CPLM-004535

Genbank Nucleotide ID

High mobility group protein HMG-I/HMG-Y

Protein Synonyms/Alias

HMG-I(Y); High mobility group AT-hook protein 1; High mobility group protein A1; High mobility group protein R

Homo sapiens (Human)

Position	Peptide	Type	References
7	*MSESSSKSSQPLAS	acetylation	[1]
7	*MSESSSKSSQPLAS	ubiquitination	[2]
15	SSQPLASKQEKDGTE	acetylation	[1, 3]
15	SSQPLASKQEKDGTE	ubiquitination	[4]
31	RGRGRPRKQPPVSPG	methylation	[5]
31	RGRGRPRKQPPVSPG	ubiquitination	[4]
46	TALVGSQKEPSEVPT	methylation	[6]
46	TALVGSQKEPSEVPT	ubiquitination	[4]
55	PSEVPTPKRPRGRPK	methylation	[5]
65	RGRPKGSKNKGAAKT	acetylation	[7, 8]
65	RGRPKGSKNKGAAKT	methylation	[6]
67	RPKGSKNKGAAKTRK	acetylation	[9]
67	RPKGSKNKGAAKTRK	methylation	[6]
71	SKNKGAAKTRKTTTT	acetylation	[7, 8]
74	KGAAKTRKTTTTPGR	acetylation	[9]
74	KGAAKTRKTTTTPGR	methylation	[6]
92	GRPKKLEKEEEEGIS	methylation	[6]

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[2] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[3] Acetylation and phosphorylation of high-mobility group A1 proteins in PC-3 human tumor cells.
Jiang X, Wang Y.
Biochemistry. 2006 Jun 13;45(23):7194-201. [PMID: 16752910]
[4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[5] High mobility group proteins and their post-translational modifications.
Zhang Q, Wang Y.
Biochim Biophys Acta. 2008 Sep;1784(9):1159-66. [PMID: 18513496]
[6] Dynamic and differential in vivo modifications of the isoform HMGA1a and HMGA1b chromatin proteins.
Edberg DD, Adkins JN, Springer DL, Reeves R.
J Biol Chem. 2005 Mar 11;280(10):8961-73. [PMID: 15591590]
[7] Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome.
Munshi N, Merika M, Yie J, Senger K, Chen G, Thanos D.
Mol Cell. 1998 Oct;2(4):457-67. [PMID: 9809067]
[8] Coordination of a transcriptional switch by HMGI(Y) acetylation.
Munshi N, Agalioti T, Lomvardas S, Merika M, Chen G, Thanos D.
Science. 2001 Aug 10;293(5532):1133-6. [PMID: 11498590]
[9] A quantitative study on the in vitro and in vivo acetylation of high mobility group A1 proteins.
Zhang Q, Zhang K, Zou Y, Perna A, Wang Y.
J Am Soc Mass Spectrom. 2007 Sep;18(9):1569-78. [PMID: 17627840]

Functional Description

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.

DNA_BIND 21 31 A.T hook 1.
DNA_BIND 53 63 A.T hook 2.
DNA_BIND 78 89 A.T hook 3.
REGION 53 77 Interaction with HIPK2 (By similarity).
MOD_RES 2 2 N-acetylserine (By similarity).
MOD_RES 15 15 N6-acetyllysine.
MOD_RES 26 26 Asymmetric dimethylarginine; in isoform
MOD_RES 26 26 Omega-N-methylarginine; in isoform HMG-I;
MOD_RES 26 26 Symmetric dimethylarginine; in isoform
MOD_RES 36 36 Phosphoserine; by HIPK2 and CDC2; in
MOD_RES 39 39 Phosphothreonine.
MOD_RES 44 44 Phosphoserine.
MOD_RES 49 49 Phosphoserine.
MOD_RES 53 53 Phosphothreonine; by HIPK2 and CDC2; in
MOD_RES 58 58 Asymmetric dimethylarginine; by PRMT6;
MOD_RES 58 58 Omega-N-methylarginine; by PRMT6;
MOD_RES 60 60 Asymmetric dimethylarginine; by PRMT6;
MOD_RES 60 60 Omega-N-methylarginine; by PRMT6;
MOD_RES 78 78 Phosphothreonine; by HIPK2 and CDC2; in
MOD_RES 99 99 Phosphoserine; in isoform HMG-I and
MOD_RES 102 102 Phosphoserine; by CK; in isoform HMG-I
MOD_RES 103 103 Phosphoserine; by CK; in isoform HMG-I

3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement; Chromosome; Complete proteome; Direct protein sequencing; DNA-binding; Host-virus interaction; Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0035985; C:senescence-associated heterochromatin focus; IDA:UniProtKB.
GO:0005667; C:transcription factor complex; TAS:UniProtKB.
GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:UniProtKB.
GO:0003680; F:AT DNA binding; TAS:UniProtKB.
GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:UniProtKB.
GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IMP:UniProtKB.
GO:0042975; F:peroxisome proliferator activated receptor binding; IDA:UniProtKB.
GO:0046965; F:retinoid X receptor binding; IDA:UniProtKB.
GO:0003700; F:sequence-specific DNA binding transcription factor activity; IMP:UniProtKB.
GO:0006284; P:base-excision repair; IDA:UniProtKB.
GO:0006268; P:DNA unwinding involved in replication; NAS:UniProtKB.
GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO:0031936; P:negative regulation of chromatin silencing; TAS:UniProtKB.
GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:UniProtKB.
GO:0006337; P:nucleosome disassembly; TAS:UniProtKB.
GO:0090402; P:oncogene-induced senescence; IDA:UniProtKB.
GO:2000774; P:positive regulation of cellular senescence; IMP:UniProtKB.
GO:0006461; P:protein complex assembly; TAS:UniProtKB.
GO:0009615; P:response to virus; IEP:UniProtKB.
GO:0035986; P:senescence-associated heterochromatin focus assembly; IDA:UniProtKB.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR020478; AT_hook-like.
IPR017956; AT_hook_DNA-bd_motif.
IPR000116; HMGI/HMGY.
IPR000637; HMGI/Y_DNA-bd_CS.

PR00929; ATHOOK.
PR00930; HIGHMOBLTYIY.