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P17096

- HMGA1_HUMAN

UniProt

P17096 - HMGA1_HUMAN

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Protein

High mobility group protein HMG-I/HMG-Y

Gene

HMGA1

Organism
Homo sapiens (Human)
Status
Reviewed - 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.

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

  1. 5'-deoxyribose-5-phosphate lyase activity Source: UniProtKB
  2. AT DNA binding Source: UniProtKB
  3. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB
  4. DNA binding Source: ProtInc
  5. enzyme binding Source: UniProtKB
  6. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  7. peroxisome proliferator activated receptor binding Source: UniProtKB
  8. retinoic acid receptor binding Source: UniProtKB
  9. retinoid X receptor binding Source: UniProtKB
  10. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  11. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. base-excision repair Source: UniProtKB
  2. DNA catabolic process, endonucleolytic Source: GOC
  3. DNA unwinding involved in DNA replication Source: UniProtKB
  4. establishment of integrated proviral latency Source: Reactome
  5. negative regulation of cell proliferation Source: UniProtKB
  6. negative regulation of chromatin silencing Source: UniProtKB
  7. negative regulation of transcription, DNA-templated Source: UniProtKB
  8. nucleosome disassembly Source: UniProtKB
  9. oncogene-induced cell senescence Source: UniProtKB
  10. positive regulation of cellular senescence Source: UniProtKB
  11. positive regulation of transcription, DNA-templated Source: UniProtKB
  12. protein complex assembly Source: UniProtKB
  13. regulation of transcription, DNA-templated Source: ProtInc
  14. response to virus Source: UniProtKB
  15. senescence-associated heterochromatin focus assembly Source: UniProtKB
  16. transcription, DNA-templated Source: UniProtKB-KW
  17. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
REACT_6866. Autointegration results in viral DNA circles.
REACT_6918. Integration of provirus.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_8990. Integration of viral DNA into host genomic DNA.
REACT_9058. 2-LTR circle formation.
REACT_9406. APOBEC3G mediated resistance to HIV-1 infection.
SignaLinkiP17096.

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
High mobility group protein R
Gene namesi
Name:HMGA1
Synonyms:HMGIY
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:5010. HMGA1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. focal adhesion Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. senescence-associated heterochromatin focus Source: UniProtKB
  6. transcription factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving HMGA1 is found in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24) with RAD51B.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi26 – 261R → A: Does not affect methylation by PRMT6. 1 Publication
Mutagenesisi58 – 581R → A: Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-60. 1 Publication
Mutagenesisi60 – 601R → A: Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-58. 1 Publication

Organism-specific databases

PharmGKBiPA35094.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 107106High mobility group protein HMG-I/HMG-YPRO_0000206708Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei7 – 71N6-acetyllysineBy similarity
Modified residuei15 – 151N6-acetyllysine1 Publication
Modified residuei26 – 261Asymmetric dimethylarginine; alternate2 Publications
Modified residuei26 – 261Omega-N-methylarginine; alternate2 Publications
Modified residuei26 – 261Symmetric dimethylarginine; alternate2 Publications
Modified residuei36 – 361Phosphoserine; by HIPK2 and CDC25 Publications
Modified residuei39 – 391Phosphothreonine1 Publication
Modified residuei44 – 441Phosphoserine2 Publications
Modified residuei49 – 491Phosphoserine1 Publication
Modified residuei53 – 531Phosphothreonine; by HIPK2 and CDC24 Publications
Modified residuei58 – 581Asymmetric dimethylarginine; by PRMT6; alternate1 Publication
Modified residuei58 – 581Omega-N-methylarginine; by PRMT6; alternate1 Publication
Modified residuei60 – 601Asymmetric dimethylarginine; by PRMT6; alternate1 Publication
Modified residuei60 – 601Omega-N-methylarginine; by PRMT6; alternate1 Publication
Modified residuei78 – 781Phosphothreonine; by HIPK2 and CDC21 Publication
Modified residuei99 – 991Phosphoserine6 Publications
Modified residuei102 – 1021Phosphoserine; by CK6 Publications
Modified residuei103 – 1031Phosphoserine; by CK5 Publications

Post-translational modificationi

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.9 Publications
HMG-Y is not methylated.
Methylation at Arg-58 is mutually exclusive with methylation at Arg-60.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP17096.
PaxDbiP17096.
PRIDEiP17096.

PTM databases

PhosphoSiteiP17096.

Expressioni

Gene expression databases

BgeeiP17096.
CleanExiHS_HMGA1.
ExpressionAtlasiP17096. baseline and differential.
GenevestigatoriP17096.

Organism-specific databases

HPAiCAB032200.

Interactioni

Subunit structurei

Interacts with HIPK2 (By similarity). Interacts with HIV-1 pre-integration complex.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PRMT6Q96LA84EBI-746854,EBI-912440

Protein-protein interaction databases

BioGridi109402. 70 interactions.
DIPiDIP-29687N.
IntActiP17096. 39 interactions.
MINTiMINT-262941.
STRINGi9606.ENSP00000308227.

Structurei

Secondary structure

1
107
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi53 – 553

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EZDNMR-A51-71[»]
2EZENMR-A51-75[»]
2EZFNMR-A80-89[»]
2EZGNMR-A80-89[»]
DisProtiDP00040.
ProteinModelPortaliP17096.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiNOG41800.
GeneTreeiENSGT00730000111329.
HOGENOMiHOG000076308.
HOVERGENiHBG063451.
InParanoidiP17096.
KOiK09282.
OMAiQQEPSEA.
TreeFamiTF351623.

Family and domain databases

InterProiIPR020478. AT_hook-like.
IPR017956. AT_hook_DNA-bd_motif.
IPR000116. HMGI/HMGY.
IPR000637. HMGI/Y_DNA-bd_CS.
[Graphical view]
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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform HMG-I (identifier: P17096-1) [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
MSESSSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE
60 70 80 90 100
VPTPKRPRGR PKGSKNKGAA KTRKTTTTPG RKPRGRPKKL EKEEEEGISQ

ESSEEEQ
Length:107
Mass (Da):11,676
Last modified:January 23, 2007 - v3
Checksum:iE9C4E3F2200914B8
GO
Isoform HMG-Y (identifier: P17096-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:96
Mass (Da):10,679
Checksum:iB82DCAA29E6D18FD
GO
Isoform HMG-R (identifier: P17096-3) [UniParc]FASTAAdd to Basket

Also known as: HMGA1c

The sequence of this isoform differs from the canonical sequence as follows:
     66-107: NKGAAKTRKT...ISQESSEEEQ → KNWRRRKRRA...RIHTCPPGQG

Show »
Length:179
Mass (Da):19,694
Checksum:i91E56E235C504AAA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071Q → QQQ AA sequence (PubMed:2920035)Curated

Mass spectrometryi

Isoform HMG-I : Molecular mass is 11750±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl and 2 phosphate groups.1 Publication
Isoform HMG-I : Molecular mass is 11828±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl and 3 phosphate groups.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei35 – 4511Missing in isoform HMG-Y. 3 PublicationsVSP_002182Add
BLAST
Alternative sequencei66 – 10742NKGAA…SEEEQ → KNWRRRKRRASRRSPRRRSS DPCVPPAPHWRSSFLLGLDS FAPLPPPPPLPQAHHHHRLW PPPPSSTCALTTTLHSTPAA AGLPWAEWGAVFPWPQFPAP PAHPRIHTCPPGQG in isoform HMG-R. 1 PublicationVSP_018084Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4788.1. [P17096-2]
CCDS4789.1. [P17096-1]
PIRiA32794.
RefSeqiNP_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]
UniGeneiHs.518805.
Hs.703764.

Genome annotation databases

EnsembliENST00000311487; ENSP00000308227; ENSG00000137309. [P17096-1]
ENST00000347617; ENSP00000288245; ENSG00000137309. [P17096-2]
ENST00000374116; ENSP00000363230; ENSG00000137309. [P17096-2]
ENST00000401473; ENSP00000385693; ENSG00000137309. [P17096-2]
ENST00000447654; ENSP00000399888; ENSG00000137309. [P17096-1]
GeneIDi3159.
KEGGihsa:3159.
UCSCiuc003oit.3. human. [P17096-1]

Polymorphism databases

DMDMi123377.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4788.1. [P17096-2 ]
CCDS4789.1. [P17096-1 ]
PIRi A32794.
RefSeqi NP_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 ]
UniGenei Hs.518805.
Hs.703764.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EZD NMR - A 51-71 [» ]
2EZE NMR - A 51-75 [» ]
2EZF NMR - A 80-89 [» ]
2EZG NMR - A 80-89 [» ]
DisProti DP00040.
ProteinModelPortali P17096.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109402. 70 interactions.
DIPi DIP-29687N.
IntActi P17096. 39 interactions.
MINTi MINT-262941.
STRINGi 9606.ENSP00000308227.

PTM databases

PhosphoSitei P17096.

Polymorphism databases

DMDMi 123377.

Proteomic databases

MaxQBi P17096.
PaxDbi P17096.
PRIDEi P17096.

Protocols and materials databases

DNASUi 3159.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311487 ; ENSP00000308227 ; ENSG00000137309 . [P17096-1 ]
ENST00000347617 ; ENSP00000288245 ; ENSG00000137309 . [P17096-2 ]
ENST00000374116 ; ENSP00000363230 ; ENSG00000137309 . [P17096-2 ]
ENST00000401473 ; ENSP00000385693 ; ENSG00000137309 . [P17096-2 ]
ENST00000447654 ; ENSP00000399888 ; ENSG00000137309 . [P17096-1 ]
GeneIDi 3159.
KEGGi hsa:3159.
UCSCi uc003oit.3. human. [P17096-1 ]

Organism-specific databases

CTDi 3159.
GeneCardsi GC06P037284.
HGNCi HGNC:5010. HMGA1.
HPAi CAB032200.
MIMi 600701. gene.
neXtProti NX_P17096.
PharmGKBi PA35094.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG41800.
GeneTreei ENSGT00730000111329.
HOGENOMi HOG000076308.
HOVERGENi HBG063451.
InParanoidi P17096.
KOi K09282.
OMAi QQEPSEA.
TreeFami TF351623.

Enzyme and pathway databases

Reactomei REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
REACT_6866. Autointegration results in viral DNA circles.
REACT_6918. Integration of provirus.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_8990. Integration of viral DNA into host genomic DNA.
REACT_9058. 2-LTR circle formation.
REACT_9406. APOBEC3G mediated resistance to HIV-1 infection.
SignaLinki P17096.

Miscellaneous databases

ChiTaRSi HMGA1. human.
GeneWikii HMGA1.
GenomeRNAii 3159.
NextBioi 12514.
PROi P17096.
SOURCEi Search...

Gene expression databases

Bgeei P17096.
CleanExi HS_HMGA1.
ExpressionAtlasi P17096. baseline and differential.
Genevestigatori P17096.

Family and domain databases

InterProi IPR020478. AT_hook-like.
IPR017956. AT_hook_DNA-bd_motif.
IPR000116. HMGI/HMGY.
IPR000637. HMGI/Y_DNA-bd_CS.
[Graphical view ]
Pfami PF02178. AT_hook. 3 hits.
[Graphical view ]
PRINTSi PR00929. ATHOOK.
PR00930. HIGHMOBLTYIY.
SMARTi SM00384. AT_hook. 3 hits.
[Graphical view ]
PROSITEi PS00354. HMGI_Y. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. 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.

Entry informationi

Entry nameiHMGA1_HUMAN
AccessioniPrimary (citable) accession number: P17096
Secondary accession number(s): P10910, Q5T6U9, Q9UKB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 176 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3