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SKA1_BOVIN
ID   SKA1_BOVIN              Reviewed;         254 AA.
AC   Q0V7M7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Spindle and kinetochore-associated protein 1;
GN   Name=SKA1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 77-254 (ISOFORM 1).
RC   TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the SKA1 complex, a microtubule-binding
CC       subcomplex of the outer kinetochore that is essential for proper
CC       chromosome segregation. Required for timely anaphase onset during
CC       mitosis, when chromosomes undergo bipolar attachment on spindle
CC       microtubules leading to silencing of the spindle checkpoint. The SKA1
CC       complex is a direct component of the kinetochore-microtubule interface
CC       and directly associates with microtubules as oligomeric assemblies. The
CC       complex facilitates the processive movement of microspheres along a
CC       microtubule in a depolymerization-coupled manner. Affinity for
CC       microtubules is synergistically enhanced in the presence of the ndc-80
CC       complex and may allow the ndc-80 complex to track depolymerizing
CC       microtubules. In the complex, it mediates the interaction with
CC       microtubules. {ECO:0000250|UniProtKB:Q96BD8}.
CC   -!- SUBUNIT: Component of the SKA1 complex, composed of SKA1, SKA2 and
CC       SKA3. Forms a heterodimer with SKA2; the heterodimer interacting with
CC       SKA3. The core SKA1 complex is composed of 2 SKA1-SKA2 heterodimers,
CC       each heterodimer interacting with a molecule of the SKA3 homodimer. The
CC       core SKA1 complex associates with microtubules and forms oligomeric
CC       assemblies. Interacts with microtubules; the interaction is direct.
CC       Interacts with SKA2. Interacts with SKA3.
CC       {ECO:0000250|UniProtKB:Q96BD8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:Q96BD8}. Chromosome, centromere, kinetochore
CC       {ECO:0000250|UniProtKB:Q96BD8}. Note=Localizes to the outer kinetochore
CC       and spindle microtubules during mitosis in a NDC80 complex-dependent
CC       manner. Localizes to both the mitotic spindle and kinetochore-
CC       associated proteins. Associates with kinetochores following microtubule
CC       attachment from prometaphase, through mid-anaphase and then vanishes in
CC       telophase. {ECO:0000250|UniProtKB:Q96BD8}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q0V7M7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0V7M7-2; Sequence=VSP_037277;
CC   -!- SIMILARITY: Belongs to the SKA1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABH06330.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BT026543; ABH06330.1; ALT_FRAME; mRNA.
DR   EMBL; EH156388; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001068795.2; NM_001075327.2.
DR   AlphaFoldDB; Q0V7M7; -.
DR   SMR; Q0V7M7; -.
DR   STRING; 9913.ENSBTAP00000024245; -.
DR   PaxDb; Q0V7M7; -.
DR   PRIDE; Q0V7M7; -.
DR   GeneID; 507703; -.
DR   KEGG; bta:507703; -.
DR   CTD; 220134; -.
DR   eggNOG; KOG4832; Eukaryota.
DR   InParanoid; Q0V7M7; -.
DR   OrthoDB; 1354933at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:0000940; C:outer kinetochore; ISS:UniProtKB.
DR   GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR   GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISS:UniProtKB.
DR   Gene3D; 1.10.10.1890; -; 1.
DR   InterPro; IPR009829; SKA1.
DR   InterPro; IPR042031; SKA1-MBD.
DR   PANTHER; PTHR28573; PTHR28573; 1.
DR   Pfam; PF07160; SKA1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis;
KW   Reference proteome.
FT   CHAIN           1..254
FT                   /note="Spindle and kinetochore-associated protein 1"
FT                   /id="PRO_0000373886"
FT   REGION          105..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..254
FT                   /note="Microtubule binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BD8"
FT   COILED          49..90
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        111..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         207..254
FT                   /note="HYFVVEADIKEFTTLKVDKRFHGILNILRHCRRLSEVRGKGLTRYVIT ->
FT                   KMRVYVCVCMSNESICVCVHVK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16305752"
FT                   /id="VSP_037277"
SQ   SEQUENCE   254 AA;  29412 MW;  005F72AA891B4AC4 CRC64;
     MASDLEQLCA HINEKIGNIK RTLSLRNCGQ EPTLKTILNK IGDEIIVVNE LLNKLELEIQ
     YQEQTNSSLK ELFESLEEDY KDVEHLKENI PPHLPQVTVT QNFVNGSDLD PEEPVKVEEP
     APTKKPPKEQ RSIKEMPFIT SDEFNGIPAY MKSRLTYCHI NDVIKEINKA VVSKYKILHQ
     PKKSMSSVAR NLYHRFIDEE TKETKGHYFV VEADIKEFTT LKVDKRFHGI LNILRHCRRL
     SEVRGKGLTR YVIT
 
 
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