ZN397_HUMAN
ID ZN397_HUMAN Reviewed; 534 AA.
AC Q8NF99; Q9BRM2;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Zinc finger protein 397;
DE AltName: Full=Zinc finger and SCAN domain-containing protein 15;
DE AltName: Full=Zinc finger protein 47;
GN Name=ZNF397; Synonyms=ZNF47, ZSCAN15;
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 3), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hepatoma;
RX PubMed=12801647; DOI=10.1016/s0378-1119(03)00551-1;
RA Wu Y., Yu L., Bi G., Luo K., Zhou G., Zhao S.;
RT "Identification and characterization of two novel human SCAN domain-
RT containing zinc finger genes ZNF396 and ZNF397.";
RL Gene 310:193-201(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-171, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-171; LYS-202 AND LYS-251,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Isoform 3 acts as a DNA-dependent transcriptional repressor.
CC {ECO:0000269|PubMed:12801647}.
CC -!- SUBUNIT: Isoforms 1 and 3 can both homo- and hetero-associate. Homo-
CC association of isoform 1 is dependent on the presence of the SCAN
CC domain. {ECO:0000269|PubMed:12801647}.
CC -!- INTERACTION:
CC Q8NF99; P61968: LMO4; NbExp=3; IntAct=EBI-10213894, EBI-2798728;
CC Q8NF99; P54646: PRKAA2; NbExp=3; IntAct=EBI-10213894, EBI-1383852;
CC Q8NF99; Q86VK4: ZNF410; NbExp=3; IntAct=EBI-10213894, EBI-720304;
CC Q8NF99; Q9NWS9: ZNF446; NbExp=4; IntAct=EBI-10213894, EBI-3925851;
CC Q8NF99; Q9NWS9-2: ZNF446; NbExp=5; IntAct=EBI-10213894, EBI-740232;
CC Q8NF99-2; P57086: SCAND1; NbExp=4; IntAct=EBI-11524467, EBI-745846;
CC Q8NF99-2; A0A0S2Z6X0: ZKSCAN4; NbExp=4; IntAct=EBI-11524467, EBI-16431094;
CC Q8NF99-2; Q969J2: ZKSCAN4; NbExp=3; IntAct=EBI-11524467, EBI-2818641;
CC Q8NF99-2; Q9NWS9-2: ZNF446; NbExp=5; IntAct=EBI-11524467, EBI-740232;
CC Q8NF99-2; O43309: ZSCAN12; NbExp=3; IntAct=EBI-11524467, EBI-1210440;
CC Q8NF99-2; P10073: ZSCAN22; NbExp=3; IntAct=EBI-11524467, EBI-10178224;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=ZNF397-fu;
CC IsoId=Q8NF99-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NF99-2; Sequence=VSP_006924, VSP_006925;
CC Name=3; Synonyms=Truncated, ZNF397-nf;
CC IsoId=Q8NF99-3; Sequence=VSP_042491, VSP_042492;
CC -!- TISSUE SPECIFICITY: Expressed strongly in testis, moderately in
CC skeletal muscle, pancreas and prostate, and weakly in heart, placenta,
CC liver, kidney, spleen, thymus and small intestine.
CC {ECO:0000269|PubMed:12801647}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION: [Isoform 3]:
CC Sequence=AAN65175.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF533250; AAM95991.2; -; mRNA.
DR EMBL; AY157641; AAN65175.1; ALT_FRAME; mRNA.
DR EMBL; BC006172; AAH06172.1; -; mRNA.
DR CCDS; CCDS32814.1; -. [Q8NF99-2]
DR CCDS; CCDS45852.1; -. [Q8NF99-1]
DR RefSeq; NP_001128650.1; NM_001135178.2. [Q8NF99-1]
DR RefSeq; NP_115723.1; NM_032347.2. [Q8NF99-2]
DR RefSeq; XP_011524533.1; XM_011526231.2. [Q8NF99-1]
DR RefSeq; XP_016881531.1; XM_017026042.1. [Q8NF99-1]
DR AlphaFoldDB; Q8NF99; -.
DR SMR; Q8NF99; -.
DR BioGRID; 124033; 62.
DR IntAct; Q8NF99; 36.
DR STRING; 9606.ENSP00000331577; -.
DR iPTMnet; Q8NF99; -.
DR PhosphoSitePlus; Q8NF99; -.
DR BioMuta; ZNF397; -.
DR DMDM; 38258943; -.
DR EPD; Q8NF99; -.
DR jPOST; Q8NF99; -.
DR MassIVE; Q8NF99; -.
DR MaxQB; Q8NF99; -.
DR PaxDb; Q8NF99; -.
DR PeptideAtlas; Q8NF99; -.
DR PRIDE; Q8NF99; -.
DR ProteomicsDB; 73277; -. [Q8NF99-1]
DR ProteomicsDB; 73278; -. [Q8NF99-2]
DR ProteomicsDB; 73279; -. [Q8NF99-3]
DR Antibodypedia; 8557; 206 antibodies from 28 providers.
DR DNASU; 84307; -.
DR Ensembl; ENST00000261333.10; ENSP00000261333.5; ENSG00000186812.13. [Q8NF99-2]
DR Ensembl; ENST00000330501.12; ENSP00000331577.6; ENSG00000186812.13. [Q8NF99-1]
DR Ensembl; ENST00000585800.1; ENSP00000466760.1; ENSG00000186812.13. [Q8NF99-3]
DR Ensembl; ENST00000591206.5; ENSP00000466317.1; ENSG00000186812.13. [Q8NF99-3]
DR GeneID; 84307; -.
DR KEGG; hsa:84307; -.
DR MANE-Select; ENST00000330501.12; ENSP00000331577.6; NM_001135178.3; NP_001128650.1.
DR UCSC; uc002kyi.4; human. [Q8NF99-1]
DR CTD; 84307; -.
DR GeneCards; ZNF397; -.
DR HGNC; HGNC:18818; ZNF397.
DR HPA; ENSG00000186812; Low tissue specificity.
DR MIM; 609601; gene.
DR neXtProt; NX_Q8NF99; -.
DR OpenTargets; ENSG00000186812; -.
DR PharmGKB; PA38694; -.
DR VEuPathDB; HostDB:ENSG00000186812; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162078; -.
DR HOGENOM; CLU_002678_49_3_1; -.
DR InParanoid; Q8NF99; -.
DR OMA; RKFCYHE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8NF99; -.
DR TreeFam; TF338304; -.
DR PathwayCommons; Q8NF99; -.
DR SignaLink; Q8NF99; -.
DR BioGRID-ORCS; 84307; 8 hits in 1102 CRISPR screens.
DR ChiTaRS; ZNF397; human.
DR GenomeRNAi; 84307; -.
DR Pharos; Q8NF99; Tbio.
DR PRO; PR:Q8NF99; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q8NF99; protein.
DR Bgee; ENSG00000186812; Expressed in secondary oocyte and 181 other tissues.
DR ExpressionAtlas; Q8NF99; baseline and differential.
DR Genevisible; Q8NF99; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 9.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..534
FT /note="Zinc finger protein 397"
FT /id="PRO_0000047564"
FT DOMAIN 50..132
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 285..307
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 313..335
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 341..363
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 369..391
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 397..419
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 425..447
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 453..475
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 481..503
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 509..531
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 180..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 55
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 251
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 186..207
FT /note="DCENSETATKEGISEEKSQGLP -> GEEWEIIWKLLTLRPLFLRMQN (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:12801647"
FT /id="VSP_042491"
FT VAR_SEQ 208..534
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12801647"
FT /id="VSP_042492"
FT VAR_SEQ 216..275
FT /note="SEHESNLVWKQGSATGEKLRSPSQGGSFSQVIFTNKSLGKRDLYDEAERCLI
FT LTTDSIMC -> KLSRPPKASSAIRWECVSPGSFPGDIIAAEATHSTISCFAINTLPAT
FT ILPSKNVNRKYFS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006924"
FT VAR_SEQ 276..534
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006925"
SQ SEQUENCE 534 AA; 61139 MW; E990609DABABDE2A CRC64;
MAVESGVIST LIPQDPPEQE LILVKVEDNF SWDEKFKQNG STQSCQELFR QQFRKFCYQE
TPGPREALSR LQELCYQWLM PELHTKEQIL ELLVLEQFLS ILPEELQIWV QQHNPESGEE
AVTLLEDLER EFDDPGQQVP ASPQGPAVPW KDLTCLRASQ ESTDIHLQPL KTQLKSWKPC
LSPKSDCENS ETATKEGISE EKSQGLPQEP SFRGISEHES NLVWKQGSAT GEKLRSPSQG
GSFSQVIFTN KSLGKRDLYD EAERCLILTT DSIMCQKVPP EERPYRCDVC GHSFKQHSSL
TQHQRIHTGE KPYKCNQCGK AFSLRSYLII HQRIHSGEKA YECSECGKAF NQSSALIRHR
KIHTGEKACK CNECGKAFSQ SSYLIIHQRI HTGEKPYECN ECGKTFSQSS KLIRHQRIHT
GERPYECNEC GKAFRQSSEL ITHQRIHSGE KPYECSECGK AFSLSSNLIR HQRIHSGEEP
YQCNECGKTF KRSSALVQHQ RIHSGDEAYI CNECGKAFRH RSVLMRHQRV HTIK
