ID   ZN473_HUMAN             Reviewed;         871 AA.
AC   Q8WTR7; A8K8T7; Q9ULS9; Q9Y4Q7;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Zinc finger protein 473;
DE   AltName: Full=Zinc finger protein 100 homolog;
DE            Short=Zfp-100;
GN   Name=ZNF473; Synonyms=KIAA1141, ZFP100;
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 [MRNA], FUNCTION, AND INTERACTION WITH SLBP/PRE-MRNA
RP   COMPLEX.
RX   PubMed=11782445; DOI=10.1101/gad.932302;
RA   Dominski Z., Erkmann J.A., Yang X., Sanchez R., Marzluff W.F.;
RT   "A novel zinc finger protein is associated with U7 snRNP and interacts with
RT   the stem-loop binding protein in the histone pre-mRNP to stimulate 3'-end
RT   processing.";
RL   Genes Dev. 16:58-71(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis from
RT   size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-871.
RC   TISSUE=Testis;
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   [7]
RP   INTERACTION WITH LSM11.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=12975319; DOI=10.1101/gad.274403;
RA   Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R., Fischer U.,
RA   Schuemperli D.;
RT   "Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN
RT   complex and the role of a new component, Lsm11, in histone RNA
RT   processing.";
RL   Genes Dev. 17:2321-2333(2003).
RN   [8]
RP   INTERACTION WITH LSM11.
RX   PubMed=15824063; DOI=10.1093/nar/gki516;
RA   Azzouz T.N., Gruber A., Schuemperli D.;
RT   "U7 snRNP-specific Lsm11 protein: dual binding contacts with the 100 kDa
RT   zinc finger processing factor (ZFP100) and a ZFP100-independent function in
RT   histone RNA 3'-end processing.";
RL   Nucleic Acids Res. 33:2106-2117(2005).
RN   [9]
RP   FUNCTION.
RX   PubMed=16914750; DOI=10.1128/mcb.00391-06;
RA   Wagner E.J., Marzluff W.F.;
RT   "ZFP100, a component of the active U7 snRNP limiting for histone pre-mRNA
RT   processing, is required for entry into S phase.";
RL   Mol. Cell. Biol. 26:6702-6712(2006).
RN   [10]
RP   FUNCTION, INTERACTION WITH LSM11, AND SUBCELLULAR LOCATION.
RX   PubMed=16714279; DOI=10.1261/rna.2606;
RA   Wagner E.J., Ospina J.K., Hu Y., Dundr M., Matera A.G., Marzluff W.F.;
RT   "Conserved zinc fingers mediate multiple functions of ZFP100, a U7snRNP
RT   associated protein.";
RL   RNA 12:1206-1218(2006).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-148; LYS-419; LYS-549; LYS-558
RP   AND LYS-635, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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).
RN   [12]
RP   STRUCTURE BY NMR OF 205-841.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the C2H2 type zinc finger region of human zinc
RT   finger protein 473.";
RL   Submitted (OCT-2007) to the PDB data bank.
CC   -!- FUNCTION: Involved in histone 3'-end pre-mRNA processing by associating
CC       with U7 snRNP and interacting with SLBP/pre-mRNA complex. Increases
CC       histone 3'-end pre-mRNA processing but has no effect on U7 snRNP
CC       levels, when overexpressed. Required for cell cycle progression from G1
CC       to S phases. {ECO:0000269|PubMed:11782445, ECO:0000269|PubMed:16714279,
CC       ECO:0000269|PubMed:16914750}.
CC   -!- SUBUNIT: Interacts with the SLBP/pre-mRNA complex but not with SLBP
CC       alone. Interacts with LSM11 in a U7 snRNP-dependent manner.
CC       {ECO:0000269|PubMed:11782445, ECO:0000269|PubMed:12975319,
CC       ECO:0000269|PubMed:15824063, ECO:0000269|PubMed:16714279}.
CC   -!- INTERACTION:
CC       Q8WTR7; Q8WTP8: AEN; NbExp=5; IntAct=EBI-751409, EBI-8637627;
CC       Q8WTR7; P49760: CLK2; NbExp=3; IntAct=EBI-751409, EBI-750020;
CC       Q8WTR7; P49761: CLK3; NbExp=3; IntAct=EBI-751409, EBI-745579;
CC       Q8WTR7; Q6P158: DHX57; NbExp=3; IntAct=EBI-751409, EBI-1051531;
CC       Q8WTR7; Q9NWQ4: GPATCH2L; NbExp=4; IntAct=EBI-751409, EBI-5666657;
CC       Q8WTR7; P60014: KRTAP10-10; NbExp=3; IntAct=EBI-751409, EBI-11955579;
CC       Q8WTR7; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-751409, EBI-10171774;
CC       Q8WTR7; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-751409, EBI-10172052;
CC       Q8WTR7; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-751409, EBI-1567797;
CC       Q8WTR7; P98175: RBM10; NbExp=3; IntAct=EBI-751409, EBI-721525;
CC       Q8WTR7; D3DU92: RNPS1; NbExp=3; IntAct=EBI-751409, EBI-10176640;
CC       Q8WTR7; Q8WV44: TRIM41; NbExp=5; IntAct=EBI-751409, EBI-725997;
CC       Q8WTR7; P15622-3: ZNF250; NbExp=3; IntAct=EBI-751409, EBI-10177272;
CC       Q8WTR7; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-751409, EBI-347633;
CC       Q8WTR7; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-751409, EBI-10486136;
CC       Q8WTR7; Q3KQV3: ZNF792; NbExp=5; IntAct=EBI-751409, EBI-10240849;
CC       Q8WTR7; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-751409, EBI-11962574;
CC       Q8WTR7; O43309: ZSCAN12; NbExp=3; IntAct=EBI-751409, EBI-1210440;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16714279}.
CC       Note=Stable component of Cajal bodies (CBs). Colocalizes with SMN,
CC       coilin and U7 snRNA.
CC   -!- DOMAIN: The C2H2-type zinc finger 2 to 6 are necessary and sufficient
CC       for discrete Cajal bodies localization. The C2H2-type zinc finger 5 to
CC       10 are necessary and sufficient for interaction with LSM11. The C2H2-
CC       type zinc finger 2 to 8 are necessary for interaction with the SLBP/RNA
CC       complex in the histone pre-mRNAs. The C2H2-type zinc finger 2 to 10
CC       confer activity in histone pre-mRNA processing.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA86455.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF454744; AAL51029.1; -; mRNA.
DR   EMBL; AB032967; BAA86455.1; ALT_INIT; mRNA.
DR   EMBL; AK292452; BAF85141.1; -; mRNA.
DR   EMBL; CH471177; EAW52593.1; -; Genomic_DNA.
DR   EMBL; BC018612; AAH18612.1; -; mRNA.
DR   EMBL; AL080143; CAB45736.1; -; mRNA.
DR   CCDS; CCDS33077.1; -.
DR   PIR; T12527; T12527.
DR   RefSeq; NP_001006657.1; NM_001006656.3.
DR   RefSeq; NP_001295353.1; NM_001308424.2.
DR   RefSeq; NP_056243.1; NM_015428.3.
DR   PDB; 2EMB; NMR; -; A=342-372.
DR   PDB; 2EMC; NMR; -; A=641-673.
DR   PDB; 2EME; NMR; -; A=725-757.
DR   PDB; 2EOU; NMR; -; A=370-400.
DR   PDB; 2EOX; NMR; -; A=315-345.
DR   PDB; 2EOY; NMR; -; A=557-589.
DR   PDB; 2EOZ; NMR; -; A=809-841.
DR   PDB; 2YRH; NMR; -; A=699-729.
DR   PDB; 2YRJ; NMR; -; A=781-813.
DR   PDB; 2YSV; NMR; -; A=755-783.
DR   PDB; 2YTD; NMR; -; A=426-458.
DR   PDB; 2YTE; NMR; -; A=484-512.
DR   PDB; 2YTT; NMR; -; A=204-236.
DR   PDB; 2YU5; NMR; -; A=669-699.
DR   PDBsum; 2EMB; -.
DR   PDBsum; 2EMC; -.
DR   PDBsum; 2EME; -.
DR   PDBsum; 2EOU; -.
DR   PDBsum; 2EOX; -.
DR   PDBsum; 2EOY; -.
DR   PDBsum; 2EOZ; -.
DR   PDBsum; 2YRH; -.
DR   PDBsum; 2YRJ; -.
DR   PDBsum; 2YSV; -.
DR   PDBsum; 2YTD; -.
DR   PDBsum; 2YTE; -.
DR   PDBsum; 2YTT; -.
DR   PDBsum; 2YU5; -.
DR   AlphaFoldDB; Q8WTR7; -.
DR   SMR; Q8WTR7; -.
DR   BioGRID; 117398; 27.
DR   IntAct; Q8WTR7; 24.
DR   STRING; 9606.ENSP00000472808; -.
DR   iPTMnet; Q8WTR7; -.
DR   PhosphoSitePlus; Q8WTR7; -.
DR   BioMuta; ZNF473; -.
DR   DMDM; 51702187; -.
DR   EPD; Q8WTR7; -.
DR   jPOST; Q8WTR7; -.
DR   MassIVE; Q8WTR7; -.
DR   PaxDb; 9606-ENSP00000472808; -.
DR   PeptideAtlas; Q8WTR7; -.
DR   ProteomicsDB; 74591; -.
DR   Antibodypedia; 32254; 144 antibodies from 21 providers.
DR   DNASU; 25888; -.
DR   Ensembl; ENST00000270617.8; ENSP00000270617.3; ENSG00000142528.16.
DR   Ensembl; ENST00000391821.6; ENSP00000375697.1; ENSG00000142528.16.
DR   Ensembl; ENST00000595661.5; ENSP00000472808.1; ENSG00000142528.16.
DR   GeneID; 25888; -.
DR   KEGG; hsa:25888; -.
DR   MANE-Select; ENST00000270617.8; ENSP00000270617.3; NM_015428.4; NP_056243.1.
DR   UCSC; uc002prm.4; human.
DR   AGR; HGNC:23239; -.
DR   CTD; 25888; -.
DR   GeneCards; ZNF473; -.
DR   HGNC; HGNC:23239; ZNF473.
DR   HPA; ENSG00000142528; Tissue enriched (testis).
DR   MIM; 617908; gene.
DR   neXtProt; NX_Q8WTR7; -.
DR   OpenTargets; ENSG00000142528; -.
DR   PharmGKB; PA134987987; -.
DR   VEuPathDB; HostDB:ENSG00000142528; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00840000130048; -.
DR   HOGENOM; CLU_002678_27_0_1; -.
DR   InParanoid; Q8WTR7; -.
DR   OMA; YSCAKCK; -.
DR   OrthoDB; 5249044at2759; -.
DR   PhylomeDB; Q8WTR7; -.
DR   TreeFam; TF350932; -.
DR   PathwayCommons; Q8WTR7; -.
DR   Reactome; R-HSA-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR   Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR   SignaLink; Q8WTR7; -.
DR   BioGRID-ORCS; 25888; 8 hits in 1178 CRISPR screens.
DR   EvolutionaryTrace; Q8WTR7; -.
DR   GeneWiki; ZNF473; -.
DR   GenomeRNAi; 25888; -.
DR   Pharos; Q8WTR7; Tbio.
DR   PRO; PR:Q8WTR7; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q8WTR7; Protein.
DR   Bgee; ENSG00000142528; Expressed in right uterine tube and 142 other cell types or tissues.
DR   ExpressionAtlas; Q8WTR7; baseline and differential.
DR   GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator 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:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 20.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR47772:SF4; REDUCED EXPRESSION 2-RELATED; 1.
DR   PANTHER; PTHR47772; ZINC FINGER PROTEIN 200; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 15.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 20.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 11.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 18.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 20.
DR   Genevisible; Q8WTR7; HS.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..871
FT                   /note="Zinc finger protein 473"
FT                   /id="PRO_0000047604"
FT   DOMAIN          6..75
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         209..231
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         265..286
FT                   /note="C2H2-type 2; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         320..342
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         347..369
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         375..397
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         403..425
FT                   /note="C2H2-type 6; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         431..453
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         459..481
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         487..509
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         515..537
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         562..584
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         591..613
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         646..668
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         674..696
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         702..724
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         730..752
FT                   /note="C2H2-type 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         758..780
FT                   /note="C2H2-type 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         786..808
FT                   /note="C2H2-type 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         814..836
FT                   /note="C2H2-type 19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         842..864
FT                   /note="C2H2-type 20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          47..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..552
FT                   /note="Interaction with SLBP/pre-mRNA complex"
FT   COMPBIAS        290..317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        148
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        419
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        549
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        558
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        635
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         59
FT                   /note="S -> G (in dbSNP:rs10419876)"
FT                   /id="VAR_052839"
FT   VARIANT         74
FT                   /note="S -> G (in dbSNP:rs10419911)"
FT                   /id="VAR_052840"
FT   VARIANT         164
FT                   /note="T -> M (in dbSNP:rs16981705)"
FT                   /id="VAR_052841"
FT   VARIANT         309
FT                   /note="E -> G (in dbSNP:rs16981706)"
FT                   /id="VAR_052842"
FT   VARIANT         654
FT                   /note="T -> I (in dbSNP:rs10424809)"
FT                   /id="VAR_052843"
FT   VARIANT         662
FT                   /note="S -> A (in dbSNP:rs10426374)"
FT                   /id="VAR_052844"
FT   CONFLICT        486
FT                   /note="P -> A (in Ref. 6)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        588
FT                   /note="V -> M (in Ref. 2; BAA86455)"
FT                   /evidence="ECO:0000305"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:2YTT"
FT   HELIX           221..228
FT                   /evidence="ECO:0007829|PDB:2YTT"
FT   HELIX           230..233
FT                   /evidence="ECO:0007829|PDB:2YTT"
FT   STRAND          320..322
FT                   /evidence="ECO:0007829|PDB:2EOX"
FT   TURN            323..326
FT                   /evidence="ECO:0007829|PDB:2EOX"
FT   STRAND          327..332
FT                   /evidence="ECO:0007829|PDB:2EOX"
FT   HELIX           333..336
FT                   /evidence="ECO:0007829|PDB:2EOX"
FT   HELIX           339..342
FT                   /evidence="ECO:0007829|PDB:2EOX"
FT   STRAND          345..348
FT                   /evidence="ECO:0007829|PDB:2EMB"
FT   TURN            350..352
FT                   /evidence="ECO:0007829|PDB:2EMB"
FT   STRAND          355..357
FT                   /evidence="ECO:0007829|PDB:2EMB"
FT   HELIX           359..365
FT                   /evidence="ECO:0007829|PDB:2EMB"
FT   HELIX           366..369
FT                   /evidence="ECO:0007829|PDB:2EMB"
FT   STRAND          370..372
FT                   /evidence="ECO:0007829|PDB:2EOU"
FT   TURN            378..380
FT                   /evidence="ECO:0007829|PDB:2EOU"
FT   HELIX           387..397
FT                   /evidence="ECO:0007829|PDB:2EOU"
FT   STRAND          430..432
FT                   /evidence="ECO:0007829|PDB:2YTD"
FT   STRAND          434..436
FT                   /evidence="ECO:0007829|PDB:2YTD"
FT   STRAND          439..442
FT                   /evidence="ECO:0007829|PDB:2YTD"
FT   HELIX           443..453
FT                   /evidence="ECO:0007829|PDB:2YTD"
FT   TURN            490..492
FT                   /evidence="ECO:0007829|PDB:2YTE"
FT   HELIX           499..508
FT                   /evidence="ECO:0007829|PDB:2YTE"
FT   STRAND          565..567
FT                   /evidence="ECO:0007829|PDB:2EOY"
FT   STRAND          570..574
FT                   /evidence="ECO:0007829|PDB:2EOY"
FT   HELIX           575..581
FT                   /evidence="ECO:0007829|PDB:2EOY"
FT   STRAND          645..647
FT                   /evidence="ECO:0007829|PDB:2EMC"
FT   STRAND          649..651
FT                   /evidence="ECO:0007829|PDB:2EMC"
FT   STRAND          654..657
FT                   /evidence="ECO:0007829|PDB:2EMC"
FT   HELIX           658..665
FT                   /evidence="ECO:0007829|PDB:2EMC"
FT   TURN            666..670
FT                   /evidence="ECO:0007829|PDB:2EMC"
FT   STRAND          673..675
FT                   /evidence="ECO:0007829|PDB:2YU5"
FT   STRAND          677..680
FT                   /evidence="ECO:0007829|PDB:2YU5"
FT   STRAND          682..686
FT                   /evidence="ECO:0007829|PDB:2YU5"
FT   HELIX           687..695
FT                   /evidence="ECO:0007829|PDB:2YU5"
FT   TURN            705..707
FT                   /evidence="ECO:0007829|PDB:2YRH"
FT   STRAND          710..713
FT                   /evidence="ECO:0007829|PDB:2YRH"
FT   HELIX           714..721
FT                   /evidence="ECO:0007829|PDB:2YRH"
FT   TURN            722..724
FT                   /evidence="ECO:0007829|PDB:2YRH"
FT   STRAND          729..731
FT                   /evidence="ECO:0007829|PDB:2EME"
FT   STRAND          733..735
FT                   /evidence="ECO:0007829|PDB:2EME"
FT   STRAND          738..741
FT                   /evidence="ECO:0007829|PDB:2EME"
FT   HELIX           742..749
FT                   /evidence="ECO:0007829|PDB:2EME"
FT   HELIX           750..752
FT                   /evidence="ECO:0007829|PDB:2EME"
FT   STRAND          761..763
FT                   /evidence="ECO:0007829|PDB:2YSV"
FT   STRAND          768..771
FT                   /evidence="ECO:0007829|PDB:2YSV"
FT   HELIX           772..778
FT                   /evidence="ECO:0007829|PDB:2YSV"
FT   STRAND          789..791
FT                   /evidence="ECO:0007829|PDB:2YRJ"
FT   STRAND          794..797
FT                   /evidence="ECO:0007829|PDB:2YRJ"
FT   HELIX           798..805
FT                   /evidence="ECO:0007829|PDB:2YRJ"
FT   TURN            806..808
FT                   /evidence="ECO:0007829|PDB:2YRJ"
FT   STRAND          813..816
FT                   /evidence="ECO:0007829|PDB:2EOZ"
FT   TURN            817..820
FT                   /evidence="ECO:0007829|PDB:2EOZ"
FT   STRAND          821..825
FT                   /evidence="ECO:0007829|PDB:2EOZ"
FT   HELIX           826..836
FT                   /evidence="ECO:0007829|PDB:2EOZ"
SQ   SEQUENCE   871 AA;  100182 MW;  959AFB7C3C2D5456 CRC64;
     MAEEFVTLKD VGMDFTLGDW EQLGLEQGDT FWDTALDNCQ DLFLLDPPRP NLTSHPDGSE
     DLEPLAGGSP EATSPDVTET KNSPLMEDFF EEGFSQEIIE MLSKDGFWNS NFGEACIEDT
     WLDSLLGDPE SLLRSDIATN GESPTECKSH ELKRGLSPVS TVSTGEDSMV HNVSEKTLTP
     AKSKEYRGEF FSYSDHSQQD SVQEGEKPYQ CSECGKSFSG SYRLTQHWIT HTREKPTVHQ
     ECEQGFDRNA SLSVYPKTHT GYKFYVCNEY GTTFSQSTYL WHQKTHTGEK PCKSQDSDHP
     PSHDTQPGEH QKTHTDSKSY NCNECGKAFT RIFHLTRHQK IHTRKRYECS KCQATFNLRK
     HLIQHQKTHA AKTTSECQEC GKIFRHSSLL IEHQALHAGE EPYKCNERGK SFRHNSTLKI
     HQRVHSGEKP YKCSECGKAF HRHTHLNEHR RIHTGYRPHK CQECVRSFSR PSHLMRHQAI
     HTAEKPYSCA ECKETFSDNN RLVQHQKMHT VKTPYECQEC GERFICGSTL KCHESVHARE
     KQGFFVSGKI LDQNPEQKEK CFKCNKCEKT FSCSKYLTQH ERIHTRGVKP FECDQCGKAF
     GQSTRLIHHQ RIHSRVRLYK WGEQGKAISS ASLIKLQSFH TKEHPFKCNE CGKTFSHSAH
     LSKHQLIHAG ENPFKCSKCD RVFTQRNYLV QHERTHARKK PLVCNECGKT FRQSSCLSKH
     QRIHSGEKPY VCDYCGKAFG LSAELVRHQR IHTGEKPYVC QECGKAFTQS SCLSIHRRVH
     TGEKPYRCGE CGKAFAQKAN LTQHQRIHTG EKPYSCNVCG KAFVLSAHLN QHLRVHTQET
     LYQCQRCQKA FRCHSSLSRH QRVHNKQQYC L
//