ZNF34_HUMAN
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 03-AUG-2022, entry version 159.
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};
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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; 4.
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; Q8IZ26; -.
DR PeptideAtlas; Q8IZ26; -.
DR PRIDE; Q8IZ26; -.
DR ProteomicsDB; 71275; -.
DR Antibodypedia; 28631; 114 antibodies from 17 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 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; 1318335at2759; -.
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 1099 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 126 other tissues.
DR ExpressionAtlas; Q8IZ26; baseline and differential.
DR Genevisible; Q8IZ26; HS.
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 InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
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
