ZN473_HUMAN
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 03-AUG-2022, entry version 175.
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};
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; 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; 26.
DR IntAct; Q8WTR7; 26.
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; Q8WTR7; -.
DR PeptideAtlas; Q8WTR7; -.
DR PRIDE; Q8WTR7; -.
DR ProteomicsDB; 74591; -.
DR Antibodypedia; 32254; 125 antibodies from 20 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 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; 1318335at2759; -.
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; 7 hits in 1100 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 140 other tissues.
DR ExpressionAtlas; Q8WTR7; baseline and differential.
DR Genevisible; Q8WTR7; HS.
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 InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 20.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 11.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 18.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 20.
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
