CENPN_MOUSE
ID CENPN_MOUSE Reviewed; 337 AA.
AC Q9CZW2; Q6PE73; Q8R2W7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Centromere protein N;
DE Short=CENP-N;
GN Name=Cenpn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 7-337 (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Olfactory epithelium;
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).
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:0000250|UniProtKB:Q96H22}.
CC -!- SUBUNIT: Component of the CENPA-NAC complex, at least composed of
CC CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC
CC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK,
CC CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Interacts directly with
CC CENPA. Identified in a centromere complex containing histones H2A, H2B
CC and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H,
CC SSRP1 and RSF1. {ECO:0000250|UniProtKB:Q96H22}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}.
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. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9CZW2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CZW2-2; Sequence=VSP_020443;
CC Name=3;
CC IsoId=Q9CZW2-3; Sequence=VSP_020444, VSP_020445;
CC -!- SIMILARITY: Belongs to the CENP-N/CHL4 family. {ECO:0000305}.
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DR EMBL; AK012097; BAB28028.1; -; mRNA.
DR EMBL; BC027119; AAH27119.1; -; mRNA.
DR EMBL; BC058243; AAH58243.1; -; mRNA.
DR CCDS; CCDS22693.1; -. [Q9CZW2-1]
DR RefSeq; NP_082407.1; NM_028131.3. [Q9CZW2-1]
DR RefSeq; XP_006531450.1; XM_006531387.3. [Q9CZW2-1]
DR AlphaFoldDB; Q9CZW2; -.
DR SMR; Q9CZW2; -.
DR ComplexPortal; CPX-5704; Kinetochore CCAN complex.
DR IntAct; Q9CZW2; 1.
DR MINT; Q9CZW2; -.
DR STRING; 10090.ENSMUSP00000034205; -.
DR iPTMnet; Q9CZW2; -.
DR PhosphoSitePlus; Q9CZW2; -.
DR EPD; Q9CZW2; -.
DR MaxQB; Q9CZW2; -.
DR PaxDb; Q9CZW2; -.
DR PRIDE; Q9CZW2; -.
DR ProteomicsDB; 280065; -. [Q9CZW2-1]
DR ProteomicsDB; 280066; -. [Q9CZW2-2]
DR ProteomicsDB; 280067; -. [Q9CZW2-3]
DR Antibodypedia; 30430; 112 antibodies from 26 providers.
DR DNASU; 72155; -.
DR Ensembl; ENSMUST00000034205; ENSMUSP00000034205; ENSMUSG00000031756. [Q9CZW2-1]
DR Ensembl; ENSMUST00000212263; ENSMUSP00000148413; ENSMUSG00000031756. [Q9CZW2-2]
DR GeneID; 72155; -.
DR KEGG; mmu:72155; -.
DR UCSC; uc009noo.1; mouse. [Q9CZW2-1]
DR CTD; 55839; -.
DR MGI; MGI:1919405; Cenpn.
DR VEuPathDB; HostDB:ENSMUSG00000031756; -.
DR eggNOG; ENOG502QSE8; Eukaryota.
DR GeneTree; ENSGT00390000004738; -.
DR HOGENOM; CLU_070600_0_0_1; -.
DR InParanoid; Q9CZW2; -.
DR OMA; YFVITDN; -.
DR OrthoDB; 1145159at2759; -.
DR PhylomeDB; Q9CZW2; -.
DR TreeFam; TF329714; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 72155; 27 hits in 75 CRISPR screens.
DR ChiTaRS; Cenpn; mouse.
DR PRO; PR:Q9CZW2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9CZW2; protein.
DR Bgee; ENSMUSG00000031756; Expressed in animal zygote and 157 other tissues.
DR ExpressionAtlas; Q9CZW2; baseline and differential.
DR Genevisible; Q9CZW2; MM.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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 2: Evidence at transcript level;
KW Alternative splicing; Centromere; Chromosome; Kinetochore; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..337
FT /note="Centromere protein N"
FT /id="PRO_0000249495"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96H22"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96H22"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020443"
FT VAR_SEQ 231..250
FT /note="LDSKITHENTEEKVRVHRVT -> CMYALSQSWAWGSCAAKHLC (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020444"
FT VAR_SEQ 251..337
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020445"
SQ SEQUENCE 337 AA; 39240 MW; D3EF2CE4DAC900E8 CRC64;
MKENVAEFLR RTILKIPLSE MKSILEAWDF LSEDQLQTIN LKQRKDYLAQ EVILLCEDKR
ASLDDVVLLD IVYTQFHRHQ KLWNVFQMSK EPGEDVDLFD MEQFQSSFKR ILQRALKNVT
VSFRVYEKDS VWIRVAWGTQ YSQPNQYKPT FVVYYPQTPY AFISSCHLKN TVPLLHQALK
VASKHHQIVH LDLRSRHLDS LKAIVFREYN QTCENYSSTT SLQEASLSMC LDSKITHENT
EEKVRVHRVT QETFGTYPQP QLEFAQYKLE TKFKSNIGGG LLADRKEPFR CLVKFSSPHL
LEALKSLAPA GIADAPLSPL LTCIPSKKMN YFKIRDK