ID ZN106_HUMAN Reviewed; 1883 AA. AC Q9H2Y7; B4DZ40; E9PE29; Q6NSD9; Q6PEK1; Q86T43; Q86T45; Q86T50; Q86T58; AC Q86TA9; Q96M37; Q9H7B8; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 180. DE RecName: Full=Zinc finger protein 106; DE Short=Zfp-106; DE AltName: Full=Zinc finger protein 474; GN Name=ZNF106; Synonyms=SH3BP3, ZFP106, ZNF474; 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 [GENOMIC DNA / MRNA] (ISOFORM 1). RA Mashima H., Horikawa Y., Cox N.J., Bell G.I.; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 256-1033 AND 1604-1883 (ISOFORM 1). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-467 (ISOFORM 1). RC TISSUE=Skeletal muscle; 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 [LARGE SCALE MRNA] OF 544-1883 (ISOFORM 1). RC TISSUE=Skeletal muscle; 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 [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-861; SER-864; RP SER-937; THR-1021; SER-1025; SER-1026; SER-1031; SER-1279 AND SER-1328, AND 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590; SER-861; SER-1025; RP SER-1026; SER-1370 AND THR-1372, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-861; SER-893; SER-1025; RP SER-1026; SER-1279; SER-1328 AND SER-1370, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1025; SER-1026; SER-1031; RP SER-1279; SER-1284; SER-1302; SER-1328 AND SER-1370, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422; SER-641; SER-661; RP SER-861; SER-864; SER-893; SER-937; THR-1021; SER-1025; SER-1026; SER-1249; RP SER-1279; SER-1302; SER-1328; SER-1370; THR-1372 AND SER-1468, 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 [13] RP IDENTIFICATION BY 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 [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-371; LYS-775; LYS-911 RP AND LYS-1737, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1737, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-356; LYS-371; LYS-775; LYS-911; RP LYS-1265 AND LYS-1737, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-371; LYS-911; LYS-1265 AND RP LYS-1737, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-69; LYS-76; LYS-133; LYS-243; RP LYS-287; LYS-305; LYS-356; LYS-365; LYS-371; LYS-417; LYS-451; LYS-461; RP LYS-477; LYS-492; LYS-505; LYS-515; LYS-525; LYS-539; LYS-557; LYS-603; RP LYS-671; LYS-684; LYS-705; LYS-721; LYS-741; LYS-775; LYS-807; LYS-905; RP LYS-911; LYS-953; LYS-1265; LYS-1299; LYS-1324; LYS-1380; LYS-1392; RP LYS-1395; LYS-1454; LYS-1486; LYS-1504; LYS-1585; LYS-1737 AND LYS-1864, RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-37 (ISOFORM 2), AND RP 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: RNA-binding protein. Specifically binds to 5'-GGGGCC-3' CC sequence repeats in RNA. Essential for maintenance of peripheral motor CC neuron and skeletal muscle function. Required for normal expression CC and/or alternative splicing of a number of genes in spinal cord and CC skeletal muscle, including the neurite outgrowth inhibitor RTN4. Also CC contributes to normal mitochondrial respiratory function in motor CC neurons, via an unknown mechanism. {ECO:0000250|UniProtKB:O88466}. CC -!- SUBUNIT: Interacts with KNOP1. Interacts with TARDBP and NUP107. CC Interacts (via N-terminus) with RBM39. Interacts with the SH3 domains CC of FYN and GRB2. {ECO:0000250|UniProtKB:O88466}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus CC {ECO:0000250|UniProtKB:O88466}. Nucleus speckle CC {ECO:0000250|UniProtKB:O88466}. Note=Colocalizes with RBM39 in nuclear CC speckles. Inhibition of RNA synthesis, or overexpression of KNOP1, CC induces translocation from nuclear speckles to the nucleolus. CC {ECO:0000250|UniProtKB:O88466}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9H2Y7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H2Y7-2; Sequence=VSP_057120, VSP_057121; CC -!- PTM: Phosphorylated by FYN in vitro. {ECO:0000250|UniProtKB:O88466}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH58023.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH70244.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAB14976.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAD91134.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AF205632; AAG35666.1; -; mRNA. DR EMBL; AF209502; AAL40184.1; -; Genomic_DNA. DR EMBL; AK024726; BAB14976.1; ALT_INIT; mRNA. DR EMBL; AK057410; BAB71475.1; -; mRNA. DR EMBL; AK302735; BAG63952.1; -; mRNA. DR EMBL; AC012651; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC018362; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC058023; AAH58023.1; ALT_SEQ; mRNA. DR EMBL; BC070244; AAH70244.1; ALT_SEQ; mRNA. DR EMBL; AL832455; CAD89926.1; -; mRNA. DR EMBL; AL831983; CAD91134.1; ALT_INIT; mRNA. DR EMBL; AL833301; CAD91142.1; -; mRNA. DR EMBL; AL832014; CAD91147.1; -; mRNA. DR EMBL; AL832352; CAD91149.1; -; mRNA. DR CCDS; CCDS32208.1; -. [Q9H2Y7-1] DR CCDS; CCDS61603.1; -. [Q9H2Y7-2] DR RefSeq; NP_001271235.1; NM_001284306.1. DR RefSeq; NP_001271236.1; NM_001284307.1. [Q9H2Y7-2] DR RefSeq; NP_071918.1; NM_022473.2. [Q9H2Y7-1] DR AlphaFoldDB; Q9H2Y7; -. DR SMR; Q9H2Y7; -. DR BioGRID; 122154; 80. DR IntAct; Q9H2Y7; 40. DR MINT; Q9H2Y7; -. DR STRING; 9606.ENSP00000263805; -. DR GlyCosmos; Q9H2Y7; 1 site, 1 glycan. DR GlyGen; Q9H2Y7; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q9H2Y7; -. DR PhosphoSitePlus; Q9H2Y7; -. DR SwissPalm; Q9H2Y7; -. DR BioMuta; ZNF106; -. DR DMDM; 51702191; -. DR EPD; Q9H2Y7; -. DR jPOST; Q9H2Y7; -. DR MassIVE; Q9H2Y7; -. DR MaxQB; Q9H2Y7; -. DR PaxDb; 9606-ENSP00000263805; -. DR PeptideAtlas; Q9H2Y7; -. DR ProteomicsDB; 19800; -. DR ProteomicsDB; 80634; -. [Q9H2Y7-1] DR Pumba; Q9H2Y7; -. DR Antibodypedia; 10821; 135 antibodies from 24 providers. DR DNASU; 64397; -. DR Ensembl; ENST00000263805.8; ENSP00000263805.4; ENSG00000103994.18. [Q9H2Y7-1] DR Ensembl; ENST00000565380.5; ENSP00000455674.1; ENSG00000103994.18. [Q9H2Y7-2] DR GeneID; 64397; -. DR KEGG; hsa:64397; -. DR UCSC; uc001zpv.5; human. [Q9H2Y7-1] DR AGR; HGNC:12886; -. DR CTD; 64397; -. DR DisGeNET; 64397; -. DR GeneCards; ZNF106; -. DR HGNC; HGNC:12886; ZNF106. DR HPA; ENSG00000103994; Group enriched (heart muscle, skeletal muscle, tongue). DR neXtProt; NX_Q9H2Y7; -. DR OpenTargets; ENSG00000103994; -. DR PharmGKB; PA166048944; -. DR VEuPathDB; HostDB:ENSG00000103994; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000157336; -. DR HOGENOM; CLU_001566_0_0_1; -. DR InParanoid; Q9H2Y7; -. DR OrthoDB; 3032887at2759; -. DR PhylomeDB; Q9H2Y7; -. DR TreeFam; TF105569; -. DR PathwayCommons; Q9H2Y7; -. DR SignaLink; Q9H2Y7; -. DR BioGRID-ORCS; 64397; 23 hits in 1163 CRISPR screens. DR ChiTaRS; ZNF106; human. DR GeneWiki; ZFP106; -. DR GenomeRNAi; 64397; -. DR Pharos; Q9H2Y7; Tbio. DR PRO; PR:Q9H2Y7; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q9H2Y7; Protein. DR Bgee; ENSG00000103994; Expressed in skeletal muscle tissue of rectus abdominis and 206 other cell types or tissues. DR ExpressionAtlas; Q9H2Y7; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central. DR GO; GO:0008286; P:insulin receptor signaling pathway; IBA:GO_Central. DR CDD; cd00200; WD40; 1. DR DisProt; DP02007; -. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR InterPro; IPR042622; Znf106. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR14435; ZINC FINGER PROTEIN 106; 1. DR PANTHER; PTHR14435:SF2; ZINC FINGER PROTEIN 106; 1. DR Pfam; PF00400; WD40; 4. DR SMART; SM00320; WD40; 6. DR SMART; SM00355; ZnF_C2H2; 3. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50082; WD_REPEATS_2; 2. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR Genevisible; Q9H2Y7; HS. PE 1: Evidence at protein level; KW Alternative splicing; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; WD repeat; KW Zinc; Zinc-finger. FT CHAIN 1..1883 FT /note="Zinc finger protein 106" FT /id="PRO_0000051467" FT REPEAT 1529..1568 FT /note="WD 1" FT REPEAT 1570..1611 FT /note="WD 2" FT REPEAT 1654..1695 FT /note="WD 3" FT REPEAT 1698..1737 FT /note="WD 4" FT REPEAT 1738..1775 FT /note="WD 5" FT REPEAT 1778..1815 FT /note="WD 6" FT ZN_FING 20..44 FT /note="C2H2-type 1; atypical" FT ZN_FING 1813..1838 FT /note="C2H2-type 2; atypical" FT REGION 39..162 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 322..356 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 389..423 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 457..501 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 586..637 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 879..945 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 958..982 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 997..1048 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1121..1143 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1182..1218 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1252..1483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1502..1527 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 69..86 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 97..113 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 126..142 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 322..338 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 458..497 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 586..600 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 601..618 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 619..635 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 882..910 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1258..1272 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1273..1316 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1402..1421 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1440..1454 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1455..1483 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 422 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 590 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 641 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 661 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 859 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 861 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 864 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 893 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 937 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1021 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1025 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1026 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1031 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1249 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1279 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1281 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O88466" FT MOD_RES 1284 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1302 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1328 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1370 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1372 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1468 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 69 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 76 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 133 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 243 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 287 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 305 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 356 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 365 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 371 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 417 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 451 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 461 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 477 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 492 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 505 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 515 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 525 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 539 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 557 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 603 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 671 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 684 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 705 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 721 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 741 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 775 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 807 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 905 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 911 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 953 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1265 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 1299 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1324 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1380 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1392 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1395 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1454 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1486 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1504 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1585 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1737 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 1864 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..38 FT /note="MPVGRIECPSSPSFPRDISHECRVCGVTEVGLSAYAKH -> MVRERKCILC FT HIVYSSKKEMDEHMRSMLHHRELENLKG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057120" FT VAR_SEQ 39..810 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057121" FT VARIANT 103 FT /note="W -> R (in dbSNP:rs12440118)" FT /id="VAR_053440" FT VARIANT 646 FT /note="I -> T (in dbSNP:rs12101559)" FT /id="VAR_053441" FT VARIANT 656 FT /note="M -> V (in dbSNP:rs34792942)" FT /id="VAR_053442" FT VARIANT 1162 FT /note="P -> T (in dbSNP:rs34983340)" FT /id="VAR_053443" FT CONFLICT 475 FT /note="N -> D (in Ref. 2; BAB71475)" FT /evidence="ECO:0000305" FT CONFLICT 680 FT /note="D -> G (in Ref. 5; CAD91147)" FT /evidence="ECO:0000305" FT CONFLICT 757 FT /note="I -> V (in Ref. 2; BAB71475)" FT /evidence="ECO:0000305" FT CONFLICT 1293 FT /note="E -> G (in Ref. 5; CAD91142)" FT /evidence="ECO:0000305" FT CONFLICT 1509 FT /note="S -> P (in Ref. 2; BAG63952)" FT /evidence="ECO:0000305" FT CONFLICT 1606 FT /note="R -> L (in Ref. 2; BAB14976)" FT /evidence="ECO:0000305" FT CROSSLNK Q9H2Y7-2:6 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK Q9H2Y7-2:37 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" SQ SEQUENCE 1883 AA; 208883 MW; 7D1CBD6193F8888C CRC64; MPVGRIECPS SPSFPRDISH ECRVCGVTEV GLSAYAKHIS GQLHKDNVDA QEREDDGKGE EEEEDYFDKE LIQLIKQRKE QSRQDEPSNS NQEINSDDRR PQWRREDRIP YQDRESYSQP AWHHRGPPQR DWKWEKDGFN NTRKNSFPHS LRNGGGPRGR SGWHKGVAGG SSTWFHNHSN SGGGWLSNSG AVDWNHNGTG RNSSWLSEGT GGFSSWHMNN SNGNWKSSVR STNNWNYSGP GDKFQPGRNR NSNCQMEDMT MLWNKKSNKS NKYSHDRYNW QRQENDKLGT VATYRGPSEG FTSDKFPSEG LLDFNFEQLE SQTTKQADTA TSKVSGKNGS AAREKPRRWT PYPSQKTLDL QSGLKDITGN KSEMIEKPLF DFSLITTGIQ EPQTDETRNS PTQKTQKEIH TGSLNHKASS DSAASFEVVR QCPTAEKPEQ EHTPNKMPSL KSPLLPCPAT KSLSQKQDPK NISKNTKTNF FSPGEHSNPS NKPTVEDNHG PYISKLRSSC PHVLKGNKST FGSQKQSGDN LNDTLRKAKE VLQCHESLQN PLLSTSKSTR NYAKASRNVE ESEKGSLKIE FQVHALEDES DGETSDTEKH GTKIGTLGSA TTELLSGSTR TADEKEEDDR ILKTSRELST SPCNPIVRQK ESELQMTSAA SPHPGLLLDL KTSLEDAQVD DSIKSHVSYE TEGFESASLD AELQKSDISQ PSGPLLPELS KLGFPASLQR DLTRHISLKS KTGVHLPEPN LNSARRIRNI SGHRKSETEK ESGLKPTLRQ ILNASRRNVN WEQVIQQVTK KKQELGKGLP RFGIEMVPLV QNEQEALDLD GEPDLSSLEG FQWEGVSISS SPGLARKRSL SESSVIMDRA PSVYSFFSEE GTGKENEPQQ MVSPSNSLRA GQSQKATMHL KQEVTPRAAS LRTGERAENV ATQRRHSAQL SSDHIIPLMH LAKDLNSQER SIPPSENQNS QESNGEGNCL SSSASSALAI SSLADAATDS SCTSGAEQND GQSIRKKRRA TGDGSSPELP SLERKNKRRK IKGKKERSQV DQLLNISLRE EELSKSLQCM DNNLLQARAA LQTAYVEVQR LLMLKQQITM EMSALRTHRI QILQGLQETY EPSEHPDQVP CSLTRERRNS RSQTSIDAAL LPTPFFPLFL EPPSSHVSPS PTGASLQITT SPTFQTHGSV PAPDSSVQIK QEPMSPEQDE NVNAVPPSSA CNVSKELLEA NREISDSCPV YPVITARLSL PESTESFHEP SQELKFSVEQ RNTRNRENSP SSQSAGLSSI NKEGEEPTKG NSGSEACTSS FLRLSFASET PLEKEPHSPA DQPEQQAEST LTSAETRGSK KKKKLRKKKS LRAAHVPENS DTEQDVLTVK PVRKVKAGKL IKGGKVTTST WEDSRTGREQ ESVRDEPDSD SSLEVLEIPN PQLEVVAIDS SESGEEKPDS PSKKDIWNST EQNPLETSRS GCDEVSSTSE IGTRYKDGIP VSVAETQTVI SSIKGSKNSS EISSEPGDDD EPTEGSFEGH QAAVNAIQIF GNLLYTCSAD KTVRVYNLVS RKCIGVFEGH TSKVNCLLVT QTSGKNAALY TGSSDHTIRC YNVKSRECVE QLQLEDRVLC LHSRWRILYA GLANGTVVTF NIKNNKRLEI FECHGPRAVS CLATAQEGAR KLLVVGSYDC TISVRDARNG LLLRTLEGHS KTILCMKVVN DLVFSGSSDQ SVHAHNIHTG ELVRIYKGHN HAVTVVNILG KVMVTACLDK FVRVYELQSH DRLQVYGGHK DMIMCMTIHK SMIYTGCYDG SIQAVRLNLM QNYRCWWHGC SLIFGVVDHL KQHLLTDHTN PNFQTLKCRW KNCDAFFTAR KGSKQDAAGH IERHAEDDSK IDS //