NASP_HUMAN
ID NASP_HUMAN Reviewed; 788 AA.
AC P49321; A8K6H2; B4DQP3; D3DQ07; F5H3J2; Q53GW5; Q5T622; Q5T625; Q96A69;
AC Q9BTW2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Nuclear autoantigenic sperm protein;
DE Short=NASP;
GN Name=NASP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 NUCLEOTIDE
RP 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP HISTONE-BINDING REGIONS, SUBUNIT, AND INTERACTION WITH HISTONES H2A; H2B;
RP H3 AND H4.
RX PubMed=8724350; DOI=10.1095/biolreprod54.6.1238;
RA Batova I., O'Rand M.G.;
RT "Histone-binding domains in a human nuclear autoantigenic sperm protein.";
RL Biol. Reprod. 54:1238-1244(1996).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-451; SER-503 AND
RP SER-726, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT 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 phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-464, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
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, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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-321; THR-390; SER-408; SER-421; SER-451; THR-464; THR-477;
RP SER-480; THR-490; SER-497; SER-503; SER-726 AND SER-751, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT THR-138 AND SER-141 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170; SER-176; SER-189;
RP SER-191; SER-244; SER-299; THR-390; SER-397; SER-421; THR-464; THR-477;
RP SER-480; THR-490; SER-497; SER-662; SER-705; SER-706; SER-745; SER-751 AND
RP SER-756, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-736, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [22]
RP SUBUNIT, AND INTERACTION WITH HISTONES H2A; H2B; H3 AND H4.
RX PubMed=27618665; DOI=10.1016/j.str.2016.08.001;
RA Zhang M., Liu H., Gao Y., Zhu Z., Chen Z., Zheng P., Xue L., Li J.,
RA Teng M., Niu L.;
RT "Structural Insights into the Association of Hif1 with Histones H2A-H2B
RT Dimer and H3-H4 Tetramer.";
RL Structure 24:1810-1820(2016).
RN [23]
RP INTERACTION WITH HISTONE H3.3.
RX PubMed=33857403; DOI=10.1016/j.molcel.2021.03.041;
RA Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y.,
RA Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L.,
RA Patel D.J., Huang H., Groth A.;
RT "DNAJC9 integrates heat shock molecular chaperones into the histone
RT chaperone network.";
RL Mol. Cell 0:0-0(2021).
CC -!- FUNCTION: Required for DNA replication, normal cell cycle progression
CC and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1
CC linker histones and stimulates HSP90 ATPase activity. NASP and H1
CC histone are subsequently released from the complex and translocate to
CC the nucleus where the histone is released for binding to DNA.
CC {ECO:0000250|UniProtKB:Q99MD9}.
CC -!- SUBUNIT: Binds to linker H1 histones but not to core histones (By
CC similarity). Interacts with histones H2A, H2B, H3 and H4
CC (PubMed:8724350, PubMed:27618665). Interacts with histone H3.3
CC (PubMed:33857403). Also binds to HSP90 in the cytoplasm. This
CC interaction stimulates binding of NASP to H1-6/H1T (By similarity).
CC {ECO:0000250|UniProtKB:Q99MD9, ECO:0000269|PubMed:27618665,
CC ECO:0000269|PubMed:33857403, ECO:0000269|PubMed:8724350}.
CC -!- INTERACTION:
CC P49321; P68431: H3C12; NbExp=9; IntAct=EBI-716205, EBI-79722;
CC P49321; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-716205, EBI-750109;
CC P49321-2; Q9Y294: ASF1A; NbExp=3; IntAct=EBI-7038920, EBI-749553;
CC P49321-2; P84243: H3-3B; NbExp=3; IntAct=EBI-7038920, EBI-120658;
CC P49321-2; Q16695: H3-4; NbExp=6; IntAct=EBI-7038920, EBI-358900;
CC P49321-2; Q6NXT2: H3-5; NbExp=11; IntAct=EBI-7038920, EBI-2868501;
CC P49321-2; P68431: H3C12; NbExp=7; IntAct=EBI-7038920, EBI-79722;
CC P49321-2; Q71DI3: H3C15; NbExp=4; IntAct=EBI-7038920, EBI-750650;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99MD9}. Nucleus
CC {ECO:0000250|UniProtKB:Q99MD9}.
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 Name=3;
CC IsoId=P49321-3; Sequence=VSP_036616;
CC Name=4;
CC IsoId=P49321-4; Sequence=VSP_047028;
CC -!- TISSUE SPECIFICITY: Isoform 1 is testis- and sperm-specific.
CC -!- SIMILARITY: Belongs to the NASP family. {ECO:0000305}.
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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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS524.1; -. [P49321-1]
DR CCDS; CCDS525.1; -. [P49321-2]
DR CCDS; CCDS55597.1; -. [P49321-4]
DR PIR; A48819; A48819.
DR RefSeq; NP_001182122.1; NM_001195193.1. [P49321-4]
DR RefSeq; NP_002473.2; NM_002482.3. [P49321-1]
DR RefSeq; NP_689511.2; NM_152298.3. [P49321-2]
DR RefSeq; XP_005270945.1; XM_005270888.2. [P49321-3]
DR PDB; 7V6P; X-ray; 2.90 A; A=454-659.
DR PDB; 7V6Q; X-ray; 3.00 A; D/H=454-659.
DR PDBsum; 7V6P; -.
DR PDBsum; 7V6Q; -.
DR AlphaFoldDB; P49321; -.
DR SMR; P49321; -.
DR BioGRID; 110759; 114.
DR CORUM; P49321; -.
DR DIP; DIP-47269N; -.
DR IntAct; P49321; 45.
DR MINT; P49321; -.
DR STRING; 9606.ENSP00000255120; -.
DR GlyGen; P49321; 9 sites, 2 O-linked glycans (9 sites).
DR iPTMnet; P49321; -.
DR MetOSite; P49321; -.
DR PhosphoSitePlus; P49321; -.
DR SwissPalm; P49321; -.
DR BioMuta; NASP; -.
DR DMDM; 23503077; -.
DR CPTAC; CPTAC-411; -.
DR CPTAC; CPTAC-412; -.
DR EPD; P49321; -.
DR jPOST; P49321; -.
DR MassIVE; P49321; -.
DR MaxQB; P49321; -.
DR PaxDb; P49321; -.
DR PeptideAtlas; P49321; -.
DR PRIDE; P49321; -.
DR ProteomicsDB; 26289; -.
DR ProteomicsDB; 55984; -. [P49321-1]
DR ProteomicsDB; 55985; -. [P49321-2]
DR ProteomicsDB; 55986; -. [P49321-3]
DR Antibodypedia; 32662; 196 antibodies from 29 providers.
DR DNASU; 4678; -.
DR Ensembl; ENST00000350030.8; ENSP00000255120.5; ENSG00000132780.17. [P49321-1]
DR Ensembl; ENST00000351223.7; ENSP00000255121.4; ENSG00000132780.17. [P49321-2]
DR Ensembl; ENST00000537798.5; ENSP00000438871.1; ENSG00000132780.17. [P49321-4]
DR GeneID; 4678; -.
DR KEGG; hsa:4678; -.
DR MANE-Select; ENST00000350030.8; ENSP00000255120.5; NM_002482.4; NP_002473.2.
DR UCSC; uc001coi.3; human. [P49321-1]
DR CTD; 4678; -.
DR DisGeNET; 4678; -.
DR GeneCards; NASP; -.
DR HGNC; HGNC:7644; NASP.
DR HPA; ENSG00000132780; Low tissue specificity.
DR MIM; 603185; gene.
DR neXtProt; NX_P49321; -.
DR OpenTargets; ENSG00000132780; -.
DR PharmGKB; PA31448; -.
DR VEuPathDB; HostDB:ENSG00000132780; -.
DR eggNOG; KOG4563; Eukaryota.
DR GeneTree; ENSGT00390000016650; -.
DR HOGENOM; CLU_010162_0_0_1; -.
DR InParanoid; P49321; -.
DR OMA; SSAFPCE; -.
DR OrthoDB; 1176629at2759; -.
DR PhylomeDB; P49321; -.
DR TreeFam; TF317297; -.
DR PathwayCommons; P49321; -.
DR SignaLink; P49321; -.
DR BioGRID-ORCS; 4678; 301 hits in 1089 CRISPR screens.
DR ChiTaRS; NASP; human.
DR GeneWiki; NASP_(gene); -.
DR GenomeRNAi; 4678; -.
DR Pharos; P49321; Tbio.
DR PRO; PR:P49321; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P49321; protein.
DR Bgee; ENSG00000132780; Expressed in ventricular zone and 210 other tissues.
DR ExpressionAtlas; P49321; baseline and differential.
DR Genevisible; P49321; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0001824; P:blastocyst development; ISS:UniProtKB.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0043486; P:histone exchange; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR019544; Tetratricopeptide_SHNi-TPR_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF10516; SHNi-TPR; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Coiled coil;
KW Cytoplasm; DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; TPR repeat; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..788
FT /note="Nuclear autoantigenic sperm protein"
FT /id="PRO_0000106299"
FT REPEAT 43..76
FT /note="TPR 1"
FT REPEAT 542..575
FT /note="TPR 2"
FT REPEAT 584..617
FT /note="TPR 3"
FT REGION 114..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..127
FT /note="Histone-binding"
FT /evidence="ECO:0000269|PubMed:8724350"
FT REGION 151..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..244
FT /note="Histone-binding"
FT /evidence="ECO:0000269|PubMed:8724350"
FT REGION 469..512
FT /note="Histone-binding"
FT /evidence="ECO:0000269|PubMed:8724350"
FT REGION 678..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 136..164
FT /evidence="ECO:0000255"
FT COILED 460..487
FT /evidence="ECO:0000255"
FT COILED 597..665
FT /evidence="ECO:0000255"
FT COILED 753..778
FT /evidence="ECO:0000255"
FT MOTIF 716..722
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 151..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 123
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MD9"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MD9"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 390
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 464
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 477
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 490
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 683
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 736
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 1..36
FT /note="MAMESTATAAVAAELVSADKIEDVPAPSTSADKVES -> MFLLLLHLQIKW
FT RATINLLSVTEDGLHFVEYYLNRIIH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036616"
FT VAR_SEQ 36..99
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047028"
FT VAR_SEQ 138..476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006551"
FT VARIANT 620
FT /note="V -> G (in dbSNP:rs34618000)"
FT /id="VAR_052619"
FT CONFLICT 14..15
FT /note="EL -> DV (in Ref. 1; AAA36027)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="K -> T (in Ref. 3; BAD96536)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="R -> G (in Ref. 2; BAG61005)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="T -> Q (in Ref. 1; AAA36027)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="Missing (in Ref. 1; AAA36027)"
FT /evidence="ECO:0000305"
FT CONFLICT 767..770
FT /note="AESR -> LKRG (in Ref. 1; AAA36027)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="V -> L (in Ref. 1; AAA36027)"
FT /evidence="ECO:0000305"
FT HELIX 508..531
FT /evidence="ECO:0007829|PDB:7V6P"
FT HELIX 535..554
FT /evidence="ECO:0007829|PDB:7V6P"
FT HELIX 558..575
FT /evidence="ECO:0007829|PDB:7V6P"
FT HELIX 581..596
FT /evidence="ECO:0007829|PDB:7V6P"
FT HELIX 600..658
FT /evidence="ECO:0007829|PDB:7V6P"
FT MOD_RES P49321-2:138
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES P49321-2:141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
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
