ID SNIP1_HUMAN Reviewed; 396 AA. AC Q8TAD8; Q96SP9; Q9H9T7; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 177. DE RecName: Full=Smad nuclear-interacting protein 1; DE AltName: Full=FHA domain-containing protein SNIP1; GN Name=SNIP1; 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], INTERACTION WITH SMAD4 AND CREBBP/EP300, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Embryonic kidney; RX PubMed=10887155; RA Kim R.H., Wang D., Tsang M., Martin J., Huff C., de Caestecker M.P., RA Parks T.W., Meng X., Lechleider R.J., Wang T., Roberts A.B.; RT "A novel Smad nuclear interacting protein, SNIP1, suppresses p300-dependent RT TGF-beta signal transduction."; RL Genes Dev. 14:1605-1616(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Teratocarcinoma; 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 MRNA]. RC TISSUE=Testis; 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 FUNCTION, AND INTERACTION WITH CREBBP AND EP300. RX PubMed=11567019; DOI=10.1074/jbc.m103819200; RA Kim R.H., Flanders K.C., Birkey Reffey S., Anderson L.A., Duckett C.S., RA Perkins N.D., Roberts A.B.; RT "SNIP1 inhibits NF-kappa B signaling by competing for its binding to the RT C/H1 domain of CBP/p300 transcriptional co-activators."; RL J. Biol. Chem. 276:46297-46304(2001). RN [5] RP INTERACTION WITH THE SMAD1/OAZ1/PSMB4 COMPLEX, AND DEGRADATION BY THE RP PROTEASOME. RX PubMed=12097147; DOI=10.1186/1471-2121-3-15; RA Lin Y., Martin J., Gruendler C., Farley J., Meng X., Li B.-Y., RA Lechleider R., Huff C., Kim R.H., Grasser W.A., Paralkar V., Wang T.; RT "A novel link between the proteasome pathway and the signal transduction RT pathway of the bone morphogenetic proteins (BMPs)."; RL BMC Cell Biol. 3:15-15(2002). RN [6] RP FUNCTION, AND INTERACTION WITH SMARCA4. RX PubMed=15378006; DOI=10.1038/sj.onc.1208025; RA Roche K.C., Wiechens N., Owen-Hughes T., Perkins N.D.; RT "The FHA domain protein SNIP1 is a regulator of the cell cycle and cyclin RT D1 expression."; RL Oncogene 23:8185-8195(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY RP 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 [8] RP SUMOYLATION AT LYS-30, AND MUTAGENESIS OF LYS-30. RX PubMed=16371476; DOI=10.1073/pnas.0503698102; RA Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J., RA Nakai A., Sistonen L.; RT "PDSM, a motif for phosphorylation-dependent SUMO modification."; RL Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006). RN [9] RP FUNCTION, AND IDENTIFICATION IN THE SNARP COMPLEX. RX PubMed=18794151; DOI=10.1158/0008-5472.can-08-1217; RA Bracken C.P., Wall S.J., Barre B., Panov K.I., Ajuh P.M., Perkins N.D.; RT "Regulation of cyclin D1 RNA stability by SNIP1."; RL Cancer Res. 68:7621-7628(2008). RN [10] RP FUNCTION, AND INTERACTION WITH DROSHA. RX PubMed=18632581; DOI=10.1073/pnas.0804218105; RA Yu B., Bi L., Zheng B., Ji L., Chevalier D., Agarwal M., Ramachandran V., RA Li W., Lagrange T., Walker J.C., Chen X.; RT "The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act in RT small RNA biogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10073-10078(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-52 AND SER-54, 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY RP MASS SPECTROMETRY [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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-394, AND RP IDENTIFICATION BY MASS 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-54, AND RP IDENTIFICATION BY 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-52; SER-54; THR-57; RP SER-58 AND SER-202, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-54, AND 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 [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-30, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-30, 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 [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-30 AND LYS-108, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-30 AND LYS-108, AND RP 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 [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-108 AND LYS-223, 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). RN [23] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z57, ECO:0007744|PDB:5Z58} RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=29360106; DOI=10.1038/cr.2018.14; RA Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.; RT "Structure of the human activated spliceosome in three conformational RT states."; RL Cell Res. 28:307-322(2018). RN [24] {ECO:0007744|PDB:7DVQ} RP STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS), AND SUBUNIT. RX PubMed=33509932; DOI=10.1126/science.abg0879; RA Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.; RT "Structure of the activated human minor spliceosome."; RL Science 371:0-0(2021). RN [25] RP VARIANT NEDHCS GLY-366. RX PubMed=22279524; DOI=10.1371/journal.pone.0028936; RA Puffenberger E.G., Jinks R.N., Sougnez C., Cibulskis K., Willert R.A., RA Achilly N.P., Cassidy R.P., Fiorentini C.J., Heiken K.F., Lawrence J.J., RA Mahoney M.H., Miller C.J., Nair D.T., Politi K.A., Worcester K.N., RA Setton R.A., Dipiazza R., Sherman E.A., Eastman J.T., Francklyn C., RA Robey-Bond S., Rider N.L., Gabriel S., Morton D.H., Strauss K.A.; RT "Genetic mapping and exome sequencing identify variants associated with RT five novel diseases."; RL PLoS ONE 7:E28936-E28936(2012). CC -!- FUNCTION: Required for pre-mRNA splicing as component of the CC spliceosome (PubMed:29360106). As a component of the minor spliceosome, CC involved in the splicing of U12-type introns in pre-mRNAs (Probable). CC Down-regulates NF-kappa-B signaling by competing with RELA for CC CREBBP/EP300 binding. Involved in the microRNA (miRNA) biogenesis. May CC be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex CC which associates with both the 3'end of the CCND1 gene and its mRNA. CC {ECO:0000269|PubMed:11567019, ECO:0000269|PubMed:15378006, CC ECO:0000269|PubMed:18632581, ECO:0000269|PubMed:18794151, CC ECO:0000269|PubMed:29360106, ECO:0000305|PubMed:33509932}. CC -!- SUBUNIT: Component of activated spliceosome complexes CC (PubMed:29360106). Component of the minor spliceosome, which splices CC U12-type introns (PubMed:33509932). Binds SMAD4 and CREBBP/EP300. Binds CC the SMAD1/OAZ1/PSMB4 complex. Interacts with DROSHA and SMARCA4. CC Component of the SNARP complex which consists at least of SNIP1, SNW1, CC THRAP3, BCLAF1 and PNN. {ECO:0000269|PubMed:10887155, CC ECO:0000269|PubMed:11567019, ECO:0000269|PubMed:12097147, CC ECO:0000269|PubMed:15378006, ECO:0000269|PubMed:18632581, CC ECO:0000269|PubMed:18794151, ECO:0000269|PubMed:29360106, CC ECO:0000269|PubMed:33509932}. CC -!- INTERACTION: CC Q8TAD8; P49760: CLK2; NbExp=8; IntAct=EBI-749336, EBI-750020; CC Q8TAD8; P49761: CLK3; NbExp=3; IntAct=EBI-749336, EBI-745579; CC Q8TAD8; Q92997: DVL3; NbExp=3; IntAct=EBI-749336, EBI-739789; CC Q8TAD8; P62508-3: ESRRG; NbExp=3; IntAct=EBI-749336, EBI-12001340; CC Q8TAD8; P13807: GYS1; NbExp=3; IntAct=EBI-749336, EBI-740553; CC Q8TAD8; Q13123: IK; NbExp=2; IntAct=EBI-749336, EBI-713456; CC Q8TAD8; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-749336, EBI-12012928; CC Q8TAD8; P55081: MFAP1; NbExp=4; IntAct=EBI-749336, EBI-1048159; CC Q8TAD8; P01106: MYC; NbExp=9; IntAct=EBI-749336, EBI-447544; CC Q8TAD8; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-749336, EBI-2339674; CC Q8TAD8; P14859-6: POU2F1; NbExp=3; IntAct=EBI-749336, EBI-11526590; CC Q8TAD8; Q13573: SNW1; NbExp=8; IntAct=EBI-749336, EBI-632715; CC Q8TAD8; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-749336, EBI-12023934; CC Q8TAD8; P78362: SRPK2; NbExp=4; IntAct=EBI-749336, EBI-593303; CC Q8TAD8; A7MD48: SRRM4; NbExp=6; IntAct=EBI-749336, EBI-3867173; CC Q8TAD8; Q13188: STK3; NbExp=3; IntAct=EBI-749336, EBI-992580; CC Q8TAD8; Q15025: TNIP1; NbExp=4; IntAct=EBI-749336, EBI-357849; CC Q8TAD8; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-749336, EBI-947459; CC Q8TAD8; Q96C00: ZBTB9; NbExp=6; IntAct=EBI-749336, EBI-395708; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10887155, CC ECO:0000269|PubMed:29360106}. CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart and CC skeletal muscle. {ECO:0000269|PubMed:10887155}. CC -!- PTM: Degraded by the proteasome upon binding to the SMAD1/OAZ1/PSMB4 CC complex. CC -!- DISEASE: Neurodevelopmental disorder with hypotonia, craniofacial CC abnormalities, and seizures (NEDHCS) [MIM:614501]: An autosomal CC recessive disease characterized by severe psychomotor retardation, CC intractable seizures, dysmorphic features, and a lumpy skull surface. CC Patients are hypotonic and have poor feeding in the neonatal period. CC {ECO:0000269|PubMed:22279524}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; AY081909; AAL91140.1; -; mRNA. DR EMBL; AK022615; BAB14134.1; -; mRNA. DR EMBL; AK027622; BAB55241.1; -; mRNA. DR EMBL; BC027040; AAH27040.1; -; mRNA. DR CCDS; CCDS419.1; -. DR RefSeq; NP_078976.2; NM_024700.3. DR PDB; 5Z56; EM; 5.10 A; X=1-396. DR PDB; 5Z57; EM; 6.50 A; X=1-396. DR PDB; 5Z58; EM; 4.90 A; X=1-396. DR PDB; 6FF7; EM; 4.50 A; 0=1-396. DR PDB; 7ABG; EM; 7.80 A; 0=1-396. DR PDB; 7ABH; EM; 4.50 A; 0=1-396. DR PDB; 7ABI; EM; 8.00 A; 0=1-396. DR PDB; 7DVQ; EM; 2.89 A; X=1-396. DR PDBsum; 5Z56; -. DR PDBsum; 5Z57; -. DR PDBsum; 5Z58; -. DR PDBsum; 6FF7; -. DR PDBsum; 7ABG; -. DR PDBsum; 7ABH; -. DR PDBsum; 7ABI; -. DR PDBsum; 7DVQ; -. DR AlphaFoldDB; Q8TAD8; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11696; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-30875; -. DR EMDB; EMD-6889; -. DR EMDB; EMD-6890; -. DR EMDB; EMD-6891; -. DR SMR; Q8TAD8; -. DR BioGRID; 122864; 409. DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-2653; SNIP1/SkIP associated RNA-processing complex. DR DIP; DIP-38956N; -. DR IntAct; Q8TAD8; 108. DR MINT; Q8TAD8; -. DR STRING; 9606.ENSP00000296215; -. DR MoonDB; Q8TAD8; Predicted. DR GlyGen; Q8TAD8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8TAD8; -. DR PhosphoSitePlus; Q8TAD8; -. DR BioMuta; SNIP1; -. DR DMDM; 48428655; -. DR EPD; Q8TAD8; -. DR jPOST; Q8TAD8; -. DR MassIVE; Q8TAD8; -. DR MaxQB; Q8TAD8; -. DR PaxDb; 9606-ENSP00000296215; -. DR PeptideAtlas; Q8TAD8; -. DR ProteomicsDB; 73865; -. DR Pumba; Q8TAD8; -. DR Antibodypedia; 17552; 190 antibodies from 25 providers. DR DNASU; 79753; -. DR Ensembl; ENST00000296215.8; ENSP00000296215.5; ENSG00000163877.11. DR GeneID; 79753; -. DR KEGG; hsa:79753; -. DR MANE-Select; ENST00000296215.8; ENSP00000296215.5; NM_024700.4; NP_078976.2. DR UCSC; uc001cbi.5; human. DR AGR; HGNC:30587; -. DR CTD; 79753; -. DR DisGeNET; 79753; -. DR GeneCards; SNIP1; -. DR HGNC; HGNC:30587; SNIP1. DR HPA; ENSG00000163877; Low tissue specificity. DR MalaCards; SNIP1; -. DR MIM; 608241; gene. DR MIM; 614501; phenotype. DR neXtProt; NX_Q8TAD8; -. DR OpenTargets; ENSG00000163877; -. DR PharmGKB; PA142670893; -. DR VEuPathDB; HostDB:ENSG00000163877; -. DR eggNOG; KOG1882; Eukaryota. DR GeneTree; ENSGT00940000156553; -. DR HOGENOM; CLU_022457_2_0_1; -. DR InParanoid; Q8TAD8; -. DR OMA; ALQFRYV; -. DR OrthoDB; 9299at2759; -. DR PhylomeDB; Q8TAD8; -. DR TreeFam; TF312797; -. DR PathwayCommons; Q8TAD8; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q8TAD8; -. DR SIGNOR; Q8TAD8; -. DR BioGRID-ORCS; 79753; 490 hits in 1168 CRISPR screens. DR ChiTaRS; SNIP1; human. DR GeneWiki; SNIP1; -. DR GenomeRNAi; 79753; -. DR Pharos; Q8TAD8; Tbio. DR PRO; PR:Q8TAD8; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8TAD8; Protein. DR Bgee; ENSG00000163877; Expressed in secondary oocyte and 174 other cell types or tissues. DR ExpressionAtlas; Q8TAD8; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; NAS:ComplexPortal. DR GO; GO:0005686; C:U2 snRNP; NAS:ComplexPortal. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0140416; F:transcription regulator inhibitor activity; IEA:Ensembl. DR GO; GO:0035196; P:miRNA processing; IMP:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl. DR GO; GO:1903241; P:U2-type prespliceosome assembly; NAS:ComplexPortal. DR CDD; cd22718; FHA_SNIP1; 1. DR Gene3D; 2.60.200.20; -; 1. DR InterPro; IPR000253; FHA_dom. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR PANTHER; PTHR23308:SF53; KANADAPTIN-RELATED; 1. DR PANTHER; PTHR23308; NUCLEAR INHIBITOR OF PROTEIN PHOSPHATASE-1; 1. DR Pfam; PF00498; FHA; 1. DR SMART; SM00240; FHA; 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. DR Genevisible; Q8TAD8; HS. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Disease variant; Epilepsy; Isopeptide bond; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; RNA-mediated gene silencing; Spliceosome; KW Ubl conjugation. FT CHAIN 1..396 FT /note="Smad nuclear-interacting protein 1" FT /id="PRO_0000072009" FT DOMAIN 281..344 FT /note="FHA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086" FT REGION 1..227 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 373..396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 165..196 FT /evidence="ECO:0000255" FT COMPBIAS 1..21 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 68..102 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 103..138 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 154..169 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 170..195 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 379..396 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 35 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 49 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 52 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 54 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 57 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5M9G6" FT MOD_RES 153 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5M9G6" FT MOD_RES 202 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 394 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT CROSSLNK 30 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT CROSSLNK 30 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 30 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" 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 108 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 223 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 366 FT /note="E -> G (in NEDHCS; dbSNP:rs387906986)" FT /evidence="ECO:0000269|PubMed:22279524" FT /id="VAR_067542" FT MUTAGEN 30 FT /note="K->R: Abolishes sumoylation." FT /evidence="ECO:0000269|PubMed:16371476" FT CONFLICT 181 FT /note="F -> S (in Ref. 2; BAB55241)" FT /evidence="ECO:0000305" FT CONFLICT 364 FT /note="S -> I (in Ref. 2; BAB14134)" FT /evidence="ECO:0000305" FT HELIX 230..233 FT /evidence="ECO:0007829|PDB:7DVQ" FT TURN 234..236 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 240..243 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 259..265 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 278..285 FT /evidence="ECO:0007829|PDB:7DVQ" FT TURN 287..289 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 304..314 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 320..330 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 357..360 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 366..371 FT /evidence="ECO:0007829|PDB:7DVQ" SQ SEQUENCE 396 AA; 45778 MW; B183F83EC3184676 CRC64; MKAVKSERER GSRRRHRDGD VVLPAGVVVK QERLSPEVAP PAHRRPDHSG GSPSPPTSEP ARSGHRGNRA RGVSRSPPKK KNKASGRRSK SPRSKRNRSP HHSTVKVKQE REDHPRRGRE DRQHREPSEQ EHRRARNSDR DRHRGHSHQR RTSNERPGSG QGQGRDRDTQ NLQAQEEERE FYNARRREHR QRNDVGGGGS ESQELVPRPG GNNKEKEVPA KEKPSFELSG ALLEDTNTFR GVVIKYSEPP EARIPKKRWR LYPFKNDEVL PVMYIHRQSA YLLGRHRRIA DIPIDHPSCS KQHAVFQYRL VEYTRADGTV GRRVKPYIID LGSGNGTFLN NKRIEPQRYY ELKEKDVLKF GFSSREYVLL HESSDTSEID RKDDEDEEEE EEVSDS //