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CKP2L_BOVIN
ID   CKP2L_BOVIN             Reviewed;         744 AA.
AC   A5PK21; Q0V8I3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Cytoskeleton-associated protein 2-like;
DE   AltName: Full=Radial fiber and mitotic spindle protein;
DE            Short=Radmis;
GN   Name=CKAP2L;
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].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-744.
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).
CC   -!- FUNCTION: Microtubule-associated protein required for mitotic spindle
CC       formation and cell-cycle progression in neural progenitor cells.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250}. Note=Uniformly distributed along each microtubule bundle
CC       of spindles in addition to centrioles during mitosis, expression
CC       promptly diminishes at interphase. {ECO:0000250}.
CC   -!- DOMAIN: The KEN box is required for the association with the APC/C-Cdh1
CC       complex, ubiquitination and degradation. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CKAP2 family. {ECO:0000305}.
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DR   EMBL; BC142323; AAI42324.1; -; mRNA.
DR   EMBL; BT026235; ABG67074.1; -; mRNA.
DR   RefSeq; NP_001092371.1; NM_001098901.2.
DR   AlphaFoldDB; A5PK21; -.
DR   SMR; A5PK21; -.
DR   STRING; 9913.ENSBTAP00000002964; -.
DR   PaxDb; A5PK21; -.
DR   PRIDE; A5PK21; -.
DR   Ensembl; ENSBTAT00000002964; ENSBTAP00000002964; ENSBTAG00000002298.
DR   GeneID; 507498; -.
DR   KEGG; bta:507498; -.
DR   CTD; 150468; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002298; -.
DR   VGNC; VGNC:27381; CKAP2L.
DR   eggNOG; ENOG502RZUT; Eukaryota.
DR   GeneTree; ENSGT00530000063691; -.
DR   HOGENOM; CLU_022701_0_0_1; -.
DR   InParanoid; A5PK21; -.
DR   OMA; QKSTQPC; -.
DR   OrthoDB; 417608at2759; -.
DR   TreeFam; TF333003; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000002298; Expressed in semen and 97 other tissues.
DR   ExpressionAtlas; A5PK21; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   InterPro; IPR029197; CKAP2_C.
DR   Pfam; PF15297; CKAP2_C; 2.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..744
FT                   /note="Cytoskeleton-associated protein 2-like"
FT                   /id="PRO_0000324334"
FT   REGION          35..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         744
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYA6"
FT   CROSSLNK        195
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYA6"
FT   CROSSLNK        195
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYA6"
SQ   SEQUENCE   744 AA;  82608 MW;  3751BB248DBFC036 CRC64;
     MVRPGLSAAA EERQRKLQEY LAAKGKLKCQ NTKPYLKAKN NCPNPPHSKS TIGPKKDVTN
     HVALPVKTTR SINIKLQSRP ANITRSQRPK LEPPKLGKRL TSESVSSNPN GKPPGNSQQL
     RGFGSSTDGK QPRKTMGSLN VQKLKTTKQQ VTDQRTAKGT DPVDNTHVEN ESLGGCLKEM
     NKENLPQDLP NSERKPNPES WTINKPQTNQ TKSSLASTRE VLDKSSVNSA ALKEGVIKPF
     VEETQISVPP GKSQKLSRVA DLIRPGGKPP KTLPSHFVQT LNRTQATKKT VVKDIKSIKV
     NRSKYERPNE AKLQSYTVTE QKVKHSKPST HPSVLQGGCN HRHPNIKQDH KPTQACCRPQ
     TSYALQKSKA ISQRPNLTVG SFNSVIPSTP SIRANGATGN KCNNSCQQRA RTLDSKFKSA
     PPQKCFLNKT APRTQAGGPT ISGRGVPNGA QTNPCKKIAA EDRRKQLEEW RKSKGKIYKR
     PPMELKTKRK IIEEMNISFW KSMEKEEEEK KAQLELSNKI NNTLTECLQL IERGVLSNEV
     FAILSSIPEA EKFAKFWICK AKLLASKGTF DVIGLYEEAI RNGATPIQEL REVVLNILQD
     RNRTTEGMTS NSLVAETNIT SIEELAKKTE SGASCLSPKE SEQMSVTPQI TKSEQDGHPG
     IKLQIAPIPR INGMPEVQDM KLITPVRRSA RIERAVSRYP EMLQEHDLVV ASLNELLEVE
     ETECFIFRKN EALPVTLGFP VSES
 
 
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