ZSC21_HUMAN
ID ZSC21_HUMAN Reviewed; 473 AA.
AC Q9Y5A6; A4D2A6; D6W5T9; Q9H0B5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 21;
DE AltName: Full=Renal carcinoma antigen NY-REN-21;
DE AltName: Full=Zinc finger protein 38 homolog;
DE Short=Zfp-38;
GN Name=ZSCAN21; Synonyms=ZFP38, ZNF38;
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].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 62-473, AND IDENTIFICATION AS A RENAL CANCER
RP ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27; LYS-221; LYS-232 AND LYS-349,
RP 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: Strong transcriptional activator (By similarity). Plays an
CC important role in spermatogenesis; essential for the progression of
CC meiotic prophase I in spermatocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q07231}.
CC -!- INTERACTION:
CC Q9Y5A6; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-10281938, EBI-2559016;
CC Q9Y5A6; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-10281938, EBI-739624;
CC Q9Y5A6; P49760: CLK2; NbExp=5; IntAct=EBI-10281938, EBI-750020;
CC Q9Y5A6; Q92997: DVL3; NbExp=3; IntAct=EBI-10281938, EBI-739789;
CC Q9Y5A6; O75791: GRAP2; NbExp=4; IntAct=EBI-10281938, EBI-740418;
CC Q9Y5A6; Q6A162: KRT40; NbExp=3; IntAct=EBI-10281938, EBI-10171697;
CC Q9Y5A6; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-10281938, EBI-10172150;
CC Q9Y5A6; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10281938, EBI-10172290;
CC Q9Y5A6; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-10281938, EBI-10171774;
CC Q9Y5A6; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-10281938, EBI-10172052;
CC Q9Y5A6; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-10281938, EBI-11953334;
CC Q9Y5A6; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10281938, EBI-79165;
CC Q9Y5A6; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-10281938, EBI-725997;
CC Q9Y5A6; Q969J2: ZKSCAN4; NbExp=4; IntAct=EBI-10281938, EBI-2818641;
CC Q9Y5A6; Q9P0L1: ZKSCAN7; NbExp=3; IntAct=EBI-10281938, EBI-743851;
CC Q9Y5A6; Q9P0L1-2: ZKSCAN7; NbExp=3; IntAct=EBI-10281938, EBI-10698225;
CC Q9Y5A6; O14771: ZNF213; NbExp=3; IntAct=EBI-10281938, EBI-12838388;
CC Q9Y5A6; P17028: ZNF24; NbExp=6; IntAct=EBI-10281938, EBI-707773;
CC Q9Y5A6; Q96N95-3: ZNF396; NbExp=3; IntAct=EBI-10281938, EBI-12328453;
CC Q9Y5A6; Q9NWS9-2: ZNF446; NbExp=8; IntAct=EBI-10281938, EBI-740232;
CC Q9Y5A6; Q6P088: ZNF483; NbExp=3; IntAct=EBI-10281938, EBI-10196963;
CC Q9Y5A6; Q96IT1: ZNF496; NbExp=6; IntAct=EBI-10281938, EBI-743906;
CC Q9Y5A6; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-10281938, EBI-11962574;
CC Q9Y5A6; O43309: ZSCAN12; NbExp=3; IntAct=EBI-10281938, EBI-1210440;
CC Q9Y5A6; P10073: ZSCAN22; NbExp=3; IntAct=EBI-10281938, EBI-10178224;
CC Q9Y5A6; Q3MJ62: ZSCAN23; NbExp=3; IntAct=EBI-10281938, EBI-5667532;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AL136865; CAB66799.1; -; mRNA.
DR EMBL; CH236956; EAL23860.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76609.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76610.1; -; Genomic_DNA.
DR EMBL; BC047309; AAH47309.1; -; mRNA.
DR EMBL; AF155100; AAD42866.1; -; mRNA.
DR CCDS; CCDS5681.1; -.
DR RefSeq; NP_666019.1; NM_145914.2.
DR RefSeq; XP_005250625.1; XM_005250568.4.
DR RefSeq; XP_006716176.1; XM_006716113.3.
DR RefSeq; XP_016868073.1; XM_017012584.1.
DR AlphaFoldDB; Q9Y5A6; -.
DR SMR; Q9Y5A6; -.
DR BioGRID; 113416; 98.
DR IntAct; Q9Y5A6; 47.
DR STRING; 9606.ENSP00000292450; -.
DR iPTMnet; Q9Y5A6; -.
DR PhosphoSitePlus; Q9Y5A6; -.
DR BioMuta; ZSCAN21; -.
DR DMDM; 20141976; -.
DR EPD; Q9Y5A6; -.
DR jPOST; Q9Y5A6; -.
DR MassIVE; Q9Y5A6; -.
DR MaxQB; Q9Y5A6; -.
DR PaxDb; Q9Y5A6; -.
DR PeptideAtlas; Q9Y5A6; -.
DR PRIDE; Q9Y5A6; -.
DR ProteomicsDB; 86323; -.
DR ABCD; Q9Y5A6; 2 sequenced antibodies.
DR Antibodypedia; 16310; 416 antibodies from 30 providers.
DR DNASU; 7589; -.
DR Ensembl; ENST00000292450.9; ENSP00000292450.4; ENSG00000166529.16.
DR GeneID; 7589; -.
DR KEGG; hsa:7589; -.
DR MANE-Select; ENST00000292450.9; ENSP00000292450.4; NM_145914.3; NP_666019.1.
DR UCSC; uc003uso.5; human.
DR CTD; 7589; -.
DR DisGeNET; 7589; -.
DR GeneCards; ZSCAN21; -.
DR HGNC; HGNC:13104; ZSCAN21.
DR HPA; ENSG00000166529; Low tissue specificity.
DR neXtProt; NX_Q9Y5A6; -.
DR OpenTargets; ENSG00000166529; -.
DR PharmGKB; PA162410981; -.
DR VEuPathDB; HostDB:ENSG00000166529; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161607; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; Q9Y5A6; -.
DR OMA; WEPLYIQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Y5A6; -.
DR TreeFam; TF338304; -.
DR PathwayCommons; Q9Y5A6; -.
DR SignaLink; Q9Y5A6; -.
DR BioGRID-ORCS; 7589; 9 hits in 1100 CRISPR screens.
DR ChiTaRS; ZSCAN21; human.
DR GeneWiki; ZSCAN21; -.
DR GenomeRNAi; 7589; -.
DR Pharos; Q9Y5A6; Tbio.
DR PRO; PR:Q9Y5A6; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y5A6; protein.
DR Bgee; ENSG00000166529; Expressed in oocyte and 166 other tissues.
DR ExpressionAtlas; Q9Y5A6; baseline and differential.
DR Genevisible; Q9Y5A6; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:NTNU_SB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd07936; SCAN; 1.
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; 7.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
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; 7.
PE 1: Evidence at protein level;
KW Activator; Differentiation; DNA-binding; Isopeptide bond; Meiosis;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Spermatogenesis;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..473
FT /note="Zinc finger and SCAN domain-containing protein 21"
FT /id="PRO_0000047297"
FT DOMAIN 45..127
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 277..299
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 305..327
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 333..354
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 360..382
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 388..410
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 416..438
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 444..466
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 127..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 349
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 473 AA; 53658 MW; D9A26694B114B96F CRC64;
MMTKVLGMAP VLGPRPPQEQ VGPLMVKVEE KEEKGKYLPS LEMFRQRFRQ FGYHDTPGPR
EALSQLRVLC CEWLRPEIHT KEQILELLVL EQFLTILPQE LQAWVQEHCP ESAEEAVTLL
EDLERELDEP GHQVSTPPNE QKPVWEKISS SGTAKESPSS MQPQPLETSH KYESWGPLYI
QESGEEQEFA QDPRKVRDCR LSTQHEESAD EQKGSEAEGL KGDIISVIIA NKPEASLERQ
CVNLENEKGT KPPLQEAGSK KGRESVPTKP TPGERRYICA ECGKAFSNSS NLTKHRRTHT
GEKPYVCTKC GKAFSHSSNL TLHYRTHLVD RPYDCKCGKA FGQSSDLLKH QRMHTEEAPY
QCKDCGKAFS GKGSLIRHYR IHTGEKPYQC NECGKSFSQH AGLSSHQRLH TGEKPYKCKE
CGKAFNHSSN FNKHHRIHTG EKPYWCHHCG KTFCSKSNLS KHQRVHTGEG EAP
