ZN787_HUMAN
ID ZN787_HUMAN Reviewed; 382 AA.
AC Q6DD87; A0A087WUD1; O00455;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Zinc finger protein 787;
DE AltName: Full=TTF-I-interacting peptide 20;
GN Name=ZNF787;
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].
RC TISSUE=Lung;
RA Jansa P., Grummt I.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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 MRNA].
RC TISSUE=Pancreas;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-191 AND LYS-211, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB58413.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF000560; AAB58413.1; ALT_INIT; mRNA.
DR EMBL; AC024580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF573663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC077728; AAH77728.1; -; mRNA.
DR CCDS; CCDS42634.1; -.
DR RefSeq; NP_001002836.2; NM_001002836.3.
DR RefSeq; XP_011524747.1; XM_011526445.2.
DR AlphaFoldDB; Q6DD87; -.
DR SMR; Q6DD87; -.
DR BioGRID; 125966; 61.
DR IntAct; Q6DD87; 5.
DR MINT; Q6DD87; -.
DR STRING; 9606.ENSP00000478557; -.
DR iPTMnet; Q6DD87; -.
DR PhosphoSitePlus; Q6DD87; -.
DR BioMuta; ZNF787; -.
DR DMDM; 527504074; -.
DR EPD; Q6DD87; -.
DR jPOST; Q6DD87; -.
DR MassIVE; Q6DD87; -.
DR PaxDb; Q6DD87; -.
DR PeptideAtlas; Q6DD87; -.
DR PRIDE; Q6DD87; -.
DR ProteomicsDB; 66222; -.
DR Antibodypedia; 33179; 88 antibodies from 16 providers.
DR DNASU; 126208; -.
DR Ensembl; ENST00000610935.2; ENSP00000478557.1; ENSG00000142409.6.
DR GeneID; 126208; -.
DR KEGG; hsa:126208; -.
DR MANE-Select; ENST00000610935.2; ENSP00000478557.1; NM_001002836.4; NP_001002836.2.
DR CTD; 126208; -.
DR DisGeNET; 126208; -.
DR GeneCards; ZNF787; -.
DR HGNC; HGNC:26998; ZNF787.
DR HPA; ENSG00000142409; Low tissue specificity.
DR neXtProt; NX_Q6DD87; -.
DR OpenTargets; ENSG00000142409; -.
DR PharmGKB; PA162410481; -.
DR VEuPathDB; HostDB:ENSG00000142409; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163064; -.
DR InParanoid; Q6DD87; -.
DR OMA; PKPYVCM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6DD87; -.
DR TreeFam; TF337689; -.
DR PathwayCommons; Q6DD87; -.
DR SignaLink; Q6DD87; -.
DR BioGRID-ORCS; 126208; 23 hits in 1102 CRISPR screens.
DR ChiTaRS; ZNF787; human.
DR GenomeRNAi; 126208; -.
DR Pharos; Q6DD87; Tdark.
DR PRO; PR:Q6DD87; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6DD87; protein.
DR Bgee; ENSG00000142409; Expressed in hindlimb stylopod muscle and 159 other tissues.
DR ExpressionAtlas; Q6DD87; baseline and differential.
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:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..381
FT /note="Zinc finger protein 787"
FT /id="PRO_0000287606"
FT ZN_FING 66..88
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 94..116
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 122..144
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 150..172
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 178..200
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 280..303
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 317..339
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 122
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 379
FT /note="G -> A (in dbSNP:rs4077285)"
FT /id="VAR_032336"
FT CONFLICT 363
FT /note="D -> DD (in Ref. 2; AC024580)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="G -> A (in Ref. 1; AAB58413 and 3; AAH77728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 40428 MW; E34481D98570C2A5 CRC64;
MELREEAWSP GPLDSEDQQM ASHENPVDIL IMDDDDVPSW PPTKLSPPQS APPAGPPPRP
RPPAPYICNE CGKSFSHWSK LTRHQRTHTG ERPNACADCG KTFSQSSHLV QHRRIHTGEK
PYACLECGKR FSWSSNLMQH QRIHTGEKPY TCPDCGRSFT QSKSLAKHRR SHSGLKPFVC
PRCGRGFSQP KSLARHLRLH PELSGPGVAA KVLAASVRRA KGPEEAVAAD GEIAIPVGDG
EGIIVVGAPG EGAAAAAAMA GAGAKAAGPR SRRAPAPKPY VCLECGKGFG HGAGLLAHQR
AQHGDGLGAA GGEEPAHICV ECGEGFVQGA ALRRHKKIHA VGAPSVCSSC GQSYYRAGGE
EEDDDDEAAG GRCPECRGGE GR
