SNIP1_HUMAN
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 03-AUG-2022, entry version 168.
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]
RP VARIANT PMRED 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). Down-regulates NF-kappa-B signaling by
CC competing with RELA for CREBBP/EP300 binding. Involved in the microRNA
CC (miRNA) biogenesis. May be involved in cyclin-D1/CCND1 mRNA stability
CC through the SNARP complex which associates with both the 3'end of the
CC CCND1 gene and its mRNA. {ECO:0000269|PubMed:11567019,
CC ECO:0000269|PubMed:15378006, ECO:0000269|PubMed:18632581,
CC ECO:0000269|PubMed:18794151, ECO:0000269|PubMed:29360106}.
CC -!- SUBUNIT: Component of activated spliceosome complexes
CC (PubMed:29360106). Binds SMAD4 and CREBBP/EP300. Binds the
CC SMAD1/OAZ1/PSMB4 complex. Interacts with DROSHA and SMARCA4. Component
CC of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3,
CC 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 -!- 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: Psychomotor retardation, epilepsy, and craniofacial
CC dysmorphism (PMRED) [MIM:614501]: A disease characterized by severe
CC psychomotor retardation, intractable seizures, dysmorphic features, and
CC a lumpy skull surface. Patients are hypotonic and have poor feeding in
CC the neonatal period. {ECO:0000269|PubMed:22279524}. Note=The disease is
CC caused by variants 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 SMR; Q8TAD8; -.
DR BioGRID; 122864; 373.
DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex.
DR DIP; DIP-38956N; -.
DR IntAct; Q8TAD8; 108.
DR MINT; Q8TAD8; -.
DR STRING; 9606.ENSP00000296215; -.
DR MoonDB; Q8TAD8; Predicted.
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; Q8TAD8; -.
DR PeptideAtlas; Q8TAD8; -.
DR PRIDE; Q8TAD8; -.
DR ProteomicsDB; 73865; -.
DR Antibodypedia; 17552; 173 antibodies from 24 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 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; MTKEKRH; -.
DR OrthoDB; 955935at2759; -.
DR PhylomeDB; Q8TAD8; -.
DR TreeFam; TF312797; -.
DR PathwayCommons; Q8TAD8; -.
DR SignaLink; Q8TAD8; -.
DR SIGNOR; Q8TAD8; -.
DR BioGRID-ORCS; 79753; 470 hits in 1090 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 173 other tissues.
DR ExpressionAtlas; Q8TAD8; baseline and differential.
DR Genevisible; Q8TAD8; HS.
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; IC:ComplexPortal.
DR GO; GO:0005686; C:U2 snRNP; IC: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:0007249; P:I-kappaB kinase/NF-kappaB signaling; 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:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
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 PMRED; 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
