Q9ERH4 (NUSAP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleolar and spindle-associated protein 1
Short name=NuSAP

Gene names

Name:

Nusap1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.7
Subunit structure	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.
Subcellular location	Cytoplasm. Nucleus › nucleolus. Cytoplasm › cytoskeleton › spindle. 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. Ref.5 Ref.7
Developmental stage	Expression peaks at G2/M phase and is low in G1 phase. Expressed at higher levels in immature erythroblasts relative to mature erythroblasts. Ref.5 Ref.6
Domain	The KEN box is required for the FZR1-dependent degradation of this protein subsequent to ubiquitination By similarity.
Post-translational modification	Ubiquitinated. Ubiquitination by FZR1 may lead to proteasome-dependent degradation of this protein By similarity.
Sequence similarities	Belongs to the NUSAP family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Chromosome Cytoplasm Cytoskeleton Microtubule Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	DNA-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokinesis after mitosis Inferred from sequence alignment Ref.5. Source: MGI establishment of mitotic spindle localization Inferred from sequence alignment Ref.5. Source: MGI mitotic chromosome condensation Inferred from sequence alignment Ref.5. Source: MGI positive regulation of mitosis Inferred from sequence alignment Ref.5. Source: MGI
Cellular_component	chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay Ref.5. Source: MGI spindle microtubule Inferred from direct assay Ref.5. Source: MGI
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule binding Inferred from direct assay Ref.5. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9ERH4-1)

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.

Isoform 2 (identifier: Q9ERH4-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 427	427	Nucleolar and spindle-associated protein 1		PRO_0000302035
Regions
	Region	243 – 367	125	Interaction with microtubules
	Coiled coil	393 – 425	33	Potential
	Motif	369 – 375	7	KEN box By similarity
Amino acid modifications
	Modified residue	139	1	Phosphoserine By similarity
	Modified residue	191	1	Phosphothreonine By similarity
	Modified residue	246	1	Phosphoserine By similarity
	Modified residue	250	1	Phosphothreonine By similarity
	Modified residue	323	1	Phosphothreonine By similarity
	Modified residue	337	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	161 – 193	33	Missing in isoform 2.		VSP_027913
Experimental info
	Sequence conflict	64	1	T → TEIHVSSEEQA in BAC40322. Ref.2
	Sequence conflict	91	1	K → R in BAC40322. Ref.2
	Sequence conflict	104	1	T → N in BAC40322. Ref.2
	Sequence conflict	201	1	R → H in BAC40322. Ref.2
	Sequence conflict	201	1	R → H in AAH09096. Ref.4
	Sequence conflict	331	1	A → P in AAH09096. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: F80EF15848A94BE9	FASTA	427	48,573
	10 20 30 40 50 60 MTVPSAEELD SFKYSDLQNL AKRLGLRANM KADKLLKALK AHLNPETRKE NKNQDENQFS 70 80 90 100 110 120 TDETEIHVSS EEQAETESGG HVTKTRRRRR KKHKTIHGIP TSQTLLQDHL EMKGTDSSNF 130 140 150 160 170 180 QNQENQENQD PRDTAEVPSL PEQRPEDGNA ASSGEGEVND IKDSKKPLEK RSLCTDEFSK 190 200 210 220 230 240 LGNNKRTSAT TPNFKKLHEA RFKKMESIDE YIMRKKKHLK EHSSLNELKL DKKGIVTPVP 250 260 270 280 290 300 PRGRLSVPCT PARQQCPQGH SATKMNVRFS AATKDNEHKC SLTKTPARKS PHVTAPGSAS 310 320 330 340 350 360 KGQAVFRTPK SKATERTSIA VITPFKLMTE ATQTPSSSKK PVFDLKASLS RPLNYKPHKG 370 380 390 400 410 420 KLKPWGQAKE NNSLNERVSR VTFHRKTYKQ PHLQTREERW KRQEQERKEK KEKLLEARRN LGVTKAQ
	Isoform 2 [UniParc]. Checksum: 65CE2F37E60FCFE1	FASTA	394	44,883
	10 20 30 40 50 60 MTVPSAEELD SFKYSDLQNL AKRLGLRANM KADKLLKALK AHLNPETRKE NKNQDENQFS 70 80 90 100 110 120 TDETEIHVSS EEQAETESGG HVTKTRRRRR KKHKTIHGIP TSQTLLQDHL EMKGTDSSNF 130 140 150 160 170 180 QNQENQENQD PRDTAEVPSL PEQRPEDGNA ASSGEGEVND FKKLHEARFK KMESIDEYIM 190 200 210 220 230 240 RKKKHLKEHS SLNELKLDKK GIVTPVPPRG RLSVPCTPAR QQCPQGHSAT KMNVRFSAAT 250 260 270 280 290 300 KDNEHKCSLT KTPARKSPHV TAPGSASKGQ AVFRTPKSKA TERTSIAVIT PFKLMTEATQ 310 320 330 340 350 360 TPSSSKKPVF DLKASLSRPL NYKPHKGKLK PWGQAKENNS LNERVSRVTF HRKTYKQPHL 370 380 390 QTREERWKRQ EQERKEKKEK LLEARRNLGV TKAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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/6. 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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00224693. IPI00406091.
RefSeq	NP_001036117.1. NM_001042652.1. NP_598612.1. NM_133851.3.
UniGene	Mm.290015. Mm.439488.
3D structure databases
ProteinModelPortal	Q9ERH4.
ModBase	Search...
PTM databases
PhosphoSite	Q9ERH4.
Proteomic databases
PaxDb	Q9ERH4.
PRIDE	Q9ERH4.
Protocols and materials databases
DNASU	108907.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000028771; ENSMUSP00000028771; ENSMUSG00000027306. ENSMUST00000068225; ENSMUSP00000068713; ENSMUSG00000027306.
GeneID	108907.
KEGG	mmu:108907.
UCSC	uc008lua.1. mouse. uc008lub.1. mouse.
Organism-specific databases
CTD	51203.
MGI	MGI:2675669. Nusap1.
Phylogenomic databases
eggNOG	NOG43775.
GeneTree	ENSGT00390000006370.
HOGENOM	HOG000054205.
HOVERGEN	HBG108204.
InParanoid	Q9ERH4.
OMA	AVITPFK.
OrthoDB	EOG4F1X3H.
Gene expression databases
Bgee	Q9ERH4.
CleanEx	MM_NUSAP1.
Genevestigator	Q9ERH4.
Family and domain databases
InterPro	IPR026756. NuSAP. [Graphical view]
PANTHER	PTHR32473:SF0. PTHR32473:SF0. 1 hit.
ProtoNet	Search...
Other
NextBio	361445.
SOURCE	Search...

Entry information

Entry name

NUSAP_MOUSE

Accession

Primary (citable) accession number: Q9ERH4
Secondary accession number(s): Q8C2L8, Q8C989, Q921Z0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	March 1, 2001
Last modified:	April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program