Full text data of NASP
NASP
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Nuclear autoantigenic sperm protein; NASP
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Nuclear autoantigenic sperm protein; NASP
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P49321
ID NASP_HUMAN Reviewed; 788 AA.
AC P49321; A8K6H2; B4DQP3; D3DQ07; F5H3J2; Q53GW5; Q5T622; Q5T625;
read moreAC Q96A69; Q9BTW2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Nuclear autoantigenic sperm protein;
DE Short=NASP;
GN Name=NASP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=1426632; DOI=10.1016/0012-1606(92)90045-I;
RA O'Rand M.G., Richardson R.T., Zimmerman L.J., Widgren E.E.;
RT "Sequence and localization of human NASP: conservation of a Xenopus
RT histone-binding protein.";
RL Dev. Biol. 154:37-44(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-635 (ISOFORM 3).
RC TISSUE=Placenta, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, Lung, Placenta, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP HISTONE-BINDING REGIONS.
RX PubMed=8724350;
RA Batova I., O'Rand M.G.;
RT "Histone-binding domains in a human nuclear autoantigenic sperm
RT protein.";
RL Biol. Reprod. 54:1238-1244(1996).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-451; SER-503
RP AND SER-726, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141
RP (ISOFORM 2), AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-464, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-244; THR-390;
RP SER-408 AND THR-683, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-123; SER-127; SER-189;
RP SER-451; THR-490; SER-497 AND SER-503, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-138 AND SER-141 (ISOFORM 2), AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-123; SER-127; SER-189;
RP SER-244; SER-299; SER-321; THR-390; SER-408; SER-421; SER-451;
RP THR-464; THR-477; SER-480; THR-490; SER-497; SER-503; SER-726 AND
RP SER-751, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138 AND SER-141
RP (ISOFORM 2), AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Required for DNA replication, normal cell cycle
CC progression and cell proliferation. Forms a cytoplasmic complex
CC with HSP90 and H1 linker histones and stimulates HSP90 ATPase
CC activity. NASP and H1 histone are subsequently released from the
CC complex and translocate to the nucleus where the histone is
CC released for binding to DNA (By similarity).
CC -!- SUBUNIT: Binds to linker H1 histones but not to core histones.
CC Also binds to HSP90 in the cytoplasm. This interaction stimulates
CC binding of NASP to HIST1H1T/H1T (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P49321-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49321-2; Sequence=VSP_006551;
CC Note=Contains a phosphoserine at position 141. Contains a
CC phosphothreonine at position 138;
CC Name=3;
CC IsoId=P49321-3; Sequence=VSP_036616;
CC Name=4;
CC IsoId=P49321-4; Sequence=VSP_047028;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Isoform 1 is testis- and sperm-specific.
CC -!- SIMILARITY: Belongs to the NASP family.
CC -!- SIMILARITY: Contains 3 TPR repeats.
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DR EMBL; M97856; AAA36027.1; -; mRNA.
DR EMBL; AK056161; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK291637; BAF84326.1; -; mRNA.
DR EMBL; AK298893; BAG61005.1; -; mRNA.
DR EMBL; AK222816; BAD96536.1; -; mRNA.
DR EMBL; AL355480; CAI22462.1; -; Genomic_DNA.
DR EMBL; AL355480; CAI22465.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06968.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06969.1; -; Genomic_DNA.
DR EMBL; BC003113; AAH03113.1; -; mRNA.
DR EMBL; BC053608; AAH53608.1; -; mRNA.
DR EMBL; BC010105; AAH10105.1; -; mRNA.
DR EMBL; BC011580; AAH11580.1; -; mRNA.
DR PIR; A48819; A48819.
DR RefSeq; NP_001182122.1; NM_001195193.1.
DR RefSeq; NP_002473.2; NM_002482.3.
DR RefSeq; NP_689511.2; NM_152298.3.
DR RefSeq; XP_005270945.1; XM_005270888.1.
DR UniGene; Hs.319334; -.
DR ProteinModelPortal; P49321; -.
DR DIP; DIP-47269N; -.
DR IntAct; P49321; 10.
DR MINT; MINT-4656497; -.
DR STRING; 9606.ENSP00000345532; -.
DR PhosphoSite; P49321; -.
DR DMDM; 23503077; -.
DR PaxDb; P49321; -.
DR PRIDE; P49321; -.
DR DNASU; 4678; -.
DR Ensembl; ENST00000350030; ENSP00000255120; ENSG00000132780.
DR Ensembl; ENST00000351223; ENSP00000255121; ENSG00000132780.
DR Ensembl; ENST00000402363; ENSP00000384529; ENSG00000132780.
DR Ensembl; ENST00000537798; ENSP00000438871; ENSG00000132780.
DR GeneID; 4678; -.
DR KEGG; hsa:4678; -.
DR UCSC; uc010olr.2; human.
DR CTD; 4678; -.
DR GeneCards; GC01P046049; -.
DR HGNC; HGNC:7644; NASP.
DR MIM; 603185; gene.
DR neXtProt; NX_P49321; -.
DR PharmGKB; PA31448; -.
DR eggNOG; NOG135556; -.
DR HOVERGEN; HBG002186; -.
DR KO; K11291; -.
DR OMA; REKGGQE; -.
DR OrthoDB; EOG7X9G7Z; -.
DR ChiTaRS; NASP; human.
DR GeneWiki; NASP_(gene); -.
DR GenomeRNAi; 4678; -.
DR NextBio; 18032; -.
DR PMAP-CutDB; P49321; -.
DR PRO; PR:P49321; -.
DR ArrayExpress; P49321; -.
DR Bgee; P49321; -.
DR CleanEx; HS_NASP; -.
DR Genevestigator; P49321; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; ISS:UniProtKB.
DR GO; GO:0001824; P:blastocyst development; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; ISS:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0043486; P:histone exchange; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR019544; Tetratricopeptide_SHNi-TPR_dom.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF10516; SHNi-TPR; 1.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00028; TPR; 3.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Coiled coil;
KW Complete proteome; Cytoplasm; DNA replication; Nucleus;
KW Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW Repeat; TPR repeat; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 788 Nuclear autoantigenic sperm protein.
FT /FTId=PRO_0000106299.
FT REPEAT 43 76 TPR 1.
FT REPEAT 542 575 TPR 2.
FT REPEAT 584 617 TPR 3.
FT REGION 116 127 Histone-binding.
FT REGION 211 244 Histone-binding.
FT REGION 469 512 Histone-binding.
FT COILED 136 164 Potential.
FT COILED 460 487 Potential.
FT COILED 597 665 Potential.
FT COILED 753 778 Potential.
FT MOTIF 716 722 Nuclear localization signal (Potential).
FT COMPBIAS 111 658 Glu-rich (acidic).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 33 33 N6-acetyllysine.
FT MOD_RES 123 123 Phosphothreonine.
FT MOD_RES 127 127 Phosphoserine.
FT MOD_RES 189 189 Phosphoserine.
FT MOD_RES 244 244 Phosphoserine.
FT MOD_RES 299 299 Phosphoserine.
FT MOD_RES 321 321 Phosphoserine.
FT MOD_RES 390 390 Phosphothreonine.
FT MOD_RES 408 408 Phosphoserine.
FT MOD_RES 421 421 Phosphoserine.
FT MOD_RES 451 451 Phosphoserine.
FT MOD_RES 464 464 Phosphothreonine.
FT MOD_RES 477 477 Phosphothreonine.
FT MOD_RES 480 480 Phosphoserine.
FT MOD_RES 490 490 Phosphothreonine.
FT MOD_RES 497 497 Phosphoserine.
FT MOD_RES 503 503 Phosphoserine.
FT MOD_RES 683 683 Phosphothreonine.
FT MOD_RES 726 726 Phosphoserine.
FT MOD_RES 751 751 Phosphoserine.
FT VAR_SEQ 1 36 MAMESTATAAVAAELVSADKIEDVPAPSTSADKVES -> M
FT FLLLLHLQIKWRATINLLSVTEDGLHFVEYYLNRIIH (in
FT isoform 3).
FT /FTId=VSP_036616.
FT VAR_SEQ 36 99 Missing (in isoform 4).
FT /FTId=VSP_047028.
FT VAR_SEQ 138 476 Missing (in isoform 2).
FT /FTId=VSP_006551.
FT VARIANT 620 620 V -> G (in dbSNP:rs34618000).
FT /FTId=VAR_052619.
FT CONFLICT 14 15 EL -> DV (in Ref. 1; AAA36027).
FT CONFLICT 159 159 K -> T (in Ref. 3; BAD96536).
FT CONFLICT 183 183 R -> G (in Ref. 2; BAG61005).
FT CONFLICT 348 348 T -> Q (in Ref. 1; AAA36027).
FT CONFLICT 633 633 Missing (in Ref. 1; AAA36027).
FT CONFLICT 767 770 AESR -> LKRG (in Ref. 1; AAA36027).
FT CONFLICT 777 777 V -> L (in Ref. 1; AAA36027).
SQ SEQUENCE 788 AA; 85238 MW; 0F4EB2BBE71534E8 CRC64;
MAMESTATAA VAAELVSADK IEDVPAPSTS ADKVESLDVD SEAKKLLGLG QKHLVMGDIP
AAVNAFQEAA SLLGKKYGET ANECGEAFFF YGKSLLELAR MENGVLGNAL EGVHVEEEEG
EKTEDESLVE NNDNIDEEAR EELREQVYDA MGEKEEAKKT EDKSLAKPET DKEQDSEMEK
GGREDMDISK SAEEPQEKVD LTLDWLTETS EEAKGGAAPE GPNEAEVTSG KPEQEVPDAE
EEKSVSGTDV QEECREKGGQ EKQGEVIVSI EEKPKEVSEE QPVVTLEKQG TAVEVEAESL
DPTVKPVDVG GDEPEEKVVT SENEAGKAVL EQLVGQEVPP AEESPEVTTE AAEASAVEAG
SEVSEKPGQE APVLPKDGAV NGPSVVGDQT PIEPQTSIER LTETKDGSGL EEKVRAKLVP
SQEETKLSVE ESEAAGDGVD TKVAQGATEK SPEDKVQIAA NEETQEREEQ MKEGEETEGS
EEDDKENDKT EEMPNDSVLE NKSLQENEEE EIGNLELAWD MLDLAKIIFK RQETKEAQLY
AAQAHLKLGE VSVESENYVQ AVEEFQSCLN LQEQYLEAHD RLLAETHYQL GLAYGYNSQY
DEAVAQFSKS IEVIENRMAV LNEQVKEAEG SSAEYKKEIE ELKELLPEIR EKIEDAKESQ
RSGNVAELAL KATLVESSTS GFTPGGGGSS VSMIASRKPT DGASSSNCVT DISHLVRKKR
KPEEESPRKD DAKKAKQEPE VNGGSGDAVP SGNEVSENME EEAENQAESR AAVEGTVEAG
ATVESTAC
//
ID NASP_HUMAN Reviewed; 788 AA.
AC P49321; A8K6H2; B4DQP3; D3DQ07; F5H3J2; Q53GW5; Q5T622; Q5T625;
read moreAC Q96A69; Q9BTW2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Nuclear autoantigenic sperm protein;
DE Short=NASP;
GN Name=NASP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=1426632; DOI=10.1016/0012-1606(92)90045-I;
RA O'Rand M.G., Richardson R.T., Zimmerman L.J., Widgren E.E.;
RT "Sequence and localization of human NASP: conservation of a Xenopus
RT histone-binding protein.";
RL Dev. Biol. 154:37-44(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-635 (ISOFORM 3).
RC TISSUE=Placenta, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, Lung, Placenta, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP HISTONE-BINDING REGIONS.
RX PubMed=8724350;
RA Batova I., O'Rand M.G.;
RT "Histone-binding domains in a human nuclear autoantigenic sperm
RT protein.";
RL Biol. Reprod. 54:1238-1244(1996).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-451; SER-503
RP AND SER-726, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141
RP (ISOFORM 2), AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-464, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-244; THR-390;
RP SER-408 AND THR-683, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-123; SER-127; SER-189;
RP SER-451; THR-490; SER-497 AND SER-503, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-138 AND SER-141 (ISOFORM 2), AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-123; SER-127; SER-189;
RP SER-244; SER-299; SER-321; THR-390; SER-408; SER-421; SER-451;
RP THR-464; THR-477; SER-480; THR-490; SER-497; SER-503; SER-726 AND
RP SER-751, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138 AND SER-141
RP (ISOFORM 2), AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Required for DNA replication, normal cell cycle
CC progression and cell proliferation. Forms a cytoplasmic complex
CC with HSP90 and H1 linker histones and stimulates HSP90 ATPase
CC activity. NASP and H1 histone are subsequently released from the
CC complex and translocate to the nucleus where the histone is
CC released for binding to DNA (By similarity).
CC -!- SUBUNIT: Binds to linker H1 histones but not to core histones.
CC Also binds to HSP90 in the cytoplasm. This interaction stimulates
CC binding of NASP to HIST1H1T/H1T (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P49321-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49321-2; Sequence=VSP_006551;
CC Note=Contains a phosphoserine at position 141. Contains a
CC phosphothreonine at position 138;
CC Name=3;
CC IsoId=P49321-3; Sequence=VSP_036616;
CC Name=4;
CC IsoId=P49321-4; Sequence=VSP_047028;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Isoform 1 is testis- and sperm-specific.
CC -!- SIMILARITY: Belongs to the NASP family.
CC -!- SIMILARITY: Contains 3 TPR repeats.
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DR EMBL; M97856; AAA36027.1; -; mRNA.
DR EMBL; AK056161; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK291637; BAF84326.1; -; mRNA.
DR EMBL; AK298893; BAG61005.1; -; mRNA.
DR EMBL; AK222816; BAD96536.1; -; mRNA.
DR EMBL; AL355480; CAI22462.1; -; Genomic_DNA.
DR EMBL; AL355480; CAI22465.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06968.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06969.1; -; Genomic_DNA.
DR EMBL; BC003113; AAH03113.1; -; mRNA.
DR EMBL; BC053608; AAH53608.1; -; mRNA.
DR EMBL; BC010105; AAH10105.1; -; mRNA.
DR EMBL; BC011580; AAH11580.1; -; mRNA.
DR PIR; A48819; A48819.
DR RefSeq; NP_001182122.1; NM_001195193.1.
DR RefSeq; NP_002473.2; NM_002482.3.
DR RefSeq; NP_689511.2; NM_152298.3.
DR RefSeq; XP_005270945.1; XM_005270888.1.
DR UniGene; Hs.319334; -.
DR ProteinModelPortal; P49321; -.
DR DIP; DIP-47269N; -.
DR IntAct; P49321; 10.
DR MINT; MINT-4656497; -.
DR STRING; 9606.ENSP00000345532; -.
DR PhosphoSite; P49321; -.
DR DMDM; 23503077; -.
DR PaxDb; P49321; -.
DR PRIDE; P49321; -.
DR DNASU; 4678; -.
DR Ensembl; ENST00000350030; ENSP00000255120; ENSG00000132780.
DR Ensembl; ENST00000351223; ENSP00000255121; ENSG00000132780.
DR Ensembl; ENST00000402363; ENSP00000384529; ENSG00000132780.
DR Ensembl; ENST00000537798; ENSP00000438871; ENSG00000132780.
DR GeneID; 4678; -.
DR KEGG; hsa:4678; -.
DR UCSC; uc010olr.2; human.
DR CTD; 4678; -.
DR GeneCards; GC01P046049; -.
DR HGNC; HGNC:7644; NASP.
DR MIM; 603185; gene.
DR neXtProt; NX_P49321; -.
DR PharmGKB; PA31448; -.
DR eggNOG; NOG135556; -.
DR HOVERGEN; HBG002186; -.
DR KO; K11291; -.
DR OMA; REKGGQE; -.
DR OrthoDB; EOG7X9G7Z; -.
DR ChiTaRS; NASP; human.
DR GeneWiki; NASP_(gene); -.
DR GenomeRNAi; 4678; -.
DR NextBio; 18032; -.
DR PMAP-CutDB; P49321; -.
DR PRO; PR:P49321; -.
DR ArrayExpress; P49321; -.
DR Bgee; P49321; -.
DR CleanEx; HS_NASP; -.
DR Genevestigator; P49321; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; ISS:UniProtKB.
DR GO; GO:0001824; P:blastocyst development; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; ISS:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0043486; P:histone exchange; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR019544; Tetratricopeptide_SHNi-TPR_dom.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF10516; SHNi-TPR; 1.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00028; TPR; 3.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Coiled coil;
KW Complete proteome; Cytoplasm; DNA replication; Nucleus;
KW Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW Repeat; TPR repeat; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 788 Nuclear autoantigenic sperm protein.
FT /FTId=PRO_0000106299.
FT REPEAT 43 76 TPR 1.
FT REPEAT 542 575 TPR 2.
FT REPEAT 584 617 TPR 3.
FT REGION 116 127 Histone-binding.
FT REGION 211 244 Histone-binding.
FT REGION 469 512 Histone-binding.
FT COILED 136 164 Potential.
FT COILED 460 487 Potential.
FT COILED 597 665 Potential.
FT COILED 753 778 Potential.
FT MOTIF 716 722 Nuclear localization signal (Potential).
FT COMPBIAS 111 658 Glu-rich (acidic).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 33 33 N6-acetyllysine.
FT MOD_RES 123 123 Phosphothreonine.
FT MOD_RES 127 127 Phosphoserine.
FT MOD_RES 189 189 Phosphoserine.
FT MOD_RES 244 244 Phosphoserine.
FT MOD_RES 299 299 Phosphoserine.
FT MOD_RES 321 321 Phosphoserine.
FT MOD_RES 390 390 Phosphothreonine.
FT MOD_RES 408 408 Phosphoserine.
FT MOD_RES 421 421 Phosphoserine.
FT MOD_RES 451 451 Phosphoserine.
FT MOD_RES 464 464 Phosphothreonine.
FT MOD_RES 477 477 Phosphothreonine.
FT MOD_RES 480 480 Phosphoserine.
FT MOD_RES 490 490 Phosphothreonine.
FT MOD_RES 497 497 Phosphoserine.
FT MOD_RES 503 503 Phosphoserine.
FT MOD_RES 683 683 Phosphothreonine.
FT MOD_RES 726 726 Phosphoserine.
FT MOD_RES 751 751 Phosphoserine.
FT VAR_SEQ 1 36 MAMESTATAAVAAELVSADKIEDVPAPSTSADKVES -> M
FT FLLLLHLQIKWRATINLLSVTEDGLHFVEYYLNRIIH (in
FT isoform 3).
FT /FTId=VSP_036616.
FT VAR_SEQ 36 99 Missing (in isoform 4).
FT /FTId=VSP_047028.
FT VAR_SEQ 138 476 Missing (in isoform 2).
FT /FTId=VSP_006551.
FT VARIANT 620 620 V -> G (in dbSNP:rs34618000).
FT /FTId=VAR_052619.
FT CONFLICT 14 15 EL -> DV (in Ref. 1; AAA36027).
FT CONFLICT 159 159 K -> T (in Ref. 3; BAD96536).
FT CONFLICT 183 183 R -> G (in Ref. 2; BAG61005).
FT CONFLICT 348 348 T -> Q (in Ref. 1; AAA36027).
FT CONFLICT 633 633 Missing (in Ref. 1; AAA36027).
FT CONFLICT 767 770 AESR -> LKRG (in Ref. 1; AAA36027).
FT CONFLICT 777 777 V -> L (in Ref. 1; AAA36027).
SQ SEQUENCE 788 AA; 85238 MW; 0F4EB2BBE71534E8 CRC64;
MAMESTATAA VAAELVSADK IEDVPAPSTS ADKVESLDVD SEAKKLLGLG QKHLVMGDIP
AAVNAFQEAA SLLGKKYGET ANECGEAFFF YGKSLLELAR MENGVLGNAL EGVHVEEEEG
EKTEDESLVE NNDNIDEEAR EELREQVYDA MGEKEEAKKT EDKSLAKPET DKEQDSEMEK
GGREDMDISK SAEEPQEKVD LTLDWLTETS EEAKGGAAPE GPNEAEVTSG KPEQEVPDAE
EEKSVSGTDV QEECREKGGQ EKQGEVIVSI EEKPKEVSEE QPVVTLEKQG TAVEVEAESL
DPTVKPVDVG GDEPEEKVVT SENEAGKAVL EQLVGQEVPP AEESPEVTTE AAEASAVEAG
SEVSEKPGQE APVLPKDGAV NGPSVVGDQT PIEPQTSIER LTETKDGSGL EEKVRAKLVP
SQEETKLSVE ESEAAGDGVD TKVAQGATEK SPEDKVQIAA NEETQEREEQ MKEGEETEGS
EEDDKENDKT EEMPNDSVLE NKSLQENEEE EIGNLELAWD MLDLAKIIFK RQETKEAQLY
AAQAHLKLGE VSVESENYVQ AVEEFQSCLN LQEQYLEAHD RLLAETHYQL GLAYGYNSQY
DEAVAQFSKS IEVIENRMAV LNEQVKEAEG SSAEYKKEIE ELKELLPEIR EKIEDAKESQ
RSGNVAELAL KATLVESSTS GFTPGGGGSS VSMIASRKPT DGASSSNCVT DISHLVRKKR
KPEEESPRKD DAKKAKQEPE VNGGSGDAVP SGNEVSENME EEAENQAESR AAVEGTVEAG
ATVESTAC
//
MIM
603185
*RECORD*
*FIELD* NO
603185
*FIELD* TI
*603185 NUCLEAR AUTOANTIGENIC SPERM PROTEIN; NASP
;;N1/N2, XENOPUS, HOMOLOG OF
*FIELD* TX
read moreDuring mammalian spermatogenesis, testis-specific histones (see H1FT;
142712) and other testis- and sperm-specific proteins are expressed.
NASP (nuclear autoantigenic sperm protein) is a testis- and
sperm-specific histone-binding protein. O'Rand et al. (1992) cloned NASP
cDNA from a human testis cDNA library. The gene encodes a 787-amino acid
polypeptide with a predicted mass of 85 kD. The protein sequence is 53%
identical to that of the Xenopus ortholog, and 85% identical to that of
the rabbit ortholog when the N terminal of the rabbit sequence is
aligned with amino acid 101 of the human sequence. Two histone-binding
domains are strongly conserved. Northern blot analysis revealed a 3.2 kb
mRNA. Immunolocalization experiments demonstrated that in the testis,
NASP is found primarily in the cytoplasm of primary spermatocytes and
around or within the nuclei of spermatids. NASP is present near the
acrosomal region in mature human sperm.
*FIELD* RF
1. O'Rand, M. G.; Richardson, R. T.; Zimmerman, L. J.; Widgren, E.
E.: Sequence and localization of human NASP: conservation of a Xenopus
histone-binding protein. Dev. Biol. 154: 37-44, 1992.
*FIELD* CD
Jennifer P. Macke: 10/22/1998
*FIELD* ED
alopez: 10/22/1998
*RECORD*
*FIELD* NO
603185
*FIELD* TI
*603185 NUCLEAR AUTOANTIGENIC SPERM PROTEIN; NASP
;;N1/N2, XENOPUS, HOMOLOG OF
*FIELD* TX
read moreDuring mammalian spermatogenesis, testis-specific histones (see H1FT;
142712) and other testis- and sperm-specific proteins are expressed.
NASP (nuclear autoantigenic sperm protein) is a testis- and
sperm-specific histone-binding protein. O'Rand et al. (1992) cloned NASP
cDNA from a human testis cDNA library. The gene encodes a 787-amino acid
polypeptide with a predicted mass of 85 kD. The protein sequence is 53%
identical to that of the Xenopus ortholog, and 85% identical to that of
the rabbit ortholog when the N terminal of the rabbit sequence is
aligned with amino acid 101 of the human sequence. Two histone-binding
domains are strongly conserved. Northern blot analysis revealed a 3.2 kb
mRNA. Immunolocalization experiments demonstrated that in the testis,
NASP is found primarily in the cytoplasm of primary spermatocytes and
around or within the nuclei of spermatids. NASP is present near the
acrosomal region in mature human sperm.
*FIELD* RF
1. O'Rand, M. G.; Richardson, R. T.; Zimmerman, L. J.; Widgren, E.
E.: Sequence and localization of human NASP: conservation of a Xenopus
histone-binding protein. Dev. Biol. 154: 37-44, 1992.
*FIELD* CD
Jennifer P. Macke: 10/22/1998
*FIELD* ED
alopez: 10/22/1998