ID A2AS70_MOUSE Unreviewed; 990 AA.
AC A2AS70;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Myeloid/lymphoid or mixed-lineage leukemia; translocated to, 10 {ECO:0000313|Ensembl:ENSMUSP00000110319.2};
GN Name=Mllt10 {ECO:0000313|Ensembl:ENSMUSP00000110319.2,
GN ECO:0000313|MGI:MGI:1329038};
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 {ECO:0000313|Ensembl:ENSMUSP00000110319.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000110319.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110319.2,
RC ECO:0000313|Proteomes:UP000000589};
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 [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000110319.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110319.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; NP_001239490.1; NM_001252561.1.
DR RefSeq; XP_017171568.1; XM_017316079.1.
DR AlphaFoldDB; A2AS70; -.
DR SMR; A2AS70; -.
DR jPOST; A2AS70; -.
DR MaxQB; A2AS70; -.
DR PeptideAtlas; A2AS70; -.
DR ProteomicsDB; 365175; -.
DR Antibodypedia; 1417; 459 antibodies from 33 providers.
DR DNASU; 17354; -.
DR Ensembl; ENSMUST00000114671.8; ENSMUSP00000110319.2; ENSMUSG00000026743.17.
DR GeneID; 17354; -.
DR UCSC; uc008ilp.2; mouse.
DR AGR; MGI:1329038; -.
DR CTD; 8028; -.
DR MGI; MGI:1329038; Mllt10.
DR VEuPathDB; HostDB:ENSMUSG00000026743; -.
DR GeneTree; ENSGT00940000157711; -.
DR BioGRID-ORCS; 17354; 5 hits in 83 CRISPR screens.
DR ChiTaRS; Mllt10; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000026743; Expressed in spermatocyte and 264 other cell types or tissues.
DR ExpressionAtlas; A2AS70; baseline and differential.
DR Genevisible; A2AS70; MM.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20901; CC_AF10; 1.
DR CDD; cd15708; ePHD_AF10; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR049773; AF10-like_CC.
DR InterPro; IPR049775; AF10_ePHD.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR PANTHER; PTHR13793:SF93; PROTEIN AF-10; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00249; PHD; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|EPD:A2AS70,
KW ECO:0007829|PeptideAtlas:A2AS70};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 1..120
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 56..119
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 129..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 664..701
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 261..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 990 AA; 104528 MW; 9B013801A209E15C CRC64;
MKRCELCPHK DGALKRTDNG GWAHVVCALY IPEVQFANVS TMEPIVLQSV PHDRYNKTCY
ICDEQGRESK AATGACMTCN KHGCRQAFHV TCAQFAGLLC EEEGNGADNV QYCGYCKYHF
SKLKKSKRGS NRSYEQSLSD SSSHSQDKHH EKEKKKYKEK DKHKQKHKKQ PEPSPALVPS
LTVTTEKTYT STSNNSISGS LKRLEDTAAR FTNANFQEVS AHTSSGKDVS EARGSEGKGK
KSSAHSSGQR GRKPGAGRNP GTAVSASSPF PQGSFSGTPG SVKSSSGSSV QSPQDFLSFT
DSDLRSDSYT HTQQPSSTKD VHKGESGSQE AAVNSFSSLV GHPVTSTVIS QPKSFDNSPG
ELGSSSLPTA GYKRAQTSGI EEEAVKEKKR KGNKQSKHGP GRPKGNKNQE NVSHLSVSSA
SPTSSVASAA GSVTSSSLQK SPTLLRNGSL QSLSVGSSPV GSEISMQYRH DGACPTTTFS
ELLNAIHNGI YNSNDVAVSF PNVVSGSGSS TPVSSSHIPQ QSSGHLQQVG ALSPSAASSV
TPAAATTQAN TVSGSSLSQA PAHMYGSRLN QNPSMAVLIA QSESSQTDQD LGDNARSLGG
RGSSPRGSLS PRSPVSNLQL RYDQPSNSSL ETVPPVAASI EQLLERQWSE GQQFLLEQGT
PGDILGMLKS LHQLQVENRR LEEQIKNLTA KKERLQLLNA QLSVPFPAIT TNPSPSHQMH
TYTAQTAPPP DSLNSSKSPH IGNSFLPDNS LPVLNQDLTS SGQSTSSSSA LSTPPPAGQS
PAQQSSGVSG VQQVNGVTVG ALASGMQTVT STIPAVSAVG GIIGALPGNQ LAINGIVGAL
NGVIQTPVTI SQNPAPLTHT SVPPNAAHPM PAAALTNSAS GLGLLSDQQR QMFIQQQQFQ
QLLNSQQLTP EQHQAFLYQL MQQQHHPPEL QQLQLPGPTQ IPINNLLAGA QAPPLHTATT
NPFLTIHGDS TSQKVTRLSD KTGPVAQEKS
//
