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Protein

High mobility group protein HMG-I/HMG-Y

Gene

Hmga1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi21 – 3111A.T hook 1Add
BLAST
DNA bindingi53 – 6311A.T hook 2Add
BLAST
DNA bindingi78 – 8912A.T hook 3Add
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
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
Gene namesi
Name:Hmga1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi628699. Hmga1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 107106High mobility group protein HMG-I/HMG-YPRO_0000206710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei7 – 71N6-acetyllysineBy similarity
Modified residuei15 – 151N6-acetyllysineBy similarity
Modified residuei26 – 261Asymmetric dimethylarginine; alternateBy similarity
Modified residuei26 – 261Omega-N-methylarginine; alternateBy similarity
Modified residuei26 – 261Symmetric dimethylarginine; alternateBy similarity
Modified residuei36 – 361Phosphoserine; by HIPK2 and CDC2By similarity
Modified residuei39 – 391PhosphothreonineBy similarity
Modified residuei44 – 441PhosphoserineBy similarity
Modified residuei49 – 491PhosphoserineBy similarity
Modified residuei53 – 531Phosphothreonine; by HIPK2 and CDC2By similarity
Modified residuei58 – 581Asymmetric dimethylarginine; by PRMT6; alternateBy similarity
Modified residuei58 – 581Omega-N-methylarginine; by PRMT6; alternateBy similarity
Modified residuei60 – 601Asymmetric dimethylarginine; by PRMT6; alternateBy similarity
Modified residuei60 – 601Omega-N-methylarginine; by PRMT6; alternateBy similarity
Modified residuei78 – 781Phosphothreonine; by HIPK2 and CDC2By similarity
Modified residuei99 – 991PhosphoserineBy similarity
Modified residuei102 – 1021PhosphoserineBy similarity
Modified residuei103 – 1031Phosphoserine1 Publication

Post-translational modificationi

Isoforms HMG-I and HMG-Y can be phosphorylated by HIPK2. Phosphorylation may modulate DNA-binding affinity (By similarity).By similarity
Methylation at Arg-58 is mutually exclusive with methylation at Arg-60.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ8K585.
PRIDEiQ8K585.

PTM databases

iPTMnetiQ8K585.
PhosphoSiteiQ8K585.

Interactioni

Subunit structurei

Interacts with HIPK2.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi250659. 1 interaction.
STRINGi10116.ENSRNOP00000000580.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 7725Interaction with HIPK2By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi91 – 10616Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the HMGA family.Curated
Contains 3 A.T hook DNA-binding domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410J4ZT. Eukaryota.
ENOG410Z566. LUCA.
GeneTreeiENSGT00730000111329.
HOGENOMiHOG000076308.
HOVERGENiHBG063451.
InParanoidiQ8K585.
KOiK09282.
OMAiKPQVSAN.
OrthoDBiEOG71CFQJ.
PhylomeDBiQ8K585.
TreeFamiTF351623.

Family and domain databases

InterProiIPR017956. AT_hook_DNA-bd_motif.
IPR000116. HMGA.
IPR031079. HMGA1_mammal.
IPR000637. HMGI/Y_DNA-bd_CS.
[Graphical view]
PANTHERiPTHR23341:SF1. PTHR23341:SF1. 1 hit.
PfamiPF02178. AT_hook. 3 hits.
[Graphical view]
PRINTSiPR00929. ATHOOK.
PR00930. HIGHMOBLTYIY.
SMARTiSM00384. AT_hook. 3 hits.
[Graphical view]
PROSITEiPS00354. HMGI_Y. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform HMG-I (identifier: Q8K585-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSESVSKSSQ PLASKQEKDG TEKRGRGRPR KQPSVSPGTA LVGSQKEPSE
60 70 80 90 100
VPTPKRPRGR PKGSKNKGTA KTRKVTTTPG RKPRGRPKKL EKEEEEGISQ

ESSEEEQ
Length:107
Mass (Da):11,706
Last modified:January 23, 2007 - v3
Checksum:i0F944B183384C10E
GO
Isoform HMG-Y (identifier: Q8K585-2) [UniParc]FASTAAdd to basket

Also known as: HMGA1b

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

Show »
Length:96
Mass (Da):10,709
Checksum:i1C685D17CB68561D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51V → G in AAM33433 (Ref. 2) Curated

Mass spectrometryi

Isoform HMG-I : Molecular mass is 11776.8±1 Da from positions 2 - 106. Determined by MALDI. With 1 acetyl and 2 phosphate groups.1 Publication
Isoform HMG-I : Molecular mass is 11856.8±1 Da from positions 2 - 106. Determined by MALDI. With 1 acetyl and 3 phosphate groups.1 Publication
Isoform HMG-I : Molecular mass is 11791.2±1 Da from positions 2 - 106. Determined by MALDI. With 1 acetyl, 1 methyl and 2 phosphate groups.1 Publication
Isoform HMG-I : Molecular mass is 11871.3±1 Da from positions 2 - 106. Determined by MALDI. With 1 acetyl, 1 methyl and 3 phosphate groups.1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei35 – 4511Missing in isoform HMG-Y. 1 PublicationVSP_016395Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF511040 mRNA. Translation: AAM74157.1.
AF507966 mRNA. Translation: AAM33433.1.
RefSeqiNP_647543.1. NM_139327.1.
XP_006256218.1. XM_006256156.1. [Q8K585-1]
XP_006256219.1. XM_006256157.2. [Q8K585-1]
XP_006256220.1. XM_006256158.2. [Q8K585-1]
XP_006256223.1. XM_006256161.1. [Q8K585-2]
XP_006256224.1. XM_006256162.2. [Q8K585-2]
XP_006256225.1. XM_006256163.2. [Q8K585-2]
UniGeneiRn.228608.

Genome annotation databases

EnsembliENSRNOT00000000580; ENSRNOP00000000580; ENSRNOG00000000488. [Q8K585-1]
GeneIDi117062.
KEGGirno:117062.
UCSCiRGD:628699. rat. [Q8K585-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF511040 mRNA. Translation: AAM74157.1.
AF507966 mRNA. Translation: AAM33433.1.
RefSeqiNP_647543.1. NM_139327.1.
XP_006256218.1. XM_006256156.1. [Q8K585-1]
XP_006256219.1. XM_006256157.2. [Q8K585-1]
XP_006256220.1. XM_006256158.2. [Q8K585-1]
XP_006256223.1. XM_006256161.1. [Q8K585-2]
XP_006256224.1. XM_006256162.2. [Q8K585-2]
XP_006256225.1. XM_006256163.2. [Q8K585-2]
UniGeneiRn.228608.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250659. 1 interaction.
STRINGi10116.ENSRNOP00000000580.

PTM databases

iPTMnetiQ8K585.
PhosphoSiteiQ8K585.

Proteomic databases

PaxDbiQ8K585.
PRIDEiQ8K585.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000000580; ENSRNOP00000000580; ENSRNOG00000000488. [Q8K585-1]
GeneIDi117062.
KEGGirno:117062.
UCSCiRGD:628699. rat. [Q8K585-1]

Organism-specific databases

CTDi3159.
RGDi628699. Hmga1.

Phylogenomic databases

eggNOGiENOG410J4ZT. Eukaryota.
ENOG410Z566. LUCA.
GeneTreeiENSGT00730000111329.
HOGENOMiHOG000076308.
HOVERGENiHBG063451.
InParanoidiQ8K585.
KOiK09282.
OMAiKPQVSAN.
OrthoDBiEOG71CFQJ.
PhylomeDBiQ8K585.
TreeFamiTF351623.

Miscellaneous databases

NextBioi619926.
PROiQ8K585.

Family and domain databases

InterProiIPR017956. AT_hook_DNA-bd_motif.
IPR000116. HMGA.
IPR031079. HMGA1_mammal.
IPR000637. HMGI/Y_DNA-bd_CS.
[Graphical view]
PANTHERiPTHR23341:SF1. PTHR23341:SF1. 1 hit.
PfamiPF02178. AT_hook. 3 hits.
[Graphical view]
PRINTSiPR00929. ATHOOK.
PR00930. HIGHMOBLTYIY.
SMARTiSM00384. AT_hook. 3 hits.
[Graphical view]
PROSITEiPS00354. HMGI_Y. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HMG-I AND HMG-Y), PHOSPHORYLATION, METHYLATION AT ARG-26, MASS SPECTROMETRY.
    Strain: COP.
    Tissue: Prostatic carcinoma.
  2. Claus P.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HMG-I).
    Strain: Sprague-Dawley.
    Tissue: Lung.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHMGA1_RAT
AccessioniPrimary (citable) accession number: Q8K585
Secondary accession number(s): Q8K1F5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.