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Kinetochore protein NDC80 homolog (Highly expressed in cancer protein) (Kinetochore protein Hec1) (HsHec1) (Kinetochore-associated protein 2) (Retinoblastoma-associated protein HEC)

 NDC80_HUMAN             Reviewed;         642 AA.
O14777; Q6PJX2;
19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 153.
RecName: Full=Kinetochore protein NDC80 homolog;
AltName: Full=Highly expressed in cancer protein;
AltName: Full=Kinetochore protein Hec1;
Short=HsHec1;
AltName: Full=Kinetochore-associated protein 2;
AltName: Full=Retinoblastoma-associated protein HEC;
Name=NDC80; Synonyms=HEC, HEC1, KNTC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=9315664; DOI=10.1128/MCB.17.10.6049;
Chen Y., Riley D.J., Chen P.-L., Lee W.-H.;
"HEC, a novel nuclear protein rich in leucine heptad repeats
specifically involved in mitosis.";
Mol. Cell. Biol. 17:6049-6056(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
INTERACTION WITH NEK2; PSMC2; PSMC5 AND SMC1A, SUBCELLULAR LOCATION,
AND DEVELOPMENTAL STAGE.
PubMed=9295362; DOI=10.1074/jbc.272.38.24081;
Chen Y., Sharp Z.D., Lee W.-H.;
"HEC binds to the seventh regulatory subunit of the 26 S proteasome
and modulates the proteolysis of mitotic cyclins.";
J. Biol. Chem. 272:24081-24087(1997).
[4]
INTERACTION WITH NEK2; PSMC2; PSMC5; RB1 AND SMC1A.
PubMed=10409732; DOI=10.1128/MCB.19.8.5417;
Zheng L., Chen Y., Lee W.-H.;
"Hec1p, an evolutionarily conserved coiled-coil protein, modulates
chromosome segregation through interaction with SMC proteins.";
Mol. Cell. Biol. 19:5417-5428(1999).
[5]
INTERACTION WITH RB1 AND SMC1A, AND MUTAGENESIS OF GLU-234.
PubMed=10779342; DOI=10.1128/MCB.20.10.3529-3537.2000;
Zheng L., Chen Y., Riley D.J., Chen P.-L., Lee W.-H.;
"Retinoblastoma protein enhances the fidelity of chromosome
segregation mediated by hsHec1p.";
Mol. Cell. Biol. 20:3529-3537(2000).
[6]
INTERACTION WITH NEK2, AND PHOSPHORYLATION AT SER-165 BY NEK2.
PubMed=12386167; DOI=10.1074/jbc.M207069200;
Chen Y., Riley D.J., Zheng L., Chen P.-L., Lee W.-H.;
"Phosphorylation of the mitotic regulator protein Hec1 by Nek2 kinase
is essential for faithful chromosome segregation.";
J. Biol. Chem. 277:49408-49416(2002).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12351790; DOI=10.1126/science.1075596;
Martin-Lluesma S., Stucke V.M., Nigg E.A.;
"Role of Hec1 in spindle checkpoint signaling and kinetochore
recruitment of Mad1/Mad2.";
Science 297:2267-2270(2002).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14654001; DOI=10.1016/j.cub.2003.10.056;
DeLuca J.G., Howell B.J., Canman J.C., Hickey J.M., Fang G.,
Salmon E.D.;
"Nuf2 and Hec1 are required for retention of the checkpoint proteins
Mad1 and Mad2 to kinetochores.";
Curr. Biol. 13:2103-2109(2003).
[9]
FUNCTION.
PubMed=15235793; DOI=10.1007/s00412-004-0288-2;
Stucke V.M., Baumann C., Nigg E.A.;
"Kinetochore localization and microtubule interaction of the human
spindle checkpoint kinase Mps1.";
Chromosoma 113:1-15(2004).
[10]
FUNCTION.
PubMed=15062103; DOI=10.1016/j.cub.2004.03.031;
Joseph J., Liu S.-T., Jablonski S.A., Yen T.J., Dasso M.;
"The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore
interactions in vivo.";
Curr. Biol. 14:611-617(2004).
[11]
FUNCTION.
PubMed=15239953; DOI=10.1016/j.devcel.2004.06.006;
Meraldi P., Draviam V.M., Sorger P.K.;
"Timing and checkpoints in the regulation of mitotic progression.";
Dev. Cell 7:45-60(2004).
[12]
SUBCELLULAR LOCATION.
PubMed=15133482; DOI=10.1038/sj.embor.7400154;
Steensgaard P., Garre M., Muradore I., Transidico P., Nigg E.A.,
Kitagawa K., Earnshaw W.C., Faretta M., Musacchio A.;
"Sgt1 is required for human kinetochore assembly.";
EMBO Rep. 5:626-631(2004).
[13]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN
THE NDC80 COMPLEX.
PubMed=14699129; DOI=10.1074/jbc.M310224200;
Bharadwaj R., Qi W., Yu H.;
"Identification of two novel components of the human NDC80 kinetochore
complex.";
J. Biol. Chem. 279:13076-13085(2004).
[14]
SUBCELLULAR LOCATION.
PubMed=14978040; DOI=10.1074/jbc.M314205200;
Lou Y., Yao J., Zereshki A., Dou Z., Ahmed K., Wang H., Hu J.,
Wang Y., Yao X.;
"NEK2A interacts with MAD1 and possibly functions as a novel
integrator of the spindle checkpoint signaling.";
J. Biol. Chem. 279:20049-20057(2004).
[15]
INTERACTION WITH AURKB AND CDCA1, AND PHOSPHORYLATION BY AURKA AND
AURKB.
PubMed=14602875; DOI=10.1074/mcp.M300072-MCP200;
Tien A.-C., Lin M.-H., Su L.-J., Hong Y.-R., Cheng T.-S., Lee Y.-C.G.,
Lin W.-J., Still I.H., Huang C.-Y.F.;
"Identification of the substrates and interaction proteins of aurora
kinases from a protein-protein interaction model.";
Mol. Cell. Proteomics 3:93-104(2004).
[16]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A COMPLEX
WITH MIS12.
PubMed=15502821; DOI=10.1038/ncb1187;
Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y.,
Yanagida M.;
"A conserved Mis12 centromere complex is linked to heterochromatic HP1
and outer kinetochore protein Zwint-1.";
Nat. Cell Biol. 6:1135-1141(2004).
[17]
SUBCELLULAR LOCATION.
PubMed=15964272; DOI=10.1016/j.cub.2005.05.026;
Ahonen L.J., Kallio M.J., Daum J.R., Bolton M., Manke I.A.,
Yaffe M.B., Stukenberg P.T., Gorbsky G.J.;
"Polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope
and modulates the association of spindle-checkpoint proteins at
kinetochores.";
Curr. Biol. 15:1078-1089(2005).
[18]
CHARACTERIZATION OF THE NDC80 COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=15961401; DOI=10.1074/jbc.M504070200;
Ciferri C., De Luca J., Monzani S., Ferrari K.J., Ristic D., Wyman C.,
Stark H., Kilmartin J., Salmon E.D., Musacchio A.;
"Architecture of the human Ndc80-Hec1 complex, a critical constituent
of the outer kinetochore.";
J. Biol. Chem. 280:29088-29095(2005).
[19]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A COMPLEX
WITH ZWINT.
PubMed=15824131; DOI=10.1083/jcb.200411118;
Kops G.J.P.L., Kim Y., Weaver B.A.A., Mao Y., McLeod I.,
Yates J.R. III, Tagaya M., Cleveland D.W.;
"ZW10 links mitotic checkpoint signaling to the structural
kinetochore.";
J. Cell Biol. 169:49-60(2005).
[20]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15548592; DOI=10.1091/mbc.E04-09-0852;
DeLuca J.G., Dong Y., Hergert P., Strauss J., Hickey J.M.,
Salmon E.D., McEwen B.F.;
"Hec1 and Nuf2 are core components of the kinetochore outer plate
essential for organizing microtubule attachment sites.";
Mol. Biol. Cell 16:519-531(2005).
[21]
INTERACTION WITH CENPH.
PubMed=15713649; DOI=10.1128/MCB.25.5.1958-1970.2005;
Mikami Y., Hori T., Kimura H., Fukagawa T.;
"The functional region of CENP-H interacts with the Nuf2 complex that
localizes to centromere during mitosis.";
Mol. Cell. Biol. 25:1958-1970(2005).
[22]
FUNCTION, INTERACTION WITH ZWINT, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=16732327; DOI=10.1038/sj.onc.1209687;
Lin Y.-T., Chen Y., Wu G., Lee W.-H.;
"Hec1 sequentially recruits Zwint-1 and ZW10 to kinetochores for
faithful chromosome segregation and spindle checkpoint control.";
Oncogene 25:6901-6914(2006).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
FUNCTION.
PubMed=23085020; DOI=10.1016/j.devcel.2012.09.012;
Schmidt J.C., Arthanari H., Boeszoermenyi A., Dashkevich N.M.,
Wilson-Kubalek E.M., Monnier N., Markus M., Oberer M., Milligan R.A.,
Bathe M., Wagner G., Grishchuk E.L., Cheeseman I.M.;
"The kinetochore-bound Ska1 complex tracks depolymerizing microtubules
and binds to curved protofilaments.";
Dev. Cell 23:968-980(2012).
[26]
INTERACTION WITH CDT1.
PubMed=22581055; DOI=10.1038/ncb2489;
Varma D., Chandrasekaran S., Sundin L.J., Reidy K.T., Wan X.,
Chasse D.A., Nevis K.R., DeLuca J.G., Salmon E.D., Cook J.G.;
"Recruitment of the human Cdt1 replication licensing protein by the
loop domain of Hec1 is required for stable kinetochore-microtubule
attachment.";
Nat. Cell Biol. 14:593-603(2012).
[27]
FUNCTION.
PubMed=23891108; DOI=10.1016/j.cub.2013.06.040;
Shrestha R.L., Draviam V.M.;
"Lateral to end-on conversion of chromosome-microtubule attachment
requires kinesins CENP-E and MCAK.";
Curr. Biol. 23:1514-1526(2013).
[28]
ERRATUM.
Shrestha R.L., Draviam V.M.;
Curr. Biol. 23:2440-2441(2013).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-69, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
FUNCTION.
PubMed=25743205; DOI=10.1038/ncomms7447;
Iemura K., Tanaka K.;
"Chromokinesin Kid and kinetochore kinesin CENP-E differentially
support chromosome congression without end-on attachment to
microtubules.";
Nat. Commun. 6:6447-6447(2015).
[31]
INTERACTION WITH CKAP5.
PubMed=27156448; DOI=10.1016/j.cell.2016.04.030;
Miller M.P., Asbury C.L., Biggins S.;
"A TOG protein confers tension sensitivity to kinetochore-microtubule
attachments.";
Cell 165:1428-1439(2016).
-!- FUNCTION: Acts as a component of the essential kinetochore-
associated NDC80 complex, which is required for chromosome
segregation and spindle checkpoint activity (PubMed:9315664,
PubMed:12351790, PubMed:14654001, PubMed:14699129,
PubMed:15062103, PubMed:15235793, PubMed:15239953,
PubMed:15548592, PubMed:16732327). Required for kinetochore
integrity and the organization of stable microtubule binding sites
in the outer plate of the kinetochore (PubMed:15548592). The NDC80
complex synergistically enhances the affinity of the SKA1 complex
for microtubules and may allow the NDC80 complex to track
depolymerizing microtubules (PubMed:23085020). Plays a role in
chromosome congression and is essential for the end-on attachment
of the kinetochores to spindle microtubules (PubMed:25743205,
PubMed:23891108). {ECO:0000269|PubMed:12351790,
ECO:0000269|PubMed:14654001, ECO:0000269|PubMed:14699129,
ECO:0000269|PubMed:15062103, ECO:0000269|PubMed:15235793,
ECO:0000269|PubMed:15239953, ECO:0000269|PubMed:15548592,
ECO:0000269|PubMed:16732327, ECO:0000269|PubMed:23085020,
ECO:0000269|PubMed:23891108, ECO:0000269|PubMed:25743205,
ECO:0000269|PubMed:9315664}.
-!- SUBUNIT: Component of the NDC80 complex, which consists of
NDC80/HEC1, CDCA1, SPBC24 and SPBC25. The NDC80 complex is formed
by two subcomplexes composed of NDC80/HEC1-CDCA1 and SPBC24-
SPBC25. Each subcomplex is formed by parallel interactions through
the coiled-coil domains of individual subunits. Formation of a
tetrameric complex is mediated by interactions between the C-
terminal regions of both subunits of the NDC80/HEC1-CDCA1
subcomplex and the N-terminal regions of both subunits of the
SPBC24-SPBC25 complex. The tetrameric NDC80 complex has an
elongated rod-like structure with globular domains at either end.
Interacts with isoform 1 of NEK2 and ZWINT specifically during
mitosis. Interacts with CENPH and MIS12. May interact with AURKB,
PSMC2, PSMC5 and SMC1A. May interact with RB1 during G2 phase and
mitosis. Interacts with CKAP5 (PubMed:27156448). Interacts with
CDT1; leading to kinetochore localization of CDT1
(PubMed:22581055). {ECO:0000269|PubMed:10409732,
ECO:0000269|PubMed:10779342, ECO:0000269|PubMed:12386167,
ECO:0000269|PubMed:14602875, ECO:0000269|PubMed:14699129,
ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:15713649,
ECO:0000269|PubMed:15824131, ECO:0000269|PubMed:16732327,
ECO:0000269|PubMed:22581055, ECO:0000269|PubMed:27156448,
ECO:0000269|PubMed:9295362}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-715849, EBI-715849;
P18848:ATF4; NbExp=5; IntAct=EBI-715849, EBI-492498;
P48047:ATP5O; NbExp=3; IntAct=EBI-715849, EBI-355815;
Q9P1Z2:CALCOCO1; NbExp=4; IntAct=EBI-715849, EBI-749920;
Q8TD31-3:CCHCR1; NbExp=7; IntAct=EBI-715849, EBI-10175300;
P51946:CCNH; NbExp=3; IntAct=EBI-715849, EBI-741406;
O75909:CCNK; NbExp=3; IntAct=EBI-715849, EBI-739806;
Q9H211:CDT1; NbExp=7; IntAct=EBI-715849, EBI-456953;
Q9H3R5:CENPH; NbExp=5; IntAct=EBI-715849, EBI-1003700;
Q8IYI6:EXOC8; NbExp=4; IntAct=EBI-715849, EBI-742102;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-715849, EBI-2514791;
O14964:HGS; NbExp=5; IntAct=EBI-715849, EBI-740220;
O75146-2:HIP1R; NbExp=4; IntAct=EBI-715849, EBI-12292427;
Q8IY31:IFT20; NbExp=5; IntAct=EBI-715849, EBI-744203;
Q9BVG8-5:KIFC3; NbExp=4; IntAct=EBI-715849, EBI-14069005;
Q6P597:KLC3; NbExp=3; IntAct=EBI-715849, EBI-1643885;
P04259:KRT6B; NbExp=3; IntAct=EBI-715849, EBI-740907;
Q9NPJ6:MED4; NbExp=3; IntAct=EBI-715849, EBI-394607;
P55081:MFAP1; NbExp=3; IntAct=EBI-715849, EBI-1048159;
Q9GZM8:NDEL1; NbExp=3; IntAct=EBI-715849, EBI-928842;
Q9BZD4:NUF2; NbExp=13; IntAct=EBI-715849, EBI-724102;
Q6ZNE9:RUFY4; NbExp=5; IntAct=EBI-715849, EBI-10181525;
Q86XK3:SFR1; NbExp=3; IntAct=EBI-715849, EBI-1104535;
Q96ES7:SGF29; NbExp=6; IntAct=EBI-715849, EBI-743117;
Q9HBM1:SPC25; NbExp=10; IntAct=EBI-715849, EBI-999909;
O75558:STX11; NbExp=3; IntAct=EBI-715849, EBI-714135;
Q9UBB9:TFIP11; NbExp=5; IntAct=EBI-715849, EBI-1105213;
Q15025:TNIP1; NbExp=5; IntAct=EBI-715849, EBI-357849;
Q05BL1:TP53BP2; NbExp=4; IntAct=EBI-715849, EBI-11952721;
Q13625-3:TP53BP2; NbExp=3; IntAct=EBI-715849, EBI-10175039;
P33981-1:TTK; NbExp=4; IntAct=EBI-715849, EBI-15986834;
P40222:TXLNA; NbExp=3; IntAct=EBI-715849, EBI-359793;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-715849, EBI-739895;
Q9Y3C0:WASHC3; NbExp=6; IntAct=EBI-715849, EBI-712969;
O95229:ZWINT; NbExp=13; IntAct=EBI-715849, EBI-1001132;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere,
kinetochore. Note=Localizes to kinetochores from late prophase to
anaphase. Localizes specifically to the outer plate of the
kinetochore.
-!- DEVELOPMENTAL STAGE: Expression peaks in mitosis.
{ECO:0000269|PubMed:16732327, ECO:0000269|PubMed:9295362,
ECO:0000269|PubMed:9315664}.
-!- PTM: Phosphorylation begins in S phase of the cell cycle and peaks
in mitosis. Phosphorylated by NEK2. May also be phosphorylated by
AURKA and AURKB. {ECO:0000269|PubMed:12386167,
ECO:0000269|PubMed:14602875}.
-!- SIMILARITY: Belongs to the NDC80/HEC1 family. {ECO:0000305}.
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EMBL; AF017790; AAB80726.1; -; mRNA.
EMBL; BC010171; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS11827.1; -.
RefSeq; NP_006092.1; NM_006101.2.
UniGene; Hs.414407; -.
PDB; 2IGP; X-ray; 1.80 A; A=81-196.
PDB; 2VE7; X-ray; 2.88 A; A/B=80-286.
PDB; 3IZ0; EM; -; C/E=80-286.
PDBsum; 2IGP; -.
PDBsum; 2VE7; -.
PDBsum; 3IZ0; -.
ProteinModelPortal; O14777; -.
SMR; O14777; -.
BioGrid; 115675; 87.
CORUM; O14777; -.
DIP; DIP-35100N; -.
IntAct; O14777; 79.
MINT; MINT-1411676; -.
STRING; 9606.ENSP00000261597; -.
ChEMBL; CHEMBL5660; -.
iPTMnet; O14777; -.
PhosphoSitePlus; O14777; -.
BioMuta; NDC80; -.
EPD; O14777; -.
MaxQB; O14777; -.
PaxDb; O14777; -.
PeptideAtlas; O14777; -.
PRIDE; O14777; -.
DNASU; 10403; -.
Ensembl; ENST00000261597; ENSP00000261597; ENSG00000080986.
GeneID; 10403; -.
KEGG; hsa:10403; -.
UCSC; uc002kli.3; human.
CTD; 10403; -.
DisGeNET; 10403; -.
EuPathDB; HostDB:ENSG00000080986.12; -.
GeneCards; NDC80; -.
HGNC; HGNC:16909; NDC80.
HPA; HPA066330; -.
MIM; 607272; gene.
neXtProt; NX_O14777; -.
OpenTargets; ENSG00000080986; -.
PharmGKB; PA162397359; -.
eggNOG; KOG0995; Eukaryota.
eggNOG; COG5185; LUCA.
GeneTree; ENSGT00390000018386; -.
HOGENOM; HOG000012981; -.
HOVERGEN; HBG081861; -.
InParanoid; O14777; -.
KO; K11547; -.
OMA; KSPTQKD; -.
OrthoDB; EOG091G046M; -.
PhylomeDB; O14777; -.
TreeFam; TF101177; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SignaLink; O14777; -.
SIGNOR; O14777; -.
ChiTaRS; NDC80; human.
EvolutionaryTrace; O14777; -.
GeneWiki; NDC80; -.
GenomeRNAi; 10403; -.
PRO; PR:O14777; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000080986; -.
CleanEx; HS_NDC80; -.
ExpressionAtlas; O14777; baseline and differential.
Genevisible; O14777; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0000775; C:chromosome, centromeric region; TAS:ProtInc.
GO; GO:0000777; C:condensed chromosome kinetochore; IDA:UniProtKB.
GO; GO:0000942; C:condensed nuclear chromosome outer kinetochore; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0031262; C:Ndc80 complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:UniProtKB.
GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
GO; GO:0051383; P:kinetochore organization; IMP:CAFA.
GO; GO:0051310; P:metaphase plate congression; IMP:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
GO; GO:0000070; P:mitotic sister chromatid segregation; TAS:ProtInc.
GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB.
GO; GO:1905342; P:positive regulation of protein localization to kinetochore; IMP:CAFA.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
InterPro; IPR005550; Kinetochore_Ndc80.
Pfam; PF03801; Ndc80_HEC; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
Coiled coil; Complete proteome; Kinetochore; Mitosis; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 642 Kinetochore protein NDC80 homolog.
/FTId=PRO_0000249550.
REGION 1 445 Interaction with the N-terminus of CDCA1.
REGION 1 250 Nuclear localization.
REGION 128 251 Interaction with RB1.
REGION 251 618 Interaction with NEK2 and ZWINT.
{ECO:0000269|PubMed:16732327}.
REGION 251 431 Interaction with SMC1A.
REGION 361 547 Interaction with PSMC2 and SMC1A.
REGION 446 642 Interaction with the C-terminus of CDCA1
and the SPBC24-SPBC25 subcomplex.
COILED 261 403 {ECO:0000255}.
COILED 458 642 {ECO:0000255}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 165 165 Phosphoserine; by NEK2.
{ECO:0000269|PubMed:12386167}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D0F1}.
VARIANT 66 66 S -> A (in dbSNP:rs16943490).
/FTId=VAR_027436.
VARIANT 348 348 E -> D (in dbSNP:rs12456560).
/FTId=VAR_027437.
VARIANT 605 605 A -> P (in dbSNP:rs1983346).
/FTId=VAR_027438.
MUTAGEN 234 234 E->K: Abrogates binding to RB1.
{ECO:0000269|PubMed:10779342}.
HELIX 89 105 {ECO:0000244|PDB:2IGP}.
TURN 114 117 {ECO:0000244|PDB:2IGP}.
HELIX 122 133 {ECO:0000244|PDB:2IGP}.
TURN 134 136 {ECO:0000244|PDB:2IGP}.
HELIX 147 157 {ECO:0000244|PDB:2IGP}.
HELIX 166 170 {ECO:0000244|PDB:2IGP}.
TURN 171 173 {ECO:0000244|PDB:2IGP}.
TURN 175 177 {ECO:0000244|PDB:2IGP}.
HELIX 178 194 {ECO:0000244|PDB:2IGP}.
HELIX 222 238 {ECO:0000244|PDB:2VE7}.
HELIX 244 258 {ECO:0000244|PDB:2VE7}.
HELIX 264 286 {ECO:0000244|PDB:2VE7}.
SEQUENCE 642 AA; 73913 MW; 6A82DA4D8B77ECDC CRC64;
MKRSSVSSGG AGRLSMQELR SQDVNKQGLY TPQTKEKPTF GKLSINKPTS ERKVSLFGKR
TSGHGSRNSQ LGIFSSSEKI KDPRPLNDKA FIQQCIRQLC EFLTENGYAH NVSMKSLQAP
SVKDFLKIFT FLYGFLCPSY ELPDTKFEEE VPRIFKDLGY PFALSKSSMY TVGAPHTWPH
IVAALVWLID CIKIHTAMKE SSPLFDDGQP WGEETEDGIM HNKLFLDYTI KCYESFMSGA
DSFDEMNAEL QSKLKDLFNV DAFKLESLEA KNRALNEQIA RLEQEREKEP NRLESLRKLK
ASLQGDVQKY QAYMSNLESH SAILDQKLNG LNEEIARVEL ECETIKQENT RLQNIIDNQK
YSVADIERIN HERNELQQTI NKLTKDLEAE QQKLWNEELK YARGKEAIET QLAEYHKLAR
KLKLIPKGAE NSKGYDFEIK FNPEAGANCL VKYRAQVYVP LKELLNETEE EINKALNKKM
GLEDTLEQLN AMITESKRSV RTLKEEVQKL DDLYQQKIKE AEEEDEKCAS ELESLEKHKH
LLESTVNQGL SEAMNELDAV QREYQLVVQT TTEERRKVGN NLQRLLEMVA THVGSVEKHL
EEQIAKVDRE YEECMSEDLS ENIKEIRDKY EKKATLIKSS EE


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