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Database: UniProt
Entry: Q5XJV7
LinkDB: Q5XJV7
Original site: Q5XJV7 
ID   SETD5_MOUSE             Reviewed;        1441 AA.
AC   Q5XJV7; Q80T94; Q8BKD5; Q8BX30;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   10-APR-2019, entry version 106.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD5 {ECO:0000305};
DE            EC=2.1.1.43 {ECO:0000269|PubMed:22939622};
DE   AltName: Full=SET domain-containing protein 5 {ECO:0000305};
GN   Name=Setd5 {ECO:0000303|PubMed:27864380, ECO:0000312|MGI:MGI:1920145};
GN   Synonyms=Kiaa1757 {ECO:0000303|PubMed:12693553};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 245-1071.
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-852 AND THR-855,
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70 AND SER-74 (ISOFORM
RP   2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LEO1; CTR9; CDC73 AND
RP   NCOR1, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=27864380; DOI=10.1242/dev.141465;
RA   Osipovich A.B., Gangula R., Vianna P.G., Magnuson M.A.;
RT   "Setd5 is essential for mammalian development and the co-
RT   transcriptional regulation of histone acetylation.";
RL   Development 143:4595-4607(2016).
CC   -!- FUNCTION: Displays histone methyltransferase activity and
CC       monomethylates 'Lys-9' of histone H3 in vitro (PubMed:22939622).
CC       The physiological significance of this activity is unclear
CC       (Probable) (PubMed:22939622). Probable transcriptional regulator
CC       that acts via the formation of large multiprotein complexes that
CC       modify and/or remodel the chromatin. Acts as a regulator of
CC       histone acetylation during gene transcription (PubMed:27864380).
CC       {ECO:0000269|PubMed:22939622, ECO:0000269|PubMed:27864380,
CC       ECO:0000305|PubMed:22939622}.
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:0000269|PubMed:22939622};
CC   -!- SUBUNIT: Interacts with components of the PAF1 complex (PAF1C)
CC       such as LEO1, CTR9 and CDC73 (PubMed:27864380). Interacts with
CC       NCOR1 (PubMed:27864380). {ECO:0000269|PubMed:27864380}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27864380}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5XJV7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5XJV7-2; Sequence=VSP_024097;
CC         Note=No experimental confirmation available. Contains a
CC         phosphothreonine at position 70. Contains a phosphoserine at
CC         position 74. {ECO:0000244|PubMed:21183079};
CC       Name=3;
CC         IsoId=Q5XJV7-3; Sequence=VSP_024096;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:27864380}.
CC   -!- DISRUPTION PHENOTYPE: Mid-gestation lethality due to severe
CC       developmental delay such as vascular abnormalities in the embryo
CC       and placenta, reduced cellular proliferation and increased
CC       apoptosis (PubMed:27864380). Defects are probably due to a
CC       widespread impairment in the regulation of gene expression
CC       (PubMed:27864380). {ECO:0000269|PubMed:27864380}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33569.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC65833.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AK122551; BAC65833.1; ALT_INIT; mRNA.
DR   EMBL; AK049143; BAC33569.1; ALT_INIT; mRNA.
DR   EMBL; AK053541; BAC35420.1; -; mRNA.
DR   EMBL; BC083184; AAH83184.1; -; mRNA.
DR   CCDS; CCDS20411.1; -. [Q5XJV7-1]
DR   RefSeq; NP_082661.1; NM_028385.1. [Q5XJV7-1]
DR   RefSeq; NP_766593.1; NM_173005.1. [Q5XJV7-2]
DR   RefSeq; XP_011239784.1; XM_011241482.2. [Q5XJV7-2]
DR   UniGene; Mm.367159; -.
DR   ProteinModelPortal; Q5XJV7; -.
DR   SMR; Q5XJV7; -.
DR   BioGrid; 215631; 6.
DR   IntAct; Q5XJV7; 6.
DR   STRING; 10090.ENSMUSP00000047398; -.
DR   iPTMnet; Q5XJV7; -.
DR   PhosphoSitePlus; Q5XJV7; -.
DR   EPD; Q5XJV7; -.
DR   jPOST; Q5XJV7; -.
DR   PaxDb; Q5XJV7; -.
DR   PeptideAtlas; Q5XJV7; -.
DR   PRIDE; Q5XJV7; -.
DR   Ensembl; ENSMUST00000042889; ENSMUSP00000047398; ENSMUSG00000034269. [Q5XJV7-1]
DR   Ensembl; ENSMUST00000113155; ENSMUSP00000108780; ENSMUSG00000034269. [Q5XJV7-2]
DR   Ensembl; ENSMUST00000113157; ENSMUSP00000108782; ENSMUSG00000034269. [Q5XJV7-2]
DR   GeneID; 72895; -.
DR   KEGG; mmu:72895; -.
DR   UCSC; uc009deq.1; mouse. [Q5XJV7-1]
DR   UCSC; uc009der.1; mouse. [Q5XJV7-2]
DR   UCSC; uc009deu.1; mouse. [Q5XJV7-3]
DR   CTD; 55209; -.
DR   MGI; MGI:1920145; Setd5.
DR   eggNOG; ENOG410IMXD; Eukaryota.
DR   eggNOG; ENOG410ZTNX; LUCA.
DR   GeneTree; ENSGT00940000157446; -.
DR   HOGENOM; HOG000154294; -.
DR   HOVERGEN; HBG068103; -.
DR   InParanoid; Q5XJV7; -.
DR   OMA; PEEECRN; -.
DR   OrthoDB; 86638at2759; -.
DR   PhylomeDB; Q5XJV7; -.
DR   TreeFam; TF106417; -.
DR   ChiTaRS; Setd5; mouse.
DR   PRO; PR:Q5XJV7; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000034269; Expressed in 265 organ(s), highest expression level in ascending aorta.
DR   Genevisible; Q5XJV7; MM.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016569; P:covalent chromatin modification; IMP:UniProtKB.
DR   GO; GO:1902275; P:regulation of chromatin organization; IMP:UniProtKB.
DR   GO; GO:0035065; P:regulation of histone acetylation; IMP:UniProtKB.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Complete proteome;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN         1   1441       Histone-lysine N-methyltransferase SETD5.
FT                                /FTId=PRO_0000281906.
FT   DOMAIN      269    390       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   COMPBIAS   1088   1410       Ser-rich.
FT   MOD_RES      72     72       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     829    829       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9C0A6}.
FT   MOD_RES     852    852       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     855    855       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1197   1197       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9C0A6}.
FT   VAR_SEQ       1    792       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024096.
FT   VAR_SEQ      59     59       A -> ADHNYGAPPPPTPPASPPVQ (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_024097.
FT   CONFLICT   1381   1381       L -> F (in Ref. 3; AAH83184).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1441 AA;  157426 MW;  67120734D6EB6DD9 CRC64;
     MSIAIPLGVT TPDTSYSDMA AGSDPESVEA SPAVNEKSVY STHNYGTTQR HGCRGLPYAT
     IIPRSDLNGL PSPVEERCGD SPNSEGETVP TWCPCGLSQD GFLLNCDKCR GMSRGKVIRL
     HRRKQDNISG GDSSATESWD EELSPSTVLY TATQHTPTSI TLTVRRTKPK KRKKSPEKGR
     AAPKTKKIKN SPSEAQNLDE NTTEGWENRI RLWTDQYEEA FTNQYSADVQ NALEQHLHSN
     KEFVGKPAIL DTINKTELAC NNTVIGSQMQ LQLGRVTRVQ KHRKILRAAR DLALDTLIIE
     YRGKVMLRQQ FEVNGHFFKK PYPFVLFYSK FNGVEMCVDA RTFGNDARFI RRSCTPNAEV
     RHMIADGMIH LCIYAVSAIT KDAEVTIAFD YEYSNCNYKV DCACHKGNRN CPIQKRNPNA
     AELPLPPPPS FPTIGAETRR RKARRKELEL EQQNEVPEEN PDPQPQEVPE KVTVSNEHEE
     VDNPEEKPEE EEKEEATDDQ ENSAHSRRTR EDRKVEAIMH AFESLEKRKK RRDQPVEQSS
     SDIEITTSSS EIVVGEETKT AAPESEVSSP VSNVAIPSTP QSTGVNTRRS SHAGDVAAEK
     PIPKPPPAKP SRPRPKSRIS RYRTSSAQRL KRQKQAIAQQ AELSQAALEE GGSNNSVTPP
     EAGNTDSSGE NRQLTGSDPT VISVTGSHVN RAASKYPKTK KYLVTEWLND KAEKQECPVE
     CPLRITTDPT VLATTLNMLP GLIHSPLICT TPKHYIRFGS PFMPERRRRP LLPDGTFSSC
     KKRWIKQALE EGMTQTSSVP QETRTQHLYQ SNETSNSSSI CKDNADLLSP LKKWKSRYLM
     EQNITKLLQP LSPVTPPPPS SGSKSPQLTT PGQTHPGEEE CRNGYSLMFS PITSLTTASR
     SNTPLQFELC HRKDLDLTKV GFPDSSTHSC ADRPSLLNCN HPDLASHPSV VPTSEAGFPS
     RSGDGPQTLL RNSDQAFRTE FNLMYAYSPL NAMPRADGLY RGSPLVGDRK PLHLDGGYCS
     PAEGFSSRYE HGFMKDLSRG SMSPGGERTC EGVPSAPQNP PQRKKVSLLE YRKRKQEAKE
     NSGGGNDSSQ SKSKSSGAGQ GSSNSVSDTG AHGVQGSSAG TPSSPHKKFS PSHSSASHLE
     AVSPSDSRGT SSSHCRPQEN ISSRWMVPTS VERLREGGSI PKVLRSSVRV AQKGEPSPTW
     ESNITEKESD PADGEGPEPL SSALSKGATV YSPSRYSYQL LQCDSPRTES QSLLQQSSSP
     FRGHPTQSPG YSYRTTALRP GNPPSHGSSE SSLSSTSYPS PAHPVSTDSL APFTGTPGYY
     SSQPHSGNST GSNLPRRSCS SSAASPTPQG PSDSPTSDSV SQSSTGTLSS TSFPQNSRSS
     LPSDLRTISL PNAGQSAAYQ ASRVSAVSNS QHYPHRGSGG VHQYRLQPLQ GSGVKTQTGL
     S
//
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