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SKA1_MOUSE
ID   SKA1_MOUSE              Reviewed;         254 AA.
AC   Q9CPV1; Q005W7; Q8VE34; Q9CYW9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Spindle and kinetochore-associated protein 1;
GN   Name=Ska1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1;
RA   Chatterjee B., Richard K., Bucan M., Lo C.;
RT   "Deletion in chromosome 18 is associated with no turning mutation.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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: 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   -!- SIMILARITY: Belongs to the SKA1 family. {ECO:0000305}.
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DR   EMBL; DQ926863; ABJ15826.1; -; mRNA.
DR   EMBL; DQ926864; ABJ15827.1; -; mRNA.
DR   EMBL; AK006442; BAB24591.1; -; mRNA.
DR   EMBL; AK013233; BAB28731.1; -; mRNA.
DR   EMBL; AK021226; BAB32336.1; -; mRNA.
DR   EMBL; AK172500; BAE43036.1; -; mRNA.
DR   EMBL; BC019940; AAH19940.1; -; mRNA.
DR   CCDS; CCDS29341.1; -.
DR   RefSeq; NP_001157827.1; NM_001164355.1.
DR   RefSeq; NP_079857.3; NM_025581.4.
DR   AlphaFoldDB; Q9CPV1; -.
DR   SMR; Q9CPV1; -.
DR   BioGRID; 211496; 8.
DR   ComplexPortal; CPX-5700; Kinetochore SKA complex.
DR   IntAct; Q9CPV1; 5.
DR   STRING; 10090.ENSMUSP00000049156; -.
DR   PhosphoSitePlus; Q9CPV1; -.
DR   EPD; Q9CPV1; -.
DR   MaxQB; Q9CPV1; -.
DR   PaxDb; Q9CPV1; -.
DR   PeptideAtlas; Q9CPV1; -.
DR   PRIDE; Q9CPV1; -.
DR   ProteomicsDB; 257187; -.
DR   DNASU; 66468; -.
DR   GeneID; 66468; -.
DR   KEGG; mmu:66468; -.
DR   UCSC; uc008fpe.2; mouse.
DR   CTD; 220134; -.
DR   MGI; MGI:1913718; Ska1.
DR   eggNOG; KOG4832; Eukaryota.
DR   InParanoid; Q9CPV1; -.
DR   OrthoDB; 1354933at2759; -.
DR   PhylomeDB; Q9CPV1; -.
DR   TreeFam; TF324442; -.
DR   Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-MMU-68877; Mitotic Prometaphase.
DR   Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR   BioGRID-ORCS; 66468; 19 hits in 73 CRISPR screens.
DR   ChiTaRS; Ska1; mouse.
DR   PRO; PR:Q9CPV1; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9CPV1; protein.
DR   GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR   GO; GO:0000776; C:kinetochore; ISO:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
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   Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Kinetochore; Microtubule; Mitosis; Reference proteome.
FT   CHAIN           1..254
FT                   /note="Spindle and kinetochore-associated protein 1"
FT                   /id="PRO_0000273156"
FT   REGION          89..129
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          56..90
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        106..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        7
FT                   /note="D -> E (in Ref. 1; ABJ15827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        27
FT                   /note="N -> D (in Ref. 2; BAB28731)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="V -> I (in Ref. 2; BAB24591/BAB28731/BAB32336)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   254 AA;  29445 MW;  E1123577C1D0753A CRC64;
     MDSELEDLCS YVNEKIGNIK KILSIRNLGQ DPALKTTLSK IGDEIIAVNE LLNKFELEIQ
     YQEQTNSSLK ELCESLREEC EDVEHLKEHV PPHLPQVTAT QSLVHKPEPD PKESDKAEEP
     GLPKKPPREQ RVIKEMQFIT MDEFSDVPAY MKSRLTYCQI NDIIKEINKA VVSKYKIMHQ
     PKASMSSVKR NLYQRFINEE TKDTKGHHFI VEADIKEFTA LKVDKRFYVI MHILRHCHRL
     SEVRGGGLTR YVIT
 
 
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