ZSC22_HUMAN
ID ZSC22_HUMAN Reviewed; 491 AA.
AC P10073; Q15922; Q7Z3L8;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 22;
DE AltName: Full=Krueppel-related zinc finger protein 2;
DE AltName: Full=Protein HKR2;
DE AltName: Full=Zinc finger protein 50;
GN Name=ZSCAN22; Synonyms=HKR2, ZNF50;
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=Uterus;
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].
RC TISSUE=Fetal kidney;
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 MRNA].
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 370-457.
RC TISSUE=Placenta;
RX PubMed=1505991; DOI=10.1016/0888-7543(92)90013-i;
RA Lichter P., Bray P., Ried T., Dawid I.B., Ward D.C.;
RT "Clustering of C2-H2 zinc finger motif sequences within telomeric and
RT fragile site regions of human chromosomes.";
RL Genomics 13:999-1007(1992).
RN [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2850480; DOI=10.1128/mcb.8.8.3104-3113.1988;
RA Ruppert J.M., Kinzler K.W., Wong A.J., Bigner S.H., Kao F.T., Law M.L.,
RA Seuanez H.N., O'Brien S.J., Vogelstein B.;
RT "The GLI-Kruppel family of human genes.";
RL Mol. Cell. Biol. 8:3104-3113(1988).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-443, AND IDENTIFICATION BY MASS
RP 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 P10073; Q13895: BYSL; NbExp=3; IntAct=EBI-10178224, EBI-358049;
CC P10073; Q86X02: CDR2L; NbExp=3; IntAct=EBI-10178224, EBI-11063830;
CC P10073; G5E9A7: DMWD; NbExp=3; IntAct=EBI-10178224, EBI-10976677;
CC P10073; Q01658: DR1; NbExp=3; IntAct=EBI-10178224, EBI-750300;
CC P10073; Q92997: DVL3; NbExp=3; IntAct=EBI-10178224, EBI-739789;
CC P10073; P14136: GFAP; NbExp=3; IntAct=EBI-10178224, EBI-744302;
CC P10073; Q00403: GTF2B; NbExp=3; IntAct=EBI-10178224, EBI-389564;
CC P10073; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-10178224, EBI-1054873;
CC P10073; Q17RG1: KCTD19; NbExp=3; IntAct=EBI-10178224, EBI-10239046;
CC P10073; P02545: LMNA; NbExp=3; IntAct=EBI-10178224, EBI-351935;
CC P10073; P19404: NDUFV2; NbExp=3; IntAct=EBI-10178224, EBI-713665;
CC P10073; Q0ZGT2-4: NEXN; NbExp=3; IntAct=EBI-10178224, EBI-10977819;
CC P10073; Q96JS3: PGBD1; NbExp=9; IntAct=EBI-10178224, EBI-10290053;
CC P10073; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-10178224, EBI-1567797;
CC P10073; P57086: SCAND1; NbExp=6; IntAct=EBI-10178224, EBI-745846;
CC P10073; Q14140: SERTAD2; NbExp=3; IntAct=EBI-10178224, EBI-2822051;
CC P10073; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-10178224, EBI-5235340;
CC P10073; Q9UKI8: TLK1; NbExp=3; IntAct=EBI-10178224, EBI-740492;
CC P10073; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-10178224, EBI-10183064;
CC P10073; A0A0S2Z6X0: ZKSCAN4; NbExp=3; IntAct=EBI-10178224, EBI-16431094;
CC P10073; Q969J2: ZKSCAN4; NbExp=3; IntAct=EBI-10178224, EBI-2818641;
CC P10073; Q9P0L1-2: ZKSCAN7; NbExp=3; IntAct=EBI-10178224, EBI-10698225;
CC P10073; Q15697-2: ZNF174; NbExp=3; IntAct=EBI-10178224, EBI-11158827;
CC P10073; P17028: ZNF24; NbExp=6; IntAct=EBI-10178224, EBI-707773;
CC P10073; O14978: ZNF263; NbExp=3; IntAct=EBI-10178224, EBI-744493;
CC P10073; Q8NF99-2: ZNF397; NbExp=3; IntAct=EBI-10178224, EBI-11524467;
CC P10073; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-10178224, EBI-12010736;
CC P10073; Q9NWS9-2: ZNF446; NbExp=8; IntAct=EBI-10178224, EBI-740232;
CC P10073; Q6P9G9: ZNF449; NbExp=3; IntAct=EBI-10178224, EBI-10215956;
CC P10073; Q6P088: ZNF483; NbExp=3; IntAct=EBI-10178224, EBI-10196963;
CC P10073; Q96IT1: ZNF496; NbExp=7; IntAct=EBI-10178224, EBI-743906;
CC P10073; Q8NBB4-2: ZSCAN1; NbExp=3; IntAct=EBI-10178224, EBI-12021938;
CC P10073; Q9H4T2: ZSCAN16; NbExp=6; IntAct=EBI-10178224, EBI-723596;
CC P10073; Q8TBC5: ZSCAN18; NbExp=3; IntAct=EBI-10178224, EBI-3919096;
CC P10073; Q9Y5A6: ZSCAN21; NbExp=3; IntAct=EBI-10178224, EBI-10281938;
CC P10073; Q3MJ62: ZSCAN23; NbExp=3; IntAct=EBI-10178224, EBI-5667532;
CC P10073; Q6NSZ9-2: ZSCAN25; NbExp=3; IntAct=EBI-10178224, EBI-14650477;
CC P10073; Q9NX65: ZSCAN32; NbExp=7; IntAct=EBI-10178224, EBI-739949;
CC P10073; O15535: ZSCAN9; NbExp=3; IntAct=EBI-10178224, EBI-751531;
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; AK128716; BAC87588.1; -; mRNA.
DR EMBL; BX537741; CAD97822.1; -; mRNA.
DR EMBL; BC101630; AAI01631.1; -; mRNA.
DR EMBL; BC112277; AAI12278.1; -; mRNA.
DR EMBL; M88360; AAA61318.1; -; Genomic_DNA.
DR CCDS; CCDS12975.1; -.
DR PIR; D31201; D31201.
DR PIR; D43284; D43284.
DR RefSeq; NP_001308045.1; NM_001321116.1.
DR RefSeq; NP_001308046.1; NM_001321117.1.
DR RefSeq; NP_862829.1; NM_181846.2.
DR RefSeq; XP_006723255.1; XM_006723192.3.
DR RefSeq; XP_011525219.1; XM_011526917.2.
DR AlphaFoldDB; P10073; -.
DR SMR; P10073; -.
DR BioGRID; 131214; 35.
DR IntAct; P10073; 41.
DR STRING; 9606.ENSP00000332433; -.
DR iPTMnet; P10073; -.
DR PhosphoSitePlus; P10073; -.
DR BioMuta; ZSCAN22; -.
DR DMDM; 134047986; -.
DR EPD; P10073; -.
DR jPOST; P10073; -.
DR MassIVE; P10073; -.
DR MaxQB; P10073; -.
DR PaxDb; P10073; -.
DR PeptideAtlas; P10073; -.
DR PRIDE; P10073; -.
DR ProteomicsDB; 52560; -.
DR ABCD; P10073; 5 sequenced antibodies.
DR Antibodypedia; 1829; 171 antibodies from 25 providers.
DR DNASU; 342945; -.
DR Ensembl; ENST00000329665.5; ENSP00000332433.3; ENSG00000182318.6.
DR GeneID; 342945; -.
DR KEGG; hsa:342945; -.
DR MANE-Select; ENST00000329665.5; ENSP00000332433.3; NM_181846.3; NP_862829.1.
DR UCSC; uc002qsc.3; human.
DR CTD; 342945; -.
DR DisGeNET; 342945; -.
DR GeneCards; ZSCAN22; -.
DR HGNC; HGNC:4929; ZSCAN22.
DR HPA; ENSG00000182318; Low tissue specificity.
DR MIM; 165260; gene.
DR neXtProt; NX_P10073; -.
DR OpenTargets; ENSG00000182318; -.
DR PharmGKB; PA29307; -.
DR VEuPathDB; HostDB:ENSG00000182318; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163014; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; P10073; -.
DR OMA; CRECRKM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P10073; -.
DR TreeFam; TF337913; -.
DR PathwayCommons; P10073; -.
DR SignaLink; P10073; -.
DR BioGRID-ORCS; 342945; 11 hits in 1101 CRISPR screens.
DR ChiTaRS; ZSCAN22; human.
DR GenomeRNAi; 342945; -.
DR Pharos; P10073; Tdark.
DR PRO; PR:P10073; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P10073; protein.
DR Bgee; ENSG00000182318; Expressed in ileal mucosa and 112 other tissues.
DR Genevisible; P10073; 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: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; 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; 8.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..491
FT /note="Zinc finger and SCAN domain-containing protein 22"
FT /id="PRO_0000047271"
FT DOMAIN 49..131
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 268..290
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 296..318
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 324..346
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 352..374
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 380..402
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 408..430
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 436..458
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 464..486
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 134..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 491 AA; 54561 MW; 4FD4BF55E1D00C74 CRC64;
MAIPKHSLSP VPWEEDSFLQ VKVEEEEEAS LSQGGESSHD HIAHSEAARL RFRHFRYEEA
SGPHEALAHL RALCCQWLQP EAHSKEQILE LLVLEQFLGA LPPEIQAWVG AQSPKSGEEA
AVLVEDLTQV LDKRGWDPGA EPTEASCKQS DLGESEPSNV TETLMGGVSL GPAFVKACEP
EGSSERSGLS GEIWTKSVTQ QIHFKKTSGP YKDVPTDQRG RESGASRNSS SAWPNLTSQE
KPPSEDKFDL VDAYGTEPPY TYSGKRSSKC RECRKMFQSA SALEAHQKTH SRKTPYACSE
CGKAFSRSTH LAQHQVVHTG AKPHECKECG KAFSRVTHLT QHQRIHTGEK PYKCGECGKT
FSRSTHLTQH QRVHTGERPY ECDACGKAFS QSTHLTQHQR IHTGEKPYKC DACGRAFSDC
SALIRHLRIH SGEKPYQCKV CPKAFAQSSS LIEHQRIHTG EKPYKCSDCG KAFSRSSALM
VHLRIHITVL Q
