NUSAP_MOUSE
ID NUSAP_MOUSE Reviewed; 427 AA.
AC Q9ERH4; Q8C2L8; Q8C989; Q921Z0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Nucleolar and spindle-associated protein 1;
DE Short=NuSAP;
GN Name=Nusap1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Sato H., Tanaka Y., Taniguchi M.;
RT "A novel nucleolar protein expressed in proliferating cells.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Embryo, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Embryonic germ cell, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12963707; DOI=10.1083/jcb.200302129;
RA Raemaekers T., Ribbeck K., Beaudouin J., Annaert W., Van Camp M.,
RA Stockmans I., Smets N., Bouillon R., Ellenberg J., Carmeliet G.;
RT "NuSAP, a novel microtubule-associated protein involved in mitotic spindle
RT organization.";
RL J. Cell Biol. 162:1017-1029(2003).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=17054671; DOI=10.1111/j.1365-2141.2006.06340.x;
RA Fujiwara T., Harigae H., Okitsu Y., Takahashi S., Yokoyama H., Yamada M.F.,
RA Ishizawa K., Kameoka J., Kaku M., Sasaki T.;
RT "Expression analyses and transcriptional regulation of mouse nucleolar
RT spindle-associated protein gene in erythroid cells: essential role of NF-
RT Y.";
RL Br. J. Haematol. 135:583-590(2006).
RN [7]
RP FUNCTION, DNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=17276916; DOI=10.1016/j.cub.2006.11.050;
RA Ribbeck K., Raemaekers T., Carmeliet G., Mattaj I.W.;
RT "A role for NuSAP in linking microtubules to mitotic chromosomes.";
RL Curr. Biol. 17:230-236(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC {ECO:0000269|PubMed:12963707, ECO:0000269|PubMed:17276916}.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Cytoplasm,
CC cytoskeleton, spindle. Chromosome. Note=Found in the cytoplasm and
CC nucleolus 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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ERH4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ERH4-2; Sequence=VSP_027913;
CC -!- DEVELOPMENTAL STAGE: Expression peaks at G2/M phase and is low in G1
CC phase. Expressed at higher levels in immature erythroblasts relative to
CC mature erythroblasts. {ECO:0000269|PubMed:12963707,
CC ECO:0000269|PubMed:17054671}.
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; AF305710; AAG31285.1; -; mRNA.
DR EMBL; AK042697; BAC31337.1; -; mRNA.
DR EMBL; AK076028; BAC36131.1; -; mRNA.
DR EMBL; AK088389; BAC40322.1; -; mRNA.
DR EMBL; AL844536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004787; AAH04787.1; -; mRNA.
DR EMBL; BC009096; AAH09096.1; -; mRNA.
DR EMBL; BC100392; AAI00393.1; -; mRNA.
DR CCDS; CCDS16605.1; -. [Q9ERH4-1]
DR CCDS; CCDS38206.1; -. [Q9ERH4-2]
DR RefSeq; NP_001036117.1; NM_001042652.1. [Q9ERH4-2]
DR RefSeq; NP_598612.1; NM_133851.3. [Q9ERH4-1]
DR AlphaFoldDB; Q9ERH4; -.
DR SMR; Q9ERH4; -.
DR BioGRID; 224465; 2.
DR STRING; 10090.ENSMUSP00000068713; -.
DR iPTMnet; Q9ERH4; -.
DR PhosphoSitePlus; Q9ERH4; -.
DR EPD; Q9ERH4; -.
DR jPOST; Q9ERH4; -.
DR MaxQB; Q9ERH4; -.
DR PaxDb; Q9ERH4; -.
DR PeptideAtlas; Q9ERH4; -.
DR PRIDE; Q9ERH4; -.
DR ProteomicsDB; 293784; -. [Q9ERH4-1]
DR ProteomicsDB; 293785; -. [Q9ERH4-2]
DR DNASU; 108907; -.
DR Ensembl; ENSMUST00000028771; ENSMUSP00000028771; ENSMUSG00000027306. [Q9ERH4-2]
DR Ensembl; ENSMUST00000068225; ENSMUSP00000068713; ENSMUSG00000027306. [Q9ERH4-1]
DR GeneID; 108907; -.
DR KEGG; mmu:108907; -.
DR UCSC; uc008lua.1; mouse. [Q9ERH4-1]
DR UCSC; uc008lub.1; mouse. [Q9ERH4-2]
DR CTD; 51203; -.
DR MGI; MGI:2675669; Nusap1.
DR VEuPathDB; HostDB:ENSMUSG00000027306; -.
DR eggNOG; ENOG502QVI7; Eukaryota.
DR GeneTree; ENSGT00390000006370; -.
DR HOGENOM; CLU_050701_0_0_1; -.
DR InParanoid; Q9ERH4; -.
DR OMA; ATHDNEY; -.
DR OrthoDB; 1573441at2759; -.
DR PhylomeDB; Q9ERH4; -.
DR TreeFam; TF329459; -.
DR BioGRID-ORCS; 108907; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Nusap1; mouse.
DR PRO; PR:Q9ERH4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9ERH4; protein.
DR Bgee; ENSMUSG00000027306; Expressed in undifferentiated genital tubercle and 185 other tissues.
DR Genevisible; Q9ERH4; MM.
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; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; ISO:MGI.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISO:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISO:MGI.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:MGI.
DR InterPro; IPR026756; NuSAP.
DR PANTHER; PTHR15874; PTHR15874; 1.
DR Pfam; PF16006; NUSAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Chromosome; Coiled coil;
KW Cytoplasm; Cytoskeleton; DNA-binding; Microtubule; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..427
FT /note="Nucleolar and spindle-associated protein 1"
FT /id="PRO_0000302035"
FT REGION 41..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..367
FT /note="Interaction with microtubules"
FT REGION 354..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 393..425
FT /evidence="ECO:0000255"
FT MOTIF 369..375
FT /note="KEN box"
FT /evidence="ECO:0000250"
FT COMPBIAS 41..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 191
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 250
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 323
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS6"
FT VAR_SEQ 161..193
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027913"
FT CONFLICT 64
FT /note="T -> TEIHVSSEEQA (in Ref. 2; BAC40322)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="K -> R (in Ref. 2; BAC40322)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="T -> N (in Ref. 2; BAC40322)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="R -> H (in Ref. 2; BAC40322 and 4; AAH09096)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="A -> P (in Ref. 4; AAH09096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 48573 MW; F80EF15848A94BE9 CRC64;
MTVPSAEELD SFKYSDLQNL AKRLGLRANM KADKLLKALK AHLNPETRKE NKNQDENQFS
TDETEIHVSS EEQAETESGG HVTKTRRRRR KKHKTIHGIP TSQTLLQDHL EMKGTDSSNF
QNQENQENQD PRDTAEVPSL PEQRPEDGNA ASSGEGEVND IKDSKKPLEK RSLCTDEFSK
LGNNKRTSAT TPNFKKLHEA RFKKMESIDE YIMRKKKHLK EHSSLNELKL DKKGIVTPVP
PRGRLSVPCT PARQQCPQGH SATKMNVRFS AATKDNEHKC SLTKTPARKS PHVTAPGSAS
KGQAVFRTPK SKATERTSIA VITPFKLMTE ATQTPSSSKK PVFDLKASLS RPLNYKPHKG
KLKPWGQAKE NNSLNERVSR VTFHRKTYKQ PHLQTREERW KRQEQERKEK KEKLLEARRN
LGVTKAQ
