ID ZN800_HUMAN Reviewed; 664 AA.
AC Q2TB10; Q9HBN0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=Zinc finger protein 800;
GN Name=ZNF800; ORFNames=PP902;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-471.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317; THR-319; SER-336;
RP SER-455 AND SER-457, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-319, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-409, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-409, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-409, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-409, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-132; LYS-279; LYS-392; LYS-409;
RP LYS-476 AND LYS-599, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAG17274.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG17274.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; CH471070; EAW83626.1; -; Genomic_DNA.
DR EMBL; BC110623; AAI10624.1; -; mRNA.
DR EMBL; BC110624; AAI10625.1; -; mRNA.
DR EMBL; AF218032; AAG17274.1; ALT_SEQ; mRNA.
DR CCDS; CCDS5795.1; -.
DR RefSeq; NP_789784.2; NM_176814.4.
DR RefSeq; XP_005250238.1; XM_005250181.3.
DR AlphaFoldDB; Q2TB10; -.
DR BioGRID; 127973; 48.
DR IntAct; Q2TB10; 19.
DR MINT; Q2TB10; -.
DR STRING; 9606.ENSP00000265827; -.
DR GlyGen; Q2TB10; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q2TB10; -.
DR PhosphoSitePlus; Q2TB10; -.
DR SwissPalm; Q2TB10; -.
DR BioMuta; ZNF800; -.
DR DMDM; 121941799; -.
DR EPD; Q2TB10; -.
DR jPOST; Q2TB10; -.
DR MassIVE; Q2TB10; -.
DR MaxQB; Q2TB10; -.
DR PaxDb; 9606-ENSP00000376989; -.
DR PeptideAtlas; Q2TB10; -.
DR ProteomicsDB; 61479; -.
DR Pumba; Q2TB10; -.
DR Antibodypedia; 17720; 97 antibodies from 18 providers.
DR DNASU; 168850; -.
DR Ensembl; ENST00000265827.8; ENSP00000265827.3; ENSG00000048405.11.
DR Ensembl; ENST00000393312.5; ENSP00000376988.1; ENSG00000048405.11.
DR Ensembl; ENST00000393313.5; ENSP00000376989.1; ENSG00000048405.11.
DR GeneID; 168850; -.
DR KEGG; hsa:168850; -.
DR MANE-Select; ENST00000265827.8; ENSP00000265827.3; NM_176814.5; NP_789784.2.
DR UCSC; uc003vly.2; human.
DR AGR; HGNC:27267; -.
DR CTD; 168850; -.
DR DisGeNET; 168850; -.
DR GeneCards; ZNF800; -.
DR HGNC; HGNC:27267; ZNF800.
DR HPA; ENSG00000048405; Tissue enhanced (bone).
DR neXtProt; NX_Q2TB10; -.
DR OpenTargets; ENSG00000048405; -.
DR PharmGKB; PA162410582; -.
DR VEuPathDB; HostDB:ENSG00000048405; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00390000008140; -.
DR HOGENOM; CLU_015050_0_0_1; -.
DR InParanoid; Q2TB10; -.
DR OMA; HSESKHD; -.
DR OrthoDB; 5392910at2759; -.
DR PhylomeDB; Q2TB10; -.
DR TreeFam; TF333197; -.
DR PathwayCommons; Q2TB10; -.
DR SignaLink; Q2TB10; -.
DR BioGRID-ORCS; 168850; 21 hits in 1192 CRISPR screens.
DR ChiTaRS; ZNF800; human.
DR GenomeRNAi; 168850; -.
DR Pharos; Q2TB10; Tdark.
DR PRO; PR:Q2TB10; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q2TB10; Protein.
DR Bgee; ENSG00000048405; Expressed in bone marrow cell and 164 other cell types or tissues.
DR ExpressionAtlas; Q2TB10; baseline and differential.
DR Genevisible; Q2TB10; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090425; P:acinar cell differentiation; IEA:Ensembl.
DR GO; GO:0031018; P:endocrine pancreas development; IEA:Ensembl.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
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; UNCHARACTERIZED; 1.
DR PANTHER; PTHR21020:SF0; ZINC FINGER PROTEIN 800; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR Pfam; PF16624; zf-C2H2_assoc2; 1.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
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..664
FT /note="Zinc finger protein 800"
FT /id="PRO_0000304410"
FT ZN_FING 69..91
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 230..253
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 287..310
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 486..508
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 519..542
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 618..640
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 154..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VEE6"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VEE6"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VEE6"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 392
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 409
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 409
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 476
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 599
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 102
FT /note="L -> V (in dbSNP:rs17865569)"
FT /id="VAR_052904"
SQ SEQUENCE 664 AA; 75236 MW; F0F0DA1214AC6F2E CRC64;
MPLRDKYCQT DHHHHGCCEP VYILEPGDPP LLQQPLQTSK SGIQQIIECF RSGTKQLKHI
LLKDVDTIFE CKLCRSLFRG LPNLITHKKF YCPPSLQMDD NLPDVNDKQS QAINDLLEAI
YPSVDKREYI IKLEPIETNQ NAVFQYISRT DNPIEVTESS STPEQTEVQI QETSTEQSKT
VPVTDTEVET VEPPPVEIVT DEVAPTSDEQ PQESQADLET SDNSDFGHQL ICCLCRKEFN
SRRGVRRHIR KVHKKKMEEL KKYIETRKNP NQSSKGRSKN VLVPLSRSCP VCCKSFATKA
NVRRHFDEVH RGLRRDSITP DIATKPGQPL FLDSISPKKS FKTRKQKSSS KAEYNLTACK
CLLCKRKYSS QIMLKRHMQI VHKITLSGTN SKREKGPNNT ANSSEIKVKV EPADSVESSP
PSITHSPQNE LKGTNHSNEK KNTPAAQKNK VKQDSESPKS TSPSAAGGQQ KTRKPKLSAG
FDFKQLYCKL CKRQFTSKQN LTKHIELHTD GNNIYVKFYK CPLCTYETRR KRDVIRHITV
VHKKSSRYLG KITASLEIRA IKKPIDFVLN KVAKRGPSRD EAKHSDSKHD GTSNSPSKKY
EVADVGIEVK VTKNFSLHRC NKCGKAFAKK TYLEHHKKTH KANASNSPEG NKTKGRSTRS
KALV
//
