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MARE1_CHICK
ID   MARE1_CHICK             Reviewed;         258 AA.
AC   Q5ZLC7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Microtubule-associated protein RP/EB family member 1;
GN   Name=MAPRE1; ORFNames=RCJMB04_6l6;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Plus-end tracking protein (+TIP) that binds to the plus-end
CC       of microtubules and regulates the dynamics of the microtubule
CC       cytoskeleton. Promotes cytoplasmic microtubule nucleation and
CC       elongation. Involved in mitotic spindle positioning by stabilizing
CC       microtubules and promoting dynamic connection between astral
CC       microtubules and the cortex during mitotic chromosome segregation.
CC       {ECO:0000250|UniProtKB:Q15691}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q15691}. Golgi
CC       apparatus {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton,
CC       spindle {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton,
CC       spindle pole {ECO:0000250|UniProtKB:Q15691}.
CC   -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
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DR   EMBL; AJ719807; CAG31466.1; -; mRNA.
DR   RefSeq; NP_001026031.1; NM_001030860.1.
DR   AlphaFoldDB; Q5ZLC7; -.
DR   BMRB; Q5ZLC7; -.
DR   SMR; Q5ZLC7; -.
DR   STRING; 9031.ENSGALP00000010754; -.
DR   PaxDb; Q5ZLC7; -.
DR   GeneID; 419288; -.
DR   KEGG; gga:419288; -.
DR   CTD; 22919; -.
DR   VEuPathDB; HostDB:geneid_419288; -.
DR   eggNOG; KOG3000; Eukaryota.
DR   HOGENOM; CLU_041744_1_1_1; -.
DR   InParanoid; Q5ZLC7; -.
DR   PhylomeDB; Q5ZLC7; -.
DR   TreeFam; TF313620; -.
DR   PRO; PR:Q5ZLC7; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0031253; C:cell projection membrane; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR   GO; GO:0030981; C:cortical microtubule cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR   GO; GO:1905721; C:mitotic spindle astral microtubule end; IEA:Ensembl.
DR   GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR   GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR   GO; GO:0001578; P:microtubule bundle formation; IEA:Ensembl.
DR   GO; GO:0046785; P:microtubule polymerization; IEA:Ensembl.
DR   GO; GO:0031115; P:negative regulation of microtubule polymerization; ISS:UniProtKB.
DR   GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
DR   GO; GO:1903033; P:positive regulation of microtubule plus-end binding; IEA:Ensembl.
DR   GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:Ensembl.
DR   GO; GO:1902888; P:protein localization to astral microtubule; ISS:UniProtKB.
DR   GO; GO:0071539; P:protein localization to centrosome; IEA:Ensembl.
DR   GO; GO:0035372; P:protein localization to microtubule; ISS:UniProtKB.
DR   GO; GO:1904825; P:protein localization to microtubule plus-end; IBA:GO_Central.
DR   GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR   GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR   Gene3D; 1.10.418.10; -; 1.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR004953; EB1_C.
DR   InterPro; IPR036133; EB1_C_sf.
DR   InterPro; IPR027739; EB1_Meta.
DR   InterPro; IPR027328; MAPRE.
DR   PANTHER; PTHR10623; PTHR10623; 1.
DR   PANTHER; PTHR10623:SF20; PTHR10623:SF20; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF03271; EB1; 1.
DR   SUPFAM; SSF140612; SSF140612; 1.
DR   SUPFAM; SSF47576; SSF47576; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51230; EB1_C; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW   Microtubule; Mitosis; Reference proteome.
FT   CHAIN           1..258
FT                   /note="Microtubule-associated protein RP/EB family member
FT                   1"
FT                   /id="PRO_0000213421"
FT   DOMAIN          14..116
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          175..245
FT                   /note="EB1 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
SQ   SEQUENCE   258 AA;  29143 MW;  752FEB40D1033F52 CRC64;
     MAVNVYSTSV TSDNLSRHDM LAWINESLQL TLTKIEQLCS GAAYCQFMDM LFPGSVALKK
     VKFQAKLEHE YIQNFKVLQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD
     GKEYDPVAAR QGQETVAPNL VAPVVNKPKK PLAPQRPIVA QRTPATPKGS TGMVKKAAGD
     DESAGLIEQI NVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ RIVEILYATD
     EGFVIPDEGA PQEEQEEY
 
 
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