UBX2B_RAT
ID UBX2B_RAT Reviewed; 331 AA.
AC P0C627;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=UBX domain-containing protein 2B;
DE AltName: Full=NSFL1 cofactor p37;
DE AltName: Full=p97 cofactor p37;
GN Name=Ubxn2b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-235, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000269|PubMed:17141156}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:17141156}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:17141156}. Golgi apparatus
CC {ECO:0000269|PubMed:17141156}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q0KL01}.
CC Note=Localizes to centrosome during mitotic prophase and metaphase.
CC {ECO:0000250|UniProtKB:Q0KL01}.
CC -!- TISSUE SPECIFICITY: Present at high level in brain. Also present in
CC liver, kidney, spleen, testis, lung and heart (at protein level).
CC {ECO:0000269|PubMed:17141156}.
CC -!- SIMILARITY: Belongs to the NSFL1C family. {ECO:0000305}.
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DR EMBL; AABR03041043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001101375.1; NM_001107905.1.
DR RefSeq; XP_006237899.1; XM_006237837.3.
DR AlphaFoldDB; P0C627; -.
DR SMR; P0C627; -.
DR BioGRID; 260285; 1.
DR STRING; 10116.ENSRNOP00000012551; -.
DR iPTMnet; P0C627; -.
DR PhosphoSitePlus; P0C627; -.
DR PaxDb; P0C627; -.
DR PRIDE; P0C627; -.
DR Ensembl; ENSRNOT00000093925; ENSRNOP00000076685; ENSRNOG00000071045.
DR GeneID; 312965; -.
DR KEGG; rno:312965; -.
DR UCSC; RGD:1308557; rat.
DR CTD; 137886; -.
DR RGD; 1308557; Ubxn2b.
DR eggNOG; KOG2086; Eukaryota.
DR GeneTree; ENSGT00520000055567; -.
DR HOGENOM; CLU_029402_0_0_1; -.
DR InParanoid; P0C627; -.
DR OMA; IQSRPEF; -.
DR OrthoDB; 1175850at2759; -.
DR PhylomeDB; P0C627; -.
DR TreeFam; TF312973; -.
DR PRO; PR:P0C627; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009137; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; P0C627; RN.
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; ISO:RGD.
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:RGD.
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:RGD.
DR GO; GO:0031468; P:nuclear membrane reassembly; IBA:GO_Central.
DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; ISO:RGD.
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_0000315230"
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..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
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:0007744|PubMed:22673903"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 331 AA; 37075 MW; 208726A4A562FC35 CRC64;
MAEGGGAEPE EQERRSSRPR PPSARDLQLA LAELYEDEMK CKSSKPDRST ATAFKSPRTP
PLRLYSGDQE YGGLHIAQPP TGKIVNELFK EAREHGAVPL NEATRSSSDD KAKSFTGGGY
RLGSSFYKRS EYIYGENQLQ DVQILLRLWS NGFSLDDGEL RPYSDPTNAQ FLESVKRGEI
PLELQRLVHG SQVSLDMEDH QDQEYIKPRL RFKAFSGEGQ KLGSLTPEIV STPSSPEEED
KSILNAAVLI DDSVPTTKIQ IRLADGSRLI QRFNSTHRIL DVRDFIVQSR PEFATTDFIL
VTSFPSKELT DESVTLQDAD ILNTVILQQL K
