ZN768_HUMAN
ID ZN768_HUMAN Reviewed; 540 AA.
AC Q9H5H4; Q569L7; Q96CX4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Zinc finger protein 768;
GN Name=ZNF768;
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], AND VARIANT ASP-181.
RC TISSUE=Ovary, and PNS;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-540.
RC TISSUE=Epithelium;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-83, AND
RP IDENTIFICATION BY 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-90 AND SER-97, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-90; SER-97; SER-125;
RP SER-132; SER-139 AND SER-160, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q9H5H4; P49760: CLK2; NbExp=3; IntAct=EBI-1210580, EBI-750020;
CC Q9H5H4; O95967: EFEMP2; NbExp=3; IntAct=EBI-1210580, EBI-743414;
CC Q9H5H4; Q92979: EMG1; NbExp=3; IntAct=EBI-1210580, EBI-718638;
CC Q9H5H4; Q13526: PIN1; NbExp=5; IntAct=EBI-1210580, EBI-714158;
CC Q9H5H4; O00560: SDCBP; NbExp=3; IntAct=EBI-1210580, EBI-727004;
CC Q9H5H4; P15622-3: ZNF250; NbExp=3; IntAct=EBI-1210580, EBI-10177272;
CC Q9H5H4; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-1210580, EBI-373456;
CC Q9H5H4; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-1210580, EBI-740727;
CC Q9H5H4; Q5T619: ZNF648; NbExp=3; IntAct=EBI-1210580, EBI-11985915;
CC Q9H5H4; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-1210580, EBI-5667516;
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=AAH13760.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH92403.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15652.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC013760; AAH13760.1; ALT_INIT; mRNA.
DR EMBL; BC092403; AAH92403.2; ALT_INIT; mRNA.
DR EMBL; AK027089; BAB15652.1; ALT_INIT; mRNA.
DR CCDS; CCDS10681.2; -.
DR RefSeq; NP_078947.3; NM_024671.3.
DR AlphaFoldDB; Q9H5H4; -.
DR SMR; Q9H5H4; -.
DR BioGRID; 122839; 171.
DR IntAct; Q9H5H4; 41.
DR MINT; Q9H5H4; -.
DR STRING; 9606.ENSP00000369777; -.
DR iPTMnet; Q9H5H4; -.
DR PhosphoSitePlus; Q9H5H4; -.
DR BioMuta; ZNF768; -.
DR DMDM; 158564024; -.
DR EPD; Q9H5H4; -.
DR jPOST; Q9H5H4; -.
DR MassIVE; Q9H5H4; -.
DR MaxQB; Q9H5H4; -.
DR PaxDb; Q9H5H4; -.
DR PeptideAtlas; Q9H5H4; -.
DR PRIDE; Q9H5H4; -.
DR ProteomicsDB; 80905; -.
DR Antibodypedia; 13715; 138 antibodies from 19 providers.
DR DNASU; 79724; -.
DR Ensembl; ENST00000380412.7; ENSP00000369777.5; ENSG00000169957.10.
DR GeneID; 79724; -.
DR KEGG; hsa:79724; -.
DR MANE-Select; ENST00000380412.7; ENSP00000369777.5; NM_024671.4; NP_078947.3.
DR UCSC; uc002dyk.4; human.
DR CTD; 79724; -.
DR GeneCards; ZNF768; -.
DR HGNC; HGNC:26273; ZNF768.
DR HPA; ENSG00000169957; Low tissue specificity.
DR MIM; 618032; gene.
DR neXtProt; NX_Q9H5H4; -.
DR OpenTargets; ENSG00000169957; -.
DR PharmGKB; PA162410327; -.
DR VEuPathDB; HostDB:ENSG00000169957; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162267; -.
DR InParanoid; Q9H5H4; -.
DR OMA; FEPQNPE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9H5H4; -.
DR TreeFam; TF350793; -.
DR PathwayCommons; Q9H5H4; -.
DR SignaLink; Q9H5H4; -.
DR BioGRID-ORCS; 79724; 9 hits in 1103 CRISPR screens.
DR ChiTaRS; ZNF768; human.
DR GenomeRNAi; 79724; -.
DR Pharos; Q9H5H4; Tdark.
DR PRO; PR:Q9H5H4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9H5H4; protein.
DR Bgee; ENSG00000169957; Expressed in apex of heart and 201 other tissues.
DR ExpressionAtlas; Q9H5H4; baseline and differential.
DR Genevisible; Q9H5H4; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0003723; F:RNA binding; HDA:UniProtKB.
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 GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 4.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..540
FT /note="Zinc finger protein 768"
FT /id="PRO_0000304408"
FT ZN_FING 261..283
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..311
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 317..339
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 345..367
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 373..395
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 401..423
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 429..451
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 457..479
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 485..507
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 513..535
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0T2"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0T2"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0T2"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 181
FT /note="E -> D (in dbSNP:rs10871453)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035024"
FT VARIANT 488
FT /note="A -> S (in dbSNP:rs3751848)"
FT /id="VAR_052900"
SQ SEQUENCE 540 AA; 60229 MW; 7E9299F7C1BEE866 CRC64;
MEREALPWGL EPQDVQSSDE MRSPEGYLRG NMSENEEEEI SQQEGSGDYE VEEIPFGLEP
QSPGFEPQSP EFEPQSPRFE PESPGFESRS PGLVPPSPEF APRSPESDSQ SPEFESQSPR
YEPQSPGYEP RSPGYEPRSP GYESESSRYE SQNTELKTQS PEFEAQSSKF QEGAEMLLNP
EEKSPLNISV GVHPLDSFTQ GFGEQPTGDL PIGPPFEMPT GALLSTPQFE MLQNPLGLTG
ALRGPGRRGG RARGGQGPRP NICGICGKSF GRGSTLIQHQ RIHTGEKPYK CEVCSKAFSQ
SSDLIKHQRT HTGERPYKCP RCGKAFADSS YLLRHQRTHS GQKPYKCPHC GKAFGDSSYL
LRHQRTHSHE RPYSCTECGK CYSQNSSLRS HQRVHTGQRP FSCGICGKSF SQRSALIPHA
RSHAREKPFK CPECGKRFGQ SSVLAIHART HLPGRTYSCP DCGKTFNRSS TLIQHQRSHT
GERPYRCAVC GKGFCRSSTL LQHHRVHSGE RPYKCDDCGK AFSQSSDLIR HQRTHAAGRR
