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Protein

Nucleolar and spindle-associated protein 1

Gene

Nusap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Microtubule-associated protein with the capacity to bundle and stabilize microtubules. May associate with chromosomes and promote the organization of mitotic spindle microtubules around them.2 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • microtubule binding Source: MGI
  • poly(A) RNA binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolar and spindle-associated protein 1
Short name:
NuSAP
Gene namesi
Name:Nusap1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2675669. Nusap1.

Subcellular locationi

  • Cytoplasm
  • Nucleusnucleolus
  • Cytoplasmcytoskeletonspindle
  • Chromosome

  • Note: Found in the cytoplasm and nucleolus during interphase and redistributes to the mitotic spindle in prometaphase. Localizes to the mitotic spindle and to the chromosomes during anaphase and telophase then disappears from around the chromosomes during cytokinesis.

GO - Cellular componenti

  • chromosome Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • microtubule Source: UniProtKB-KW
  • nucleolus Source: MGI
  • nucleus Source: MGI
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Nucleolar and spindle-associated protein 1PRO_0000302035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei139 – 1391PhosphoserineBy similarity
Modified residuei191 – 1911PhosphothreonineBy similarity
Modified residuei246 – 2461PhosphoserineBy similarity
Modified residuei250 – 2501PhosphothreonineBy similarity
Modified residuei261 – 2611PhosphoserineBy similarity
Modified residuei323 – 3231PhosphothreonineBy similarity
Modified residuei334 – 3341PhosphothreonineBy similarity
Modified residuei337 – 3371PhosphoserineBy similarity
Modified residuei348 – 3481PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated. Ubiquitination by FZR1 may lead to proteasome-dependent degradation of this protein (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9ERH4.
MaxQBiQ9ERH4.
PaxDbiQ9ERH4.
PeptideAtlasiQ9ERH4.
PRIDEiQ9ERH4.

PTM databases

iPTMnetiQ9ERH4.
PhosphoSiteiQ9ERH4.

Expressioni

Developmental stagei

Expression peaks at G2/M phase and is low in G1 phase. Expressed at higher levels in immature erythroblasts relative to mature erythroblasts.2 Publications

Gene expression databases

BgeeiQ9ERH4.
CleanExiMM_NUSAP1.
GenevisibleiQ9ERH4. MM.

Interactioni

Subunit structurei

Interacts with DNA and microtubules. Microtubule bundling is inhibited by IPO7, KPNA2 and KPNB1 while association with DNA is also inhibited by IPO7 and KPNA2.

GO - Molecular functioni

  • microtubule binding Source: MGI

Protein-protein interaction databases

BioGridi224465. 1 interaction.
STRINGi10090.ENSMUSP00000068713.

Structurei

3D structure databases

ProteinModelPortaliQ9ERH4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni243 – 367125Interaction with microtubulesAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili393 – 42533Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi369 – 3757KEN boxBy similarity

Domaini

The KEN box is required for the FZR1-dependent degradation of this protein subsequent to ubiquitination.By similarity

Sequence similaritiesi

Belongs to the NUSAP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IGHS. Eukaryota.
ENOG4111I6V. LUCA.
GeneTreeiENSGT00390000006370.
HOGENOMiHOG000054205.
HOVERGENiHBG108204.
InParanoidiQ9ERH4.
OMAiQGRSCGP.
OrthoDBiEOG7BP85G.
PhylomeDBiQ9ERH4.
TreeFamiTF329459.

Family and domain databases

InterProiIPR026756. NuSAP.
[Graphical view]
PANTHERiPTHR15874. PTHR15874. 1 hit.
PfamiPF16006. NUSAP. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ERH4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTVPSAEELD SFKYSDLQNL AKRLGLRANM KADKLLKALK AHLNPETRKE
60 70 80 90 100
NKNQDENQFS TDETEIHVSS EEQAETESGG HVTKTRRRRR KKHKTIHGIP
110 120 130 140 150
TSQTLLQDHL EMKGTDSSNF QNQENQENQD PRDTAEVPSL PEQRPEDGNA
160 170 180 190 200
ASSGEGEVND IKDSKKPLEK RSLCTDEFSK LGNNKRTSAT TPNFKKLHEA
210 220 230 240 250
RFKKMESIDE YIMRKKKHLK EHSSLNELKL DKKGIVTPVP PRGRLSVPCT
260 270 280 290 300
PARQQCPQGH SATKMNVRFS AATKDNEHKC SLTKTPARKS PHVTAPGSAS
310 320 330 340 350
KGQAVFRTPK SKATERTSIA VITPFKLMTE ATQTPSSSKK PVFDLKASLS
360 370 380 390 400
RPLNYKPHKG KLKPWGQAKE NNSLNERVSR VTFHRKTYKQ PHLQTREERW
410 420
KRQEQERKEK KEKLLEARRN LGVTKAQ
Length:427
Mass (Da):48,573
Last modified:March 1, 2001 - v1
Checksum:iF80EF15848A94BE9
GO
Isoform 2 (identifier: Q9ERH4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     161-193: Missing.

Show »
Length:394
Mass (Da):44,883
Checksum:i65CE2F37E60FCFE1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641T → TEIHVSSEEQA in BAC40322 (PubMed:16141072).Curated
Sequence conflicti91 – 911K → R in BAC40322 (PubMed:16141072).Curated
Sequence conflicti104 – 1041T → N in BAC40322 (PubMed:16141072).Curated
Sequence conflicti201 – 2011R → H in BAC40322 (PubMed:16141072).Curated
Sequence conflicti201 – 2011R → H in AAH09096 (PubMed:15489334).Curated
Sequence conflicti331 – 3311A → P in AAH09096 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei161 – 19333Missing in isoform 2. 1 PublicationVSP_027913Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305710 mRNA. Translation: AAG31285.1.
AK042697 mRNA. Translation: BAC31337.1.
AK076028 mRNA. Translation: BAC36131.1.
AK088389 mRNA. Translation: BAC40322.1.
AL844536 Genomic DNA. Translation: CAM18073.1.
AL844536 Genomic DNA. Translation: CAM18074.1.
BC004787 mRNA. Translation: AAH04787.1.
BC009096 mRNA. Translation: AAH09096.1.
BC100392 mRNA. Translation: AAI00393.1.
CCDSiCCDS16605.1. [Q9ERH4-1]
CCDS38206.1. [Q9ERH4-2]
RefSeqiNP_001036117.1. NM_001042652.1. [Q9ERH4-2]
NP_598612.1. NM_133851.3. [Q9ERH4-1]
UniGeneiMm.290015.
Mm.439488.

Genome annotation databases

EnsembliENSMUST00000028771; ENSMUSP00000028771; ENSMUSG00000027306. [Q9ERH4-2]
ENSMUST00000068225; ENSMUSP00000068713; ENSMUSG00000027306. [Q9ERH4-1]
GeneIDi108907.
KEGGimmu:108907.
UCSCiuc008lua.1. mouse. [Q9ERH4-1]
uc008lub.1. mouse. [Q9ERH4-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305710 mRNA. Translation: AAG31285.1.
AK042697 mRNA. Translation: BAC31337.1.
AK076028 mRNA. Translation: BAC36131.1.
AK088389 mRNA. Translation: BAC40322.1.
AL844536 Genomic DNA. Translation: CAM18073.1.
AL844536 Genomic DNA. Translation: CAM18074.1.
BC004787 mRNA. Translation: AAH04787.1.
BC009096 mRNA. Translation: AAH09096.1.
BC100392 mRNA. Translation: AAI00393.1.
CCDSiCCDS16605.1. [Q9ERH4-1]
CCDS38206.1. [Q9ERH4-2]
RefSeqiNP_001036117.1. NM_001042652.1. [Q9ERH4-2]
NP_598612.1. NM_133851.3. [Q9ERH4-1]
UniGeneiMm.290015.
Mm.439488.

3D structure databases

ProteinModelPortaliQ9ERH4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi224465. 1 interaction.
STRINGi10090.ENSMUSP00000068713.

PTM databases

iPTMnetiQ9ERH4.
PhosphoSiteiQ9ERH4.

Proteomic databases

EPDiQ9ERH4.
MaxQBiQ9ERH4.
PaxDbiQ9ERH4.
PeptideAtlasiQ9ERH4.
PRIDEiQ9ERH4.

Protocols and materials databases

DNASUi108907.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028771; ENSMUSP00000028771; ENSMUSG00000027306. [Q9ERH4-2]
ENSMUST00000068225; ENSMUSP00000068713; ENSMUSG00000027306. [Q9ERH4-1]
GeneIDi108907.
KEGGimmu:108907.
UCSCiuc008lua.1. mouse. [Q9ERH4-1]
uc008lub.1. mouse. [Q9ERH4-2]

Organism-specific databases

CTDi51203.
MGIiMGI:2675669. Nusap1.

Phylogenomic databases

eggNOGiENOG410IGHS. Eukaryota.
ENOG4111I6V. LUCA.
GeneTreeiENSGT00390000006370.
HOGENOMiHOG000054205.
HOVERGENiHBG108204.
InParanoidiQ9ERH4.
OMAiQGRSCGP.
OrthoDBiEOG7BP85G.
PhylomeDBiQ9ERH4.
TreeFamiTF329459.

Miscellaneous databases

PROiQ9ERH4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ERH4.
CleanExiMM_NUSAP1.
GenevisibleiQ9ERH4. MM.

Family and domain databases

InterProiIPR026756. NuSAP.
[Graphical view]
PANTHERiPTHR15874. PTHR15874. 1 hit.
PfamiPF16006. NUSAP. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel nucleolar protein expressed in proliferating cells."
    Sato H., Tanaka Y., Taniguchi M.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Cerebellum, Embryo and Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J, Czech II and FVB/N.
    Tissue: Embryonic germ cell and Mammary tumor.
  5. "NuSAP, a novel microtubule-associated protein involved in mitotic spindle organization."
    Raemaekers T., Ribbeck K., Beaudouin J., Annaert W., Van Camp M., Stockmans I., Smets N., Bouillon R., Ellenberg J., Carmeliet G.
    J. Cell Biol. 162:1017-1029(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  6. "Expression analyses and transcriptional regulation of mouse nucleolar spindle-associated protein gene in erythroid cells: essential role of NF-Y."
    Fujiwara T., Harigae H., Okitsu Y., Takahashi S., Yokoyama H., Yamada M.F., Ishizawa K., Kameoka J., Kaku M., Sasaki T.
    Br. J. Haematol. 135:583-590(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  7. "A role for NuSAP in linking microtubules to mitotic chromosomes."
    Ribbeck K., Raemaekers T., Carmeliet G., Mattaj I.W.
    Curr. Biol. 17:230-236(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiNUSAP_MOUSE
AccessioniPrimary (citable) accession number: Q9ERH4
Secondary accession number(s): Q8C2L8, Q8C989, Q921Z0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.