ZN134_HUMAN
ID ZN134_HUMAN Reviewed; 427 AA.
AC P52741; Q9Y4B2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger protein 134;
GN Name=ZNF134;
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 2).
RC TISSUE=Insulinoma;
RX PubMed=7557990; DOI=10.1006/geno.1995.1040;
RA Tommerup N., Vissing H.;
RT "Isolation and fine mapping of 16 novel human zinc finger-encoding cDNAs
RT identify putative candidate genes for developmental and malignant
RT disorders.";
RL Genomics 27:259-264(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-135 AND LYS-139, AND
RP IDENTIFICATION BY MASS 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 P52741; P55081: MFAP1; NbExp=3; IntAct=EBI-18054945, EBI-1048159;
CC P52741; Q63HR2: TNS2; NbExp=3; IntAct=EBI-18054945, EBI-949753;
CC P52741; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-18054945, EBI-725997;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P52741-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52741-2; Sequence=VSP_035666;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U09412; AAC50253.1; -; mRNA.
DR EMBL; AK291763; BAF84452.1; -; mRNA.
DR EMBL; AC003682; AAC24610.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72518.1; -; Genomic_DNA.
DR EMBL; BC112294; AAI12295.1; -; mRNA.
DR EMBL; BC113410; AAI13411.1; -; mRNA.
DR CCDS; CCDS42638.1; -. [P52741-1]
DR PIR; I38599; I38599.
DR RefSeq; NP_003426.3; NM_003435.4. [P52741-1]
DR AlphaFoldDB; P52741; -.
DR SMR; P52741; -.
DR BioGRID; 113488; 2.
DR IntAct; P52741; 3.
DR STRING; 9606.ENSP00000379464; -.
DR iPTMnet; P52741; -.
DR PhosphoSitePlus; P52741; -.
DR BioMuta; ZNF134; -.
DR DMDM; 212276482; -.
DR EPD; P52741; -.
DR MassIVE; P52741; -.
DR MaxQB; P52741; -.
DR PaxDb; P52741; -.
DR PeptideAtlas; P52741; -.
DR PRIDE; P52741; -.
DR ProteomicsDB; 56516; -. [P52741-1]
DR ProteomicsDB; 56517; -. [P52741-2]
DR Antibodypedia; 1817; 206 antibodies from 29 providers.
DR DNASU; 7693; -.
DR Ensembl; ENST00000396161.10; ENSP00000379464.4; ENSG00000213762.12. [P52741-1]
DR GeneID; 7693; -.
DR KEGG; hsa:7693; -.
DR MANE-Select; ENST00000396161.10; ENSP00000379464.4; NM_003435.5; NP_003426.3.
DR UCSC; uc002qpn.3; human. [P52741-1]
DR CTD; 7693; -.
DR DisGeNET; 7693; -.
DR GeneCards; ZNF134; -.
DR HGNC; HGNC:12918; ZNF134.
DR HPA; ENSG00000213762; Low tissue specificity.
DR MIM; 604076; gene.
DR neXtProt; NX_P52741; -.
DR OpenTargets; ENSG00000213762; -.
DR PharmGKB; PA37506; -.
DR VEuPathDB; HostDB:ENSG00000213762; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154734; -.
DR HOGENOM; CLU_002678_0_2_1; -.
DR InParanoid; P52741; -.
DR OMA; VKNCRVC; -.
DR PhylomeDB; P52741; -.
DR TreeFam; TF342033; -.
DR PathwayCommons; P52741; -.
DR SignaLink; P52741; -.
DR BioGRID-ORCS; 7693; 11 hits in 1099 CRISPR screens.
DR GenomeRNAi; 7693; -.
DR Pharos; P52741; Tdark.
DR PRO; PR:P52741; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P52741; protein.
DR Bgee; ENSG00000213762; Expressed in secondary oocyte and 163 other tissues.
DR ExpressionAtlas; P52741; baseline and differential.
DR Genevisible; P52741; HS.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor 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; 9.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..427
FT /note="Zinc finger protein 134"
FT /id="PRO_0000047418"
FT ZN_FING 50..72
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 78..100
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 176..198
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 204..226
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 232..254
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 260..282
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 288..310
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 316..338
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 344..366
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 372..394
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..422
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..91
FT /note="MTLVTAGGAWTGPGCWHEVKDEESSSEQSISIAVSHVNTSKAGLPAQTALPC
FT DICGPILKDILHLDEHQGTHHGLKLHTCGACGRQFWFSA -> MWGMWETILVQC (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:7557990"
FT /id="VSP_035666"
FT VARIANT 30
FT /note="I -> T (in dbSNP:rs10414451)"
FT /id="VAR_052771"
FT VARIANT 46
FT /note="A -> T (in dbSNP:rs10413455)"
FT /id="VAR_052772"
FT VARIANT 207
FT /note="S -> R (in dbSNP:rs34034473)"
FT /id="VAR_052773"
SQ SEQUENCE 427 AA; 48480 MW; AADF3DD519F12712 CRC64;
MTLVTAGGAW TGPGCWHEVK DEESSSEQSI SIAVSHVNTS KAGLPAQTAL PCDICGPILK
DILHLDEHQG THHGLKLHTC GACGRQFWFS ANLHQYQKCY SIEQPLRRDK SEASIVKNCT
VSKEPHPSEK PFTCKEEQKN FQATLGGCQQ KAIHSKRKTH RSTESGDAFH GEQMHYKCSE
CGKAFSRKDT LVQHQRIHSG EKPYECSECG KAFSRKATLV QHQRIHTGER PYECSECGKT
FSRKDNLTQH KRIHTGEMPY KCNECGKYFS HHSNLIVHQR VHNGARPYKC SDCGKVFRHK
STLVQHESIH TGENPYDCSD CGKSFGHKYT LIKHQRIHTE SKPFECIECG KFFSRSSDYI
AHQRVHTGER PFVCSKCGKD FIRTSHLVRH QRVHTGERPY ECSECGKAYS LSSHLNRHQK
VHTAGRL
