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P17095 (HMGA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. 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·Alt products·Sequence annotation·Sequences·References·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
Gene names
Name:Hmga1
Synonyms:Hmgi, Hmgiy
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.6

Subcellular location

Nucleus. Chromosome.

Post-translational modification

Isoforms HMG-I and HMG-Y can be phosphorylated by HIPK2. Phosphorylation may modulate DNA-binding affinity By similarity. Ref.5 Ref.6

Methylation at Arg-58 is mutually exclusive with methylation at Arg-60 By similarity.

Sequence similarities

Belongs to the HMGA family.

Contains 3 A.T hook DNA-binding domains.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandDNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of cell proliferation

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

positive regulation of cellular senescence

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

senescence-associated heterochromatin focus assembly

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from sequence or structural similarity. Source: UniProtKB

senescence-associated heterochromatin focus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

peroxisome proliferator activated receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

retinoic acid receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

retinoid X receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform HMG-I (identifier: P17095-2)

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: P17095-1)

Also known as: HMGA1b; HMGI-E;

The sequence of this isoform differs from the canonical sequence as follows:
     35-45: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 107106High mobility group protein HMG-I/HMG-Y
PRO_0000206709

Regions

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

Amino acid modifications

Modified residue21N-acetylserine Ref.5 Ref.13
Modified residue71N6-acetyllysine Ref.13
Modified residue151N6-acetyllysine Ref.13
Modified residue261Asymmetric dimethylarginine; alternate By similarity
Modified residue261Omega-N-methylarginine; alternate By similarity
Modified residue261Symmetric dimethylarginine; alternate By similarity
Modified residue361Phosphoserine; by HIPK2 and CDC2 By similarity
Modified residue391Phosphothreonine By similarity
Modified residue441Phosphoserine
Modified residue491Phosphoserine
Modified residue531Phosphothreonine; by HIPK2 and CDC2 Ref.12
Modified residue581Asymmetric dimethylarginine; by PRMT6; alternate By similarity
Modified residue581Omega-N-methylarginine; by PRMT6; alternate By similarity
Modified residue601Asymmetric dimethylarginine; by PRMT6; alternate By similarity
Modified residue601Omega-N-methylarginine; by PRMT6; alternate By similarity
Modified residue991Phosphoserine Ref.5 Ref.8 Ref.12
Modified residue1021Phosphoserine Ref.5 Ref.8 Ref.9 Ref.11 Ref.12
Modified residue1031Phosphoserine Ref.5 Ref.8 Ref.9 Ref.11 Ref.12

Natural variations

Alternative sequence35 – 4511Missing in isoform HMG-Y.
VSP_012406

Experimental info

Sequence conflict1061E → G in AAK66158. Ref.2
Sequence conflict1061E → G in AAK66159. Ref.2

Sequences

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

Last modified January 23, 2007. Version 4.
Checksum: 4EC39386611959FC

FASTA10711,614
        10         20         30         40         50         60 
MSESGSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE VPTPKRPRGR 

        70         80         90        100 
PKGSKNKGAA KTRKVTTAPG RKPRGRPKKL EKEEEEGISQ ESSEEEQ 

« Hide

Isoform HMG-Y (HMGA1b) (HMGI-E) [UniParc].

Checksum: A77A3FD7CA6C08EC
Show »

FASTA9610,617

References

« Hide 'large scale' references
[1]"Complete murine cDNA sequence, genomic structure, and tissue expression of the high mobility group protein HMG-I(Y)."
Johnson K.R., Lehn D.A., Elton T.S., Barr P.J., Reeves R.
J. Biol. Chem. 263:18338-18342(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HMG-Y).
[2]"Sequence and analysis of the murine Hmgiy (Hmga1) gene locus."
Pedulla M.L., Treff N.R., Resar L.M.S., Reeves R.
Gene 271:51-58(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS HMG-I AND HMG-Y).
Strain: BALB/c.
[3]"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] (ISOFORM HMG-Y).
Strain: C57BL/6J.
Tissue: Embryonic stem cell.
[4]"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] (ISOFORM HMG-I).
Strain: FVB/N.
Tissue: Colon.
[5]"Mass spectrometric analysis of the HMGY protein from Lewis lung carcinoma. Identification of phosphorylation sites."
Ferranti P., Malorni A., Marino G., Pucci P., Goodwin G.H., Manfioletti G., Giancotti V.
J. Biol. Chem. 267:22486-22489(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"High mobility group I (Y) proteins bind HIPK2, a serine-threonine kinase protein which inhibits cell growth."
Pierantoni G.M., Fedele M., Pentimalli F., Benvenuto G., Pero R., Viglietto G., Santoro M., Chiariotti L., Fusco A.
Oncogene 20:6132-6141(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIPK2, PHOSPHORYLATION.
[7]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[8]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(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: Teratocarcinoma.
[9]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[11]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[12]"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 THR-53; SER-99; SER-102 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[13]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-7 AND LYS-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04179 mRNA. Translation: AAA37820.1.
AF285780 Genomic DNA. Translation: AAK66158.1.
AF285780 Genomic DNA. Translation: AAK66159.1.
AK010617 mRNA. Translation: BAB27065.1.
BC013455 mRNA. Translation: AAH13455.1.
CCDSCCDS28564.1. [P17095-2]
CCDS49010.1. [P17095-2]
CCDS50044.1. [P17095-1]
PIRA31895.
RefSeqNP_001020598.1. NM_001025427.3. [P17095-2]
NP_001034445.1. NM_001039356.2. [P17095-2]
NP_001159948.1. NM_001166476.1. [P17095-2]
NP_001159949.1. NM_001166477.1. [P17095-1]
NP_001160007.1. NM_001166535.1. [P17095-2]
NP_001160008.1. NM_001166536.1. [P17095-2]
NP_001160009.1. NM_001166537.1. [P17095-1]
NP_001160011.1. NM_001166539.1. [P17095-1]
NP_001160012.1. NM_001166540.1. [P17095-1]
NP_001160013.1. NM_001166541.1. [P17095-1]
NP_001160014.1. NM_001166542.1. [P17095-1]
NP_057869.2. NM_016660.3. [P17095-2]
UniGeneMm.426212.
Mm.440289.
Mm.4438.

3D structure databases

ProteinModelPortalP17095.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200340. 8 interactions.
DIPDIP-53N.
IntActP17095. 4 interactions.
MINTMINT-1848156.
STRING10090.ENSMUSP00000113015.

PTM databases

PhosphoSiteP17095.

Proteomic databases

PaxDbP17095.
PRIDEP17095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000105046; ENSMUSP00000100667; ENSMUSG00000078249. [P17095-2]
ENSMUST00000114888; ENSMUSP00000110538; ENSMUSG00000046711. [P17095-1]
ENSMUST00000117254; ENSMUSP00000113011; ENSMUSG00000046711. [P17095-2]
ENSMUST00000117600; ENSMUSP00000113068; ENSMUSG00000046711. [P17095-2]
ENSMUST00000118570; ENSMUSP00000114101; ENSMUSG00000046711. [P17095-1]
ENSMUST00000118599; ENSMUSP00000113015; ENSMUSG00000046711. [P17095-2]
ENSMUST00000119486; ENSMUSP00000113916; ENSMUSG00000046711. [P17095-2]
GeneID111241.
15361.
KEGGmmu:111241.
mmu:15361.
UCSCuc008boz.2. mouse. [P17095-2]

Organism-specific databases

CTD111241.
3159.
MGIMGI:96160. Hmga1.

Phylogenomic databases

eggNOGNOG41800.
HOGENOMHOG000076308.
HOVERGENHBG063451.
InParanoidP17095.
KOK09282.
OMAQQEPSEA.
OrthoDBEOG71CFQJ.
PhylomeDBP17095.
TreeFamTF351623.

Gene expression databases

BgeeP17095.
CleanExMM_HMGA1.
GenevestigatorP17095.

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

NextBio287980.
PROP17095.
SOURCESearch...

Entry information

Entry nameHMGA1_MOUSE
AccessionPrimary (citable) accession number: P17095
Secondary accession number(s): Q91WV2, Q924L7, Q924L8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 147 of the entry and version 4 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