MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Zinc finger protein 74; AltName: Full=Zinc finger protein 520; AltName: Full=hZNF7; |
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| MyHits synonyms | ZNF74_HUMAN , Q16587 , B5MCE3 , B7Z5Y2 , Q6IBV2 , Q6PJP1 , Q9UC04 , Q9UF05 , Q9UF06 , Q9UF07 , 87E5AA122BBC82F1 |
 Legends: 1, VARIANT E -> K (in dbSNP:rs3747076). {ECO:0000269|PubMed:11705709, ECO:0000269|PubMed:14702039}; 2, CONFLICT V -> A (in Ref. 7; AAH13395). {ECO:0000305}; 3, CONFLICT V -> M (in Ref. 1; CAA63379, 2; CAA50632 and 4; AAF21777/AAF21778/AAF21779/ AAF21780). {ECO:0000305}; 4, CONFLICT S -> P (in Ref. 5; BAH13068). {ECO:0000305}; 5, KRAB. {ECO:0000255|PROSITE- ProRule:PRU00119}; 6, ZN_FING C2H2-type 1. {ECO:0000255|PROSITE- ProRule:PRU00042}; 7, ZN_FING C2H2-type 2. {ECO:0000255|PROSITE- ProRule:PRU00042}; 8, ZN_FING C2H2-type 3. {ECO:0000255|PROSITE- ProRule:PRU00042}; 9, ZN_FING C2H2-type 4. {ECO:0000255|PROSITE- ProRule:PRU00042}; 10, ZN_FING C2H2-type 5. {ECO:0000255|PROSITE- ProRule:PRU00042}; 11, ZN_FING C2H2-type 6. {ECO:0000255|PROSITE- ProRule:PRU00042}; 12, ZN_FING C2H2-type 7. {ECO:0000255|PROSITE- ProRule:PRU00042}; 13, ZN_FING C2H2-type 8. {ECO:0000255|PROSITE- ProRule:PRU00042}; 14, ZN_FING C2H2-type 9. {ECO:0000255|PROSITE- ProRule:PRU00042}; 15, ZN_FING C2H2-type 10. {ECO:0000255|PROSITE- ProRule:PRU00042}; 16, ZN_FING C2H2-type 11. {ECO:0000255|PROSITE- ProRule:PRU00042}; 17, ZN_FING C2H2-type 12. {ECO:0000255|PROSITE- ProRule:PRU00042}; 18, VAR_SEQ MEIPAPEPEKTALSSQDPALSLKENLEDISGWGLPEARSKE SVSFKDVAVDFTQEEWGQLDSPQRALYRDVMLENYQNLLAL -> MPSPPFSPRA (in isoform 4). {ECO:0000305}; 19, VAR_SEQ Missing (in isoform 1). {ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:8268910, ECO:0000303|PubMed:8663113}; 20, VAR_SEQ ALSSQDPALSLKENLEDISGWGLPEARSKESVSFKDVAVDF TQEEWGQLDSPQRALYRDVMLENYQNLLALGPPLHKPDVIS HLERGEEPWSMQREVPRGPCPEWELKAVPSQQQGICKEEPA QEPIMERPLGGAQAWGRQAGALQRSQAAPWAPAPAMVWDVP VEE -> GIGEFQGCGCGLHPGGVGSTRLPSEGLVPGCDVG ELPEPSCPRTSTAQARCDLSSGTRRGAMEHAEGSPQRALSR MGAEGGALSTAGHLQRRTGPGAHHGAAPRRGAGVGAPGRCS AEESGCALGARTCHGLGRPCRGIPPQVSPLRPATRSRGGTL AGHTQERPGH (in isoform 5). {ECO:0000303|PubMed:15489334}; 21, VAR_SEQ Missing (in isoform 3). {ECO:0000305}; 22, VARIANT KL -> NF; 23, ismart:ZnF_C2H2 [T]; 24, ipat:ZINC_FINGER_C2H2_1 [T]; 25, iprf:ZINC_FINGER_C2H2_2 [T]; 26, ismart:KRAB [T]; 27, iprf:KRAB [T]; 28, ipfam:KRAB [T].
| |
ID ZNF74_HUMAN Reviewed; 644 AA.
AC Q16587; B5MCE3; B7Z5Y2; Q6IBV2; Q6PJP1; Q9UC04; Q9UF05; Q9UF06;
AC Q9UF07;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 30-NOV-2016, entry version 159.
DE RecName: Full=Zinc finger protein 74;
DE AltName: Full=Zinc finger protein 520;
DE AltName: Full=hZNF7;
GN Name=ZNF74; Synonyms=ZNF520;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8663113; DOI=10.1074/jbc.271.26.15458;
RA Grondin B., Bazinet M., Aubry M.;
RT "The KRAB zinc finger gene ZNF74 encodes an RNA-binding protein
RT tightly associated with the nuclear matrix.";
RL J. Biol. Chem. 271:15458-15467(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8268910; DOI=10.1093/hmg/2.10.1583;
RA Aubry M., Demczuk S., Desmaze C., Aikem M., Aurias M., Julien J.-P.,
RA Rouleau G.A.;
RT "Isolation of a zinc finger gene consistently deleted in DiGeorge
RT syndrome.";
RL Hum. Mol. Genet. 2:1583-1587(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RA Aubry M., Cote F.;
RT "Alternative promoter usage and splicing of ZNF74 gene.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP LYS-117.
RC TISSUE=Brain;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC TISSUE=Muscle, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 499-583.
RX PubMed=1639391; DOI=10.1016/0888-7543(92)90135-F;
RA Aubry M., Marineau C., Zhang F.R., Zahed L., Figlewicz D.,
RA Delattre O., Thomas G., de Jong P.J., Julien J.-P., Rouleau G.A.;
RT "Cloning of six new genes with zinc finger motifs mapping to short and
RT long arms of human acrocentric chromosome 22 (p and q11.2).";
RL Genomics 13:641-648(1992).
RN [9]
RP VARIANTS LYS-117 AND 623-ASN-PHE-624.
RX PubMed=11705709; DOI=10.1016/S0920-9964(00)00191-2;
RA Takase K., Ohtsuki T., Migita O., Toru M., Inada T.,
RA Yamakawa-Kobayashi K., Arinami T.;
RT "Association of ZNF74 gene genotypes with age-at-onset of
RT schizophrenia.";
RL Schizophr. Res. 52:161-165(2001).
CC -!- FUNCTION: May play a role in RNA metabolism.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=2;
CC IsoId=Q16587-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q16587-2; Sequence=VSP_006891;
CC Name=3;
CC IsoId=Q16587-3; Sequence=VSP_006892;
CC Name=4;
CC IsoId=Q16587-4; Sequence=VSP_006893;
CC Name=5;
CC IsoId=Q16587-5; Sequence=VSP_045530, VSP_045531;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Highly expressed in the fetal brain.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 12 C2H2-type zinc fingers.
CC {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC -!- SIMILARITY: Contains 1 KRAB domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00119}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF21777.1; Type=Frameshift; Positions=164, 173; Evidence={ECO:0000305};
CC Sequence=AAF21778.1; Type=Frameshift; Positions=164, 173; Evidence={ECO:0000305};
CC Sequence=AAF21779.1; Type=Frameshift; Positions=164, 173; Evidence={ECO:0000305};
CC Sequence=AAF21780.1; Type=Frameshift; Positions=164, 173; Evidence={ECO:0000305};
CC Sequence=CAA50632.1; Type=Frameshift; Positions=164, 173; Evidence={ECO:0000305};
CC Sequence=CAA63379.1; Type=Frameshift; Positions=164, 173; Evidence={ECO:0000305};
DR EMBL; X92715; CAA63379.1; ALT_FRAME; mRNA.
DR EMBL; X71623; CAA50632.1; ALT_FRAME; mRNA.
DR EMBL; CR456616; CAG30502.1; -; mRNA.
DR EMBL; AF072567; AAF21777.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF072557; AAF21777.1; JOINED; Genomic_DNA.
DR EMBL; AF072562; AAF21777.1; JOINED; Genomic_DNA.
DR EMBL; AF072567; AAF21778.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF072557; AAF21778.1; JOINED; Genomic_DNA.
DR EMBL; AF072562; AAF21778.1; JOINED; Genomic_DNA.
DR EMBL; AF072567; AAF21779.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF072562; AAF21779.1; JOINED; Genomic_DNA.
DR EMBL; AF072567; AAF21780.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF072562; AAF21780.1; JOINED; Genomic_DNA.
DR EMBL; AK299569; BAH13068.1; -; mRNA.
DR EMBL; AC007731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013395; AAH13395.1; -; mRNA.
DR EMBL; BC056902; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X63182; CAC16149.1; -; Genomic_DNA.
DR CCDS; CCDS42982.1; -. [Q16587-1]
DR CCDS; CCDS58794.1; -. [Q16587-5]
DR PIR; I39311; I39311.
DR RefSeq; NP_001243452.1; NM_001256523.1. [Q16587-5]
DR RefSeq; NP_001243453.1; NM_001256524.1. [Q16587-1]
DR RefSeq; NP_001243454.1; NM_001256525.1. [Q16587-2]
DR RefSeq; NP_003417.2; NM_003426.3. [Q16587-1]
DR UniGene; Hs.517418; -.
DR ProteinModelPortal; Q16587; -.
DR SMR; Q16587; -.
DR BioGrid; 113444; 4.
DR IntAct; Q16587; 3.
DR STRING; 9606.ENSP00000349098; -.
DR iPTMnet; Q16587; -.
DR PhosphoSitePlus; Q16587; -.
DR BioMuta; ZNF74; -.
DR DMDM; 292495055; -.
DR EPD; Q16587; -.
DR PaxDb; Q16587; -.
DR PeptideAtlas; Q16587; -.
DR PRIDE; Q16587; -.
DR DNASU; 7625; -.
DR Ensembl; ENST00000400451; ENSP00000383301; ENSG00000185252. [Q16587-1]
DR Ensembl; ENST00000403682; ENSP00000384750; ENSG00000185252. [Q16587-5]
DR Ensembl; ENST00000405993; ENSP00000385855; ENSG00000185252. [Q16587-3]
DR Ensembl; ENST00000611540; ENSP00000483077; ENSG00000185252. [Q16587-1]
DR GeneID; 7625; -.
DR KEGG; hsa:7625; -.
DR UCSC; uc002zsh.5; human. [Q16587-1]
DR CTD; 7625; -.
DR DisGeNET; 7625; -.
DR GeneCards; ZNF74; -.
DR HGNC; HGNC:13144; ZNF74.
DR HPA; HPA003354; -.
DR MIM; 194548; gene.
DR neXtProt; NX_Q16587; -.
DR OpenTargets; ENSG00000185252; -.
DR PharmGKB; PA37718; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; COG5048; LUCA.
DR GeneTree; ENSGT00860000133913; -.
DR HOGENOM; HOG000074097; -.
DR HOVERGEN; HBG018163; -.
DR InParanoid; Q16587; -.
DR KO; K09228; -.
DR OMA; RCWKAFS; -.
DR OrthoDB; EOG091G02KC; -.
DR PhylomeDB; Q16587; -.
DR TreeFam; TF341817; -.
DR BioCyc; ZFISH:G66-31624-MONOMER; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR GeneWiki; ZNF74; -.
DR GenomeRNAi; 7625; -.
DR PRO; PR:Q16587; -.
DR Proteomes; UP000005640; Chromosome 22.
DR Bgee; ENSG00000185252; -.
DR CleanEx; HS_ZNF74; -.
DR ExpressionAtlas; Q16587; baseline and differential.
DR Genevisible; Q16587; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR CDD; cd07765; KRAB_A-box; 1.
DR Gene3D; 3.30.160.60; -; 12.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; DNA-binding; Metal-binding;
KW Nucleus; Polymorphism; Reference proteome; Repeat; RNA-binding;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 644 Zinc finger protein 74.
FT /FTId=PRO_0000047383.
FT DOMAIN 43 114 KRAB. {ECO:0000255|PROSITE-
FT ProRule:PRU00119}.
FT ZN_FING 248 270 C2H2-type 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 276 298 C2H2-type 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 304 326 C2H2-type 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 332 354 C2H2-type 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 360 382 C2H2-type 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 388 410 C2H2-type 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 416 438 C2H2-type 7. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 444 466 C2H2-type 8. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 472 494 C2H2-type 9. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 500 522 C2H2-type 10. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 528 550 C2H2-type 11. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 556 578 C2H2-type 12. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT VAR_SEQ 1 82 MEIPAPEPEKTALSSQDPALSLKENLEDISGWGLPEARSKE
FT SVSFKDVAVDFTQEEWGQLDSPQRALYRDVMLENYQNLLAL
FT -> MPSPPFSPRA (in isoform 4).
FT {ECO:0000305}.
FT /FTId=VSP_006893.
FT VAR_SEQ 1 71 Missing (in isoform 1).
FT {ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8268910,
FT ECO:0000303|PubMed:8663113}.
FT /FTId=VSP_006891.
FT VAR_SEQ 12 178 ALSSQDPALSLKENLEDISGWGLPEARSKESVSFKDVAVDF
FT TQEEWGQLDSPQRALYRDVMLENYQNLLALGPPLHKPDVIS
FT HLERGEEPWSMQREVPRGPCPEWELKAVPSQQQGICKEEPA
FT QEPIMERPLGGAQAWGRQAGALQRSQAAPWAPAPAMVWDVP
FT VEE -> GIGEFQGCGCGLHPGGVGSTRLPSEGLVPGCDVG
FT ELPEPSCPRTSTAQARCDLSSGTRRGAMEHAEGSPQRALSR
FT MGAEGGALSTAGHLQRRTGPGAHHGAAPRRGAGVGAPGRCS
FT AEESGCALGARTCHGLGRPCRGIPPQVSPLRPATRSRGGTL
FT AGHTQERPGH (in isoform 5).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_045530.
FT VAR_SEQ 83 114 Missing (in isoform 3). {ECO:0000305}.
FT /FTId=VSP_006892.
FT VAR_SEQ 179 644 Missing (in isoform 5).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_045531.
FT VARIANT 117 117 E -> K (in dbSNP:rs3747076).
FT {ECO:0000269|PubMed:11705709,
FT ECO:0000269|PubMed:14702039}.
FT /FTId=VAR_012993.
FT VARIANT 623 624 KL -> NF.
FT /FTId=VAR_012994.
FT CONFLICT 171 171 V -> A (in Ref. 7; AAH13395).
FT {ECO:0000305}.
FT CONFLICT 517 517 V -> M (in Ref. 1; CAA63379, 2; CAA50632
FT and 4; AAF21777/AAF21778/AAF21779/
FT AAF21780). {ECO:0000305}.
FT CONFLICT 569 569 S -> P (in Ref. 5; BAH13068).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 276 298 ismart:ZnF_C2H2 [T]
FT MYHIT 502 522 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 248 270 ismart:ZnF_C2H2 [T]
FT MYHIT 416 443 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 278 298 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 332 354 ismart:ZnF_C2H2 [T]
FT MYHIT 304 331 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 528 550 ismart:ZnF_C2H2 [T]
FT MYHIT 388 410 ismart:ZnF_C2H2 [T]
FT MYHIT 530 550 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 306 326 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 474 494 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 558 578 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 500 522 ismart:ZnF_C2H2 [T]
FT MYHIT 43 103 ismart:KRAB [T]
FT MYHIT 248 275 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 472 494 ismart:ZnF_C2H2 [T]
FT MYHIT 500 527 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 304 326 ismart:ZnF_C2H2 [T]
FT MYHIT 418 438 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 556 583 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 276 303 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 250 270 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 388 415 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 472 499 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 446 466 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 390 410 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 360 387 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 362 382 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 528 555 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 334 354 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 444 466 ismart:ZnF_C2H2 [T]
FT MYHIT 360 382 ismart:ZnF_C2H2 [T]
FT MYHIT 332 359 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 43 114 iprf:KRAB [T]
FT MYHIT 42 83 ipfam:KRAB [T]
FT MYHIT 416 438 ismart:ZnF_C2H2 [T]
FT MYHIT 444 471 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 556 578 ismart:ZnF_C2H2 [T]
SQ SEQUENCE 644 AA; 72207 MW; 87E5AA122BBC82F1 CRC64;
MEIPAPEPEK TALSSQDPAL SLKENLEDIS GWGLPEARSK ESVSFKDVAV DFTQEEWGQL
DSPQRALYRD VMLENYQNLL ALGPPLHKPD VISHLERGEE PWSMQREVPR GPCPEWELKA
VPSQQQGICK EEPAQEPIME RPLGGAQAWG RQAGALQRSQ AAPWAPAPAM VWDVPVEEFP
LRCPLFAQQR VPEGGPLLDT RKNVQATEGR TKAPARLCAG ENASTPSEPE KFPQVRRQRG
AGAGEGEFVC GECGKAFRQS SSLTLHRRWH SREKAYKCDE CGKAFTWSTN LLEHRRIHTG
EKPFFCGECG KAFSCHSSLN VHQRIHTGER PYKCSACEKA FSCSSLLSMH LRVHTGEKPY
RCGECGKAFN QRTHLTRHHR IHTGEKPYQC GSCGKAFTCH SSLTVHEKIH SGDKPFKCSD
CEKAFNSRSR LTLHQRTHTG EKPFKCADCG KGFSCHAYLL VHRRIHSGEK PFKCNECGKA
FSSHAYLIVH RRIHTGEKPF DCSQCWKAFS CHSSLIVHQR IHTGEKPYKC SECGRAFSQN
HCLIKHQKIH SGEKSFKCEK CGEMFNWSSH LTEHQRLHSE GKPLAIQFNK HLLSTYYVPG
SLLGAGDAGL RDVDPIDALD VAKLLCVVPP RAGRNFSLGS KPRN
//
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