P49321 (NASP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear autoantigenic sperm protein
Short name=NASP

Gene names

Name:

NASP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	788 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1 linker histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA By similarity.
Subunit structure	Binds to linker H1 histones but not to core histones. Also binds to HSP90 in the cytoplasm. This interaction stimulates binding of NASP to HIST1H1T/H1T By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus.
Tissue specificity	Isoform 1 is testis- and sperm-specific.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Sequence similarities	Belongs to the NASP family. Contains 3 TPR repeats.

Ontologies

Keywords
Biological process	Cell cycle DNA replication Protein transport Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat TPR repeat
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from sequence or structural similarity. Source: UniProtKB blastocyst development Inferred from sequence or structural similarity. Source: UniProtKB cell cycle Inferred from sequence or structural similarity. Source: UniProtKB cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB histone exchange Inferred from sequence or structural similarity. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	Hsp90 protein binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P49321-1)

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: P49321-2)

The sequence of this isoform differs from the canonical sequence as follows:
     138-476: Missing.

Isoform 3 (identifier: P49321-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MAMESTATAAVAAELVSADKIEDVPAPSTSADKVES → MFLLLLHLQIKWRATINLLSVTEDGLHFVEYYLNRIIH

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 788	787	Nuclear autoantigenic sperm protein		PRO_0000106299
Regions
	Repeat	43 – 76	34	TPR 1
	Repeat	542 – 575	34	TPR 2
	Repeat	584 – 617	34	TPR 3
	Region	116 – 127	12	Histone-binding
	Region	211 – 244	34	Histone-binding
	Region	469 – 512	44	Histone-binding
	Coiled coil	136 – 164	29	Potential
	Coiled coil	460 – 487	28	Potential
	Coiled coil	597 – 665	69	Potential
	Coiled coil	753 – 778	26	Potential
	Motif	716 – 722	7	Nuclear localization signal Potential
	Compositional bias	111 – 658	548	Glu-rich (acidic)
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.14
	Modified residue	30	1	Phosphoserine Ref.14
	Modified residue	33	1	N6-acetyllysine Ref.16
	Modified residue	189	1	Phosphoserine Ref.9 Ref.13
	Modified residue	228	1	Phosphothreonine Ref.11
	Modified residue	244	1	Phosphoserine Ref.9 Ref.13
	Modified residue	390	1	Phosphothreonine Ref.8 Ref.10 Ref.11 Ref.13 Ref.15
	Modified residue	408	1	Phosphoserine Ref.13
	Modified residue	421	1	Phosphoserine Ref.8 Ref.12 Ref.14
	Modified residue	451	1	Phosphoserine Ref.9 Ref.12
	Modified residue	464	1	Phosphothreonine Ref.12
	Modified residue	477	1	Phosphothreonine Ref.9 Ref.11
	Modified residue	480	1	Phosphoserine Ref.9 Ref.11
	Modified residue	497	1	Phosphoserine Ref.11 Ref.14
	Modified residue	503	1	Phosphoserine Ref.9 Ref.15
	Modified residue	683	1	Phosphothreonine Ref.13
	Modified residue	726	1	Phosphoserine Ref.9 Ref.11
Natural variations
	Alternative sequence	1 – 36	36	MAMES…DKVES → MFLLLLHLQIKWRATINLLS VTEDGLHFVEYYLNRIIH in isoform 3.		VSP_036616
	Alternative sequence	138 – 476	339	Missing in isoform 2.		VSP_006551
	Natural variant	620	1	V → G. Corresponds to variant rs34618000 [ dbSNP | Ensembl ].		VAR_052619
Experimental info
	Sequence conflict	14 – 15	2	EL → DV in AAA36027. Ref.1
	Sequence conflict	159	1	K → T in BAD96536. Ref.3
	Sequence conflict	348	1	T → Q in AAA36027. Ref.1
	Sequence conflict	633	1	Missing in AAA36027. Ref.1
	Sequence conflict	767 – 770	4	AESR → LKRG in AAA36027. Ref.1
	Sequence conflict	777	1	V → L in AAA36027. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 19, 2002. Version 2. Checksum: 0F4EB2BBE71534E8	FASTA	788	85,238
	10 20 30 40 50 60 MAMESTATAA VAAELVSADK IEDVPAPSTS ADKVESLDVD SEAKKLLGLG QKHLVMGDIP 70 80 90 100 110 120 AAVNAFQEAA SLLGKKYGET ANECGEAFFF YGKSLLELAR MENGVLGNAL EGVHVEEEEG 130 140 150 160 170 180 EKTEDESLVE NNDNIDEEAR EELREQVYDA MGEKEEAKKT EDKSLAKPET DKEQDSEMEK 190 200 210 220 230 240 GGREDMDISK SAEEPQEKVD LTLDWLTETS EEAKGGAAPE GPNEAEVTSG KPEQEVPDAE 250 260 270 280 290 300 EEKSVSGTDV QEECREKGGQ EKQGEVIVSI EEKPKEVSEE QPVVTLEKQG TAVEVEAESL 310 320 330 340 350 360 DPTVKPVDVG GDEPEEKVVT SENEAGKAVL EQLVGQEVPP AEESPEVTTE AAEASAVEAG 370 380 390 400 410 420 SEVSEKPGQE APVLPKDGAV NGPSVVGDQT PIEPQTSIER LTETKDGSGL EEKVRAKLVP 430 440 450 460 470 480 SQEETKLSVE ESEAAGDGVD TKVAQGATEK SPEDKVQIAA NEETQEREEQ MKEGEETEGS 490 500 510 520 530 540 EEDDKENDKT EEMPNDSVLE NKSLQENEEE EIGNLELAWD MLDLAKIIFK RQETKEAQLY 550 560 570 580 590 600 AAQAHLKLGE VSVESENYVQ AVEEFQSCLN LQEQYLEAHD RLLAETHYQL GLAYGYNSQY 610 620 630 640 650 660 DEAVAQFSKS IEVIENRMAV LNEQVKEAEG SSAEYKKEIE ELKELLPEIR EKIEDAKESQ 670 680 690 700 710 720 RSGNVAELAL KATLVESSTS GFTPGGGGSS VSMIASRKPT DGASSSNCVT DISHLVRKKR 730 740 750 760 770 780 KPEEESPRKD DAKKAKQEPE VNGGSGDAVP SGNEVSENME EEAENQAESR AAVEGTVEAG ATVESTAC
	Isoform 2 [UniParc]. Checksum: A69B7FE13AAA3433	FASTA	449	48,804
	10 20 30 40 50 60 MAMESTATAA VAAELVSADK IEDVPAPSTS ADKVESLDVD SEAKKLLGLG QKHLVMGDIP 70 80 90 100 110 120 AAVNAFQEAA SLLGKKYGET ANECGEAFFF YGKSLLELAR MENGVLGNAL EGVHVEEEEG 130 140 150 160 170 180 EKTEDESLVE NNDNIDETEG SEEDDKENDK TEEMPNDSVL ENKSLQENEE EEIGNLELAW 190 200 210 220 230 240 DMLDLAKIIF KRQETKEAQL YAAQAHLKLG EVSVESENYV QAVEEFQSCL NLQEQYLEAH 250 260 270 280 290 300 DRLLAETHYQ LGLAYGYNSQ YDEAVAQFSK SIEVIENRMA VLNEQVKEAE GSSAEYKKEI 310 320 330 340 350 360 EELKELLPEI REKIEDAKES QRSGNVAELA LKATLVESST SGFTPGGGGS SVSMIASRKP 370 380 390 400 410 420 TDGASSSNCV TDISHLVRKK RKPEEESPRK DDAKKAKQEP EVNGGSGDAV PSGNEVSENM 430 440 EEEAENQAES RAAVEGTVEA GATVESTAC
	Isoform 3 [UniParc]. Checksum: 6C7299FFBC62B4B2	FASTA	790	86,268
	10 20 30 40 50 60 MFLLLLHLQI KWRATINLLS VTEDGLHFVE YYLNRIIHLD VDSEAKKLLG LGQKHLVMGD 70 80 90 100 110 120 IPAAVNAFQE AASLLGKKYG ETANECGEAF FFYGKSLLEL ARMENGVLGN ALEGVHVEEE 130 140 150 160 170 180 EGEKTEDESL VENNDNIDEE AREELREQVY DAMGEKEEAK KTEDKSLAKP ETDKEQDSEM 190 200 210 220 230 240 EKGGREDMDI SKSAEEPQEK VDLTLDWLTE TSEEAKGGAA PEGPNEAEVT SGKPEQEVPD 250 260 270 280 290 300 AEEEKSVSGT DVQEECREKG GQEKQGEVIV SIEEKPKEVS EEQPVVTLEK QGTAVEVEAE 310 320 330 340 350 360 SLDPTVKPVD VGGDEPEEKV VTSENEAGKA VLEQLVGQEV PPAEESPEVT TEAAEASAVE 370 380 390 400 410 420 AGSEVSEKPG QEAPVLPKDG AVNGPSVVGD QTPIEPQTSI ERLTETKDGS GLEEKVRAKL 430 440 450 460 470 480 VPSQEETKLS VEESEAAGDG VDTKVAQGAT EKSPEDKVQI AANEETQERE EQMKEGEETE 490 500 510 520 530 540 GSEEDDKEND KTEEMPNDSV LENKSLQENE EEEIGNLELA WDMLDLAKII FKRQETKEAQ 550 560 570 580 590 600 LYAAQAHLKL GEVSVESENY VQAVEEFQSC LNLQEQYLEA HDRLLAETHY QLGLAYGYNS 610 620 630 640 650 660 QYDEAVAQFS KSIEVIENRM AVLNEQVKEA EGSSAEYKKE IEELKELLPE IREKIEDAKE 670 680 690 700 710 720 SQRSGNVAEL ALKATLVESS TSGFTPGGGG SSVSMIASRK PTDGASSSNC VTDISHLVRK 730 740 750 760 770 780 KRKPEEESPR KDDAKKAKQE PEVNGGSGDA VPSGNEVSEN MEEEAENQAE SRAAVEGTVE 790 AGATVESTAC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and localization of human NASP: conservation of a Xenopus histone-binding protein." O'Rand M.G., Richardson R.T., Zimmerman L.J., Widgren E.E. Dev. Biol. 154:37-44(1992) [PubMed: 1426632] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-635 (ISOFORM 3). Tissue: Placenta and Teratocarcinoma.
[3]	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 1). Tissue: Liver.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Eye, Lung, Placenta and Testis.
[7]	"Histone-binding domains in a human nuclear autoantigenic sperm protein." Batova I., O'Rand M.G. Biol. Reprod. 54:1238-1244(1996) [PubMed: 8724350] [Abstract] Cited for: HISTONE-BINDING REGIONS.
[8]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390 AND SER-421, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-244; SER-451; THR-477; SER-480; SER-503 AND SER-726, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-228; THR-390; THR-477; SER-480; SER-497 AND SER-726, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421; SER-451 AND THR-464, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-244; THR-390; SER-408 AND THR-683, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-421 AND SER-497, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390 AND SER-503, 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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, MASS SPECTROMETRY.
[17]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M97856 mRNA. Translation: AAA36027.1. AK056161 mRNA. No translation available. AK291637 mRNA. Translation: BAF84326.1. AK222816 mRNA. Translation: BAD96536.1. AL355480 Genomic DNA. Translation: CAI22462.1. AL355480 Genomic DNA. Translation: CAI22465.1. CH471059 Genomic DNA. Translation: EAX06968.1. CH471059 Genomic DNA. Translation: EAX06969.1. BC003113 mRNA. Translation: AAH03113.1. BC053608 mRNA. Translation: AAH53608.1. BC010105 mRNA. Translation: AAH10105.1. BC011580 mRNA. Translation: AAH11580.1.
IPI	IPI00179953. IPI00219821. IPI00332499.
PIR	A48819.
RefSeq	NP_001182122.1. NM_001195193.1. NP_002473.2. NM_002482.3. NP_689511.2. NM_152298.3.
UniGene	Hs.319334.
3D structure databases
ProteinModelPortal	P49321.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-47269N.
IntAct	P49321. 8 interactions.
STRING	P49321.
PTM databases
PhosphoSite	P49321.
Polymorphism databases
DMDM	23503077.
Proteomic databases
PRIDE	P49321.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000350030; ENSP00000255120; ENSG00000132780.
GeneID	4678.
KEGG	hsa:4678.
UCSC	uc001coi.1. human.
Organism-specific databases
CTD	4678.
GeneCards	GC01P046049.
H-InvDB	HIX0000535.
HGNC	HGNC:7644. NASP.
MIM	603185. gene.
neXtProt	NX_P49321.
PharmGKB	PA31448.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG002186.
OMA	GGDEPKE.
Gene expression databases
ArrayExpress	P49321.
Bgee	P49321.
CleanEx	HS_NASP.
Genevestigator	P49321.
GermOnline	ENSG00000132780. Homo sapiens.
Family and domain databases
InterPro	IPR019544. Tetratricopeptide_SHNi-TPR_dom. IPR001440. TPR-1. IPR013026. TPR-contain. IPR011990. TPR-like_helical. IPR019734. TPR_repeat. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 2 hits.
KO	K11291.
Pfam	PF10516. SHNi-TPR. 1 hit. PF00515. TPR_1. 1 hit. [Graphical view]
SMART	SM00028. TPR. 3 hits. [Graphical view]
PROSITE	PS50005. TPR. 3 hits. PS50293. TPR_REGION. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	18032.
PMAP-CutDB	P49321.
SOURCE	Search...

Entry information

Entry name

NASP_HUMAN

Accession

Primary (citable) accession number: P49321
Secondary accession number(s): A8K6H2 , D3DQ07, Q53GW5, Q5T622, Q5T625, Q96A69, Q9BTW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	September 19, 2002
Last modified:	January 25, 2012
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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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.