ID ZN367_HUMAN Reviewed; 350 AA. AC Q7RTV3; Q6Q7C8; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 08-NOV-2023, entry version 152. DE RecName: Full=Zinc finger protein 367; DE AltName: Full=C2H2 zinc finger protein ZFF29; GN Name=ZNF367; Synonyms=ZFF29; 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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR RP LOCATION, AND ALTERNATIVE SPLICING. RC TISSUE=Fetal liver; RX PubMed=15344908; DOI=10.1042/bj20040394; RA Asano H., Murate T., Naoe T., Saito H., Stamatoyannopoulos G.; RT "Molecular cloning and characterization of ZFF29: a protein containing a RT unique Cys2His2 zinc-finger motif."; RL Biochem. J. 384:647-653(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [4] RP IDENTIFICATION (ISOFORM 1). RX PubMed=12234665; DOI=10.1016/s0378-1119(02)00793-x; RA Gilligan P., Brenner S., Venkatesh B.; RT "Fugu and human sequence comparison identifies novel human genes and RT conserved non-coding sequences."; RL Gene 294:35-44(2002). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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). CC -!- FUNCTION: Transcriptional activator. Isoform 1 may be involved in CC transcriptional activation of erythroid genes. CC {ECO:0000269|PubMed:15344908}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15344908}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=ZFF29B; CC IsoId=Q7RTV3-1; Sequence=Displayed; CC Name=2; Synonyms=ZFF29A; CC IsoId=Q7RTV3-2; Sequence=VSP_024865; 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; AY554164; AAS66302.1; -; mRNA. DR EMBL; AY554165; AAS66303.1; -; mRNA. DR EMBL; AL133477; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC126141; AAI26142.1; -; mRNA. DR EMBL; BK000211; DAA00067.1; -; mRNA. DR CCDS; CCDS6718.1; -. [Q7RTV3-1] DR RefSeq; NP_710162.1; NM_153695.3. [Q7RTV3-1] DR AlphaFoldDB; Q7RTV3; -. DR SMR; Q7RTV3; -. DR STRING; 9606.ENSP00000364405; -. DR iPTMnet; Q7RTV3; -. DR PhosphoSitePlus; Q7RTV3; -. DR BioMuta; ZNF367; -. DR DMDM; 74762420; -. DR EPD; Q7RTV3; -. DR jPOST; Q7RTV3; -. DR MassIVE; Q7RTV3; -. DR MaxQB; Q7RTV3; -. DR PaxDb; 9606-ENSP00000364405; -. DR PeptideAtlas; Q7RTV3; -. DR ProteomicsDB; 68913; -. [Q7RTV3-1] DR ProteomicsDB; 68914; -. [Q7RTV3-2] DR Antibodypedia; 14186; 98 antibodies from 17 providers. DR DNASU; 195828; -. DR Ensembl; ENST00000375256.5; ENSP00000364405.4; ENSG00000165244.7. [Q7RTV3-1] DR GeneID; 195828; -. DR KEGG; hsa:195828; -. DR MANE-Select; ENST00000375256.5; ENSP00000364405.4; NM_153695.4; NP_710162.1. DR UCSC; uc004awf.4; human. [Q7RTV3-1] DR AGR; HGNC:18320; -. DR CTD; 195828; -. DR DisGeNET; 195828; -. DR GeneCards; ZNF367; -. DR HGNC; HGNC:18320; ZNF367. DR HPA; ENSG00000165244; Tissue enhanced (bone). DR MIM; 610160; gene. DR neXtProt; NX_Q7RTV3; -. DR OpenTargets; ENSG00000165244; -. DR PharmGKB; PA38316; -. DR VEuPathDB; HostDB:ENSG00000165244; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00670000098074; -. DR HOGENOM; CLU_068261_0_0_1; -. DR InParanoid; Q7RTV3; -. DR OMA; NKHPHVI; -. DR OrthoDB; 2913077at2759; -. DR PhylomeDB; Q7RTV3; -. DR TreeFam; TF321334; -. DR PathwayCommons; Q7RTV3; -. DR BioGRID-ORCS; 195828; 36 hits in 1178 CRISPR screens. DR GenomeRNAi; 195828; -. DR Pharos; Q7RTV3; Tbio. DR PRO; PR:Q7RTV3; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q7RTV3; Protein. DR Bgee; ENSG00000165244; Expressed in thymus and 126 other tissues. DR Genevisible; Q7RTV3; HS. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR44699; IMMUNOGLOBULIN SUPERFAMILY MEMBER 11; 1. DR PANTHER; PTHR44699:SF1; IMMUNOGLOBULIN SUPERFAMILY MEMBER 11; 1. DR Pfam; PF00096; zf-C2H2; 1. DR Pfam; PF13912; zf-C2H2_6; 1. DR SMART; SM00355; ZnF_C2H2; 2. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Coiled coil; DNA-binding; Metal-binding; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..350 FT /note="Zinc finger protein 367" FT /id="PRO_0000285297" FT ZN_FING 167..189 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 195..219 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 104..151 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 290..327 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 308..342 FT /evidence="ECO:0000255" FT COMPBIAS 131..151 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 311..327 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 310 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 278..350 FT /note="YWEMREQRTPTLKGKLVQKADQEQQDPLEYLQSDEEDDEKRGAQRRLQEQRE FT RLHGALALIELANLTGAPLRQ -> SGMLPLVHREDAQRGLGLCQGPGHASHFK (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:15344908" FT /id="VSP_024865" SQ SEQUENCE 350 AA; 38411 MW; 01C3A79E0E408454 CRC64; MIRGFEAPMA ENPPPPPPPV IFCHDSPKRV LVSVIRTTPI KPTCGGGGEP EPPPPLIPTS PGFSDFMVYP WRWGENAHNV TLSPGAAGAA ASAALPAAAA AEHSGLRGRG APPPAASASA AASGGEDEEE ASSPDSGHLK DGIRRGRPRA DTVRDLINEG EHSSSRIRCN ICNRVFPREK SLQAHKRTHT GERPYLCDYP DCGKAFVQSG QLKTHQRLHT GEKPFVCSEN GCLSRFTHAN RHCPKHPYAR LKREEPTDTL SKHQAADNKA AAEWLARYWE MREQRTPTLK GKLVQKADQE QQDPLEYLQS DEEDDEKRGA QRRLQEQRER LHGALALIEL ANLTGAPLRQ //