NUSAP_BOVIN
ID NUSAP_BOVIN Reviewed; 465 AA.
AC Q2YDJ0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Nucleolar and spindle-associated protein 1;
DE Short=NuSAP;
GN Name=NUSAP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-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 mitotic spindle microtubules around them (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DNA and microtubules. Microtubule bundling is
CC inhibited by IPO7, KPNA2 and KPNB1 while association with DNA is also
CC inhibited by IPO7 and KPNA2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC Chromosome {ECO:0000250}. Note=Found in the cytoplasm and nucleolus
CC during interphase and redistributes to the mitotic spindle in
CC prometaphase. Localizes to the mitotic spindle and to the chromosomes
CC during anaphase and telophase then disappears from around the
CC chromosomes during cytokinesis. {ECO:0000250}.
CC -!- DOMAIN: The KEN box is required for the FZR1-dependent degradation of
CC this protein subsequent to ubiquitination. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Ubiquitination by FZR1 may lead to proteasome-
CC dependent degradation of this protein (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NUSAP family. {ECO:0000305}.
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DR EMBL; BC110197; AAI10198.1; -; mRNA.
DR RefSeq; NP_001040036.1; NM_001046571.2.
DR AlphaFoldDB; Q2YDJ0; -.
DR SMR; Q2YDJ0; -.
DR STRING; 9913.ENSBTAP00000014263; -.
DR PaxDb; Q2YDJ0; -.
DR PRIDE; Q2YDJ0; -.
DR Ensembl; ENSBTAT00000014263; ENSBTAP00000014263; ENSBTAG00000010774.
DR GeneID; 616028; -.
DR KEGG; bta:616028; -.
DR CTD; 51203; -.
DR VEuPathDB; HostDB:ENSBTAG00000010774; -.
DR VGNC; VGNC:32370; NUSAP1.
DR eggNOG; ENOG502QVI7; Eukaryota.
DR GeneTree; ENSGT00390000006370; -.
DR HOGENOM; CLU_050701_0_0_1; -.
DR InParanoid; Q2YDJ0; -.
DR OMA; ATHDNEY; -.
DR OrthoDB; 1573441at2759; -.
DR TreeFam; TF329459; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000010774; Expressed in oocyte and 105 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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:0007076; P:mitotic chromosome condensation; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
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; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; DNA-binding; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..465
FT /note="Nucleolar and spindle-associated protein 1"
FT /id="PRO_0000302033"
FT REGION 44..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..405
FT /note="Interaction with microtubules"
FT /evidence="ECO:0000250"
FT REGION 308..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..61
FT /evidence="ECO:0000255"
FT COILED 430..457
FT /evidence="ECO:0000255"
FT MOTIF 407..413
FT /note="KEN box"
FT /evidence="ECO:0000250"
FT COMPBIAS 56..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 269
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 361
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 372
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
SQ SEQUENCE 465 AA; 52328 MW; 7093B4B7D495A625 CRC64;
MIVPSLEELN SFKYSDLQNL AKSLGLRANL RADKLLRALK AHLKNEARKE NENQDEIQTS
ASSCDEPEIQ TSSQEQAERE PDDHVTKTRG RRKTVHRSPD SQANGNVQTE KKLPPVPNLQ
NHSEIKLCGP TKSQNQEKHE NQVLRTAVEV PSLPNESQGD ENTVSSGKHG IDGNEDPRVP
SKRKKSLYTD GFSKPGKNKT ASTTPNFKKL HEARFKEMES IDQYVERKKK HFEEHNSFNE
LKVLQRQPVT KGVPATPVPA RGRLSVACTP GSQRRSQGRP HAGRSTLCVK GSAKRSALSA
AKMNVRFSAA TKDNEHKRSL TKTPARKSPH VTTSVNTPKG QAVLGTHKLK TTRGESVAVI
TPFKLTTEAS QTPISHKKPV FDLKASLSRP LNYEPHKGKL KPWGQSKENN SLHEHVNRVS
FHKKTYKQPR LQTREEQRKK HERERKEKKE KVLGVRRGLI IAERS
