ZN195_HUMAN
ID ZN195_HUMAN Reviewed; 629 AA.
AC O14628; A8K234; B3KTK2; B4DEL0; C9JLY9; L7MNK2; Q0VAJ6; Q658N8; Q6ZNA9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Zinc finger protein 195;
GN Name=ZNF195; Synonyms=ZNFP104;
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] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RX PubMed=9344677; DOI=10.1006/geno.1997.4958;
RA Hussey D.J., Parker N.J., Hussey N.D., Little P.F.R., Dobrovic A.;
RT "Characterization of a KRAB family zinc finger gene, ZNF195, mapping to
RT chromosome band 11p15.5.";
RL Genomics 45:451-455(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4; 6 AND 7).
RC TISSUE=Brain, Cerebellum, and Subthalamic nucleus;
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 MRNA] (ISOFORM 4).
RC TISSUE=Stomach;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 8).
RC TISSUE=Retinoblastoma;
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-408, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-383 AND LYS-492, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-492, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=A;
CC IsoId=O14628-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=O14628-2; Sequence=Not described;
CC Name=3; Synonyms=C;
CC IsoId=O14628-3; Sequence=Not described;
CC Name=4;
CC IsoId=O14628-4; Sequence=VSP_036880;
CC Name=5;
CC IsoId=O14628-5; Sequence=VSP_036881;
CC Name=6;
CC IsoId=O14628-6; Sequence=VSP_036879, VSP_036881;
CC Name=7;
CC IsoId=O14628-7; Sequence=VSP_036879, VSP_036880;
CC Name=8;
CC IsoId=O14628-8; Sequence=VSP_036879, VSP_045071, VSP_045072;
CC -!- TISSUE SPECIFICITY: Expressed in adult heart, brain, placenta, skeletal
CC muscle and pancreas, and in fetal lung, kidney and brain. There is
CC little expression in adult lung, liver and kidney.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG57121.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF003540; AAB86596.1; -; mRNA.
DR EMBL; AK095720; BAG53114.1; -; mRNA.
DR EMBL; AK131296; BAD18466.1; -; mRNA.
DR EMBL; AK290099; BAF82788.1; -; mRNA.
DR EMBL; AK293679; BAG57121.1; ALT_FRAME; mRNA.
DR EMBL; AL833722; CAH56261.1; -; mRNA.
DR EMBL; AC123788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471158; EAX02548.1; -; Genomic_DNA.
DR EMBL; CH471158; EAX02549.1; -; Genomic_DNA.
DR EMBL; BC121028; AAI21029.1; -; mRNA.
DR EMBL; BC121029; AAI21030.1; -; mRNA.
DR EMBL; BM462194; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS41604.1; -. [O14628-4]
DR CCDS; CCDS44521.1; -. [O14628-5]
DR CCDS; CCDS44522.1; -. [O14628-1]
DR CCDS; CCDS55736.1; -. [O14628-7]
DR CCDS; CCDS55737.1; -. [O14628-6]
DR CCDS; CCDS58111.1; -. [O14628-8]
DR RefSeq; NP_001123991.1; NM_001130519.2. [O14628-5]
DR RefSeq; NP_001123992.1; NM_001130520.2. [O14628-1]
DR RefSeq; NP_001229770.1; NM_001242841.1. [O14628-6]
DR RefSeq; NP_001229771.1; NM_001242842.1.
DR RefSeq; NP_001229772.1; NM_001242843.1. [O14628-7]
DR RefSeq; NP_001243752.1; NM_001256823.1. [O14628-8]
DR RefSeq; NP_001243753.1; NM_001256824.1.
DR RefSeq; NP_001243754.1; NM_001256825.1. [O14628-7]
DR RefSeq; NP_009083.2; NM_007152.4. [O14628-4]
DR RefSeq; XP_016873752.1; XM_017018263.1.
DR AlphaFoldDB; O14628; -.
DR SMR; O14628; -.
DR BioGRID; 113532; 85.
DR IntAct; O14628; 11.
DR STRING; 9606.ENSP00000382511; -.
DR iPTMnet; O14628; -.
DR PhosphoSitePlus; O14628; -.
DR BioMuta; ZNF195; -.
DR REPRODUCTION-2DPAGE; O14628; -.
DR EPD; O14628; -.
DR jPOST; O14628; -.
DR MassIVE; O14628; -.
DR MaxQB; O14628; -.
DR PaxDb; O14628; -.
DR PeptideAtlas; O14628; -.
DR PRIDE; O14628; -.
DR ProteomicsDB; 10773; -.
DR ProteomicsDB; 48126; -. [O14628-1]
DR ProteomicsDB; 48127; -. [O14628-4]
DR ProteomicsDB; 48128; -. [O14628-5]
DR ProteomicsDB; 48129; -. [O14628-6]
DR ProteomicsDB; 48130; -. [O14628-7]
DR Antibodypedia; 5737; 139 antibodies from 24 providers.
DR DNASU; 7748; -.
DR Ensembl; ENST00000005082.13; ENSP00000005082.9; ENSG00000005801.18. [O14628-5]
DR Ensembl; ENST00000343338.11; ENSP00000344483.7; ENSG00000005801.18. [O14628-7]
DR Ensembl; ENST00000354599.10; ENSP00000346613.6; ENSG00000005801.18. [O14628-4]
DR Ensembl; ENST00000399602.9; ENSP00000382511.4; ENSG00000005801.18. [O14628-1]
DR Ensembl; ENST00000429541.6; ENSP00000387998.2; ENSG00000005801.18. [O14628-7]
DR Ensembl; ENST00000438262.6; ENSP00000414353.2; ENSG00000005801.18. [O14628-8]
DR Ensembl; ENST00000526601.5; ENSP00000435828.1; ENSG00000005801.18. [O14628-6]
DR Ensembl; ENST00000528218.5; ENSP00000436384.1; ENSG00000005801.18. [O14628-8]
DR Ensembl; ENST00000618467.4; ENSP00000482411.1; ENSG00000005801.18. [O14628-8]
DR GeneID; 7748; -.
DR KEGG; hsa:7748; -.
DR MANE-Select; ENST00000399602.9; ENSP00000382511.4; NM_001130520.3; NP_001123992.1.
DR UCSC; uc001lxs.4; human. [O14628-1]
DR CTD; 7748; -.
DR DisGeNET; 7748; -.
DR GeneCards; ZNF195; -.
DR HGNC; HGNC:12986; ZNF195.
DR HPA; ENSG00000005801; Low tissue specificity.
DR MIM; 602187; gene.
DR neXtProt; NX_O14628; -.
DR OpenTargets; ENSG00000005801; -.
DR PharmGKB; PA37566; -.
DR VEuPathDB; HostDB:ENSG00000005801; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000153165; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; O14628; -.
DR OMA; NISHTGQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O14628; -.
DR TreeFam; TF342117; -.
DR PathwayCommons; O14628; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; O14628; -.
DR BioGRID-ORCS; 7748; 8 hits in 1099 CRISPR screens.
DR ChiTaRS; ZNF195; human.
DR GenomeRNAi; 7748; -.
DR Pharos; O14628; Tdark.
DR PRO; PR:O14628; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O14628; protein.
DR Bgee; ENSG00000005801; Expressed in buccal mucosa cell and 190 other tissues.
DR ExpressionAtlas; O14628; baseline and differential.
DR Genevisible; O14628; 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
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; 7.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..629
FT /note="Zinc finger protein 195"
FT /id="PRO_0000047447"
FT DOMAIN 4..75
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 244..266
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 272..294
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 410..432
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..488
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 494..516
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 522..544
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 550..572
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 578..600
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 606..628
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 76..243
FT /note="Spacer"
FT MOD_RES 408
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 383
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MAGAQ (in isoform 6, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036879"
FT VAR_SEQ 76..147
FT /note="Missing (in isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_036880"
FT VAR_SEQ 76..86
FT /note="EMGFHHATQAC -> GIFFVVTMEII (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045071"
FT VAR_SEQ 87..629
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045072"
FT VAR_SEQ 125..147
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036881"
FT CONFLICT 290
FT /note="P -> R (in Ref. 2; BAG53114)"
FT /evidence="ECO:0000305"
FT CONFLICT 352..407
FT /note="Missing (in Ref. 2; BAD18466)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="V -> A (in Ref. 1; AAB86596)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="K -> Q (in Ref. 1; AAB86596)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 629 AA; 72332 MW; D048217DFC6BFDFB CRC64;
MTLLTFRDVA IEFSLEEWKC LDLAQQNLYR DVMLENYRNL FSVGLTVCKP GLITCLEQRK
EPWNVKRQEA ADGHPEMGFH HATQACLELL GSSDLPASAS QSAGITGVNH RAQPGLNVSV
DKFTALCSPG VLQTVKWFLE FRCIFSLAMS SHFTQDLLPE QGIQDAFPKR ILRGYGNCGL
DNLYLRKDWE SLDECKLQKD YNGLNQCSST THSKIFQYNK YVKIFDNFSN LHRRNISNTG
EKPFKCQECG KSFQMLSFLT EHQKIHTGKK FQKCGECGKT FIQCSHFTEP ENIDTGEKPY
KCQECNNVIK TCSVLTKNRI YAGGEHYRCE EFGKVFNQCS HLTEHEHGTE EKPCKYEECS
SVFISCSSLS NQQMILAGEK LSKCETWYKG FNHSPNPSKH QRNEIGGKPF KCEECDSIFK
WFSDLTKHKR IHTGEKPYKC DECGKAYTQS SHLSEHRRIH TGEKPYQCEE CGKVFRTCSS
LSNHKRTHSE EKPYTCEECG NIFKQLSDLT KHKKTHTGEK PYKCDECGKN FTQSSNLIVH
KRIHTGEKPY KCEECGRVFM WFSDITKHKK THTGEKPYKC DECGKNFTQS SNLIVHKRIH
TGEKPYKCEK CGKAFTQFSH LTVHESIHT
