UBX11_HUMAN
ID UBX11_HUMAN Reviewed; 520 AA.
AC Q5T124; D3DPK6; Q5T117; Q5T120; Q5T125; Q5T126; Q5T129; Q5T131; Q5T133;
AC Q63HM6; Q71RB3; Q8IY27; Q8N1L6; Q8N9M4; Q8NA18; Q8NFE3; Q8NFE4; Q8NFE6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=UBX domain-containing protein 11;
DE AltName: Full=Colorectal tumor-associated antigen COA-1;
DE AltName: Full=Socius;
DE AltName: Full=UBX domain-containing protein 5;
GN Name=UBXN11; Synonyms=SOC, UBXD5; ORFNames=PP2243;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), AND VARIANT VAL-474.
RC TISSUE=Colon cancer;
RX PubMed=14583468;
RA Maccalli C., Li Y.F., El-Gamil M., Rosenberg S.A., Robbins P.F.;
RT "Identification of a colorectal tumor-associated antigen (COA-1) recognized
RT by CD4(+) T lymphocytes.";
RL Cancer Res. 63:6735-6743(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 8), AND VARIANTS
RP ARG-312; 487-PRO--SER-494 DEL; 488-PRO--SER-502 DEL AND SER-509.
RA Cai Q., Yu L.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7).
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
RP ARG-312; PRO-GLY-PRO-GLY-PRO-GLY-PRO-SER-486 INS; 487-PRO--SER-494 DEL AND
RP SER-509.
RC TISSUE=Synovium, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT
RP PRO-GLY-PRO-GLY-PRO-GLY-PRO-SER-486 INS.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Testis;
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 [9]
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).
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 -!- INTERACTION:
CC Q5T124; Q8IYR0: CFAP206; NbExp=4; IntAct=EBI-746004, EBI-749051;
CC Q5T124; P06730: EIF4E; NbExp=3; IntAct=EBI-746004, EBI-73440;
CC Q5T124; O60573: EIF4E2; NbExp=3; IntAct=EBI-746004, EBI-398610;
CC Q5T124; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-746004, EBI-744099;
CC Q5T124; Q13131: PRKAA1; NbExp=3; IntAct=EBI-746004, EBI-1181405;
CC Q5T124; O43741: PRKAB2; NbExp=3; IntAct=EBI-746004, EBI-1053424;
CC Q5T124; P25786: PSMA1; NbExp=3; IntAct=EBI-746004, EBI-359352;
CC Q5T124; O94955: RHOBTB3; NbExp=4; IntAct=EBI-746004, EBI-2367123;
CC Q5T124; Q63HN8-6: RNF213; NbExp=3; IntAct=EBI-746004, EBI-10248548;
CC Q5T124; Q9BWG6: SCNM1; NbExp=4; IntAct=EBI-746004, EBI-748391;
CC Q5T124; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-746004, EBI-747035;
CC Q5T124; Q08117: TLE5; NbExp=3; IntAct=EBI-746004, EBI-717810;
CC Q5T124; Q12933: TRAF2; NbExp=5; IntAct=EBI-746004, EBI-355744;
CC Q5T124; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-746004, EBI-739895;
CC Q5T124-6; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-11524408, EBI-725606;
CC Q5T124-6; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-11524408, EBI-749051;
CC Q5T124-6; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-11524408, EBI-744099;
CC Q5T124-6; O14964: HGS; NbExp=3; IntAct=EBI-11524408, EBI-740220;
CC Q5T124-6; Q14005-2: IL16; NbExp=3; IntAct=EBI-11524408, EBI-17178971;
CC Q5T124-6; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-11524408, EBI-726510;
CC Q5T124-6; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-11524408, EBI-11750983;
CC Q5T124-6; Q8N3J5: PPM1K; NbExp=3; IntAct=EBI-11524408, EBI-3923368;
CC Q5T124-6; Q99633: PRPF18; NbExp=3; IntAct=EBI-11524408, EBI-2798416;
CC Q5T124-6; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-11524408, EBI-1567797;
CC Q5T124-6; P0CG20: PRR35; NbExp=3; IntAct=EBI-11524408, EBI-11986293;
CC Q5T124-6; P25786: PSMA1; NbExp=3; IntAct=EBI-11524408, EBI-359352;
CC Q5T124-6; P14678-2: SNRPB; NbExp=3; IntAct=EBI-11524408, EBI-372475;
CC Q5T124-6; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-11524408, EBI-11955057;
CC Q5T124-6; Q08117-2: TLE5; NbExp=3; IntAct=EBI-11524408, EBI-11741437;
CC Q5T124-6; Q12933: TRAF2; NbExp=3; IntAct=EBI-11524408, EBI-355744;
CC Q5T124-6; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-11524408, EBI-9090990;
CC Q5T124-6; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-11524408, EBI-739895;
CC Q5T124-6; P55072: VCP; NbExp=7; IntAct=EBI-11524408, EBI-355164;
CC Q5T124-6; Q9Y2B5: VPS9D1; NbExp=3; IntAct=EBI-11524408, EBI-9031083;
CC Q5T124-6; Q64LD2-2: WDR25; NbExp=3; IntAct=EBI-11524408, EBI-12032042;
CC Q5T124-6; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-11524408, EBI-10183064;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q5T124-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T124-2; Sequence=VSP_024774;
CC Name=3;
CC IsoId=Q5T124-3; Sequence=VSP_024775;
CC Name=4;
CC IsoId=Q5T124-4; Sequence=VSP_024773;
CC Name=5;
CC IsoId=Q5T124-5; Sequence=VSP_024771;
CC Name=6;
CC IsoId=Q5T124-6; Sequence=VSP_024776, VSP_024777;
CC Name=7;
CC IsoId=Q5T124-7; Sequence=VSP_024774, VSP_024776, VSP_024777;
CC Name=8;
CC IsoId=Q5T124-8; Sequence=VSP_024772;
CC -!- POLYMORPHISM: The number of repeats is polymorphic and varies from 1 to
CC 4. {ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15498874,
CC ECO:0000269|Ref.2}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM74202.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAQ15261.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF521017; AAM74201.1; -; mRNA.
DR EMBL; AF521018; AAM74202.1; ALT_FRAME; mRNA.
DR EMBL; AF520989; AAM76060.1; -; mRNA.
DR EMBL; CR749413; CAH18255.1; -; mRNA.
DR EMBL; BX648412; CAH56155.1; -; mRNA.
DR EMBL; AK093258; BAC04112.1; -; mRNA.
DR EMBL; AK094198; BAC04307.1; -; mRNA.
DR EMBL; AK097368; BAC05024.1; -; mRNA.
DR EMBL; AF370425; AAQ15261.1; ALT_FRAME; mRNA.
DR EMBL; AL451139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07823.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07826.1; -; Genomic_DNA.
DR EMBL; BC038106; AAH38106.1; -; mRNA.
DR CCDS; CCDS41286.1; -. [Q5T124-2]
DR CCDS; CCDS41287.1; -. [Q5T124-3]
DR CCDS; CCDS41288.1; -. [Q5T124-1]
DR RefSeq; NP_001070730.1; NM_001077262.1. [Q5T124-3]
DR RefSeq; NP_663320.2; NM_145345.2. [Q5T124-2]
DR RefSeq; NP_892120.2; NM_183008.2. [Q5T124-1]
DR AlphaFoldDB; Q5T124; -.
DR SMR; Q5T124; -.
DR BioGRID; 124844; 61.
DR IntAct; Q5T124; 41.
DR MINT; Q5T124; -.
DR STRING; 9606.ENSP00000363339; -.
DR iPTMnet; Q5T124; -.
DR PhosphoSitePlus; Q5T124; -.
DR BioMuta; UBXN11; -.
DR DMDM; 146325810; -.
DR jPOST; Q5T124; -.
DR MassIVE; Q5T124; -.
DR PaxDb; Q5T124; -.
DR PeptideAtlas; Q5T124; -.
DR PRIDE; Q5T124; -.
DR ProteomicsDB; 64223; -. [Q5T124-1]
DR ProteomicsDB; 64224; -. [Q5T124-2]
DR ProteomicsDB; 64225; -. [Q5T124-3]
DR ProteomicsDB; 64226; -. [Q5T124-4]
DR ProteomicsDB; 64227; -. [Q5T124-5]
DR ProteomicsDB; 64228; -. [Q5T124-6]
DR ProteomicsDB; 64229; -. [Q5T124-7]
DR ProteomicsDB; 64230; -. [Q5T124-8]
DR Antibodypedia; 30597; 76 antibodies from 23 providers.
DR DNASU; 91544; -.
DR Ensembl; ENST00000314675.11; ENSP00000324721.7; ENSG00000158062.21. [Q5T124-3]
DR Ensembl; ENST00000357089.8; ENSP00000349601.4; ENSG00000158062.21. [Q5T124-2]
DR Ensembl; ENST00000374217.7; ENSP00000363334.2; ENSG00000158062.21. [Q5T124-2]
DR Ensembl; ENST00000374221.7; ENSP00000363338.3; ENSG00000158062.21. [Q5T124-1]
DR Ensembl; ENST00000374222.6; ENSP00000363339.1; ENSG00000158062.21. [Q5T124-1]
DR GeneID; 91544; -.
DR KEGG; hsa:91544; -.
DR MANE-Select; ENST00000374222.6; ENSP00000363339.1; NM_001389556.1; NP_001376485.1.
DR UCSC; uc001blw.4; human. [Q5T124-1]
DR CTD; 91544; -.
DR DisGeNET; 91544; -.
DR GeneCards; UBXN11; -.
DR HGNC; HGNC:30600; UBXN11.
DR HPA; ENSG00000158062; Low tissue specificity.
DR MIM; 609151; gene.
DR neXtProt; NX_Q5T124; -.
DR OpenTargets; ENSG00000158062; -.
DR PharmGKB; PA162408338; -.
DR VEuPathDB; HostDB:ENSG00000158062; -.
DR eggNOG; KOG2086; Eukaryota.
DR GeneTree; ENSGT00520000055567; -.
DR HOGENOM; CLU_044433_0_1_1; -.
DR InParanoid; Q5T124; -.
DR OMA; NQVHEME; -.
DR OrthoDB; 690078at2759; -.
DR PhylomeDB; Q5T124; -.
DR TreeFam; TF329799; -.
DR PathwayCommons; Q5T124; -.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q5T124; -.
DR BioGRID-ORCS; 91544; 8 hits in 1079 CRISPR screens.
DR ChiTaRS; UBXN11; human.
DR GeneWiki; UBXD5; -.
DR GenomeRNAi; 91544; -.
DR Pharos; Q5T124; Tbio.
DR PRO; PR:Q5T124; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5T124; protein.
DR Bgee; ENSG00000158062; Expressed in right uterine tube and 143 other tissues.
DR ExpressionAtlas; Q5T124; baseline and differential.
DR Genevisible; Q5T124; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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;
KW Reference proteome; Repeat.
FT CHAIN 1..520
FT /note="UBX domain-containing protein 11"
FT /id="PRO_0000284921"
FT DOMAIN 230..294
FT /note="SEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00732"
FT DOMAIN 392..469
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REPEAT 487..494
FT /note="1"
FT REPEAT 495..502
FT /note="2"
FT REPEAT 503..510
FT /note="3"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..510
FT /note="3 X 8 AA tandem repeats of P-G-P-G-P-G-P-S"
FT COILED 76..149
FT /evidence="ECO:0000255"
FT COMPBIAS 482..520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..312
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_024771"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14583468, ECO:0000303|Ref.2"
FT /id="VSP_024772"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_024773"
FT VAR_SEQ 34..66
FT /note="Missing (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2"
FT /id="VSP_024774"
FT VAR_SEQ 67..186
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024775"
FT VAR_SEQ 286..324
FT /note="SDLRNQVYLEDGLDPFPGEGRVVGRQLMHKALDRVEEHP -> ISCSSNHTF
FT GDFEGSGDTQPPQTPPILRGSRCTPWGTPV (in isoform 6 and isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_024776"
FT VAR_SEQ 325..520
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_024777"
FT VARIANT 165
FT /note="E -> G (in dbSNP:rs6695966)"
FT /id="VAR_031860"
FT VARIANT 312
FT /note="L -> R (in dbSNP:rs4332350)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT /id="VAR_031861"
FT VARIANT 474
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:14583468"
FT /id="VAR_031862"
FT VARIANT 486
FT /note="C -> CPGPGPGPS"
FT /evidence="ECO:0000269|PubMed:15498874"
FT /id="VAR_031863"
FT VARIANT 487..494
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT /id="VAR_031864"
FT VARIANT 488..502
FT /note="Missing"
FT /id="VAR_031865"
FT VARIANT 509
FT /note="P -> S (in dbSNP:rs1134584)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT /id="VAR_052690"
FT CONFLICT 19
FT /note="E -> G (in Ref. 2; CAH56155)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="K -> M (in Ref. 4; BAC05024)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="N -> D (in Ref. 4; BAC05024)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="V -> L (in Ref. 5; AAQ15261)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="S -> L (in Ref. 2; AAM74202)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="N -> D (in Ref. 3; BAC04307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 57373 MW; 8642DB07C023276E CRC64;
MSSPLASLSK TRKVPLPSEP MNPGRRGIRI YGDEDEVDML SDGCGSEEKI SVPSCYGGIG
APVSRQVPAS HDSELMAFMT RKLWDLEQQV KAQTDEILSK DQKIAALEDL VQTLRPHPAE
ATLQRQEELE TMCVQLQRQV REMERFLSDY GLQWVGEPMD QEDSESKTVS EHGERDWMTA
KKFWKPGDSL APPEVDFDRL LASLQDLSEL VVEGDTQVTP VPGGARLRTL EPIPLKLYRN
GIMMFDGPFQ PFYDPSTQRC LRDILDGFFP SELQRLYPNG VPFKVSDLRN QVYLEDGLDP
FPGEGRVVGR QLMHKALDRV EEHPGSRMTA EKFLNRLPKF VIRQGEVIDI RGPIRDTLQN
CCPLPARIQE IVVETPTLAA ERERSQESPN TPAPPLSMLR IKSENGEQAF LLMMQPDNTI
GDVRALLAQA RVMDASAFEI FSTFPPTLYQ DDTLTLQAAG LVPKAALLLR ARRAPKSSLK
FSPGPCPGPG PGPSPGPGPG PSPGPGPGPS PCPGPSPSPQ
