ZN791_HUMAN
ID ZN791_HUMAN Reviewed; 576 AA.
AC Q3KP31; B7Z586; Q8NC99;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Zinc finger protein 791;
GN Name=ZNF791;
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 1 AND 2).
RC TISSUE=Teratocarcinoma;
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).
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.
CC -!- INTERACTION:
CC Q3KP31; P28799: GRN; NbExp=3; IntAct=EBI-2849119, EBI-747754;
CC Q3KP31; O76024: WFS1; NbExp=3; IntAct=EBI-2849119, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3KP31-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3KP31-2; Sequence=VSP_056674;
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; AK074877; BAC11261.1; -; mRNA.
DR EMBL; AK298597; BAH12822.1; -; mRNA.
DR EMBL; CH471106; EAW84278.1; -; Genomic_DNA.
DR EMBL; BC106937; AAI06938.1; -; mRNA.
DR EMBL; BC106938; AAI06939.1; -; mRNA.
DR CCDS; CCDS12273.1; -. [Q3KP31-1]
DR RefSeq; NP_699189.2; NM_153358.2. [Q3KP31-1]
DR RefSeq; XP_016881901.1; XM_017026412.1. [Q3KP31-2]
DR AlphaFoldDB; Q3KP31; -.
DR SMR; Q3KP31; -.
DR BioGRID; 127843; 24.
DR IntAct; Q3KP31; 6.
DR STRING; 9606.ENSP00000342974; -.
DR iPTMnet; Q3KP31; -.
DR PhosphoSitePlus; Q3KP31; -.
DR BioMuta; ZNF791; -.
DR DMDM; 121942546; -.
DR EPD; Q3KP31; -.
DR jPOST; Q3KP31; -.
DR MassIVE; Q3KP31; -.
DR MaxQB; Q3KP31; -.
DR PaxDb; Q3KP31; -.
DR PeptideAtlas; Q3KP31; -.
DR PRIDE; Q3KP31; -.
DR ProteomicsDB; 61711; -. [Q3KP31-1]
DR ProteomicsDB; 6665; -.
DR Antibodypedia; 26057; 99 antibodies from 16 providers.
DR DNASU; 163049; -.
DR Ensembl; ENST00000343325.9; ENSP00000342974.4; ENSG00000173875.14. [Q3KP31-1]
DR GeneID; 163049; -.
DR KEGG; hsa:163049; -.
DR MANE-Select; ENST00000343325.9; ENSP00000342974.4; NM_153358.3; NP_699189.2.
DR UCSC; uc002mua.3; human. [Q3KP31-1]
DR CTD; 163049; -.
DR DisGeNET; 163049; -.
DR GeneCards; ZNF791; -.
DR HGNC; HGNC:26895; ZNF791.
DR HPA; ENSG00000173875; Low tissue specificity.
DR neXtProt; NX_Q3KP31; -.
DR OpenTargets; ENSG00000173875; -.
DR PharmGKB; PA162410522; -.
DR VEuPathDB; HostDB:ENSG00000173875; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00950000182755; -.
DR HOGENOM; CLU_002678_44_17_1; -.
DR InParanoid; Q3KP31; -.
DR OMA; IRIHKRT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q3KP31; -.
DR TreeFam; TF338854; -.
DR PathwayCommons; Q3KP31; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q3KP31; -.
DR BioGRID-ORCS; 163049; 14 hits in 1095 CRISPR screens.
DR ChiTaRS; ZNF791; human.
DR GenomeRNAi; 163049; -.
DR Pharos; Q3KP31; Tdark.
DR PRO; PR:Q3KP31; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q3KP31; protein.
DR Bgee; ENSG00000173875; Expressed in nipple and 191 other tissues.
DR ExpressionAtlas; Q3KP31; baseline and differential.
DR Genevisible; Q3KP31; 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:0000977; F:RNA polymerase II transcription 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 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; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 17.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 17.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 17.
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..576
FT /note="Zinc finger protein 791"
FT /id="PRO_0000311799"
FT DOMAIN 4..90
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 100..122
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 132..154
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 160..182
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 188..210
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 216..238
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..266
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 272..294
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..322
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 468..490
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 524..546
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 552..574
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056674"
FT CONFLICT 177
FT /note="R -> S (in Ref. 1; BAC11261)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 66872 MW; 5F6FD2569DAABD43 CRC64;
MDSVAFEDVS VSFSQEEWAL LAPSQKKLYR DVMQETFKNL ASIGEKWEDP NVEDQHKNQG
RNLRSHTGER LCEGKEGSQC AENFSPNLSV TKKTAGVKPY ECTICGKAFM RLSSLTRHMR
SHTGYELFEK PYKCKECEKA FSYLKSFQRH ERSHTGEKPY KCKQCGKTFI YHQPFQRHER
THIGEKPYEC KQCGKALSCS SSLRVHERIH TGEKPYECKQ CGKAFSCSSS IRVHERTHTG
EKPYACKECG KAFISHTSVL THMITHNGDR PYKCKECGKA FIFPSFLRVH ERIHTGEKPY
KCKQCGKAFR CSTSIQIHER IHTGEKPYKC KECGKSFSAR PAFRVHVRVH TGEKPYKCKE
CGKAFSRISY FRIHERTHTG EKPYECKKCG KTFNYPLDLK IHKRNHTGEK PYECKECAKT
FISLENFRRH MITHTGDGPY KCRDCGKVFI FPSALRTHER THTGEKPYEC KQCGKAFSCS
SYIRIHKRTH TGEKPYECKE CGKAFIYPTS FQGHMRMHTG EKPYKCKECG KAFSLHSSFQ
RHTRIHNYEK PLECKQCGKA FSVSTSLKKH MRMHNR
