ID   NSAPB_XENLA             Reviewed;         496 AA.
AC   A0JMZ1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Nucleolar and spindle-associated protein 1-B;
DE            Short=NuSAP B;
GN   Name=nusap1-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Microtubule-associated protein with the capacity to bundle
CC       and stabilize microtubules. May associate with chromosomes and promote
CC       the organization of meiotic or mitotic spindle microtubules around them
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DNA, microtubules, ipo7, kpna2 and kpnb1.
CC       Microtubule stabilization is inhibited by ipo7 and kpna2, while
CC       microtubule bundling is inhibited by kpnb1. Active GTP-bound ran causes
CC       dissociation of ipo7 and kpnb1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Associates with
CC       meiotic or mitotic spindle microtubules, particularly in the vicinity
CC       of chromosomes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NUSAP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI26058.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC126057; AAI26058.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; A0JMZ1; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0040001; P:establishment of mitotic spindle localization; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR   InterPro; IPR026756; NuSAP.
DR   PANTHER; PTHR15874; PTHR15874; 1.
DR   Pfam; PF16006; NUSAP; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; DNA-binding; Meiosis;
KW   Microtubule; Mitosis; Nucleus; Reference proteome.
FT   CHAIN           1..496
FT                   /note="Nucleolar and spindle-associated protein 1-B"
FT                   /id="PRO_0000302039"
FT   REGION          44..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..489
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  55446 MW;  68A097CC53084A85 CRC64;
     MDAPTLSELE GLRYSELQKL AKTAGLKANL KADKLLKALK VHFYPESKDE SPDSDGCTSL
     TDTDELNSSQ EKEEPVSVSF VTHRRGRGRK PLQNQAIPKD EFLSDSAGVG SESLASEIDN
     TQDKDCLESK KKEVSLPILD NKHKKRSRSQ DTSKQNNSET TEKRQKKASN VSSIPSAGKI
     PRYVGRLSKP GSKPSTPNFK KLHEAHFKKM ESIDKFMERK QKRLDAVSSS IQEVKMLTKK
     SNLLKLVEKT PVSDIKKPVK SRLSLLSPLP RTTGASPSRT PMSRRRSGRF STANKSILVD
     RSGFKPSVLS SSKMNVRFSE ATKDNEYKRS LIKTPARKSS SFLPITPKSE PRQTLSSIKK
     TDLLTSPEKA KKPDHNTTIQ PSPAITESPC QQNKANTPFK FMAQNTETPN TNKKGSFDLQ
     ASLSRPLGYQ PHRGKLKPWG ESKENKSGSN SNVSVLKNNF KQPQLQTREE RRKQHELDRK
     GKRDQALGTR RGVPVK