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Database: UniProt
Entry: Q9C0A6
LinkDB: Q9C0A6
Original site: Q9C0A6 
ID   SETD5_HUMAN             Reviewed;        1442 AA.
AC   Q9C0A6; Q6AI17; Q8WUB6; Q9H3X4; Q9H6V7; Q9H7S3; Q9NVI9;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   10-APR-2019, entry version 116.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD5 {ECO:0000305};
DE            EC=2.1.1.43 {ECO:0000250|UniProtKB:Q5XJV7};
DE   AltName: Full=SET domain-containing protein 5 {ECO:0000305};
GN   Name=SETD5 {ECO:0000312|HGNC:HGNC:25566};
GN   Synonyms=KIAA1757 {ECO:0000303|PubMed:11214970};
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 [LARGE SCALE MRNA] (ISOFORM 2).
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 527-1442.
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 445-1442.
RC   TISSUE=Colon;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 456-1442.
RC   TISSUE=Hepatoma, Placenta, and Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-1198, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [12]
RP   INVOLVEMENT IN MRD23, AND VARIANTS MRD23 399-LYS--SER-1442 DEL;
RP   445-ARG--SER-1442 DEL; 622-TYR--SER-1442 DEL AND 1001-ARG--SER-1442
RP   DEL.
RX   PubMed=24680889; DOI=10.1016/j.ajhg.2014.03.006;
RG   UK10K Consortium;
RA   Grozeva D., Carss K., Spasic-Boskovic O., Parker M.J., Archer H.,
RA   Firth H.V., Park S.M., Canham N., Holder S.E., Wilson M., Hackett A.,
RA   Field M., Floyd J.A., Hurles M., Raymond F.L.;
RT   "De novo loss-of-function mutations in SETD5, encoding a
RT   methyltransferase in a 3p25 microdeletion syndrome critical region,
RT   cause intellectual disability.";
RL   Am. J. Hum. Genet. 94:618-624(2014).
RN   [13]
RP   VARIANTS MRD23 GLY-175 AND 768-ARG--SER-1442 DEL.
RX   PubMed=25138099; DOI=10.1038/ejhg.2014.165;
RA   Kuechler A., Zink A.M., Wieland T., Luedecke H.J., Cremer K.,
RA   Salviati L., Magini P., Najafi K., Zweier C., Czeschik J.C., Aretz S.,
RA   Endele S., Tamburrino F., Pinato C., Clementi M., Gundlach J.,
RA   Maylahn C., Mazzanti L., Wohlleber E., Schwarzmayr T., Kariminejad R.,
RA   Schlessinger A., Wieczorek D., Strom T.M., Novarino G., Engels H.;
RT   "Loss-of-function variants of SETD5 cause intellectual disability and
RT   the core phenotype of microdeletion 3p25.3 syndrome.";
RL   Eur. J. Hum. Genet. 23:753-760(2015).
RN   [14]
RP   VARIANTS MRD23 973-SER--SER-1442 DEL AND CYS-1071.
RX   PubMed=27375234; DOI=10.1002/ajmg.a.37832;
RA   Szczaluba K., Brzezinska M., Kot J., Rydzanicz M., Walczak A.,
RA   Stawinski P., Werner B., Ploski R.;
RT   "SETD5 loss-of-function mutation as a likely cause of a familial
RT   syndromic intellectual disability with variable phenotypic
RT   expression.";
RL   Am. J. Med. Genet. A 170:2322-2327(2016).
RN   [15]
RP   INVOLVEMENT IN MRD23.
RX   PubMed=28549204; DOI=10.4238/gmr16029615;
RA   Stur E., Soares L.A., Louro I.D.;
RT   "SETD5 gene variant associated with mild intellectual disability - a
RT   case report.";
RL   Genet. Mol. Res. 16:0-0(2017).
CC   -!- FUNCTION: Displays histone methyltransferase activity and
CC       monomethylates 'Lys-9' of histone H3 in vitro. The physiological
CC       significance of this activity is unclear. Probable transcriptional
CC       regulator that acts via the formation of large multiprotein
CC       complexes that modify and/or remodel the chromatin. Acts as a
CC       regulator of histone acetylation during gene transcription.
CC       {ECO:0000250|UniProtKB:Q5XJV7}.
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:Q5XJV7};
CC   -!- SUBUNIT: Interacts with components of the PAF1 complex (PAF1C)
CC       such as LEO1, CTR9 and CDC73. Interacts with NCOR1.
CC       {ECO:0000250|UniProtKB:Q5XJV7}.
CC   -!- INTERACTION:
CC       Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-10303449, EBI-739624;
CC       Q6A162:KRT40; NbExp=3; IntAct=EBI-10303449, EBI-10171697;
CC       Q5JR59:MTUS2; NbExp=3; IntAct=EBI-10303449, EBI-742948;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5XJV7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9C0A6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9C0A6-2; Sequence=VSP_024094;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q9C0A6-3; Sequence=VSP_024094, VSP_024095;
CC         Note=No experimental confirmation available.;
CC   -!- DISEASE: Mental retardation, autosomal dominant 23 (MRD23)
CC       [MIM:615761]: A disorder characterized by significantly below
CC       average general intellectual functioning associated with
CC       impairments in adaptive behavior and manifested during the
CC       developmental period. MRD23 patients manifest moderate to severe
CC       intellectual disability with additional variable features of
CC       brachycephaly, a low hairline, depressed nasal bridge, prominent
CC       high nasal root, tubular nose, upslanting palpebral fissures, long
CC       and smooth philtrum, micrognathia, thin upper lip, and crowded
CC       teeth. Behavioral problems, including obsessive-compulsive
CC       disorder, hand flapping with ritualized behavior, and autism, are
CC       prominent features. {ECO:0000269|PubMed:24680889,
CC       ECO:0000269|PubMed:25138099, ECO:0000269|PubMed:27375234,
CC       ECO:0000269|PubMed:28549204}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH20956.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAA91762.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAB14903.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAB15144.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAB21848.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; AB051544; BAB21848.1; ALT_INIT; mRNA.
DR   EMBL; AL442073; CAC09439.2; -; mRNA.
DR   EMBL; CR627408; CAH10497.1; -; mRNA.
DR   EMBL; AC018506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC020956; AAH20956.1; ALT_INIT; mRNA.
DR   EMBL; AK001569; BAA91762.1; ALT_INIT; mRNA.
DR   EMBL; AK024384; BAB14903.1; ALT_INIT; mRNA.
DR   EMBL; AK025478; BAB15144.1; ALT_INIT; mRNA.
DR   CCDS; CCDS46741.1; -. [Q9C0A6-1]
DR   CCDS; CCDS74892.1; -. [Q9C0A6-3]
DR   RefSeq; NP_001073986.1; NM_001080517.2. [Q9C0A6-1]
DR   RefSeq; NP_001278972.1; NM_001292043.1. [Q9C0A6-3]
DR   RefSeq; XP_016862270.1; XM_017006781.1.
DR   UniGene; Hs.288164; -.
DR   ProteinModelPortal; Q9C0A6; -.
DR   SMR; Q9C0A6; -.
DR   BioGrid; 120505; 15.
DR   IntAct; Q9C0A6; 13.
DR   STRING; 9606.ENSP00000385852; -.
DR   iPTMnet; Q9C0A6; -.
DR   PhosphoSitePlus; Q9C0A6; -.
DR   BioMuta; SETD5; -.
DR   DMDM; 143584285; -.
DR   EPD; Q9C0A6; -.
DR   jPOST; Q9C0A6; -.
DR   MaxQB; Q9C0A6; -.
DR   PaxDb; Q9C0A6; -.
DR   PeptideAtlas; Q9C0A6; -.
DR   PRIDE; Q9C0A6; -.
DR   ProteomicsDB; 79978; -.
DR   ProteomicsDB; 79979; -. [Q9C0A6-2]
DR   ProteomicsDB; 79980; -. [Q9C0A6-3]
DR   Ensembl; ENST00000302463; ENSP00000302028; ENSG00000168137. [Q9C0A6-3]
DR   Ensembl; ENST00000402198; ENSP00000385852; ENSG00000168137. [Q9C0A6-1]
DR   Ensembl; ENST00000406341; ENSP00000383939; ENSG00000168137. [Q9C0A6-1]
DR   GeneID; 55209; -.
DR   KEGG; hsa:55209; -.
DR   UCSC; uc003brt.3; human. [Q9C0A6-1]
DR   CTD; 55209; -.
DR   DisGeNET; 55209; -.
DR   EuPathDB; HostDB:ENSG00000168137.15; -.
DR   GeneCards; SETD5; -.
DR   H-InvDB; HIX0003027; -.
DR   HGNC; HGNC:25566; SETD5.
DR   HPA; CAB017093; -.
DR   HPA; HPA035574; -.
DR   MalaCards; SETD5; -.
DR   MIM; 615743; gene.
DR   MIM; 615761; phenotype.
DR   neXtProt; NX_Q9C0A6; -.
DR   OpenTargets; ENSG00000168137; -.
DR   Orphanet; 199; Cornelia de Lange syndrome.
DR   Orphanet; 404440; Intellectual disability-facial dysmorphism syndrome due to SETD5 haploinsufficiency.
DR   PharmGKB; PA143485613; -.
DR   eggNOG; ENOG410IMXD; Eukaryota.
DR   eggNOG; ENOG410ZTNX; LUCA.
DR   GeneTree; ENSGT00940000157446; -.
DR   HOGENOM; HOG000154294; -.
DR   HOVERGEN; HBG068103; -.
DR   InParanoid; Q9C0A6; -.
DR   OrthoDB; 86638at2759; -.
DR   PhylomeDB; Q9C0A6; -.
DR   TreeFam; TF106417; -.
DR   ChiTaRS; SETD5; human.
DR   GenomeRNAi; 55209; -.
DR   PRO; PR:Q9C0A6; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000168137; Expressed in 227 organ(s), highest expression level in intestine.
DR   ExpressionAtlas; Q9C0A6; baseline and differential.
DR   Genevisible; Q9C0A6; HS.
DR   GO; GO:0016593; C:Cdc73/Paf1 complex; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016569; P:covalent chromatin modification; ISS:UniProtKB.
DR   GO; GO:1902275; P:regulation of chromatin organization; ISS:UniProtKB.
DR   GO; GO:0035065; P:regulation of histone acetylation; ISS: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; Autism; Autism spectrum disorder;
KW   Chromatin regulator; Complete proteome; Disease mutation;
KW   Mental retardation; Methyltransferase; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1   1442       Histone-lysine N-methyltransferase SETD5.
FT                                /FTId=PRO_0000281905.
FT   DOMAIN      269    390       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   COMPBIAS   1089   1411       Ser-rich.
FT   MOD_RES      72     72       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     829    829       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     852    852       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5XJV7}.
FT   MOD_RES     855    855       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q5XJV7}.
FT   MOD_RES    1198   1198       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ       1    111       Missing (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:11214970,
FT                                ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_024094.
FT   VAR_SEQ     188    188       I -> IKAFREGSRKSLRM (in isoform 3).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_024095.
FT   VARIANT      77     77       R -> H (in dbSNP:rs41387348).
FT                                /FTId=VAR_051336.
FT   VARIANT     119    119       R -> I (in dbSNP:rs11720526).
FT                                /FTId=VAR_051337.
FT   VARIANT     175    175       S -> G (in MRD23).
FT                                {ECO:0000269|PubMed:25138099}.
FT                                /FTId=VAR_078954.
FT   VARIANT     399   1442       Missing (in MRD23; dbSNP:rs587777325).
FT                                {ECO:0000269|PubMed:24680889}.
FT                                /FTId=VAR_078955.
FT   VARIANT     445   1442       Missing (in MRD23).
FT                                {ECO:0000269|PubMed:24680889}.
FT                                /FTId=VAR_078956.
FT   VARIANT     622   1442       Missing (in MRD23).
FT                                {ECO:0000269|PubMed:24680889}.
FT                                /FTId=VAR_078957.
FT   VARIANT     768   1442       Missing (in MRD23; dbSNP:rs864321657).
FT                                {ECO:0000269|PubMed:25138099}.
FT                                /FTId=VAR_078958.
FT   VARIANT     973   1442       Missing (in MRD23).
FT                                {ECO:0000269|PubMed:27375234}.
FT                                /FTId=VAR_078959.
FT   VARIANT    1001   1442       Missing (in MRD23; dbSNP:rs587777327).
FT                                {ECO:0000269|PubMed:24680889}.
FT                                /FTId=VAR_078960.
FT   VARIANT    1071   1071       Y -> C (in MRD23; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:27375234}.
FT                                /FTId=VAR_078961.
FT   VARIANT    1137   1137       M -> V (in dbSNP:rs13327456).
FT                                /FTId=VAR_051338.
FT   VARIANT    1308   1308       T -> I (in dbSNP:rs11542009).
FT                                /FTId=VAR_061705.
FT   CONFLICT    369    369       I -> N (in Ref. 2; CAH10497).
FT                                {ECO:0000305}.
FT   CONFLICT    869    869       A -> V (in Ref. 2; CAH10497).
FT                                {ECO:0000305}.
FT   CONFLICT    985    985       Y -> H (in Ref. 2; CAH10497).
FT                                {ECO:0000305}.
FT   CONFLICT   1123   1123       P -> S (in Ref. 5; BAB14903).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1442 AA;  157515 MW;  E3CDBA72E2ED0DB4 CRC64;
     MSIAIPLGVT TSDTSYSDMA AGSDPESVEA SPAVNEKSVY STHNYGTTQR HGCRGLPYAT
     IIPRSDLNGL PSPVEERCGD SPNSEGETVP TWCPCGLSQD GFLLNCDKCR GMSRGKVIRL
     HRRKQDNISG GDSSATESWD EELSPSTVLY TATQHTPTSI TLTVRRTKPK KRKKSPEKGR
     AAPKTKKIKN SPSEAQNLDE NTTEGWENRI RLWTDQYEEA FTNQYSADVQ NALEQHLHSS
     KEFVGKPTIL DTINKTELAC NNTVIGSQMQ LQLGRVTRVQ KHRKILRAAR DLALDTLIIE
     YRGKVMLRQQ FEVNGHFFKK PYPFVLFYSK FNGVEMCVDA RTFGNDARFI RRSCTPNAEV
     RHMIADGMIH LCIYAVSAIT KDAEVTIAFD YEYSNCNYKV DCACHKGNRN CPIQKRNPNA
     TELPLLPPPP SLPTIGAETR RRKARRKELE MEQQNEASEE NNDQQSQEVP EKVTVSSDHE
     EVDNPEEKPE EEKEEVIDDQ ENLAHSRRTR EDRKVEAIMH AFENLEKRKK RRDQPLEQSN
     SDVEITTTTS ETPVGEETKT EAPESEVSNS VSNVTIPSTP QSVGVNTRRS SQAGDIAAEK
     LVPKPPPAKP SRPRPKSRIS RYRTSSAQRL KRQKQANAQQ AELSQAALEE GGSNSLVTPT
     EAGSLDSSGE NRPLTGSDPT VVSITGSHVN RAASKYPKTK KYLVTEWLND KAEKQECPVE
     CPLRITTDPT VLATTLNMLP GLIHSPLICT TPKHYIRFGS PFIPERRRRP LLPDGTFSSC
     KKRWIKQALE EGMTQTSSVP QETRTQHLYQ SNENSSSSSI CKDNADLLSP LKKWKSRYLM
     EQNVTKLLRP LSPVTPPPPN SGSKSPQLAT PGSSHPGEEE CRNGYSLMFS PVTSLTTASR
     CNTPLQFELC HRKDLDLAKV GYLDSNTNSC ADRPSLLNSG HSDLAPHPSL GPTSETGFPS
     RSGDGHQTLV RNSDQAFRTE FNLMYAYSPL NAMPRADGLY RGSPLVGDRK PLHLDGGYCS
     PAEGFSSRYE HGLMKDLSRG SLSPGGERAC EGVPSAPQNP PQRKKVSLLE YRKRKQEAKE
     NSAGGGGDSA QSKSKSAGAG QGSSNSVSDT GAHGVQGSSA RTPSSPHKKF SPSHSSMSHL
     EAVSPSDSRG TSSSHCRPQE NISSRWMVPT SVERLREGGS IPKVLRSSVR VAQKGEPSPT
     WESNITEKDS DPADGEGPET LSSALSKGAT VYSPSRYSYQ LLQCDSPRTE SQSLLQQSSS
     PFRGHPTQSP GYSYRTTALR PGNPPSHGSS ESSLSSTSYS SPAHPVSTDS LAPFTGTPGY
     FSSQPHSGNS TGSNLPRRSC PSSAASPTLQ GPSDSPTSDS VSQSSTGTLS STSFPQNSRS
     SLPSDLRTIS LPSAGQSAVY QASRVSAVSN SQHYPHRGSG GVHQYRLQPL QGSGVKTQTG
     LS
//
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