HMGA1
entrez
3159
canonical
uniprot
P17096
canonical
ensembl
ENSG00000137309
resolver
ensp
ENSP00000288245
resolver
ensp
ENSP00000308227
resolver
ensp
ENSP00000363230
resolver
ensp
ENSP00000385693
resolver
ensp
ENSP00000399888
resolver
ensp
ENSP00000515486
resolver
ensp
ENSP00000543238
resolver
ensp
ENSP00000543244
resolver
ensp
ENSP00000594563
resolver
ensp
ENSP00000594580
resolver
ensp
ENSP00000633418
resolver
ensp
ENSP00000728546
resolver
enst
ENST00000703808
resolver
enst
ENST00000873185
resolver
enst
ENST00000924521
resolver
genesymbol
HMGA1
resolver
genesymbol_syn
HMGIY
resolver
hgnc
HGNC:5010
resolver
uniprot
A0A994J434
resolver
uniprot
P10910
resolver
uniprot
Q5T6U8
resolver
uniprot
Q5T6U9
resolver
uniprot
Q9UKB0
resolver
uniprot_entry
A0A994J434_HUMAN
resolver
uniprot_entry
HMGA1_HUMAN
resolver
uniprot_entry
Q5T6U8_HUMAN
resolver
uniprot_sec
P10910
resolver
uniprot_sec
Q5T6U9
resolver
uniprot_sec
Q9UKB0
resolver
amino_acid_sequence
MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving HMGA1 is found in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24) with RAD51B. {ECO:0000269|PubMed:11978964}.
uniprot
proteins
function
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.
uniprot
proteins
mass_dalton
11676
uniprot
proteins
mutagenesis
MUTAGEN 26; /note="R->A: Does not affect methylation by PRMT6."; /evidence="ECO:0000269|PubMed:16159886"; MUTAGEN 58; /note="R->A: Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-60."; /evidence="ECO:0000269|PubMed:16159886"; MUTAGEN 60; /note="R->A: Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-58."; /evidence="ECO:0000269|PubMed:16159886
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:12653562, ECO:0000269|PubMed:15835918}.; PTM: HMG-Y is not methylated.; PTM: Methylation at Arg-58 is mutually exclusive with methylation at Arg-60. {ECO:0000269|PubMed:16159886}.
uniprot
proteins
protein_family
HMGA family
uniprot
proteins
pubmed
10428834
uniprot
proteins
pubmed
11978964
uniprot
proteins
pubmed
12653562
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15835918
uniprot
proteins
pubmed
16157300
uniprot
proteins
pubmed
16159886
uniprot
proteins
pubmed
1692833
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
17960875
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2505228
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
2701943
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28190768
uniprot
proteins
pubmed
2920035
uniprot
proteins
pubmed
3619901
uniprot
proteins
pubmed
8414980
uniprot
proteins
pubmed
9253416
uniprot
proteins
sequence_length
107
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Chromosome.
uniprot
proteins