UBX2B_CHICK
ID UBX2B_CHICK Reviewed; 365 AA.
AC Q5ZLK2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=UBX domain-containing protein 2B;
DE AltName: Full=NSFL1 cofactor p37;
DE AltName: Full=p97 cofactor p37;
GN Name=UBXN2B; ORFNames=RCJMB04_5m7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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.
CC Regulates the centrosomal levels of kinase AURKA/Aurora A during
CC mitotic progression by promoting AURKA removal from centrosomes in
CC prophase. Also, regulates spindle orientation during mitosis.
CC {ECO:0000250|UniProtKB:Q14CS0}.
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; AJ719732; CAG31391.1; -; mRNA.
DR RefSeq; NP_001026194.1; NM_001031023.1.
DR AlphaFoldDB; Q5ZLK2; -.
DR SMR; Q5ZLK2; -.
DR STRING; 9031.ENSGALP00000024843; -.
DR PaxDb; Q5ZLK2; -.
DR GeneID; 421135; -.
DR KEGG; gga:421135; -.
DR CTD; 137886; -.
DR VEuPathDB; HostDB:geneid_421135; -.
DR eggNOG; KOG2086; Eukaryota.
DR InParanoid; Q5ZLK2; -.
DR OrthoDB; 1175850at2759; -.
DR PhylomeDB; Q5ZLK2; -.
DR PRO; PR:Q5ZLK2; -.
DR Proteomes; UP000000539; Unplaced.
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:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:0031468; P:nuclear membrane reassembly; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Endoplasmic reticulum; Golgi apparatus; Nucleus;
KW Reference proteome.
FT CHAIN 1..365
FT /note="UBX domain-containing protein 2B"
FT /id="PRO_0000315231"
FT DOMAIN 175..240
FT /note="SEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00732"
FT DOMAIN 286..363
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 40844 MW; 9C53F2C48CE006AE CRC64;
MADGGASPAQ QEGEMSAAGP GLRRERQHRG SGRPPSARDL QLALAELYED EAKRQSLRSD
KPTTTKMSNS KGLKIDSFRS LRKPERSMSD DKENQRFYSG DSEYRGLQIW GASNNPSKIV
AELFKEAKEH GAVPLDEASR TSGDFSKAKS FSGGGYRLGD SSQKHSEYIY GENQDVQILL
KLWRNGFSLD DGELRSYSDP INAQFLESVK RGEIPVDLQR LVHGGQVNLD MEDHQEQEYV
KPRLRFKAFS GEGQKLGSLT PEIVSTPSSP EEEDKSILNA PVLIDDSVPA TKIQIRLADG
SRLIQRFNQT HRIKDIRDFI IQSRPAFATT DFVLVTTFPN KELTDESLTL READILNTVI
LQQLK