ZN568_HUMAN
ID ZN568_HUMAN Reviewed; 644 AA.
AC Q3ZCX4; B4DS92; E7ER33; Q6N060; Q8NA64;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Zinc finger protein 568;
GN Name=ZNF568;
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] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-594 (ISOFORM 2).
RC TISSUE=Brain, and Testis;
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 MRNA] (ISOFORM 2).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-401 (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP POLYMORPHISM.
RX PubMed=23071813; DOI=10.1371/journal.pone.0047481;
RA Chien H.C., Wang H.Y., Su Y.N., Lai K.Y., Lu L.C., Chen P.C., Tsai S.F.,
RA Wu C.I., Hsieh W.S., Shen C.K.;
RT "Targeted disruption in mice of a neural stem cell-maintaining, KRAB-Zn
RT finger-encoding gene that has rapidly evolved in the human lineage.";
RL PLoS ONE 7:E47481-E47481(2012).
CC -!- FUNCTION: Has transcriptional repression activity, partially through
CC the recruitment of the corepressor TRIM28 but has also repression
CC activity independently of this interaction. Essential during embryonic
CC development, where it acts as direct repressor of a placental-specific
CC transcript of IGF2 in early development and regulates convergent
CC extension movements required for axis elongation and tissue
CC morphogenesis in all germ layers. Also important for normal
CC morphogenesis of extraembryonic tissues including the yolk sac,
CC extraembryonic mesoderm and placenta. May enhance proliferation or
CC maintenance of neural stem cells. {ECO:0000250|UniProtKB:E9PYI1}.
CC -!- SUBUNIT: Interacts with TRIM28. {ECO:0000250|UniProtKB:E9PYI1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:E9PYI1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3ZCX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3ZCX4-2; Sequence=VSP_028556;
CC Name=3;
CC IsoId=Q3ZCX4-3; Sequence=VSP_028556, VSP_046815;
CC -!- POLYMORPHISM: Isoform 3 is highly polymorphic with three major alleles:
CC H, C1 and C1. The H allele is found at higher frequencies in Japanese
CC (0.71) and Taiwan Chinese (0.72) populations compared to European
CC (0.45) and African (0.39) populations. The H allele may be associated
CC with smaller head size in infants. {ECO:0000269|PubMed:23071813}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31218.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH31218.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=CAE45810.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK093123; BAC04064.1; -; mRNA.
DR EMBL; AK299626; BAG61554.1; -; mRNA.
DR EMBL; BX640681; CAE45810.1; ALT_FRAME; mRNA.
DR EMBL; AC008733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031218; AAH31218.1; ALT_SEQ; mRNA.
DR CCDS; CCDS42558.1; -. [Q3ZCX4-1]
DR CCDS; CCDS56092.1; -. [Q3ZCX4-2]
DR CCDS; CCDS56093.1; -. [Q3ZCX4-3]
DR RefSeq; NP_001191764.1; NM_001204835.1.
DR RefSeq; NP_001191765.1; NM_001204836.1. [Q3ZCX4-2]
DR RefSeq; NP_001191766.1; NM_001204837.1. [Q3ZCX4-2]
DR RefSeq; NP_001191767.1; NM_001204838.1.
DR RefSeq; NP_001191768.1; NM_001204839.1. [Q3ZCX4-3]
DR RefSeq; NP_940941.2; NM_198539.3. [Q3ZCX4-1]
DR RefSeq; XP_016882262.1; XM_017026773.1. [Q3ZCX4-2]
DR RefSeq; XP_016882263.1; XM_017026774.1. [Q3ZCX4-2]
DR RefSeq; XP_016882264.1; XM_017026775.1. [Q3ZCX4-3]
DR AlphaFoldDB; Q3ZCX4; -.
DR SMR; Q3ZCX4; -.
DR BioGRID; 131935; 7.
DR IntAct; Q3ZCX4; 1.
DR STRING; 9606.ENSP00000481819; -.
DR iPTMnet; Q3ZCX4; -.
DR PhosphoSitePlus; Q3ZCX4; -.
DR BioMuta; ZNF568; -.
DR DMDM; 158706494; -.
DR jPOST; Q3ZCX4; -.
DR MassIVE; Q3ZCX4; -.
DR MaxQB; Q3ZCX4; -.
DR PaxDb; Q3ZCX4; -.
DR PeptideAtlas; Q3ZCX4; -.
DR PRIDE; Q3ZCX4; -.
DR ProteomicsDB; 17705; -.
DR ProteomicsDB; 61920; -. [Q3ZCX4-1]
DR ProteomicsDB; 61921; -. [Q3ZCX4-2]
DR Antibodypedia; 29844; 124 antibodies from 15 providers.
DR DNASU; 374900; -.
DR Ensembl; ENST00000333987.12; ENSP00000334685.7; ENSG00000198453.14. [Q3ZCX4-1]
DR Ensembl; ENST00000415168.5; ENSP00000394514.1; ENSG00000198453.14. [Q3ZCX4-2]
DR Ensembl; ENST00000455427.6; ENSP00000413396.2; ENSG00000198453.14. [Q3ZCX4-3]
DR Ensembl; ENST00000619231.4; ENSP00000481819.1; ENSG00000198453.14. [Q3ZCX4-1]
DR GeneID; 374900; -.
DR KEGG; hsa:374900; -.
DR MANE-Select; ENST00000333987.12; ENSP00000334685.7; NM_198539.4; NP_940941.2.
DR UCSC; uc002ofc.4; human. [Q3ZCX4-1]
DR CTD; 374900; -.
DR DisGeNET; 374900; -.
DR GeneCards; ZNF568; -.
DR HGNC; HGNC:25392; ZNF568.
DR HPA; ENSG00000198453; Low tissue specificity.
DR MIM; 617566; gene.
DR neXtProt; NX_Q3ZCX4; -.
DR OpenTargets; ENSG00000198453; -.
DR PharmGKB; PA134893477; -.
DR VEuPathDB; HostDB:ENSG00000198453; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162857; -.
DR HOGENOM; CLU_002678_57_1_1; -.
DR InParanoid; Q3ZCX4; -.
DR OMA; HCSSHVV; -.
DR PhylomeDB; Q3ZCX4; -.
DR TreeFam; TF337898; -.
DR PathwayCommons; Q3ZCX4; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q3ZCX4; -.
DR BioGRID-ORCS; 374900; 12 hits in 1095 CRISPR screens.
DR ChiTaRS; ZNF568; human.
DR GenomeRNAi; 374900; -.
DR Pharos; Q3ZCX4; Tdark.
DR PRO; PR:Q3ZCX4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q3ZCX4; protein.
DR Bgee; ENSG00000198453; Expressed in calcaneal tendon and 134 other tissues.
DR ExpressionAtlas; Q3ZCX4; baseline and differential.
DR Genevisible; Q3ZCX4; 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:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0060669; P:embryonic placenta morphogenesis; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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; 15.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..644
FT /note="Zinc finger protein 568"
FT /id="PRO_0000306877"
FT DOMAIN 48..119
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 222..244
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 250..272
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 278..300
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 306..328
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..356
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..384
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 390..412
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 418..440
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 446..468
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 474..496
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 502..524
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 530..552
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 558..580
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 586..608
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 614..636
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VAR_SEQ 1..64
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_028556"
FT VAR_SEQ 121..644
FT /note="VWEVDEQIKKQQETLVRKVTSISKKILIKEKVIECKKVAKIFPLSSDIVTSR
FT QSFYDCDSLDKGLEHNLDLLRYEKGCVREKQSNEFGKPFYHCASYVVTPFKCNQCGQDF
FT SHKFDLIRHERIHAGEKPYECKECGKAFSRKENLITHQKIHTGEKPYKCNECGKAFIQM
FT SNLIRHHRIHTGEKPYACKDCWKAFSQKSNLIEHERIHTGEKPYECKECGKSFSQKQNL
FT IEHEKIHTGEKPYACNECGRAFSRMSSVTLHMRSHTGEKPYKCNKCGKAFSQCSVFIIH
FT MRSHTGEKPYVCSECGKAFSQSSSLTVHMRNHTAEKPYECKECGKAFSRKENLITHQKI
FT HTGEKPYECSECGKAFIQMSNLIRHQRIHTGEKPYACTVCGKAFSQKSNLTEHEKIHTG
FT EKPYHCNQCGKAFSQRQNLLEHEKIHTGEKPFKCNECGKAFSRISSLTLHVRSHTGEKP
FT YECNKCGKAFSQCSLLIIHMRSHTGEKPFECNECGKAFSQRASLSIHKRGHTGERHQVY
FT -> PRRGENCCASEVMAEGLKFKDVVIYFSQKEWECLHSAQKDLYRDVMLENYGNLVLL
FT GLSDTKPNVISLLEQKKEPWMVKRKETKEWCPDWEFGRETKNLSPKENIYEIRSPQQEK
FT ARVIREIRCQVERQQGHQEGHFRPAVIPFTSMQCTAHREYQWLHTGEKSCECRKCKNAF
FT RYQSCPIQHEIIHNKEKEPECGECRKIFNSGSDLIKHQTLHESKKHSENNKCAFNHDSG
FT ITQPQSINTGEKPHKCKECGKAFRSSSQISQHQRMHLGEKPYKCRECGKAFPSTAQLNL
FT HQRIHTDEKYYESKACGKAFTRPSHLFRHQRIHTGEKPHKCKECGKAFRYDTQLSLHQI
FT IHTGERRYECRECGKVYSCASQLSLHQRIHTGEKPHECKECGKAFISDSHLIRHQSVHT
FT GEKPCKCKECGKSFRRGSELTRHQRAHTGEKPYECKECEKAFTCSTELVRHQKVHTGER
FT PHKCKECGKAFIRRSELTHHERSHTGEKPYECKECGKPFGGGSELS (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046815"
FT VARIANT 437
FT /note="M -> T (in dbSNP:rs547483)"
FT /id="VAR_052867"
FT VARIANT 642
FT /note="Q -> R (in dbSNP:rs1644634)"
FT /id="VAR_052868"
FT CONFLICT 96
FT /note="V -> M (in Ref. 4; AAH31218)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="I -> V (in Ref. 2; CAE45810)"
FT /evidence="ECO:0000305"
FT CONFLICT Q3ZCX4-3:542
FT /note="L -> P (in Ref. 1; BAG61554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 644 AA; 74369 MW; CEEED67D5D8E7DA2 CRC64;
MTSQSSVISN SCVTMERLSH MMERKAWCSQ ESALSEEEED TTRPLETVTF KDVAVDLTQE
EWEQMKPAQR NLYRDVMLEN YSNLVTVGCQ VTKPDVIFKL EQEEEPWVME EEMFGRHCPE
VWEVDEQIKK QQETLVRKVT SISKKILIKE KVIECKKVAK IFPLSSDIVT SRQSFYDCDS
LDKGLEHNLD LLRYEKGCVR EKQSNEFGKP FYHCASYVVT PFKCNQCGQD FSHKFDLIRH
ERIHAGEKPY ECKECGKAFS RKENLITHQK IHTGEKPYKC NECGKAFIQM SNLIRHHRIH
TGEKPYACKD CWKAFSQKSN LIEHERIHTG EKPYECKECG KSFSQKQNLI EHEKIHTGEK
PYACNECGRA FSRMSSVTLH MRSHTGEKPY KCNKCGKAFS QCSVFIIHMR SHTGEKPYVC
SECGKAFSQS SSLTVHMRNH TAEKPYECKE CGKAFSRKEN LITHQKIHTG EKPYECSECG
KAFIQMSNLI RHQRIHTGEK PYACTVCGKA FSQKSNLTEH EKIHTGEKPY HCNQCGKAFS
QRQNLLEHEK IHTGEKPFKC NECGKAFSRI SSLTLHVRSH TGEKPYECNK CGKAFSQCSL
LIIHMRSHTG EKPFECNECG KAFSQRASLS IHKRGHTGER HQVY
