ZSC29_HUMAN
ID ZSC29_HUMAN Reviewed; 852 AA.
AC Q8IWY8; B3KVB9; Q32M75; Q32M76; Q8NA40;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 29;
DE AltName: Full=Zinc finger protein 690;
GN Name=ZSCAN29; Synonyms=ZNF690;
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), AND VARIANTS
RP GLY-104 AND SER-199.
RC TISSUE=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 [MRNA] OF 2-852 (ISOFORM 1).
RC TISSUE=Erythroid cell;
RX PubMed=12434312; DOI=10.1086/344781;
RA Dgany O., Avidan N., Delaunay J., Krasnov T., Shalmon L., Shalev H.,
RA Eidelitz-Markus T., Kapelushnik J., Cattan D., Pariente A., Tulliez M.,
RA Cretien A., Schischmanoff P.-O., Iolascon A., Fibach E., Koren A.,
RA Roessler J., Le Merrer M., Yaniv I., Zaizov R., Ben-Asher E., Olender T.,
RA Lancet D., Beckmann J.S., Tamary H.;
RT "Congenital dyserythropoietic anemia type I is caused by mutations in
RT codanin-1.";
RL Am. J. Hum. Genet. 71:1467-1474(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-852 (ISOFORMS 3 AND 4).
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-561, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-112; LYS-180; LYS-576 AND
RP LYS-652, AND 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 -!- INTERACTION:
CC Q8IWY8-3; Q9BRL7: SEC22C; NbExp=3; IntAct=EBI-14188237, EBI-10297029;
CC Q8IWY8-3; Q9NWS9-2: ZNF446; NbExp=3; IntAct=EBI-14188237, EBI-740232;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8IWY8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IWY8-2; Sequence=VSP_018179;
CC Name=3;
CC IsoId=Q8IWY8-3; Sequence=VSP_018181, VSP_018182;
CC Name=4;
CC IsoId=Q8IWY8-4; Sequence=VSP_018180;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK093186; BAC04088.1; -; mRNA.
DR EMBL; AK122788; BAG53731.1; -; mRNA.
DR EMBL; AF525399; AAO14995.1; -; mRNA.
DR EMBL; BC109270; AAI09271.1; -; mRNA.
DR EMBL; BC109271; AAI09272.1; -; mRNA.
DR CCDS; CCDS10095.2; -. [Q8IWY8-1]
DR RefSeq; NP_689668.3; NM_152455.3. [Q8IWY8-1]
DR RefSeq; XP_006720464.1; XM_006720401.3.
DR RefSeq; XP_011519568.1; XM_011521266.2.
DR AlphaFoldDB; Q8IWY8; -.
DR SMR; Q8IWY8; -.
DR BioGRID; 126960; 27.
DR IntAct; Q8IWY8; 12.
DR STRING; 9606.ENSP00000380174; -.
DR iPTMnet; Q8IWY8; -.
DR PhosphoSitePlus; Q8IWY8; -.
DR BioMuta; ZSCAN29; -.
DR DMDM; 259016454; -.
DR EPD; Q8IWY8; -.
DR jPOST; Q8IWY8; -.
DR MassIVE; Q8IWY8; -.
DR MaxQB; Q8IWY8; -.
DR PaxDb; Q8IWY8; -.
DR PeptideAtlas; Q8IWY8; -.
DR PRIDE; Q8IWY8; -.
DR ProteomicsDB; 70928; -. [Q8IWY8-1]
DR ProteomicsDB; 70929; -. [Q8IWY8-2]
DR ProteomicsDB; 70930; -. [Q8IWY8-3]
DR ProteomicsDB; 70931; -. [Q8IWY8-4]
DR ABCD; Q8IWY8; 10 sequenced antibodies.
DR Antibodypedia; 11192; 122 antibodies from 21 providers.
DR DNASU; 146050; -.
DR Ensembl; ENST00000396976.6; ENSP00000380174.2; ENSG00000140265.14. [Q8IWY8-1]
DR Ensembl; ENST00000684362.1; ENSP00000507363.1; ENSG00000140265.14. [Q8IWY8-1]
DR GeneID; 146050; -.
DR KEGG; hsa:146050; -.
DR MANE-Select; ENST00000684362.1; ENSP00000507363.1; NM_001372080.1; NP_001359009.1.
DR UCSC; uc001zrk.2; human. [Q8IWY8-1]
DR CTD; 146050; -.
DR GeneCards; ZSCAN29; -.
DR HGNC; HGNC:26673; ZSCAN29.
DR HPA; ENSG00000140265; Low tissue specificity.
DR neXtProt; NX_Q8IWY8; -.
DR OpenTargets; ENSG00000140265; -.
DR PharmGKB; PA162411015; -.
DR VEuPathDB; HostDB:ENSG00000140265; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161523; -.
DR HOGENOM; CLU_002678_88_0_1; -.
DR InParanoid; Q8IWY8; -.
DR OMA; SERKIPC; -.
DR PhylomeDB; Q8IWY8; -.
DR TreeFam; TF336839; -.
DR PathwayCommons; Q8IWY8; -.
DR SignaLink; Q8IWY8; -.
DR BioGRID-ORCS; 146050; 13 hits in 1099 CRISPR screens.
DR ChiTaRS; ZSCAN29; human.
DR GenomeRNAi; 146050; -.
DR Pharos; Q8IWY8; Tdark.
DR PRO; PR:Q8IWY8; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8IWY8; protein.
DR Bgee; ENSG00000140265; Expressed in secondary oocyte and 196 other tissues.
DR ExpressionAtlas; Q8IWY8; baseline and differential.
DR Genevisible; Q8IWY8; 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:0000978; F:RNA polymerase II cis-regulatory region 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 CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR044822; Myb_DNA-bind_4.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF13837; Myb_DNA-bind_4; 2.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..852
FT /note="Zinc finger and SCAN domain-containing protein 29"
FT /id="PRO_0000234011"
FT DOMAIN 18..100
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 678..700
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 706..728
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 734..756
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 762..784
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 790..812
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 818..840
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 96..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..546
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 576
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 652
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018179"
FT VAR_SEQ 176..564
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018180"
FT VAR_SEQ 495..557
FT /note="SVRVAAPPNDGQEETASCPVQGTSEAEAQKQAEEADEATEEDSDDDEEDTEI
FT PPGAVITRAPV -> LKLDLRMKIIQNGIFLRKYNCIGHYLQDLKGKFPGIFIRVKAMR
FT VTVDQEDSGQRPQGRKEEN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018181"
FT VAR_SEQ 558..852
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018182"
FT VARIANT 104
FT /note="R -> G (in dbSNP:rs3809482)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_059949"
FT VARIANT 199
FT /note="G -> S (in dbSNP:rs3917221)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_057459"
FT CONFLICT 182
FT /note="G -> S (in Ref. 3; AAI09271)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 852 AA; 96719 MW; B92BE704821F8EC8 CRC64;
MMAKSALREN GTNSETFRQR FRRFHYQEVA GPREAFSQLW ELCCRWLRPE VRTKEQIVEL
LVLEQFLTVL PGEIQNWVQE QCPENGEEAV TLVEDLEREP GRPRSSVTVS VKGQEVRLEK
MTPPKSSQEL LSVRQESVEP QPRGVPKKER ARSPDLGPQE QMNPKEKLKP FQRSGLPFPK
SGVVSRLEQG EPWIPDLLGS KEKELPSGSH IGDRRVHADL LPSKKDRRSW VEQDHWSFED
EKVAGVHWGY EETRTLLAIL SQTEFYEALR NCHRNSQVYG AVAERLREYG FLRTLEQCRT
KFKGLQKSYR KVKSGHPPET CPFFEEMEAL MSAQVIALPS NGLEAAASHS GLVGSDAETE
EPGQRGWQHE EGAEEAVAQE SDSDDMDLEA TPQDPNSAAP VVFRSPGGVH WGYEETKTYL
AILSETQFYE ALRNCHRNSQ LYGAVAERLW EYGFLRTPEQ CRTKFKSLQT SYRKVKNGQA
PETCPFFEEM DALVSVRVAA PPNDGQEETA SCPVQGTSEA EAQKQAEEAD EATEEDSDDD
EEDTEIPPGA VITRAPVLFQ SPRGFEAGFE NEDNSKRDIS EEVQLHRTLL ARSERKIPRY
LHQGKGNESD CRSGRQWAKT SGEKRGKLTL PEKSLSEVLS QQRPCLGERP YKYLKYSKSF
GPNSLLMHQV SHQVENPYKC ADCGKSFSRS ARLIRHRRIH TGEKPYKCLD CGKSFRDSSN
FITHRRIHTG EKPYQCGECG KCFNQSSSLI IHQRTHTGEK PYQCEECGKS FNNSSHFSAH
RRIHTGERPH VCPDCGKSFS KSSDLRAHHR THTGEKPYGC HDCGKCFSKS SALNKHGEIH
AREKLLTQSA PK
