ZN697_HUMAN
ID ZN697_HUMAN Reviewed; 545 AA.
AC Q5TEC3; Q96IT2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Zinc finger protein 697;
GN Name=ZNF697;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 316-545.
RC TISSUE=Skin;
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2, 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).
RN [4]
RP VARIANT THR-158.
RX PubMed=28236339; DOI=10.1002/humu.23205;
RA Musante L., Puettmann L., Kahrizi K., Garshasbi M., Hu H., Stehr H.,
RA Lipkowitz B., Otto S., Jensen L.R., Tzschach A., Jamali P., Wienker T.,
RA Najmabadi H., Ropers H.H., Kuss A.W.;
RT "Mutations of the aminoacyl-tRNA-synthetases SARS and WARS2 are implicated
RT in the aetiology of autosomal recessive intellectual disability.";
RL Hum. Mutat. 38:621-636(2017).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- INTERACTION:
CC Q5TEC3; P50570-2: DNM2; NbExp=3; IntAct=EBI-25845217, EBI-10968534;
CC Q5TEC3; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-25845217, EBI-11110431;
CC Q5TEC3; P28799: GRN; NbExp=3; IntAct=EBI-25845217, EBI-747754;
CC Q5TEC3; P42858: HTT; NbExp=3; IntAct=EBI-25845217, EBI-466029;
CC Q5TEC3; O76024: WFS1; NbExp=3; IntAct=EBI-25845217, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AL109966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007260; AAH07260.1; -; mRNA.
DR CCDS; CCDS44202.1; -.
DR RefSeq; NP_001073939.1; NM_001080470.1.
DR RefSeq; XP_005271372.1; XM_005271315.3.
DR RefSeq; XP_011540718.1; XM_011542416.2.
DR AlphaFoldDB; Q5TEC3; -.
DR SMR; Q5TEC3; -.
DR BioGRID; 124778; 13.
DR IntAct; Q5TEC3; 5.
DR STRING; 9606.ENSP00000396857; -.
DR iPTMnet; Q5TEC3; -.
DR PhosphoSitePlus; Q5TEC3; -.
DR BioMuta; ZNF697; -.
DR DMDM; 158706492; -.
DR MassIVE; Q5TEC3; -.
DR MaxQB; Q5TEC3; -.
DR PaxDb; Q5TEC3; -.
DR PeptideAtlas; Q5TEC3; -.
DR PRIDE; Q5TEC3; -.
DR ProteomicsDB; 65041; -.
DR Antibodypedia; 33915; 98 antibodies from 17 providers.
DR DNASU; 90874; -.
DR Ensembl; ENST00000421812.3; ENSP00000396857.2; ENSG00000143067.5.
DR GeneID; 90874; -.
DR KEGG; hsa:90874; -.
DR MANE-Select; ENST00000421812.3; ENSP00000396857.2; NM_001080470.2; NP_001073939.1.
DR UCSC; uc001ehy.2; human.
DR CTD; 90874; -.
DR DisGeNET; 90874; -.
DR GeneCards; ZNF697; -.
DR HGNC; HGNC:32034; ZNF697.
DR HPA; ENSG00000143067; Low tissue specificity.
DR neXtProt; NX_Q5TEC3; -.
DR OpenTargets; ENSG00000143067; -.
DR PharmGKB; PA142670495; -.
DR VEuPathDB; HostDB:ENSG00000143067; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00820000127150; -.
DR HOGENOM; CLU_002678_57_3_1; -.
DR InParanoid; Q5TEC3; -.
DR OMA; PPMLPWR; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5TEC3; -.
DR TreeFam; TF350831; -.
DR PathwayCommons; Q5TEC3; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q5TEC3; -.
DR BioGRID-ORCS; 90874; 11 hits in 1101 CRISPR screens.
DR ChiTaRS; ZNF697; human.
DR GenomeRNAi; 90874; -.
DR Pharos; Q5TEC3; Tdark.
DR PRO; PR:Q5TEC3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5TEC3; protein.
DR Bgee; ENSG00000143067; Expressed in cartilage tissue and 145 other tissues.
DR Genevisible; Q5TEC3; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
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..545
FT /note="Zinc finger protein 697"
FT /id="PRO_0000305138"
FT ZN_FING 189..211
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 261..283
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..311
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 317..339
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 353..375
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 381..403
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 409..431
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 437..459
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 465..487
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 493..515
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 521..543
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 2
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 158
FT /note="P -> T"
FT /evidence="ECO:0000269|PubMed:28236339"
FT /id="VAR_078436"
SQ SEQUENCE 545 AA; 60461 MW; 15860E7AECBE5ACC CRC64;
MKQEDNQGVC AHQDSEDKGM GSDFEDSEDR EGDPEEREMG SNPHDTNKRE GHPEPEMGSN
PQDSRHREAV PDICTEGQLS EEEGVSVRGE EDDQSGVADM AMFPGLSESD SISRSLREDD
DESAGENRLE EEEEQPAPPV LPWRRHLSLG SRHRGDKPAH RRFHRLHHPM AVDLGELDSL
VASIMDAPTI CPDCGESFSP GAAFLQHQRI HRLAEAAAAA SLEPFGLAGE CDAMVGMMGV
GVAGGFGAGP PLARPPREKP FRCGECGKGF SRNTYLTNHL RLHTGERPNL CADCGKSFSW
RADLLKHRRL HTGEKPYPCP ECGEAFSLSS HLLSHRRAHA AASGAGAAAL RPFACGECGK
GFVRRSHLAN HQRIHTGEKP HGCGECGKRF SWRSDLVKHQ RVHTGEKPYM CSECGETFSV
SSHLFTHKRT HSGERPYVCR ECGKGFGRNS HLVNHLRVHT GEKPFRCGQC EKRFSDFSTL
TQHQRTHTGE KPYTCIECGK SFIQSSHLIR HRRIHTGNKP HKCAGCGKGF RYKTHLAQHQ
KLHLC
