APCL_HUMAN
ID APCL_HUMAN Reviewed; 2303 AA.
AC O95996; Q05BW4; Q9UBZ1; Q9UEM8; Q9UQJ8; Q9UQJ9; Q9Y632;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Adenomatous polyposis coli protein 2 {ECO:0000305};
DE AltName: Full=Adenomatous polyposis coli protein-like;
DE Short=APC-like;
GN Name=APC2 {ECO:0000312|HGNC:HGNC:24036}; Synonyms=APCL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CTNNB1,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9823329;
RA Nakagawa H., Murata Y., Koyama K., Fujiyama A., Miyoshi Y., Monden M.,
RA Akiyama T., Nakamura Y.;
RT "Identification of a brain-specific APC homologue, APCL, and its
RT interaction with beta-catenin.";
RL Cancer Res. 58:5176-5181(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=10551328; DOI=10.1111/j.1349-7006.1999.tb00845.x;
RA Nakagawa H., Koyama K., Monden M., Nakamura Y.;
RT "Analysis of APCL, a brain-specific adenomatous polyposis coli homologue,
RT for mutations and expression in brain tumors.";
RL Jpn. J. Cancer Res. 90:982-986(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1521 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] OF 34-86 AND 476-555 (ISOFORM 2).
RA Carr I.M., Markham A.F., Colleta P.L., Wai L., Askham J., Morrison E.,
RA Meredith D.M.;
RT "APC2 alternatively spliced cDNA sequence.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-731 (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] OF 618-2303 (ISOFORM 3), FUNCTION, INTERACTION WITH AXIN2,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Kidney;
RX PubMed=10021369; DOI=10.1016/s0960-9822(99)80024-4;
RA van Es J.H., Kirkpatrick C., van de Wetering M., Molenaar M., Miles A.,
RA Kuipers J., Destree O., Peifer M., Clevers H.;
RT "Identification of APC2, a homologue of the adenomatous polyposis coli
RT tumour suppressor.";
RL Curr. Biol. 9:105-108(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-702 (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP INTERACTION WITH TP53BP2, AND SUBCELLULAR LOCATION.
RX PubMed=10646860;
RA Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.;
RT "APCL, a central nervous system-specific homologue of adenomatous polyposis
RT coli tumor suppressor, binds to p53-binding protein 2 and translocates it
RT to the perinucleus.";
RL Cancer Res. 60:101-105(2000).
RN [8]
RP INTERACTION WITH MAPRE1 AND MAPRE3, AND SUBCELLULAR LOCATION.
RC TISSUE=Fetal brain;
RX PubMed=10644998; DOI=10.1038/sj.onc.1203308;
RA Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.;
RT "EB3, a novel member of the EB1 family preferentially expressed in the
RT central nervous system, binds to a CNS-specific APC homologue.";
RL Oncogene 19:210-216(2000).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APC, AND TISSUE
RP SPECIFICITY.
RX PubMed=11691822;
RA Jarrett C.R., Blancato J., Cao T., Bressette D.S., Cepeda M., Young P.E.,
RA King C.R., Byers S.W.;
RT "Human APC2 localization and allelic imbalance.";
RL Cancer Res. 61:7978-7984(2001).
RN [10]
RP INVOLVEMENT IN MRT74, FUNCTION, SUBCELLULAR LOCATION, AND REGION.
RX PubMed=25753423; DOI=10.1016/j.celrep.2015.02.011;
RA Almuriekhi M., Shintani T., Fahiminiya S., Fujikawa A., Kuboyama K.,
RA Takeuchi Y., Nawaz Z., Nadaf J., Kamel H., Kitam A.K., Samiha Z.,
RA Mahmoud L., Ben-Omran T., Majewski J., Noda M.;
RT "Loss-of-function mutation in APC2 causes Sotos syndrome features.";
RL Cell Rep. 10:1585-1598(2015).
RN [11]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-562 AND SER-2003.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [12] {ECO:0000305}
RP VARIANT ASN-1921.
RX PubMed=29120066; DOI=10.1111/cge.13171;
RA Mejecase C., Mohand-Said S., El Shamieh S., Antonio A., Condroyer C.,
RA Blanchard S., Letexier M., Saraiva J.P., Sahel J.A., Audo I., Zeitz C.;
RT "A novel nonsense variant in REEP6 is involved in a sporadic rod-cone
RT dystrophy case.";
RL Clin. Genet. 93:707-711(2018).
RN [13]
RP INVOLVEMENT IN CDCBM10, AND VARIANTS CDCBM10 246-SER--GLU-2303 DEL;
RP 361-GLN--GLU-2303 DEL AND 628-GLN--GLU-2303 DEL.
RX PubMed=31585108; DOI=10.1016/j.ajhg.2019.08.013;
RA Lee S., Chen D.Y., Zaki M.S., Maroofian R., Houlden H., Di Donato N.,
RA Abdin D., Morsy H., Mirzaa G.M., Dobyns W.B., McEvoy-Venneri J.,
RA Stanley V., James K.N., Mancini G.M.S., Schot R., Kalayci T., Altunoglu U.,
RA Karimiani E.G., Brick L., Kozenko M., Jamshidi Y., Manzini M.C.,
RA Beiraghi Toosi M., Gleeson J.G.;
RT "Bi-allelic Loss of Human APC2, Encoding Adenomatous Polyposis Coli Protein
RT 2, Leads to Lissencephaly, Subcortical Heterotopia, and Global
RT Developmental Delay.";
RL Am. J. Hum. Genet. 105:844-853(2019).
CC -!- FUNCTION: Stabilizes microtubules and may regulate actin fiber dynamics
CC through the activation of Rho family GTPases (PubMed:25753423). May
CC also function in Wnt signaling by promoting the rapid degradation of
CC CTNNB1 (PubMed:10021369, PubMed:11691822, PubMed:9823329).
CC {ECO:0000269|PubMed:10021369, ECO:0000269|PubMed:11691822,
CC ECO:0000269|PubMed:25753423, ECO:0000269|PubMed:9823329}.
CC -!- SUBUNIT: Interacts with PSRC1 (By similarity). Interacts with APC,
CC CTNNB1, MAPRE1, MAPRE3, TP53BP2 and possibly with AXIN2. {ECO:0000250,
CC ECO:0000269|PubMed:10021369, ECO:0000269|PubMed:10644998,
CC ECO:0000269|PubMed:10646860, ECO:0000269|PubMed:11691822,
CC ECO:0000269|PubMed:9823329}.
CC -!- INTERACTION:
CC O95996; Q15691: MAPRE1; NbExp=3; IntAct=EBI-1053045, EBI-1004115;
CC O95996; Q9UPY8: MAPRE3; NbExp=7; IntAct=EBI-1053045, EBI-726739;
CC O95996; Q13625: TP53BP2; NbExp=4; IntAct=EBI-1053045, EBI-77642;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:11691822,
CC ECO:0000269|PubMed:25753423}. Golgi apparatus
CC {ECO:0000269|PubMed:11691822}. Cytoplasm {ECO:0000269|PubMed:11691822}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:10646860}.
CC Note=Associated with actin filaments (PubMed:11691822,
CC PubMed:25753423). Associated with microtubule network (PubMed:10644998,
CC PubMed:11691822, PubMed:25753423). {ECO:0000269|PubMed:10644998,
CC ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95996-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95996-2; Sequence=VSP_030106;
CC Name=3;
CC IsoId=O95996-3; Sequence=VSP_030107;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). Specifically
CC expressed in the CNS. {ECO:0000269|PubMed:10021369,
CC ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:9823329}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain.
CC {ECO:0000269|PubMed:10021369}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 74
CC (MRT74) [MIM:617169]: A disorder characterized by intellectual
CC impairment, macrocephaly, and dysmorphic features. Epilepsy with eyelid
CC myoclonus has also been reported. {ECO:0000269|PubMed:25753423}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Cortical dysplasia, complex, with other brain malformations 10
CC (CDCBM10) [MIM:618677]: An autosomal recessive disorder of aberrant
CC neuronal migration during brain development. CDCBM10 is clinically
CC characterized by onset in infancy of global developmental delay,
CC impaired intellectual development, seizures, inability to ambulate, and
CC absent language. Brain imaging shows lissencephaly, cortical dysplasia,
CC subcortical heterotopia, and paucity of white matter.
CC {ECO:0000269|PubMed:31585108}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD28183.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF01784.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC Sequence=CAA10317.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB61207.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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DR EMBL; AB012162; BAA34611.1; -; mRNA.
DR EMBL; AB022529; BAA75469.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69498.1; -; Genomic_DNA.
DR EMBL; AF110334; AAD28183.1; ALT_FRAME; mRNA.
DR EMBL; AF110335; AAD29273.1; -; Genomic_DNA.
DR EMBL; AF110337; AAD29274.1; -; Genomic_DNA.
DR EMBL; AF110336; AAD29274.1; JOINED; Genomic_DNA.
DR EMBL; AF128222; AAF01784.1; ALT_SEQ; mRNA.
DR EMBL; AJ012652; CAB61207.1; ALT_SEQ; mRNA.
DR EMBL; AJ131187; CAA10317.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC032573; AAH32573.1; -; mRNA.
DR CCDS; CCDS12068.1; -. [O95996-1]
DR RefSeq; NP_005874.1; NM_005883.2. [O95996-1]
DR RefSeq; XP_006722672.1; XM_006722609.3. [O95996-1]
DR AlphaFoldDB; O95996; -.
DR SMR; O95996; -.
DR BioGRID; 115585; 12.
DR ComplexPortal; CPX-440; Beta-catenin destruction core complex, variant 4.
DR ComplexPortal; CPX-442; Beta-catenin destruction core complex, variant 6.
DR ComplexPortal; CPX-443; Beta-catenin destruction core complex, variant 8.
DR ComplexPortal; CPX-99; Beta-catenin destruction core complex, variant 2.
DR ELM; O95996; -.
DR IntAct; O95996; 11.
DR MINT; O95996; -.
DR STRING; 9606.ENSP00000442954; -.
DR CarbonylDB; O95996; -.
DR iPTMnet; O95996; -.
DR PhosphoSitePlus; O95996; -.
DR BioMuta; APC2; -.
DR jPOST; O95996; -.
DR MassIVE; O95996; -.
DR PaxDb; O95996; -.
DR PeptideAtlas; O95996; -.
DR PRIDE; O95996; -.
DR ProteomicsDB; 51171; -. [O95996-1]
DR ProteomicsDB; 51172; -. [O95996-2]
DR ProteomicsDB; 51173; -. [O95996-3]
DR Antibodypedia; 10529; 129 antibodies from 24 providers.
DR DNASU; 10297; -.
DR Ensembl; ENST00000233607.6; ENSP00000233607.2; ENSG00000115266.12. [O95996-1]
DR Ensembl; ENST00000535453.5; ENSP00000442954.1; ENSG00000115266.12. [O95996-1]
DR Ensembl; ENST00000590469.6; ENSP00000467073.2; ENSG00000115266.12. [O95996-1]
DR GeneID; 10297; -.
DR KEGG; hsa:10297; -.
DR MANE-Select; ENST00000590469.6; ENSP00000467073.2; NM_005883.3; NP_005874.1.
DR UCSC; uc002lsr.1; human. [O95996-1]
DR CTD; 10297; -.
DR DisGeNET; 10297; -.
DR GeneCards; APC2; -.
DR HGNC; HGNC:24036; APC2.
DR HPA; ENSG00000115266; Tissue enriched (brain).
DR MalaCards; APC2; -.
DR MIM; 612034; gene.
DR MIM; 617169; phenotype.
DR MIM; 618677; phenotype.
DR neXtProt; NX_O95996; -.
DR OpenTargets; ENSG00000115266; -.
DR Orphanet; 821; Sotos syndrome.
DR PharmGKB; PA134906843; -.
DR VEuPathDB; HostDB:ENSG00000115266; -.
DR eggNOG; KOG2122; Eukaryota.
DR GeneTree; ENSGT00530000063749; -.
DR HOGENOM; CLU_001012_0_0_1; -.
DR InParanoid; O95996; -.
DR OMA; NGKTQIC; -.
DR OrthoDB; 31524at2759; -.
DR PhylomeDB; O95996; -.
DR TreeFam; TF106496; -.
DR PathwayCommons; O95996; -.
DR SignaLink; O95996; -.
DR SIGNOR; O95996; -.
DR BioGRID-ORCS; 10297; 20 hits in 1067 CRISPR screens.
DR ChiTaRS; APC2; human.
DR GenomeRNAi; 10297; -.
DR Pharos; O95996; Tbio.
DR PRO; PR:O95996; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O95996; protein.
DR Bgee; ENSG00000115266; Expressed in paraflocculus and 162 other tissues.
DR ExpressionAtlas; O95996; baseline and differential.
DR Genevisible; O95996; HS.
DR GO; GO:0005884; C:actin filament; IDA:BHF-UCL.
DR GO; GO:0030877; C:beta-catenin destruction complex; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0031258; C:lamellipodium membrane; IDA:BHF-UCL.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL.
DR GO; GO:0030496; C:midbody; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
DR GO; GO:0045295; F:gamma-catenin binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0007389; P:pattern specification process; IBA:GO_Central.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR026837; APC2.
DR InterPro; IPR009234; APC_basic_dom.
DR InterPro; IPR026831; APC_dom.
DR InterPro; IPR026818; Apc_fam.
DR InterPro; IPR032038; APC_N.
DR InterPro; IPR036149; APC_N_sf.
DR InterPro; IPR041257; APC_rep.
DR InterPro; IPR009223; APC_rpt.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR009224; SAMP.
DR PANTHER; PTHR12607; PTHR12607; 1.
DR PANTHER; PTHR12607:SF3; PTHR12607:SF3; 1.
DR Pfam; PF05956; APC_basic; 1.
DR Pfam; PF16689; APC_N_CC; 1.
DR Pfam; PF05923; APC_r; 4.
DR Pfam; PF18797; APC_rep; 1.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF05924; SAMP; 2.
DR SMART; SM00185; ARM; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF58050; SSF58050; 1.
DR SUPFAM; SSF82931; SSF82931; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Golgi apparatus; Intellectual disability; Lissencephaly;
KW Microtubule; Phosphoprotein; Reference proteome; Repeat;
KW Wnt signaling pathway.
FT CHAIN 1..2303
FT /note="Adenomatous polyposis coli protein 2"
FT /id="PRO_0000313686"
FT REPEAT 302..341
FT /note="ARM 1"
FT REPEAT 479..518
FT /note="ARM 2"
FT REPEAT 522..562
FT /note="ARM 3"
FT REPEAT 566..609
FT /note="ARM 4"
FT REPEAT 615..654
FT /note="ARM 5"
FT REPEAT 657..696
FT /note="ARM 6"
FT REPEAT 1058..1077
FT /note="1"
FT REPEAT 1150..1169
FT /note="2"
FT REPEAT 1263..1282
FT /note="3"
FT REPEAT 1391..1410
FT /note="4"
FT REPEAT 1568..1587
FT /note="5"
FT REGION 94..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1587
FT /note="5 X 20 AA approximate repeat of F-X-V-E-X-T-P-X-C-F-
FT S-R-X-S-S-L-S-S-L-S"
FT REGION 1058..1587
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000269|PubMed:9823329"
FT REGION 1069..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1724..2031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1821..1900
FT /note="Required for localization to microtubules and
FT function in microtubule stabilization"
FT /evidence="ECO:0000269|PubMed:25753423"
FT REGION 2046..2232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2067..2144
FT /note="Interaction with MAPRE1 and MAPRE3"
FT /evidence="ECO:0000269|PubMed:10644998"
FT COILED 8..59
FT /evidence="ECO:0000255"
FT COILED 840..864
FT /evidence="ECO:0000255"
FT COMPBIAS 1173..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1222
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1574..1589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1651..1684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1835..1884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1978..1992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2196..2211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1K7"
FT MOD_RES 1587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1K7"
FT VAR_SEQ 168..441
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_030106"
FT VAR_SEQ 175
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10021369"
FT /id="VSP_030107"
FT VARIANT 246..2303
FT /note="Missing (in CDCBM10)"
FT /evidence="ECO:0000269|PubMed:31585108"
FT /id="VAR_083414"
FT VARIANT 361..2303
FT /note="Missing (in CDCBM10)"
FT /evidence="ECO:0000269|PubMed:31585108"
FT /id="VAR_083415"
FT VARIANT 562
FT /note="A -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_037703"
FT VARIANT 628..2303
FT /note="Missing (in CDCBM10)"
FT /evidence="ECO:0000269|PubMed:31585108"
FT /id="VAR_083416"
FT VARIANT 1921
FT /note="H -> N"
FT /evidence="ECO:0000269|PubMed:29120066"
FT /id="VAR_081224"
FT VARIANT 2003
FT /note="G -> S (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1288757495)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_037704"
FT VARIANT 2241
FT /note="S -> A (in dbSNP:rs265277)"
FT /id="VAR_037705"
FT CONFLICT 463
FT /note="Missing (in Ref. 4; AAD28183)"
FT /evidence="ECO:0000305"
FT CONFLICT 526..527
FT /note="KV -> NL (in Ref. 4; AAD28183/AAD29274)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="E -> A (in Ref. 5; AAF01784/CAB61207)"
FT /evidence="ECO:0000305"
FT CONFLICT 816
FT /note="L -> Q (in Ref. 4; AAD28183)"
FT /evidence="ECO:0000305"
FT CONFLICT 971
FT /note="L -> P (in Ref. 4; AAD28183)"
FT /evidence="ECO:0000305"
FT CONFLICT 1106
FT /note="S -> I (in Ref. 4; AAD28183)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="E -> G (in Ref. 5; CAA10317)"
FT /evidence="ECO:0000305"
FT CONFLICT 1188
FT /note="Q -> H (in Ref. 4; AAD28183)"
FT /evidence="ECO:0000305"
FT CONFLICT 1361
FT /note="A -> G (in Ref. 4; AAD28183)"
FT /evidence="ECO:0000305"
FT CONFLICT 1456
FT /note="R -> P (in Ref. 4; AAD28183)"
FT /evidence="ECO:0000305"
FT CONFLICT 1515
FT /note="D -> V (in Ref. 4; AAD28183)"
FT /evidence="ECO:0000305"
FT CONFLICT 2219
FT /note="A -> V (in Ref. 5; CAA10317)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2303 AA; 243949 MW; 7BF940183ACD643D CRC64;
MASSVAPYEQ LVRQVEALKA ENSHLRQELR DNSSHLSKLE TETSGMKEVL KHLQGKLEQE
ARVLVSSGQT EVLEQLKALQ MDITSLYNLK FQPPTLGPEP AARTPEGSPV HGSGPSKDSF
GELSRATIRL LEELDRERCF LLNEIEKEEK EKLWYYSQLQ GLSKRLDELP HVETQFSMQM
DLIRQQLEFE AQHIRSLMEE RFGTSDEMVQ RAQIRASRLE QIDKELLEAQ DRVQQTEPQA
LLAVKSVPVD EDPETEVPTH PEDGTPQPGN SKVEVVFWLL SMLATRDQED TARTLLAMSS
SPESCVAMRR SGCLPLLLQI LHGTEAAAGG RAGAPGAPGA KDARMRANAA LHNIVFSQPD
QGLARKEMRV LHVLEQIRAY CETCWDWLQA RDGGPEGGGA GSAPIPIEPQ ICQATCAVMK
LSFDEEYRRA MNELGGLQAV AELLQVDYEM HKMTRDPLNL ALRRYAGMTL TNLTFGDVAN
KATLCARRGC MEAIVAQLAS DSEELHQVVS SILRNLSWRA DINSKKVLRE AGSVTALVQC
VLRATKESTL KSVLSALWNL SAHSTENKAA ICQVDGALGF LVSTLTYKCQ SNSLAIIESG
GGILRNVSSL VATREDYRQV LRDHNCLQTL LQHLTSHSLT IVSNACGTLW NLSARSARDQ
ELLWDLGAVG MLRNLVHSKH KMIAMGSAAA LRNLLAHRPA KHQAAATAVS PGSCVPSLYV
RKQRALEAEL DARHLAQALE HLEKQGPPAA EAATKKPLPP LRHLDGLAQD YASDSGCFDD
DDAPSSLAAA AATGEPASPA ALSLFLGSPF LQGQALARTP PTRRGGKEAE KDTSGEAAVA
AKAKAKLALA VARIDQLVED ISALHTSSDD SFSLSSGDPG QEAPREGRAQ SCSPCRGPEG
GRREAGSRAH PLLRLKAAHA SLSNDSLNSG SASDGYCPRE HMLPCPLAAL ASRREDPRCG
QPRPSRLDLD LPGCQAEPPA REATSADARV RTIKLSPTYQ HVPLLEGASR AGAEPLAGPG
ISPGARKQAW LPADHLSKVP EKLAAAPLSV ASKALQKLAA QEGPLSLSRC SSLSSLSSAG
RPGPSEGGDL DDSDSSLEGL EEAGPSEAEL DSTWRAPGAT SLPVAIPAPR RNRGRGLGVE
DATPSSSSEN YVQETPLVLS RCSSVSSLGS FESPSIASSI PSEPCSGQGS GTISPSELPD
SPGQTMPPSR SKTPPLAPAP QGPPEATQFS LQWESYVKRF LDIADCRERC RLPSELDAGS
VRFTVEKPDE NFSCASSLSA LALHEHYVQQ DVELRLLPSA CPERGGGAGG AGLHFAGHRR
REEGPAPTGS RPRGAADQEL ELLRECLGAA VPARLRKVAS ALVPGRRALP VPVYMLVPAP
APAQEDDSCT DSAEGTPVNF SSAASLSDET LQGPPRDQPG GPAGRQRPTG RPTSARQAMG
HRHKAGGAGR SAEQSRGAGK NRAGLELPLG RPPSAPADKD GSKPGRTRGD GALQSLCLTT
PTEEAVYCFY GNDSDEEPPA AAPTPTHRRT SAIPRAFTRE RPQGRKEAPA PSKAAPAAPP
PARTQPSLIA DETPPCYSLS SSASSLSEPE PSEPPAVHPR GREPAVTKDP GPGGGRDSSP
SPRAAEELLQ RCISSALPRR RPPVSGLRRR KPRATRLDER PAEGSRERGE EAAGSDRASD
LDSVEWRAIQ EGANSIVTWL HQAAAATREA SSESDSILSF VSGLSVGSTL QPPKHRKGRQ
AEGEMGSARR PEKRGAASVK TSGSPRSPAG PEKPRGTQKT TPGVPAVLRG RTVIYVPSPA
PRAQPKGTPG PRATPRKVAP PCLAQPAAPA KVPSPGQQRS RSLHRPAKTS ELATLSQPPR
SATPPARLAK TPSSSSSQTS PASQPLPRKR PPVTQAAGAL PGPGASPVPK TPARTLLAKQ
HKTQRSPVRI PFMQRPARRG PPPLARAVPE PGPRGRAGTE AGPGARGGRL GLVRVASALS
SGSESSDRSG FRRQLTFIKE SPGLRRRRSE LSSAESAASA PQGASPRRGR PALPAVFLCS
SRCEELRAAP RQGPAPARQR PPAARPSPGE RPARRTTSES PSRLPVRAPA ARPETVKRYA
SLPHISVARR PDGAVPAAPA SADAARRSSD GEPRPLPRVA APGTTWRRIR DEDVPHILRS
TLPATALPLR GSTPEDAPAG PPPRKTSDAV VQTEEVAAPK TNSSTSPSLE TREPPGAPAG
GQLSLLGSDV DGPSLAKAPI SAPFVHEGLG VAVGGFPASR HGSPSRSARV PPFNYVPSPM
VVAATTDSAA EKAPATASAT LLE
