UBXN6_MOUSE
ID UBXN6_MOUSE Reviewed; 442 AA.
AC Q99PL6; B8JJA5; Q3TTP1; Q3UG19; Q8C4D6; Q91W79; Q9D7L9;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=UBX domain-containing protein 6 {ECO:0000305};
DE AltName: Full=UBX domain-containing protein 1 {ECO:0000303|PubMed:11342112};
GN Name=Ubxn6 {ECO:0000312|MGI:MGI:1913780};
GN Synonyms=Ubxd1 {ECO:0000303|PubMed:11342112}, Ubxdc2;
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 [MRNA] (ISOFORM 1).
RX PubMed=11342112; DOI=10.1016/s0167-4781(00)00248-7;
RA Carim-Todd L., Escarceller M., Estivill X., Sumoy L.;
RT "Identification and characterization of UBXD1, a novel UBX domain-
RT containing gene on human chromosome 19p13, and its mouse ortholog.";
RL Biochim. Biophys. Acta 1517:298-301(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Testis, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Mammary gland;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=18656546; DOI=10.1016/j.biocel.2008.06.008;
RA Madsen L., Andersen K.M., Prag S., Moos T., Semple C.A., Seeger M.,
RA Hartmann-Petersen R.;
RT "Ubxd1 is a novel co-factor of the human p97 ATPase.";
RL Int. J. Biochem. Cell Biol. 40:2927-2942(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Spleen, 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: May negatively regulate the ATPase activity of VCP, an ATP-
CC driven segregase that associates with different cofactors to control a
CC wide variety of cellular processes. As a cofactor of VCP, it may play a
CC role in the transport of CAV1 to lysosomes for degradation. It may also
CC play a role in endoplasmic reticulum-associated degradation (ERAD) of
CC misfolded proteins. Together with VCP and other cofactors, it may play
CC a role in macroautophagy, regulating for instance the clearance of
CC damaged lysosomes. {ECO:0000250|UniProtKB:Q9BZV1}.
CC -!- SUBUNIT: Interacts with VCP through the PUB domain (via C-terminus) and
CC VIM motif (via N-terminus); the interaction is direct. Forms a ternary
CC complex with CAV1 and VCP. Interacts with SYVN1. Interacts with
CC HERPUD1. Interacts with VCPKMT. May interact with DERL1. Interacts with
CC PLAA, VCP and YOD1; may form a complex involved in macroautophagy.
CC Interacts with LMAN1. {ECO:0000250|UniProtKB:Q9BZV1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BZV1}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BZV1}. Membrane
CC {ECO:0000250|UniProtKB:Q9BZV1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9BZV1}. Nucleus {ECO:0000250|UniProtKB:Q9BZV1}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9BZV1}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9BZV1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9BZV1}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9BZV1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9BZV1}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9BZV1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9BZV1}. Note=Localizes at the centrosome both
CC in interphase and during mitosis. May be recruited to endosomal and
CC lysosomal membranes as part of a ternary complex with CAV1 and VCP.
CC Recruited to damaged lysosomes decorated with K48-linked ubiquitin
CC chains. {ECO:0000250|UniProtKB:Q9BZV1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99PL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99PL6-2; Sequence=VSP_007454;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). Highest
CC expression in brain (at protein level). {ECO:0000269|PubMed:18656546}.
CC -!- DOMAIN: The UBX domain lacks key residues critical for VCP binding.
CC {ECO:0000250|UniProtKB:Q9BZV1}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26082.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC38512.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE36284.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF272895; AAK13259.1; -; mRNA.
DR EMBL; AK009117; BAB26082.1; ALT_FRAME; mRNA.
DR EMBL; AK082510; BAC38512.1; ALT_FRAME; mRNA.
DR EMBL; AK148170; BAE28390.1; -; mRNA.
DR EMBL; AK161273; BAE36284.1; ALT_FRAME; mRNA.
DR EMBL; CH466559; EDL23709.1; -; Genomic_DNA.
DR EMBL; CT009719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016412; AAH16412.1; -; mRNA.
DR EMBL; BC049963; AAH49963.1; -; mRNA.
DR CCDS; CCDS28893.1; -. [Q99PL6-1]
DR RefSeq; NP_077752.1; NM_024432.2. [Q99PL6-1]
DR RefSeq; XP_006524859.1; XM_006524796.2.
DR RefSeq; XP_017173099.1; XM_017317610.1.
DR AlphaFoldDB; Q99PL6; -.
DR SMR; Q99PL6; -.
DR BioGRID; 211538; 14.
DR STRING; 10090.ENSMUSP00000019722; -.
DR iPTMnet; Q99PL6; -.
DR PhosphoSitePlus; Q99PL6; -.
DR EPD; Q99PL6; -.
DR MaxQB; Q99PL6; -.
DR PaxDb; Q99PL6; -.
DR PeptideAtlas; Q99PL6; -.
DR PRIDE; Q99PL6; -.
DR ProteomicsDB; 298186; -. [Q99PL6-1]
DR ProteomicsDB; 298187; -. [Q99PL6-2]
DR Antibodypedia; 42425; 178 antibodies from 26 providers.
DR DNASU; 66530; -.
DR Ensembl; ENSMUST00000019722; ENSMUSP00000019722; ENSMUSG00000019578. [Q99PL6-1]
DR GeneID; 66530; -.
DR KEGG; mmu:66530; -.
DR UCSC; uc008dat.2; mouse. [Q99PL6-1]
DR CTD; 80700; -.
DR MGI; MGI:1913780; Ubxn6.
DR VEuPathDB; HostDB:ENSMUSG00000019578; -.
DR eggNOG; KOG2699; Eukaryota.
DR GeneTree; ENSGT00940000157273; -.
DR HOGENOM; CLU_033280_0_0_1; -.
DR InParanoid; Q99PL6; -.
DR OMA; FFRCPMI; -.
DR OrthoDB; 1288120at2759; -.
DR PhylomeDB; Q99PL6; -.
DR TreeFam; TF314617; -.
DR BioGRID-ORCS; 66530; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Ubxn6; mouse.
DR PRO; PR:Q99PL6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q99PL6; protein.
DR Bgee; ENSMUSG00000019578; Expressed in superior surface of tongue and 258 other tissues.
DR ExpressionAtlas; Q99PL6; baseline and differential.
DR Genevisible; Q99PL6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; ISS:UniProtKB.
DR GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR CDD; cd10460; PUB_UBXD1; 1.
DR InterPro; IPR036339; PUB-like_dom_sf.
DR InterPro; IPR018997; PUB_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR InterPro; IPR042774; UBXN6_PUB.
DR Pfam; PF09409; PUB; 1.
DR Pfam; PF00789; UBX; 1.
DR SUPFAM; SSF143503; SSF143503; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Endosome; Lysosome;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..442
FT /note="UBX domain-containing protein 6"
FT /id="PRO_0000211026"
FT DOMAIN 175..244
FT /note="PUB"
FT /evidence="ECO:0000255"
FT DOMAIN 332..408
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 1..10
FT /note="Mediates interaction with LMAN1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZV1"
FT REGION 13..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..63
FT /note="VCP/p97-interacting motif (VIM)"
FT /evidence="ECO:0000250|UniProtKB:Q9BZV1"
FT COMPBIAS 25..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007454"
FT CONFLICT 151
FT /note="T -> S (in Ref. 2; BAC38512)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="L -> V (in Ref. 2; BAB26082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 49796 MW; 9240DB2870F25B11 CRC64;
MKKFFQEIKA DIKFKSAGPG QKLTDSAGEK TTKGKSPQLA LRQPRQGPTD EAQMAAAAAL
ARLEQKQPRA RGPTSQDSIR NQVRKELQAE ATSSNNPGAP GTNSVPEPKE EISPHLAVPG
VFFICPLTGV TLRRDQRDAH IKQAILSHFS TDPVAASIMK IHTFNRDRDR VKLGVDTIAK
YLDNIHLHPE EEKYQKIKLQ NKVFQERINC LEGSHEFFEA IGFKKVTLPV PDQEGQEEFY
VLGEDARAQP QNLARHKQQL LDAEPVRATL DRQLRVFRPS ALASHFELPS DFFSLTAEEV
KREQRLRTEA VERLSSLRTK AMREKEEQRE LRKYTYALVR VRLPDGCLLQ GTFYAREKLS
ALFRFVREAL QNDWLPFELR ASGGQKLEEN EALALNECGL VPSALLTFSW DASVLEDIRA
AGAEPAKSVL RPELLAAIEQ LS
