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ZN140_HUMAN
ID   ZN140_HUMAN             Reviewed;         457 AA.
AC   P52738; D3DXJ3; Q05CP6; Q8IV75;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Zinc finger protein 140;
GN   Name=ZNF140;
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).
RC   TISSUE=Insulinoma;
RX   PubMed=7649249; DOI=10.1016/0014-5793(95)00728-r;
RA   Vissing H., Meyer W.-K., Aagaard L., Tommerup N., Thiesen H.-J.;
RT   "Repression of transcriptional activity by heterologous KRAB domains
RT   present in zinc finger proteins.";
RL   FEBS Lett. 369:153-157(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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).
CC   -!- FUNCTION: May be involved in transcriptional regulation as a repressor.
CC   -!- INTERACTION:
CC       P52738; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-12069140, EBI-742909;
CC       P52738; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-12069140, EBI-12011224;
CC       P52738; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-12069140, EBI-739624;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P52738-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P52738-2; Sequence=VSP_056436;
CC   -!- TISSUE SPECIFICITY: Seems ubiquitous. Seen in the heart, brain,
CC       placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; U09368; AAC50262.1; -; mRNA.
DR   EMBL; AK122741; BAG53698.1; -; mRNA.
DR   EMBL; AK303240; BAG64326.1; -; mRNA.
DR   EMBL; AC026786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471218; EAW54795.1; -; Genomic_DNA.
DR   EMBL; CH471218; EAW54797.1; -; Genomic_DNA.
DR   EMBL; CH471218; EAW54798.1; -; Genomic_DNA.
DR   EMBL; BC022291; AAH22291.1; -; mRNA.
DR   EMBL; BC040561; AAH40561.1; -; mRNA.
DR   CCDS; CCDS73550.1; -. [P52738-2]
DR   CCDS; CCDS9282.1; -. [P52738-1]
DR   PIR; C57785; C57785.
DR   RefSeq; NP_001287705.1; NM_001300776.1. [P52738-2]
DR   RefSeq; NP_001287706.1; NM_001300777.1.
DR   RefSeq; NP_001287707.1; NM_001300778.1. [P52738-2]
DR   RefSeq; NP_003431.2; NM_003440.3. [P52738-1]
DR   RefSeq; XP_011533137.1; XM_011534835.2. [P52738-1]
DR   RefSeq; XP_011533142.1; XM_011534840.2. [P52738-2]
DR   RefSeq; XP_016875413.1; XM_017019924.1. [P52738-2]
DR   RefSeq; XP_016875414.1; XM_017019925.1. [P52738-2]
DR   AlphaFoldDB; P52738; -.
DR   SMR; P52738; -.
DR   BioGRID; 113493; 7.
DR   IntAct; P52738; 5.
DR   STRING; 9606.ENSP00000347755; -.
DR   iPTMnet; P52738; -.
DR   PhosphoSitePlus; P52738; -.
DR   BioMuta; ZNF140; -.
DR   DMDM; 206729944; -.
DR   EPD; P52738; -.
DR   MassIVE; P52738; -.
DR   PaxDb; P52738; -.
DR   PeptideAtlas; P52738; -.
DR   PRIDE; P52738; -.
DR   ProteomicsDB; 56511; -. [P52738-1]
DR   ProteomicsDB; 58394; -.
DR   Antibodypedia; 45872; 57 antibodies from 18 providers.
DR   DNASU; 7699; -.
DR   Ensembl; ENST00000355557.7; ENSP00000347755.2; ENSG00000196387.10. [P52738-1]
DR   Ensembl; ENST00000544426.5; ENSP00000445411.1; ENSG00000196387.10. [P52738-2]
DR   GeneID; 7699; -.
DR   KEGG; hsa:7699; -.
DR   MANE-Select; ENST00000355557.7; ENSP00000347755.2; NM_003440.4; NP_003431.2.
DR   UCSC; uc001ulo.4; human. [P52738-1]
DR   CTD; 7699; -.
DR   DisGeNET; 7699; -.
DR   GeneCards; ZNF140; -.
DR   HGNC; HGNC:12925; ZNF140.
DR   HPA; ENSG00000196387; Low tissue specificity.
DR   MIM; 604082; gene.
DR   neXtProt; NX_P52738; -.
DR   OpenTargets; ENSG00000196387; -.
DR   PharmGKB; PA37512; -.
DR   VEuPathDB; HostDB:ENSG00000196387; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000163022; -.
DR   HOGENOM; CLU_002678_0_9_1; -.
DR   InParanoid; P52738; -.
DR   OMA; NQGCIRQ; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P52738; -.
DR   TreeFam; TF337055; -.
DR   PathwayCommons; P52738; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; P52738; -.
DR   SIGNOR; P52738; -.
DR   BioGRID-ORCS; 7699; 7 hits in 1095 CRISPR screens.
DR   ChiTaRS; ZNF140; human.
DR   GenomeRNAi; 7699; -.
DR   Pharos; P52738; Tdark.
DR   PRO; PR:P52738; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P52738; protein.
DR   Bgee; ENSG00000196387; Expressed in calcaneal tendon and 173 other tissues.
DR   ExpressionAtlas; P52738; baseline and differential.
DR   Genevisible; P52738; 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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
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; 8.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 6.
DR   PROSITE; PS50805; KRAB; 1.
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; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..457
FT                   /note="Zinc finger protein 140"
FT                   /id="PRO_0000047423"
FT   DOMAIN          6..77
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         161..183
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         189..211
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         217..239
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         245..267
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         273..295
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         301..323
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         329..351
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         357..379
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         385..407
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         413..435
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   VAR_SEQ         1..103
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056436"
FT   VARIANT         386
FT                   /note="A -> V (in dbSNP:rs2229373)"
FT                   /id="VAR_046562"
FT   CONFLICT        338
FT                   /note="F -> L (in Ref. 1; AAC50262)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   457 AA;  52996 MW;  F4FF0B7D85E03731 CRC64;
     MSQGSVTFRD VAIDFSQEEW KWLQPAQRDL YRCVMLENYG HLVSLGLSIS KPDVVSLLEQ
     GKEPWLGKRE VKRDLFSVSE SSGEIKDFSP KNVIYDDSSQ YLIMERILSQ GPVYSSFKGG
     WKCKDHTEML QENQGCIRKV TVSHQEALAQ HMNISTVERP YGCHECGKTF GRRFSLVLHQ
     RTHTGEKPYA CKECGKTFSQ ISNLVKHQMI HTGKKPHECK DCNKTFSYLS FLIEHQRTHT
     GEKPYECTEC GKAFSRASNL TRHQRIHIGK KQYICRKCGK AFSSGSELIR HQITHTGEKP
     YECIECGKAF RRFSHLTRHQ SIHTTKTPYE CNECRKAFRC HSFLIKHQRI HAGEKLYECD
     ECGKVFTWHA SLIQHTKSHT GEKPYACAEC DKAFSRSFSL ILHQRTHTGE KPYVCKVCNK
     SFSWSSNLAK HQRTHTLDNP YEYENSFNYH SFLTEHQ
 
 
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