ID A0A2K5NMW0_CERAT Unreviewed; 1102 AA.
AC A0A2K5NMW0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=MLLT6, PHD finger containing {ECO:0000313|Ensembl:ENSCATP00000038869.1};
GN Name=MLLT6 {ECO:0000313|Ensembl:ENSCATP00000038869.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000038869.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000038869.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K5NMW0; -.
DR STRING; 9531.ENSCATP00000038869; -.
DR Ensembl; ENSCATT00000063177.1; ENSCATP00000038869.1; ENSCATG00000042085.1.
DR GeneTree; ENSGT00940000158572; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000042085; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:Ensembl.
DR GO; GO:0035811; P:negative regulation of urine volume; IEA:Ensembl.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0036359; P:renal potassium excretion; IEA:Ensembl.
DR GO; GO:0035812; P:renal sodium excretion; IEA:Ensembl.
DR GO; GO:0070295; P:renal water absorption; IEA:Ensembl.
DR CDD; cd15574; PHD_AF10_AF17; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR049781; AF10/AF17_PHD.
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 PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR PANTHER; PTHR13793:SF90; PROTEIN AF-17; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 5..57
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 62..187
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 191..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 728..762
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 237..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..397
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 112809 MW; 45E149F2AA272276 CRC64;
MKEMVGGCCV CSDERGWAEN PLVYCDGHAC SVAVHQACYG IVQVPTGPWF CRKCESQERA
ARVRCELCPH KDGALKRTDN GGWAHVVCAL YIPEVQFANV LTMEPIVLQY VPHDRFNKTC
YICEEQGRES KAASGACMTC NRHGCRQVAH LICGLSRLSA QMAGLLCEEE VLEVDNVKYC
GYCKYHFSKM KTSRHSSGGG GGGTGGGGGS GGSMGGGGSG FISGRRSRSA SPSTQQEKHP
THHERGQKKS RKDKERLKQK HKKRPESPPS ILTPPVVPTA DKVSSSASSS SHHEASTQET
SESSRDSKGK KSSSHSLSHK GKKLSSGKGV SSFTSASSSS SSSSSSSGGP FQPAVSSLQS
SPDFSAFPKL EQPEEDKYSK PTAPAPSAPP SPSAPEPPKA DLFEQKVVFS GFGPIMRFST
TTSSSGRARA PSPGDYKSPH VTGSGASAGT HKRMPALSAT PVPADETPET GLKEKKHKAS
KRSRHGPGRP KGSRNKEGTG GPAAPSLPSA QLAGFTATAA SPFSGGSLVS SGLGGLASRT
FGPSGSLPSL SLESPLLGAG IYTSNKDPIS HSGGMLRAVC STPLSSSLLG PPGTSALPRL
SRSPFTSTLP SSSASISTTQ VFSLAGSTFS LPSAHIFGTP MGAVNPLLAQ AESSHTEPDL
EDCSFRCRGT SPQESLSSMS PISSLPALFD QTASAPCGGG QLDPAAPGTT NMEQLLEKQG
DGEAGVNIVE MLKALHALQK ENQRLQEQIL SLTAKKERLQ ILNVQLSVPF PALPAALPAA
NGPVPGPYGL PPQAGSSDSL STSKSPPGKS SLGLDNSLST SSEDPHSGCP SRSSSSLSFH
STPPPLPLLQ QSPATLPLAL PGAPAPLPPQ PQNGLGRAPG AAGLGAMPMA EGLLGGLAGS
GGLPLNGLLG GLNGAAAPNP ASLSQAGGAP TLQLPGCLNS LTEQQRHLLQ QQEQQLQQLQ
QLLASPQLTP EHQTVVYQMI QQIQQKRELQ RLQMAGGSQL PMASLLAGSS TPLLSAGTPG
LLPTASAPPL LPAGALVAPS LGNNTSLMAA AAAAAAVAAA GGPPVLTAQT NPFLSLSGAD
GSGGGPKGGT ADKGASVNQE KG
//
