ZN135_HUMAN
ID ZN135_HUMAN Reviewed; 658 AA.
AC P52742; B4DHH9; E9PEV2; F5GYY9; I3L0B3; Q5U5L3; Q8N1I7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Zinc finger protein 135;
DE AltName: Full=Zinc finger protein 61;
DE AltName: Full=Zinc finger protein 78-like 1;
GN Name=ZNF135; Synonyms=ZNF61, ZNF78L1;
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] (ISOFORMS 2 AND 3), AND VARIANT
RP ASP-22.
RC TISSUE=Brain, and 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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-22.
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 166-658 (ISOFORM 1).
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 [6]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. May be involved in transcriptional
CC regulation. {ECO:0000269|PubMed:21834987}.
CC -!- INTERACTION:
CC P52742; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-7101455, EBI-11954519;
CC P52742; P61968: LMO4; NbExp=3; IntAct=EBI-7101455, EBI-2798728;
CC P52742; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-7101455, EBI-748391;
CC P52742; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-7101455, EBI-12040603;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P52742-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52742-2; Sequence=VSP_046073, VSP_046074;
CC Name=3;
CC IsoId=P52742-3; Sequence=VSP_046706;
CC Name=4;
CC IsoId=P52742-4; Sequence=VSP_046073, VSP_046706;
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50254.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK098011; BAC05214.1; -; mRNA.
DR EMBL; AK295110; BAG58141.1; -; mRNA.
DR EMBL; AC008751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72553.1; -; Genomic_DNA.
DR EMBL; BC046434; AAH46434.1; -; mRNA.
DR EMBL; U09413; AAC50254.1; ALT_FRAME; mRNA.
DR CCDS; CCDS12970.2; -. [P52742-3]
DR CCDS; CCDS54329.1; -. [P52742-4]
DR CCDS; CCDS54330.1; -. [P52742-2]
DR CCDS; CCDS74471.1; -. [P52742-1]
DR PIR; I38600; I38600.
DR RefSeq; NP_001158001.1; NM_001164529.1.
DR RefSeq; NP_001158002.1; NM_001164530.1. [P52742-2]
DR RefSeq; NP_001276330.1; NM_001289401.1. [P52742-1]
DR RefSeq; NP_001276331.1; NM_001289402.1.
DR RefSeq; NP_003427.3; NM_003436.3. [P52742-3]
DR RefSeq; NP_009065.1; NM_007134.1. [P52742-4]
DR RefSeq; XP_006723425.1; XM_006723362.3. [P52742-3]
DR RefSeq; XP_006723426.1; XM_006723363.3. [P52742-3]
DR RefSeq; XP_016882729.1; XM_017027240.1. [P52742-1]
DR AlphaFoldDB; P52742; -.
DR SMR; P52742; -.
DR BioGRID; 113489; 10.
DR IntAct; P52742; 11.
DR MINT; P52742; -.
DR STRING; 9606.ENSP00000441410; -.
DR iPTMnet; P52742; -.
DR PhosphoSitePlus; P52742; -.
DR BioMuta; ZNF135; -.
DR DMDM; 296453071; -.
DR EPD; P52742; -.
DR jPOST; P52742; -.
DR MassIVE; P52742; -.
DR PaxDb; P52742; -.
DR PeptideAtlas; P52742; -.
DR PRIDE; P52742; -.
DR ProteomicsDB; 19965; -.
DR ProteomicsDB; 24883; -.
DR ProteomicsDB; 46318; -.
DR ProteomicsDB; 56518; -. [P52742-1]
DR Antibodypedia; 1840; 77 antibodies from 16 providers.
DR DNASU; 7694; -.
DR Ensembl; ENST00000313434.10; ENSP00000321406.5; ENSG00000176293.20. [P52742-1]
DR Ensembl; ENST00000359978.10; ENSP00000369437.4; ENSG00000176293.20. [P52742-2]
DR Ensembl; ENST00000401053.8; ENSP00000441410.1; ENSG00000176293.20. [P52742-4]
DR Ensembl; ENST00000511556.5; ENSP00000422074.1; ENSG00000176293.20. [P52742-3]
DR GeneID; 7694; -.
DR KEGG; hsa:7694; -.
DR MANE-Select; ENST00000313434.10; ENSP00000321406.5; NM_001289401.2; NP_001276330.1.
DR UCSC; uc002qrd.3; human. [P52742-1]
DR CTD; 7694; -.
DR DisGeNET; 7694; -.
DR GeneCards; ZNF135; -.
DR HGNC; HGNC:12919; ZNF135.
DR HPA; ENSG00000176293; Low tissue specificity.
DR MIM; 604077; gene.
DR neXtProt; NX_P52742; -.
DR OpenTargets; ENSG00000176293; -.
DR PharmGKB; PA37507; -.
DR VEuPathDB; HostDB:ENSG00000176293; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000153104; -.
DR HOGENOM; CLU_002678_44_0_1; -.
DR InParanoid; P52742; -.
DR OMA; TCAKEKP; -.
DR PhylomeDB; P52742; -.
DR TreeFam; TF350822; -.
DR PathwayCommons; P52742; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; P52742; -.
DR BioGRID-ORCS; 7694; 13 hits in 1090 CRISPR screens.
DR GenomeRNAi; 7694; -.
DR Pharos; P52742; Tbio.
DR PRO; PR:P52742; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P52742; protein.
DR Bgee; ENSG00000176293; Expressed in ganglionic eminence and 112 other tissues.
DR ExpressionAtlas; P52742; baseline and differential.
DR Genevisible; P52742; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; 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; 16.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..658
FT /note="Zinc finger protein 135"
FT /id="PRO_0000047419"
FT DOMAIN 14..85
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 214..236
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 242..264
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 270..292
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 298..320
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 326..348
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..376
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 382..404
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 410..432
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..488
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 494..516
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 522..544
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 550..572
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 578..600
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 606..628
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 171..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..11
FT /note="MTPGVRVSTDP -> MELGSRRRSVGCRCRGLCLAVRR (in isoform 2
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046073"
FT VAR_SEQ 85
FT /note="P -> PEIKGHFQFLLLS (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046706"
FT VAR_SEQ 359..638
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046074"
FT VARIANT 22
FT /note="G -> D (in dbSNP:rs1469087)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_052774"
FT VARIANT 507
FT /note="S -> L (in dbSNP:rs2228277)"
FT /id="VAR_052775"
FT VARIANT 517
FT /note="T -> A (in dbSNP:rs2228278)"
FT /id="VAR_052776"
FT VARIANT 579
FT /note="G -> R (in dbSNP:rs2228279)"
FT /id="VAR_052777"
FT VARIANT 592
FT /note="S -> L (in dbSNP:rs2228275)"
FT /id="VAR_052778"
FT CONFLICT 166
FT /note="G -> R (in Ref. 5; AAC50254)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="C -> F (in Ref. 1; BAG58141)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="S -> C (in Ref. 1; BAG58141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 658 AA; 75261 MW; ED6A4FB042CB3CE5 CRC64;
MTPGVRVSTD PEQVTFEDVV VGFSQEEWGQ LKPAQRTLYR DVMLDTFRLL VSVGHWLPKP
NVISLLEQEA ELWAVESRLP QGVYPDLETR PKVKLSVLKQ GISEEISNSV ILVERFLWDG
LWYCRGEDTE GHWEWSCESL ESLAVPVAFT PVKTPVLEQW QRNGFGENIS LNPDLPHQPM
TPERQSPHTW GTRGKREKPD LNVLQKTCVK EKPYKCQECG KAFSHSSALI EHHRTHTGER
PYECHECLKG FRNSSALTKH QRIHTGEKPY KCTQCGRTFN QIAPLIQHQR THTGEKPYEC
SECGKSFSFR SSFSQHERTH TGEKPYECSE CGKAFRQSIH LTQHLRIHTG EKPYQCGECG
KAFSHSSSLT KHQRIHTGEK PYECHECGKA FTQITPLIQH QRTHTGEKPY ECGECGKAFS
QSTLLTEHRR IHTGEKPYGC NECGKTFSHS SSLSQHERTH TGEKPYECSQ CGKAFRQSTH
LTQHQRIHTG EKPYECNDCG KAFSHSSSLT KHQRIHTGEK PYECNQCGRA FSQLAPLIQH
QRIHTGEKPY ECNQCGRAFS QSSLLIEHQR IHTKEKPYGC NECGKSFSHS SSLSQHERTH
TGEKPYECHD CGKSFRQSTH LTQHRRIHTG EKPYACRDCG KAFTHSSSLT KHQRTHTG
