PRD10_MOUSE
ID PRD10_MOUSE Reviewed; 1184 AA.
AC Q3UTQ7; Q6P397;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=PR domain zinc finger protein 10;
DE EC=2.1.1.-;
DE AltName: Full=PR domain-containing protein 10;
DE AltName: Full=Tristanin;
GN Name=Prdm10; Synonyms=Gm1112, Tris;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12175877; DOI=10.1016/s0736-5748(02)00055-2;
RA Siegel D.A., Huang M.K., Becker S.F.;
RT "Ectopic dendrite initiation: CNS pathogenesis as a model of CNS
RT development.";
RL Int. J. Dev. Neurosci. 20:373-389(2002).
RN [5]
RP ERRATUM OF PUBMED:12175877.
RA Siegel D.A., Huang M.K., Becker S.F.;
RL Int. J. Dev. Neurosci. 21:169-170(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-422, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12175877}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UTQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UTQ7-2; Sequence=VSP_036382, VSP_036383;
CC -!- TISSUE SPECIFICITY: Present in brain, liver, kidney, spleen and thymus
CC (at protein level). {ECO:0000269|PubMed:12175877}.
CC -!- DOMAIN: The SET domain is degenerated, suggesting that it has lost
CC methyltransferase activity.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AK139221; BAE23923.1; -; mRNA.
DR EMBL; AC167244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064128; AAH64128.1; -; mRNA.
DR CCDS; CCDS90529.1; -. [Q3UTQ7-2]
DR AlphaFoldDB; Q3UTQ7; -.
DR SMR; Q3UTQ7; -.
DR STRING; 10090.ENSMUSP00000074104; -.
DR iPTMnet; Q3UTQ7; -.
DR PhosphoSitePlus; Q3UTQ7; -.
DR EPD; Q3UTQ7; -.
DR MaxQB; Q3UTQ7; -.
DR PeptideAtlas; Q3UTQ7; -.
DR PRIDE; Q3UTQ7; -.
DR ProteomicsDB; 289835; -. [Q3UTQ7-1]
DR ProteomicsDB; 289836; -. [Q3UTQ7-2]
DR Antibodypedia; 19222; 239 antibodies from 33 providers.
DR Ensembl; ENSMUST00000117389; ENSMUSP00000112588; ENSMUSG00000042496. [Q3UTQ7-2]
DR UCSC; uc009oro.1; mouse. [Q3UTQ7-2]
DR MGI; MGI:2682952; Prdm10.
DR VEuPathDB; HostDB:ENSMUSG00000042496; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158740; -.
DR HOGENOM; CLU_749978_0_0_1; -.
DR InParanoid; Q3UTQ7; -.
DR PhylomeDB; Q3UTQ7; -.
DR ChiTaRS; Prdm10; mouse.
DR PRO; PR:Q3UTQ7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3UTQ7; protein.
DR Bgee; ENSMUSG00000042496; Expressed in animal zygote and 211 other tissues.
DR ExpressionAtlas; Q3UTQ7; baseline and differential.
DR Genevisible; Q3UTQ7; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd19194; PR-SET_PRDM10; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044403; PRDM10_PR/SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 4.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1184
FT /note="PR domain zinc finger protein 10"
FT /id="PRO_0000363963"
FT DOMAIN 202..320
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 349..371
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 520..542
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 550..572
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 578..600
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 606..629
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 662..685
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 717..740
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 850..873
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 122..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..152
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..398
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV6"
FT MOD_RES 422
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV6"
FT VAR_SEQ 318..341
FT /note="WYAASYAEFVNQKIHDISEEERKV -> QNWIHSCLPARVMIRALSYKRILP
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_036382"
FT VAR_SEQ 342..1184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_036383"
FT CONFLICT 227
FT /note="F -> S (in Ref. 1; BAE23923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1184 AA; 133746 MW; 99563C0C4184C15D CRC64;
MDPKDESAHV WPTSADHEQS TAQVHFVPDA GTVAQIVYTD DQVRPPQQVV YTADGASYTS
VDGPEHTLVY IHPVEAAQTL FTDPAQVAYV QQDATAQQVL PSIESVHGSD PLATLQNPIA
RLDAKEEEEE EEDEDEDTEE EEEEDAEDTD VDDWQPDPPR PFDPHDLWCE ECNNAHSSVC
PKHGPLHPIP NRPVLTRARA SLPLVLYIDR FLGGVFSKRR IPKRTQFGPV EGPLVRGSEL
KDCYIHLKVS LDKGDRKDRD LHEDLWFELS DETLCNWMMF VRPAQNHLEQ NLVAYQYGHH
VYYTTIKNVE PKQELKVWYA ASYAEFVNQK IHDISEEERK VLREQEKNWP CYECNRRFIS
SEQLQQHLNS HDEKLDVFTR TRGRGRGRGK RRFGPGRRPG RPPKFIRLEI TSENGEKSDD
GTQDLLHFPT KEQFDEAEPA TLNGLDQPEQ ASIPIPQLPQ ETPPSLEQEP ETHTLHLQPQ
QEESLVPTQT TLTADDMRRA KRIRNAALQH LFIRKSFRPF KCLQCGKAFR EKDKLDQHLR
FHGREGNCPL TCDLCNKGFI SSASLESHMK LHSDQKTYSC IFCPESFDRL DLLKDHVAIH
VNDGCFTCPT CKKRFPDFIQ VKKHVRSFHS EKIYQCTECD KAFCRPDKLR LHMLRHSDRK
DFLCSTCGKQ FKRKDKLREH MQRMHNPERE AKKADRISRS KTFKPRITST DYDSFTFKCR
LCMMGFRRRG MLVNHLSKRH PDMKIEEVPE LTLPIIKPNR DYFCQYCDKN EMSYFALSKK
VALYIAFMVK YLTLQVYKSA SKRKAHILKN HPGAELPPSI RKLRPAGPGE PDPMLSTHTQ
LTGTIATPPV CCPHCSKQYS SKTKMVQHIR KKHPEYAQLP NTIHTPLTTA VISATPAVLT
TDSATGETVV TTDLLTQAMT ELSQTLTTDY RTPQGDYQRI QYIPVSQSAS GLQQPQHIQL
QVVQVAPATS PHQSQQSTVD VGQLHDPQTY TQHAIQVQHI QVTEPAPAAP SASQVAGQPL
SPSAQQVQQG LSPSHIQGSS STQGQALQQQ QNSSVQHTYL PNAWNSFRGY SAVSAGDTSH
ESASEIQMMT LPPGQFVITD SGVATPVTSG QVKAVTPGHY VLSESQPELE EKQASALSGA
VQVQPSAHSD SLDSTGPSQQ QTTQYIITTT TNGNGGSEVH ITKP
