UBXN2_CAEEL
ID UBXN2_CAEEL Reviewed; 301 AA.
AC Q9N2W5; Q86DD7;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=UBX domain-containing protein 2 {ECO:0000305};
GN Name=ubxn-2 {ECO:0000312|WormBase:Y94H6A.9a};
GN ORFNames=Y94H6A.9 {ECO:0000312|EMBL:CCD74209.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17498661; DOI=10.1016/j.bbrc.2007.04.163;
RA Yamauchi S., Sasagawa Y., Ogura T., Yamanaka K.;
RT "Differential expression pattern of UBX family genes in Caenorhabditis
RT elegans.";
RL Biochem. Biophys. Res. Commun. 358:545-552(2007).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CDC-48.1 AND CDC-48.2, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20977550; DOI=10.1111/j.1365-2443.2010.01454.x;
RA Sasagawa Y., Yamanaka K., Saito-Sasagawa Y., Ogura T.;
RT "Caenorhabditis elegans UBX cofactors for CDC-48/p97 control
RT spermatogenesis.";
RL Genes Cells 15:1201-1215(2010).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CDC-48.1; CDC-48.2 AND AIR-1, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
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: Ubiquitin-binding protein which acts as an adapter for ATPase
CC cdc-48.1 and/or cdc-48.2, conferring substrate specificity
CC (PubMed:20977550). Together with ubxn-2 and ubxn-3, plays a role in
CC hermaphrodite spermatogenesis probably by promoting the degradation of
CC sex determination terminal factor tra-1 (PubMed:20977550). Probably in
CC association with ATPase cdc-48.1 or/and cdc-48.2, regulates the
CC centrosomal levels of kinase air-1 levels during mitotic progression by
CC promoting air-1 removal from centrosomes in prophase (PubMed:23649807).
CC Also, regulates spindle orientation in the one-cell embryo by
CC controlling centration and rotation of the pronuclei-centrosome complex
CC in prophase (PubMed:23649807). {ECO:0000269|PubMed:20977550,
CC ECO:0000269|PubMed:23649807}.
CC -!- SUBUNIT: Interacts with cdc-48.1 (via N-terminus) and cdc-48.2 (via N-
CC terminus) (PubMed:20977550, PubMed:23649807). Interacts with kinase
CC air-1 (PubMed:23649807). {ECO:0000269|PubMed:20977550,
CC ECO:0000269|PubMed:23649807}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:20977550}. Nucleus {ECO:0000269|PubMed:23649807}.
CC Cytoplasm {ECO:0000269|PubMed:23649807}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:23649807}. Note=Colocalizes with cdc-48.1 to the
CC perinuclear region in spermatocytes (PubMed:20977550). Nuclear
CC localization is cdc-48-dependent (PubMed:23649807). During embryonic
CC mitotic metaphase, telophase and to a certain extent prophase,
CC localizes to centrosomes (PubMed:23649807).
CC {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:23649807}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y94H6A.9a};
CC IsoId=Q9N2W5-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y94H6A.9b};
CC IsoId=Q9N2W5-2; Sequence=VSP_059591;
CC -!- TISSUE SPECIFICITY: Expressed in the germline (at protein level)
CC (PubMed:20977550). Expressed in spermatocytes but not in mature sperm
CC (at protein level) (PubMed:20977550). Ubiquitously expressed
CC (PubMed:17498661). Predominantly expressed in the spermatheca
CC (PubMed:17498661). {ECO:0000269|PubMed:17498661,
CC ECO:0000269|PubMed:20977550}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults.
CC {ECO:0000269|PubMed:17498661}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown does not cause any
CC visible phenotype (PubMed:20977550). Causes 82 percent embryonic
CC lethality (PubMed:23649807). One-cell embryos have defects in pronuclei
CC positioning and spindle orientation during prophase; however the
CC duration of cell division and establishment of embryo polarity are
CC normal (PubMed:23649807). During prophase, increases active air-1 and
CC to a lesser extent zyg-9, plk-1 and spd-2, accumulation at centrosomes,
CC centrosome size and microtubule growth rate (PubMed:23649807).
CC Simultaneous RNAi-mediated knockdown of air-1 restores normal pronuclei
CC positioning and spindle orientation but not embryonic lethality
CC (PubMed:23649807). Simultaneous RNAi-mediated knockdown of ubxn-1 and
CC ubxn-3, causes 50 percent embryonic lethality (PubMed:20977550). The
CC surviving hermaphrodite progeny are sterile due to a lack of sperm
CC (PubMed:20977550). Abnormal accumulation of sex determination terminal
CC factor tra-1 (PubMed:20977550). Germline development is normal
CC (PubMed:20977550). In males, sperm production is normal
CC (PubMed:20977550). {ECO:0000269|PubMed:20977550,
CC ECO:0000269|PubMed:23649807}.
CC -!- SIMILARITY: Belongs to the NSFL1C family. {ECO:0000305}.
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DR EMBL; BX284604; CCD74209.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD74210.1; -; Genomic_DNA.
DR RefSeq; NP_001023590.1; NM_001028419.3. [Q9N2W5-1]
DR RefSeq; NP_001023591.1; NM_001028420.3.
DR AlphaFoldDB; Q9N2W5; -.
DR SMR; Q9N2W5; -.
DR DIP; DIP-26140N; -.
DR IntAct; Q9N2W5; 2.
DR STRING; 6239.Y94H6A.9a; -.
DR EPD; Q9N2W5; -.
DR PaxDb; Q9N2W5; -.
DR PeptideAtlas; Q9N2W5; -.
DR EnsemblMetazoa; Y94H6A.9a.1; Y94H6A.9a.1; WBGene00022381. [Q9N2W5-1]
DR EnsemblMetazoa; Y94H6A.9b.1; Y94H6A.9b.1; WBGene00022381. [Q9N2W5-2]
DR GeneID; 177057; -.
DR KEGG; cel:CELE_Y94H6A.9; -.
DR UCSC; Y94H6A.9b; c. elegans.
DR CTD; 177057; -.
DR WormBase; Y94H6A.9a; CE27555; WBGene00022381; ubxn-2. [Q9N2W5-1]
DR WormBase; Y94H6A.9b; CE33955; WBGene00022381; ubxn-2. [Q9N2W5-2]
DR eggNOG; KOG2086; Eukaryota.
DR HOGENOM; CLU_029402_1_0_1; -.
DR InParanoid; Q9N2W5; -.
DR OMA; FNETHTI; -.
DR OrthoDB; 1175850at2759; -.
DR PhylomeDB; Q9N2W5; -.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR PRO; PR:Q9N2W5; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00022381; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q9N2W5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0031616; C:spindle pole centrosome; IDA:UniProtKB.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0042006; P:masculinization of hermaphroditic germ-line; IGI:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:1904780; P:negative regulation of protein localization to centrosome; IMP:UniProtKB.
DR GO; GO:0031468; P:nuclear membrane reassembly; IBA:GO_Central.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IGI:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IGI:UniProtKB.
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 Alternative splicing; Cytoplasm; Cytoskeleton; Differentiation; Nucleus;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..301
FT /note="UBX domain-containing protein 2"
FT /id="PRO_0000444374"
FT DOMAIN 89..153
FT /note="SEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00732"
FT DOMAIN 218..295
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059591"
SQ SEQUENCE 301 AA; 32550 MW; BD3A9AEAF937416E CRC64;
MSRNIRTFRD IGNNDDGGPD SDDSGADAAE RGAPQEFYAG SGQAVQGPRG AAARGPDSEA
HIRRILQAAE VVQPEGGEAP RGRPSGRETI SLTLHLWSDG LSIEDGPLMS RQDPRTIEFL
ESVGKGEIPP SLVQQYPGKE IDFKVNRHHE EYVAPKMKPF GGSGVRLGNV VPTVLGQSSS
SATTAGTSSA TTDHNPDHTA ENEAKQLEDA KKELSTNMNE PTTNIQIRLP NNQRLVGIFN
HSHTLEAVRT FICTARPDMI YAPFQMMAAY PPKPFEDESQ TLKDANVLNS VVAVKILPTT
N
