ZN367_HUMAN
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 03-AUG-2022, entry version 147.
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}.
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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; Q7RTV3; -.
DR PeptideAtlas; Q7RTV3; -.
DR PRIDE; Q7RTV3; -.
DR ProteomicsDB; 68913; -. [Q7RTV3-1]
DR ProteomicsDB; 68914; -. [Q7RTV3-2]
DR Antibodypedia; 14186; 99 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 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; 1318335at2759; -.
DR PhylomeDB; Q7RTV3; -.
DR TreeFam; TF321334; -.
DR PathwayCommons; Q7RTV3; -.
DR BioGRID-ORCS; 195828; 29 hits in 1100 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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 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
