Z780A_HUMAN
ID Z780A_HUMAN Reviewed; 641 AA.
AC O75290; E9PB48; Q6ZN87;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger protein 780A;
GN Name=ZNF780A;
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=Esophagus, and Tongue;
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).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- INTERACTION:
CC O75290; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-13335739, EBI-725997;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75290-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75290-2; Sequence=VSP_037718, VSP_037719, VSP_037720;
CC Name=3;
CC IsoId=O75290-3; Sequence=VSP_046465;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC34327.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK091274; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK131328; BAD18488.1; -; mRNA.
DR EMBL; AC005614; AAC34327.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS33026.2; -. [O75290-1]
DR CCDS; CCDS46078.1; -. [O75290-2]
DR CCDS; CCDS46079.1; -. [O75290-3]
DR RefSeq; NP_001010880.2; NM_001010880.2. [O75290-1]
DR RefSeq; NP_001136050.1; NM_001142578.1. [O75290-1]
DR RefSeq; NP_001136051.1; NM_001142579.1. [O75290-2]
DR RefSeq; XP_005258830.1; XM_005258773.2. [O75290-3]
DR RefSeq; XP_006723213.1; XM_006723150.3. [O75290-3]
DR RefSeq; XP_011525073.1; XM_011526771.2. [O75290-3]
DR RefSeq; XP_011525074.1; XM_011526772.2. [O75290-3]
DR RefSeq; XP_016882106.1; XM_017026617.1.
DR RefSeq; XP_016882107.1; XM_017026618.1. [O75290-1]
DR RefSeq; XP_016882108.1; XM_017026619.1. [O75290-1]
DR AlphaFoldDB; O75290; -.
DR SMR; O75290; -.
DR BioGRID; 129827; 26.
DR IntAct; O75290; 5.
DR STRING; 9606.ENSP00000400997; -.
DR iPTMnet; O75290; -.
DR PhosphoSitePlus; O75290; -.
DR BioMuta; ZNF780A; -.
DR jPOST; O75290; -.
DR MassIVE; O75290; -.
DR MaxQB; O75290; -.
DR PaxDb; O75290; -.
DR PeptideAtlas; O75290; -.
DR PRIDE; O75290; -.
DR ProteomicsDB; 19143; -.
DR ProteomicsDB; 49876; -. [O75290-1]
DR Antibodypedia; 30462; 88 antibodies from 13 providers.
DR DNASU; 284323; -.
DR Ensembl; ENST00000340963.9; ENSP00000341507.5; ENSG00000197782.15. [O75290-1]
DR Ensembl; ENST00000414720.6; ENSP00000416294.1; ENSG00000197782.15. [O75290-2]
DR Ensembl; ENST00000455521.5; ENSP00000400997.1; ENSG00000197782.15. [O75290-3]
DR Ensembl; ENST00000594395.5; ENSP00000469786.1; ENSG00000197782.15. [O75290-3]
DR Ensembl; ENST00000595687.6; ENSP00000472189.1; ENSG00000197782.15. [O75290-1]
DR Ensembl; ENST00000626168.2; ENSP00000487366.1; ENSG00000280568.2. [O75290-3]
DR Ensembl; ENST00000626829.2; ENSP00000487177.1; ENSG00000280568.2. [O75290-1]
DR Ensembl; ENST00000628273.2; ENSP00000487520.1; ENSG00000280568.2. [O75290-1]
DR Ensembl; ENST00000630440.2; ENSP00000486672.1; ENSG00000280568.2. [O75290-2]
DR Ensembl; ENST00000630528.2; ENSP00000486345.1; ENSG00000280568.2. [O75290-3]
DR Ensembl; ENST00000683561.1; ENSP00000506741.1; ENSG00000197782.15. [O75290-1]
DR GeneID; 284323; -.
DR KEGG; hsa:284323; -.
DR MANE-Select; ENST00000683561.1; ENSP00000506741.1; NM_001142578.2; NP_001136050.1.
DR UCSC; uc002omw.5; human. [O75290-1]
DR CTD; 284323; -.
DR GeneCards; ZNF780A; -.
DR HGNC; HGNC:27603; ZNF780A.
DR HPA; ENSG00000197782; Low tissue specificity.
DR neXtProt; NX_O75290; -.
DR OpenTargets; ENSG00000197782; -.
DR PharmGKB; PA162410417; -.
DR VEuPathDB; HostDB:ENSG00000197782; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162062; -.
DR HOGENOM; CLU_002678_17_1_1; -.
DR InParanoid; O75290; -.
DR OMA; YSEYGRF; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O75290; -.
DR TreeFam; TF341817; -.
DR PathwayCommons; O75290; -.
DR SignaLink; O75290; -.
DR BioGRID-ORCS; 284323; 19 hits in 1033 CRISPR screens.
DR ChiTaRS; ZNF780A; human.
DR GenomeRNAi; 284323; -.
DR Pharos; O75290; Tdark.
DR PRO; PR:O75290; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75290; protein.
DR Bgee; ENSG00000197782; Expressed in monocyte and 105 other tissues.
DR ExpressionAtlas; O75290; baseline and differential.
DR Genevisible; O75290; 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: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; 14.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 17.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 9.
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..641
FT /note="Zinc finger protein 780A"
FT /id="PRO_0000263690"
FT DOMAIN 6..77
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 165..187
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 193..215
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 221..243
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 249..271
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 277..299
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 305..327
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 333..355
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 361..383
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 389..411
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 417..439
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 445..467
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 473..495
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 501..523
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 529..551
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 557..579
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 585..607
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 613..635
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VAR_SEQ 1
FT /note="M -> MGRSPRKIDQFCNSSNM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037718"
FT VAR_SEQ 45
FT /note="L -> LA (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_046465"
FT VAR_SEQ 103..141
FT /note="VIKQISTTLGIEAFYFRNDSEYRQFEGLQGYQEGNINQK -> ISSLASKPS
FT FTAIHIQRRIHCRICIAFGYLSLVYCSLEIL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037719"
FT VAR_SEQ 142..641
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037720"
FT CONFLICT 104
FT /note="I -> L (in Ref. 1; AK091274)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 74531 MW; FE92AF740839A86D CRC64;
MVHGSVTFRD VAIDFSQEEW ECLQPDQRTL YRDVMLENYS HLISLGSSIS KPDVITLLEQ
EKEPWMVVRK ETSRRYPDLE LKYGPEKVSP ENDTSEVNLP KQVIKQISTT LGIEAFYFRN
DSEYRQFEGL QGYQEGNINQ KMISYEKLPT HTPHASLICN THKPYECKEC GKYFSRSANL
IQHQSIHTGE KPFECKECGK AFRLHIQFTR HQKFHTGEKP FECNECGKAF SLLTLLNRHK
NIHTGEKLFE CKECGKSFNR SSNLVQHQSI HSGVKPYECK ECGKGFNRGA HLIQHQKIHS
NEKPFVCKEC GMAFRYHYQL IEHCQIHTGE KPFECKECGK AFTLLTKLVR HQKIHTGEKP
FECRECGKAF SLLNQLNRHK NIHTGEKPFE CKECGKSFNR SSNLVQHQSI HAGIKPYECK
ECGKGFNRGA HLIQHQKIHS NEKPFVCREC EMAFRYHCQL IEHSRIHTGD KPFECQDCGK
AFNRGSSLVQ HQSIHTGEKP YECKECGKAF RLYLQLSQHQ KTHTGEKPFE CKECGKFFRR
GSNLNQHRSI HTGKKPFECK ECGKAFRLHM HLIRHQKLHT GEKPFECKEC GKAFRLHMQL
IRHQKLHTGE KPFECKECGK VFSLPTQLNR HKNIHTGEKA S
