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P17096 (HMGA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length107 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DomainRepeat
   LigandDNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay PubMed 19465398PubMed 19465398. Source: GOC

DNA unwinding involved in DNA replication

Non-traceable author statement Ref.4. Source: UniProtKB

base-excision repair

Inferred from direct assay PubMed 19465398PubMed 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-templated

Inferred from mutant phenotype PubMed 16901784. Source: UniProtKB

nucleosome disassembly

Traceable author statement Ref.4. Source: UniProtKB

oncogene-induced cell senescence

Inferred from direct assay PubMed 16901784. Source: UniProtKB

positive regulation of cellular senescence

Inferred from mutant phenotype PubMed 16901784. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.4. Source: UniProtKB

protein complex assembly

Traceable author statement Ref.4. Source: UniProtKB

regulation of transcription, DNA-templated

Traceable author statement PubMed 10871404. Source: ProtInc

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-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 16901784. Source: UniProtKB

senescence-associated heterochromatin focus

Inferred from direct assay PubMed 16901784. Source: UniProtKB

transcription factor complex

Traceable author statement Ref.4. Source: UniProtKB

   Molecular_function5'-deoxyribose-5-phosphate lyase activity

Inferred from direct assay PubMed 19465398PubMed 19465398. Source: UniProtKB

AT DNA binding

Traceable author statement Ref.4. Source: UniProtKB

DNA binding

Traceable author statement PubMed 10871404. Source: ProtInc

DNA-(apurinic or apyrimidinic site) lyase activity

Inferred from direct assay PubMed 19465398PubMed 19465398. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.12. 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 PubMed 16293633. Source: IntAct

retinoic acid 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

transcription factor binding

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRMT6Q96LA84EBI-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. Contains a phosphothreonine at position 67.
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 107106High mobility group protein HMG-I/HMG-Y
PRO_0000206708

Regions

DNA binding21 – 3111A.T hook 1 Ref.9
DNA binding53 – 6311A.T hook 2 Ref.9
DNA binding78 – 8912A.T hook 3 Ref.9
Region53 – 7725Interaction with HIPK2 By similarity
Compositional bias91 – 10616Glu-rich (acidic)

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue71N6-acetyllysine By similarity
Modified residue151N6-acetyllysine Ref.24
Modified residue261Asymmetric dimethylarginine; alternate Ref.11 Ref.13
Modified residue261Omega-N-methylarginine; alternate Ref.11 Ref.13
Modified residue261Symmetric dimethylarginine; alternate Ref.11 Ref.13
Modified residue361Phosphoserine; by HIPK2 and CDC2 Ref.15 Ref.16 Ref.17 Ref.20 Ref.25 Ref.27
Modified residue391Phosphothreonine Ref.20
Modified residue441Phosphoserine Ref.20 Ref.27
Modified residue491Phosphoserine Ref.20
Modified residue531Phosphothreonine; by HIPK2 and CDC2 Ref.16 Ref.17 Ref.20 Ref.25 Ref.27
Modified residue581Asymmetric dimethylarginine; by PRMT6; alternate Ref.14
Modified residue581Omega-N-methylarginine; by PRMT6; alternate Ref.14
Modified residue601Asymmetric dimethylarginine; by PRMT6; alternate Ref.14
Modified residue601Omega-N-methylarginine; by PRMT6; alternate Ref.14
Modified residue781Phosphothreonine; by HIPK2 and CDC2 Ref.17
Modified residue991Phosphoserine Ref.13 Ref.15 Ref.18 Ref.23 Ref.25 Ref.27
Modified residue1021Phosphoserine; by CK Ref.13 Ref.15 Ref.18 Ref.23 Ref.25 Ref.27
Modified residue1031Phosphoserine; by CK Ref.13 Ref.15 Ref.18 Ref.23 Ref.25

Natural variations

Alternative sequence35 – 4511Missing in isoform HMG-Y.
VSP_002182
Alternative sequence66 – 10742NKGAA…SEEEQ → KNWRRRKRRASRRSPRRRSS DPCVPPAPHWRSSFLLGLDS FAPLPPPPPLPQAHHHHRLW PPPPSSTCALTTTLHSTPAA AGLPWAEWGAVFPWPQFPAP PAHPRIHTCPPGQG in isoform HMG-R.
VSP_018084

Experimental info

Mutagenesis261R → A: Does not affect methylation by PRMT6. Ref.14
Mutagenesis581R → A: Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-60. Ref.14
Mutagenesis601R → A: Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-58. Ref.14
Sequence conflict1071Q → QQQ AA sequence Ref.8

Secondary structure

... 107
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform HMG-I (HMGA1a) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E9C4E3F2200914B8

FASTA10711,676
        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 »

FASTA9610,679
Isoform HMG-R (HMGA1c) [UniParc].

Checksum: 91E56E235C504AAA
Show »

FASTA17919,694

References

« Hide '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. expand/collapse author list , 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] [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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 (ISOFORM HMG-I), PHOSPHORYLATION AT THR-42 AND THR-67 BY HIPK2 AND CDK1/CDC2 (ISOFORM HMG-Y).
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[24]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"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].
[27]"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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 51-75 AND 80-89.
+Additional computationally mapped references.

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.
CCDSCCDS4788.1. [P17096-2]
CCDS4789.1. [P17096-1]
PIRA32794.
RefSeqNP_002122.1. NM_002131.3. [P17096-2]
NP_665906.1. NM_145899.2. [P17096-1]
NP_665908.1. NM_145901.2. [P17096-1]
NP_665909.1. NM_145902.2. [P17096-2]
NP_665910.1. NM_145903.2. [P17096-2]
NP_665912.1. NM_145905.2. [P17096-2]
XP_005249118.1. XM_005249061.1. [P17096-1]
UniGeneHs.518805.
Hs.703764.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EZDNMR-A51-71[»]
2EZENMR-A51-75[»]
2EZFNMR-A80-89[»]
2EZGNMR-A80-89[»]
DisProtDP00040.
ProteinModelPortalP17096.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109402. 70 interactions.
DIPDIP-29687N.
IntActP17096. 39 interactions.
MINTMINT-262941.
STRING9606.ENSP00000308227.

PTM databases

PhosphoSiteP17096.

Polymorphism databases

DMDM123377.

Proteomic databases

MaxQBP17096.
PaxDbP17096.
PRIDEP17096.

Protocols and materials databases

DNASU3159.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311487; ENSP00000308227; ENSG00000137309. [P17096-1]
ENST00000347617; ENSP00000288245; ENSG00000137309. [P17096-2]
ENST00000374116; ENSP00000363230; ENSG00000137309. [P17096-2]
ENST00000401473; ENSP00000385693; ENSG00000137309. [P17096-2]
ENST00000447654; ENSP00000399888; ENSG00000137309. [P17096-1]
GeneID3159.
KEGGhsa:3159.
UCSCuc003oit.3. human. [P17096-1]

Organism-specific databases

CTD3159.
GeneCardsGC06P036298.
HGNCHGNC:5010. HMGA1.
HPACAB032200.
MIM600701. gene.
neXtProtNX_P17096.
PharmGKBPA35094.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41800.
HOGENOMHOG000076308.
HOVERGENHBG063451.
KOK09282.
OMAQQEPSEA.
TreeFamTF351623.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_120956. Cellular responses to stress.
SignaLinkP17096.

Gene expression databases

ArrayExpressP17096.
BgeeP17096.
CleanExHS_HMGA1.
GenevestigatorP17096.

Family and domain databases

InterProIPR020478. AT_hook-like.
IPR017956. AT_hook_DNA-bd_motif.
IPR000116. HMGI/HMGY.
IPR000637. HMGI/Y_DNA-bd_CS.
[Graphical view]
PfamPF02178. AT_hook. 3 hits.
[Graphical view]
PRINTSPR00929. ATHOOK.
PR00930. HIGHMOBLTYIY.
SMARTSM00384. AT_hook. 3 hits.
[Graphical view]
PROSITEPS00354. HMGI_Y. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHMGA1. human.
GeneWikiHMGA1.
GenomeRNAi3159.
NextBio12514.
PROP17096.
SOURCESearch...

Entry information

Entry nameHMGA1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 173 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 6

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