by CK; in isoform HMG-I and isoform HMG-Y Ref.12 Ref.14 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26

Modified residue

103

1

Phosphoserine; by CK; in isoform HMG-I and isoform HMG-Y Ref.12 Ref.14 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26

Natural variations

Alternative sequence

35 – 45

11

Missing in isoform HMG-Y.

VSP_002182

Alternative sequence

66 – 107

42

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

VSP_018084

Experimental info

Mutagenesis

26

1

R → A: Does not affect methylation by PRMT6. Ref.15

Mutagenesis

58

1

R → A: Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-60. Ref.15

Mutagenesis

60

1

R → A: Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-58. Ref.15

Sequence conflict

107

1

Q → QQQ AA sequence Ref.8

Secondary structure

1

.

.

.

107

Helix Strand Turn

Details...

Turn

62 – 63

2

Sequences

	Sequence		Length	Mass (Da)
	Isoform HMG-I (HMGA1a) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E9C4E3F2200914B8	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
	Isoform HMG-Y (HMGA1b) [UniParc]. Checksum: B82DCAA29E6D18FD	FASTA	96	10,679
	10 20 30 40 50 60 MSESSSKSSQ PLASKQEKDG TEKRGRGRPR KQPPKEPSEV PTPKRPRGRP KGSKNKGAAK 70 80 90 TRKTTTTPGR KPRGRPKKLE KEEEEGISQE SSEEEQ
	Isoform HMG-R (HMGA1c) [UniParc]. Checksum: 91E56E235C504AAA	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

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: 2505228] [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: 2701943] [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: 8414980] [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: 10428834] [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. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [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: 15489334] [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: 3619901] [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: 2920035] [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: 1692833] [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: 11978964] [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: 12653562] [Abstract] Cited for: PHOSPHORYLATION, METHYLATION AT ARG-26, MASS SPECTROMETRY.
[12]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 16157300] [Abstract] Cited for: METHYLATION BY PRMT6.
[14]	"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: 15835918] [Abstract] Cited for: PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, METHYLATION AT ARG-26, MASS SPECTROMETRY.
[15]	"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: 16159886] [Abstract] Cited for: METHYLATION AT ARG-58 AND ARG-60 BY PRMT6, MUTAGENESIS OF ARG-26; ARG-58 AND ARG-60.
[16]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[17]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-99; SER-102 AND SER-103, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-53, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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: 17960875] [Abstract] Cited for: PHOSPHORYLATION AT SER-36; THR-53 AND THR-78 BY HIPK2 AND CDK1/CDC2.
[20]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-99; SER-102 AND SER-103, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[21]	"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: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, MASS SPECTROMETRY. Tissue: T-cell.
[22]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39; SER-44; SER-49; THR-53; SER-99; SER-102 AND SER-103, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, MASS SPECTROMETRY. Tissue: Liver.
[24]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39 AND THR-53, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[25]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, MASS SPECTROMETRY.
[26]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[27]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-15, MASS SPECTROMETRY.
[28]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]	"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: 9253416] [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	[»]

ProteinModelPortal

P17096.

DisProt

DP00040.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29687N.

IntAct

P17096. 35 interactions.

MINT

MINT-262941.

STRING

P17096.

PTM databases

PhosphoSite

P17096.

Polymorphism databases

DMDM

123377.

Proteomic databases

PRIDE

P17096.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000311487; ENSP00000308227; ENSG00000137309.
ENST00000357318; ENSP00000349871; ENSG00000137309.
ENST00000447654; ENSP00000399888; ENSG00000137309.

GeneID

3159.

KEGG

hsa:3159.

UCSC

uc003oit.1. human.

Organism-specific databases

CTD

3159.

GeneCards

GC06P034205.

HGNC

HGNC:5010. HMGA1.

HPA

CAB032200.

MIM

600701. gene.

neXtProt

NX_P17096.

PharmGKB

PA35094.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20925.

GeneTree

ENSGT00530000064045.

HOVERGEN

HBG063451.

OMA

TTAPGRK.

Enzyme and pathway databases

Pathway_Interaction_DB

il4_2pathway. IL4-mediated signaling events.

Reactome

REACT_6185. HIV Infection.

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]

KO

K09282.

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

Search...

Other

NextBio

12514.

SOURCE

Search...

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:	January 25, 2012
This is version 147 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.