SOBP_MOUSE
ID SOBP_MOUSE Reviewed; 864 AA.
AC Q0P5V2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Sine oculis-binding protein homolog;
DE AltName: Full=Jackson circler protein 1;
GN Name=Sobp {ECO:0000312|MGI:MGI:1924427};
GN Synonyms=Jxc1 {ECO:0000312|EMBL:ABA39879.1};
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] {ECO:0000312|EMBL:ABA39879.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:ABA39879.1};
RC TISSUE=Cochlea {ECO:0000312|EMBL:ABA39879.1};
RA Calderon A., Chen Z., Noben-Trauth K.;
RT "Mutations in Jxc1 cause cochlea malformation and deafness in the Jackson
RT circler (jc) mouse mutant.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAH59851.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH59851.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH59851.1};
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 DEVELOPMENTAL STAGE.
RX PubMed=21035105; DOI=10.1016/j.ajhg.2010.10.005;
RA Birk E., Har-Zahav A., Manzini C.M., Pasmanik-Chor M., Kornreich L.,
RA Walsh C.A., Noben-Trauth K., Albin A., Simon A.J., Colleaux L., Morad Y.,
RA Rainshtein L., Tischfield D.J., Wang P., Magal N., Maya I., Shoshani N.,
RA Rechavi G., Gothelf D., Maydan G., Shohat M., Basel-Vanagaite L.;
RT "SOBP is mutated in syndromic and nonsyndromic intellectual disability and
RT is highly expressed in the brain limbic system.";
RL Am. J. Hum. Genet. 87:694-700(2010).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627 AND SER-694, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and 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: Implicated in development of the cochlea.
CC {ECO:0000269|Ref.1}.
CC -!- SUBUNIT: Interacts (via SIM domains) with SUMO1 and SUMO2.
CC {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Present at 14.5 dpc throughout the developing
CC brain, with high expression in the cortical plate. During postnatal
CC development, detected in all neurons, with an intense expression in the
CC limbic system, with highest levels throughout layer V neurons in the
CC cortex, the hippocampus, the pyriform cortex, the dorsomedial nucleus
CC of the thalamus, the amygdala, and the hypothalamus. Cortical
CC expression is strong throughout development, with no clear dorsoventral
CC or rostrocaudal gradient, highest levels at P10 in layers II/III and V
CC and in the subplate. Relatively strong expression in the mitral cells
CC layer and anterior olfactory bulb, as well as in the Purkinje cell
CC layer in the cerebellum. Expression in the limbic system postnatally
CC corresponds to the time window of active synaptogenesis.
CC {ECO:0000269|PubMed:21035105}.
CC -!- SIMILARITY: Belongs to the SOBP family. {ECO:0000255}.
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DR EMBL; DQ157775; ABA39879.1; -; mRNA.
DR EMBL; BC059851; AAH59851.1; -; mRNA.
DR CCDS; CCDS35890.1; -.
DR RefSeq; NP_780616.4; NM_175407.3.
DR AlphaFoldDB; Q0P5V2; -.
DR BioGRID; 224598; 2.
DR STRING; 10090.ENSMUSP00000040072; -.
DR iPTMnet; Q0P5V2; -.
DR PhosphoSitePlus; Q0P5V2; -.
DR PaxDb; Q0P5V2; -.
DR PRIDE; Q0P5V2; -.
DR ProteomicsDB; 261314; -.
DR Antibodypedia; 32175; 60 antibodies from 14 providers.
DR Ensembl; ENSMUST00000040275; ENSMUSP00000040072; ENSMUSG00000038248.
DR GeneID; 109205; -.
DR KEGG; mmu:109205; -.
DR UCSC; uc007ezf.1; mouse.
DR CTD; 55084; -.
DR MGI; MGI:1924427; Sobp.
DR VEuPathDB; HostDB:ENSMUSG00000038248; -.
DR eggNOG; ENOG502QZ8A; Eukaryota.
DR GeneTree; ENSGT00940000154164; -.
DR HOGENOM; CLU_012732_0_0_1; -.
DR InParanoid; Q0P5V2; -.
DR OMA; MAPCVIS; -.
DR OrthoDB; 184811at2759; -.
DR PhylomeDB; Q0P5V2; -.
DR TreeFam; TF324359; -.
DR BioGRID-ORCS; 109205; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Sobp; mouse.
DR PRO; PR:Q0P5V2; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q0P5V2; protein.
DR Bgee; ENSMUSG00000038248; Expressed in rostral migratory stream and 107 other tissues.
DR Genevisible; Q0P5V2; MM.
DR GO; GO:0005634; C:nucleus; IDA:HGNC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032184; F:SUMO polymer binding; IDA:UniProtKB.
DR GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR GO; GO:0090102; P:cochlea development; IMP:HGNC.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR InterPro; IPR026092; RAI2/SOBP.
DR PANTHER; PTHR23186; PTHR23186; 1.
DR Pfam; PF15279; SOBP; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..864
FT /note="Sine oculis-binding protein homolog"
FT /id="PRO_0000312233"
FT ZN_FING 142..180
FT /note="FCS-type 1"
FT /evidence="ECO:0000255"
FT ZN_FING 216..256
FT /note="FCS-type 2"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 618..622
FT /note="SUMO interaction motif 1 (SIM); mediates the binding
FT to polysumoylated substrates"
FT /evidence="ECO:0000250"
FT MOTIF 648..652
FT /note="SUMO interaction motif 2 (SIM); mediates the binding
FT to polysumoylated substrates"
FT /evidence="ECO:0000250"
FT COMPBIAS 315..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..748
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 672
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:A7XYQ1"
SQ SEQUENCE 864 AA; 91784 MW; DB06CB90A9F6FDB2 CRC64;
MAEMEKEGRP PENKRSRKPA HPVKREINEE MKNFAENTMN ELLGWYGYDK VELKDGEDIE
FRSYTTDGES RQHISVLKEN SLPKPKLPED SVISSYNIST GYSGLATGNG LSDSPAGSKD
HGNVPIIVPL IPPPFIKPPA EDDVSNVQIM CAWCQKVGIK RYSLSMGSEV KSFCSEKCFA
ACRRAYFKRN KARDEDGRAE TFPQQHYAKE TPRLAFKNNC ELLVCDWCKH IRHTKEYLDF
GDGERRLQFC SAKCLNQYKM DIFYKETQAN LPAGLCSTLH PHMESKAEGT GVQLLTPDSW
NIPLTDARRK APSPVTAAGQ SQGPGPSSST TVSPSDTANC SVTKIPTPVP KSLPISETPS
IPPVSVQPPA SIGPPLGVPP RSPPMVMTNR GPVPLPIFME QQIIQQIRPP FIRGPPHHAS
NPNSPLSNPM LPGIGAPPGG PRNLGPTSSP MHRPMLSPHI HPPSTPTMPG NPPGLLPPPP
PGAPLPSLPF PPVSMMPNGP MPVPQMMNFG LPSLAPLVPP PTLLVPYPVI VPLPVPIPIP
IPIPHVNDSK PPNGFSSNGE SFVPSAPGDS SAAGGKAGGR SLSPRDSKQG SSKSADSPPG
SSGQALSLAP AERGRGEVVD LTRRAGSPAG AGGQPGFAGV LHGPQDGVID LTVGHRARLH
NVIHRALHAH VKAEREPGAA ERRTCGGCRD GHCSPPAAGD PGPGAPAGPE AAAACNVIVN
GTRSAPAEAK GAEPPPEQPP PPAPPKKLLS SEEPVVNELE SVKENNCASN CHLDGEATKK
LMGEEALAGG DKSDPNLNNP ADEDHAYALR MLPKTGCVIQ PVPKPAEKAA MTPCVISSPM
LSAGPEDLEP PLKRRCLRIR NQNK
