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Q96H22 (CENPN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence 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 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. Chromosomecentromerekinetochore. 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

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Centromere protein N
PRO_0000249494

Amino acid modifications

Modified residue2261Phosphoserine Ref.6 Ref.11 Ref.12 Ref.14 Ref.15
Modified residue2821Phosphoserine Ref.11 Ref.12 Ref.14 Ref.15

Natural variations

Alternative sequence73 – 9321YMQFH…SKGPG → C in isoform 4.
VSP_044689
Alternative sequence177 – 21034Missing in isoform 5.
VSP_044690
Alternative sequence178 – 20427ALTIA…SLKAI → ELEATGKIYLRQEEIILDIT EMKKACN in isoform 2.
VSP_020441
Alternative sequence205 – 339135Missing in isoform 2.
VSP_020442
Alternative sequence313 – 33927GIADA…KIRDK → ALVCRIQKLLCYSGSHSQGT QDPSSWQKDLYLLFVPLYPR C in isoform 3.
VSP_044565
Natural variant841E → D. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs935939 [ dbSNP | Ensembl ].
VAR_027419
Natural variant2231Q → R.
Corresponds to variant rs11641523 [ dbSNP | Ensembl ].
VAR_048689
Natural variant2881E → K. Ref.2
Corresponds to variant rs2549887 [ dbSNP | Ensembl ].
VAR_048690

Experimental info

Mutagenesis111R → A: Decreases the binding to centromeres. Ref.13
Mutagenesis1961R → A: Decreases the binding to centromeres. Ref.13
Sequence conflict1391T → A in AK026313. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 7A0D3326032DE99B

FASTA33939,555
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 3954E4F78E020360
Show »

FASTA20424,067
Isoform 3 [UniParc].

Checksum: B3366A33C89CD296
Show »

FASTA35341,194
Isoform 4 [UniParc].

Checksum: 52873DA13A654ED2
Show »

FASTA31937,083
Isoform 5 [UniParc].

Checksum: 5D7E6CFAB91045CD
Show »

FASTA30535,556

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
CCDSCCDS10931.1. [Q96H22-2]
CCDS42199.1. [Q96H22-3]
CCDS42200.1. [Q96H22-1]
CCDS58482.1. [Q96H22-5]
CCDS58483.1. [Q96H22-4]
RefSeqNP_001094094.2. NM_001100624.2. [Q96H22-1]
NP_001094095.2. NM_001100625.2. [Q96H22-3]
NP_001257402.1. NM_001270473.1. [Q96H22-4]
NP_001257403.1. NM_001270474.1. [Q96H22-5]
NP_060925.2. NM_018455.5. [Q96H22-2]
XP_006721299.1. XM_006721236.1. [Q96H22-1]
UniGeneHs.726537.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120942. 13 interactions.
IntActQ96H22. 1 interaction.
MINTMINT-4995499.
STRING9606.ENSP00000377007.

PTM databases

PhosphoSiteQ96H22.

Polymorphism databases

DMDM308153423.

Proteomic databases

MaxQBQ96H22.
PaxDbQ96H22.
PRIDEQ96H22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299572; ENSP00000299572; ENSG00000166451. [Q96H22-2]
ENST00000305850; ENSP00000305608; ENSG00000166451. [Q96H22-1]
ENST00000393335; ENSP00000377007; ENSG00000166451. [Q96H22-3]
ENST00000428963; ENSP00000393991; ENSG00000166451. [Q96H22-5]
ENST00000439957; ENSP00000395235; ENSG00000166451. [Q96H22-4]
GeneID55839.
KEGGhsa:55839.
UCSCuc002ffw.4. human. [Q96H22-2]
uc002ffx.2. human. [Q96H22-1]

Organism-specific databases

CTD55839.
GeneCardsGC16P081040.
HGNCHGNC:30873. CENPN.
HPAHPA052870.
MIM611509. gene.
neXtProtNX_Q96H22.
PharmGKBPA143485397.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG17730.
HOGENOMHOG000015409.
HOVERGENHBG058868.
KOK11506.
OMAHEDMEEA.
OrthoDBEOG7P8PB4.
PhylomeDBQ96H22.
TreeFamTF329714.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ96H22.
BgeeQ96H22.
CleanExHS_CENPN.
GenevestigatorQ96H22.

Family and domain databases

InterProIPR027715. CENP-N.
IPR007902. Chl4/mis15/CENP-N.
[Graphical view]
PANTHERPTHR32250. PTHR32250. 1 hit.
PfamPF05238. CENP-N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCENPN.
GenomeRNAi55839.
NextBio35472500.
PROQ96H22.
SOURCESearch...

Entry information

Entry nameCENPN_HUMAN
AccessionPrimary (citable) accession number: Q96H22
Secondary accession number(s): A8MZE6 expand/collapse secondary AC list , 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: July 9, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM