UBX11_MOUSE
ID UBX11_MOUSE Reviewed; 484 AA.
AC Q9D572; Q8C843; Q8VCP5; Q9CWP0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=UBX domain-containing protein 11;
DE AltName: Full=Socius;
DE AltName: Full=UBX domain-containing protein 5;
GN Name=Ubxn11; Synonyms=D4Bwg1540e, Soc, Ubxd5;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, Head, and Testis;
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 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP IDENTIFICATION.
RX PubMed=11940653; DOI=10.1128/mcb.22.9.2952-2964.2002;
RA Katoh H., Harada A., Mori K., Negishi M.;
RT "Socius is a novel Rnd GTPase-interacting protein involved in disassembly
RT of actin stress fibers.";
RL Mol. Cell. Biol. 22:2952-2964(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478 AND SER-482, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: May be involved in the reorganization of actin cytoskeleton
CC mediated by RND1, RND2 AND RND3. Promotes RHOA activation mediated by
CC GNA12 and GNA13 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GNA12, GNA13, RND1, RND2 AND RND3.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D572-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D572-2; Sequence=VSP_024778, VSP_024779;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26982.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC33351.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK010492; BAB26982.1; ALT_FRAME; mRNA.
DR EMBL; AK015720; BAB29947.1; -; mRNA.
DR EMBL; AK048494; BAC33351.1; ALT_FRAME; mRNA.
DR EMBL; AL670680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019461; AAH19461.1; -; mRNA.
DR CCDS; CCDS18763.1; -. [Q9D572-1]
DR RefSeq; NP_080533.1; NM_026257.3. [Q9D572-1]
DR AlphaFoldDB; Q9D572; -.
DR SMR; Q9D572; -.
DR STRING; 10090.ENSMUSP00000074255; -.
DR iPTMnet; Q9D572; -.
DR PhosphoSitePlus; Q9D572; -.
DR EPD; Q9D572; -.
DR MaxQB; Q9D572; -.
DR PaxDb; Q9D572; -.
DR PRIDE; Q9D572; -.
DR ProteomicsDB; 298377; -. [Q9D572-1]
DR ProteomicsDB; 298378; -. [Q9D572-2]
DR Antibodypedia; 30597; 76 antibodies from 23 providers.
DR DNASU; 67586; -.
DR Ensembl; ENSMUST00000074690; ENSMUSP00000074255; ENSMUSG00000012126. [Q9D572-1]
DR GeneID; 67586; -.
DR KEGG; mmu:67586; -.
DR UCSC; uc008veb.2; mouse. [Q9D572-1]
DR CTD; 91544; -.
DR MGI; MGI:1914836; Ubxn11.
DR VEuPathDB; HostDB:ENSMUSG00000012126; -.
DR eggNOG; KOG2086; Eukaryota.
DR GeneTree; ENSGT00520000055567; -.
DR HOGENOM; CLU_044433_0_1_1; -.
DR InParanoid; Q9D572; -.
DR OMA; NQVHEME; -.
DR OrthoDB; 690078at2759; -.
DR PhylomeDB; Q9D572; -.
DR TreeFam; TF329799; -.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 67586; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q9D572; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D572; protein.
DR Bgee; ENSMUSG00000012126; Expressed in seminiferous tubule of testis and 112 other tissues.
DR ExpressionAtlas; Q9D572; baseline and differential.
DR Genevisible; Q9D572; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.420.210; -; 1.
DR InterPro; IPR036241; NSFL1C_SEP_dom_sf.
DR InterPro; IPR012989; SEP_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF08059; SEP; 1.
DR Pfam; PF00789; UBX; 1.
DR SUPFAM; SSF102848; SSF102848; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51399; SEP; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..484
FT /note="UBX domain-containing protein 11"
FT /id="PRO_0000284922"
FT DOMAIN 227..291
FT /note="SEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00732"
FT DOMAIN 389..466
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..147
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 282..284
FT /note="VSD -> APG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024778"
FT VAR_SEQ 285..484
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024779"
FT CONFLICT 151
FT /note="Q -> R (in Ref. 1; BAB26982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 54875 MW; 03289562FDD928F8 CRC64;
MSSPLASLSK TRKVPLESES VNPGRRGIRV YGNEDEVDMW NDGQDSEEKI SLPSCYGGIG
APVSRQGPHD SELMASMTRK LQELEQQLQA QNDEMLSKER KILDLEDLVQ TLQQHQNNAA
LQRQEELETQ CIQLQRQIGE MERFLSDYGL QWVGEPMDQE NSEEKTVSEN DERDWMKAKK
FWKPGDSFVP PEVDFDKLMA SLQDLSELVE GEAQVTPVPG GARFRTLEPI PLKVYRNGIM
MFDGPFRPFY DPSTQRCLRD ILDGFFPSEL QRLYPDGVPF KVSDLRNQIY PEDGLGQFPG
EGRVVGRQKM RKVTDRVEET SGSRMTAEQF LNRLPKCIIR QGEVIDIRGP IRDTLQNCCP
MPARIQEIIV ETPALASERQ RSQESPDMPM PLLSMLRIKS ENGEQAFLLM MWPEDTIGDV
RKLLAQARDM DSAAFEILST FPPTVYQDDT VTLQAAGLVP NATLLLRTRR ALLSNPISRP
GSLP
