ZN117_HUMAN
ID ZN117_HUMAN Reviewed; 483 AA.
AC Q03924; Q02313; Q7Z7Q7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 5.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Zinc finger protein 117;
DE AltName: Full=Provirus-linked krueppel;
DE Short=h-PLK;
DE AltName: Full=Zinc finger protein HPF9;
GN Name=ZNF117;
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].
RC TISSUE=Placenta;
RX PubMed=2505992; DOI=10.1089/dna.1.1989.8.377;
RA Bellefroid E.J., Lecocq P.J., Benhida A., Poncelet D.A., Belayew A.,
RA Martial J.A.;
RT "The human genome contains hundreds of genes coding for finger proteins of
RT the Kruppel type.";
RL DNA 8:377-387(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=2115127; DOI=10.1128/mcb.10.8.4401-4405.1990;
RA Kato N., Shimotohno K., VanLeeuwen D., Cohen M.;
RT "Human proviral mRNAs down regulated in choriocarcinoma encode a zinc
RT finger protein related to Kruppel.";
RL Mol. Cell. Biol. 10:4401-4405(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-131.
RX PubMed=2023909; DOI=10.1073/pnas.88.9.3608;
RA Bellefroid E.J., Poncelet D.A., Lecocq P.J., Revelant O., Martial J.A.;
RT "The evolutionarily conserved Kruppel-associated box domain defines a
RT subfamily of eukaryotic multifingered proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3608-3612(1991).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed early during embryonic development.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36010.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA58666.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG41761.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; M27879; AAG41761.1; ALT_SEQ; mRNA.
DR EMBL; M55422; AAA36010.1; ALT_SEQ; mRNA.
DR EMBL; AC073210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M61867; AAA58666.1; ALT_INIT; mRNA.
DR CCDS; CCDS43593.1; -.
DR PIR; A35659; A35659.
DR PIR; B39384; B39384.
DR RefSeq; NP_001334979.1; NM_001348050.1.
DR RefSeq; NP_056936.2; NM_015852.3.
DR AlphaFoldDB; Q03924; -.
DR SMR; Q03924; -.
DR BioGRID; 119493; 1.
DR STRING; 9606.ENSP00000282869; -.
DR iPTMnet; Q03924; -.
DR PhosphoSitePlus; Q03924; -.
DR BioMuta; ZNF117; -.
DR DMDM; 327478609; -.
DR jPOST; Q03924; -.
DR MassIVE; Q03924; -.
DR MaxQB; Q03924; -.
DR PaxDb; Q03924; -.
DR PeptideAtlas; Q03924; -.
DR PRIDE; Q03924; -.
DR ProteomicsDB; 58227; -.
DR Antibodypedia; 28146; 95 antibodies from 17 providers.
DR DNASU; 51351; -.
DR Ensembl; ENST00000282869.11; ENSP00000282869.5; ENSG00000152926.16.
DR Ensembl; ENST00000620222.4; ENSP00000479944.1; ENSG00000152926.16.
DR GeneID; 109504726; -.
DR GeneID; 51351; -.
DR KEGG; hsa:109504726; -.
DR KEGG; hsa:51351; -.
DR UCSC; uc003ttr.3; human.
DR CTD; 109504726; -.
DR CTD; 51351; -.
DR DisGeNET; 109504726; -.
DR DisGeNET; 51351; -.
DR GeneCards; ZNF117; -.
DR HGNC; HGNC:12897; ZNF117.
DR HPA; ENSG00000152926; Low tissue specificity.
DR MIM; 194624; gene.
DR neXtProt; NX_Q03924; -.
DR OpenTargets; ENSG00000152926; -.
DR PharmGKB; PA37486; -.
DR VEuPathDB; HostDB:ENSG00000152926; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161765; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q03924; -.
DR OMA; QFSTFNT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q03924; -.
DR TreeFam; TF342117; -.
DR PathwayCommons; Q03924; -.
DR BioGRID-ORCS; 51351; 10 hits in 1053 CRISPR screens.
DR Pharos; Q03924; Tdark.
DR PRO; PR:Q03924; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q03924; protein.
DR Bgee; ENSG00000152926; Expressed in endometrium epithelium and 181 other tissues.
DR ExpressionAtlas; Q03924; baseline and differential.
DR Genevisible; Q03924; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..483
FT /note="Zinc finger protein 117"
FT /id="PRO_0000047407"
FT ZN_FING 109..131
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 137..159
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 165..187
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 193..215
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 221..243
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 249..271
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 277..299
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 305..327
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 333..355
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 361..383
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 389..411
FT /note="C2H2-type 11; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 417..439
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 445..467
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VARIANT 83
FT /note="C -> Y (in dbSNP:rs3807069)"
FT /id="VAR_057396"
FT VARIANT 112
FT /note="K -> N (in dbSNP:rs3807068)"
FT /id="VAR_057397"
FT CONFLICT 40
FT /note="R -> G (in Ref. 4; AAA58666)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..44
FT /note="GY -> RH (in Ref. 4; AAA58666)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="Q -> H (in Ref. 1; AAG41761 and 4; AAA58666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 56376 MW; E2729363C0E68C8E CRC64;
MKRHEMVAKH LVMFYYFAQH LWPEQNIRDS FQKVTLRRYR KCGYENLQLR KGCKSVVECK
QHKGDYSGLN QCLKTTLSKI FQCNKYVEVF HKISNSNRHK MRHTENKHFK CKECRKTFCM
LSHLTQHKRI QTRVNFYKCE AYGRAFNWSS TLNKHKRIHT GEKPYKCKEC GKAFNQTSHL
IRHKRIHTEE KPYKCEECGK AFNQSSTLTT HNIIHTGEIP YKCEKCVRAF NQASKLTEHK
LIHTGEKRYE CEECGKAFNR SSKLTEHKYI HTGEKLYKCE ECGKAFNQSS TLTTHKRIHS
GEKPYKCEEC GKAFKQFSNL TDHKKIHTGE KPYKCEECGK AFNQLSNLTR HKVIHTGEKP
YKCGECGKAF NQSSALNTHK IIHTGENPHK CRESGKVFHL SSKLSTCKKI HTGEKLYKCE
ECGKAFNRSS TLIGHKRIHT GEKPYKCEEC GKAFNQSSTL TTHKIIHTEE KQYKCDECGK
AST
