ZSC10_HUMAN
ID ZSC10_HUMAN Reviewed; 725 AA.
AC Q96SZ4; B3KQD3; H0YFS6; Q1WWM2;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 10;
DE AltName: Full=Zinc finger protein 206;
GN Name=ZSCAN10; Synonyms=ZNF206;
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=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 SER-107; SER-153 AND THR-213, 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 [5]
RP METHYLATION AT GLN-428, AND MUTAGENESIS OF GLN-428.
RX PubMed=26797129; DOI=10.1074/jbc.m115.711952;
RA Kusevic D., Kudithipudi S., Jeltsch A.;
RT "Substrate specificity of the HEMK2 protein glutamine methyltransferase and
RT identification of novel substrates.";
RL J. Biol. Chem. 291:6124-6133(2016).
CC -!- FUNCTION: Embryonic stem (ES) cell-specific transcription factor
CC required to maintain ES cell pluripotency. Can both activate and /or
CC repress expression of target genes, depending on the context.
CC Specifically binds the 5'-[GA]CGCNNGCG[CT]-3' DNA consensus sequence.
CC Regulates expression of POU5F1/OCT4, ZSCAN4 and ALYREF/THOC4.
CC {ECO:0000250|UniProtKB:Q3URR7}.
CC -!- SUBUNIT: Interacts with POU5F1/OCT4 and SOX2.
CC {ECO:0000250|UniProtKB:Q3URR7}.
CC -!- INTERACTION:
CC Q96SZ4; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-14934888, EBI-10172290;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96SZ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96SZ4-2; Sequence=VSP_039221;
CC Name=3;
CC IsoId=Q96SZ4-3; Sequence=VSP_054601, VSP_054602;
CC -!- PTM: Methylated at Gln-428 by N6AMT1. {ECO:0000269|PubMed:26797129}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI14453.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AK027455; BAB55124.1; -; mRNA.
DR EMBL; AK074736; BAG51995.1; -; mRNA.
DR EMBL; AC108134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC114452; AAI14453.1; ALT_INIT; mRNA.
DR CCDS; CCDS61813.1; -. [Q96SZ4-2]
DR CCDS; CCDS61814.1; -. [Q96SZ4-3]
DR RefSeq; NP_001269344.1; NM_001282415.1. [Q96SZ4-2]
DR RefSeq; NP_001269345.1; NM_001282416.1. [Q96SZ4-3]
DR RefSeq; NP_116194.2; NM_032805.2.
DR AlphaFoldDB; Q96SZ4; -.
DR SMR; Q96SZ4; -.
DR BioGRID; 124331; 3.
DR IntAct; Q96SZ4; 1.
DR STRING; 9606.ENSP00000252463; -.
DR GlyGen; Q96SZ4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96SZ4; -.
DR PhosphoSitePlus; Q96SZ4; -.
DR BioMuta; ZSCAN10; -.
DR DMDM; 55976759; -.
DR EPD; Q96SZ4; -.
DR jPOST; Q96SZ4; -.
DR MassIVE; Q96SZ4; -.
DR PaxDb; Q96SZ4; -.
DR PeptideAtlas; Q96SZ4; -.
DR PRIDE; Q96SZ4; -.
DR ProteomicsDB; 38166; -.
DR ProteomicsDB; 78162; -. [Q96SZ4-1]
DR ProteomicsDB; 78163; -. [Q96SZ4-2]
DR Antibodypedia; 58023; 28 antibodies from 11 providers.
DR DNASU; 84891; -.
DR Ensembl; ENST00000252463.6; ENSP00000252463.2; ENSG00000130182.8. [Q96SZ4-1]
DR Ensembl; ENST00000538082.5; ENSP00000440047.2; ENSG00000130182.8. [Q96SZ4-3]
DR Ensembl; ENST00000575108.5; ENSP00000459520.1; ENSG00000130182.8. [Q96SZ4-2]
DR GeneID; 84891; -.
DR KEGG; hsa:84891; -.
DR UCSC; uc002ctv.3; human. [Q96SZ4-1]
DR CTD; 84891; -.
DR DisGeNET; 84891; -.
DR GeneCards; ZSCAN10; -.
DR HGNC; HGNC:12997; ZSCAN10.
DR HPA; ENSG00000130182; Tissue enriched (brain).
DR MIM; 618365; gene.
DR neXtProt; NX_Q96SZ4; -.
DR OpenTargets; ENSG00000130182; -.
DR PharmGKB; PA162410957; -.
DR VEuPathDB; HostDB:ENSG00000130182; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162513; -.
DR HOGENOM; CLU_002678_63_1_1; -.
DR InParanoid; Q96SZ4; -.
DR PhylomeDB; Q96SZ4; -.
DR TreeFam; TF338010; -.
DR PathwayCommons; Q96SZ4; -.
DR Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
DR SignaLink; Q96SZ4; -.
DR BioGRID-ORCS; 84891; 14 hits in 1091 CRISPR screens.
DR ChiTaRS; ZSCAN10; human.
DR GenomeRNAi; 84891; -.
DR Pharos; Q96SZ4; Tdark.
DR PRO; PR:Q96SZ4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96SZ4; protein.
DR Bgee; ENSG00000130182; Expressed in bone marrow cell and 64 other tissues.
DR ExpressionAtlas; Q96SZ4; baseline and differential.
DR Genevisible; Q96SZ4; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
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:0043565; F:sequence-specific DNA binding; 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 Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 11.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..725
FT /note="Zinc finger and SCAN domain-containing protein 10"
FT /id="PRO_0000047452"
FT DOMAIN 1..71
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 292..315
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 321..343
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 349..371
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 377..399
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 421..443
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 467..489
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 523..545
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 551..573
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 579..601
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 607..629
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 635..657
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 669..691
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 697..719
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 98..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 428
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000269|PubMed:26797129"
FT VAR_SEQ 1..339
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039221"
FT VAR_SEQ 1..85
FT /note="MGPRASLSRLRELCGHWLRPALHTKKQILELLVLEQFLSVLPPHLLGRLQGQ
FT PLRDGEEVVLLLEGIHREPSHAGPLDFSCNAGK -> MLPVSGGHGATGVPEPAPGALR
FT PLAAAGSAHQETDPGAAGAGAVPECAASAPPGPPAGAAAQGWGGGGAAARGHPPGAQPR
FT GAAG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054601"
FT VAR_SEQ 86..167
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054602"
FT MUTAGEN 428
FT /note="Q->R: Abolishes methylation by N6AMT1."
FT /evidence="ECO:0000269|PubMed:26797129"
SQ SEQUENCE 725 AA; 80387 MW; 046163DA13669F12 CRC64;
MGPRASLSRL RELCGHWLRP ALHTKKQILE LLVLEQFLSV LPPHLLGRLQ GQPLRDGEEV
VLLLEGIHRE PSHAGPLDFS CNAGKSCPRA DVTLEEKGCA SQVPSHSPKK ELPAEEPSVL
GPSDEPPRPQ PRAAQPAEPG QWRLPPSSKQ PLSPGPQKTF QALQESSPQG PSPWPEESSR
DQELAAVLEC LTFEDVPENK AWPAHPLGFG SRTPDKEEFK QEEPKGAAWP TPILAESQAD
SPGVPGEPCA QSLGRGAAAS GPGEDGSLLG SSEILEVKVA EGVPEPNPEL QFICADCGVS
FPQLSRLKAH QLRSHPAGRS FLCLCCGKSF GRSSILKLHM RTHTDERPHA CHLCGHRFRQ
SSHLSKHLLT HSSEPAFLCA ECGRGFQRRA SLVQHLLAHA QDQKPPCAPE SKAEAPPLTD
VLCSHCGQSF QRRSSLKRHL RIHARDKDRR SSEGSGSRRR DSDRRPFVCS DCGKAFRRSE
HLVAHRRVHT GERPFSCQAC GRSFTQSSQL VSHQRVHTGE KPYACPQCGK RFVRRASLAR
HLLTHGGPRP HHCTQCGKSF GQTQDLARHQ RSHTGEKPCR CSECGEGFSQ SAHLARHQRI
HTGEKPHACD TCGHRFRNSS NLARHRRSHT GERPYSCQTC GRSFRRNAHL RRHLATHAEP
GQEQAEPPQE CVECGKSFSR SCNLLRHLLV HTGARPYSCT QCGRSFSRNS HLLRHLRTHA
RETLY
