UBX10_MOUSE
ID UBX10_MOUSE Reviewed; 277 AA.
AC Q8BG34; Q3TTR1; Q8BP58; Q8R0B6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=UBX domain-containing protein 10 {ECO:0000305};
DE AltName: Full=UBX domain-containing protein 3;
GN Name=Ubxn10 {ECO:0000312|MGI:MGI:2443123};
GN Synonyms=Ubxd3 {ECO:0000312|MGI:MGI:2443123};
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].
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Cerebellum, Corpora quadrigemina, 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 MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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).
CC -!- FUNCTION: VCP/p97-binding protein required for ciliogenesis. Acts as a
CC tethering factor that facilitates recruitment of VCP/p97 to the
CC intraflagellar transport complex B (IFT-B) in cilia. UBX domain-
CC containing proteins act as tethering factors for VCP/p97 and may
CC specify substrate specificity of VCP/p97.
CC {ECO:0000250|UniProtKB:Q96LJ8}.
CC -!- SUBUNIT: Interacts with CLUAP1; the interaction is direct and mediates
CC interaction with the intraflagellar transport complex B (IFT-B).
CC Interacts with VCP; the interaction is direct.
CC {ECO:0000250|UniProtKB:Q96LJ8}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q96LJ8}. Note=Recruited to cilia in a VCP-
CC dependent manner. {ECO:0000250|UniProtKB:Q96LJ8}.
CC -!- SIMILARITY: Belongs to the UBXN10 family. {ECO:0000305}.
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DR EMBL; AK045964; BAC32548.1; -; mRNA.
DR EMBL; AK046949; BAC32924.1; -; mRNA.
DR EMBL; AK077656; BAC36931.1; -; mRNA.
DR EMBL; AK080662; BAC37971.1; -; mRNA.
DR EMBL; AK133185; BAE21549.1; -; mRNA.
DR EMBL; AK161245; BAE36264.1; -; mRNA.
DR EMBL; BC027099; AAH27099.1; -; mRNA.
DR CCDS; CCDS18830.1; -.
DR RefSeq; NP_001272857.1; NM_001285928.1.
DR RefSeq; NP_001272858.1; NM_001285929.1.
DR RefSeq; NP_001272859.1; NM_001285930.1.
DR RefSeq; NP_848786.1; NM_178671.5.
DR AlphaFoldDB; Q8BG34; -.
DR SMR; Q8BG34; -.
DR STRING; 10090.ENSMUSP00000101437; -.
DR iPTMnet; Q8BG34; -.
DR PhosphoSitePlus; Q8BG34; -.
DR PaxDb; Q8BG34; -.
DR PRIDE; Q8BG34; -.
DR ProteomicsDB; 298376; -.
DR Antibodypedia; 29784; 181 antibodies from 22 providers.
DR Ensembl; ENSMUST00000105809; ENSMUSP00000101435; ENSMUSG00000043621.
DR Ensembl; ENSMUST00000105810; ENSMUSP00000101436; ENSMUSG00000043621.
DR Ensembl; ENSMUST00000105811; ENSMUSP00000101437; ENSMUSG00000043621.
DR Ensembl; ENSMUST00000146415; ENSMUSP00000117219; ENSMUSG00000043621.
DR GeneID; 212190; -.
DR KEGG; mmu:212190; -.
DR UCSC; uc008vlc.3; mouse.
DR CTD; 127733; -.
DR MGI; MGI:2443123; Ubxn10.
DR VEuPathDB; HostDB:ENSMUSG00000043621; -.
DR eggNOG; ENOG502S4IN; Eukaryota.
DR GeneTree; ENSGT00390000012939; -.
DR HOGENOM; CLU_079919_0_0_1; -.
DR InParanoid; Q8BG34; -.
DR OMA; ECRIPHK; -.
DR OrthoDB; 1474017at2759; -.
DR PhylomeDB; Q8BG34; -.
DR TreeFam; TF335927; -.
DR BioGRID-ORCS; 212190; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8BG34; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BG34; protein.
DR Bgee; ENSMUSG00000043621; Expressed in spermatid and 126 other tissues.
DR Genevisible; Q8BG34; MM.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030992; C:intraciliary transport particle B; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..277
FT /note="UBX domain-containing protein 10"
FT /id="PRO_0000211030"
FT DOMAIN 191..268
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96LJ8"
FT CONFLICT 32
FT /note="L -> F (in Ref. 2; AAH27099)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="V -> M (in Ref. 2; AAH27099)"
FT /evidence="ECO:0000305"
FT CONFLICT 230..231
FT /note="KA -> QT (in Ref. 1; BAC36931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 30341 MW; CD39B6AD7A46E238 CRC64;
MAIEAPVNFA PPERSTVVST AGDSSTWQPS SLRMHVIRPK SAKGRKRPNL HRPQGMGDGS
PSALSSSPPP RSSGSPSNQK PGVCATVSTS QGAPDEMPEL LLQQAPTRTA SSLNRYPVLP
SINRRSLEVG AVDTVASKTS SLQLSSVQAL YQEDSSQEDS RTQVCALEKK FIIRTKRQSS
SRASNIEEPS DEEPRLLLAV RSPSGQRFVR YFRPSDDLQT VLEVAEQKNK ATYQHCSIET
MEVPRRRFSD LTKSLQECGI LHKSVLGISQ EEGEAWP
