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Protein

Centromere protein N

Gene

CENPN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Centromere protein N
Short name:
CENP-N
Alternative name(s):
Interphase centromere complex protein 32
Gene namesi
Name:CENPN
Synonyms:C16orf60, ICEN32
ORF Names:BM-309
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:30873. CENPN.

Subcellular locationi

  • 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.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111R → A: Decreases the binding to centromeres. 1 Publication
Mutagenesisi196 – 1961R → A: Decreases the binding to centromeres. 1 Publication

Organism-specific databases

PharmGKBiPA143485397.

Polymorphism and mutation databases

BioMutaiCENPN.
DMDMi308153423.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 339339Centromere protein NPRO_0000249494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei226 – 2261Phosphoserine5 Publications
Modified residuei282 – 2821Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96H22.
PaxDbiQ96H22.
PRIDEiQ96H22.

PTM databases

PhosphoSiteiQ96H22.

Expressioni

Gene expression databases

BgeeiQ96H22.
CleanExiHS_CENPN.
ExpressionAtlasiQ96H22. baseline and differential.
GenevisibleiQ96H22. HS.

Interactioni

Subunit structurei

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.3 Publications

Protein-protein interaction databases

BioGridi120942. 17 interactions.
IntActiQ96H22. 1 interaction.
MINTiMINT-4995499.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG17730.
GeneTreeiENSGT00390000004738.
HOGENOMiHOG000015409.
HOVERGENiHBG058868.
InParanoidiQ96H22.
KOiK11506.
OMAiMTILKAW.
OrthoDBiEOG7P8PB4.
PhylomeDBiQ96H22.
TreeFamiTF329714.

Family and domain databases

InterProiIPR027715. CENP-N.
IPR007902. Chl4/mis15/CENP-N.
[Graphical view]
PANTHERiPTHR32250. PTHR32250. 1 hit.
PfamiPF05238. CENP-N. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96H22-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDETVAEFIK RTILKIPMNE LTTILKAWDF LSENQLQTVN FRQRKESVVQ
60 70 80 90 100
HLIHLCEEKR ASISDAALLD IIYMQFHQHQ KVWEVFQMSK GPGEDVDLFD
110 120 130 140 150
MKQFKNSFKK ILQRALKNVT VSFRETEENA VWIRIAWGTQ YTKPNQYKPT
160 170 180 190 200
YVVYYSQTPY AFTSSSMLRR NTPLLGQALT IASKHHQIVK MDLRSRYLDS
210 220 230 240 250
LKAIVFKQYN QTFETHNSTT PLQERSLGLD INMDSRIIHE NIVEKERVQR
260 270 280 290 300
ITQETFGDYP QPQLEFAQYK LETKFKSGLN GSILAEREEP LRCLIKFSSP
310 320 330
HLLEALKSLA PAGIADAPLS PLLTCIPNKR MNYFKIRDK
Length:339
Mass (Da):39,555
Last modified:October 5, 2010 - v2
Checksum:i7A0D3326032DE99B
GO
Isoform 2 (identifier: Q96H22-2) [UniParc]FASTAAdd to basket

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

Show »
Length:204
Mass (Da):24,067
Checksum:i3954E4F78E020360
GO
Isoform 3 (identifier: Q96H22-3) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:353
Mass (Da):41,194
Checksum:iB3366A33C89CD296
GO
Isoform 4 (identifier: Q96H22-4) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:319
Mass (Da):37,083
Checksum:i52873DA13A654ED2
GO
Isoform 5 (identifier: Q96H22-5) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:305
Mass (Da):35,556
Checksum:i5D7E6CFAB91045CD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391T → A in AK026313 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti84 – 841E → D.4 Publications
Corresponds to variant rs935939 [ dbSNP | Ensembl ].
VAR_027419
Natural varianti223 – 2231Q → R.
Corresponds to variant rs11641523 [ dbSNP | Ensembl ].
VAR_048689
Natural varianti288 – 2881E → K.1 Publication
Corresponds to variant rs2549887 [ dbSNP | Ensembl ].
VAR_048690

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei73 – 9321YMQFH…SKGPG → C in isoform 4. 1 PublicationVSP_044689Add
BLAST
Alternative sequencei177 – 21034Missing in isoform 5. 1 PublicationVSP_044690Add
BLAST
Alternative sequencei178 – 20427ALTIA…SLKAI → ELEATGKIYLRQEEIILDIT EMKKACN in isoform 2. 2 PublicationsVSP_020441Add
BLAST
Alternative sequencei205 – 339135Missing in isoform 2. 2 PublicationsVSP_020442Add
BLAST
Alternative sequencei313 – 33927GIADA…KIRDK → ALVCRIQKLLCYSGSHSQGT QDPSSWQKDLYLLFVPLYPR C in isoform 3. 1 PublicationVSP_044565Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10931.1. [Q96H22-2]
CCDS42199.1. [Q96H22-3]
CCDS42200.1. [Q96H22-1]
CCDS58482.1. [Q96H22-5]
CCDS58483.1. [Q96H22-4]
RefSeqiNP_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_006721236.2. [Q96H22-1]
UniGeneiHs.726537.

Genome annotation databases

EnsembliENST00000299572; ENSP00000299572; ENSG00000166451. [Q96H22-2]
ENST00000305850; ENSP00000305608; ENSG00000166451. [Q96H22-1]
ENST00000393335; ENSP00000377007; ENSG00000166451. [Q96H22-3]
ENST00000428963; ENSP00000393991; ENSG00000166451. [Q96H22-5]
ENST00000439957; ENSP00000395235; ENSG00000166451. [Q96H22-4]
GeneIDi55839.
KEGGihsa:55839.
UCSCiuc002ffw.4. human. [Q96H22-2]
uc002ffx.2. human. [Q96H22-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10931.1. [Q96H22-2]
CCDS42199.1. [Q96H22-3]
CCDS42200.1. [Q96H22-1]
CCDS58482.1. [Q96H22-5]
CCDS58483.1. [Q96H22-4]
RefSeqiNP_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_006721236.2. [Q96H22-1]
UniGeneiHs.726537.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120942. 17 interactions.
IntActiQ96H22. 1 interaction.
MINTiMINT-4995499.

PTM databases

PhosphoSiteiQ96H22.

Polymorphism and mutation databases

BioMutaiCENPN.
DMDMi308153423.

Proteomic databases

MaxQBiQ96H22.
PaxDbiQ96H22.
PRIDEiQ96H22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299572; ENSP00000299572; ENSG00000166451. [Q96H22-2]
ENST00000305850; ENSP00000305608; ENSG00000166451. [Q96H22-1]
ENST00000393335; ENSP00000377007; ENSG00000166451. [Q96H22-3]
ENST00000428963; ENSP00000393991; ENSG00000166451. [Q96H22-5]
ENST00000439957; ENSP00000395235; ENSG00000166451. [Q96H22-4]
GeneIDi55839.
KEGGihsa:55839.
UCSCiuc002ffw.4. human. [Q96H22-2]
uc002ffx.2. human. [Q96H22-1]

Organism-specific databases

CTDi55839.
GeneCardsiGC16P081040.
HGNCiHGNC:30873. CENPN.
MIMi611509. gene.
neXtProtiNX_Q96H22.
PharmGKBiPA143485397.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG17730.
GeneTreeiENSGT00390000004738.
HOGENOMiHOG000015409.
HOVERGENiHBG058868.
InParanoidiQ96H22.
KOiK11506.
OMAiMTILKAW.
OrthoDBiEOG7P8PB4.
PhylomeDBiQ96H22.
TreeFamiTF329714.

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

GeneWikiiCENPN.
GenomeRNAii55839.
NextBioi35472500.
PROiQ96H22.
SOURCEiSearch...

Gene expression databases

BgeeiQ96H22.
CleanExiHS_CENPN.
ExpressionAtlasiQ96H22. baseline and differential.
GenevisibleiQ96H22. HS.

Family and domain databases

InterProiIPR027715. CENP-N.
IPR007902. Chl4/mis15/CENP-N.
[Graphical view]
PANTHERiPTHR32250. PTHR32250. 1 hit.
PfamiPF05238. CENP-N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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].

Entry informationi

Entry nameiCENPN_HUMAN
AccessioniPrimary (citable) accession number: Q96H22
Secondary accession number(s): A8MZE6
, B3KN53, B4DJD1, B4DPY7, C9JJM5, D3DUK8, E7ES30, E7ETS3, Q9NZ83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: October 5, 2010
Last modified: June 24, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.