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   12-AUG-2020, entry version 159.
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 SOTOS3, 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: Sotos syndrome 3 (SOTOS3) [MIM:617169]: A form of Sotos
CC       syndrome, a childhood overgrowth syndrome characterized by prenatal and
CC       postnatal overgrowth, developmental delay, mental retardation, advanced
CC       bone age, and abnormal craniofacial morphology. SOTOS3 patients do not
CC       have advanced bone age, hypotonia, seizures, or autism. SOTOS3
CC       transmission pattern is consistent with autosomal recessive
CC       inheritance. {ECO:0000269|PubMed:25753423}. Note=The disease is caused
CC       by mutations affecting the gene represented 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 mutations
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   SMR; O95996; -.
DR   BioGRID; 115585; 7.
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; 6.
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; 119 antibodies.
DR   Ensembl; ENST00000233607; ENSP00000233607; ENSG00000115266. [O95996-1]
DR   Ensembl; ENST00000535453; ENSP00000442954; ENSG00000115266. [O95996-1]
DR   GeneID; 10297; -.
DR   KEGG; hsa:10297; -.
DR   UCSC; uc002lsr.1; human. [O95996-1]
DR   CTD; 10297; -.
DR   DisGeNET; 10297; -.
DR   EuPathDB; HostDB:ENSG00000115266.11; -.
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   eggNOG; KOG2122; Eukaryota.
DR   GeneTree; ENSGT00530000063749; -.
DR   HOGENOM; CLU_001012_0_0_1; -.
DR   InParanoid; O95996; -.
DR   KO; K02085; -.
DR   OMA; MCAIMKL; -.
DR   OrthoDB; 31524at2759; -.
DR   PhylomeDB; O95996; -.
DR   TreeFam; TF106496; -.
DR   PathwayCommons; O95996; -.
DR   SignaLink; O95996; -.
DR   SIGNOR; O95996; -.
DR   BioGRID-ORCS; 10297; 8 hits in 870 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 193 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; IEA:InterPro.
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: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: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 mutation; Golgi apparatus; Lissencephaly; Microtubule;
KW   Phosphoprotein; Polymorphism; 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          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          1821..1900
FT                   /note="Required for localization to microtubules and
FT                   function in microtubule stabilization"
FT                   /evidence="ECO:0000269|PubMed:25753423"
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        1145..1196
FT                   /note="Ser-rich"
FT   COMPBIAS        1518..1622
FT                   /note="Pro-rich"
FT   COMPBIAS        1765..1953
FT                   /note="Pro-rich"
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
//