MARE1_RAT
ID MARE1_RAT Reviewed; 268 AA.
AC Q66HR2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Microtubule-associated protein RP/EB family member 1;
DE AltName: Full=APC-binding protein EB1;
DE AltName: Full=End-binding protein 1;
DE Short=EB1;
GN Name=Mapre1;
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=Heart;
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).
RN [2]
RP PROTEIN SEQUENCE OF 2-17; 67-98; 113-150; 182-201 AND 205-214, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Pheochromocytoma;
RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
RL Submitted (AUG-2006) to UniProtKB.
RN [3]
RP LACK OF INTERACTION WITH MAPRE1.
RX PubMed=19553473; DOI=10.1091/mbc.e09-01-0009;
RA Fong K.W., Hau S.Y., Kho Y.S., Jia Y., He L., Qi R.Z.;
RT "Interaction of CDK5RAP2 with EB1 to track growing microtubule tips and to
RT regulate microtubule dynamics.";
RL Mol. Biol. Cell 20:3660-3670(2009).
RN [4]
RP INTERACTION WITH KCNAB2.
RX PubMed=21357749; DOI=10.1083/jcb.201007113;
RA Vacher H., Yang J.W., Cerda O., Autillo-Touati A., Dargent B.,
RA Trimmer J.S.;
RT "Cdk-mediated phosphorylation of the Kvbeta2 auxiliary subunit regulates
RT Kv1 channel axonal targeting.";
RL J. Cell Biol. 192:813-824(2011).
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. Also
CC acts as a regulator of minus-end microtubule organization: interacts
CC with the complex formed by AKAP9 and PDE4DIP, leading to recruit
CC CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal
CC minus-end microtubules to the Golgi, an important step for polarized
CC cell movement. Promotes elongation of CAMSAP2-decorated microtubule
CC stretches on the minus-end of microtubules. Acts as a regulator of
CC autophagosome transport via interaction with CAMSAP2 (By similarity).
CC May play a role in cell migration (By similarity).
CC {ECO:0000250|UniProtKB:Q15691, ECO:0000250|UniProtKB:Q61166}.
CC -!- SUBUNIT: Homodimer. Heterodimer with MAPRE3. Interacts with DCTN1,
CC DCTN2, TERF1 and dynein intermediate chain (By similarity). Interaction
CC with DIAPH1 and DIAPH2 (By similarity). Interacts with APC (via C-
CC terminal domain), CLASP2, DST, KIF2C and STIM1; probably required for
CC their targeting to the growing microtubule plus ends. Interacts with
CC MTUS2; interaction is direct and probably targets MTUS2 to
CC microtubules. Interacts with APC2. Interacts with CLASP1. Interacts
CC with CDK5RAP2 (By similarity). According to another report, MAPRE1 does
CC not interact with CDK5RAP2 (PubMed:19553473). Interacts with MACF1 (By
CC similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-
CC bound RABL2 (By similarity). Interacts with KCNAB2 (PubMed:21357749).
CC Interacts (via C-terminus) with CLIP1. Interacts with SLAIN2 and
CC SLAIN1. Interacts with KIF18B; this interaction is required for
CC efficient accumulation of KIF18B at microtubule plus ends. Interacts
CC with MISP. Interacts with KNSTRN. Interacts with NCKAP5L. Interacts
CC with AKAP9. Interacts with PDE4DIP; this interaction, which is PDE4DIP
CC isoform-specific, is required for its recruitment to the Golgi
CC apparatus. Interacts with CAMSAP2 (By similarity). May form a
CC pericentrosomal complex with AKAP9, CDK5RAP2 and PDE4DIP isoform
CC 2/MMG8/SMYLE; within this complex, MAPRE1 binding to CDK5RAP2 may be
CC mediated by PDE4DIP (By similarity). Contrary to other mammalian
CC species, does not interact with CDK5RAP2, possibly due to the lack of
CC conservation of the MAPRE1-binding motif in rat CDK5RAP2 (Probable).
CC Interacts with AKNA (By similarity). Interacts with GAS2L1, GAS2L2, and
CC GAS2L3 (By similarity). Interacts with RARRES1 and AGBL2 (By
CC similarity). {ECO:0000250|UniProtKB:Q15691,
CC ECO:0000250|UniProtKB:Q61166, ECO:0000269|PubMed:19553473,
CC ECO:0000269|PubMed:21357749, ECO:0000305|PubMed:19553473}.
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}. Note=Associated with the
CC microtubule growing distal tips. Recruitment to the Golgi apparatus
CC requires the presence of PDE4DIP isoform 13/MMG8/SMYLE.
CC {ECO:0000250|UniProtKB:Q15691}.
CC -!- DOMAIN: Composed of two functionally independent domains. The N-
CC terminal domain forms a hydrophobic cleft involved in microtubule
CC binding and the C-terminal is involved in the formation of mutually
CC exclusive complexes with APC and DCTN1. {ECO:0000250|UniProtKB:Q15691}.
CC -!- PTM: Acetylation at Lys-220 by KAT2B/PCAF promotes dynamic kinetochore-
CC microtubule interactions in early mitosis.
CC {ECO:0000250|UniProtKB:Q15691}.
CC -!- PTM: Crotonylated by KAT5 during mitosis, promoting astral microtubule
CC plasticity and dynamic connection between astral microtubules and the
CC cortex during mitotic chromosome segregation, thereby ensuring accurate
CC spindle positioning in mitosis. Decrotonylated by HDAC3.
CC {ECO:0000250|UniProtKB:Q15691}.
CC -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
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DR EMBL; BC081726; AAH81726.1; -; mRNA.
DR RefSeq; NP_612518.2; NM_138509.3.
DR RefSeq; XP_006235356.1; XM_006235294.3.
DR RefSeq; XP_006235357.1; XM_006235295.3.
DR AlphaFoldDB; Q66HR2; -.
DR BMRB; Q66HR2; -.
DR SMR; Q66HR2; -.
DR BioGRID; 250409; 1.
DR IntAct; Q66HR2; 1.
DR MINT; Q66HR2; -.
DR STRING; 10116.ENSRNOP00000016220; -.
DR iPTMnet; Q66HR2; -.
DR PhosphoSitePlus; Q66HR2; -.
DR jPOST; Q66HR2; -.
DR PaxDb; Q66HR2; -.
DR PRIDE; Q66HR2; -.
DR GeneID; 114764; -.
DR KEGG; rno:114764; -.
DR UCSC; RGD:621781; rat.
DR CTD; 22919; -.
DR RGD; 621781; Mapre1.
DR VEuPathDB; HostDB:ENSRNOG00000011798; -.
DR eggNOG; KOG3000; Eukaryota.
DR HOGENOM; CLU_041744_1_1_1; -.
DR InParanoid; Q66HR2; -.
DR OMA; ICQEKES; -.
DR OrthoDB; 1237523at2759; -.
DR PhylomeDB; Q66HR2; -.
DR TreeFam; TF313620; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q66HR2; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000011798; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; Q66HR2; baseline and differential.
DR Genevisible; Q66HR2; RN.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0031253; C:cell projection membrane; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0030981; C:cortical microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; ISO:RGD.
DR GO; GO:1905721; C:mitotic spindle astral microtubule end; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISO:RGD.
DR GO; GO:0046785; P:microtubule polymerization; ISO:RGD.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISO:RGD.
DR GO; GO:1905515; P:non-motile cilium assembly; ISO:RGD.
DR GO; GO:1903033; P:positive regulation of microtubule plus-end binding; ISO:RGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:RGD.
DR GO; GO:1902888; P:protein localization to astral microtubule; ISS:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Golgi apparatus; Microtubule; Mitosis;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..268
FT /note="Microtubule-associated protein RP/EB family member
FT 1"
FT /id="PRO_0000213419"
FT DOMAIN 14..116
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 185..255
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 124..268
FT /note="Interaction with MTUS2/TIP150"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT REGION 146..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..268
FT /note="DCTN1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT REGION 220..242
FT /note="APC-binding"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.2"
FT MOD_RES 66
FT /note="N6-crotonyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT MOD_RES 124
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT MOD_RES 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
SQ SEQUENCE 268 AA; 30004 MW; CEDE13116FC79F93 CRC64;
MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GAAYCQFMDM LFPGSIALKK
VKFQAKLEHE YIQNFKILQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD
GKEYDPVAAR QGQETAVAPS LVAPALSKPK KPLGSGSAAP QRPIATQRTT AAPKAGPGMV
RKNPGMGNGD DEAAELMQQV KVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ
RIVDILYATD EGFVIPDEGG PQEEQEEY
