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SPDLY_XENTR
ID   SPDLY_XENTR             Reviewed;         611 AA.
AC   B3DLE8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Protein Spindly {ECO:0000255|HAMAP-Rule:MF_03041};
DE   AltName: Full=Coiled-coil domain-containing protein 99 {ECO:0000255|HAMAP-Rule:MF_03041};
DE   AltName: Full=Spindle apparatus coiled-coil domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03041};
GN   Name=spdl1; Synonyms=ccdc99;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the localization of dynein and dynactin to the
CC       mitotic kintochore. Dynein is believed to control the initial lateral
CC       interaction between the kinetochore and spindle microtubules and to
CC       facilitate the subsequent formation of end-on kinetochore-microtubule
CC       attachments mediated by the NDC80 complex. May act as an adapter
CC       protein linking the dynein motor complex to various cargos (By
CC       similarity). {ECO:0000250|UniProtKB:Q96EA4, ECO:0000255|HAMAP-
CC       Rule:MF_03041}.
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC       {ECO:0000255|HAMAP-Rule:MF_03041}.
CC   -!- SIMILARITY: Belongs to the Spindly family. {ECO:0000255|HAMAP-
CC       Rule:MF_03041}.
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DR   EMBL; BC167418; AAI67418.1; -; mRNA.
DR   RefSeq; NP_001123745.1; NM_001130273.1.
DR   AlphaFoldDB; B3DLE8; -.
DR   SMR; B3DLE8; -.
DR   STRING; 8364.ENSXETP00000043089; -.
DR   PaxDb; B3DLE8; -.
DR   GeneID; 100170491; -.
DR   KEGG; xtr:100170491; -.
DR   CTD; 54908; -.
DR   Xenbase; XB-GENE-5754925; spdl1.
DR   eggNOG; ENOG502S27G; Eukaryota.
DR   InParanoid; B3DLE8; -.
DR   OrthoDB; 1595638at2759; -.
DR   Reactome; R-XTR-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-XTR-2467813; Separation of Sister Chromatids.
DR   Reactome; R-XTR-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-XTR-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-XTR-9648025; EML4 and NUDC in mitotic spindle formation.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000940; C:outer kinetochore; ISS:UniProtKB.
DR   GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR   GO; GO:0043515; F:kinetochore binding; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR   GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR   GO; GO:0034501; P:protein localization to kinetochore; ISS:UniProtKB.
DR   HAMAP; MF_03041; SPDLY; 1.
DR   InterPro; IPR028593; SPDLY_chordates.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Coiled coil;
KW   Kinetochore; Mitosis; Reference proteome.
FT   CHAIN           1..611
FT                   /note="Protein Spindly"
FT                   /id="PRO_0000383345"
FT   REGION          499..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..288
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03041"
FT   COMPBIAS        525..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..592
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  70708 MW;  AC1318511998B376 CRC64;
     MEESETVLKL RLQLKEAEEE RIKAAQYGLE LLESQSDLQN QLEEQRNEMT STIENLEQEK
     YSLQREVELK NRMLESLTSE CENIRQQQKL CLEQLQEQLE RNHHRELSEI KDKLEKLKAE
     LDEARLSEKQ LKHKLEYQSE VLANKSEELR MMSERVHETM SSEMLTLQLE KTELESAKAN
     LEQEVNELQY REQQLLLTNG TQSRQLERLQ DEKEDREKEA VGYFKALEKA REANQDLQAQ
     LDIALQQAQD PNSKGNSLFA EVEDRRAEME RQLISMKVQF QSLQKQHAFS RQQMHRMKVQ
     IATLLQLKGS QSDPEQLERL QAMVAQKNSE FETLVMKVRQ LEKSQQICEN GPVANSSDGL
     GQGDETYYVD LLKMKLVNSS KEIEKIKDEL SLQRMKALAE SQRVLDLERK LFANDRHLKL
     SQGENMKLRV NLDEMKMKYE PDEIAKIRTQ KRRKEQLPLD CAIDNTSATV TSGSQAHGLS
     DAIPEDMCPA ESTVHRNLLK EDSSLSTKEQ DLSSVAVKPI EPANGQPPKE RKRVRIVENE
     NDNQDINKRN TNNCSVTSTS PRSASEESTS ESKRFDEEQE KRKQERKSRL RAPPVLHVPS
     KPAATTQCPQ Q
 
 
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