ZN675_HUMAN
ID ZN675_HUMAN Reviewed; 568 AA.
AC Q8TD23; Q8N211;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Zinc finger protein 675;
DE AltName: Full=TRAF6-binding zinc finger protein;
DE AltName: Full=TRAF6-inhibitory zinc finger protein;
GN Name=ZNF675; Synonyms=TIZ;
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], INTERACTION WITH TRAF6, AND VARIANT VAL-124.
RX PubMed=11751921; DOI=10.1074/jbc.m110964200;
RA Shin J.N., Kim I., Lee J.S., Koh G.Y., Lee Z.H., Kim H.-H.;
RT "A novel zinc finger protein that inhibits osteoclastogenesis and the
RT function of tumor necrosis factor receptor-associated factor 6.";
RL J. Biol. Chem. 277:8346-8353(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-124.
RC TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
CC -!- FUNCTION: May be involved in transcriptional regulation. May play a
CC role during osteoclast differentiation by modulating TRAF6 signaling
CC activity.
CC -!- SUBUNIT: Interacts with TRAF6. {ECO:0000269|PubMed:11751921}.
CC -!- INTERACTION:
CC Q8TD23; Q9Y4K3: TRAF6; NbExp=4; IntAct=EBI-528190, EBI-359276;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; AY044432; AAK95822.1; -; mRNA.
DR EMBL; AK093669; BAC04216.1; -; mRNA.
DR EMBL; AC073544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS32981.1; -.
DR PIR; F42075; F42075.
DR RefSeq; NP_612203.2; NM_138330.2.
DR AlphaFoldDB; Q8TD23; -.
DR SMR; Q8TD23; -.
DR BioGRID; 128116; 12.
DR IntAct; Q8TD23; 3.
DR MINT; Q8TD23; -.
DR STRING; 9606.ENSP00000352836; -.
DR iPTMnet; Q8TD23; -.
DR PhosphoSitePlus; Q8TD23; -.
DR BioMuta; ZNF675; -.
DR DMDM; 296453065; -.
DR EPD; Q8TD23; -.
DR jPOST; Q8TD23; -.
DR MassIVE; Q8TD23; -.
DR MaxQB; Q8TD23; -.
DR PaxDb; Q8TD23; -.
DR PeptideAtlas; Q8TD23; -.
DR PRIDE; Q8TD23; -.
DR ProteomicsDB; 74222; -.
DR Antibodypedia; 28764; 90 antibodies from 14 providers.
DR DNASU; 171392; -.
DR Ensembl; ENST00000359788.9; ENSP00000352836.3; ENSG00000197372.10.
DR GeneID; 171392; -.
DR KEGG; hsa:171392; -.
DR MANE-Select; ENST00000359788.9; ENSP00000352836.3; NM_138330.3; NP_612203.2.
DR UCSC; uc002nri.4; human.
DR CTD; 171392; -.
DR DisGeNET; 171392; -.
DR GeneCards; ZNF675; -.
DR HGNC; HGNC:30768; ZNF675.
DR HPA; ENSG00000197372; Low tissue specificity.
DR neXtProt; NX_Q8TD23; -.
DR OpenTargets; ENSG00000197372; -.
DR PharmGKB; PA142670476; -.
DR VEuPathDB; HostDB:ENSG00000197372; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT01050000244908; -.
DR HOGENOM; CLU_002678_44_0_1; -.
DR InParanoid; Q8TD23; -.
DR OMA; DRTFNQF; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8TD23; -.
DR TreeFam; TF342117; -.
DR PathwayCommons; Q8TD23; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q8TD23; -.
DR BioGRID-ORCS; 171392; 13 hits in 1027 CRISPR screens.
DR ChiTaRS; ZNF675; human.
DR GenomeRNAi; 171392; -.
DR Pharos; Q8TD23; Tbio.
DR PRO; PR:Q8TD23; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8TD23; protein.
DR Bgee; ENSG00000197372; Expressed in buccal mucosa cell and 111 other tissues.
DR ExpressionAtlas; Q8TD23; baseline and differential.
DR Genevisible; Q8TD23; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; 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:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0045453; P:bone resorption; TAS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IDA:BHF-UCL.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IDA:BHF-UCL.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..568
FT /note="Zinc finger protein 675"
FT /id="PRO_0000304875"
FT DOMAIN 4..75
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 144..166
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 172..194
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 200..222
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 228..250
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 256..278
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 284..306
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 312..334
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 340..362
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 368..390
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 396..418
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 424..446
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 452..474
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 480..502
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 508..530
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 536..558
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VARIANT 124
FT /note="L -> V (in dbSNP:rs4380159)"
FT /evidence="ECO:0000269|PubMed:11751921,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_060430"
FT VARIANT 197
FT /note="V -> A (in dbSNP:rs11671053)"
FT /id="VAR_057440"
FT VARIANT 410
FT /note="A -> T (in dbSNP:rs73029758)"
FT /id="VAR_060431"
FT CONFLICT 29
FT /note="Y -> C (in Ref. 1; AAK95822)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="K -> E (in Ref. 1; AAK95822)"
FT /evidence="ECO:0000305"
FT CONFLICT 191..218
FT /note="Missing (in Ref. 2; BAC04216)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="F -> S (in Ref. 1; AAK95822)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="H -> Y (in Ref. 1; AAK95822)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="G -> S (in Ref. 1; AAK95822)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="K -> E (in Ref. 1; AAK95822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 66299 MW; D11640BF26D10B04 CRC64;
MGLLTFRDVA IEFSLEEWQC LDTAQRNLYK NVILENYRNL VFLGIAVSKQ DLITCLEQEK
EPLTVKRHEM VNEPPVMCSH FAQEFWPEQN IKDSFEKVTL RRYEKCGNDN FQLKGCKSVD
ECKLHKGGYN GLNQCLPTMQ SKMFQCDKYV KVFNKFSHSD RHKIKHMENK PFKCKECGRS
FCMLSHLTRH ERNYTKVNFC KCEECEKAVN QSSKLTKHKR IYTCEKLYKC QECDRTFNQF
SNLTEYKKDY AREKPYKCEE CGKAFNQSSH LTTHKIIHTG EKPYKCEECG KAFNQFSNLT
THKKIHTGEQ PYICEECGKA FTQSSTLTTH KRIHTGEKPY KCEECGKAFN RSSKLTEHKN
IHTGEQPYKC EECGKAFNRS SNLTEHRKIH TEEKPYKCKE CGKAFKHSSA LTTHKRIHTG
EKPYKCEECG KAFNRSSKLT EHKKLHTGKK PYKCEECGKA FIQSSKLTEH KKIHSGEIPY
KCEECGKAFK HSSSLTTHKR IHTGEKPYKC EECGKAFSRS SKLTEHKIIH TGEKPYKCER
CDKAFNQSAN LTKHKKIHTG EKLQNWNV
