SNIP1_RAT
ID SNIP1_RAT Reviewed; 389 AA.
AC Q5M9G6;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Smad nuclear interacting protein 1;
GN Name=Snip1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-48; SER-95 AND
RP SER-149, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC087118; AAH87118.1; -; mRNA.
DR RefSeq; NP_001014091.1; NM_001014069.1.
DR RefSeq; XP_017449307.1; XM_017593818.1.
DR RefSeq; XP_017458578.1; XM_017603089.1.
DR AlphaFoldDB; Q5M9G6; -.
DR SMR; Q5M9G6; -.
DR STRING; 10116.ENSRNOP00000030728; -.
DR iPTMnet; Q5M9G6; -.
DR PhosphoSitePlus; Q5M9G6; -.
DR PaxDb; Q5M9G6; -.
DR PRIDE; Q5M9G6; -.
DR Ensembl; ENSRNOT00000037510; ENSRNOP00000030728; ENSRNOG00000024889.
DR GeneID; 313588; -.
DR KEGG; rno:313588; -.
DR UCSC; RGD:1359268; rat.
DR CTD; 79753; -.
DR RGD; 1359268; Snip1.
DR eggNOG; KOG1882; Eukaryota.
DR GeneTree; ENSGT00940000156553; -.
DR HOGENOM; CLU_022457_2_0_1; -.
DR InParanoid; Q5M9G6; -.
DR OMA; MTKEKRH; -.
DR OrthoDB; 955935at2759; -.
DR PhylomeDB; Q5M9G6; -.
DR TreeFam; TF312797; -.
DR PRO; PR:Q5M9G6; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000024889; Expressed in testis and 12 other tissues.
DR Genevisible; Q5M9G6; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; ISO:RGD.
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; ISO:RGD.
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..389
FT /note="Smad nuclear interacting protein 1"
FT /id="PRO_0000391412"
FT DOMAIN 272..335
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 166..197
FT /evidence="ECO:0000255"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..98
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..389
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:22673903"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 386
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 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TAD8"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TAD8"
SQ SEQUENCE 389 AA; 44923 MW; 6FFD73E2CA7BBAC1 CRC64;
MKAGKSERER SSRRRHRSGD ALATVVVKQE RLSPEPVAHR RPDAPAASPP PPAAESGSAG
HRGSRARGAS RSPAKKKSKS SGRRSKSPRT KRSRSPHYST VKVKQEREDH PRRGREDRQH
RELSEQEHRR ARNSERDRHR GHARQRRSSD ERPVSGQGRD RDSQILQAQE EERDFNNARR
REHRQQNESA GAEAQEVIPR PAGNKNKEVP VKEKPSFELS GALLEDTNTF RGVVIKYSEP
PEARIPKKRW RLYPFKNDEV LPVMYIHRQS AYLLGRHRRI ADIPIDHPSC SKQHAVFQYR
LVEYTRADGT VGRRVKPYII DLGSGNGTFL NNKRIEPQRY YELKEKDVLK FGFSSREYVL
LHESSDTSEL DRKEDEDEEE EEEMVSDSS
