SNIP1_MOUSE
ID SNIP1_MOUSE Reviewed; 383 AA.
AC Q8BIZ6; Q3V106; Q8BIZ4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Smad nuclear-interacting protein 1;
GN Name=Snip1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, Spleen, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-48 AND SER-50, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome. Down-regulates NF-kappa-B signaling by competing with RELA
CC for CREBBP/EP300 binding. Involved in the microRNA (miRNA) biogenesis.
CC May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP
CC complex which associates with both the 3'end of the CCND1 gene and its
CC mRNA. {ECO:0000250|UniProtKB:Q8TAD8}.
CC -!- SUBUNIT: Component of activated spliceosome complexes. Binds SMAD4 and
CC CREBBP/EP300. Binds the SMAD1/OAZ1/PSMB4 complex. Interacts with DROSHA
CC and SMARCA4. Component of the SNARP complex which consists at least of
CC SNIP1, SNW1, THRAP3, BCLAF1 and PNN. {ECO:0000250|UniProtKB:Q8TAD8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TAD8}.
CC -!- PTM: Degraded by the proteasome upon binding to the SMAD1/OAZ1/PSMB4
CC complex. {ECO:0000250}.
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DR EMBL; AK040571; BAE20582.1; -; mRNA.
DR EMBL; AK049254; BAC33638.1; -; mRNA.
DR EMBL; AK049318; BAC33680.1; -; mRNA.
DR EMBL; AK132768; BAE21347.1; -; mRNA.
DR EMBL; AK143801; BAE25543.1; -; mRNA.
DR EMBL; BC064067; AAH64067.1; -; mRNA.
DR CCDS; CCDS18636.1; -.
DR RefSeq; NP_780455.2; NM_175246.4.
DR AlphaFoldDB; Q8BIZ6; -.
DR SMR; Q8BIZ6; -.
DR BioGRID; 218318; 2.
DR IntAct; Q8BIZ6; 1.
DR STRING; 10090.ENSMUSP00000060721; -.
DR iPTMnet; Q8BIZ6; -.
DR PhosphoSitePlus; Q8BIZ6; -.
DR EPD; Q8BIZ6; -.
DR jPOST; Q8BIZ6; -.
DR MaxQB; Q8BIZ6; -.
DR PaxDb; Q8BIZ6; -.
DR PeptideAtlas; Q8BIZ6; -.
DR PRIDE; Q8BIZ6; -.
DR ProteomicsDB; 261291; -.
DR Antibodypedia; 17552; 173 antibodies from 24 providers.
DR DNASU; 76793; -.
DR Ensembl; ENSMUST00000052183; ENSMUSP00000060721; ENSMUSG00000050213.
DR GeneID; 76793; -.
DR KEGG; mmu:76793; -.
DR UCSC; uc008urq.2; mouse.
DR CTD; 79753; -.
DR MGI; MGI:2156003; Snip1.
DR VEuPathDB; HostDB:ENSMUSG00000050213; -.
DR eggNOG; KOG1882; Eukaryota.
DR GeneTree; ENSGT00940000156553; -.
DR HOGENOM; CLU_022457_2_0_1; -.
DR InParanoid; Q8BIZ6; -.
DR OMA; MTKEKRH; -.
DR OrthoDB; 955935at2759; -.
DR PhylomeDB; Q8BIZ6; -.
DR TreeFam; TF312797; -.
DR BioGRID-ORCS; 76793; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Snip1; mouse.
DR PRO; PR:Q8BIZ6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BIZ6; protein.
DR Bgee; ENSMUSG00000050213; Expressed in spermatocyte and 265 other tissues.
DR Genevisible; Q8BIZ6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0035196; P:miRNA processing; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
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 Coiled coil; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-mediated gene silencing;
KW Spliceosome; Ubl conjugation.
FT CHAIN 1..383
FT /note="Smad nuclear-interacting protein 1"
FT /id="PRO_0000072010"
FT DOMAIN 268..331
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..194
FT /evidence="ECO:0000255"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..87
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..383
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TAD8"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M9G6"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M9G6"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TAD8"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8TAD8"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8TAD8"
FT CROSSLNK 100
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TAD8"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TAD8"
FT CONFLICT 223
FT /note="T -> P (in Ref. 1; BAC33680)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 44415 MW; 0ADD646D4CB952BE CRC64;
MKAGKSERER SGRRRHRSGD ALTTVVVKQE RLSPEPVAHR RPDAPAASLS PPAAEPGHSG
HRGSRARSPA KKKSKSSGRR SKSPRTKRSQ SPHYPMVKVK QEREDHPRRG REDRQHREPS
EQEHRRARNS ERDRHRGHSR QGRSSDERPV SGQDRDRDSQ NLQAQEEERD FHNARRREHR
QQNESAGSEA QEVIPRPAGN RSKEVPVKEK PSFELSGALL EDTNTFRGVV IKYSEPPEAR
IPKKRWRLYP FKNDEVLPVM YIHRQSAYLL GRHRRIADIP IDHPSCSKQH AVFQYRLVEY
TRADGTVGRR VKPYIIDLGS GNGTFLNNKR IEPQRYYELK EKDVLKFGFS SREYVLLHES
SDTSELDRKE DEDDEEEEMV SDS
