UBX2B_MOUSE
ID UBX2B_MOUSE Reviewed; 331 AA.
AC Q0KL01; Q8BGY8; Q8CCQ0; Q9CZA8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=UBX domain-containing protein 2B;
DE AltName: Full=NSFL1 cofactor p37;
DE AltName: Full=p97 cofactor p37;
GN Name=Ubxn2b;
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], AND INTERACTION WITH VCP.
RX PubMed=17141156; DOI=10.1016/j.devcel.2006.10.016;
RA Uchiyama K., Totsukawa G., Puhka M., Kaneko Y., Jokitalo E., Dreveny I.,
RA Beuron F., Zhang X., Freemont P., Kondo H.;
RT "p37 is a p97 adaptor required for Golgi and ER biogenesis in interphase
RT and at the end of mitosis.";
RL Dev. Cell 11:803-816(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Olfactory bulb;
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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=23649807; DOI=10.1083/jcb.201209107;
RA Kress E., Schwager F., Holtackers R., Seiler J., Prodon F., Zanin E.,
RA Eiteneuer A., Toya M., Sugimoto A., Meyer H., Meraldi P., Gotta M.;
RT "The UBXN-2/p37/p47 adaptors of CDC-48/p97 regulate mitosis by limiting the
RT centrosomal recruitment of Aurora A.";
RL J. Cell Biol. 201:559-575(2013).
CC -!- FUNCTION: Adapter protein required for Golgi and endoplasmic reticulum
CC biogenesis. Involved in Golgi and endoplasmic reticulum maintenance
CC during interphase and in their reassembly at the end of mitosis. The
CC complex formed with VCP has membrane fusion activity; membrane fusion
CC activity requires USO1-GOLGA2 tethering and BET1L. VCPIP1 is also
CC required, but not its deubiquitinating activity. Together with
CC NSFL1C/p47, regulates the centrosomal levels of kinase AURKA/Aurora A
CC during mitotic progression by promoting AURKA removal from centrosomes
CC in prophase. Also, regulates spindle orientation during mitosis.
CC {ECO:0000250|UniProtKB:Q14CS0}.
CC -!- SUBUNIT: Interacts with VCP. Does not bind ubiquitin.
CC {ECO:0000269|PubMed:17141156}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C627}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:P0C627}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:P0C627}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P0C627}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:23649807}.
CC Note=Localizes to centrosome during mitotic prophase and metaphase.
CC {ECO:0000269|PubMed:23649807}.
CC -!- SIMILARITY: Belongs to the NSFL1C family. {ECO:0000305}.
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DR EMBL; AB120715; BAF30880.1; -; mRNA.
DR EMBL; AK012822; BAB28494.1; -; mRNA.
DR EMBL; AK028268; BAC25851.1; -; mRNA.
DR EMBL; AK032332; BAC27819.1; -; mRNA.
DR EMBL; AK049018; BAC33515.1; -; mRNA.
DR EMBL; AL772385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC076632; AAH76632.1; -; mRNA.
DR CCDS; CCDS17949.1; -.
DR RefSeq; NP_080810.2; NM_026534.2.
DR AlphaFoldDB; Q0KL01; -.
DR SMR; Q0KL01; -.
DR BioGRID; 212631; 10.
DR IntAct; Q0KL01; 1.
DR MINT; Q0KL01; -.
DR STRING; 10090.ENSMUSP00000029907; -.
DR iPTMnet; Q0KL01; -.
DR PhosphoSitePlus; Q0KL01; -.
DR EPD; Q0KL01; -.
DR MaxQB; Q0KL01; -.
DR PaxDb; Q0KL01; -.
DR PeptideAtlas; Q0KL01; -.
DR PRIDE; Q0KL01; -.
DR ProteomicsDB; 298426; -.
DR Antibodypedia; 51502; 178 antibodies from 13 providers.
DR DNASU; 68053; -.
DR Ensembl; ENSMUST00000029907; ENSMUSP00000029907; ENSMUSG00000028243.
DR GeneID; 68053; -.
DR KEGG; mmu:68053; -.
DR UCSC; uc008rxj.1; mouse.
DR CTD; 137886; -.
DR MGI; MGI:1915303; Ubxn2b.
DR VEuPathDB; HostDB:ENSMUSG00000028243; -.
DR eggNOG; KOG2086; Eukaryota.
DR GeneTree; ENSGT00520000055567; -.
DR HOGENOM; CLU_029402_0_0_1; -.
DR InParanoid; Q0KL01; -.
DR OMA; IQSRPEF; -.
DR OrthoDB; 1175850at2759; -.
DR PhylomeDB; Q0KL01; -.
DR TreeFam; TF312973; -.
DR BioGRID-ORCS; 68053; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ubxn2b; mouse.
DR PRO; PR:Q0KL01; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q0KL01; protein.
DR Bgee; ENSMUSG00000028243; Expressed in otic placode and 232 other tissues.
DR Genevisible; Q0KL01; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031616; C:spindle pole centrosome; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:1904780; P:negative regulation of protein localization to centrosome; ISO:MGI.
DR GO; GO:0031468; P:nuclear membrane reassembly; IBA:GO_Central.
DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; ISO:MGI.
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 SMART; SM00553; SEP; 1.
DR SMART; SM00166; 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 Acetylation; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW Golgi apparatus; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14CS0"
FT CHAIN 2..331
FT /note="UBX domain-containing protein 2B"
FT /id="PRO_0000315229"
FT DOMAIN 141..206
FT /note="SEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00732"
FT DOMAIN 252..329
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14CS0"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14CS0"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14CS0"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14CS0"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14CS0"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C627"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14CS0"
FT CONFLICT 8
FT /note="E -> K (in Ref. 2; BAB28494)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="S -> N (in Ref. 2; BAC27819)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="S -> N (in Ref. 1; BAF30880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 37444 MW; 61AD4AD6FE784FFA CRC64;
MAEGGRAEPE EQERGSSRPR PPSARDLQLA LAELYEDEMK CKSSKPDRST PATCRSPRTP
PHRLYSGDHK YDGLHIVQPP TGKIVNELFK EAREHGAVPL NEATRSSRED KTKSFTGGGY
RLGNSFYKRS EYIYGENQLQ DVQVLLKLWR NGFSLDDGEL RPYSDPTNAQ FLESVKRGET
PLELQRLVHG AQVNLDMEDH QDQEYIKPRL RFKAFSGEGQ KLGSLTPEIV STPSSPEEED
KSILNAAVLI DDSMPTTKIQ IRLADGSRLV QRFNSTHRIL DVRDFIVRSR PEFATTDFIL
VTSFPSKELT DETVTLQEAD ILNTVILQQL K
