ID ZNF34_HUMAN Reviewed; 560 AA. AC Q8IZ26; D3DWN1; Q9BSZ0; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 27-MAR-2024, entry version 167. DE RecName: Full=Zinc finger protein 34; DE AltName: Full=Zinc finger protein KOX32; GN Name=ZNF34; Synonyms=KOX32; 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 MRNA]. RC TISSUE=Substantia nigra; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [2] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Blood, and Lung; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY RP 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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: May be involved in transcriptional regulation. CC -!- INTERACTION: CC Q8IZ26; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-10264496, EBI-10172150; CC Q8IZ26; Q08AM6: VAC14; NbExp=4; IntAct=EBI-10264496, EBI-2107455; 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=AAH04480.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH28136.1; Type=Miscellaneous discrepancy; Note=Codon in position 67 corresponds to a stop codon in genome.; Evidence={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; AL833814; CAD38677.1; -; mRNA. DR EMBL; CH471162; EAW82055.1; -; Genomic_DNA. DR EMBL; CH471162; EAW82056.1; -; Genomic_DNA. DR EMBL; BC004480; AAH04480.1; ALT_INIT; mRNA. DR EMBL; BC028136; AAH28136.1; ALT_SEQ; mRNA. DR CCDS; CCDS47945.1; -. DR RefSeq; NP_001273698.1; NM_001286769.1. DR RefSeq; NP_085057.3; NM_030580.4. DR RefSeq; XP_011515616.1; XM_011517314.2. DR RefSeq; XP_011515617.1; XM_011517315.2. DR RefSeq; XP_011515618.1; XM_011517316.2. DR RefSeq; XP_011515620.1; XM_011517318.2. DR RefSeq; XP_016869361.1; XM_017013872.1. DR RefSeq; XP_016869362.1; XM_017013873.1. DR RefSeq; XP_016869363.1; XM_017013874.1. DR RefSeq; XP_016869364.1; XM_017013875.1. DR AlphaFoldDB; Q8IZ26; -. DR SMR; Q8IZ26; -. DR BioGRID; 123310; 53. DR IntAct; Q8IZ26; 6. DR STRING; 9606.ENSP00000341528; -. DR iPTMnet; Q8IZ26; -. DR PhosphoSitePlus; Q8IZ26; -. DR BioMuta; ZNF34; -. DR DMDM; 317373492; -. DR EPD; Q8IZ26; -. DR jPOST; Q8IZ26; -. DR MassIVE; Q8IZ26; -. DR MaxQB; Q8IZ26; -. DR PaxDb; 9606-ENSP00000341528; -. DR PeptideAtlas; Q8IZ26; -. DR ProteomicsDB; 71275; -. DR Antibodypedia; 28631; 133 antibodies from 18 providers. DR DNASU; 80778; -. DR Ensembl; ENST00000343459.8; ENSP00000341528.4; ENSG00000196378.13. DR GeneID; 80778; -. DR KEGG; hsa:80778; -. DR UCSC; uc003zdx.6; human. DR AGR; HGNC:13098; -. DR CTD; 80778; -. DR DisGeNET; 80778; -. DR GeneCards; ZNF34; -. DR HGNC; HGNC:13098; ZNF34. DR HPA; ENSG00000196378; Low tissue specificity. DR MIM; 194526; gene. DR neXtProt; NX_Q8IZ26; -. DR OpenTargets; ENSG00000196378; -. DR PharmGKB; PA37673; -. DR VEuPathDB; HostDB:ENSG00000196378; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000154712; -. DR HOGENOM; CLU_002678_0_7_1; -. DR InParanoid; Q8IZ26; -. DR OrthoDB; 5247610at2759; -. DR PhylomeDB; Q8IZ26; -. DR TreeFam; TF337055; -. DR PathwayCommons; Q8IZ26; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; Q8IZ26; -. DR BioGRID-ORCS; 80778; 20 hits in 1177 CRISPR screens. DR ChiTaRS; ZNF34; human. DR GeneWiki; ZNF34; -. DR GenomeRNAi; 80778; -. DR Pharos; Q8IZ26; Tdark. DR PRO; PR:Q8IZ26; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q8IZ26; Protein. DR Bgee; ENSG00000196378; Expressed in tibial artery and 128 other cell types or tissues. DR ExpressionAtlas; Q8IZ26; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 12. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23232; KRAB DOMAIN C2H2 ZINC FINGER; 1. DR PANTHER; PTHR23232:SF143; ZINC FINGER PROTEIN 747; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 12. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 12. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12. DR Genevisible; Q8IZ26; HS. PE 1: Evidence at protein level; KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..560 FT /note="Zinc finger protein 34" FT /id="PRO_0000047365" FT DOMAIN 35..108 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 195..217 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 251..273 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 279..301 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 307..329 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 335..357 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 363..385 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 391..413 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 419..441 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 447..469 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 475..497 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 503..525 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 531..553 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 163..188 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 167..181 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" SQ SEQUENCE 560 AA; 64038 MW; B66056E75C42C324 CRC64; MLLLLSDQLL LTALRKPNPQ AMAALFLSAP PQAEVTFEDV AVYLSREEWG RLGPAQRGLY RDVMLETYGN LVSLGVGPAG PKPGVISQLE RGDEPWVLDV QGTSGKEHLR VNSPALGTRT EYKELTSQET FGEEDPQGSE PVEACDHISK SEGSLEKLVE QRGPRAVTLT NGESSRESGG NLRLLSRPVP DQRPHKCDIC EQSFEQRSYL NNHKRVHRSK KTNTVRNSGE IFSANLVVKE DQKIPTGKKL HYCSYCGKTF RYSANLVKHQ RLHTEEKPYK CDECGKAFSQ SCEFINHRRM HSGEIPYRCD ECGKTFTRRP NLMKHQRIHT GEKPYKCGEC GKHFSAYSSL IYHQRIHTGE KPYKCNDCGK AFSDGSILIR HRRTHTGEKP FECKECGKGF TQSSNLIQHQ RIHTGEKPYK CNECEKAFIQ KTKLVEHQRS HTGEKPYECN DCGKVFSQST HLIQHQRIHT GEKPYKCSEC GKAFHNSSRL IHHQRLHHGE KPYRCSDCKK AFSQSTYLIQ HRRIHTGEKP YKCSECGKAF RHSSNMCQHQ RIHLREDFSM //