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   05-OCT-2010, entry version 52.
DE   RecName: Full=Zinc finger protein 800;
GN   Name=ZNF800; ORFNames=PP902;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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.,
RA   Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA   Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA   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; SER-336; SER-387;
RP   SER-403; SER-426; SER-462 AND SER-595, AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=19007248; DOI=10.1021/ac801708p;
RA   Wang B., Malik R., Nigg E.A., Korner R.;
RT   "Evaluation of the low-specificity protease elastase for large-scale
RT   phosphoproteome analysis.";
RL   Anal. Chem. 80:9526-9533(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317; THR-319; SER-334;
RP   SER-336; SER-455; SER-457 AND SER-462, AND MASS SPECTROMETRY.
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 7 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG17274.1; Type=Frameshift; Positions=335;
CC       Sequence=AAG17274.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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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   IPI; IPI00396098; -.
DR   RefSeq; NP_789784.2; -.
DR   UniGene; Hs.159006; -.
DR   ProteinModelPortal; Q2TB10; -.
DR   SMR; Q2TB10; 483-550, 488-640.
DR   PhosphoSite; Q2TB10; -.
DR   PRIDE; Q2TB10; -.
DR   Ensembl; ENST00000265827; ENSP00000265827; ENSG00000048405.
DR   Ensembl; ENST00000393312; ENSP00000376988; ENSG00000048405.
DR   Ensembl; ENST00000393313; ENSP00000376989; ENSG00000048405.
DR   GeneID; 168850; -.
DR   KEGG; hsa:168850; -.
DR   UCSC; uc003vlw.1; human.
DR   CTD; 168850; -.
DR   GeneCards; GC07M126986; -.
DR   HGNC; HGNC:27267; ZNF800.
DR   HPA; HPA023090; -.
DR   HOGENOM; HBG714482; -.
DR   HOVERGEN; HBG106061; -.
DR   InParanoid; Q2TB10; -.
DR   OMA; VSPKKSF; -.
DR   OrthoDB; EOG9W10ZR; -.
DR   PhylomeDB; Q2TB10; -.
DR   NextBio; 88772; -.
DR   ArrayExpress; Q2TB10; -.
DR   Bgee; Q2TB10; -.
DR   CleanEx; HS_ZNF800; -.
DR   Genevestigator; Q2TB10; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Complete proteome; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    664       Zinc finger protein 800.
FT                                /FTId=PRO_0000304410.
FT   ZN_FING      69     91       C2H2-type 1; degenerate.
FT   ZN_FING     230    253       C2H2-type 2.
FT   ZN_FING     287    310       C2H2-type 3.
FT   ZN_FING     357    382       C2H2-type 4.
FT   ZN_FING     486    508       C2H2-type 5.
FT   ZN_FING     519    542       C2H2-type 6.
FT   ZN_FING     618    640       C2H2-type 7.
FT   COMPBIAS     12     15       Poly-His.
FT   MOD_RES     317    317       Phosphoserine.
FT   MOD_RES     319    319       Phosphothreonine.
FT   MOD_RES     334    334       Phosphoserine.
FT   MOD_RES     336    336       Phosphoserine.
FT   MOD_RES     350    350       Phosphoserine.
FT   MOD_RES     387    387       Phosphoserine.
FT   MOD_RES     403    403       Phosphoserine.
FT   MOD_RES     422    422       Phosphoserine (By similarity).
FT   MOD_RES     426    426       Phosphoserine.
FT   MOD_RES     455    455       Phosphoserine.
FT   MOD_RES     457    457       Phosphoserine.
FT   MOD_RES     462    462       Phosphoserine.
FT   MOD_RES     595    595       Phosphoserine.
FT   VARIANT     102    102       L -> V (in dbSNP:rs17865569).
FT                                /FTId=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
//