INSM2_MOUSE
ID INSM2_MOUSE Reviewed; 493 AA.
AC Q9JMC2; E9QNA9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Insulinoma-associated protein 2;
DE AltName: Full=Methylated in liver tumor 1;
GN Name=Insm2; Synonyms=Mlt1;
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 [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Kidney;
RX PubMed=11221845;
RA Tateno M., Fukunishi Y., Komatsu S., Okazaki Y., Kawai J., Shibata K.,
RA Itoh M., Muramatsu M., Held W.A., Hayashizaki Y.;
RT "Identification of a novel member of the snail/Gfi-1 repressor family, mlt
RT 1, which is methylated and silenced in liver tumors of SV40 T antigen
RT transgenic mice.";
RL Cancer Res. 61:1144-1153(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=21343251; DOI=10.1210/en.2010-1065;
RA Cai T., Chen X., Wang R., Xu H., You Y., Zhang T., Lan M.S., Notkins A.L.;
RT "Expression of insulinoma-associated 2 (INSM2) in pancreatic islet cells is
RT regulated by the transcription factors Ngn3 and NeuroD1.";
RL Endocrinology 152:1961-1969(2011).
CC -!- FUNCTION: May function as a growth suppressor or tumor suppressor in
CC liver cells and in certain neurons. {ECO:0000269|PubMed:11221845}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21343251}. Nucleus
CC {ECO:0000269|PubMed:21343251}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, stomach, liver, kidney and
CC testis. In the pancreas, expressed in islet cells, including insulin-
CC producing beta-cells, but not in acinar cells (at protein level). In
CC the brain, expressed in the neuronal cells of the cerebral cortex, the
CC Purkinje cells of the cerebellum and the hippocampal region including
CC CA1 and CA3 (at protein level). {ECO:0000269|PubMed:11221845,
CC ECO:0000269|PubMed:21343251}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 6.5 to 18.5 dpc embryos and
CC transiently up-regulated from 11.5 to 13.5 dpc. In the developing
CC brain, up-regulated 2 weeks postnatally, with gradual decrease
CC thereafter. Still detectable at 52 weeks.
CC {ECO:0000269|PubMed:21343251}.
CC -!- INDUCTION: Up-regulated by NEUROG3 and NEUROD1.
CC {ECO:0000269|PubMed:21343251}.
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DR EMBL; AB032418; BAA92776.1; -; Genomic_DNA.
DR EMBL; AC158398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25919.1; -.
DR RefSeq; NP_064683.2; NM_020287.2.
DR AlphaFoldDB; Q9JMC2; -.
DR STRING; 10090.ENSMUSP00000061046; -.
DR PhosphoSitePlus; Q9JMC2; -.
DR MaxQB; Q9JMC2; -.
DR PaxDb; Q9JMC2; -.
DR PRIDE; Q9JMC2; -.
DR Antibodypedia; 23212; 77 antibodies from 19 providers.
DR DNASU; 56856; -.
DR Ensembl; ENSMUST00000051857; ENSMUSP00000061046; ENSMUSG00000045440.
DR GeneID; 56856; -.
DR KEGG; mmu:56856; -.
DR UCSC; uc007not.1; mouse.
DR CTD; 84684; -.
DR MGI; MGI:1930787; Insm2.
DR VEuPathDB; HostDB:ENSMUSG00000045440; -.
DR eggNOG; KOG3993; Eukaryota.
DR GeneTree; ENSGT00940000162391; -.
DR HOGENOM; CLU_033476_1_0_1; -.
DR InParanoid; Q9JMC2; -.
DR OMA; HLQARDS; -.
DR OrthoDB; 1306883at2759; -.
DR PhylomeDB; Q9JMC2; -.
DR TreeFam; TF320538; -.
DR BioGRID-ORCS; 56856; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9JMC2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9JMC2; protein.
DR Bgee; ENSMUSG00000045440; Expressed in lumbar dorsal root ganglion and 33 other tissues.
DR Genevisible; Q9JMC2; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:MGI.
DR GO; GO:0017053; C:transcription repressor complex; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:MGI.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0010564; P:regulation of cell cycle process; IBA:GO_Central.
DR InterPro; IPR042972; INSM1/2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15065; PTHR15065; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..493
FT /note="Insulinoma-associated protein 2"
FT /id="PRO_0000331577"
FT ZN_FING 203..223
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 231..253
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..376
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 398..420
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 452..475
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..20
FT /note="SNAG domain"
FT /evidence="ECO:0000250"
FT REGION 248..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 74
FT /note="R -> K (in Ref. 1; BAA92776)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="V -> I (in Ref. 1; BAA92776)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 52225 MW; 3FF3EEE6C72C4BA1 CRC64;
MPRGFLVKRT KRSGSSYRAR PVEPLFPPPG PLAAQSSPEE PGRGLLGSPC LAPPQDDAEW
GAGGGDGPGP SPARPAGPEL RRAFLERCLR SPVSAESFPS ATAFCSAAPA AVTSGEELVP
PQVPVSVPIP VPGPAPHGLQ RRGKGAPVCA SAPAAVRKPK AVRRLSFADE VTTSPVLGLK
IKEEEPGAPA RALGGVRTPL GEFICQLCKH QYADPFALAQ HRCSRIVRVE YRCPECDKVF
SCPANLASHR RWHKPRPTPA CAASKPPHAP LTPPDPSLAT GKENGRVPRT DDQHPQAPDS
SGDGQHRDSA ARPGLQALVY PEAARPQAPY PEVILGRHGP GSSGASAGAT SEVFVCPYCH
KKFRRQAYLR KHLGTHETGS ARAPTPGFGS ERTAPLTFAC PLCGAHFPSA DIREKHRLWH
AVREELLLPA LVGAPSEAGP GGASDGSAQQ IFSCKYCPST FFSSPGLTRH INKCHPSESR
QVLLLQMPLR PGC
