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 05-OCT-2010, entry version 70. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 MEDLINE=20347038; 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- RT dependent 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 RT project: 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., RA Duckett C.S., Perkins N.D., Roberts A.B.; RT "SNIP1 inhibits NF-kappa B signaling by competing for its binding to RT the 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 RT transduction pathway of the bone morphogenetic proteins (BMPs)."; RL BMC Cell Biol. 3:15-15(2002). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-89; SER-91 AND RP SER-153, AND MASS SPECTROMETRY. 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [7] 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169 AND SER-202, AND RP MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=19007248; DOI=10.1021/ac801708p; RA Wang B., Malik R., Nigg E.A., Korner R.; RT "Evaluation of the low-specificity protease elastase for large-scale RT phosphoproteome analysis."; RL Anal. Chem. 80:9526-9533(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND MASS RP SPECTROMETRY. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using RT sequential IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [12] RP FUNCTION, AND INTERACTION WITH RNASEN. RX PubMed=18632581; DOI=10.1073/pnas.0804218105; RA Yu B., Bi L., Zheng B., Ji L., Chevalier D., Agarwal M., RA Ramachandran V., Li W., Lagrange T., Walker J.C., Chen X.; RT "The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act RT in small RNA biogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10073-10078(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-49; SER-52 AND RP SER-54, AND MASS SPECTROMETRY. 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-54, AND MASS RP SPECTROMETRY. 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). CC -!- FUNCTION: Down-regulates NF-kappa-B signaling by competing with CC RELA for CREBBP/EP300 binding. Involved in the microRNA (miRNA) CC biogenesis. CC -!- SUBUNIT: Binds SMAD4 and CREBBP/EP300. Binds the SMAD1/OAZ1/PSMB4 CC complex. Interacts with RNASEN. CC -!- INTERACTION: CC P61244:MAX; NbExp=1; IntAct=EBI-749336, EBI-878388; CC P01106:MYC; NbExp=5; IntAct=EBI-749336, EBI-447544; CC Q9NRR4:RNASEN; NbExp=1; IntAct=EBI-749336, EBI-528367; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart CC and skeletal muscle. CC -!- PTM: Degraded by the proteasome upon binding to the CC SMAD1/OAZ1/PSMB4 complex. CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. CC -!- SIMILARITY: Contains 1 FHA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs 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 IPI; IPI00154515; -. DR RefSeq; NP_078976.2; -. DR UniGene; Hs.471951; -. DR ProteinModelPortal; Q8TAD8; -. DR SMR; Q8TAD8; 236-370. DR DIP; DIP-38956N; -. DR IntAct; Q8TAD8; 15. DR MINT; MINT-1181692; -. DR STRING; Q8TAD8; -. DR PhosphoSite; Q8TAD8; -. DR PRIDE; Q8TAD8; -. DR Ensembl; ENST00000296215; ENSP00000296215; ENSG00000163877. DR GeneID; 79753; -. DR KEGG; hsa:79753; -. DR UCSC; uc001cbi.1; human. DR CTD; 79753; -. DR GeneCards; GC01M038002; -. DR H-InvDB; HIX0000434; -. DR HGNC; HGNC:30587; SNIP1. DR MIM; 608241; gene. DR PharmGKB; PA142670893; -. DR eggNOG; prNOG08408; -. DR HOGENOM; HBG717219; -. DR HOVERGEN; HBG056615; -. DR InParanoid; Q8TAD8; -. DR OMA; KQEREDH; -. DR OrthoDB; EOG9B2WH7; -. DR PhylomeDB; Q8TAD8; -. DR Pathway_Interaction_DB; smad2_3nuclearpathway; Regulation of nuclear SMAD2/3 signaling. DR NextBio; 69203; -. DR ArrayExpress; Q8TAD8; -. DR Bgee; Q8TAD8; -. DR CleanEx; HS_SNIP1; -. DR Genevestigator; Q8TAD8; -. DR GermOnline; ENSG00000163877; Homo sapiens. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0035196; P:production of miRNAs involved in gene silen...; IMP:UniProtKB. DR InterPro; IPR000253; FHA_dom. DR InterPro; IPR008984; SMAD_FHA_domain. DR Gene3D; G3DSA:2.60.200.20; FHA; 1. DR Pfam; PF00498; FHA; 1. DR SMART; SM00240; FHA; 1. DR SUPFAM; SSF49879; SMAD_FHA; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. PE 1: Evidence at protein level; KW Coiled coil; Complete proteome; Isopeptide bond; Nucleus; KW Phosphoprotein; RNA-mediated gene silencing; Ubl conjugation. FT CHAIN 1 396 Smad nuclear-interacting protein 1. FT /FTId=PRO_0000072009. FT DOMAIN 281 344 FHA. FT COILED 165 196 Potential. FT COMPBIAS 62 192 Arg-rich. FT COMPBIAS 385 392 Poly-Glu. FT MOD_RES 35 35 Phosphoserine. FT MOD_RES 49 49 Phosphoserine. FT MOD_RES 52 52 Phosphoserine. FT MOD_RES 54 54 Phosphoserine. FT MOD_RES 89 89 Phosphoserine. FT MOD_RES 91 91 Phosphoserine. FT MOD_RES 153 153 Phosphoserine. FT MOD_RES 169 169 Phosphothreonine. FT MOD_RES 202 202 Phosphoserine. FT MOD_RES 394 394 Phosphoserine. FT CROSSLNK 30 30 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT MUTAGEN 30 30 K->R: Abolishes sumoylation. FT CONFLICT 181 181 F -> S (in Ref. 2; BAB55241). FT CONFLICT 364 364 S -> I (in Ref. 2; BAB14134). 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 //