ID   NUSAP_XENTR             Reviewed;         500 AA.
AC   Q5BKG8; Q0IHZ1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Nucleolar and spindle-associated protein 1;
DE            Short=NuSAP;
GN   Name=nusap1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2005) 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=AAH91079.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAI22899.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC091079; AAH91079.1; ALT_INIT; mRNA.
DR   EMBL; BC122898; AAI22899.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q5BKG8; -.
DR   SMR; Q5BKG8; -.
DR   STRING; 8364.ENSXETP00000053820; -.
DR   PaxDb; Q5BKG8; -.
DR   eggNOG; ENOG502QVI7; Eukaryota.
DR   HOGENOM; CLU_050701_0_0_1; -.
DR   InParanoid; Q5BKG8; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0040001; P:establishment of mitotic spindle localization; IBA:GO_Central.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IBA:GO_Central.
DR   GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
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..500
FT                   /note="Nucleolar and spindle-associated protein 1"
FT                   /id="PRO_0000302041"
FT   REGION          48..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        97
FT                   /note="T -> I (in Ref. 1; AAH91079)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="T -> I (in Ref. 1; AAH91079)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176
FT                   /note="S -> N (in Ref. 1; AAI22899)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285
FT                   /note="M -> L (in Ref. 1; AAH91079)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  55838 MW;  8B46F799AE6F1530 CRC64;
     MEAPTLSQLE GLRYSELQKL AKTAGLKANL KADKLLKVLK AHFYPESKNE TLDSDGSSSL
     TDTDELNSSQ EKEEPVSVSF VTHRRGRGRK PIRNQDTPKD EFLTVSAGVG TENMASSIDR
     TQQQNCTESK KEETTSPIID NKHRKRSRSE DTSKQNNLES TGKTEKRQKK ASNVTSVAST
     GKIPRLAGRL SKPGSKPSTP NFKKLHEAHF KKMESIDKYM ERKQKRLDAV SSSIQEVKML
     TKKSNLLKSV EKTPVSDIKK PVKSRLSLLS PLPRTTGASP SRTPMSQRRS CRSSTASKSI
     LVDRSGFKPS VFSSSKMNVR FSEATKDNEH KRSLIKTPAR KSSSFLAVTP ESEPRRILPS
     VRKTELLPAP EKADKPDVNI TLNTTTQPSP ATGMSACKAI TPFKFTAQNT ETPNTKKKGK
     FDLQASLSRQ LGYQPHKGKL KPWGESKENK PDPNSNVSVL KNNYKQPHLQ TREDRRNQHV
     QNRKNKRDQA LGTRRGVPVK