ZN800_MOUSE
ID ZN800_MOUSE Reviewed; 662 AA.
AC Q0VEE6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Zinc finger protein 800;
GN Name=Znf800; Synonyms=Zfp800;
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 TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318; SER-337; SER-420;
RP SER-455; SER-458 AND SER-460, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
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.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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 EMBL; BC119236; AAI19237.1; -; mRNA.
DR EMBL; BC119262; AAI19263.1; -; mRNA.
DR CCDS; CCDS39445.1; -.
DR RefSeq; NP_001075147.1; NM_001081678.1.
DR RefSeq; XP_006505214.1; XM_006505151.1.
DR RefSeq; XP_006505215.1; XM_006505152.3.
DR AlphaFoldDB; Q0VEE6; -.
DR BioGRID; 553137; 1.
DR STRING; 10090.ENSMUSP00000110976; -.
DR iPTMnet; Q0VEE6; -.
DR PhosphoSitePlus; Q0VEE6; -.
DR EPD; Q0VEE6; -.
DR jPOST; Q0VEE6; -.
DR MaxQB; Q0VEE6; -.
DR PaxDb; Q0VEE6; -.
DR PRIDE; Q0VEE6; -.
DR ProteomicsDB; 299603; -.
DR Antibodypedia; 17720; 80 antibodies from 17 providers.
DR Ensembl; ENSMUST00000035930; ENSMUSP00000039222; ENSMUSG00000039841.
DR Ensembl; ENSMUST00000115320; ENSMUSP00000110975; ENSMUSG00000039841.
DR Ensembl; ENSMUST00000115321; ENSMUSP00000110976; ENSMUSG00000039841.
DR GeneID; 627049; -.
DR KEGG; mmu:627049; -.
DR UCSC; uc009bcm.1; mouse.
DR CTD; 627049; -.
DR MGI; MGI:1889334; Zfp800.
DR VEuPathDB; HostDB:ENSMUSG00000039841; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00390000008140; -.
DR HOGENOM; CLU_015050_0_0_1; -.
DR InParanoid; Q0VEE6; -.
DR OMA; CCEPVYL; -.
DR OrthoDB; 1528947at2759; -.
DR PhylomeDB; Q0VEE6; -.
DR TreeFam; TF333197; -.
DR BioGRID-ORCS; 627049; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Zfp800; mouse.
DR PRO; PR:Q0VEE6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q0VEE6; protein.
DR Bgee; ENSMUSG00000039841; Expressed in spermatocyte and 221 other tissues.
DR ExpressionAtlas; Q0VEE6; baseline and differential.
DR Genevisible; Q0VEE6; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR041697; Znf-C2H2_11.
DR InterPro; IPR039149; ZNF800.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR21020; PTHR21020; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..662
FT /note="Zinc finger protein 800"
FT /id="PRO_0000304411"
FT ZN_FING 69..91
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 231..254
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 288..311
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 357..382
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 484..506
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 517..540
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 616..638
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 172..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 320
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2TB10"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2TB10"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2TB10"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q2TB10"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q2TB10"
FT CROSSLNK 392
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q2TB10"
FT CROSSLNK 474
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q2TB10"
FT CROSSLNK 597
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q2TB10"
SQ SEQUENCE 662 AA; 74813 MW; 037359A69380D96D CRC64;
MPLRDKYCQT DHHHHGCCEP VYILEPGDPP LLQQPVQTSK SGIQQIIECF RSGTKQLKHI
LLKDVDTIFE CKLCRSLFRG LPNLITHKKF YCPPSLQMDD NLPDVNDKQS QAISDLLEAI
YPRVDKREYI IKLEPIETNQ NAVFQYISRT DNPAEVTESS STPEQTEVQI QETSSEQLKA
VPDADTEVEE AIEPPSIETV VDEAAAPTEE QPQESQADLE TSDSSDLGHQ LICCLCRKEF
NSRRGVRRHI RKVHKKKMEE LKKYIETRKT PNQSSKGRSK SVLVSLSRSC PVCCKSFATK
ANVRRHFDEV HRGLRRDSIT PDIATKPGQP LFLDSASPKK SFKTRKQKSS KAEYNLTACK
CLLCKRKYSS QIMLKRHMQI VHKITLSGAN SKREKGPNNT ANSSEVKVEL ADSVESSPPS
ITHSPQNELK GTNHSNEKKN TPATQKNKVK QDSESPKSAS PSAAGGQQKT RKPKLSAGFD
FKQLYCKLCK RQFTSKQNLT KHIELHTDGN NIYVKFYKCP LCTYETRRKR DVIRHITVVH
KKSSRYLGKI TASLEIRAIK KPIDFVLNKV AKRGPSREEA KHNDSKQDGT SNSPSKKYEV
ADVGIEVKVT KNFSLHRCNK CGKAFAKKTY LEHHKKTHKA NATNSPEGNK TKGRSTRSKA
LV
