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Database: UniProt
Entry: H0VU90_CAVPO
LinkDB: H0VU90_CAVPO
Original site: H0VU90_CAVPO 
ID   H0VU90_CAVPO            Unreviewed;      1702 AA.
AC   H0VU90;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=SET domain containing 1A, histone lysine methyltransferase {ECO:0000313|Ensembl:ENSCPOP00000014263.1};
GN   Name=SETD1A {ECO:0000313|Ensembl:ENSCPOP00000014263.1};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000014263.1, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000014263.1}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000014263.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AAKN02007783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003477932.1; XM_003477884.3.
DR   RefSeq; XP_012997158.1; XM_013141704.1.
DR   RefSeq; XP_012997159.1; XM_013141705.1.
DR   STRING; 10141.ENSCPOP00000014263; -.
DR   Ensembl; ENSCPOT00000024181.2; ENSCPOP00000014263.1; ENSCPOG00000025456.2.
DR   GeneID; 100715930; -.
DR   KEGG; cpoc:100715930; -.
DR   CTD; 9739; -.
DR   VEuPathDB; HostDB:ENSCPOG00000025456; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   GeneTree; ENSGT00940000154575; -.
DR   HOGENOM; CLU_001226_2_0_1; -.
DR   InParanoid; H0VU90; -.
DR   OMA; KVSRYPD; -.
DR   OrthoDB; 950362at2759; -.
DR   TreeFam; TF106436; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000025456; Expressed in pituitary gland and 13 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IEA:Ensembl.
DR   GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:1902275; P:regulation of chromatin organization; IEA:Ensembl.
DR   GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; IEA:Ensembl.
DR   CDD; cd12548; RRM_Set1A; 1.
DR   CDD; cd19169; SET_SETD1; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR024657; COMPASS_Set1_N-SET.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR044570; Set1-like.
DR   InterPro; IPR034467; Set1A_RRM.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR037841; SET_SETD1A/B.
DR   PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   PANTHER; PTHR45814:SF3; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1A; 1.
DR   Pfam; PF11764; N-SET; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01291; N-SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}; S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          84..172
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          1563..1680
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1686..1702
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          194..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..853
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          893..1243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1260..1286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1341..1413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1466..1494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..443
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..579
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..654
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..919
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..963
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        970..990
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1014
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1015..1053
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1068..1088
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1113..1134
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1141..1155
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1219..1238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1353..1369
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1398..1412
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1472..1486
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1702 AA;  185558 MW;  04C88319927D6920 CRC64;
     MDQEGGGDGQ KAPSFQWRNY KLIVDPALDP ALRRPSQKVY RYDGIHFSVN DSKYIPVEDL
     QDPRCHVRSK NRDFSLPVPK FKLDEFYIGQ IPLKEVTFAR LNDNVRETFL KDMCRKYGEV
     EEVEILLHPR TRKHLGLARV LFTSTRGAKE TVKNLHLTSV MGNIIHAQLD IKGQQRMKYY
     ELIVNGSYTP QTVPTGGKAL SEKFQGSGAA TETTESRRRS SSDTAAYPSG TAVVGTPGNG
     TPCSQDTSFS SSRQDTPSSF GQFTPQSSQG TPYTSRGSTP YSQDSAYSSS TTSTSFKPRR
     SENSYQDSFS RRHFSASSVP TTVSTAISAT TAATAASSSS SSSSSSSSTS SSSSSSQFRG
     SDSNYPAYYE SWNRYQRHAS YPPRRATREE PSGAPFSEST AERFPPSYTS YLPPEPSRST
     DQDYRPPASE APPPEPPEPG GGGGGGGPSP EREEARTSPR AASPTRSGSP APETTNESVP
     FAQHSSLDSR IEMLLKEQRS KFSFLASDTE EEEENCSAGS GARDTGSEVP SGSGHGPCTP
     PPAPANFEDV APTGSGEPGA TRESPKTNGQ NQASPCSSGE DMEISDDDRG GSPPPAPTPP
     QQPPPPPPPP PPPPPYLASL PLGYPPHQPA YLLPPRPDGP PPPEYPPPPP PPPHIYDFVN
     SLELMDRLGA QWGGMPMSFQ MQTQMLTRLH QLRQGKGLTA ASAGPPGGAF GEAFLPFPPP
     QEAAYGLPYA LYTQGQEGRG AYTREAYHLP LPMAAEPLPS SSVSGEEARL PPREEAELAE
     GKALPSAGTV GRVLATLVQE MKSIMQRDLN RKMVENVAFG AFDQWWESKE EKAKPFQNAA
     KQQAKEEDKE KTKLKEPGML SLVDWAKSGG TTGIEAFTFG SGLRGALRLP SFKVKRKEPS
     EISEASEEKR PRPSTPAEED EDDPERDKEV GEPGRPGSKP PKRDEERGKT QGKHRKSFAL
     DSEGEEASQE SSSDKDEEED EEDEEDEDRE EAVDTTKKET EASDGEDEES DASSKCSLYA
     DSDGENGSTS DSESSTSSSS SSSSSSSSSS SSSESSEEEE EEEQPTTIPS ASPPPREVPE
     PLPAPAKEPE PETAVGSPVV PLPEQEKSPA RPAGPTEEPP PSVPQPPSEP QTGPSAPSPH
     LDERPSSPIP LLPPPKKRRK TVSFSTAEEV PAPEPPPAAL PQAKSPGTVS RKVPRGAERT
     IRNLPLDHAS LVKSWPEEVS RGGRNRAGGR GRSMEEEEVE PGTEVDLAVL ADLALTPARR
     GLAALPPGDD SEATETSDEA DRLCPPLNHI LLEHNYALAI KPTPSTPPPR LPEPVLAPAA
     LFSSPADEVL EAPEVVVAEA EEPKPQQQLQ VQQEEGEEEE EEEEESESSE SSSSSSSSDG
     DGAGRRRSLR SHARRRRPPL PPPPPPPPSF EPRSEFEQMT ILYDIWNSGL DLEDMSYLRL
     TYERLLQQTS GADWLNDTHW VHHTITNLST PKRKRRPQDG PREHQTGSAR SEGYYPISKK
     EKDKYLDVCP VSARQLEGVD TQGTNRVLSE RRSEQRRLLS AIGTSAIMDS DLLKLNQLKF
     RKKKLRFGRS RIHEWGLFAM EPIAADEMVI EYVGQNIRQM VADMREKRYV QEGIGSSYLF
     RVDHDTIIDA TKCGNLARFI NHCCTPNCYA KVITIESQKK IVIYSKQPIG VDEEITYDYK
     FPLEDNKIPC LCGTESCRGS LN
//
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