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Q9BXS6

- NUSAP_HUMAN

UniProt

Q9BXS6 - NUSAP_HUMAN

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Protein

Nucleolar and spindle-associated protein 1

Gene

NUSAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Microtubule-associated protein with the capacity to bundle and stabilize microtubules By similarity. May associate with chromosomes and promote the organization of mitotic spindle microtubules around them.By similarity1 Publication

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. establishment of mitotic spindle localization Source: MGI
  2. mitotic chromosome condensation Source: MGI
  3. mitotic cytokinesis Source: MGI
  4. mitotic sister chromatid segregation Source: MGI
  5. positive regulation of mitosis Source: MGI
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
Synonyms:ANKT
ORF Names:BM-037, PRO0310
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:18538. NUSAP1.

Subcellular locationi

Cytoplasm By similarity. Nucleusnucleolus By similarity. Cytoplasmcytoskeletonspindle By similarity. Chromosome By similarity
Note: Found in the cytoplasm and nucleolus during interphase and redistributes to the mitotic spindle in prometaphase By similarity. Localizes to the mitotic spindle during anaphase and telophase then disappears from around the chromosomes during cytokinesis By similarity. Localizes to multiple distinct regions of chromosomes throughout mitosis.By similarity2 Publications

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. cytoplasm Source: HPA
  3. nucleolus Source: HPA
  4. nucleus Source: HPA
  5. spindle microtubule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134987502.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Nucleolar and spindle-associated protein 1PRO_0000302034Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241Phosphoserine; by ATM1 Publication
Modified residuei135 – 1351Phosphoserine2 Publications
Modified residuei182 – 1821Phosphothreonine1 Publication
Modified residuei240 – 2401Phosphoserine2 Publications
Modified residuei244 – 2441Phosphothreonine1 Publication
Modified residuei247 – 2471Phosphoserine1 Publication
Modified residuei276 – 2761Phosphoserine1 Publication
Modified residuei311 – 3111Phosphoserine1 Publication
Modified residuei314 – 3141Phosphothreonine2 Publications
Modified residuei338 – 3381Phosphothreonine1 Publication
Modified residuei352 – 3521Phosphoserine2 Publications
Modified residuei411 – 4111N6-acetyllysine1 Publication

Post-translational modificationi

Ubiquitinated. Ubiquitination by FZR1 may lead to proteasome-dependent degradation of this protein.1 Publication
Phosphorylation by ATM in G2/M-phase induces mitotic arrest.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9BXS6.
PaxDbiQ9BXS6.
PRIDEiQ9BXS6.

PTM databases

PhosphoSiteiQ9BXS6.

Expressioni

Gene expression databases

BgeeiQ9BXS6.
CleanExiHS_NUSAP1.
ExpressionAtlasiQ9BXS6. baseline and differential.
GenevestigatoriQ9BXS6.

Organism-specific databases

HPAiHPA042904.

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 By similarity.By similarity

Protein-protein interaction databases

BioGridi119376. 27 interactions.
IntActiQ9BXS6. 1 interaction.
MINTiMINT-5009420.
STRINGi9606.ENSP00000260359.

Structurei

3D structure databases

ProteinModelPortaliQ9BXS6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni237 – 382146Interaction with microtubulesBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili407 – 43226Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi384 – 3907KEN box

Domaini

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

Sequence similaritiesi

Belongs to the NUSAP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG43775.
GeneTreeiENSGT00390000006370.
HOVERGENiHBG108204.
InParanoidiQ9BXS6.
OMAiAVITPFK.
OrthoDBiEOG7BP85G.
PhylomeDBiQ9BXS6.
TreeFamiTF329459.

Family and domain databases

InterProiIPR026756. NuSAP.
[Graphical view]
PANTHERiPTHR15874. PTHR15874. 1 hit.

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BXS6-1) [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
MIIPSLEELD SLKYSDLQNL AKSLGLRANL RATKLLKALK GYIKHEARKG
60 70 80 90 100
NENQDESQTS ASSCDETEIQ ISNQEEAERQ PLGHVTKTRR RCKTVRVDPD
110 120 130 140 150
SQQNHSEIKI SNPTEFQNHE KQESQDLRAT AKVPSPPDEH QEAENAVSSG
160 170 180 190 200
NRDSKVPSEG KKSLYTDESS KPGKNKRTAI TTPNFKKLHE AHFKEMESID
210 220 230 240 250
QYIERKKKHF EEHNSMNELK QQPINKGGVR TPVPPRGRLS VASTPISQRR
260 270 280 290 300
SQGRSCGPAS QSTLGLKGSL KRSAISAAKT GVRFSAATKD NEHKRSLTKT
310 320 330 340 350
PARKSAHVTV SGGTPKGEAV LGTHKLKTIT GNSAAVITPF KLTTEATQTP
360 370 380 390 400
VSNKKPVFDL KASLSRPLNY EPHKGKLKPW GQSKENNYLN QHVNRINFYK
410 420 430 440
KTYKQPHLQT KEEQRKKREQ ERKEKKAKVL GMRRGLILAE D
Length:441
Mass (Da):49,452
Last modified:June 1, 2001 - v1
Checksum:i1400E1B9F3FB727F
GO
Isoform 2 (identifier: Q9BXS6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     221-221: Missing.

Show »
Length:440
Mass (Da):49,324
Checksum:iE903FADDD7341A2A
GO
Isoform 3 (identifier: Q9BXS6-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     102-102: Missing.
     221-221: Missing.

Show »
Length:439
Mass (Da):49,196
Checksum:iBF3DB4438241D00E
GO
Isoform 4 (identifier: Q9BXS6-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     102-116: Missing.
     221-221: Missing.

Show »
Length:425
Mass (Da):47,570
Checksum:iCD3A2D4A1838A7B4
GO
Isoform 5 (identifier: Q9BXS6-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     102-102: Missing.

Show »
Length:440
Mass (Da):49,324
Checksum:i2496DFF76DAE07B5
GO
Isoform 6 (identifier: Q9BXS6-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     102-116: Missing.

Note: No experimental confirmation available.

Show »
Length:426
Mass (Da):47,698
Checksum:iDF04D86E64347EC2
GO
Isoform 7 (identifier: Q9BXS6-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     32-54: Missing.
     221-221: Missing.
     336-374: Missing.

Show »
Length:378
Mass (Da):42,352
Checksum:i67DC255E553C7481
GO

Sequence cautioni

The sequence AAF24034.1 differs from that shown. Reason: Frameshift at position 205.
The sequence AAF67624.1 differs from that shown. Reason: Frameshift at positions 175 and 205.
The sequence AAH12887.2 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331T → D in AL833611. (PubMed:17974005)Curated
Sequence conflicti43 – 431I → V in BAD96539. 1 PublicationCurated
Sequence conflicti220 – 2201K → E in BAD96539. 1 PublicationCurated
Sequence conflicti331 – 3311G → V in BAG56712. (PubMed:14702039)Curated
Sequence conflicti441 – 4411D → DQ in AL833611. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331T → A.
Corresponds to variant rs7178634 [ dbSNP | Ensembl ].
VAR_057779
Natural varianti33 – 331T → N.
Corresponds to variant rs7178777 [ dbSNP | Ensembl ].
VAR_057780

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei32 – 5423Missing in isoform 7. 1 PublicationVSP_046805Add
BLAST
Alternative sequencei102 – 11615Missing in isoform 4 and isoform 6. 2 PublicationsVSP_027910Add
BLAST
Alternative sequencei102 – 1021Missing in isoform 3 and isoform 5. 1 PublicationVSP_027911
Alternative sequencei221 – 2211Missing in isoform 2, isoform 3, isoform 4 and isoform 7. 4 PublicationsVSP_027912
Alternative sequencei336 – 37439Missing in isoform 7. 1 PublicationVSP_046806Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF290612 mRNA. Translation: AAK28023.1.
AF305711 mRNA. Translation: AAG25874.1.
AF090915 mRNA. Translation: AAF24034.1. Frameshift.
AK023483 mRNA. Translation: BAB14586.1.
AK293168 mRNA. Translation: BAG56712.1.
AK222819 mRNA. Translation: BAD96539.1.
AL833611 mRNA. No translation available.
AC087721 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92483.1.
CH471125 Genomic DNA. Translation: EAW92486.1.
BC001308 mRNA. Translation: AAH01308.1.
BC010838 mRNA. Translation: AAH10838.2.
BC012887 mRNA. Translation: AAH12887.2. Different initiation.
BC024772 mRNA. Translation: AAH24772.1.
AF217513 mRNA. Translation: AAF67624.1. Frameshift.
CCDSiCCDS45234.1. [Q9BXS6-1]
CCDS45236.1. [Q9BXS6-2]
CCDS58356.1. [Q9BXS6-3]
CCDS58357.1. [Q9BXS6-6]
CCDS58358.1. [Q9BXS6-7]
CCDS73708.1. [Q9BXS6-5]
RefSeqiNP_001230071.1. NM_001243142.1. [Q9BXS6-3]
NP_001230072.1. NM_001243143.1. [Q9BXS6-6]
NP_001230073.1. NM_001243144.1. [Q9BXS6-7]
NP_057443.2. NM_016359.4. [Q9BXS6-1]
NP_060924.4. NM_018454.7. [Q9BXS6-2]
XP_005254487.1. XM_005254430.2. [Q9BXS6-4]
UniGeneiHs.615092.

Genome annotation databases

EnsembliENST00000260359; ENSP00000260359; ENSG00000137804. [Q9BXS6-6]
ENST00000414849; ENSP00000400746; ENSG00000137804. [Q9BXS6-2]
ENST00000450592; ENSP00000401014; ENSG00000137804. [Q9BXS6-7]
ENST00000559596; ENSP00000453403; ENSG00000137804. [Q9BXS6-1]
ENST00000560177; ENSP00000453657; ENSG00000137804. [Q9BXS6-5]
ENST00000560747; ENSP00000454097; ENSG00000137804. [Q9BXS6-3]
GeneIDi51203.
KEGGihsa:51203.
UCSCiuc001znr.4. human. [Q9BXS6-2]
uc001zns.4. human. [Q9BXS6-1]
uc001znt.4. human.
uc001znu.4. human. [Q9BXS6-5]
uc001znv.4. human. [Q9BXS6-3]
uc001znw.4. human. [Q9BXS6-4]

Polymorphism databases

DMDMi74717631.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF290612 mRNA. Translation: AAK28023.1 .
AF305711 mRNA. Translation: AAG25874.1 .
AF090915 mRNA. Translation: AAF24034.1 . Frameshift.
AK023483 mRNA. Translation: BAB14586.1 .
AK293168 mRNA. Translation: BAG56712.1 .
AK222819 mRNA. Translation: BAD96539.1 .
AL833611 mRNA. No translation available.
AC087721 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92483.1 .
CH471125 Genomic DNA. Translation: EAW92486.1 .
BC001308 mRNA. Translation: AAH01308.1 .
BC010838 mRNA. Translation: AAH10838.2 .
BC012887 mRNA. Translation: AAH12887.2 . Different initiation.
BC024772 mRNA. Translation: AAH24772.1 .
AF217513 mRNA. Translation: AAF67624.1 . Frameshift.
CCDSi CCDS45234.1. [Q9BXS6-1 ]
CCDS45236.1. [Q9BXS6-2 ]
CCDS58356.1. [Q9BXS6-3 ]
CCDS58357.1. [Q9BXS6-6 ]
CCDS58358.1. [Q9BXS6-7 ]
CCDS73708.1. [Q9BXS6-5 ]
RefSeqi NP_001230071.1. NM_001243142.1. [Q9BXS6-3 ]
NP_001230072.1. NM_001243143.1. [Q9BXS6-6 ]
NP_001230073.1. NM_001243144.1. [Q9BXS6-7 ]
NP_057443.2. NM_016359.4. [Q9BXS6-1 ]
NP_060924.4. NM_018454.7. [Q9BXS6-2 ]
XP_005254487.1. XM_005254430.2. [Q9BXS6-4 ]
UniGenei Hs.615092.

3D structure databases

ProteinModelPortali Q9BXS6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119376. 27 interactions.
IntActi Q9BXS6. 1 interaction.
MINTi MINT-5009420.
STRINGi 9606.ENSP00000260359.

PTM databases

PhosphoSitei Q9BXS6.

Polymorphism databases

DMDMi 74717631.

Proteomic databases

MaxQBi Q9BXS6.
PaxDbi Q9BXS6.
PRIDEi Q9BXS6.

Protocols and materials databases

DNASUi 51203.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260359 ; ENSP00000260359 ; ENSG00000137804 . [Q9BXS6-6 ]
ENST00000414849 ; ENSP00000400746 ; ENSG00000137804 . [Q9BXS6-2 ]
ENST00000450592 ; ENSP00000401014 ; ENSG00000137804 . [Q9BXS6-7 ]
ENST00000559596 ; ENSP00000453403 ; ENSG00000137804 . [Q9BXS6-1 ]
ENST00000560177 ; ENSP00000453657 ; ENSG00000137804 . [Q9BXS6-5 ]
ENST00000560747 ; ENSP00000454097 ; ENSG00000137804 . [Q9BXS6-3 ]
GeneIDi 51203.
KEGGi hsa:51203.
UCSCi uc001znr.4. human. [Q9BXS6-2 ]
uc001zns.4. human. [Q9BXS6-1 ]
uc001znt.4. human.
uc001znu.4. human. [Q9BXS6-5 ]
uc001znv.4. human. [Q9BXS6-3 ]
uc001znw.4. human. [Q9BXS6-4 ]

Organism-specific databases

CTDi 51203.
GeneCardsi GC15P041624.
HGNCi HGNC:18538. NUSAP1.
HPAi HPA042904.
MIMi 612818. gene.
neXtProti NX_Q9BXS6.
PharmGKBi PA134987502.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG43775.
GeneTreei ENSGT00390000006370.
HOVERGENi HBG108204.
InParanoidi Q9BXS6.
OMAi AVITPFK.
OrthoDBi EOG7BP85G.
PhylomeDBi Q9BXS6.
TreeFami TF329459.

Miscellaneous databases

GenomeRNAii 51203.
NextBioi 35534796.
PROi Q9BXS6.
SOURCEi Search...

Gene expression databases

Bgeei Q9BXS6.
CleanExi HS_NUSAP1.
ExpressionAtlasi Q9BXS6. baseline and differential.
Genevestigatori Q9BXS6.

Family and domain databases

InterProi IPR026756. NuSAP.
[Graphical view ]
PANTHERi PTHR15874. PTHR15874. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Homo sapiens liver nuclear protein mRNA."
    Qu X., Zhang C., Yu Y., Wu S., Wei H., Xing G., Zhai Y., Lu C., Wang M., He F.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal liver.
  2. "A novel nucleolar protein expressed in proliferating cells."
    Sato H., Tanaka Y., Taniguchi M.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Peripheral blood.
  3. "Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs."
    Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.
    Genome Res. 11:1392-1403(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Fetal liver.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 7).
    Tissue: Neuroblastoma and Placenta.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Liver.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
  7. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORMS 2; 3 AND 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-441 (ISOFORM 4).
    Tissue: Cervix, Lung, Lymph and Placenta.
  10. "A novel gene expressed in human bone marrow."
    Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-207 (ISOFORMS 1/2).
    Tissue: Bone marrow.
  11. "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.
  12. "NuSAP is degraded by APC/C-Cdh1 and its overexpression results in mitotic arrest dependent of its microtubules' affinity."
    Li L., Zhou Y., Sun L., Xing G., Tian C., Sun J., Zhang L., He F.
    Cell. Signal. 19:2046-2055(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, UBIQUITINATION.
  13. "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: SUBCELLULAR LOCATION, ASSOCIATION WITH CHROMATIN.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; THR-182; SER-240; THR-244; SER-247; THR-314 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-240; SER-276; SER-311; THR-314 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "ATM-mediated NuSAP phosphorylation induces mitotic arrest."
    Xie P., Li L., Xing G., Tian C., Yin Y., He F., Zhang L.
    Biochem. Biophys. Res. Commun. 404:413-418(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-124 BY ATM.

Entry informationi

Entry nameiNUSAP_HUMAN
AccessioniPrimary (citable) accession number: Q9BXS6
Secondary accession number(s): B4DDF1
, E7ERR5, J3KN21, Q53GW2, Q8TBT4, Q96E58, Q96FJ1, Q9GZM9, Q9NZ85, Q9UI70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3