CENPN_HUMAN
ID CENPN_HUMAN Reviewed; 339 AA.
AC Q96H22; A8MZE6; B3KN53; B4DJD1; B4DPY7; C9JJM5; D3DUK8; E7ES30; E7ETS3;
AC Q9NZ83;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Centromere protein N;
DE Short=CENP-N;
DE AltName: Full=Interphase centromere complex protein 32;
GN Name=CENPN; Synonyms=C16orf60, ICEN32; ORFNames=BM-309;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ASP-84.
RC TISSUE=Bone marrow;
RA Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z.;
RT "A novel gene expressed in human bone marrow.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5), AND
RP VARIANTS ASP-84 AND LYS-288.
RC TISSUE=Placenta, Small intestine, and Subthalamic nucleus;
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 GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-84.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ASP-84.
RC TISSUE=Cervix;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP 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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16716197; DOI=10.1111/j.1365-2443.2006.00969.x;
RA Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y.,
RA Goshima N., Nomura F., Nomura N., Yoda K.;
RT "Comprehensive analysis of the ICEN (Interphase Centromere Complex)
RT components enriched in the CENP-A chromatin of human cells.";
RL Genes Cells 11:673-684(2006).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH CENPH; CENPI; CENPK; CENPO; CENPP; CENPQ;
RP CENPR AND CENPU.
RX PubMed=16622420; DOI=10.1038/ncb1396;
RA Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X., Yates J.R. III,
RA Desai A., Fukagawa T.;
RT "The CENP-H-I complex is required for the efficient incorporation of newly
RT synthesized CENP-A into centromeres.";
RL Nat. Cell Biol. 8:446-457(2006).
RN [9]
RP IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPA; CENPC; CENPH; CENPM;
RP CENPT AND CENPU, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16622419; DOI=10.1038/ncb1397;
RA Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III,
RA Cleveland D.W.;
RT "The human CENP-A centromeric nucleosome-associated complex.";
RL Nat. Cell Biol. 8:458-469(2006).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18007590; DOI=10.1038/sj.emboj.7601927;
RA McClelland S.E., Borusu S., Amaro A.C., Winter J.R., Belwal M.,
RA McAinsh A.D., Meraldi P.;
RT "The CENP-A NAC/CAD kinetochore complex controls chromosome congression and
RT spindle bipolarity.";
RL EMBO J. 26:5033-5047(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-282, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-282, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [13]
RP FUNCTION, INTERACTION WITH CENPA, AND MUTAGENESIS OF ARG-11 AND ARG-196.
RX PubMed=19543270; DOI=10.1038/ncb1899;
RA Carroll C.W., Silva M.C.C., Godek K.M., Jansen L.E.T., Straight A.F.;
RT "Centromere assembly requires the direct recognition of CENP-A nucleosomes
RT by CENP-N.";
RL Nat. Cell Biol. 11:896-902(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-282, AND
RP IDENTIFICATION BY MASS 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-282, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-235 AND SER-282, AND
RP 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 [17]
RP SUBUNIT.
RX PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023;
RA Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M., Syed S.H.,
RA Lone I.N., Boopathi R., Fontaine E., Papai G., Tachiwana H., Gautier T.,
RA Skoufias D., Padmanabhan K., Bednar J., Kurumizaka H., Schultz P.,
RA Angelov D., Hamiche A., Dimitrov S.;
RT "The flexible ends of CENP-A nucleosome are required for mitotic
RT fidelity.";
RL Mol. Cell 63:674-685(2016).
CC -!- FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a
CC complex that plays a central role in assembly of kinetochore proteins,
CC mitotic progression and chromosome segregation. The CENPA-NAC complex
CC recruits the CENPA-CAD (nucleosome distal) complex and may be involved
CC in incorporation of newly synthesized CENPA into centromeres. CENPN is
CC the first protein to bind specifically to CENPA nucleosomes and the
CC direct binding of CENPA nucleosomes by CENPN is required for centromere
CC assembly. Required for chromosome congression and efficiently align the
CC chromosomes on a metaphase plate. {ECO:0000269|PubMed:16622419,
CC ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:18007590,
CC ECO:0000269|PubMed:19543270}.
CC -!- SUBUNIT: Component of the CENPA-NAC complex, at least composed of
CC CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU (PubMed:16622420,
CC PubMed:16622419). The CENPA-NAC complex interacts with the CENPA-CAD
CC complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR
CC and CENPS. Interacts directly with CENPA (PubMed:19543270). Identified
CC in a centromere complex containing histones H2A, H2B and H4, and at
CC least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1
CC (PubMed:27499292). {ECO:0000269|PubMed:16622419,
CC ECO:0000269|PubMed:16622420, ECO:0000269|PubMed:19543270,
CC ECO:0000269|PubMed:27499292}.
CC -!- INTERACTION:
CC Q96H22-3; Q9BT30: ALKBH7; NbExp=3; IntAct=EBI-19948078, EBI-2878075;
CC Q96H22-3; Q8IW40: CCDC103; NbExp=3; IntAct=EBI-19948078, EBI-10261970;
CC Q96H22-3; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-19948078, EBI-9057006;
CC Q96H22-3; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-19948078, EBI-3918381;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC Note=Localizes exclusively in the kinetochore domain of centromeres.
CC Kinetochore-bound levels decrease when cells enter mitosis and increase
CC again when cells exit mitosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96H22-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96H22-2; Sequence=VSP_020441, VSP_020442;
CC Name=3;
CC IsoId=Q96H22-3; Sequence=VSP_044565;
CC Name=4;
CC IsoId=Q96H22-4; Sequence=VSP_044689;
CC Name=5;
CC IsoId=Q96H22-5; Sequence=VSP_044690;
CC -!- SIMILARITY: Belongs to the CENP-N/CHL4 family. {ECO:0000305}.
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DR EMBL; AF217515; AAF67626.1; -; mRNA.
DR EMBL; AK023669; BAG51215.1; -; mRNA.
DR EMBL; AK026313; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK298554; BAG60749.1; -; mRNA.
DR EMBL; AK296024; BAG58793.1; -; mRNA.
DR EMBL; AC092718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471114; EAW95553.1; -; Genomic_DNA.
DR EMBL; CH471114; EAW95556.1; -; Genomic_DNA.
DR EMBL; BC007334; AAH07334.1; -; mRNA.
DR EMBL; BC008972; AAH08972.1; -; mRNA.
DR CCDS; CCDS10931.1; -. [Q96H22-2]
DR CCDS; CCDS42199.1; -. [Q96H22-3]
DR CCDS; CCDS42200.1; -. [Q96H22-1]
DR CCDS; CCDS58482.1; -. [Q96H22-5]
DR CCDS; CCDS58483.1; -. [Q96H22-4]
DR RefSeq; NP_001094094.2; NM_001100624.2. [Q96H22-1]
DR RefSeq; NP_001094095.2; NM_001100625.2. [Q96H22-3]
DR RefSeq; NP_001257402.1; NM_001270473.1. [Q96H22-4]
DR RefSeq; NP_001257403.1; NM_001270474.1. [Q96H22-5]
DR RefSeq; NP_060925.2; NM_018455.5. [Q96H22-2]
DR RefSeq; XP_006721299.1; XM_006721236.3. [Q96H22-1]
DR RefSeq; XP_016878945.1; XM_017023456.1. [Q96H22-2]
DR PDB; 6BUZ; EM; 3.92 A; N=1-286.
DR PDB; 6C0W; EM; 4.00 A; K=1-289.
DR PDB; 6EQT; X-ray; 2.73 A; A/B=1-213.
DR PDB; 6MUO; EM; 3.60 A; M=1-212.
DR PDB; 6MUP; EM; 3.50 A; M/N=1-212.
DR PDB; 7U46; EM; 2.68 A; K=1-289.
DR PDB; 7U47; EM; 7.50 A; K/V=1-289.
DR PDB; 7U4D; EM; 8.10 A; K/V=1-289.
DR PDBsum; 6BUZ; -.
DR PDBsum; 6C0W; -.
DR PDBsum; 6EQT; -.
DR PDBsum; 6MUO; -.
DR PDBsum; 6MUP; -.
DR PDBsum; 7U46; -.
DR PDBsum; 7U47; -.
DR PDBsum; 7U4D; -.
DR AlphaFoldDB; Q96H22; -.
DR SMR; Q96H22; -.
DR BioGRID; 120942; 58.
DR ComplexPortal; CPX-5646; Kinetochore CCAN complex.
DR CORUM; Q96H22; -.
DR IntAct; Q96H22; 25.
DR MINT; Q96H22; -.
DR STRING; 9606.ENSP00000377007; -.
DR iPTMnet; Q96H22; -.
DR PhosphoSitePlus; Q96H22; -.
DR BioMuta; CENPN; -.
DR DMDM; 308153423; -.
DR EPD; Q96H22; -.
DR jPOST; Q96H22; -.
DR MassIVE; Q96H22; -.
DR MaxQB; Q96H22; -.
DR PaxDb; Q96H22; -.
DR PeptideAtlas; Q96H22; -.
DR PRIDE; Q96H22; -.
DR ProteomicsDB; 17903; -.
DR ProteomicsDB; 18278; -.
DR ProteomicsDB; 2470; -.
DR ProteomicsDB; 76697; -. [Q96H22-1]
DR ProteomicsDB; 76698; -. [Q96H22-2]
DR Antibodypedia; 30430; 112 antibodies from 26 providers.
DR DNASU; 55839; -.
DR Ensembl; ENST00000299572.9; ENSP00000299572.5; ENSG00000166451.14. [Q96H22-2]
DR Ensembl; ENST00000305850.10; ENSP00000305608.5; ENSG00000166451.14. [Q96H22-1]
DR Ensembl; ENST00000393335.7; ENSP00000377007.3; ENSG00000166451.14. [Q96H22-3]
DR Ensembl; ENST00000428963.6; ENSP00000393991.2; ENSG00000166451.14. [Q96H22-5]
DR Ensembl; ENST00000439957.7; ENSP00000395235.3; ENSG00000166451.14. [Q96H22-4]
DR GeneID; 55839; -.
DR KEGG; hsa:55839; -.
DR MANE-Select; ENST00000305850.10; ENSP00000305608.5; NM_001100624.3; NP_001094094.2.
DR UCSC; uc002ffw.5; human. [Q96H22-1]
DR CTD; 55839; -.
DR DisGeNET; 55839; -.
DR GeneCards; CENPN; -.
DR HGNC; HGNC:30873; CENPN.
DR HPA; ENSG00000166451; Tissue enhanced (bone).
DR MIM; 611509; gene.
DR neXtProt; NX_Q96H22; -.
DR OpenTargets; ENSG00000166451; -.
DR PharmGKB; PA143485397; -.
DR VEuPathDB; HostDB:ENSG00000166451; -.
DR eggNOG; ENOG502QSE8; Eukaryota.
DR GeneTree; ENSGT00390000004738; -.
DR HOGENOM; CLU_1521215_0_0_1; -.
DR InParanoid; Q96H22; -.
DR OMA; YFVITDN; -.
DR OrthoDB; 1145159at2759; -.
DR PhylomeDB; Q96H22; -.
DR TreeFam; TF329714; -.
DR PathwayCommons; Q96H22; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q96H22; -.
DR SIGNOR; Q96H22; -.
DR BioGRID-ORCS; 55839; 762 hits in 1085 CRISPR screens.
DR ChiTaRS; CENPN; human.
DR GeneWiki; CENPN; -.
DR GenomeRNAi; 55839; -.
DR Pharos; Q96H22; Tbio.
DR PRO; PR:Q96H22; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96H22; protein.
DR Bgee; ENSG00000166451; Expressed in ventricular zone and 134 other tissues.
DR ExpressionAtlas; Q96H22; baseline and differential.
DR Genevisible; Q96H22; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0007059; P:chromosome segregation; IEA:InterPro.
DR GO; GO:0051382; P:kinetochore assembly; IEA:InterPro.
DR InterPro; IPR007902; Chl4/mis15/CENP-N.
DR Pfam; PF05238; CENP-N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Centromere; Chromosome; Kinetochore;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..339
FT /note="Centromere protein N"
FT /id="PRO_0000249494"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 73..93
FT /note="YMQFHQHQKVWEVFQMSKGPG -> C (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044689"
FT VAR_SEQ 177..210
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044690"
FT VAR_SEQ 178..204
FT /note="ALTIASKHHQIVKMDLRSRYLDSLKAI -> ELEATGKIYLRQEEIILDITE
FT MKKACN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_020441"
FT VAR_SEQ 205..339
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_020442"
FT VAR_SEQ 313..339
FT /note="GIADAPLSPLLTCIPNKRMNYFKIRDK -> ALVCRIQKLLCYSGSHSQGTQ
FT DPSSWQKDLYLLFVPLYPRC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044565"
FT VARIANT 84
FT /note="E -> D (in dbSNP:rs935939)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.4"
FT /id="VAR_027419"
FT VARIANT 223
FT /note="Q -> R (in dbSNP:rs11641523)"
FT /id="VAR_048689"
FT VARIANT 288
FT /note="E -> K (in dbSNP:rs2549887)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_048690"
FT MUTAGEN 11
FT /note="R->A: Decreases the binding to centromeres."
FT /evidence="ECO:0000269|PubMed:19543270"
FT MUTAGEN 196
FT /note="R->A: Decreases the binding to centromeres."
FT /evidence="ECO:0000269|PubMed:19543270"
FT CONFLICT 139
FT /note="T -> A (in Ref. 2; AK026313)"
FT /evidence="ECO:0000305"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:6EQT"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:6EQT"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:6EQT"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6MUP"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:6EQT"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:6EQT"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6EQT"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:6EQT"
FT HELIX 101..115
FT /evidence="ECO:0007829|PDB:6EQT"
FT STRAND 116..126
FT /evidence="ECO:0007829|PDB:6EQT"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:6EQT"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:6EQT"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6EQT"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:6EQT"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:6EQT"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:6EQT"
FT STRAND 186..196
FT /evidence="ECO:0007829|PDB:6EQT"
FT HELIX 198..212
FT /evidence="ECO:0007829|PDB:6EQT"
SQ SEQUENCE 339 AA; 39555 MW; 7A0D3326032DE99B CRC64;
MDETVAEFIK RTILKIPMNE LTTILKAWDF LSENQLQTVN FRQRKESVVQ HLIHLCEEKR
ASISDAALLD IIYMQFHQHQ KVWEVFQMSK GPGEDVDLFD MKQFKNSFKK ILQRALKNVT
VSFRETEENA VWIRIAWGTQ YTKPNQYKPT YVVYYSQTPY AFTSSSMLRR NTPLLGQALT
IASKHHQIVK MDLRSRYLDS LKAIVFKQYN QTFETHNSTT PLQERSLGLD INMDSRIIHE
NIVEKERVQR ITQETFGDYP QPQLEFAQYK LETKFKSGLN GSILAEREEP LRCLIKFSSP
HLLEALKSLA PAGIADAPLS PLLTCIPNKR MNYFKIRDK
