AF10_MOUSE
ID AF10_MOUSE Reviewed; 1068 AA.
AC O54826; Q6NS43;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein AF-10 {ECO:0000305};
GN Name=Mllt10 {ECO:0000312|MGI:MGI:1329038};
GN Synonyms=Af10 {ECO:0000303|PubMed:9878787};
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 [MRNA].
RX PubMed=9878787; DOI=10.1016/s0167-4781(98)00226-7;
RA Linder B., Jones L.K., Chaplin T., Mohd-Sarip A., Heinlein U.A.O.,
RA Young B.D., Saha V.;
RT "Expression pattern and cellular distribution of the murine homologue of
RT AF10.";
RL Biochim. Biophys. Acta 1443:285-296(1998).
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [5]
RP PROTEIN SEQUENCE OF 211-226, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; SER-532; SER-686;
RP SER-688 AND SER-691, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Kidney, 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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probably involved in transcriptional regulation. Binds to
CC cruciform DNA (By similarity). In cells, binding to unmodified histone
CC H3 regulates DOT1L functions including histone H3 'Lys-79'
CC dimethylation (H3K79me2) and gene activation (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P55197}.
CC -!- SUBUNIT: Self-associates. Interacts with FSTL3; the interaction
CC enhances MLLT10 in vitro transcriptional activity and self-association.
CC Interacts with YEATS4. Interacts with SS18. Interacts with DOT1L (By
CC similarity). Interacts with histone H3; interaction is necessary for
CC MLLT10 binding to nucleosomes; interaction is inhibited by histone H3
CC 'Lys-27' methylations (H3K27me1, H3K27me2 and H3K27me3) amd
CC acetylation; interaction stabilizes association of MLLT10 at chromatin;
CC interaction is essential for histone H3 'Lys-79' dimethylation
CC (H3K79me2) (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P55197}.
CC -!- INTERACTION:
CC O54826; Q02248: Ctnnb1; NbExp=2; IntAct=EBI-8459555, EBI-397872;
CC O54826; Q60722: Tcf4; NbExp=3; IntAct=EBI-8459555, EBI-310070;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AF010135; AAD11570.1; -; mRNA.
DR EMBL; AL928557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08096.1; -; Genomic_DNA.
DR EMBL; CH466542; EDL08097.1; -; Genomic_DNA.
DR EMBL; BC070475; AAH70475.1; -; mRNA.
DR CCDS; CCDS15708.1; -.
DR RefSeq; NP_001239489.1; NM_001252560.1.
DR RefSeq; NP_034934.2; NM_010804.4.
DR RefSeq; XP_006497440.2; XM_006497377.3.
DR AlphaFoldDB; O54826; -.
DR SMR; O54826; -.
DR BioGRID; 201436; 5.
DR DIP; DIP-58954N; -.
DR IntAct; O54826; 4.
DR STRING; 10090.ENSMUSP00000110328; -.
DR iPTMnet; O54826; -.
DR PhosphoSitePlus; O54826; -.
DR EPD; O54826; -.
DR jPOST; O54826; -.
DR MaxQB; O54826; -.
DR PaxDb; O54826; -.
DR PRIDE; O54826; -.
DR ProteomicsDB; 281946; -.
DR Antibodypedia; 1417; 392 antibodies from 33 providers.
DR DNASU; 17354; -.
DR Ensembl; ENSMUST00000028076; ENSMUSP00000028076; ENSMUSG00000026743.
DR Ensembl; ENSMUST00000114680; ENSMUSP00000110328; ENSMUSG00000026743.
DR GeneID; 17354; -.
DR KEGG; mmu:17354; -.
DR UCSC; uc008ilm.2; mouse.
DR CTD; 8028; -.
DR MGI; MGI:1329038; Mllt10.
DR VEuPathDB; HostDB:ENSMUSG00000026743; -.
DR eggNOG; KOG0956; Eukaryota.
DR GeneTree; ENSGT00940000157711; -.
DR HOGENOM; CLU_010286_0_1_1; -.
DR InParanoid; O54826; -.
DR OMA; RNDSYAH; -.
DR PhylomeDB; O54826; -.
DR TreeFam; TF316118; -.
DR BioGRID-ORCS; 17354; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Mllt10; mouse.
DR PRO; PR:O54826; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O54826; protein.
DR Bgee; ENSMUSG00000026743; Expressed in spermatocyte and 262 other tissues.
DR ExpressionAtlas; O54826; baseline and differential.
DR Genevisible; O54826; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1068
FT /note="Protein AF-10"
FT /id="PRO_0000215936"
FT ZN_FING 22..74
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 79..112
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 135..198
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 106..190
FT /note="Required for interaction with histone H3"
FT /evidence="ECO:0000250|UniProtKB:P55197"
FT REGION 207..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..780
FT /note="Leucine-zipper"
FT REGION 786..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55197"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55197"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55197"
FT CONFLICT 280
FT /note="K -> N (in Ref. 1; AAD11570)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="S -> P (in Ref. 1; AAD11570)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="F -> L (in Ref. 1; AAD11570)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="P -> T (in Ref. 1; AAD11570)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="L -> F (in Ref. 1; AAD11570)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="E -> G (in Ref. 1; AAD11570)"
FT /evidence="ECO:0000305"
FT CONFLICT 991..993
FT /note="HQA -> NKT (in Ref. 1; AAD11570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1068 AA; 113029 MW; BC88501BE15E4D8B CRC64;
MVSSDRPVSL EDEVSHSMKE MIGGCCVCSD ERGWAENPLV YCDGHGCSVA VHQACYGIVQ
VPTGPWFCRK CESQERAARV RCELCPHKDG ALKRTDNGGW AHVVCALYIP EVQFANVSTM
EPIVLQSVPH DRYNKTCYIC DEQGRESKAA TGACMTCNKH GCRQAFHVTC AQFAGLLCEE
EGNGADNVQY CGYCKYHFSK LKKSKRGSNR SYEQSLSDSS SHSQDKHHEK EKKKYKEKDK
HKQKHKKQPE PSPALVPSLT VTTEKTYTST SNNSISGSLK RLEDTAARFT NANFQEVSAH
TSSGKDVSEA RGSEGKGKKS SAHSSGQRGR KPGAGRNPGT AVSASSPFPQ GSFSGTPGSV
KSSSGSSVQS PQDFLSFTDS DLRSDSYTHT QQPSSTKDVH KGESGSQEAA VNSFSSLVGH
PVTSTVISQP KSFDNSPGEL GSSSLPTAGY KRAQTSGIEE EAVKEKKRKG NKQSKHGPGR
PKGNKNQENV SHLSVSSASP TSSVASAAGS VTSSSLQKSP TLLRNGSLQS LSVGSSPVGS
EISMQYRHDG ACPTTTFSEL LNAIHNGIYN SNDVAVSFPN VVSGSGSSTP VSSSHIPQQS
SGHLQQVGAL SPSAASSVTP AAATTQANTV SGSSLSQAPA HMYGSRLNQN PSMAVLIAQS
ESSQTDQDLG DNARSLGGRG SSPRGSLSPR SPVSNLQLRY DQPSNSSLET VPPVAASIEQ
LLERQWSEGQ QFLLEQGTPG DILGMLKSLH QLQVENRRLE EQIKNLTAKK ERLQLLNAQL
SVPFPAITTN PSPSHQMHTY TAQTAPPPDS LNSSKSPHIG NSFLPDNSLP VLNQDLTSSG
QSTSSSSALS TPPPAGQSPA QQSSGVSGVQ QVNGVTVGAL ASGMQTVTST IPAVSAVGGI
IGALPGNQLA INGIVGALNG VIQTPVTISQ NPAPLTHTSV PPNAAHPMPA AALTNSASGL
GLLSDQQRQM FIQQQQFQQL LNSQQLTPEQ HQAFLYQLMQ QQHHPPELQQ LQLPGPTQIP
INNLLAGAQA PPLHTATTNP FLTIHGDSTS QKVTRLSDKT GPVAQEKS
