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Protein

Kinetochore protein NDC80 homolog

Gene

NDC80

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

Functioni

Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore.9 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • structural constituent of cytoskeleton Source: GO_Central

GO - Biological processi

  • attachment of mitotic spindle microtubules to kinetochore Source: GO_Central
  • attachment of spindle microtubules to kinetochore Source: UniProtKB
  • cell division Source: UniProtKB-KW
  • chromosome segregation Source: UniProtKB
  • establishment of mitotic spindle orientation Source: UniProtKB
  • mitotic cell cycle Source: Reactome
  • mitotic nuclear division Source: ProtInc
  • mitotic sister chromatid segregation Source: ProtInc
  • mitotic spindle organization Source: UniProtKB
  • small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.
SignaLinkiO14777.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinetochore protein NDC80 homolog
Alternative name(s):
Highly expressed in cancer protein
Kinetochore protein Hec1
Short name:
HsHec1
Kinetochore-associated protein 2
Retinoblastoma-associated protein HEC
Gene namesi
Name:NDC80
Synonyms:HEC, HEC1, KNTC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:16909. NDC80.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric region Source: ProtInc
  • condensed chromosome kinetochore Source: UniProtKB
  • condensed nuclear chromosome kinetochore Source: GO_Central
  • condensed nuclear chromosome outer kinetochore Source: BHF-UCL
  • cytosol Source: Reactome
  • kinetochore Source: UniProtKB
  • membrane Source: UniProtKB
  • Ndc80 complex Source: UniProtKB
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi234 – 2341E → K: Abrogates binding to RB1. 1 Publication

Organism-specific databases

PharmGKBiPA162397359.

Polymorphism and mutation databases

BioMutaiNDC80.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 642642Kinetochore protein NDC80 homologPRO_0000249550Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691Phosphoserine1 Publication
Modified residuei165 – 1651Phosphoserine; by NEK21 Publication

Post-translational modificationi

Phosphorylation begins in S phase of the cell cycle and peaks in mitosis. Phosphorylated by NEK2. May also be phosphorylated by AURKA and AURKB.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO14777.
PaxDbiO14777.
PeptideAtlasiO14777.
PRIDEiO14777.

PTM databases

PhosphoSiteiO14777.

Expressioni

Developmental stagei

Expression peaks in mitosis.3 Publications

Gene expression databases

BgeeiO14777.
CleanExiHS_NDC80.
ExpressionAtlasiO14777. baseline and differential.
GenevisibleiO14777. HS.

Interactioni

Subunit structurei

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.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-715849,EBI-715849
ATF4P188483EBI-715849,EBI-492498
ATP5OP480473EBI-715849,EBI-355815
CALCOCO1Q9P1Z24EBI-715849,EBI-749920
CCDC101Q96ES74EBI-715849,EBI-743117
CCDC53Q9Y3C04EBI-715849,EBI-712969
CCHCR1Q8TD31-33EBI-715849,EBI-10175300
CCNHP519463EBI-715849,EBI-741406
CCNKO759093EBI-715849,EBI-739806
CENPHQ9H3R53EBI-715849,EBI-1003700
HAUS1Q96CS23EBI-715849,EBI-2514791
HGSO149643EBI-715849,EBI-740220
IFT20Q8IY315EBI-715849,EBI-744203
KLC3Q6P5973EBI-715849,EBI-1643885
KRT6BP042593EBI-715849,EBI-740907
MED4Q9NPJ63EBI-715849,EBI-394607
MFAP1P550813EBI-715849,EBI-1048159
NDEL1Q9GZM83EBI-715849,EBI-928842
NUF2Q9BZD412EBI-715849,EBI-724102
RUFY4Q6ZNE93EBI-715849,EBI-10181525
SFR1Q86XK33EBI-715849,EBI-1104535
SPC25Q9HBM110EBI-715849,EBI-999909
STX11O755583EBI-715849,EBI-714135
TFIP11Q9UBB93EBI-715849,EBI-1105213
TNIP1Q150253EBI-715849,EBI-357849
TP53BP2Q13625-33EBI-715849,EBI-10175039
TXLNAP402223EBI-715849,EBI-359793
ZWINTO9522912EBI-715849,EBI-1001132

Protein-protein interaction databases

BioGridi115675. 66 interactions.
IntActiO14777. 55 interactions.
MINTiMINT-1411676.
STRINGi9606.ENSP00000261597.

Structurei

Secondary structure

1
642
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi89 – 10517Combined sources
Turni114 – 1174Combined sources
Helixi122 – 13312Combined sources
Turni134 – 1363Combined sources
Helixi147 – 15711Combined sources
Helixi166 – 1705Combined sources
Turni171 – 1733Combined sources
Turni175 – 1773Combined sources
Helixi178 – 19417Combined sources
Helixi222 – 23817Combined sources
Helixi244 – 25815Combined sources
Helixi264 – 28623Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IGPX-ray1.80A81-196[»]
2VE7X-ray2.88A/B80-286[»]
3IZ0electron microscopy-C/E80-286[»]
ProteinModelPortaliO14777.
SMRiO14777. Positions 80-302.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14777.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 445445Interaction with the N-terminus of CDCA1Add
BLAST
Regioni1 – 250250Nuclear localizationAdd
BLAST
Regioni128 – 251124Interaction with RB1Add
BLAST
Regioni251 – 618368Interaction with NEK2 and ZWINTAdd
BLAST
Regioni251 – 431181Interaction with SMC1AAdd
BLAST
Regioni361 – 547187Interaction with PSMC2 and SMC1AAdd
BLAST
Regioni446 – 642197Interaction with the C-terminus of CDCA1 and the SPBC24-SPBC25 subcomplexAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili261 – 403143Sequence AnalysisAdd
BLAST
Coiled coili458 – 642185Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the NDC80/HEC1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5185.
GeneTreeiENSGT00390000018386.
HOGENOMiHOG000012981.
HOVERGENiHBG081861.
InParanoidiO14777.
KOiK11547.
OMAiREYEECM.
OrthoDBiEOG7NSB3P.
PhylomeDBiO14777.
TreeFamiTF101177.

Family and domain databases

InterProiIPR005550. Kinetochore_Ndc80.
[Graphical view]
PANTHERiPTHR10643. PTHR10643. 1 hit.
PfamiPF03801. Ndc80_HEC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14777-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRSSVSSGG AGRLSMQELR SQDVNKQGLY TPQTKEKPTF GKLSINKPTS
60 70 80 90 100
ERKVSLFGKR TSGHGSRNSQ LGIFSSSEKI KDPRPLNDKA FIQQCIRQLC
110 120 130 140 150
EFLTENGYAH NVSMKSLQAP SVKDFLKIFT FLYGFLCPSY ELPDTKFEEE
160 170 180 190 200
VPRIFKDLGY PFALSKSSMY TVGAPHTWPH IVAALVWLID CIKIHTAMKE
210 220 230 240 250
SSPLFDDGQP WGEETEDGIM HNKLFLDYTI KCYESFMSGA DSFDEMNAEL
260 270 280 290 300
QSKLKDLFNV DAFKLESLEA KNRALNEQIA RLEQEREKEP NRLESLRKLK
310 320 330 340 350
ASLQGDVQKY QAYMSNLESH SAILDQKLNG LNEEIARVEL ECETIKQENT
360 370 380 390 400
RLQNIIDNQK YSVADIERIN HERNELQQTI NKLTKDLEAE QQKLWNEELK
410 420 430 440 450
YARGKEAIET QLAEYHKLAR KLKLIPKGAE NSKGYDFEIK FNPEAGANCL
460 470 480 490 500
VKYRAQVYVP LKELLNETEE EINKALNKKM GLEDTLEQLN AMITESKRSV
510 520 530 540 550
RTLKEEVQKL DDLYQQKIKE AEEEDEKCAS ELESLEKHKH LLESTVNQGL
560 570 580 590 600
SEAMNELDAV QREYQLVVQT TTEERRKVGN NLQRLLEMVA THVGSVEKHL
610 620 630 640
EEQIAKVDRE YEECMSEDLS ENIKEIRDKY EKKATLIKSS EE
Length:642
Mass (Da):73,913
Last modified:January 1, 1998 - v1
Checksum:i6A82DA4D8B77ECDC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661S → A.
Corresponds to variant rs16943490 [ dbSNP | Ensembl ].
VAR_027436
Natural varianti348 – 3481E → D.
Corresponds to variant rs12456560 [ dbSNP | Ensembl ].
VAR_027437
Natural varianti605 – 6051A → P.
Corresponds to variant rs1983346 [ dbSNP | Ensembl ].
VAR_027438

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017790 mRNA. Translation: AAB80726.1.
BC010171 mRNA. No translation available.
CCDSiCCDS11827.1.
RefSeqiNP_006092.1. NM_006101.2.
UniGeneiHs.414407.

Genome annotation databases

EnsembliENST00000261597; ENSP00000261597; ENSG00000080986.
GeneIDi10403.
KEGGihsa:10403.
UCSCiuc002kli.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017790 mRNA. Translation: AAB80726.1.
BC010171 mRNA. No translation available.
CCDSiCCDS11827.1.
RefSeqiNP_006092.1. NM_006101.2.
UniGeneiHs.414407.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IGPX-ray1.80A81-196[»]
2VE7X-ray2.88A/B80-286[»]
3IZ0electron microscopy-C/E80-286[»]
ProteinModelPortaliO14777.
SMRiO14777. Positions 80-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115675. 66 interactions.
IntActiO14777. 55 interactions.
MINTiMINT-1411676.
STRINGi9606.ENSP00000261597.

Chemistry

ChEMBLiCHEMBL5660.

PTM databases

PhosphoSiteiO14777.

Polymorphism and mutation databases

BioMutaiNDC80.

Proteomic databases

MaxQBiO14777.
PaxDbiO14777.
PeptideAtlasiO14777.
PRIDEiO14777.

Protocols and materials databases

DNASUi10403.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261597; ENSP00000261597; ENSG00000080986.
GeneIDi10403.
KEGGihsa:10403.
UCSCiuc002kli.3. human.

Organism-specific databases

CTDi10403.
GeneCardsiGC18P002571.
HGNCiHGNC:16909. NDC80.
MIMi607272. gene.
neXtProtiNX_O14777.
PharmGKBiPA162397359.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5185.
GeneTreeiENSGT00390000018386.
HOGENOMiHOG000012981.
HOVERGENiHBG081861.
InParanoidiO14777.
KOiK11547.
OMAiREYEECM.
OrthoDBiEOG7NSB3P.
PhylomeDBiO14777.
TreeFamiTF101177.

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.
SignaLinkiO14777.

Miscellaneous databases

ChiTaRSiNDC80. human.
EvolutionaryTraceiO14777.
GeneWikiiNDC80.
GenomeRNAii10403.
NextBioi39424.
PROiO14777.
SOURCEiSearch...

Gene expression databases

BgeeiO14777.
CleanExiHS_NDC80.
ExpressionAtlasiO14777. baseline and differential.
GenevisibleiO14777. HS.

Family and domain databases

InterProiIPR005550. Kinetochore_Ndc80.
[Graphical view]
PANTHERiPTHR10643. PTHR10643. 1 hit.
PfamiPF03801. Ndc80_HEC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "HEC, a novel nuclear protein rich in leucine heptad repeats specifically involved in mitosis."
    Chen Y., Riley D.J., Chen P.-L., Lee W.-H.
    Mol. Cell. Biol. 17:6049-6056(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  2. "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].
    Tissue: Brain and Lymph.
  3. "HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins."
    Chen Y., Sharp Z.D., Lee W.-H.
    J. Biol. Chem. 272:24081-24087(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEK2; PSMC2; PSMC5 AND SMC1A, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  4. "Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins."
    Zheng L., Chen Y., Lee W.-H.
    Mol. Cell. Biol. 19:5417-5428(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEK2; PSMC2; PSMC5; RB1 AND SMC1A.
  5. "Retinoblastoma protein enhances the fidelity of chromosome segregation mediated by hsHec1p."
    Zheng L., Chen Y., Riley D.J., Chen P.-L., Lee W.-H.
    Mol. Cell. Biol. 20:3529-3537(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RB1 AND SMC1A, MUTAGENESIS OF GLU-234.
  6. "Phosphorylation of the mitotic regulator protein Hec1 by Nek2 kinase is essential for faithful chromosome segregation."
    Chen Y., Riley D.J., Zheng L., Chen P.-L., Lee W.-H.
    J. Biol. Chem. 277:49408-49416(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEK2, PHOSPHORYLATION AT SER-165 BY NEK2.
  7. "Role of Hec1 in spindle checkpoint signaling and kinetochore recruitment of Mad1/Mad2."
    Martin-Lluesma S., Stucke V.M., Nigg E.A.
    Science 297:2267-2270(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Nuf2 and Hec1 are required for retention of the checkpoint proteins Mad1 and Mad2 to kinetochores."
    DeLuca J.G., Howell B.J., Canman J.C., Hickey J.M., Fang G., Salmon E.D.
    Curr. Biol. 13:2103-2109(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Kinetochore localization and microtubule interaction of the human spindle checkpoint kinase Mps1."
    Stucke V.M., Baumann C., Nigg E.A.
    Chromosoma 113:1-15(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo."
    Joseph J., Liu S.-T., Jablonski S.A., Yen T.J., Dasso M.
    Curr. Biol. 14:611-617(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Timing and checkpoints in the regulation of mitotic progression."
    Meraldi P., Draviam V.M., Sorger P.K.
    Dev. Cell 7:45-60(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: SUBCELLULAR LOCATION.
  13. "Identification of two novel components of the human NDC80 kinetochore complex."
    Bharadwaj R., Qi W., Yu H.
    J. Biol. Chem. 279:13076-13085(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NDC80 COMPLEX.
  14. "NEK2A interacts with MAD1 and possibly functions as a novel integrator of the spindle checkpoint signaling."
    Lou Y., Yao J., Zereshki A., Dou Z., Ahmed K., Wang H., Hu J., Wang Y., Yao X.
    J. Biol. Chem. 279:20049-20057(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  15. "Identification of the substrates and interaction proteins of aurora kinases from a protein-protein interaction model."
    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.
    Mol. Cell. Proteomics 3:93-104(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AURKB AND CDCA1, PHOSPHORYLATION BY AURKA AND AURKB.
  16. "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and outer kinetochore protein Zwint-1."
    Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y., Yanagida M.
    Nat. Cell Biol. 6:1135-1141(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH MIS12.
  17. "Polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores."
    Ahonen L.J., Kallio M.J., Daum J.R., Bolton M., Manke I.A., Yaffe M.B., Stukenberg P.T., Gorbsky G.J.
    Curr. Biol. 15:1078-1089(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  18. "Architecture of the human Ndc80-Hec1 complex, a critical constituent of the outer kinetochore."
    Ciferri C., De Luca J., Monzani S., Ferrari K.J., Ristic D., Wyman C., Stark H., Kilmartin J., Salmon E.D., Musacchio A.
    J. Biol. Chem. 280:29088-29095(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE NDC80 COMPLEX, SUBCELLULAR LOCATION.
  19. "ZW10 links mitotic checkpoint signaling to the structural kinetochore."
    Kops G.J.P.L., Kim Y., Weaver B.A.A., Mao Y., McLeod I., Yates J.R. III, Tagaya M., Cleveland D.W.
    J. Cell Biol. 169:49-60(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH ZWINT.
  20. "Hec1 and Nuf2 are core components of the kinetochore outer plate essential for organizing microtubule attachment sites."
    DeLuca J.G., Dong Y., Hergert P., Strauss J., Hickey J.M., Salmon E.D., McEwen B.F.
    Mol. Biol. Cell 16:519-531(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  21. "The functional region of CENP-H interacts with the Nuf2 complex that localizes to centromere during mitosis."
    Mikami Y., Hori T., Kimura H., Fukagawa T.
    Mol. Cell. Biol. 25:1958-1970(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CENPH.
  22. "Hec1 sequentially recruits Zwint-1 and ZW10 to kinetochores for faithful chromosome segregation and spindle checkpoint control."
    Lin Y.-T., Chen Y., Wu G., Lee W.-H.
    Oncogene 25:6901-6914(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZWINT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  23. "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-69, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNDC80_HUMAN
AccessioniPrimary (citable) accession number: O14777
Secondary accession number(s): Q6PJX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: January 1, 1998
Last modified: June 24, 2015
This is version 127 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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.