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Q9BXS6 (NUSAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleolar and spindle-associated protein 1

Short name=NuSAP
Gene names
Name:NUSAP1
Synonyms:ANKT
ORF Names:BM-037, PRO0310
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

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 By similarity.

Subcellular location

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. Ref.12 Ref.13

Domain

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

Post-translational modification

Ubiquitinated. Ubiquitination by FZR1 may lead to proteasome-dependent degradation of this protein. Ref.12

Phosphorylation by ATM in G2/M-phase induces mitotic arrest.

Sequence similarities

Belongs to the NUSAP family.

Sequence caution

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.

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BXS6-1)

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: Q9BXS6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     221-221: Missing.
Isoform 3 (identifier: Q9BXS6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     102-102: Missing.
     221-221: Missing.
Isoform 4 (identifier: Q9BXS6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     102-116: Missing.
     221-221: Missing.
Isoform 5 (identifier: Q9BXS6-5)

The sequence of this isoform differs from the canonical sequence as follows:
     102-102: Missing.
Isoform 6 (identifier: Q9BXS6-6)

The sequence of this isoform differs from the canonical sequence as follows:
     102-116: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q9BXS6-7)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441Nucleolar and spindle-associated protein 1
PRO_0000302034

Regions

Region237 – 382146Interaction with microtubules By similarity
Coiled coil407 – 43226 Potential
Motif384 – 3907KEN box

Amino acid modifications

Modified residue1241Phosphoserine; by ATM Ref.20
Modified residue1351Phosphoserine Ref.14 Ref.18
Modified residue1821Phosphothreonine Ref.14
Modified residue2401Phosphoserine Ref.14 Ref.18
Modified residue2441Phosphothreonine Ref.14
Modified residue2471Phosphoserine Ref.14
Modified residue2761Phosphoserine Ref.18
Modified residue3111Phosphoserine Ref.18
Modified residue3141Phosphothreonine Ref.14 Ref.18
Modified residue3381Phosphothreonine Ref.16
Modified residue3521Phosphoserine Ref.14 Ref.18
Modified residue4111N6-acetyllysine Ref.17

Natural variations

Alternative sequence32 – 5423Missing in isoform 7.
VSP_046805
Alternative sequence102 – 11615Missing in isoform 4 and isoform 6.
VSP_027910
Alternative sequence1021Missing in isoform 3 and isoform 5.
VSP_027911
Alternative sequence2211Missing in isoform 2, isoform 3, isoform 4 and isoform 7.
VSP_027912
Alternative sequence336 – 37439Missing in isoform 7.
VSP_046806
Natural variant331T → A.
Corresponds to variant rs7178634 [ dbSNP | Ensembl ].
VAR_057779
Natural variant331T → N.
Corresponds to variant rs7178777 [ dbSNP | Ensembl ].
VAR_057780

Experimental info

Sequence conflict331T → D in AL833611. Ref.6
Sequence conflict431I → V in BAD96539. Ref.5
Sequence conflict2201K → E in BAD96539. Ref.5
Sequence conflict3311G → V in BAG56712. Ref.4
Sequence conflict4411D → DQ in AL833611. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 1400E1B9F3FB727F

FASTA44149,452
        10         20         30         40         50         60 
MIIPSLEELD SLKYSDLQNL AKSLGLRANL RATKLLKALK GYIKHEARKG NENQDESQTS 

        70         80         90        100        110        120 
ASSCDETEIQ ISNQEEAERQ PLGHVTKTRR RCKTVRVDPD SQQNHSEIKI SNPTEFQNHE 

       130        140        150        160        170        180 
KQESQDLRAT AKVPSPPDEH QEAENAVSSG NRDSKVPSEG KKSLYTDESS KPGKNKRTAI 

       190        200        210        220        230        240 
TTPNFKKLHE AHFKEMESID QYIERKKKHF EEHNSMNELK QQPINKGGVR TPVPPRGRLS 

       250        260        270        280        290        300 
VASTPISQRR SQGRSCGPAS QSTLGLKGSL KRSAISAAKT GVRFSAATKD NEHKRSLTKT 

       310        320        330        340        350        360 
PARKSAHVTV SGGTPKGEAV LGTHKLKTIT GNSAAVITPF KLTTEATQTP VSNKKPVFDL 

       370        380        390        400        410        420 
KASLSRPLNY EPHKGKLKPW GQSKENNYLN QHVNRINFYK KTYKQPHLQT KEEQRKKREQ 

       430        440 
ERKEKKAKVL GMRRGLILAE D 

« Hide

Isoform 2 [UniParc].

Checksum: E903FADDD7341A2A
Show »

FASTA44049,324
Isoform 3 [UniParc].

Checksum: BF3DB4438241D00E
Show »

FASTA43949,196
Isoform 4 [UniParc].

Checksum: CD3A2D4A1838A7B4
Show »

FASTA42547,570
Isoform 5 [UniParc].

Checksum: 2496DFF76DAE07B5
Show »

FASTA44049,324
Isoform 6 [UniParc].

Checksum: DF04D86E64347EC2
Show »

FASTA42647,698
Isoform 7 [UniParc].

Checksum: 67DC255E553C7481
Show »

FASTA37842,352

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS45234.1. [Q9BXS6-1]
CCDS45236.1. [Q9BXS6-2]
CCDS58356.1. [Q9BXS6-3]
CCDS58357.1. [Q9BXS6-6]
CCDS58358.1. [Q9BXS6-7]
RefSeqNP_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_005254486.1. XM_005254429.1. [Q9BXS6-5]
XP_005254487.1. XM_005254430.2. [Q9BXS6-4]
UniGeneHs.615092.

3D structure databases

ProteinModelPortalQ9BXS6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119376. 17 interactions.
IntActQ9BXS6. 1 interaction.
MINTMINT-5009420.
STRING9606.ENSP00000260359.

PTM databases

PhosphoSiteQ9BXS6.

Polymorphism databases

DMDM74717631.

Proteomic databases

MaxQBQ9BXS6.
PaxDbQ9BXS6.
PRIDEQ9BXS6.

Protocols and materials databases

DNASU51203.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260359; 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]
GeneID51203.
KEGGhsa:51203.
UCSCuc001znr.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

CTD51203.
GeneCardsGC15P041624.
HGNCHGNC:18538. NUSAP1.
HPAHPA042904.
MIM612818. gene.
neXtProtNX_Q9BXS6.
PharmGKBPA134987502.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43775.
HOVERGENHBG108204.
InParanoidQ9BXS6.
OMAAVITPFK.
OrthoDBEOG7BP85G.
PhylomeDBQ9BXS6.
TreeFamTF329459.

Gene expression databases

ArrayExpressQ9BXS6.
BgeeQ9BXS6.
CleanExHS_NUSAP1.
GenevestigatorQ9BXS6.

Family and domain databases

InterProIPR026756. NuSAP.
[Graphical view]
PANTHERPTHR15874. PTHR15874. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi51203.
NextBio35534796.
PROQ9BXS6.
SOURCESearch...

Entry information

Entry nameNUSAP_HUMAN
AccessionPrimary (citable) accession number: Q9BXS6
Secondary accession number(s): B4DDF1 expand/collapse secondary AC list , E7ERR5, J3KN21, Q53GW2, Q8TBT4, Q96E58, Q96FJ1, Q9GZM9, Q9NZ85, Q9UI70
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM