ZN597_HUMAN
ID ZN597_HUMAN Reviewed; 424 AA.
AC Q96LX8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Zinc finger protein 597;
GN Name=ZNF597;
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=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 IMPRINTING, AND INDUCTION.
RX PubMed=16467561; DOI=10.1101/gr.4559106;
RA Pant P.V., Tao H., Beilharz E.J., Ballinger D.G., Cox D.R., Frazer K.A.;
RT "Analysis of allelic differential expression in human white blood cells.";
RL Genome Res. 16:331-339(2006).
RN [4]
RP IMPRINTING, AND INDUCTION.
RX PubMed=21593219; DOI=10.1093/hmg/ddr224;
RA Nakabayashi K., Trujillo A.M., Tayama C., Camprubi C., Yoshida W.,
RA Lapunzina P., Sanchez A., Soejima H., Aburatani H., Nagae G., Ogata T.,
RA Hata K., Monk D.;
RT "Methylation screening of reciprocal genome-wide UPDs identifies novel
RT human-specific imprinted genes.";
RL Hum. Mol. Genet. 20:3188-3197(2011).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-300, AND IDENTIFICATION BY MASS
RP 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: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q96LX8; P55212: CASP6; NbExp=3; IntAct=EBI-9091553, EBI-718729;
CC Q96LX8; Q96Q77: CIB3; NbExp=3; IntAct=EBI-9091553, EBI-10292696;
CC Q96LX8; G5E9A7: DMWD; NbExp=3; IntAct=EBI-9091553, EBI-10976677;
CC Q96LX8; Q9NWZ3: IRAK4; NbExp=3; IntAct=EBI-9091553, EBI-448378;
CC Q96LX8; P13473-2: LAMP2; NbExp=3; IntAct=EBI-9091553, EBI-21591415;
CC Q96LX8; P02545: LMNA; NbExp=3; IntAct=EBI-9091553, EBI-351935;
CC Q96LX8; Q96CV9: OPTN; NbExp=3; IntAct=EBI-9091553, EBI-748974;
CC Q96LX8; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-9091553, EBI-5280197;
CC Q96LX8; P62826: RAN; NbExp=3; IntAct=EBI-9091553, EBI-286642;
CC Q96LX8; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-9091553, EBI-5235340;
CC Q96LX8; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-9091553, EBI-745392;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: Imprinted. Promoter methylation of the paternal allele may
CC restrict expression to the maternal allele in leukocytes.
CC {ECO:0000269|PubMed:16467561, ECO:0000269|PubMed:21593219}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK057633; BAB71538.1; -; mRNA.
DR EMBL; BC029899; AAH29899.1; -; mRNA.
DR CCDS; CCDS10505.1; -.
DR RefSeq; NP_689670.1; NM_152457.2.
DR AlphaFoldDB; Q96LX8; -.
DR SMR; Q96LX8; -.
DR BioGRID; 126986; 26.
DR IntAct; Q96LX8; 23.
DR STRING; 9606.ENSP00000301744; -.
DR iPTMnet; Q96LX8; -.
DR PhosphoSitePlus; Q96LX8; -.
DR BioMuta; ZNF597; -.
DR DMDM; 71153482; -.
DR EPD; Q96LX8; -.
DR jPOST; Q96LX8; -.
DR MassIVE; Q96LX8; -.
DR MaxQB; Q96LX8; -.
DR PaxDb; Q96LX8; -.
DR PeptideAtlas; Q96LX8; -.
DR PRIDE; Q96LX8; -.
DR ProteomicsDB; 77266; -.
DR Antibodypedia; 819; 109 antibodies from 25 providers.
DR DNASU; 146434; -.
DR Ensembl; ENST00000301744.7; ENSP00000301744.4; ENSG00000167981.7.
DR GeneID; 146434; -.
DR KEGG; hsa:146434; -.
DR MANE-Select; ENST00000301744.7; ENSP00000301744.4; NM_152457.3; NP_689670.1.
DR UCSC; uc002cvd.4; human.
DR CTD; 146434; -.
DR GeneCards; ZNF597; -.
DR HGNC; HGNC:26573; ZNF597.
DR HPA; ENSG00000167981; Low tissue specificity.
DR MIM; 614685; gene.
DR neXtProt; NX_Q96LX8; -.
DR OpenTargets; ENSG00000167981; -.
DR PharmGKB; PA134935893; -.
DR VEuPathDB; HostDB:ENSG00000167981; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162263; -.
DR HOGENOM; CLU_002678_0_7_1; -.
DR InParanoid; Q96LX8; -.
DR OMA; KRTHIKN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q96LX8; -.
DR TreeFam; TF342316; -.
DR PathwayCommons; Q96LX8; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q96LX8; -.
DR BioGRID-ORCS; 146434; 13 hits in 1089 CRISPR screens.
DR ChiTaRS; ZNF597; human.
DR GenomeRNAi; 146434; -.
DR Pharos; Q96LX8; Tbio.
DR PRO; PR:Q96LX8; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96LX8; protein.
DR Bgee; ENSG00000167981; Expressed in secondary oocyte and 116 other tissues.
DR Genevisible; Q96LX8; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator 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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
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; 5.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..424
FT /note="Zinc finger protein 597"
FT /id="PRO_0000047687"
FT DOMAIN 14..88
FT /note="KRAB"
FT ZN_FING 156..178
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 184..206
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 212..234
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 240..262
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 341..363
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 369..391
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 397..419
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 300
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 30
FT /note="T -> S (in dbSNP:rs2270493)"
FT /id="VAR_033581"
SQ SEQUENCE 424 AA; 48076 MW; 8A47D19087AA8645 CRC64;
MASMPPTPEA QGPILFEDLA VYFSQEECVT LHPAQRSLSK DGTKESLEDA ALMGEEGKPE
INQQLSLESM ELDELALEKY PIAAPLVPYP EKSSEDGVGN PEAKILSGTP TYKRRVISLL
VTIENHTPLV ELSEYLGTNT LSEILDSPWE GAKNVYKCPE CDQNFSDHSY LVLHQKIHSG
EKKHKCGDCG KIFNHRANLR THRRIHTGEK PYKCAKCSAS FRQHSHLSRH MNSHVKEKPY
TCSICGRGFM WLPGLAQHQK SHSAENTYES TNCDKHFNEK PNLALPEETF VSGPQYQHTK
CMKSFRQSLY PALSEKSHDE DSERCSDDGD NFFSFSKFKP LQCPDCDMTF PCFSELISHQ
NIHTEERPHK CKTCEESFAL DSELACHQKS HMLAEPFKCT VCGKTFKSNL HLITHKRTHI
KNTT
