NUSAP_HUMAN
ID NUSAP_HUMAN Reviewed; 441 AA.
AC Q9BXS6; B4DDF1; E7ERR5; J3KN21; Q53GW2; Q8TBT4; Q96E58; Q96FJ1; Q9GZM9;
AC Q9NZ85; Q9UI70;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Nucleolar and spindle-associated protein 1;
DE Short=NuSAP;
GN Name=NUSAP1; Synonyms=ANKT; ORFNames=BM-037, PRO0310;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal liver;
RA Qu X., Zhang C., Yu Y., Wu S., Wei H., Xing G., Zhai Y., Lu C., Wang M.,
RA He F.;
RT "Homo sapiens liver nuclear protein mRNA.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Peripheral blood;
RA Sato H., Tanaka Y., Taniguchi M.;
RT "A novel nucleolar protein expressed in proliferating cells.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal liver;
RX PubMed=11483580; DOI=10.1101/gr.175501;
RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y.,
RA Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.;
RT "Gene expression profiling in human fetal liver and identification of
RT tissue- and developmental-stage-specific genes through compiled expression
RT profiles and efficient cloning of full-length cDNAs.";
RL Genome Res. 11:1392-1403(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 7).
RC TISSUE=Neuroblastoma, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-441 (ISOFORM 4).
RC TISSUE=Cervix, Lung, Lymph, and Placenta;
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-207 (ISOFORMS 1/2).
RC TISSUE=Bone marrow;
RA Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z.;
RT "A novel gene expressed in human bone marrow.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP FUNCTION.
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 [12]
RP SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=17618083; DOI=10.1016/j.cellsig.2007.05.017;
RA Li L., Zhou Y., Sun L., Xing G., Tian C., Sun J., Zhang L., He F.;
RT "NuSAP is degraded by APC/C-Cdh1 and its overexpression results in mitotic
RT arrest dependent of its microtubules' affinity.";
RL Cell. Signal. 19:2046-2055(2007).
RN [13]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH CHROMATIN.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; THR-182; SER-240;
RP THR-244; SER-247; THR-314 AND SER-352, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-338, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-411, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-240; SER-276;
RP SER-311; THR-314 AND SER-352, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP PHOSPHORYLATION AT SER-124 BY ATM.
RX PubMed=21130744; DOI=10.1016/j.bbrc.2010.11.135;
RA Xie P., Li L., Xing G., Tian C., Yin Y., He F., Zhang L.;
RT "ATM-mediated NuSAP phosphorylation induces mitotic arrest.";
RL Biochem. Biophys. Res. Commun. 404:413-418(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; THR-182; SER-240;
RP THR-244; SER-247; SER-255; SER-269; THR-338; THR-349; SER-352 AND SER-363,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Microtubule-associated protein with the capacity to bundle
CC and stabilize microtubules (By similarity). May associate with
CC chromosomes and promote the organization of mitotic spindle
CC microtubules around them. {ECO:0000250, ECO:0000269|PubMed:12963707}.
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 -!- INTERACTION:
CC Q9BXS6; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2555618, EBI-739624;
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 (By similarity). Localizes to the mitotic spindle during
CC anaphase and telophase then disappears from around the chromosomes
CC during cytokinesis (By similarity). Localizes to multiple distinct
CC regions of chromosomes throughout mitosis. {ECO:0000250,
CC ECO:0000269|PubMed:17276916, ECO:0000269|PubMed:17618083}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q9BXS6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXS6-2; Sequence=VSP_027912;
CC Name=3;
CC IsoId=Q9BXS6-3; Sequence=VSP_027911, VSP_027912;
CC Name=4;
CC IsoId=Q9BXS6-4; Sequence=VSP_027910, VSP_027912;
CC Name=5;
CC IsoId=Q9BXS6-5; Sequence=VSP_027911;
CC Name=6;
CC IsoId=Q9BXS6-6; Sequence=VSP_027910;
CC Name=7;
CC IsoId=Q9BXS6-7; Sequence=VSP_046805, VSP_027912, VSP_046806;
CC -!- DOMAIN: The KEN box is required for the FZR1-dependent degradation of
CC this protein subsequent to ubiquitination.
CC -!- PTM: Ubiquitinated. Ubiquitination by FZR1 may lead to proteasome-
CC dependent degradation of this protein. {ECO:0000269|PubMed:17618083}.
CC -!- PTM: Phosphorylation by ATM in G2/M-phase induces mitotic arrest.
CC {ECO:0000269|PubMed:21130744}.
CC -!- SIMILARITY: Belongs to the NUSAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24034.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF67624.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH12887.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF290612; AAK28023.1; -; mRNA.
DR EMBL; AF305711; AAG25874.1; -; mRNA.
DR EMBL; AF090915; AAF24034.1; ALT_FRAME; mRNA.
DR EMBL; AK023483; BAB14586.1; -; mRNA.
DR EMBL; AK293168; BAG56712.1; -; mRNA.
DR EMBL; AK222819; BAD96539.1; -; mRNA.
DR EMBL; AL833611; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC087721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92483.1; -; Genomic_DNA.
DR EMBL; CH471125; EAW92486.1; -; Genomic_DNA.
DR EMBL; BC001308; AAH01308.1; -; mRNA.
DR EMBL; BC010838; AAH10838.2; -; mRNA.
DR EMBL; BC012887; AAH12887.2; ALT_INIT; mRNA.
DR EMBL; BC024772; AAH24772.1; -; mRNA.
DR EMBL; AF217513; AAF67624.1; ALT_FRAME; mRNA.
DR CCDS; CCDS45234.1; -. [Q9BXS6-1]
DR CCDS; CCDS45236.1; -. [Q9BXS6-2]
DR CCDS; CCDS58356.1; -. [Q9BXS6-3]
DR CCDS; CCDS58357.1; -. [Q9BXS6-6]
DR CCDS; CCDS58358.1; -. [Q9BXS6-7]
DR CCDS; CCDS73708.1; -. [Q9BXS6-5]
DR RefSeq; NP_001230071.1; NM_001243142.1. [Q9BXS6-3]
DR RefSeq; NP_001230072.1; NM_001243143.1. [Q9BXS6-6]
DR RefSeq; NP_001230073.1; NM_001243144.1. [Q9BXS6-7]
DR RefSeq; NP_001288065.1; NM_001301136.1. [Q9BXS6-5]
DR RefSeq; NP_057443.2; NM_016359.4. [Q9BXS6-1]
DR RefSeq; NP_060924.4; NM_018454.7. [Q9BXS6-2]
DR RefSeq; XP_005254487.1; XM_005254430.4. [Q9BXS6-4]
DR AlphaFoldDB; Q9BXS6; -.
DR SMR; Q9BXS6; -.
DR BioGRID; 119376; 101.
DR IntAct; Q9BXS6; 32.
DR MINT; Q9BXS6; -.
DR STRING; 9606.ENSP00000453403; -.
DR CarbonylDB; Q9BXS6; -.
DR iPTMnet; Q9BXS6; -.
DR PhosphoSitePlus; Q9BXS6; -.
DR BioMuta; NUSAP1; -.
DR DMDM; 74717631; -.
DR EPD; Q9BXS6; -.
DR jPOST; Q9BXS6; -.
DR MassIVE; Q9BXS6; -.
DR MaxQB; Q9BXS6; -.
DR PaxDb; Q9BXS6; -.
DR PeptideAtlas; Q9BXS6; -.
DR PRIDE; Q9BXS6; -.
DR ProteomicsDB; 17837; -.
DR ProteomicsDB; 79494; -. [Q9BXS6-1]
DR ProteomicsDB; 79495; -. [Q9BXS6-2]
DR ProteomicsDB; 79496; -. [Q9BXS6-3]
DR ProteomicsDB; 79497; -. [Q9BXS6-4]
DR ProteomicsDB; 79498; -. [Q9BXS6-5]
DR Antibodypedia; 23266; 240 antibodies from 27 providers.
DR DNASU; 51203; -.
DR Ensembl; ENST00000260359.10; ENSP00000260359.6; ENSG00000137804.14. [Q9BXS6-6]
DR Ensembl; ENST00000414849.6; ENSP00000400746.2; ENSG00000137804.14. [Q9BXS6-2]
DR Ensembl; ENST00000450592.6; ENSP00000401014.2; ENSG00000137804.14. [Q9BXS6-7]
DR Ensembl; ENST00000559596.6; ENSP00000453403.1; ENSG00000137804.14. [Q9BXS6-1]
DR Ensembl; ENST00000560177.5; ENSP00000453657.1; ENSG00000137804.14. [Q9BXS6-5]
DR Ensembl; ENST00000560747.5; ENSP00000454097.1; ENSG00000137804.14. [Q9BXS6-3]
DR Ensembl; ENST00000668273.1; ENSP00000499238.1; ENSG00000137804.14. [Q9BXS6-1]
DR GeneID; 51203; -.
DR KEGG; hsa:51203; -.
DR MANE-Select; ENST00000559596.6; ENSP00000453403.1; NM_016359.5; NP_057443.2.
DR UCSC; uc001znr.5; human. [Q9BXS6-1]
DR CTD; 51203; -.
DR DisGeNET; 51203; -.
DR GeneCards; NUSAP1; -.
DR HGNC; HGNC:18538; NUSAP1.
DR HPA; ENSG00000137804; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 612818; gene.
DR neXtProt; NX_Q9BXS6; -.
DR OpenTargets; ENSG00000137804; -.
DR PharmGKB; PA134987502; -.
DR VEuPathDB; HostDB:ENSG00000137804; -.
DR eggNOG; ENOG502QVI7; Eukaryota.
DR GeneTree; ENSGT00390000006370; -.
DR HOGENOM; CLU_050701_0_0_1; -.
DR InParanoid; Q9BXS6; -.
DR OMA; ATHDNEY; -.
DR OrthoDB; 1573441at2759; -.
DR PhylomeDB; Q9BXS6; -.
DR TreeFam; TF329459; -.
DR PathwayCommons; Q9BXS6; -.
DR SignaLink; Q9BXS6; -.
DR SIGNOR; Q9BXS6; -.
DR BioGRID-ORCS; 51203; 8 hits in 1093 CRISPR screens.
DR ChiTaRS; NUSAP1; human.
DR GenomeRNAi; 51203; -.
DR Pharos; Q9BXS6; Tbio.
DR PRO; PR:Q9BXS6; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9BXS6; protein.
DR Bgee; ENSG00000137804; Expressed in ventricular zone and 102 other tissues.
DR ExpressionAtlas; Q9BXS6; baseline and differential.
DR Genevisible; Q9BXS6; HS.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IDA:MGI.
DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; IDA:MGI.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IDA:MGI.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:MGI.
DR InterPro; IPR026756; NuSAP.
DR PANTHER; PTHR15874; PTHR15874; 1.
DR Pfam; PF16006; NUSAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; DNA-binding; Microtubule; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..441
FT /note="Nucleolar and spindle-associated protein 1"
FT /id="PRO_0000302034"
FT REGION 47..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..382
FT /note="Interaction with microtubules"
FT /evidence="ECO:0000250"
FT REGION 286..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 407..432
FT /evidence="ECO:0000255"
FT MOTIF 384..390
FT /note="KEN box"
FT COMPBIAS 54..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000269|PubMed:21130744"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 338
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 349
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 411
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 32..54
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046805"
FT VAR_SEQ 102..116
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_027910"
FT VAR_SEQ 102
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027911"
FT VAR_SEQ 221
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.5"
FT /id="VSP_027912"
FT VAR_SEQ 336..374
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046806"
FT VARIANT 33
FT /note="T -> A (in dbSNP:rs7178634)"
FT /id="VAR_057779"
FT VARIANT 33
FT /note="T -> N (in dbSNP:rs7178777)"
FT /id="VAR_057780"
FT CONFLICT 33
FT /note="T -> D (in Ref. 6; AL833611)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="I -> V (in Ref. 5; BAD96539)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="K -> E (in Ref. 5; BAD96539)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="G -> V (in Ref. 4; BAG56712)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="D -> DQ (in Ref. 6; AL833611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 49452 MW; 1400E1B9F3FB727F CRC64;
MIIPSLEELD SLKYSDLQNL AKSLGLRANL RATKLLKALK GYIKHEARKG NENQDESQTS
ASSCDETEIQ ISNQEEAERQ PLGHVTKTRR RCKTVRVDPD SQQNHSEIKI SNPTEFQNHE
KQESQDLRAT AKVPSPPDEH QEAENAVSSG NRDSKVPSEG KKSLYTDESS KPGKNKRTAI
TTPNFKKLHE AHFKEMESID QYIERKKKHF EEHNSMNELK QQPINKGGVR TPVPPRGRLS
VASTPISQRR SQGRSCGPAS QSTLGLKGSL KRSAISAAKT GVRFSAATKD NEHKRSLTKT
PARKSAHVTV SGGTPKGEAV LGTHKLKTIT GNSAAVITPF KLTTEATQTP VSNKKPVFDL
KASLSRPLNY EPHKGKLKPW GQSKENNYLN QHVNRINFYK KTYKQPHLQT KEEQRKKREQ
ERKEKKAKVL GMRRGLILAE D
