UBX2B_HUMAN
ID UBX2B_HUMAN Reviewed; 331 AA.
AC Q14CS0; B3KWZ3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=UBX domain-containing protein 2B;
DE AltName: Full=NSFL1 cofactor p37;
DE AltName: Full=p97 cofactor p37;
GN Name=UBXN2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP FUNCTION.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND THR-59, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-235, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP FUNCTION.
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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-235, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Adapter protein required for Golgi and endoplasmic reticulum
CC biogenesis (PubMed:17141156). Involved in Golgi and endoplasmic
CC reticulum maintenance during interphase and in their reassembly at the
CC end of mitosis (PubMed:17141156). The complex formed with VCP has
CC membrane fusion activity; membrane fusion activity requires USO1-GOLGA2
CC tethering and BET1L (PubMed:17141156). VCPIP1 is also required, but not
CC its deubiquitinating activity (PubMed:17141156). 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 (PubMed:23649807). Also, regulates spindle orientation
CC during mitosis (PubMed:23649807). {ECO:0000269|PubMed:17141156,
CC ECO:0000269|PubMed:23649807}.
CC -!- SUBUNIT: Interacts with VCP. Does not bind ubiquitin.
CC {ECO:0000250|UniProtKB:Q0KL01}.
CC -!- INTERACTION:
CC Q14CS0; O43186: CRX; NbExp=3; IntAct=EBI-1993619, EBI-748171;
CC Q14CS0; Q969W3: FAM104A; NbExp=3; IntAct=EBI-1993619, EBI-10281506;
CC Q14CS0; V9HW80: HEL-S-70; NbExp=3; IntAct=EBI-1993619, EBI-10175326;
CC Q14CS0; Q0VD86: INCA1; NbExp=6; IntAct=EBI-1993619, EBI-6509505;
CC Q14CS0; P50221: MEOX1; NbExp=3; IntAct=EBI-1993619, EBI-2864512;
CC Q14CS0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1993619, EBI-16439278;
CC Q14CS0; Q96IV0: NGLY1; NbExp=7; IntAct=EBI-1993619, EBI-6165879;
CC Q14CS0; Q02548: PAX5; NbExp=3; IntAct=EBI-1993619, EBI-296331;
CC Q14CS0; P26367: PAX6; NbExp=3; IntAct=EBI-1993619, EBI-747278;
CC Q14CS0; Q13526: PIN1; NbExp=3; IntAct=EBI-1993619, EBI-714158;
CC Q14CS0; Q9BZV1: UBXN6; NbExp=3; IntAct=EBI-1993619, EBI-1993899;
CC Q14CS0; Q9HCJ6: VAT1L; NbExp=3; IntAct=EBI-1993619, EBI-10234766;
CC Q14CS0; P55072: VCP; NbExp=11; IntAct=EBI-1993619, EBI-355164;
CC Q14CS0; Q6GPH4: XAF1; NbExp=3; IntAct=EBI-1993619, EBI-2815120;
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:0000250|UniProtKB:Q0KL01}.
CC Note=Localizes to centrosome during mitotic prophase and metaphase.
CC {ECO:0000250|UniProtKB:Q0KL01}.
CC -!- SIMILARITY: Belongs to the NSFL1C family. {ECO:0000305}.
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DR EMBL; AK126300; BAG54305.1; -; mRNA.
DR EMBL; BC113645; AAI13646.1; -; mRNA.
DR CCDS; CCDS43741.1; -.
DR RefSeq; NP_001071087.1; NM_001077619.1.
DR RefSeq; NP_001317464.1; NM_001330535.1.
DR AlphaFoldDB; Q14CS0; -.
DR SMR; Q14CS0; -.
DR BioGRID; 126491; 41.
DR IntAct; Q14CS0; 24.
DR STRING; 9606.ENSP00000382507; -.
DR iPTMnet; Q14CS0; -.
DR PhosphoSitePlus; Q14CS0; -.
DR BioMuta; UBXN2B; -.
DR DMDM; 121946691; -.
DR EPD; Q14CS0; -.
DR jPOST; Q14CS0; -.
DR MassIVE; Q14CS0; -.
DR MaxQB; Q14CS0; -.
DR PaxDb; Q14CS0; -.
DR PeptideAtlas; Q14CS0; -.
DR PRIDE; Q14CS0; -.
DR ProteomicsDB; 60331; -.
DR Antibodypedia; 51502; 178 antibodies from 13 providers.
DR DNASU; 137886; -.
DR Ensembl; ENST00000399598.7; ENSP00000382507.2; ENSG00000215114.10.
DR GeneID; 137886; -.
DR KEGG; hsa:137886; -.
DR MANE-Select; ENST00000399598.7; ENSP00000382507.2; NM_001077619.2; NP_001071087.1.
DR UCSC; uc003xtl.3; human.
DR CTD; 137886; -.
DR DisGeNET; 137886; -.
DR GeneCards; UBXN2B; -.
DR HGNC; HGNC:27035; UBXN2B.
DR HPA; ENSG00000215114; Low tissue specificity.
DR MIM; 610686; gene.
DR neXtProt; NX_Q14CS0; -.
DR OpenTargets; ENSG00000215114; -.
DR PharmGKB; PA162408394; -.
DR VEuPathDB; HostDB:ENSG00000215114; -.
DR eggNOG; KOG2086; Eukaryota.
DR GeneTree; ENSGT00520000055567; -.
DR HOGENOM; CLU_029402_0_0_1; -.
DR InParanoid; Q14CS0; -.
DR OMA; IQSRPEF; -.
DR OrthoDB; 1175850at2759; -.
DR PhylomeDB; Q14CS0; -.
DR TreeFam; TF312973; -.
DR PathwayCommons; Q14CS0; -.
DR SignaLink; Q14CS0; -.
DR SIGNOR; Q14CS0; -.
DR BioGRID-ORCS; 137886; 16 hits in 1077 CRISPR screens.
DR ChiTaRS; UBXN2B; human.
DR GenomeRNAi; 137886; -.
DR Pharos; Q14CS0; Tbio.
DR PRO; PR:Q14CS0; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q14CS0; protein.
DR Bgee; ENSG00000215114; Expressed in cortical plate and 216 other tissues.
DR ExpressionAtlas; Q14CS0; baseline and differential.
DR Genevisible; Q14CS0; HS.
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; IEA:Ensembl.
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; IGI:UniProtKB.
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; IGI:UniProtKB.
DR GO; GO:0031468; P:nuclear membrane reassembly; IBA:GO_Central.
DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; IGI:UniProtKB.
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:0007744|PubMed:22814378"
FT CHAIN 2..331
FT /note="UBX domain-containing protein 2B"
FT /id="PRO_0000315228"
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 40..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C627"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
SQ SEQUENCE 331 AA; 37077 MW; 7CE8029B9E56A867 CRC64;
MAEGGGPEPG EQERRSSGPR PPSARDLQLA LAELYEDEVK CKSSKSNRPK ATVFKSPRTP
PQRFYSSEHE YSGLNIVRPS TGKIVNELFK EAREHGAVPL NEATRASGDD KSKSFTGGGY
RLGSSFCKRS EYIYGENQLQ DVQILLKLWS NGFSLDDGEL RPYNEPTNAQ FLESVKRGEI
PLELQRLVHG GQVNLDMEDH QDQEYIKPRL RFKAFSGEGQ KLGSLTPEIV STPSSPEEED
KSILNAVVLI DDSVPTTKIQ IRLADGSRLI QRFNSTHRIL DVRNFIVQSR PEFAALDFIL
VTSFPNKELT DESLTLLEAD ILNTVLLQQL K
