SKAP_RAT
ID SKAP_RAT Reviewed; 312 AA.
AC Q6AXN6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Small kinetochore-associated protein;
DE Short=SKAP;
DE AltName: Full=Kinetochore-localized astrin-binding protein;
DE Short=Kinastrin;
DE AltName: Full=Kinetochore-localized astrin/SPAG5-binding protein;
DE AltName: Full=TRAF4-associated factor 1;
GN Name=Knstrn; Synonyms=Skap, Traf4af1;
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: Essential component of the mitotic spindle required for
CC faithful chromosome segregation and progression into anaphase. Promotes
CC the metaphase-to-anaphase transition and is required for chromosome
CC alignment, normal timing of sister chromatid segregation, and
CC maintenance of spindle pole architecture. The astrin (SPAG5)-kinastrin
CC (SKAP) complex promotes stable microtubule-kinetochore attachments.
CC Required for kinetochore oscillations and dynamics of microtubule plus-
CC ends during live cell mitosis, possibly by forming a link between
CC spindle microtubule plus-ends and mitotic chromosomes to achieve
CC faithful cell division. {ECO:0000250|UniProtKB:Q9Y448}.
CC -!- SUBUNIT: Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing
CC KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2 (By similarity). Interacts with
CC SPAG5 (By similarity). Directly binds to microtubules, although at
CC relatively low affinity (By similarity). Interacts with CENPE; this
CC interaction greatly favors microtubule-binding (By similarity).
CC Interacts with DSN1/MIS13; leading to localization to kinetochores (By
CC similarity). Interacts with MAPRE1/EB1; leading to localization to the
CC microtubule plus ends (By similarity). Interacts with PRPF19 (By
CC similarity). Interacts with DYNLL1 (By similarity). Interacts with MAP4
CC (By similarity). {ECO:0000250|UniProtKB:Q9Y448}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y448}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9Y448}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9Y448}.
CC Cytoplasm, cytoskeleton, microtubule organizing center
CC {ECO:0000250|UniProtKB:Q9Y448}. Note=Colocalizes with microtubules
CC around centrosomes in prophase and with the mitotic spindle at
CC prometaphase and metaphase. From late prometaphase to anaphase, is
CC highly concentrated on kinetochores. Located at the kinetochore-
CC microtubule interface. The astrin (SPAG5)-kinastrin (SKAP) complex
CC localizes to the microtubule plus ends. {ECO:0000250|UniProtKB:Q9Y448}.
CC -!- DOMAIN: The coiled coil regions mediate binding to kinetochores.
CC {ECO:0000250|UniProtKB:Q9Y448}.
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DR EMBL; BC079438; AAH79438.1; -; mRNA.
DR RefSeq; NP_001004264.1; NM_001004264.1.
DR AlphaFoldDB; Q6AXN6; -.
DR SMR; Q6AXN6; -.
DR STRING; 10116.ENSRNOP00000012454; -.
DR iPTMnet; Q6AXN6; -.
DR PhosphoSitePlus; Q6AXN6; -.
DR PaxDb; Q6AXN6; -.
DR PRIDE; Q6AXN6; -.
DR GeneID; 311325; -.
DR KEGG; rno:311325; -.
DR UCSC; RGD:1303240; rat.
DR CTD; 90417; -.
DR RGD; 1303240; Knstrn.
DR VEuPathDB; HostDB:ENSRNOG00000009334; -.
DR eggNOG; ENOG502S60X; Eukaryota.
DR HOGENOM; CLU_076625_0_0_1; -.
DR InParanoid; Q6AXN6; -.
DR OMA; QDSCLAI; -.
DR OrthoDB; 1460326at2759; -.
DR PhylomeDB; Q6AXN6; -.
DR TreeFam; TF336302; -.
DR PRO; PR:Q6AXN6; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000009334; Expressed in testis and 16 other tissues.
DR Genevisible; Q6AXN6; RN.
DR GO; GO:0034451; C:centriolar satellite; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0051010; F:microtubule plus-end binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISO:RGD.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0007051; P:spindle organization; ISS:UniProtKB.
DR InterPro; IPR033373; SKAP.
DR PANTHER; PTHR31940; PTHR31940; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Kinetochore; Microtubule; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..312
FT /note="Small kinetochore-associated protein"
FT /id="PRO_0000274514"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..312
FT /note="Interaction with SPAG5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y448"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 169..210
FT /evidence="ECO:0000255"
FT COILED 246..288
FT /evidence="ECO:0000255"
FT COMPBIAS 71..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 34885 MW; 313382501B56AD2A CRC64;
MATHKAEAQE TDFRTTGPPT DLEQCPFPPS SRKFPFESVA ADSTEGWAVA AEHHLKRSGE
DGGWEQPASG VEPSRPTTMA SSKTVCDAQP HSMPSCGLSA DTQTRATSKL PVKSKDAEML
RHLHTGGLEP DVTKVTKPRR ENGQGKAAET ASRRNIRSSY KPLSKQKPEE DLKDKNELLE
AVNKQLHQKL TETQGELKDL TQKVELLEKF QDNCLAILES KGLNSGQETQ ESKQEPSTDP
TDSMLLLETL KDELKLFNET AKKQMEELQA LKVKLKLKEK ERIQFLEQQT LGKDEASDFT
IILEEMEQLL EM
