Q96H22 (CENPN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Centromere protein N
Short name=CENP-N

Alternative name(s):
Interphase centromere complex protein 32

Gene names

Name:	CENPN
Synonyms:	C16orf60, ICEN32
ORF Names:	BM-309

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPN is the first protein to bind specifically to CENPA nucleosomes and the direct binding of CENPA nucleosomes by CENPN is required for centromere assembly. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate. Ref.7 Ref.9 Ref.10 Ref.13
Subunit structure	Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Interacts directly with CENPA. Ref.8 Ref.9 Ref.13
Subcellular location	Nucleus. Chromosome › centromere › kinetochore. Note: Localizes exclusively in the kinetochore domain of centromeres. Kinetochore-bound levels decrease when cells enter mitosis and increase again when cells exit mitosis. Ref.7 Ref.9 Ref.10

Ontologies

Keywords
Cellular component	Centromere Chromosome Kinetochore Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CENP-A containing nucleosome assembly at centromere Traceable author statement. Source: Reactome mitotic prometaphase Traceable author statement. Source: Reactome
Cellular_component	condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96H22-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q96H22-2)

The sequence of this isoform differs from the canonical sequence as follows:
     178-204: ALTIASKHHQIVKMDLRSRYLDSLKAI → ELEATGKIYLRQEEIILDITEMKKACN
     205-339: Missing.

Isoform 3 (identifier: Q96H22-3)

The sequence of this isoform differs from the canonical sequence as follows:
     313-339: GIADAPLSPLLTCIPNKRMNYFKIRDK → ALVCRIQKLLCYSGSHSQGTQDPSSWQKDLYLLFVPLYPRC

Note: No experimental confirmation available.

Isoform 4 (identifier: Q96H22-4)

The sequence of this isoform differs from the canonical sequence as follows:
     73-93: YMQFHQHQKVWEVFQMSKGPG → C

Note: No experimental confirmation available.

Isoform 5 (identifier: Q96H22-5)

The sequence of this isoform differs from the canonical sequence as follows:
     177-210: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 339	339	Centromere protein N		PRO_0000249494
Amino acid modifications
	Modified residue	226	1	Phosphoserine Ref.6 Ref.11 Ref.12 Ref.14 Ref.15
	Modified residue	282	1	Phosphoserine Ref.11 Ref.12 Ref.14 Ref.15
Natural variations
	Alternative sequence	73 – 93	21	YMQFH…SKGPG → C in isoform 4.		VSP_044689
	Alternative sequence	177 – 210	34	Missing in isoform 5.		VSP_044690
	Alternative sequence	178 – 204	27	ALTIA…SLKAI → ELEATGKIYLRQEEIILDIT EMKKACN in isoform 2.		VSP_020441
	Alternative sequence	205 – 339	135	Missing in isoform 2.		VSP_020442
	Alternative sequence	313 – 339	27	GIADA…KIRDK → ALVCRIQKLLCYSGSHSQGT QDPSSWQKDLYLLFVPLYPR C in isoform 3.		VSP_044565
	Natural variant	84	1	E → D. Ref.1 Ref.2 Ref.4 Ref.5 Corresponds to variant rs935939 [ dbSNP | Ensembl ].		VAR_027419
	Natural variant	223	1	Q → R. Corresponds to variant rs11641523 [ dbSNP | Ensembl ].		VAR_048689
	Natural variant	288	1	E → K. Ref.2 Corresponds to variant rs2549887 [ dbSNP | Ensembl ].		VAR_048690
Experimental info
	Mutagenesis	11	1	R → A: Decreases the binding to centromeres. Ref.13
	Mutagenesis	196	1	R → A: Decreases the binding to centromeres. Ref.13
	Sequence conflict	139	1	T → A in AK026313. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 5, 2010. Version 2. Checksum: 7A0D3326032DE99B	FASTA	339	39,555
	10 20 30 40 50 60 MDETVAEFIK RTILKIPMNE LTTILKAWDF LSENQLQTVN FRQRKESVVQ HLIHLCEEKR 70 80 90 100 110 120 ASISDAALLD IIYMQFHQHQ KVWEVFQMSK GPGEDVDLFD MKQFKNSFKK ILQRALKNVT 130 140 150 160 170 180 VSFRETEENA VWIRIAWGTQ YTKPNQYKPT YVVYYSQTPY AFTSSSMLRR NTPLLGQALT 190 200 210 220 230 240 IASKHHQIVK MDLRSRYLDS LKAIVFKQYN QTFETHNSTT PLQERSLGLD INMDSRIIHE 250 260 270 280 290 300 NIVEKERVQR ITQETFGDYP QPQLEFAQYK LETKFKSGLN GSILAEREEP LRCLIKFSSP 310 320 330 HLLEALKSLA PAGIADAPLS PLLTCIPNKR MNYFKIRDK
	Isoform 2 [UniParc]. Checksum: 3954E4F78E020360	FASTA	204	24,067
	10 20 30 40 50 60 MDETVAEFIK RTILKIPMNE LTTILKAWDF LSENQLQTVN FRQRKESVVQ HLIHLCEEKR 70 80 90 100 110 120 ASISDAALLD IIYMQFHQHQ KVWEVFQMSK GPGEDVDLFD MKQFKNSFKK ILQRALKNVT 130 140 150 160 170 180 VSFRETEENA VWIRIAWGTQ YTKPNQYKPT YVVYYSQTPY AFTSSSMLRR NTPLLGQELE 190 200 ATGKIYLRQE EIILDITEMK KACN
	Isoform 3 [UniParc]. Checksum: B3366A33C89CD296	FASTA	353	41,194
	10 20 30 40 50 60 MDETVAEFIK RTILKIPMNE LTTILKAWDF LSENQLQTVN FRQRKESVVQ HLIHLCEEKR 70 80 90 100 110 120 ASISDAALLD IIYMQFHQHQ KVWEVFQMSK GPGEDVDLFD MKQFKNSFKK ILQRALKNVT 130 140 150 160 170 180 VSFRETEENA VWIRIAWGTQ YTKPNQYKPT YVVYYSQTPY AFTSSSMLRR NTPLLGQALT 190 200 210 220 230 240 IASKHHQIVK MDLRSRYLDS LKAIVFKQYN QTFETHNSTT PLQERSLGLD INMDSRIIHE 250 260 270 280 290 300 NIVEKERVQR ITQETFGDYP QPQLEFAQYK LETKFKSGLN GSILAEREEP LRCLIKFSSP 310 320 330 340 350 HLLEALKSLA PAALVCRIQK LLCYSGSHSQ GTQDPSSWQK DLYLLFVPLY PRC
	Isoform 4 [UniParc]. Checksum: 52873DA13A654ED2	FASTA	319	37,083
	10 20 30 40 50 60 MDETVAEFIK RTILKIPMNE LTTILKAWDF LSENQLQTVN FRQRKESVVQ HLIHLCEEKR 70 80 90 100 110 120 ASISDAALLD IICEDVDLFD MKQFKNSFKK ILQRALKNVT VSFRETEENA VWIRIAWGTQ 130 140 150 160 170 180 YTKPNQYKPT YVVYYSQTPY AFTSSSMLRR NTPLLGQALT IASKHHQIVK MDLRSRYLDS 190 200 210 220 230 240 LKAIVFKQYN QTFETHNSTT PLQERSLGLD INMDSRIIHE NIVEKERVQR ITQETFGDYP 250 260 270 280 290 300 QPQLEFAQYK LETKFKSGLN GSILAEREEP LRCLIKFSSP HLLEALKSLA PAGIADAPLS 310 PLLTCIPNKR MNYFKIRDK
	Isoform 5 [UniParc]. Checksum: 5D7E6CFAB91045CD	FASTA	305	35,556
	10 20 30 40 50 60 MDETVAEFIK RTILKIPMNE LTTILKAWDF LSENQLQTVN FRQRKESVVQ HLIHLCEEKR 70 80 90 100 110 120 ASISDAALLD IIYMQFHQHQ KVWEVFQMSK GPGEDVDLFD MKQFKNSFKK ILQRALKNVT 130 140 150 160 170 180 VSFRETEENA VWIRIAWGTQ YTKPNQYKPT YVVYYSQTPY AFTSSSMLRR NTPLLGQTFE 190 200 210 220 230 240 THNSTTPLQE RSLGLDINMD SRIIHENIVE KERVQRITQE TFGDYPQPQL EFAQYKLETK 250 260 270 280 290 300 FKSGLNGSIL AEREEPLRCL IKFSSPHLLE ALKSLAPAGI ADAPLSPLLT CIPNKRMNYF KIRDK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel gene expressed in human bone marrow." Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ASP-84. Tissue: Bone marrow.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5), VARIANTS ASP-84 AND LYS-288. Tissue: Placenta, Small intestine and Subthalamic nucleus.
[3]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-84.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ASP-84. Tissue: Cervix.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Comprehensive analysis of the ICEN (Interphase Centromere Complex) components enriched in the CENP-A chromatin of human cells." Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y., Goshima N., Nomura F., Nomura N., Yoda K. Genes Cells 11:673-684(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"The CENP-H-I complex is required for the efficient incorporation of newly synthesized CENP-A into centromeres." Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X., Yates J.R. III, Desai A., Fukagawa T. Nat. Cell Biol. 8:446-457(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH CENPH; CENPI; CENPK; CENPO; CENPP; CENPQ; CENPR AND CENPU.
[9]	"The human CENP-A centromeric nucleosome-associated complex." Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III, Cleveland D.W. Nat. Cell Biol. 8:458-469(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPA; CENPC; CENPH; CENPM; CENPT AND CENPU, SUBCELLULAR LOCATION, FUNCTION.
[10]	"The CENP-A NAC/CAD kinetochore complex controls chromosome congression and spindle bipolarity." McClelland S.E., Borusu S., Amaro A.C., Winter J.R., Belwal M., McAinsh A.D., Meraldi P. EMBO J. 26:5033-5047(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-282, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-282, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Centromere assembly requires the direct recognition of CENP-A nucleosomes by CENP-N." Carroll C.W., Silva M.C.C., Godek K.M., Jansen L.E.T., Straight A.F. Nat. Cell Biol. 11:896-902(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CENPA, MUTAGENESIS OF ARG-11 AND ARG-196.
[14]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-282, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-282, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF217515 mRNA. Translation: AAF67626.1. AK023669 mRNA. Translation: BAG51215.1. AK026313 mRNA. No translation available. AK298554 mRNA. Translation: BAG60749.1. AK296024 mRNA. Translation: BAG58793.1. AC092718 Genomic DNA. No translation available. CH471114 Genomic DNA. Translation: EAW95553.1. CH471114 Genomic DNA. Translation: EAW95556.1. BC007334 mRNA. Translation: AAH07334.1. BC008972 mRNA. Translation: AAH08972.1.
IPI	IPI00020485. IPI00305656. IPI00645096. IPI00908795. IPI00909615.
RefSeq	NP_001094094.2. NM_001100624.2. NP_001094095.2. NM_001100625.2. NP_001257402.1. NM_001270473.1. NP_001257403.1. NM_001270474.1. NP_060925.2. NM_018455.5.
UniGene	Hs.726537.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96H22. 1 interaction.
STRING	9606.ENSP00000377007.
PTM databases
PhosphoSite	Q96H22.
Polymorphism databases
DMDM	308153423.
Proteomic databases
PaxDb	Q96H22.
PRIDE	Q96H22.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000299572; ENSP00000299572; ENSG00000166451. ENST00000305850; ENSP00000305608; ENSG00000166451. ENST00000393335; ENSP00000377007; ENSG00000166451. ENST00000428963; ENSP00000393991; ENSG00000166451. ENST00000439957; ENSP00000395235; ENSG00000166451.
GeneID	55839.
KEGG	hsa:55839.
UCSC	uc002ffx.2. human.
Organism-specific databases
CTD	55839.
GeneCards	GC16P081040.
HGNC	HGNC:30873. CENPN.
MIM	611509. gene.
neXtProt	NX_Q96H22.
PharmGKB	PA143485397.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG17730.
HOGENOM	HOG000015409.
HOVERGEN	HBG058868.
KO	K11506.
OMA	MTILKAW.
OrthoDB	EOG4QZ7M6.
PhylomeDB	Q96H22.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	Q96H22.
Bgee	Q96H22.
CleanEx	HS_CENPN.
Genevestigator	Q96H22.
GermOnline	ENSG00000166451. Homo sapiens.
Family and domain databases
InterPro	IPR007902. CHL4. [Graphical view]
Pfam	PF05238. CENP-N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	55839.
NextBio	35472500.
SOURCE	Search...

Entry information

Entry name

CENPN_HUMAN

Accession

Primary (citable) accession number: Q96H22
Secondary accession number(s): A8MZE6 , B3KN53, B4DJD1, B4DPY7, C9JJM5, D3DUK8, E7ES30, E7ETS3, Q9NZ83

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2006
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.