Q9BXS6 (NUSAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	NUSAP1
Synonyms:	ANKT
ORF Names:	BM-037, PRO0310

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	441 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 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. Nucleus › nucleolus By similarity. Cytoplasm › cytoskeleton › spindle 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
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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Chromosome Cytoplasm Cytoskeleton Microtubule Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokinesis after mitosis Inferred from direct assay Ref.11. Source: MGI establishment of mitotic spindle localization Inferred from direct assay Ref.11. Source: MGI mitotic chromosome condensation Inferred from direct assay Ref.11. Source: MGI positive regulation of mitosis Inferred from direct assay Ref.11. Source: MGI
Cellular_component	chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay. Source: HPA spindle microtubule Inferred from electronic annotation. Source: Compara
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 6 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 441	441	Nucleolar and spindle-associated protein 1		PRO_0000302034
Regions
	Region	237 – 382	146	Interaction with microtubules By similarity
	Coiled coil	407 – 432	26	Potential
	Motif	384 – 390	7	KEN box
Amino acid modifications
	Modified residue	135	1	Phosphoserine Ref.14 Ref.17
	Modified residue	182	1	Phosphothreonine Ref.14
	Modified residue	240	1	Phosphoserine Ref.14 Ref.17
	Modified residue	244	1	Phosphothreonine Ref.14
	Modified residue	247	1	Phosphoserine Ref.14
	Modified residue	276	1	Phosphoserine Ref.17
	Modified residue	311	1	Phosphoserine Ref.17
	Modified residue	314	1	Phosphothreonine Ref.14 Ref.17
	Modified residue	338	1	Phosphothreonine Ref.15
	Modified residue	352	1	Phosphoserine Ref.14 Ref.17
	Modified residue	411	1	N6-acetyllysine Ref.16
Natural variations
	Alternative sequence	102 – 116	15	Missing in isoform 4 and isoform 6.		VSP_027910
	Alternative sequence	102	1	Missing in isoform 3 and isoform 5.		VSP_027911
	Alternative sequence	221	1	Missing in isoform 2, isoform 3 and isoform 4.		VSP_027912
	Natural variant	33	1	T → A. Corresponds to variant rs7178634 [ dbSNP | Ensembl ].		VAR_057779
	Natural variant	33	1	T → N. Corresponds to variant rs7178777 [ dbSNP | Ensembl ].		VAR_057780
Experimental info
	Sequence conflict	33	1	T → D in AL833611. Ref.6
	Sequence conflict	43	1	I → V in BAD96539. Ref.5
	Sequence conflict	220	1	K → E in BAD96539. Ref.5
	Sequence conflict	441	1	D → DQ in AL833611. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 1400E1B9F3FB727F	FASTA	441	49,452
	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
	Isoform 2 [UniParc]. Checksum: E903FADDD7341A2A	FASTA	440	49,324
	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 QPINKGGVRT PVPPRGRLSV 250 260 270 280 290 300 ASTPISQRRS QGRSCGPASQ STLGLKGSLK RSAISAAKTG VRFSAATKDN EHKRSLTKTP 310 320 330 340 350 360 ARKSAHVTVS GGTPKGEAVL GTHKLKTITG NSAAVITPFK LTTEATQTPV SNKKPVFDLK 370 380 390 400 410 420 ASLSRPLNYE PHKGKLKPWG QSKENNYLNQ HVNRINFYKK TYKQPHLQTK EEQRKKREQE 430 440 RKEKKAKVLG MRRGLILAED
	Isoform 3 [UniParc]. Checksum: BF3DB4438241D00E	FASTA	439	49,196
	10 20 30 40 50 60 MIIPSLEELD SLKYSDLQNL AKSLGLRANL RATKLLKALK GYIKHEARKG NENQDESQTS 70 80 90 100 110 120 ASSCDETEIQ ISNQEEAERQ PLGHVTKTRR RCKTVRVDPD SQNHSEIKIS NPTEFQNHEK 130 140 150 160 170 180 QESQDLRATA KVPSPPDEHQ EAENAVSSGN RDSKVPSEGK KSLYTDESSK PGKNKRTAIT 190 200 210 220 230 240 TPNFKKLHEA HFKEMESIDQ YIERKKKHFE EHNSMNELKQ PINKGGVRTP VPPRGRLSVA 250 260 270 280 290 300 STPISQRRSQ GRSCGPASQS TLGLKGSLKR SAISAAKTGV RFSAATKDNE HKRSLTKTPA 310 320 330 340 350 360 RKSAHVTVSG GTPKGEAVLG THKLKTITGN SAAVITPFKL TTEATQTPVS NKKPVFDLKA 370 380 390 400 410 420 SLSRPLNYEP HKGKLKPWGQ SKENNYLNQH VNRINFYKKT YKQPHLQTKE EQRKKREQER 430 KEKKAKVLGM RRGLILAED
	Isoform 4 [UniParc]. Checksum: CD3A2D4A1838A7B4	FASTA	425	47,570
	10 20 30 40 50 60 MIIPSLEELD SLKYSDLQNL AKSLGLRANL RATKLLKALK GYIKHEARKG NENQDESQTS 70 80 90 100 110 120 ASSCDETEIQ ISNQEEAERQ PLGHVTKTRR RCKTVRVDPD SQNHEKQESQ DLRATAKVPS 130 140 150 160 170 180 PPDEHQEAEN AVSSGNRDSK VPSEGKKSLY TDESSKPGKN KRTAITTPNF KKLHEAHFKE 190 200 210 220 230 240 MESIDQYIER KKKHFEEHNS MNELKQPINK GGVRTPVPPR GRLSVASTPI SQRRSQGRSC 250 260 270 280 290 300 GPASQSTLGL KGSLKRSAIS AAKTGVRFSA ATKDNEHKRS LTKTPARKSA HVTVSGGTPK 310 320 330 340 350 360 GEAVLGTHKL KTITGNSAAV ITPFKLTTEA TQTPVSNKKP VFDLKASLSR PLNYEPHKGK 370 380 390 400 410 420 LKPWGQSKEN NYLNQHVNRI NFYKKTYKQP HLQTKEEQRK KREQERKEKK AKVLGMRRGL ILAED
	Isoform 5 [UniParc]. Checksum: 2496DFF76DAE07B5	FASTA	440	49,324
	10 20 30 40 50 60 MIIPSLEELD SLKYSDLQNL AKSLGLRANL RATKLLKALK GYIKHEARKG NENQDESQTS 70 80 90 100 110 120 ASSCDETEIQ ISNQEEAERQ PLGHVTKTRR RCKTVRVDPD SQNHSEIKIS NPTEFQNHEK 130 140 150 160 170 180 QESQDLRATA KVPSPPDEHQ EAENAVSSGN RDSKVPSEGK KSLYTDESSK PGKNKRTAIT 190 200 210 220 230 240 TPNFKKLHEA HFKEMESIDQ YIERKKKHFE EHNSMNELKQ QPINKGGVRT PVPPRGRLSV 250 260 270 280 290 300 ASTPISQRRS QGRSCGPASQ STLGLKGSLK RSAISAAKTG VRFSAATKDN EHKRSLTKTP 310 320 330 340 350 360 ARKSAHVTVS GGTPKGEAVL GTHKLKTITG NSAAVITPFK LTTEATQTPV SNKKPVFDLK 370 380 390 400 410 420 ASLSRPLNYE PHKGKLKPWG QSKENNYLNQ HVNRINFYKK TYKQPHLQTK EEQRKKREQE 430 440 RKEKKAKVLG MRRGLILAED
	Isoform 6 [UniParc]. Checksum: DF04D86E64347EC2	FASTA	426	47,698
	10 20 30 40 50 60 MIIPSLEELD SLKYSDLQNL AKSLGLRANL RATKLLKALK GYIKHEARKG NENQDESQTS 70 80 90 100 110 120 ASSCDETEIQ ISNQEEAERQ PLGHVTKTRR RCKTVRVDPD SQNHEKQESQ DLRATAKVPS 130 140 150 160 170 180 PPDEHQEAEN AVSSGNRDSK VPSEGKKSLY TDESSKPGKN KRTAITTPNF KKLHEAHFKE 190 200 210 220 230 240 MESIDQYIER KKKHFEEHNS MNELKQQPIN KGGVRTPVPP RGRLSVASTP ISQRRSQGRS 250 260 270 280 290 300 CGPASQSTLG LKGSLKRSAI SAAKTGVRFS AATKDNEHKR SLTKTPARKS AHVTVSGGTP 310 320 330 340 350 360 KGEAVLGTHK LKTITGNSAA VITPFKLTTE ATQTPVSNKK PVFDLKASLS RPLNYEPHKG 370 380 390 400 410 420 KLKPWGQSKE NNYLNQHVNR INFYKKTYKQ PHLQTKEEQR KKREQERKEK KAKVLGMRRG LILAED

References

	« Hide 'large scale' referencesShow '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. , 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] (ISOFORM 2). Tissue: 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. , 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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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, MASS SPECTROMETRY.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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].
+	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. 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.
IPI	IPI00000398. IPI00020484. IPI00789679. IPI00793551. IPI00855788.
RefSeq	NP_001230071.1. NM_001243142.1. NP_001230072.1. NM_001243143.1. NP_001230073.1. NM_001243144.1. NP_057443.2. NM_016359.4. NP_060924.4. NM_018454.7.
UniGene	Hs.615092.
3D structure databases
ProteinModelPortal	Q9BXS6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BXS6. 1 interaction.
STRING	9606.ENSP00000260359.
PTM databases
PhosphoSite	Q9BXS6.
Polymorphism databases
DMDM	74717631.
Proteomic databases
PaxDb	Q9BXS6.
PRIDE	Q9BXS6.
Protocols and materials databases
DNASU	51203.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000260359; ENSP00000260359; ENSG00000137804. ENST00000414849; ENSP00000400746; ENSG00000137804. ENST00000559596; ENSP00000453403; ENSG00000137804. ENST00000560177; ENSP00000453657; ENSG00000137804. ENST00000560747; ENSP00000454097; ENSG00000137804.
GeneID	51203.
KEGG	hsa:51203.
UCSC	uc001znr.4. human. uc001zns.4. human. uc001znu.4. human. uc001znv.4. human. uc001znw.4. human.
Organism-specific databases
CTD	51203.
GeneCards	GC15P041624.
HGNC	HGNC:18538. NUSAP1.
HPA	HPA042904.
MIM	612818. gene.
neXtProt	NX_Q9BXS6.
PharmGKB	PA134987502.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG43775.
HOVERGEN	HBG108204.
InParanoid	Q9BXS6.
OMA	AVITPFK.
PhylomeDB	Q9BXS6.
Gene expression databases
ArrayExpress	Q9BXS6.
Bgee	Q9BXS6.
CleanEx	HS_NUSAP1.
Genevestigator	Q9BXS6.
Family and domain databases
InterPro	IPR026756. NuSAP. [Graphical view]
PANTHER	PTHR32473:SF0. PTHR32473:SF0. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	51203.
NextBio	54244.
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Entry information

Entry name

NUSAP_HUMAN

Accession

Primary (citable) accession number: Q9BXS6
Secondary accession number(s): 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:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.