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P52926 (HMGA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 HMGI-C
Alternative name(s):
High mobility group AT-hook protein 2
Gene names
Name:HMGA2
Synonyms:HMGIC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length109 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a transcriptional regulator. Functions in cell cycle regulation through CCNA2. Plays an important role in chromosome condensation during the meiotic G2/M transition of spermatocytes. Ref.12

Subunit structure

Interacts with E4F1. Interacts with NEK2 By similarity. Ref.12

Subcellular location

Nucleus.

Developmental stage

Expressed predominantly during embryogenesis.

Post-translational modification

Regulated by cell cycle-dependent phosphorylation which alters its DNA binding affinity. Phosphorylated by NEK2 By similarity.

Polymorphism

Genetic variations in HMGA2 define the stature quantitative trait locus 9 (STQTL9) [MIM:611547]. Human height is a classic, highly heritable quantitative trait.

Involvement in disease

A chromosomal aberration involving HMGA2 is associated with a subclass of benign mesenchymal tumors known as lipomas. Translocation t(3;12)(q27-q28;q13-q15) with LPP is shown in lipomas. HMGA2 is also fused with a number of other genes in lipomas.

A chromosomal aberration involving HMGA2 is associated with pulmonary chondroid hamartomas. Translocation t(3;12)(q27-q28;q14-q15) with LPP is detected in pulmonary chondroid hamartomas.

A chromosomal aberration involving HMGA2 is associated with parosteal lipomas. Translocation t(3;12)(q28;q14) with LPP is also shown in one parosteal lipoma.

A chromosomal aberration involving HMGA2 is found in uterine leiomyoma. Translocation t(12;14)(q15;q23-24) with RAD51B. Chromosomal rearrangements involving HMGA2 do not seem to be the principle pathobiological mechanism in uterine leiomyoma.

Sequence similarities

Belongs to the HMGA family.

Contains 3 A.T hook DNA-binding domains.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA condensation
Growth regulation
Mitosis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseProto-oncogene
   DomainRepeat
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay PubMed 19465398. Source: GOC

DNA damage response, detection of DNA damage

Inferred from direct assay PubMed 19465398. Source: UniProtKB

adrenal gland development

Inferred from electronic annotation. Source: Ensembl

base-excision repair

Inferred from direct assay PubMed 19465398. Source: UniProtKB

cell proliferation in forebrain

Inferred from electronic annotation. Source: Ensembl

chondrocyte differentiation

Inferred from direct assay PubMed 21484705. Source: UniProtKB

chondrocyte proliferation

Inferred from direct assay PubMed 21484705. Source: UniProtKB

chromatin organization

Traceable author statement PubMed 19551524. Source: UniProtKB

chromosome breakage

Inferred from direct assay PubMed 19549901. Source: UniProtKB

chromosome condensation

Inferred from electronic annotation. Source: UniProtKB-KW

endodermal cell differentiation

Inferred from mutant phenotype PubMed 17624332. Source: UniProtKB

epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 18832382. Source: UniProtKB

fat cell differentiation

Inferred from mutant phenotype PubMed 17624332PubMed 7606786. Source: UniProtKB

fat pad development

Inferred from electronic annotation. Source: Ensembl

heterochromatin assembly

Inferred from direct assay PubMed 16901784. Source: UniProtKB

histone H2A-S139 phosphorylation

Inferred from direct assay PubMed 16061642. Source: UniProtKB

male gonad development

Inferred from electronic annotation. Source: Ensembl

mesenchymal cell differentiation

Inferred from mutant phenotype PubMed 17624332PubMed 7606786. Source: UniProtKB

mesodermal cell differentiation

Inferred from mutant phenotype PubMed 17624332. Source: UniProtKB

mesodermal-endodermal cell signaling

Inferred from mutant phenotype PubMed 17624332. Source: UniProtKB

mitotic G2 DNA damage checkpoint

Inferred from direct assay PubMed 16061642. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

multicellular organismal development

Traceable author statement PubMed 7606786. Source: ProtInc

negative regulation by host of viral transcription

Inferred from direct assay PubMed 17005673. Source: UniProtKB

negative regulation of DNA binding

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of JAK-STAT cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from direct assay PubMed 19465398. Source: UniProtKB

negative regulation of astrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of double-strand break repair via nonhomologous end joining

Inferred from direct assay PubMed 19549901. Source: UniProtKB

negative regulation of intracellular steroid hormone receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of single stranded viral RNA replication via double stranded DNA intermediate

Inferred from direct assay PubMed 17005673. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 14627817. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18832382. Source: UniProtKB

oncogene-induced cell senescence

Inferred from direct assay PubMed 16901784. Source: UniProtKB

pituitary gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from direct assay PubMed 16061642. Source: UniProtKB

positive regulation of cell cycle arrest

Inferred from direct assay PubMed 16061642. Source: UniProtKB

positive regulation of cellular response to X-ray

Inferred from direct assay PubMed 16061642. Source: UniProtKB

positive regulation of cellular senescence

Inferred from mutant phenotype PubMed 16901784. Source: UniProtKB

positive regulation of gene expression

Inferred from direct assay PubMed 18832382. Source: UniProtKB

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of response to DNA damage stimulus

Inferred from direct assay PubMed 16061642PubMed 19465398. Source: UniProtKB

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of stem cell proliferation

Inferred from direct assay PubMed 21484705. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.12PubMed 18832382. Source: UniProtKB

positive regulation of transcription regulatory region DNA binding

Inferred from direct assay PubMed 18832382. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15225648PubMed 15755872PubMed 17005673PubMed 17324944PubMed 17426251. Source: UniProtKB

regulation of cell cycle process

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of cellular response to drug

Inferred from direct assay PubMed 16061642. Source: UniProtKB

regulation of growth hormone secretion

Inferred from electronic annotation. Source: Ensembl

regulation of stem cell maintenance

Inferred from mutant phenotype PubMed 17624332. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 7606786. 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

signal transduction

Inferred from electronic annotation. Source: Ensembl

somatic stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

stem cell differentiation

Inferred from expression pattern PubMed 17078040. Source: UniProtKB

   Cellular_componentSMAD protein complex

Inferred from direct assay PubMed 18832382. Source: UniProtKB

nuclear chromosome

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 16901784PubMed 17078040PubMed 17324944. Source: UniProtKB

protein-DNA complex

Inferred from direct assay PubMed 19465398. Source: UniProtKB

senescence-associated heterochromatin focus

Inferred from direct assay PubMed 16901784. Source: UniProtKB

   Molecular_function5'-deoxyribose-5-phosphate lyase activity

Inferred from direct assay PubMed 19465398. Source: UniProtKB

AT DNA binding

Inferred from direct assay PubMed 14627817PubMed 17078040PubMed 17426251PubMed 20108983PubMed 21533145. Source: UniProtKB

C2H2 zinc finger domain binding

Inferred from mutant phenotype Ref.12. Source: UniProtKB

DNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

DNA binding, bending

Inferred from direct assay PubMed 20108983. Source: UniProtKB

DNA-(apurinic or apyrimidinic site) lyase activity

Inferred from direct assay PubMed 19465398. Source: UniProtKB

DNA-dependent protein kinase activity

Inferred from direct assay PubMed 19549901. Source: UniProtKB

MH1 domain binding

Inferred from direct assay PubMed 18832382. Source: UniProtKB

MH2 domain binding

Inferred from direct assay PubMed 18832382. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay PubMed 14627817. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 18832382. Source: UniProtKB

SMAD binding

Inferred from physical interaction PubMed 18832382. Source: UniProtKB

cAMP response element binding

Inferred from direct assay Ref.12. Source: UniProtKB

core promoter binding

Inferred from direct assay PubMed 14627817. Source: UniProtKB

nucleosomal DNA binding

Inferred from direct assay PubMed 17078040. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17324944PubMed 19465398. Source: UniProtKB

regulatory region DNA binding

Inferred from direct assay PubMed 17426251. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRMT6Q96LA82EBI-912511,EBI-912440

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P52926-1)

Also known as: HMGA2a;

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 2 (identifier: P52926-2)

Also known as: HMGA2f;

The sequence of this isoform differs from the canonical sequence as follows:
     84-109: PQQVVQKKPAQEETEETSSQESAEED → DNLLPRTSSKKKTSLGNSTKRSH
Isoform 3 (identifier: P52926-3)

Also known as: HMGA2d';

The sequence of this isoform differs from the canonical sequence as follows:
     84-109: PQQVVQKKPAQEETEETSSQESAEED → LQN
Isoform 4 (identifier: P52926-4)

Also known as: HMGA2d;

The sequence of this isoform differs from the canonical sequence as follows:
     84-109: PQQVVQKKPAQEETEETSSQESAEED → WLLMKSPCW
Isoform 5 (identifier: P52926-5)

Also known as: HMGA2c';

The sequence of this isoform differs from the canonical sequence as follows:
     84-109: PQQVVQKKPAQEETEETSSQESAEED → LRAQALDSDGLGSNSGPSLS
Isoform 6 (identifier: P52926-6)

Also known as: HMGA2c;

The sequence of this isoform differs from the canonical sequence as follows:
     84-109: PQQVVQKKPAQEETEETSSQESAEED → EEFYIAA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 109108High mobility group protein HMGI-C
PRO_0000206711

Regions

DNA binding24 – 3411A.T hook 1
DNA binding44 – 5411A.T hook 2
DNA binding71 – 8212A.T hook 3
Region44 – 6320Interaction with E4F1

Amino acid modifications

Modified residue21N-acetylserine Ref.7 Ref.14
Modified residue401Phosphothreonine Ref.16
Modified residue441Phosphoserine Ref.16
Modified residue1051Phosphoserine Ref.16

Natural variations

Alternative sequence84 – 10926PQQVV…SAEED → DNLLPRTSSKKKTSLGNSTK RSH in isoform 2.
VSP_042564
Alternative sequence84 – 10926PQQVV…SAEED → LQN in isoform 3.
VSP_047772
Alternative sequence84 – 10926PQQVV…SAEED → WLLMKSPCW in isoform 4.
VSP_047773
Alternative sequence84 – 10926PQQVV…SAEED → LRAQALDSDGLGSNSGPSLS in isoform 5.
VSP_047774
Alternative sequence84 – 10926PQQVV…SAEED → EEFYIAA in isoform 6.
VSP_047775

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HMGA2a) [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: F36BABE623DA4615

FASTA10911,832
        10         20         30         40         50         60 
MSARGEGAGQ PSTSAQGQPA APAPQKRGRG RPRKQQQEPT GEPSPKRPRG RPKGSKNKSP 

        70         80         90        100 
SKAAQKKAEA TGEKRPRGRP RKWPQQVVQK KPAQEETEET SSQESAEED 

« Hide

Isoform 2 (HMGA2f) [UniParc].

Checksum: 0596B200B4B660B6
Show »

FASTA10611,456
Isoform 3 (HMGA2d') [UniParc].

Checksum: 18F9DE5C08244EFE
Show »

FASTA869,273
Isoform 4 (HMGA2d) [UniParc].

Checksum: 5095EAC51787CB88
Show »

FASTA9210,063
Isoform 5 (HMGA2c') [UniParc].

Checksum: CBBAAB6286C8BB91
Show »

FASTA10310,845
Isoform 6 (HMGA2c) [UniParc].

Checksum: 606D74FA0564126C
Show »

FASTA909,742

References

« Hide 'large scale' references
[1]"Expression and cDNA cloning of human HMGI-C phosphoprotein."
Patel U.A., Bandiera A., Manfioletti G., Giancotti V., Chau K.-Y., Crane-Robinson C.
Biochem. Biophys. Res. Commun. 201:63-70(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Hepatoma.
[2]"Recurrent rearrangements in the high mobility group protein gene, HMGI-C, in benign mesenchymal tumours."
Schoenmakers E.F.P.M., Wanschura S., Mols R., Bullerdiek J., van den Berghe H., van de Ven W.J.M.
Nat. Genet. 10:436-444(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[3]"The gene for the human architectural transcription factor HMGI-C consists of five exons each coding for a distinct functional element."
Chau K.-Y., Patel U.A., Lee K.-L.D., Lam H.-Y.P., Crane-Robinson C.
Nucleic Acids Res. 23:4262-4266(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Genomic characterization of human HMGIC, a member of the accessory transcription factor family found at translocation breakpoints in lipomas."
Ashar H.R., Cherath L., Przysybz K., Chada K.
Genomics 31:207-214(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Extensive expression studies revealed a complex alternative splicing pattern of the HMGA2 gene."
Hauke S., Leopold S., Schlueter C., Flohr A.M., Murua Escobar H., Rogalla P., Bullerdiek J.
Biochim. Biophys. Acta 1729:24-31(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), ALTERNATIVE SPLICING.
Tissue: Fibroblast.
[6]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Bienvenut W.V., Fleming J., Leug H.Y.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-27, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hepatoma.
[8]"Expression of reciprocal fusion transcripts of the HMGIC and LPP genes in parosteal lipoma."
Petit M.M., Swarts S., Bridge J.A., Van de Ven W.J.M.
Cancer Genet. Cytogenet. 106:18-23(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH LPP.
[9]"Allelic knockout of novel splice variants of human recombination repair gene RAD51B in t(12;14) uterine leiomyomas."
Schoenmakers E.F.P.M., Huysmans C., Van de Ven W.J.M.
Cancer Res. 59:19-23(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH RAD51B.
[10]"An identical HMGIC-LPP fusion transcript is consistently expressed in pulmonary chondroid hamartomas with t(3;12)(q27-28;q14-15)."
Rogalla P., Lemke I., Kazmierczak B., Bullerdiek J.
Genes Chromosomes Cancer 29:363-366(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH LPP.
[11]"Fusion transcripts involving HMGA2 are not a common molecular mechanism in uterine leiomyomata with rearrangements in 12q15."
Quade B.J., Weremowicz S., Neskey D.M., Vanni R., Ladd C., Dal Cin P., Morton C.C.
Cancer Res. 63:1351-1358(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH RAD51B.
[12]"Transcriptional activation of the cyclin A gene by the architectural transcription factor HMGA2."
Tessari M.A., Gostissa M., Altamura S., Sgarra R., Rustighi A., Salvagno C., Caretti G., Imbriano C., Mantovani R., Del Sal G., Giancotti V., Manfioletti G.
Mol. Cell. Biol. 23:9104-9116(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH E4F1.
[13]"A common variant of HMGA2 is associated with adult and childhood height in the general population."
The Diabetes Genetics Initiative, The Wellcome Trust case control consortium
Weedon M.N., Lettre G., Freathy R.M., Lindgren C.M., Voight B.F., Perry J.R.B., Elliott K.S., Hackett R., Guiducci C., Shields B., Zeggini E., Lango H., Lyssenko V., Timpson N.J., Burtt N.P., Rayner N.W., Saxena R., Ardlie K. expand/collapse author list , Tobias J.H., Ness A.R., Ring S.M., Palmer C.N.A., Morris A.D., Peltonen L., Salomaa V., Smith G.D., Groop L.C., Hattersley A.T., McCarthy M.I., Hirschhorn J.N., Frayling T.M.
Nat. Genet. 39:1245-1250(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN STQTL9.
[14]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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].
[16]"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 THR-40; SER-44 AND SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z31595 mRNA. Translation: CAA83472.1.
U28749 mRNA. Translation: AAA68613.1.
U28754 expand/collapse EMBL AC list , U28750, U28751, U28752, U28753 Genomic DNA. Translation: AAA68614.1.
L46353, L41044, L44578 Genomic DNA. Translation: AAA96484.1.
X92518 mRNA. Translation: CAA63295.1.
AY601861 mRNA. Translation: AAU43851.1.
AY601862 mRNA. Translation: AAU43852.1.
AY601863 mRNA. Translation: AAU43853.1.
AY601864 mRNA. Translation: AAU43854.1.
AY601867 mRNA. Translation: AAU43857.1.
AC090673 Genomic DNA. No translation available.
AC107308 Genomic DNA. No translation available.
CCDSCCDS31854.1. [P52926-2]
CCDS44936.1. [P52926-1]
PIRJC2232.
RefSeqNP_003474.1. NM_003483.4. [P52926-1]
NP_003475.1. NM_003484.1. [P52926-2]
UniGeneHs.505924.

3D structure databases

ProteinModelPortalP52926.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113763. 19 interactions.
IntActP52926. 2 interactions.
STRING9606.ENSP00000384026.

PTM databases

PhosphoSiteP52926.

Polymorphism databases

DMDM1708263.

Proteomic databases

MaxQBP52926.
PaxDbP52926.
PRIDEP52926.

Protocols and materials databases

DNASU8091.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354636; ENSP00000346658; ENSG00000149948. [P52926-2]
ENST00000393578; ENSP00000377206; ENSG00000149948. [P52926-6]
ENST00000403681; ENSP00000384026; ENSG00000149948. [P52926-1]
ENST00000425208; ENSP00000407306; ENSG00000149948. [P52926-4]
ENST00000537275; ENSP00000437747; ENSG00000149948. [P52926-5]
ENST00000537429; ENSP00000443372; ENSG00000149948. [P52926-3]
GeneID8091.
KEGGhsa:8091.
UCSCuc001ssv.3. human. [P52926-2]
uc001ssx.3. human. [P52926-1]

Organism-specific databases

CTD8091.
GeneCardsGC12P066218.
HGNCHGNC:5009. HMGA2.
HPACAB017809.
MIM150699. phenotype.
600698. gene.
611547. phenotype.
neXtProtNX_P52926.
Orphanet94063. 12q14 microdeletion syndrome.
99970. Dedifferentiated liposarcoma.
99971. Well-differentiated liposarcoma.
PharmGKBPA35093.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295015.
HOGENOMHOG000076308.
HOVERGENHBG051913.
KOK09283.
OMANSIKRSH.
OrthoDBEOG7QRQXW.
PhylomeDBP52926.
TreeFamTF351623.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
SignaLinkP52926.

Gene expression databases

ArrayExpressP52926.
BgeeP52926.
CleanExHS_HMGA2.
GenevestigatorP52926.

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. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHMGA2. human.
GeneWikiHMGA2.
GenomeRNAi8091.
NextBio30727.
PROP52926.
SOURCESearch...

Entry information

Entry nameHMGA2_HUMAN
AccessionPrimary (citable) accession number: P52926
Secondary accession number(s): E7EP85 expand/collapse secondary AC list , E7EWA2, Q1M182, Q1M185, Q1M186, Q1M187, Q1M188
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 142 of the entry and version 1 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

MIM cross-references

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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM