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EB1_DICDI
ID   EB1_DICDI               Reviewed;         506 AA.
AC   Q8WQ86; Q54QT3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Microtubule-associated protein RP/EB family member 1;
DE            Short=DdEB1;
GN   Name=eb1; ORFNames=DDB_G0283607;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=AX2;
RX   PubMed=12134070; DOI=10.1091/mbc.e02-01-0054;
RA   Rehberg M., Graef R.;
RT   "Dictyostelium EB1 is a genuine centrosomal component required for proper
RT   spindle formation.";
RL   Mol. Biol. Cell 13:2301-2310(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16782229; DOI=10.1016/j.ejcb.2006.05.008;
RA   Koch K.V., Reinders Y., Ho T.-H., Sickmann A., Graef R.;
RT   "Identification and isolation of Dictyostelium microtubule-associated
RT   protein interactors by tandem affinity purification.";
RL   Eur. J. Cell Biol. 85:1079-1090(2006).
CC   -!- FUNCTION: Involved in microtubule polymerization, and spindle function
CC       by stabilizing microtubules and anchoring them at centrosomes.
CC   -!- SUBUNIT: Interacts with mtaA/CP224 at the microtubule tip, centrosome
CC       and kinetochore. {ECO:0000269|PubMed:12134070}.
CC   -!- SUBCELLULAR LOCATION: Cell projection {ECO:0000269|PubMed:12134070}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:12134070}. Cytoplasm {ECO:0000269|PubMed:12134070}.
CC       Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12134070}.
CC       Note=Associated with the microtubule network. Accumulates at the plus
CC       end of microtubules.
CC   -!- DISRUPTION PHENOTYPE: Defects in cytokinesis due to poor mitotic
CC       spindle assembly during mitotic prometaphase.
CC       {ECO:0000269|PubMed:12134070}.
CC   -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
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DR   EMBL; AJ426053; CAD19801.1; -; mRNA.
DR   EMBL; AAFI02000056; EAL65570.1; -; Genomic_DNA.
DR   RefSeq; XP_638940.1; XM_633848.1.
DR   AlphaFoldDB; Q8WQ86; -.
DR   SMR; Q8WQ86; -.
DR   STRING; 44689.DDB0191160; -.
DR   PaxDb; Q8WQ86; -.
DR   PRIDE; Q8WQ86; -.
DR   EnsemblProtists; EAL65570; EAL65570; DDB_G0283607.
DR   GeneID; 8624179; -.
DR   KEGG; ddi:DDB_G0283607; -.
DR   dictyBase; DDB_G0283607; eb1.
DR   eggNOG; KOG3000; Eukaryota.
DR   HOGENOM; CLU_539100_0_0_1; -.
DR   InParanoid; Q8WQ86; -.
DR   OMA; FNAKYDY; -.
DR   PRO; PR:Q8WQ86; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0000235; C:astral microtubule; IDA:dictyBase.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0031592; C:centrosomal corona; IDA:dictyBase.
DR   GO; GO:0005813; C:centrosome; IDA:dictyBase.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; IDA:dictyBase.
DR   GO; GO:0005874; C:microtubule; IDA:dictyBase.
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:0005819; C:spindle; IDA:dictyBase.
DR   GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR   GO; GO:0000922; C:spindle pole; IDA:dictyBase.
DR   GO; GO:0070840; F:dynein complex binding; IDA:dictyBase.
DR   GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR   GO; GO:0008017; F:microtubule binding; IMP:dictyBase.
DR   GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR   GO; GO:0008104; P:protein localization; IMP:dictyBase.
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; IMP:dictyBase.
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; IPR027328; MAPRE.
DR   PANTHER; PTHR10623; PTHR10623; 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   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell projection; Centromere; Chromosome;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis;
KW   Reference proteome.
FT   CHAIN           1..506
FT                   /note="Microtubule-associated protein RP/EB family member
FT                   1"
FT                   /id="PRO_0000328617"
FT   DOMAIN          3..105
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          303..371
FT                   /note="EB1 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT   REGION          127..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          283..344
FT                   /evidence="ECO:0000255"
FT   COILED          377..459
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        138..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..408
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..425
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..462
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..506
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  56983 MW;  F20BC182BAAA639C CRC64;
     MEGFGRNEIL NWINDLLQLD YKKIEQLGSG AALCQLVDII HPGKINLKMV NFNAKYDYEY
     IKNFSYLQES FAKLGVEKYV EVSELVKSRP QANLEFAQWM KKYFDQYYTG EPYNAIERRI
     ALKIPTDKDR SSLKGKTAAT GAPPTSKPSP SSTLKPATTA ASKPAPVSKP TTTTAKPTPS
     SVSKPVSKPT PSSISKPVSK PTPSISKPVT KPTPTTTSTS TTTTVSTPPS TPKPTNTPIP
     STTGKPTLTQ PTFKPTPKSV SPTPPVVAGS TVTTKTVIVS EPPTELLEEL EQQKRELEQQ
     RKELEEQKSV IQEMTEKIAN FEITIQDIEK DRDFYFERLR EAEIFCQDHS DVPLLGEVLK
     ILYNSNGEEE GEEGEGEEQG GEEEEEEEEQ GENNIEQEEE EQIEQQQQQQ EEEEEHERET
     LSEPEPDQDN SAIPLEQLEI NDEEEEFNQH QEQEEEDEHF EDEEKVNGLN EEEIMNSVLQ
     NASDEDDILE STFDGNEDDS LLQDEY
 
 
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