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NUF2_RAT
ID   NUF2_RAT                Reviewed;         464 AA.
AC   Q6AYL9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Kinetochore protein Nuf2;
DE   AltName: Full=Cell division cycle-associated protein 1;
GN   Name=Nuf2; Synonyms=Cdca1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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.
CC       {ECO:0000250|UniProtKB:Q9BZD4}.
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. May interact with AURKB/Aurora-B (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere,
CC       kinetochore {ECO:0000250}. Note=Localizes to kinetochores from late
CC       prophase to anaphase. Localizes specifically to the outer plate of the
CC       kinetochore (By similarity). {ECO:0000250}.
CC   -!- PTM: Can be phosphorylated by AURKA and AURKB. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NUF2 family. {ECO:0000305}.
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DR   EMBL; BC078993; AAH78993.1; -; mRNA.
DR   RefSeq; NP_001012028.1; NM_001012028.1.
DR   AlphaFoldDB; Q6AYL9; -.
DR   SMR; Q6AYL9; -.
DR   STRING; 10116.ENSRNOP00000003650; -.
DR   PaxDb; Q6AYL9; -.
DR   Ensembl; ENSRNOT00000003650; ENSRNOP00000003650; ENSRNOG00000002711.
DR   GeneID; 304951; -.
DR   KEGG; rno:304951; -.
DR   UCSC; RGD:1307952; rat.
DR   CTD; 83540; -.
DR   RGD; 1307952; Nuf2.
DR   eggNOG; KOG4438; Eukaryota.
DR   GeneTree; ENSGT00390000004199; -.
DR   HOGENOM; CLU_589957_0_0_1; -.
DR   InParanoid; Q6AYL9; -.
DR   OMA; AHIKLYI; -.
DR   OrthoDB; 752521at2759; -.
DR   PhylomeDB; Q6AYL9; -.
DR   TreeFam; TF101067; -.
DR   Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR   Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-RNO-68877; Mitotic Prometaphase.
DR   Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR   PRO; PR:Q6AYL9; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000002711; Expressed in thymus and 19 other tissues.
DR   Genevisible; Q6AYL9; RN.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0031262; C:Ndc80 complex; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR   GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IBA:GO_Central.
DR   GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISO:RGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051383; P:kinetochore organization; IBA:GO_Central.
DR   GO; GO:0045132; P:meiotic chromosome segregation; IBA:GO_Central.
DR   GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR   Gene3D; 1.10.418.60; -; 1.
DR   InterPro; IPR005549; Kinetochore_Nuf2_N.
DR   InterPro; IPR038275; Nuf2_N_sf.
DR   Pfam; PF03800; Nuf2; 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..464
FT                   /note="Kinetochore protein Nuf2"
FT                   /id="PRO_0000249815"
FT   REGION          1..385
FT                   /note="Interaction with the N-terminus of NDC80"
FT                   /evidence="ECO:0000250"
FT   REGION          386..464
FT                   /note="Interaction with the C-terminus of NDC80 and the
FT                   SPBC24-SPBC25 subcomplex"
FT                   /evidence="ECO:0000250"
FT   COILED          148..201
FT                   /evidence="ECO:0000255"
FT   COILED          249..372
FT                   /evidence="ECO:0000255"
FT   COILED          413..443
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZD4"
FT   MOD_RES         171
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZD4"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZD4"
SQ   SEQUENCE   464 AA;  54556 MW;  5C0BFD08BB492DC4 CRC64;
     METLSFPRYN IAEIVVHIRN KLLTGADGKN LSKSDFLPNP KPEVLYMIYM RALQLVYGVR
     LEHFYMMPVN IEVMYPHIME GFLPVSNLFF HLDSFMPICR VNDFEIADIL YPKANRTSRF
     LSGIINFIHF RETCLEKYEE FLLQNKSSVD KIQQLSNAHQ EALMKLEKLN SVPVEEQEEF
     KQLKDDIQEL QHLLNQDFRQ KTTLLQERYT KMKSDFSEKT KHVNELKLSV VSLKEVQDSL
     KSKIVDSPEK LKNYKEKMKD TVQKLRSARE EVMEKYDIYR DSVDCLPSCQ LEVQLYQKKS
     QDLADNREKL SSILKESLNL EGQIDSDSSE LKKLKTEENS LIRLMTLKKE RLATMQFKIN
     KKQEDVKQYK RTMIEDCNKV QEKRDAVCEQ VTAINQDIHK IKSGIQQLRD AEKREKLKSQ
     EILVDLKSAL EKYHEGIEKT TEECCTRIGG KTAELKRRMF KMPP
 
 
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