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P52927 (HMGA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length108 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.6

Subunit structure

Interacts with E4F1 By similarity. Interacts with NEK2. Ref.6

Subcellular location

Nucleus Ref.6.

Tissue specificity

Expressed in mitotic spermatogonia, meiotic spermatocytes, and postmeiotic round spermatids (at protein level). Ref.6

Developmental stage

Expressed predominantly during embryogenesis.

Post-translational modification

Regulated by cell cycle-dependent phosphorylation which alters its DNA binding affinity. Phosphorylated by NEK2. Ref.6

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
Meiosis
Mitosis
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from sequence or structural similarity. Source: GOC

DNA damage response, detection of DNA damage

Inferred from sequence or structural similarity. Source: UniProtKB

adipose tissue development

Inferred from mutant phenotype PubMed 7958830. Source: MGI

adrenal gland development

Inferred from mutant phenotype PubMed 7958830. Source: MGI

base-excision repair

Inferred from sequence or structural similarity. Source: UniProtKB

cell proliferation

Inferred from mutant phenotype PubMed 18957199. Source: MGI

cell proliferation in forebrain

Inferred from mutant phenotype PubMed 18957199. Source: MGI

chondrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

chondrocyte proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome breakage

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome condensation

Inferred from electronic annotation. Source: UniProtKB-KW

endodermal cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: UniProtKB

fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

fat pad development

Inferred from genetic interaction PubMed 10742101. Source: MGI

heterochromatin assembly

Inferred from sequence or structural similarity. Source: UniProtKB

histone H2A-S139 phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

male gonad development

Inferred from mutant phenotype PubMed 7958830. Source: MGI

meiotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

mesenchymal cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

mesodermal cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

mesodermal-endodermal cell signaling

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic G2 DNA damage checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation by host of viral transcription

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of JAK-STAT cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of astrocyte differentiation

Inferred from direct assay PubMed 18640244. Source: MGI

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

Inferred from sequence or structural similarity. 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 sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

oncogene-induced cell senescence

Inferred from sequence or structural similarity. Source: UniProtKB

pituitary gland development

Inferred from mutant phenotype PubMed 504232. Source: MGI

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 7651535. Source: MGI

positive regulation of cellular response to X-ray

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cellular senescence

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from mutant phenotype PubMed 15225648. Source: UniProtKB

positive regulation of multicellular organism growth

Inferred from mutant phenotype PubMed 14794889PubMed 5051369PubMed 7651535PubMed 7958830. Source: MGI

positive regulation of response to DNA damage stimulus

Inferred from sequence or structural similarity. 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 sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell cycle process

Inferred from direct assay PubMed 14645522. Source: UniProtKB

regulation of cellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of growth hormone secretion

Inferred from mutant phenotype PubMed 504232. Source: MGI

regulation of peptide hormone secretion

Inferred from mutant phenotype PubMed 504232. Source: MGI

regulation of stem cell maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

response to virus

Inferred from electronic annotation. Source: Ensembl

senescence-associated heterochromatin focus assembly

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from electronic annotation. Source: Ensembl

somatic stem cell maintenance

Inferred from mutant phenotype PubMed 18957199. Source: MGI

spermatogenesis

Inferred from mutant phenotype PubMed 12032866. Source: MGI

   Cellular_componentSMAD protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear chromosome

Inferred from direct assay PubMed 11555636. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

protein-DNA complex

Inferred from sequence or structural similarity. Source: UniProtKB

senescence-associated heterochromatin focus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function5'-deoxyribose-5-phosphate lyase activity

Inferred from sequence or structural similarity. Source: UniProtKB

AT DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

C2H2 zinc finger domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

DNA binding, bending

Inferred from sequence or structural similarity. Source: UniProtKB

DNA-(apurinic or apyrimidinic site) lyase activity

Inferred from sequence or structural similarity. Source: UniProtKB

DNA-dependent protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

MH1 domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

MH2 domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

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

Inferred from sequence or structural similarity. 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 19223528. Source: MGI

cAMP response element binding

Inferred from sequence or structural similarity. Source: UniProtKB

core promoter binding

Inferred from sequence or structural similarity. Source: UniProtKB

nucleosomal DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16766265. Source: IntAct

protein binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RB1P064005EBI-912574,EBI-491274From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 108107High mobility group protein HMGI-C
PRO_0000206712

Regions

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

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue401Phosphothreonine By similarity
Modified residue441Phosphoserine By similarity
Modified residue1041Phosphoserine Ref.7

Sequences

Sequence LengthMass (Da)Tools
P52927 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 40A3E38F62268C09

FASTA10811,819
        10         20         30         40         50         60 
MSARGEGAGQ PSTSAQGQPA APVPQKRGRG RPRKQQQEPT CEPSPKRPRG RPKGSKNKSP 

        70         80         90        100 
SKAAQKKAET IGEKRPRGRP RKWPQQVVQK KPAQETEETS SQESAEED 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning of the HMGI-C phosphoprotein, a nuclear protein associated with neoplastic and undifferentiated phenotypes."
Manfioletti G., Giancotti V., Bandiera A., Buratti E., Sautiere P., Cary P., Crane-Robinson C., Coles B., Goodwin G.H.
Nucleic Acids Res. 19:6793-6797(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and characterization of the gene coding for murine high-mobility-group protein HMGI-C."
Manfioletti G., Rustighi A., Mantovani F., Goodwin G.H., Giancotti V.
Gene 167:249-253(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Genomic structure and expression of the murine Hmgi-c gene."
Zhou X., Benson K.F., Przybysz K., Liu J., Hou Y., Cherath L., Chada K.
Nucleic Acids Res. 24:4071-4077(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Eye.
[5]"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].
Tissue: Embryo and Limb.
[6]"Phosphorylation of high-mobility group protein A2 by Nek2 kinase during the first meiotic division in mouse spermatocytes."
Di Agostino S., Fedele M., Chieffi P., Fusco A., Rossi P., Geremia R., Sette C.
Mol. Biol. Cell 15:1224-1232(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH NEK2, TISSUE SPECIFICITY.
[7]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L41621 expand/collapse EMBL AC list , L41617, L41618, L41619, L41620 Genomic DNA. Translation: AAC69244.1.
X58380 mRNA. Translation: CAA41270.1.
X99915 expand/collapse EMBL AC list , X99916, X99917, X99918, X99919 Genomic DNA. Translation: CAA68187.1.
AK028346 mRNA. Translation: BAC25896.1.
AK142059 mRNA. Translation: BAE24928.1.
BC052158 mRNA. Translation: AAH52158.1.
BC085085 mRNA. Translation: AAH85085.1.
CCDSCCDS36073.1.
PIRJC4575.
RefSeqNP_034571.1. NM_010441.2.
UniGeneMm.157190.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200341. 7 interactions.
IntActP52927. 5 interactions.
MINTMINT-1847926.
STRING10090.ENSMUSP00000072556.

PTM databases

PhosphoSiteP52927.

Proteomic databases

PaxDbP52927.
PRIDEP52927.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072777; ENSMUSP00000072556; ENSMUSG00000056758.
GeneID15364.
KEGGmmu:15364.
UCSCuc007hfb.1. mouse.

Organism-specific databases

CTD8091.
MGIMGI:101761. Hmga2.

Phylogenomic databases

eggNOGNOG295015.
GeneTreeENSGT00730000111387.
HOGENOMHOG000076308.
HOVERGENHBG051913.
InParanoidP52927.
KOK09283.
OMANSIKRSH.
OrthoDBEOG7QRQXW.
PhylomeDBP52927.
TreeFamTF351623.

Gene expression databases

BgeeP52927.
CleanExMM_HMGA2.
GenevestigatorP52927.

Family and domain databases

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

Other

ChiTaRSHMGA2. mouse.
NextBio287988.
PROP52927.
SOURCESearch...

Entry information

Entry nameHMGA2_MOUSE
AccessionPrimary (citable) accession number: P52927
Secondary accession number(s): Q3UQW0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot