ZN646_MOUSE
ID ZN646_MOUSE Reviewed; 1788 AA.
AC Q6NV66;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Zinc finger protein 646 {ECO:0000305};
GN Name=Zfp646 {ECO:0000312|MGI:MGI:3665412};
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].
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 [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 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).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AC149222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC068300; AAH68300.1; -; mRNA.
DR EMBL; BC079907; AAH79907.1; -; mRNA.
DR CCDS; CCDS21882.1; -.
DR RefSeq; NP_766337.2; NM_172749.4.
DR RefSeq; XP_006507820.1; XM_006507757.3.
DR RefSeq; XP_006507821.1; XM_006507758.3.
DR RefSeq; XP_017177704.1; XM_017322215.1.
DR RefSeq; XP_017177705.1; XM_017322216.1.
DR RefSeq; XP_017177706.1; XM_017322217.1.
DR AlphaFoldDB; Q6NV66; -.
DR STRING; 10090.ENSMUSP00000052641; -.
DR iPTMnet; Q6NV66; -.
DR PhosphoSitePlus; Q6NV66; -.
DR EPD; Q6NV66; -.
DR MaxQB; Q6NV66; -.
DR PaxDb; Q6NV66; -.
DR PeptideAtlas; Q6NV66; -.
DR PRIDE; Q6NV66; -.
DR ProteomicsDB; 343228; -.
DR Antibodypedia; 27569; 27 antibodies from 12 providers.
DR DNASU; 233905; -.
DR Ensembl; ENSMUST00000050383; ENSMUSP00000052641; ENSMUSG00000049739.
DR GeneID; 233905; -.
DR KEGG; mmu:233905; -.
DR UCSC; uc009jxb.1; mouse.
DR CTD; 233905; -.
DR MGI; MGI:3665412; Zfp646.
DR VEuPathDB; HostDB:ENSMUSG00000049739; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161588; -.
DR HOGENOM; CLU_002678_44_18_1; -.
DR InParanoid; Q6NV66; -.
DR OMA; GWESQPD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6NV66; -.
DR TreeFam; TF350868; -.
DR BioGRID-ORCS; 233905; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Zfp646; mouse.
DR PRO; PR:Q6NV66; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6NV66; protein.
DR Bgee; ENSMUSG00000049739; Expressed in spermatocyte and 189 other tissues.
DR ExpressionAtlas; Q6NV66; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00355; ZnF_C2H2; 29.
DR SUPFAM; SSF57667; SSF57667; 13.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 27.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 27.
PE 1: Evidence at protein level;
KW Isopeptide bond; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1788
FT /note="Zinc finger protein 646"
FT /id="PRO_0000447436"
FT ZN_FING 8..31
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 67..89
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 231..253
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 258..280
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 286..308
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 366..389
FT /note="C2H2-type 6; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 393..415
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 457..479
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 484..506
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 606..628
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 633..655
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 806..828
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 833..855
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 866..889
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1035..1057
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1062..1084
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1170..1192
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1197..1219
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1225..1247
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1266..1285
FT /note="C2H2-type 20; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1293..1315
FT /note="C2H2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1333..1355
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1550..1572
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1640..1662
FT /note="C2H2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1667..1689
FT /note="C2H2-type 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1695..1717
FT /note="C2H2-type 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1724..1746
FT /note="C2H2-type 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 28..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15015"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15015"
FT CROSSLNK 526
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15015"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15015"
FT CROSSLNK 1127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15015"
FT CROSSLNK 1138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15015"
FT CROSSLNK 1148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15015"
SQ SEQUENCE 1788 AA; 196805 MW; E6CB9191590E09F3 CRC64;
MEDMPLSFSC SDCQRHFPNL PELARHRELR HSSAKQDGEE ADGIPHPYGS HPENLANHQR
NHETLFFPCT TCGKDFSNRL ALQSHMRTHA PESHRRHGPP HAMETAPHLG SETMATDSWG
QRLGSGEGWE NQTKLVRETH DWESGADPRA ASGTWEDPPT KQRQGLEMQP DSKGGTADWV
PAVSSEGASP LPTPASNLLS NLEQYLAESV VNFTEAQEPT EPLPTEGERK YRCSECGKTY
KHAGSLTNHR QSHTLGIYPC SICFKEFSNL MALKNHSRLH AQYRPYHCPH CPRAFRLPRD
LLEHQQSHEG LKQEQPWEDK EMPTTNGHAD ERSWGQLSKT GMLNGSGELS SSGQLEDGGS
EEYRPFCCGD CGRTYRHAGS LINHRKSHQT GIYPCSICSK QLFNAAALKN HIRAHHRPRQ
GAGEGGQSSV SSTALTSAEN TPKVDEVPTA SLDHRPYKCN ECGRAYRHRG SLVNHRHSHR
TGEYQCSLCP RKYPNLMALR NHVRVHCKAT RRSTDPGTEG SPSPVKKEQH DPVGMEAAFH
GDEEHACKRE EEATSNPSMA DRTVPQVCSI CGMLFEDLKS LEHHSVTHRE GEKSRTDSTV
SPTRTFACQD CGKSYRHSGS LINHRQTHQT GDFSCGACAK HFHTMAAMKS HLRRHSRQWN
RRRQKQDSGT GEVATLPPGG AWTLKLENDE DPDSSQDPLG ESPCETEDNL ERDGDCLQAG
SRGNECVLKR EEACFLGDKE GTEEGLEERE ACFLDDLGTP GDECNETGFC GGLPGMDSDR
KRGICHSDSS SHPADADTVW KAAATHTCSD CGDSFSHAAG LLSHRSCHPP GIYQCSLCPK
EFDSLPALRS HFQTHRPGEV ASAQPFLCCL CGMIFPGRTG YRRHLRQAHG ASAMTEGSEE
EEEGTAETAS THSPPLQLSE AELLNQLQRE VEALDGAGYG HICGCCGQTY DDLGSLERHH
QSQSSSNRTE NVPSHLEGAG DATEMVADHG FEGTVTSVSE EGGDIKSEEG VGGTVADSLC
MQAGESFLES HPRPFQCNQC GKTYRHGGSL VNHRKIHQTG DFICPVCSRC YPNLAAYRNH
LRNHPRCKGS EPQMGPISEA GGCSEPQNAA EAGQEQAVIG QLQEELKVEP LEELAGVKEE
VWEGTAVKEE ELEQELETGC QTEVTSERPF SCEVCGRTYK HAGSLINHRQ SHQTGHFGCQ
ACSKGFSNLM SLKNHRRIHA DPRQFRCSEC GKAFRLRKQL ANHQRVHAER RRSRGTQKLT
REDRPFRCGQ CGRTYRHAGS LMNHQCNPEA SRYSCPFCFK TYSNRTALKD HQRVHSDSQQ
RRQSGCPQRA AAVRCTLCGC GFSGQGSLEQ HLQEHEDTKL EVASGQGGQH ATEGSEENLD
DWGLEGRSDG TEVLQVEHET KRPGGHSQSP SSPACSGGTE STQQVGKVDG SQGDRGQMNH
NGAWVLQDQL TKPEGKLEDT VSRNPCHLSE SQSNGPTLRY RDSWKGADSG SQLQPESHCC
SQCGKAYCQP DGLLNPSING KDCHICLLCS KEFLNPVTTE IHNHTTAQRF ACSNCSKVCE
SHSELATHMK THAVEHSQMS GQMEKTRGPQ AGMAEVGPPG PGKAQEAPSE LPGDPEENGV
PANGGQGIHF PAAEDKERPF CCAQCGRSYR HAGSLLNHQK AHTIGLYPCS LCPKLLPNLL
SLKNHSRTHT DPKRYSCNIC GKAFRTAARL QGHGRVHAPQ EGPFTCSHCP RRFRHRISFL
RHQQQHQEEW PVSSSGASVA PAASREDSST ASLPNPSPQW PADLSLSL
