NDC80_MACFA
ID NDC80_MACFA Reviewed; 642 AA.
AC Q4R630;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Kinetochore protein NDC80 homolog;
DE AltName: Full=Kinetochore protein Hec1;
DE AltName: Full=Kinetochore-associated protein 2;
GN Name=NDC80; Synonyms=HEC1, KNTC2; ORFNames=QtsA-19260;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a component of the essential kinetochore-associated
CC NDC80 complex, which is required for chromosome segregation and spindle
CC checkpoint activity. Required for kinetochore integrity and the
CC organization of stable microtubule binding sites in the outer plate of
CC the kinetochore. The NDC80 complex synergistically enhances the
CC affinity of the SKA1 complex for microtubules and may allow the NDC80
CC complex to track depolymerizing microtubules. Plays a role in
CC chromosome congression and is essential for the end-on attachment of
CC the kinetochores to spindle microtubules.
CC {ECO:0000250|UniProtKB:O14777}.
CC -!- SUBUNIT: Component of the NDC80 complex, which consists of NDC80/HEC1,
CC CDCA1, SPBC24 and SPBC25. The NDC80 complex is formed by two
CC subcomplexes composed of NDC80/HEC1-CDCA1 and SPBC24-SPBC25. Each
CC subcomplex is formed by parallel interactions through the coiled-coil
CC domains of individual subunits. Formation of a tetrameric complex is
CC mediated by interactions between the C-terminal regions of both
CC subunits of the NDC80/HEC1-CDCA1 subcomplex and the N-terminal regions
CC of both subunits of the SPBC24-SPBC25 complex. The tetrameric NDC80
CC complex has an elongated rod-like structure with globular domains at
CC either end. Interacts with NEK2 and ZWINT specifically during mitosis.
CC Interacts with CENPH and MIS12. May interact with AURKB, PSMC2, PSMC5
CC and SMC1A. May interact with RB1 during G2 phase and mitosis. Interacts
CC with CKAP5 (By similarity). Interacts with CDT1; leading to kinetochore
CC localization of CDT1 (By similarity). {ECO:0000250|UniProtKB:O14777}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O14777}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O14777}.
CC Note=Localizes to kinetochores from late prophase to anaphase.
CC Localizes specifically to the outer plate of the kinetochore.
CC {ECO:0000250|UniProtKB:O14777}.
CC -!- PTM: Phosphorylation begins in S phase of the cell cycle and peaks in
CC mitosis. Phosphorylated by NEK2. Also phosphorylated by AURKA and
CC AURKB. {ECO:0000250|UniProtKB:O14777}.
CC -!- PTM: Acetylated at Lys-53 and Lys-59 by KAT5 during mitosis, promoting
CC robust kinetochore-microtubule attachment. Deacetylated by SIRT1.
CC {ECO:0000250|UniProtKB:O14777}.
CC -!- SIMILARITY: Belongs to the NDC80/HEC1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB169360; BAE01445.1; -; mRNA.
DR RefSeq; NP_001271537.1; NM_001284608.1.
DR AlphaFoldDB; Q4R630; -.
DR SMR; Q4R630; -.
DR STRING; 9541.XP_005587142.1; -.
DR PRIDE; Q4R630; -.
DR GeneID; 101925531; -.
DR CTD; 10403; -.
DR eggNOG; KOG0995; Eukaryota.
DR OrthoDB; 925552at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0031262; C:Ndc80 complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140483; F:kinetochore adaptor activity; ISS:UniProtKB.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR Gene3D; 1.10.418.30; -; 1.
DR InterPro; IPR040967; DUF5595.
DR InterPro; IPR005550; Kinetochore_Ndc80.
DR InterPro; IPR038273; Ndc80_sf.
DR PANTHER; PTHR10643; PTHR10643; 1.
DR Pfam; PF18077; DUF5595; 1.
DR Pfam; PF03801; Ndc80_HEC; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Kinetochore; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..642
FT /note="Kinetochore protein NDC80 homolog"
FT /id="PRO_0000249551"
FT REGION 1..445
FT /note="Interaction with the N-terminus of CDCA1"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT REGION 1..250
FT /note="Nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..251
FT /note="Interaction with RB1"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT REGION 251..618
FT /note="Interaction with NEK2 and ZWINT"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT REGION 251..431
FT /note="Interaction with SMC1A"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT REGION 361..547
FT /note="Interaction with PSMC2 and SMC1A"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT REGION 446..642
FT /note="Interaction with the C-terminus of CDCA1 and the
FT SPBC24-SPBC25 subcomplex"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT COILED 261..403
FT /evidence="ECO:0000255"
FT COILED 458..639
FT /evidence="ECO:0000255"
FT COMPBIAS 1..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 165
FT /note="Phosphoserine; by NEK2"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0F1"
FT MOD_RES 527
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
SQ SEQUENCE 642 AA; 73868 MW; 7E011AC48A9A5520 CRC64;
MKRSSVSTGG AGRLSMQELR SQDVNKQGLY TPQTKERPTF 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 EINKARNKKM
GLEDTLEQLN AMITESKRSV RTLKEEVQKL DDLYQQKIKE AEEEDEKCAS ELESLEKHKH
LLESTVNQGL SEAMNELDAV QREYQLVVQT TTEERRKVGN NLQRLLEMVA THVGSVEKHL
EEQIAKADRE YEECMSEDLS ENIKEIRDKY EKKAALIKSS GE
