Prdm16
entrez
70673
canonical
uniprot
A2A935
canonical
ensembl
ENSMUSG00000039410
resolver
ensp
ENSMUSP00000030902
resolver
ensp
ENSMUSP00000064546
resolver
ensp
ENSMUSP00000101261
resolver
ensp
ENSMUSP00000101262
resolver
ensp
ENSMUSP00000101263
resolver
ensp
ENSMUSP00000265170
resolver
ensp
ENSMUSP00000265172
resolver
ensp
ENSMUSP00000265173
resolver
ensp
ENSMUSP00000265174
resolver
ensp
ENSMUSP00000331489
resolver
enst
ENSMUST00000105636
resolver
enst
ENSMUST00000105637
resolver
enst
ENSMUST00000105638
resolver
genesymbol
Prdm16
resolver
genesymbol_syn
Kiaa1675
resolver
genesymbol_syn
Mel1
resolver
uniprot
A2A931
resolver
uniprot
A2A933
resolver
uniprot
A2A934
resolver
uniprot
Q69ZD6
resolver
uniprot
Q6PB79
resolver
uniprot
Q7TPF4
resolver
uniprot
Q8BNF5
resolver
uniprot_entry
A2A931_MOUSE
resolver
uniprot_entry
A2A933_MOUSE
resolver
uniprot_entry
A2A934_MOUSE
resolver
uniprot_entry
PRD16_MOUSE
resolver
uniprot_entry
Q8BNF5_MOUSE
resolver
uniprot_sec
Q69ZD6
resolver
uniprot_sec
Q6PB79
resolver
uniprot_sec
Q7TPF4
resolver
amino_acid_sequence
MRSKARARKLAKSDGDVVNNMYEPDPDLLAGQSAEEETEDGILSPIPMGPPSPFPTSEDFTPKEGSPYEAPVYIPEDIPIPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYVVTPRAALKEADFGWEMLTDTEVSSQESCIKKQISEDLGSEKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLVHVKEGAYSLGVMAPSLDEDPTFRCDECDELFQCRLDLRRHKKYACSSAGAQLYEGLGEELKPEGLGVGSDGQAHECKDCERMFPNKYSLEQHMIVHTEEREYKCDQCPKAFNWKSNLIRHQMSHDSGKRFECENCVKVFTDPSNLQRHIRSQHVGARAHACPDCGKTFATSSGLKQHKHIHSTVKPFICEVCHKSYTQFSNLCRHKRMHADCRTQIKCKDCGQMFSTTSSLNKHRRFCEGKNHYTPGSIFTPGLPLTPSPMMDKTKPSPTLNHGGLGFSEYFPSRPHPGSLPFSAAPPAFPALTPGFPGIFPPSLYPRPPLLPPTPLLKSPLNHAQDAKLPSPLGNPALPLVSAVSNSSQGATAATGSEEKFDGRLEDAYAEKVKNRSPDMSDGSDFEDINTTTGTDLDTTTGTGSDLDSDLDSDRDKGKDKGKPVESKPEFGGASVPPGAMNSVAEVPAFYSQHSFFPPPEEQLLTASGAAGDSIKAIASIAEKYFGPGFMSMQEKKLGSLPYHSVFPFQFLPNFPHSLYPFTDRALAHNLLVKAEPKSPRDALKVGGPSAECPFDLTTKPKEAKPALLAPKVPLIPSSGEEQPLDLSIGSRARASQNGGGREPRKNHVYGERKPGVSEGLPKVCPAQLPQQPSLHYAKPSPFFMDPIYRVEKRKVADPVGVLKEKYLRPSPLLFHPQMSAIETMTEKLESFAAMKADSGSSLQPLPHHPFNFRSPPPTLSDPILRKGKERYTCRYCGKIFPRSANLTRHLRTHTGEQPYRCKYCDRSFSISSNLQRHVRNIHNKEKPFKCHLCNRCFGQQTNLDRHLKKHEHEGAPVSQHSGVLTNHLGTSASSPTSESDNHALLDEKEDSYFSEIRNFIANSEMNQASTRMDKRPEIQDLDSNPPCPGSASAKPEDVEEEEEEELEEEDDDSLAGKSQEDTVSPTPEPQGVYEDEEDEEPPSLTMGFDHTRRCVEERGGGLLALEPTPTFGKGLDLRRAAEEAFEVKDVLNSTLDSEVLKQTLYRQAKNQAYAMMLSLSEDTPLHAPSQSSLDAWLNITGPSSESGAFNPINHL
uniprot
proteins
ec_number
2.1.1.367
uniprot
proteins
function
FUNCTION: Transcription regulator that acts both as a histone methyltransferase or chromatin adapter, depending on the context (PubMed:18483224, PubMed:22939622). In the cytoplasm, acts as a histone methyltransferase, which catalyzes monomethylation of 'Lys-9' of free histone H3 (H3K9me1) during translation (PubMed:22939622). Monomethylated histone H3 is then transported to the nucleus and incorporated into nucleosomes where SUV39H methyltransferases (SUV39H1 and SUV39H2) use it as a substrate to catalyze histone H3 'Lys-9' trimethylation (H3K9me3) (PubMed:22939622). Probably one of the primary histone methyltransferases along with MECOM/PRDM3 that direct cytoplasmic H3K9me1 methylation (PubMed:22939622). In the nucleus, acts as a key chromatin adapter that mediates differentiation of brown and beige adipocytes, which are specialized in dissipating chemical energy in the form of heat in response to cold or excess feeding (PubMed:17618855, PubMed:18483224, PubMed:18719582, PubMed:19641492, PubMed:21123942, PubMed:22033933, PubMed:22405074, PubMed:24196706, PubMed:24703692, PubMed:28930673, PubMed:30893596). Following recruitment to chromatin by PPARG nuclear receptor, promotes. differentiation of myoblastic precursors into brown adipose cells (PubMed:18719582, PubMed:19641492). Mechanistically, acts by mediating recruitment of (1) EHMT1 histone methyltransferase, thereby inhibiting the expression of white adipose-selective genes or (2) mediator complex, activating genes that are highly expressed in brown adipocytes, such as UCP1, PPARA, and PPARGC1A (PubMed:24196706, PubMed:24703692, PubMed:25644604, PubMed:25644605). Also mediates differentiation of beige adipocytes from white adipose cells following recruitment by PPARG (PubMed:21123942, PubMed:22405074). In addition to adipocyte differentiation, also involved in tolerance to gut microbiota: following recruitment to chromatin by RORgammaT (RORC) in a subset of antigen-presenting cells, promotes differentiation of peripherally-induced regulatory T-cells (pTreg), which suppress inflammatory responses to commensal microorganisms (PubMed:40228524). Also required in adult heart to preserve mitochondrial function and inhibit hypertrophy with advanced age (PubMed:33086060). {ECO:0000269|PubMed:17618855, ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:21123942, ECO:0000269|PubMed:22033933, ECO:0000269|PubMed:22405074, ECO:0000269|PubMed:22939622, ECO:0000269|PubMed:24196706, ECO:0000269|PubMed:24703692, ECO:0000269|PubMed:25644604, ECO:0000269|PubMed:25644605, ECO:0000269|PubMed:28930673, ECO:0000269|PubMed:30893596, ECO:0000269|PubMed:33086060, ECO:0000269|PubMed:40228524}.
uniprot
proteins
mass_dalton
140858
uniprot
proteins
mutagenesis
MUTAGEN 44; /note="S->A: Abolished interaction with PIN1; when associated with A-52, A-61, A-66 and A-116."; /evidence="ECO:0000269|PubMed:30893596"; MUTAGEN 52; /note="S->A: Abolished interaction with PIN1; when associated with A-44, A-61, A-66 and A-116."; /evidence="ECO:0000269|PubMed:30893596"; MUTAGEN 61; /note="T->A: Abolished interaction with PIN1; when associated with A-44, A-52, A-66 and A-116."; /evidence="ECO:0000269|PubMed:30893596"; MUTAGEN 66; /note="S->A: Abolished interaction with PIN1; when associated with A-44, A-52, A-61 and A-116."; /evidence="ECO:0000269|PubMed:30893596"; MUTAGEN 116; /note="T->A: Abolished interaction with PIN1; when associated with A-44, A-52, A-61 and A-66."; /evidence="ECO:0000269|PubMed:30893596"; MUTAGEN 122; /note="K->R: Abolished ubiquitination by the CRL2(APPBP2) complex; when associated with R-322, R-579, R-779, R-791 and R-833."; /evidence="ECO:0000269|PubMed:35978186"; MUTAGEN 269; /note="K->R: Does not affect sumoylation by CBX4."; /evidence="ECO:0000269|PubMed:29539416"; MUTAGEN 322; /note="K->R: Abolished ubiquitination by the CRL2(APPBP2) complex; when associated with R-122, R-579, R-779, R-791 and R-833."; /evidence="ECO:0000269|PubMed:35978186"; MUTAGEN 336; /note="K->Q: Mimics acetylation; no effect."; /evidence="ECO:0000269|PubMed:35075301"; MUTAGEN 579; /note="K->R: Abolished ubiquitination by the CRL2(APPBP2) complex; when associated with R-122, R-322, R-779, R-791 and R-833."; /evidence="ECO:0000269|PubMed:35978186"; MUTAGEN 753; /note="K->R: Does not affect sumoylation by CBX4."; /evidence="ECO:0000269|PubMed:29539416"; MUTAGEN 779; /note="K->R: Abolished ubiquitination by the CRL2(APPBP2) complex; when associated with R-122, R-322, R-579, R-791 and R-833."; /evidence="ECO:0000269|PubMed:35978186"; MUTAGEN 791; /note="K->R: Abolished ubiquitination by the CRL2(APPBP2) complex; when associated with R-122, R-322, R-579, R-779 and R-833."; /evidence="ECO:0000269|PubMed:35978186"; MUTAGEN 805..806; /note="DL->AS: Loss of interaction with CTBP1 and CTBP2 and loss of repression of white adipose tissue-specific genes."; /evidence="ECO:0000269|PubMed:18483224"; MUTAGEN 833; /note="K->R: Abolished ubiquitination by the CRL2(APPBP2) complex; when associated with R-122, R-322, R-579, R-779 and R-791."; /evidence="ECO:0000269|PubMed:35978186"; MUTAGEN 915; /note="K->Q: Mimics acetylation; impaired ability to associate with PPARG."; /evidence="ECO:0000269|PubMed:35075301"; MUTAGEN 915; /note="K->R: Abolished sumoylation by CBX4, leading to ubiquitination and degradation."; /evidence="ECO:0000269|PubMed:29539416"; MUTAGEN 996; /note="R->Q: Loss of DNA-binding activity but no effect on PRDM16-mediated BAT gene transcription activation."; /evidence="ECO:0000269|PubMed:17618855
uniprot
proteins
post_translational_modification
PTM: Acetylation at Lys-915 py EP300/p300 abolishes its association with PPARG and ability to promote differentiation of brown adipocytes (PubMed:35075301). Deacetylated by HDAC6 (PubMed:35075301). {ECO:0000269|PubMed:35075301}.; PTM: Phosphorylated; phosphorylation promotes interaction with PIN1 and degradation. {ECO:0000269|PubMed:30893596}.; PTM: Ubiquitinated by the CRL2(APPBP2) complex, leading to its degradation by the proteasome (PubMed:35978186). Interaction with EHMT1 promotes PRDM16 stability by preventing interaction with APPBP2 and subsequent ubiquitination (PubMed:35978186). {ECO:0000269|PubMed:35978186}.; PTM: Sumoylated by CBX4, promoting its stabilization by preventing PRDM16 ubiquitination and degradation. {ECO:0000269|PubMed:29539416}.
uniprot
proteins
protein_family
PRDM16 family
uniprot
proteins
pubmed
12816872
uniprot
proteins
pubmed
15368895
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17467076
uniprot
proteins
pubmed
17618855
uniprot
proteins
pubmed
18483224
uniprot
proteins
pubmed
18719582
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19641492
uniprot
proteins
pubmed
21123942
uniprot
proteins
pubmed
22033933
uniprot
proteins
pubmed
22405074
uniprot
proteins
pubmed
22939622
uniprot
proteins
pubmed
23473036
uniprot
proteins
pubmed
23768516
uniprot
proteins
pubmed
24196706
uniprot
proteins
pubmed
24439384
uniprot
proteins
pubmed
24703692
uniprot
proteins
pubmed
25578880
uniprot
proteins
pubmed
25644604
uniprot
proteins
pubmed
25644605
uniprot
proteins
pubmed
28930673
uniprot
proteins
pubmed
29539416
uniprot
proteins
pubmed
30893596
uniprot
proteins
pubmed
33086060
uniprot
proteins
pubmed
35075301
uniprot
proteins
pubmed
35978186
uniprot
proteins
pubmed
40228524
uniprot
proteins
sequence_length
1275
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:24196706}. Chromosome {ECO:0000269|PubMed:24196706, ECO:0000269|PubMed:25644604}. Cytoplasm {ECO:0000250|UniProtKB:Q9HAZ2}.
uniprot
proteins