GenomeNet

Database: UniProt
Entry: Q9HAZ2
LinkDB: Q9HAZ2
Original site: Q9HAZ2 
ID   PRD16_HUMAN             Reviewed;        1276 AA.
AC   Q9HAZ2; A6NHQ8; B1AJP7; B1AJP8; B1AJP9; B1WB48; Q8WYJ9; Q9C0I8;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 3.
DT   10-APR-2019, entry version 178.
DE   RecName: Full=Histone-lysine N-methyltransferase PRDM16 {ECO:0000305};
DE            EC=2.1.1.43 {ECO:0000250|UniProtKB:A2A935};
DE   AltName: Full=PR domain zinc finger protein 16 {ECO:0000305};
DE   AltName: Full=PR domain-containing protein 16 {ECO:0000305};
DE   AltName: Full=Transcription factor MEL1 {ECO:0000305};
DE            Short=MDS1/EVI1-like gene 1 {ECO:0000303|PubMed:11050005};
GN   Name=PRDM16 {ECO:0000312|HGNC:HGNC:14000};
GN   Synonyms=KIAA1675 {ECO:0000312|EMBL:BAB21766.2},
GN   MEL1 {ECO:0000303|PubMed:11050005}, PFM13;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT PRO-533, CHROMOSOMAL
RP   TRANSLOCATION, DISEASE, AND TISSUE SPECIFICITY.
RX   PubMed=11050005;
RA   Mochizuki N., Shimizu S., Nagasawa T., Tanaka H., Taniwaki M.,
RA   Yokota J., Morishita K.;
RT   "A novel gene, MEL1, mapped to 1p36.3 is highly homologous to the
RT   MDS1/EVI1 gene and is transcriptionally activated in t(1;3)(p36;q21)-
RT   positive leukemia cells.";
RL   Blood 96:3209-3214(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Fang W., Yang X.-H., Huang S.;
RT   "A family of novel PR-domain (PRDM) genes as candidate tumor
RT   suppressors.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   PRO-533.
RC   TISSUE=Brain;
RX   PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA   Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIX.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 7:347-355(2000).
RN   [4]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   PRO-533.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 2 AND 4), AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Placenta;
RX   PubMed=12816872; DOI=10.1182/blood-2002-12-3944;
RA   Nishikata I., Sasaki H., Iga M., Tateno Y., Imayoshi S., Asou N.,
RA   Nakamura T., Morishita K.;
RT   "A novel EVI1 gene family, MEL1, lacking a PR domain (MEL1S) is
RT   expressed mainly in t(1;3)(p36;q21)-positive AML and blocks G-CSF-
RT   induced myeloid differentiation.";
RL   Blood 102:3323-3332(2003).
RN   [8]
RP   CHROMOSOMAL TRANSLOCATION, AND DISEASE.
RX   PubMed=12557231; DOI=10.1002/gcc.10176;
RA   Xinh P.T., Tri N.K., Nagao H., Nakazato H., Taketazu F., Fujisawa S.,
RA   Yagasaki F., Chen Y.Z., Hayashi Y., Toyoda A., Hattori M., Sakaki Y.,
RA   Tokunaga K., Sato Y.;
RT   "Breakpoints at 1p36.3 in three MDS/AML(M4) patients with
RT   t(1;3)(p36;q21) occur in the first intron and in the 5' region of
RT   MEL1.";
RL   Genes Chromosomes Cancer 36:313-316(2003).
RN   [9]
RP   FUNCTION, ALTERNATIVE SPLICING (ISOFORM 4), AND DISEASE.
RX   PubMed=14656887; DOI=10.1182/blood-2003-07-2482;
RA   Yoshida M., Nosaka K., Yasunaga J., Nishikata I., Morishita K.,
RA   Matsuoka M.;
RT   "Aberrant expression of the MEL1S gene identified in association with
RT   hypomethylation in adult T-cell leukemia cells.";
RL   Blood 103:2753-2760(2004).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HDAC1; SKI; SMAD2 AND
RP   SMAD3, AND REGION.
RX   PubMed=19049980; DOI=10.1074/jbc.M808989200;
RA   Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M.,
RA   Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M.,
RA   Morishita K., Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K.,
RA   Imamura T.;
RT   "SKI and MEL1 cooperate to inhibit transforming growth factor-beta
RT   signal in gastric cancer cells.";
RL   J. Biol. Chem. 284:3334-3344(2009).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=22939622; DOI=10.1016/j.cell.2012.06.048;
RA   Pinheiro I., Margueron R., Shukeir N., Eisold M., Fritzsch C.,
RA   Richter F.M., Mittler G., Genoud C., Goyama S., Kurokawa M., Son J.,
RA   Reinberg D., Lachner M., Jenuwein T.;
RT   "Prdm3 and Prdm16 are H3K9me1 methyltransferases required for
RT   mammalian heterochromatin integrity.";
RL   Cell 150:948-960(2012).
RN   [12]
RP   INTERACTION WITH ZNF516.
RX   PubMed=25578880; DOI=10.1016/j.molcel.2014.12.005;
RA   Dempersmier J., Sambeat A., Gulyaeva O., Paul S.M., Hudak C.S.,
RA   Raposo H.F., Kwan H.Y., Kang C., Wong R.H., Sul H.S.;
RT   "Cold-inducible Zfp516 activates UCP1 transcription to promote
RT   browning of white fat and development of brown fat.";
RL   Mol. Cell 57:235-246(2015).
RN   [13]
RP   VARIANT LVNC8 SER-816, VARIANTS CMD1LL LYS-271; LEU-291 AND PRO-887,
RP   VARIANT MET-1101, AND TISSUE SPECIFICITY.
RX   PubMed=23768516; DOI=10.1016/j.ajhg.2013.05.015;
RA   Arndt A.K., Schafer S., Drenckhahn J.D., Sabeh M.K., Plovie E.R.,
RA   Caliebe A., Klopocki E., Musso G., Werdich A.A., Kalwa H., Heinig M.,
RA   Padera R.F., Wassilew K., Bluhm J., Harnack C., Martitz J.,
RA   Barton P.J., Greutmann M., Berger F., Hubner N., Siebert R.,
RA   Kramer H.H., Cook S.A., MacRae C.A., Klaassen S.;
RT   "Fine mapping of the 1p36 deletion syndrome identifies mutation of
RT   PRDM16 as a cause of cardiomyopathy.";
RL   Am. J. Hum. Genet. 93:67-77(2013).
RN   [14]
RP   VARIANT MET-1101.
RX   PubMed=27535533; DOI=10.1038/nature19057;
RG   Exome Aggregation Consortium;
RA   Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
RA   Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
RA   Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
RA   Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
RA   Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
RA   Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
RA   Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
RA   Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
RA   Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
RA   Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
RA   Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA   Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
RA   Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
RA   Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
RA   Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
RA   Wilson J.G., Daly M.J., MacArthur D.G.;
RT   "Analysis of protein-coding genetic variation in 60,706 humans.";
RL   Nature 536:285-291(2016).
CC   -!- FUNCTION: Binds DNA and functions as a transcriptional regulator
CC       (PubMed:12816872). Displays histone methyltransferase activity and
CC       monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro (By
CC       similarity). Probably catalyzes the monomethylation of free
CC       histone H3 in the cytoplasm which is then transported to the
CC       nucleus and incorporated into nucleosomes where SUV39H
CC       methyltransferases use it as a substrate to catalyze histone H3
CC       'Lys-9' trimethylation (By similarity). Likely to be one of the
CC       primary histone methyltransferases along with MECOM/PRDM3 that
CC       direct cytoplasmic H3K9me1 methylation (By similarity). Functions
CC       in the differentiation of brown adipose tissue (BAT) which is
CC       specialized in dissipating chemical energy in the form of heat in
CC       response to cold or excess feeding while white adipose tissue
CC       (WAT) is specialized in the storage of excess energy and the
CC       control of systemic metabolism (By similarity). Together with
CC       CEBPB, regulates the differentiation of myoblastic precursors into
CC       brown adipose cells (By similarity). Functions as a repressor of
CC       TGF-beta signaling (PubMed:19049980).
CC       {ECO:0000250|UniProtKB:A2A935, ECO:0000269|PubMed:12816872,
CC       ECO:0000269|PubMed:19049980}.
CC   -!- FUNCTION: Isoform 4: Binds DNA and functions as a transcriptional
CC       regulator (PubMed:12816872). Functions as a repressor of TGF-beta
CC       signaling (PubMed:14656887). May regulate granulocyte
CC       differentiation (PubMed:12816872). {ECO:0000269|PubMed:12816872,
CC       ECO:0000269|PubMed:14656887}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000250|UniProtKB:A2A935};
CC   -!- SUBUNIT: Interacts with CEBPA, CEBPB and CEBPD; the interaction is
CC       direct. Interacts with PPARG and PPARA; controls brown adipocytes
CC       differentiation. Interacts with CTBP1 and CTBP2; represses the
CC       expression of WAT-specific genes. Interacts with PPARGC1A and
CC       PPARGC1B; interaction with PPARGC1A or PPARGC1B activates the
CC       transcription of BAT-specific gene (By similarity). Interacts with
CC       HDAC1, SKI, SMAD2 and SMAD3; the interaction with SKI promotes the
CC       recruitment of SMAD3-HDAC1 complex on the promoter of TGF-beta
CC       target genes (PubMed:19049980). Interacts with ZNF516; the
CC       interaction is direct and may play a role in the transcription of
CC       brown adipose tissue-specific gene (PubMed:25578880).
CC       {ECO:0000250|UniProtKB:A2A935, ECO:0000269|PubMed:19049980,
CC       ECO:0000269|PubMed:25578880}.
CC   -!- INTERACTION:
CC       P56546:Ctbp2 (xeno); NbExp=2; IntAct=EBI-4566658, EBI-1384883;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19049980}.
CC       Cytoplasm {ECO:0000269|PubMed:22939622}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9HAZ2-1; Sequence=Displayed;
CC       Name=2; Synonyms=MEL1L;
CC         IsoId=Q9HAZ2-2; Sequence=VSP_006932;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q9HAZ2-3; Sequence=VSP_038064, VSP_038065;
CC         Note=No experimental confirmation available.;
CC       Name=4; Synonyms=MEL1S;
CC         IsoId=Q9HAZ2-4; Sequence=VSP_038063;
CC         Note=Produced by alternative promoter usage.;
CC   -!- TISSUE SPECIFICITY: Expressed in uterus and kidney. Expressed in
CC       both cardiomyocytes and interstitial cells.
CC       {ECO:0000269|PubMed:11050005, ECO:0000269|PubMed:12816872,
CC       ECO:0000269|PubMed:23768516}.
CC   -!- DISEASE: Left ventricular non-compaction 8 (LVNC8) [MIM:615373]: A
CC       form of left ventricular non-compaction, a cardiomyopathy due to
CC       myocardial morphogenesis arrest and characterized by a
CC       hypertrophic left ventricle, a severely thickened 2-layered
CC       myocardium, numerous prominent trabeculations, deep
CC       intertrabecular recesses, and poor systolic function. Clinical
CC       manifestations are variable. Some affected individuals experience
CC       no symptoms at all, others develop heart failure. In some cases,
CC       left ventricular non-compaction is associated with other
CC       congenital heart anomalies. LVNC8 is an autosomal dominant
CC       condition. {ECO:0000269|PubMed:23768516}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Cardiomyopathy, dilated 1LL (CMD1LL) [MIM:615373]: A
CC       disorder characterized by ventricular dilation and impaired
CC       systolic function, resulting in congestive heart failure and
CC       arrhythmia. Patients are at risk of premature death.
CC       {ECO:0000269|PubMed:23768516}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Note=A chromosomal aberration involving PRDM16 is found
CC       in myelodysplastic syndrome (MDS) and acute myeloid leukemia
CC       (AML). Reciprocal translocation t(1;3)(p36;q21). Isoform 4 is
CC       specifically expressed in adult T-cell leukemia.
CC       {ECO:0000269|PubMed:11050005, ECO:0000269|PubMed:12557231}.
CC   -!- SIMILARITY: Belongs to the PRDM16 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB21766.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PRDM16MEL1ID408.html";
DR   EMBL; AB078876; BAB84297.1; -; mRNA.
DR   EMBL; AF294278; AAG33382.1; -; mRNA.
DR   EMBL; AB051462; BAB21766.2; ALT_INIT; mRNA.
DR   EMBL; AL008733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL354743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL512383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL590438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC161614; AAI61614.1; -; mRNA.
DR   CCDS; CCDS41236.2; -. [Q9HAZ2-1]
DR   CCDS; CCDS44048.2; -. [Q9HAZ2-2]
DR   RefSeq; NP_071397.3; NM_022114.3. [Q9HAZ2-1]
DR   RefSeq; NP_955533.2; NM_199454.2. [Q9HAZ2-2]
DR   RefSeq; XP_011540247.1; XM_011541945.2. [Q9HAZ2-4]
DR   UniGene; Hs.99500; -.
DR   PDB; 2N1I; NMR; -; A=54-226.
DR   PDB; 6BW4; X-ray; 2.00 A; B/D=1-12.
DR   PDBsum; 2N1I; -.
DR   PDBsum; 6BW4; -.
DR   ProteinModelPortal; Q9HAZ2; -.
DR   SMR; Q9HAZ2; -.
DR   BioGrid; 122023; 7.
DR   IntAct; Q9HAZ2; 3.
DR   STRING; 9606.ENSP00000270722; -.
DR   iPTMnet; Q9HAZ2; -.
DR   PhosphoSitePlus; Q9HAZ2; -.
DR   BioMuta; PRDM16; -.
DR   DMDM; 259016328; -.
DR   jPOST; Q9HAZ2; -.
DR   MaxQB; Q9HAZ2; -.
DR   PaxDb; Q9HAZ2; -.
DR   PeptideAtlas; Q9HAZ2; -.
DR   PRIDE; Q9HAZ2; -.
DR   ProteomicsDB; 81460; -.
DR   ProteomicsDB; 81461; -. [Q9HAZ2-2]
DR   ProteomicsDB; 81462; -. [Q9HAZ2-3]
DR   ProteomicsDB; 81463; -. [Q9HAZ2-4]
DR   DNASU; 63976; -.
DR   Ensembl; ENST00000270722; ENSP00000270722; ENSG00000142611. [Q9HAZ2-1]
DR   Ensembl; ENST00000378391; ENSP00000367643; ENSG00000142611. [Q9HAZ2-2]
DR   GeneID; 63976; -.
DR   KEGG; hsa:63976; -.
DR   UCSC; uc001ake.4; human. [Q9HAZ2-1]
DR   CTD; 63976; -.
DR   DisGeNET; 63976; -.
DR   EuPathDB; HostDB:ENSG00000142611.16; -.
DR   GeneCards; PRDM16; -.
DR   HGNC; HGNC:14000; PRDM16.
DR   HPA; HPA050343; -.
DR   HPA; HPA060467; -.
DR   MalaCards; PRDM16; -.
DR   MIM; 605557; gene.
DR   MIM; 615373; phenotype.
DR   neXtProt; NX_Q9HAZ2; -.
DR   OpenTargets; ENSG00000142611; -.
DR   Orphanet; 1606; 1p36 deletion syndrome.
DR   Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR   Orphanet; 54260; Left ventricular noncompaction.
DR   PharmGKB; PA33714; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00940000160951; -.
DR   HOVERGEN; HBG005619; -.
DR   InParanoid; Q9HAZ2; -.
DR   KO; K22410; -.
DR   OMA; GMQEKKM; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q9HAZ2; -.
DR   TreeFam; TF315309; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   SIGNOR; Q9HAZ2; -.
DR   ChiTaRS; PRDM16; human.
DR   GeneWiki; PRDM16; -.
DR   GenomeRNAi; 63976; -.
DR   PRO; PR:Q9HAZ2; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000142611; Expressed in 153 organ(s), highest expression level in pigmented layer of retina.
DR   ExpressionAtlas; Q9HAZ2; baseline and differential.
DR   Genevisible; Q9HAZ2; HS.
DR   GO; GO:0016235; C:aggresome; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0017053; C:transcriptional repressor complex; ISS:UniProtKB.
DR   GO; GO:0033613; F:activating transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0050873; P:brown fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0030853; P:negative regulation of granulocyte differentiation; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0043457; P:regulation of cellular respiration; ISS:UniProtKB.
DR   GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0043586; P:tongue development; IEA:Ensembl.
DR   GO; GO:0050872; P:white fat cell differentiation; IEA:Ensembl.
DR   InterPro; IPR030414; PRDM16.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24393:SF5; PTHR24393:SF5; 1.
DR   Pfam; PF00096; zf-C2H2; 9.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative promoter usage;
KW   Alternative splicing; Cardiomyopathy; Chromosomal rearrangement;
KW   Complete proteome; Cytoplasm; Differentiation; Disease mutation;
KW   DNA-binding; Metal-binding; Methyltransferase; Nucleus; Polymorphism;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1276       Histone-lysine N-methyltransferase
FT                                PRDM16.
FT                                /FTId=PRO_0000047773.
FT   DOMAIN       82    211       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     230    253       C2H2-type 1; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     281    303       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     309    331       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     337    360       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     366    388       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     394    416       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     423    445       C2H2-type 7; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     951    973       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     979   1002       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1008   1032       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      679   1038       Interaction with CTBP1, CTBP2 and ZNF516.
FT                                {ECO:0000250|UniProtKB:A2A935}.
FT   REGION      739   1276       Mediates interaction with SKI and
FT                                regulation of TGF-beta signaling.
FT                                {ECO:0000269|PubMed:19049980}.
FT   COMPBIAS    459    557       Pro-rich.
FT   VAR_SEQ       1    184       Missing (in isoform 4). {ECO:0000305}.
FT                                /FTId=VSP_038063.
FT   VAR_SEQ     191    191       Q -> QV (in isoform 3).
FT                                {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_038064.
FT   VAR_SEQ     868    868       Missing (in isoform 3).
FT                                {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_038065.
FT   VAR_SEQ    1233   1251       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11050005}.
FT                                /FTId=VSP_006932.
FT   VARIANT     271    271       E -> K (in CMD1LL; unknown pathological
FT                                significance; dbSNP:rs200052869).
FT                                {ECO:0000269|PubMed:23768516}.
FT                                /FTId=VAR_070212.
FT   VARIANT     291    291       P -> L (in CMD1LL; unknown pathological
FT                                significance; dbSNP:rs397514744).
FT                                {ECO:0000269|PubMed:23768516}.
FT                                /FTId=VAR_070213.
FT   VARIANT     533    533       S -> P (in dbSNP:rs870124).
FT                                {ECO:0000269|PubMed:11050005,
FT                                ECO:0000269|PubMed:11214970,
FT                                ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_031433.
FT   VARIANT     633    633       P -> L (in dbSNP:rs2493292).
FT                                /FTId=VAR_031434.
FT   VARIANT     816    816       N -> S (in LVNC8; dbSNP:rs397514743).
FT                                {ECO:0000269|PubMed:23768516}.
FT                                /FTId=VAR_070214.
FT   VARIANT     887    887       L -> P (in CMD1LL; unknown pathological
FT                                significance; dbSNP:rs202115331).
FT                                {ECO:0000269|PubMed:23768516}.
FT                                /FTId=VAR_070215.
FT   VARIANT    1101   1101       V -> M (in dbSNP:rs201654872).
FT                                {ECO:0000269|PubMed:23768516}.
FT                                /FTId=VAR_070216.
FT   CONFLICT     50     52       PPS -> SPP (in Ref. 2; AAG33382).
FT                                {ECO:0000305}.
FT   CONFLICT    324    324       L -> F (in Ref. 2; AAG33382).
FT                                {ECO:0000305}.
FT   CONFLICT    491    491       S -> Y (in Ref. 2; AAG33382).
FT                                {ECO:0000305}.
FT   CONFLICT   1022   1022       N -> K (in Ref. 1; BAB84297).
FT                                {ECO:0000305}.
FT   STRAND       84     91       {ECO:0000244|PDB:2N1I}.
FT   TURN         92     94       {ECO:0000244|PDB:2N1I}.
FT   STRAND       95    102       {ECO:0000244|PDB:2N1I}.
FT   STRAND      126    129       {ECO:0000244|PDB:2N1I}.
FT   TURN        140    142       {ECO:0000244|PDB:2N1I}.
FT   TURN        153    155       {ECO:0000244|PDB:2N1I}.
FT   STRAND      161    163       {ECO:0000244|PDB:2N1I}.
FT   HELIX       167    170       {ECO:0000244|PDB:2N1I}.
FT   HELIX       178    180       {ECO:0000244|PDB:2N1I}.
FT   STRAND      183    188       {ECO:0000244|PDB:2N1I}.
FT   STRAND      191    198       {ECO:0000244|PDB:2N1I}.
FT   STRAND      212    215       {ECO:0000244|PDB:2N1I}.
FT   HELIX       216    219       {ECO:0000244|PDB:2N1I}.
FT   TURN        222    225       {ECO:0000244|PDB:2N1I}.
SQ   SEQUENCE   1276 AA;  140251 MW;  AD16C5C0EE89A528 CRC64;
     MRSKARARKL AKSDGDVVNN MYEPNRDLLA SHSAEDEAED SAMSPIPVGP PSPFPTSEDF
     TPKEGSPYEA PVYIPEDIPI PADFELRESS IPGAGLGVWA KRKMEAGERL GPCVVVPRAA
     AKETDFGWEQ ILTDVEVSPQ EGCITKISED LGSEKFCVDA NQAGAGSWLK YIRVACSCDD
     QNLTMCQISE QIYYKVIKDI EPGEELLVHV KEGVYPLGTV PPGLDEEPTF RCDECDELFQ
     SKLDLRRHKK YTCGSVGAAL YEGLAEELKP EGLGGGSGQA HECKDCERMF PNKYSLEQHM
     VIHTEEREYK CDQCPKAFNW KSNLIRHQMS HDSGKRFECE NCVKVFTDPS NLQRHIRSQH
     VGARAHACPD CGKTFATSSG LKQHKHIHST VKPFICEVCH KSYTQFSNLC RHKRMHADCR
     TQIKCKDCGQ MFSTTSSLNK HRRFCEGKNH YTPGGIFAPG LPLTPSPMMD KAKPSPSLNH
     ASLGFNEYFP SRPHPGSLPF STAPPTFPAL TPGFPGIFPP SLYPRPPLLP PTSLLKSPLN
     HTQDAKLPSP LGNPALPLVS AVSNSSQGTT AAAGPEEKFE SRLEDSCVEK LKTRSSDMSD
     GSDFEDVNTT TGTDLDTTTG TGSDLDSDVD SDPDKDKGKG KSAEGQPKFG GGLAPPGAPN
     SVAEVPVFYS QHSFFPPPDE QLLTATGAAG DSIKAIASIA EKYFGPGFMG MQEKKLGSLP
     YHSAFPFQFL PNFPHSLYPF TDRALAHNLL VKAEPKSPRD ALKVGGPSAE CPFDLTTKPK
     DVKPILPMPK GPSAPASGEE QPLDLSIGSR ARASQNGGGR EPRKNHVYGE RKLGAGEGLP
     QVCPARMPQQ PPLHYAKPSP FFMDPIYSRV EKRKVTDPVG ALKEKYLRPS PLLFHPQMSA
     IETMTEKLES FAAMKADSGS SLQPLPHHPF NFRSPPPTLS DPILRKGKER YTCRYCGKIF
     PRSANLTRHL RTHTGEQPYR CKYCDRSFSI SSNLQRHVRN IHNKEKPFKC HLCNRCFGQQ
     TNLDRHLKKH EHENAPVSQH PGVLTNHLGT SASSPTSESD NHALLDEKED SYFSEIRNFI
     ANSEMNQAST RTEKRADMQI VDGSAQCPGL ASEKQEDVEE EDDDDLEEDD EDSLAGKSQD
     DTVSPAPEPQ AAYEDEEDEE PAASLAVGFD HTRRCAEDHE GGLLALEPMP TFGKGLDLRR
     AAEEAFEVKD VLNSTLDSEA LKHTLCRQAK NQAYAMMLSL SEDTPLHTPS QGSLDAWLKV
     TGATSESGAF HPINHL
//
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