NUSAP_DANRE
ID NUSAP_DANRE Reviewed; 446 AA.
AC A1L2F3; A5D6S5; Q08CW0; Q1RLV4; Q7T2W2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Nucleolar and spindle-associated protein 1;
DE Short=NuSAP;
GN Name=nusap1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-281 (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RX PubMed=12641569; DOI=10.1046/j.1432-0436.2003.710206.x;
RA Yoda H., Momoi A., Esguerra C.V., Meyer D., Driever W., Kondoh H.,
RA Furutani-Seiki M.;
RT "An expression pattern screen for genes involved in the induction of the
RT posterior nervous system of zebrafish.";
RL Differentiation 71:152-162(2003).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Associates with
CC mitotic spindle microtubules, particularly in the vicinity of
CC chromosomes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A1L2F3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A1L2F3-2; Sequence=VSP_027914;
CC -!- DEVELOPMENTAL STAGE: Expressed in the blastoderm margin. Expression
CC shifts to the spinal cord and endodermal tissue at the somitogenesis
CC stage. {ECO:0000269|PubMed:12641569}.
CC -!- SIMILARITY: Belongs to the NUSAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI15273.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI24067.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI29495.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI39864.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC115272; AAI15273.1; ALT_INIT; mRNA.
DR EMBL; BC124066; AAI24067.1; ALT_INIT; mRNA.
DR EMBL; BC129494; AAI29495.1; ALT_INIT; mRNA.
DR EMBL; BC139863; AAI39864.1; ALT_INIT; mRNA.
DR EMBL; AB097826; BAC77540.1; -; mRNA.
DR RefSeq; NP_001139166.1; NM_001145694.1. [A1L2F3-1]
DR AlphaFoldDB; A1L2F3; -.
DR SMR; A1L2F3; -.
DR STRING; 7955.ENSDARP00000015118; -.
DR PaxDb; A1L2F3; -.
DR PeptideAtlas; A1L2F3; -.
DR PRIDE; A1L2F3; -.
DR Ensembl; ENSDART00000003314; ENSDARP00000015118; ENSDARG00000002403. [A1L2F3-1]
DR GeneID; 567446; -.
DR KEGG; dre:567446; -.
DR CTD; 51203; -.
DR ZFIN; ZDB-GENE-030827-5; nusap1.
DR eggNOG; ENOG502QVI7; Eukaryota.
DR GeneTree; ENSGT00390000006370; -.
DR HOGENOM; CLU_050701_0_0_1; -.
DR InParanoid; A1L2F3; -.
DR OrthoDB; 1573441at2759; -.
DR PhylomeDB; A1L2F3; -.
DR TreeFam; TF329459; -.
DR PRO; PR:A1L2F3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000002403; Expressed in testis and 39 other tissues.
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:0001755; P:neural crest cell migration; IMP:ZFIN.
DR InterPro; IPR026756; NuSAP.
DR PANTHER; PTHR15874; PTHR15874; 1.
DR Pfam; PF16006; NUSAP; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; DNA-binding; Microtubule; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..446
FT /note="Nucleolar and spindle-associated protein 1"
FT /id="PRO_0000302037"
FT REGION 39..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 197..223
FT /evidence="ECO:0000255"
FT COMPBIAS 68..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 52..61
FT /note="SDAHDSVPPV -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12641569, ECO:0000303|Ref.1"
FT /id="VSP_027914"
FT CONFLICT 65
FT /note="A -> T (in Ref. 2; BAC77540)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="T -> I (in Ref. 1; AAI29495 and 2; BAC77540)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="M -> V (in Ref. 1; AAI29495 and 2; BAC77540)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="G -> R (in Ref. 1; AAI29495 and 2; BAC77540)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="K -> E (in Ref. 1; AAI29495 and 2; BAC77540)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="E -> D (in Ref. 2; BAC77540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 49887 MW; 76E1D13C2D0E4DF2 CRC64;
MDLDSLKYAE LQRLAKEVGL KANMKAERLL KALKEHFSQQ QLSENGNDAA ASDAHDSVPP
VDAHAATYVT ERRGKGRTAK RKLSEPTPII SPTEEKTPQD EGRRGSKRRK VSSAKDTQTP
VPAEAFAKEN TMEKESGDLN PDSESGPTET GVKGRRTVGK IPRHKGLMKR KPAMRPTTPN
FKKLHEAHFK KMESIDSYVQ RKNKQMEVLR NSVKELKTLS EKTLKKPEAK AQTKVPSSRA
SLFSPAVQKT AVPERRRLTQ QPVSKSALKD TATFRPTVLT TNKINVRFSQ ATQDNEYKRS
LVKTPARMSP HMPLTSTPGR KSDVRSKAEL NRSASTITKT PGATPFVFNG NNSISTTPGT
TKKNTFDLKA SLSRPLTYKP HKGKLKPFGD AQENTALNKS QTVPSHQKNY KQHQVQTREE
RRVKHTEDRK QKKEKMLGAR RGLVMA
