ZN658_HUMAN
ID ZN658_HUMAN Reviewed; 1059 AA.
AC Q5TYW1; Q6PIP3; Q96M55; Q9H9S6; Q9UG02;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Zinc finger protein 658;
GN Name=ZNF658;
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] (ISOFORM 1).
RC TISSUE=Teratocarcinoma, and Testis;
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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 360-1059 (ISOFORM 1).
RC TISSUE=Subthalamic nucleus;
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 [5]
RP FUNCTION.
RX PubMed=25582195; DOI=10.1128/mcb.01298-14;
RA Ogo O.A., Tyson J., Cockell S.J., Howard A., Valentine R.A., Ford D.;
RT "The zinc finger protein ZNF658 regulates the transcription of genes
RT involved in zinc homeostasis and affects ribosome biogenesis through the
RT zinc transcriptional regulatory element.";
RL Mol. Cell. Biol. 35:977-987(2015).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178, 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: Mediates transcriptional repression in response to zinc.
CC Represses several genes, including SLC30A5, SLC30A10 and CBWD1, by
CC binding to the zinc transcriptional regulatory element (ZTRE) (5'-
CC C[AC]C[TAG]CC[TC]-N(0-50)-[GA]G[ATC]G[TG]G-3') found in the promoter
CC region. May play a role in the control of ribosome biogenesis,
CC regulating predominantly rRNA levels, as well as those of several
CC ribosomal proteins, thus coordinating this highly zinc-demanding
CC process with the available zinc supply. {ECO:0000269|PubMed:25582195}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5TYW1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5TYW1-2; Sequence=VSP_023671, VSP_023672;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31626.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14145.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB53677.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK022636; BAB14145.1; ALT_INIT; mRNA.
DR EMBL; AK057375; BAB71457.1; ALT_TERM; mRNA.
DR EMBL; BX664608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031626; AAH31626.1; ALT_INIT; mRNA.
DR EMBL; AL110217; CAB53677.2; ALT_INIT; mRNA.
DR CCDS; CCDS75846.1; -. [Q5TYW1-1]
DR PIR; T14757; T14757.
DR RefSeq; NP_001304845.1; NM_001317916.1. [Q5TYW1-1]
DR RefSeq; NP_149350.3; NM_033160.6. [Q5TYW1-1]
DR RefSeq; XP_005272572.1; XM_005272515.4. [Q5TYW1-1]
DR RefSeq; XP_011543981.1; XM_011545679.2. [Q5TYW1-1]
DR RefSeq; XP_016870103.1; XM_017014614.1. [Q5TYW1-1]
DR AlphaFoldDB; Q5TYW1; -.
DR SMR; Q5TYW1; -.
DR BioGRID; 117580; 6.
DR IntAct; Q5TYW1; 2.
DR STRING; 9606.ENSP00000482540; -.
DR iPTMnet; Q5TYW1; -.
DR PhosphoSitePlus; Q5TYW1; -.
DR BioMuta; ZNF658; -.
DR DMDM; 134035376; -.
DR jPOST; Q5TYW1; -.
DR MassIVE; Q5TYW1; -.
DR MaxQB; Q5TYW1; -.
DR PaxDb; Q5TYW1; -.
DR PeptideAtlas; Q5TYW1; -.
DR PRIDE; Q5TYW1; -.
DR ProteomicsDB; 65209; -. [Q5TYW1-1]
DR ProteomicsDB; 65210; -. [Q5TYW1-2]
DR Antibodypedia; 74757; 36 antibodies from 13 providers.
DR DNASU; 26149; -.
DR Ensembl; ENST00000612867.4; ENSP00000482540.1; ENSG00000274349.5. [Q5TYW1-1]
DR Ensembl; ENST00000621410.5; ENSP00000482447.1; ENSG00000274349.5. [Q5TYW1-1]
DR Ensembl; ENST00000622180.4; ENSP00000480919.1; ENSG00000274349.5. [Q5TYW1-2]
DR GeneID; 26149; -.
DR KEGG; hsa:26149; -.
DR MANE-Select; ENST00000621410.5; ENSP00000482447.1; NM_033160.7; NP_149350.3.
DR UCSC; uc004abs.2; human. [Q5TYW1-1]
DR CTD; 26149; -.
DR DisGeNET; 26149; -.
DR GeneCards; ZNF658; -.
DR HGNC; HGNC:25226; ZNF658.
DR HPA; ENSG00000274349; Low tissue specificity.
DR MIM; 616290; gene.
DR neXtProt; NX_Q5TYW1; -.
DR OpenTargets; ENSG00000274349; -.
DR PharmGKB; PA134907871; -.
DR VEuPathDB; HostDB:ENSG00000274349; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163669; -.
DR HOGENOM; CLU_002678_17_4_1; -.
DR InParanoid; Q5TYW1; -.
DR OMA; DEWQYMS; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5TYW1; -.
DR TreeFam; TF350905; -.
DR PathwayCommons; Q5TYW1; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q5TYW1; -.
DR BioGRID-ORCS; 26149; 67 hits in 1050 CRISPR screens.
DR GenomeRNAi; 26149; -.
DR Pharos; Q5TYW1; Tbio.
DR PRO; PR:Q5TYW1; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5TYW1; protein.
DR Bgee; ENSG00000274349; Expressed in calcaneal tendon and 104 other tissues.
DR ExpressionAtlas; Q5TYW1; baseline and differential.
DR Genevisible; Q5TYW1; 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:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:UniProtKB.
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; 20.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 20.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 14.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 19.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 21.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Ribosome biogenesis; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1059
FT /note="Zinc finger protein 658"
FT /id="PRO_0000280433"
FT DOMAIN 8..79
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 325..347
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 352..375
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 381..406
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 518..540
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 546..568
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 574..596
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 602..624
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 630..652
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 658..680
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 686..708
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 714..736
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 742..764
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 770..792
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 798..820
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 826..848
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 854..876
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 882..904
FT /note="C2H2-type 19; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 910..932
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 938..960
FT /note="C2H2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 966..988
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 994..1016
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1022..1045
FT /note="C2H2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 599..617
FT /note="EKPYECSDCEKTFAHNSAL -> LAVCHVGILMATKSLFHQS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023671"
FT VAR_SEQ 618..1059
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023672"
FT VARIANT 68
FT /note="S -> Y (in dbSNP:rs2065444)"
FT /id="VAR_052888"
SQ SEQUENCE 1059 AA; 122274 MW; 3007C61F09413440 CRC64;
MNMSQASVSF QDVTVEFTRE EWQHLGPVER TLYRDVMLEN YSHLISVGYC ITKPKVISKL
EKGEEPWSLE DEFLNQRYPG YFKVDHIKGI REKQEKPLWQ EIFISDADKT LSKEGQKVLE
KPFNLEIAPE LSEKISCKCD SHRMNLPVAS QLIISERKYS RKKTEYMNVC EKLQLDIKHE
KAHAEEKSYE HGENAKAFSY KKDQHWKFQT LEESFECDGS GQGLYDKTIC ITPQSFLTGE
KSCKDDEFRK NFDKITLFNH MRTDTRGKCS DLNEYGTSCD KTTAVEYNKV HMAMTHYECN
ERGINFSRKS PLTQSQRTIT GWSAFESNKC EENFSQSSAH IVHQKTQAGD KFGEHNECTD
ALYQKLDFTA HQRIHTEDKF YLSDEHGKCR KSFYRKAHLI QHQRPHSGEK TYQYEECAKS
FCSSSHPIQH PGTYVGFKLY ECNECGKAFC QNSNLSKHLR IHTKEKPCDN NGCGRSYKSP
LIGHQKTDAE MELCGGSEYG KTSHLKGHQR ILMGEKPYEC IECGKTFSKT SHLRAHQRIH
TGEKPYECVE CEKTFSHKTH LSVHQRVHTG EKPYECNDCG KSFTYNSALR AHQRIHTGEK
PYECSDCEKT FAHNSALRAH HRIHTGEKPY ECNECGRSFA HISVLKAHQR IHTGEKPYEC
NECGRSFTYN SALRAHQRIH TGRKPYECSD CEKTFAHNSA LKIHQRIHTG EKPYECNECE
KTFAHNSALR AHQNIHTGEK LYECSECGKT FFQKTRLSTH RRIHTGEKPY ECSKCGKTFS
QKSYLSGHER IHTGEKPYEC NVCGKTFVYK AALIVHQRIH TGEKPYECNQ CGKTFSQRTH
LCAHQRIHTG EKPYECNECG KTFADNSALR AHHRIHTGEK PYECNDCGKT FSKTSHLRAH
LRTRSGEKPY ECSECGKTFS EKSYVSAHQR VHTGEKPYEC NVCGKPFAHN STLRVHQRIH
TGEKSYECND CGKTFSQKSH LSAHQRIHTG EKPYECNECG KAFAQNSTLR VHQRIHTGEK
PYECDECGKT FVRKAALRVH HTRMHTREKT LACNGFGKS
