CABYR_HUMAN
ID CABYR_HUMAN Reviewed; 493 AA.
AC O75952; B2R857; Q8WXW5; Q9HAY3; Q9HAY4; Q9HAY5; Q9HCY9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Calcium-binding tyrosine phosphorylation-regulated protein;
DE AltName: Full=Calcium-binding protein 86;
DE AltName: Full=Cancer/testis antigen 88;
DE Short=CT88;
DE AltName: Full=Fibrousheathin II;
DE AltName: Full=Fibrousheathin-2;
DE Short=FSP-2;
DE AltName: Full=Testis-specific calcium-binding protein CBP86;
GN Name=CABYR; Synonyms=CBP86, FSP2;
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] (ISOFORMS 1; 2; 3; 4; 5 AND 6), PROTEIN SEQUENCE
RP OF 8-23; 28-48; 379-388 AND 394-410, VARIANTS ARG-448 AND ALA-490,
RP CALCIUM-BINDING, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11820818; DOI=10.1006/dbio.2001.0527;
RA Naaby-Hansen S., Mandal A., Wolkowicz M.J., Sen B., Westbrook V.A.,
RA Shetty J., Coonrod S.A., Klotz K.L., Kim Y.-H., Bush L.A., Flickinger C.J.,
RA Herr J.C.;
RT "CABYR, a novel calcium-binding tyrosine phosphorylation-regulated fibrous
RT sheath protein involved in capacitation.";
RL Dev. Biol. 242:236-254(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Ovary;
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 [6]
RP ALTERNATIVE SPLICING (ISOFORMS 3 AND 5), SUBUNIT, INTERACTION WITH GSK3B,
RP PHOSPHORYLATION AT THR-151 AND SER-155, MUTAGENESIS OF THR-146; THR-151;
RP SER-154; SER-155 AND THR-159, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15752768; DOI=10.1016/j.bbrc.2005.02.089;
RA Hsu H.-C., Lee Y.-L., Cheng T.-S., Howng S.-L., Chang L.-K., Lu P.-J.,
RA Hong Y.-R.;
RT "Characterization of two non-testis-specific CABYR variants that bind to
RT GSK3beta with a proline-rich extensin-like domain.";
RL Biochem. Biophys. Res. Commun. 329:1108-1117(2005).
RN [7]
RP CALCIUM-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16139264; DOI=10.1016/j.ydbio.2005.07.005;
RA Kim Y.-H., Jha K.N., Mandal A., Vanage G., Farris E., Snow P.L., Klotz K.,
RA Naaby-Hansen S., Flickinger C.J., Herr J.C.;
RT "Translation and assembly of CABYR coding region B in fibrous sheath and
RT restriction of calcium binding to coding region A.";
RL Dev. Biol. 286:46-56(2005).
CC -!- FUNCTION: May function as a regulator of both motility- and head-
CC associated functions such as capacitation and the acrosome reaction.
CC Isoform 1 binds calcium in vitro. Isoform 2 and isoform 6 probably bind
CC calcium. Isoform 3 and isoform 5 do not bind calcium in vitro. Isoform
CC 4 probably does not bind calcium.
CC -!- SUBUNIT: Interacts with FSCB (By similarity). Isoform 3 self-
CC associates. Isoform 3 and isoform 5 interact with GSK3B. Isoform 1 does
CC not interact with GSK3B. {ECO:0000250, ECO:0000269|PubMed:15752768}.
CC -!- INTERACTION:
CC O75952-3; P49841: GSK3B; NbExp=3; IntAct=EBI-10900795, EBI-373586;
CC O75952-5; P49841: GSK3B; NbExp=3; IntAct=EBI-10898671, EBI-373586;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, cilium,
CC flagellum. Note=Localized to fibrous sheath including the surface of
CC the longitudinal columns and ribs of the principal piece of sperm
CC flagella.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Cytoplasm. Cell projection,
CC cilium, flagellum. Note=According to PubMed:15752768, isoform 1,
CC isoform 3 and isoform 5 are both nuclear and cytoplasmic.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm. Cell projection,
CC cilium, flagellum. Note=According to PubMed:15752768, isoform 1,
CC isoform 3 and isoform 5 are both nuclear and cytoplasmic.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Nucleus. Cytoplasm. Cell projection,
CC cilium, flagellum. Note=According to PubMed:15752768, isoform 1,
CC isoform 3 and isoform 5 are both nuclear and cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O75952-1; Sequence=Displayed;
CC Name=2; Synonyms=CBP86-VII;
CC IsoId=O75952-2; Sequence=VSP_016247;
CC Name=3; Synonyms=CBP86-II;
CC IsoId=O75952-3; Sequence=VSP_016248, VSP_016251;
CC Name=4; Synonyms=CBP86-IV;
CC IsoId=O75952-4; Sequence=VSP_016249, VSP_016250;
CC Name=5; Synonyms=CBP86-III;
CC IsoId=O75952-5; Sequence=VSP_016246, VSP_016248, VSP_016251;
CC Name=6; Synonyms=CBP86-VI;
CC IsoId=O75952-6; Sequence=VSP_016245;
CC -!- TISSUE SPECIFICITY: Expressed in elongating spermatids and spermatozoa
CC (at protein level). Isoform 1 is expressed in testis. Isoform 3 and
CC isoform 5 are also expressed in brain, pancreas and numerous brain
CC tumors. {ECO:0000269|PubMed:11820818, ECO:0000269|PubMed:15752768,
CC ECO:0000269|PubMed:16139264}.
CC -!- PTM: Isoform 1 is phosphorylated on tyrosine residues during in vitro
CC capacitation. Isoform 3 and isoform 5 are phosphorylated by GSK3B in
CC vitro. Dephosphorylation affects its ability to bind calcium.
CC {ECO:0000269|PubMed:11820818, ECO:0000269|PubMed:15752768}.
CC -!- MISCELLANEOUS: [Isoform 1]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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DR EMBL; AF088868; AAC35373.1; -; mRNA.
DR EMBL; AF295037; AAG17889.1; -; mRNA.
DR EMBL; AF295038; AAG17890.1; -; mRNA.
DR EMBL; AF295039; AAG17891.1; -; mRNA.
DR EMBL; AF329634; AAL56051.1; -; mRNA.
DR EMBL; AY007205; AAG01891.1; -; mRNA.
DR EMBL; AK313243; BAG36054.1; -; mRNA.
DR EMBL; AC090772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471088; EAX01177.1; -; Genomic_DNA.
DR EMBL; BC011996; AAH11996.1; -; mRNA.
DR CCDS; CCDS11881.1; -. [O75952-1]
DR CCDS; CCDS11882.1; -. [O75952-2]
DR CCDS; CCDS11883.1; -. [O75952-5]
DR CCDS; CCDS42420.1; -. [O75952-3]
DR CCDS; CCDS45840.1; -. [O75952-4]
DR RefSeq; NP_036321.2; NM_012189.3. [O75952-1]
DR RefSeq; NP_619584.1; NM_138643.2. [O75952-5]
DR RefSeq; NP_619585.1; NM_138644.2. [O75952-3]
DR RefSeq; NP_722452.1; NM_153768.2. [O75952-2]
DR RefSeq; NP_722453.1; NM_153769.2. [O75952-3]
DR RefSeq; NP_722454.1; NM_153770.2. [O75952-4]
DR RefSeq; XP_016881195.1; XM_017025706.1.
DR AlphaFoldDB; O75952; -.
DR SMR; O75952; -.
DR BioGRID; 117642; 6.
DR IntAct; O75952; 2.
DR MINT; O75952; -.
DR STRING; 9606.ENSP00000483621; -.
DR iPTMnet; O75952; -.
DR PhosphoSitePlus; O75952; -.
DR BioMuta; CABYR; -.
DR MassIVE; O75952; -.
DR MaxQB; O75952; -.
DR PaxDb; O75952; -.
DR PeptideAtlas; O75952; -.
DR PRIDE; O75952; -.
DR ProteomicsDB; 50313; -. [O75952-1]
DR ProteomicsDB; 50314; -. [O75952-2]
DR ProteomicsDB; 50315; -. [O75952-3]
DR ProteomicsDB; 50316; -. [O75952-4]
DR ProteomicsDB; 50317; -. [O75952-5]
DR ProteomicsDB; 50318; -. [O75952-6]
DR Antibodypedia; 22085; 93 antibodies from 24 providers.
DR DNASU; 26256; -.
DR Ensembl; ENST00000327201.10; ENSP00000317095.6; ENSG00000154040.21. [O75952-5]
DR Ensembl; ENST00000399481.6; ENSP00000382404.3; ENSG00000154040.21. [O75952-2]
DR Ensembl; ENST00000399496.8; ENSP00000382419.3; ENSG00000154040.21. [O75952-3]
DR Ensembl; ENST00000399499.5; ENSP00000382421.1; ENSG00000154040.21. [O75952-3]
DR Ensembl; ENST00000415309.6; ENSP00000399973.2; ENSG00000154040.21. [O75952-4]
DR Ensembl; ENST00000463087.5; ENSP00000432870.1; ENSG00000154040.21. [O75952-1]
DR Ensembl; ENST00000486759.6; ENSP00000431142.3; ENSG00000154040.21. [O75952-1]
DR Ensembl; ENST00000621648.4; ENSP00000483621.1; ENSG00000154040.21. [O75952-1]
DR GeneID; 26256; -.
DR KEGG; hsa:26256; -.
DR MANE-Select; ENST00000399496.8; ENSP00000382419.3; NM_153769.3; NP_722453.1. [O75952-3]
DR UCSC; uc002kux.5; human. [O75952-1]
DR CTD; 26256; -.
DR DisGeNET; 26256; -.
DR GeneCards; CABYR; -.
DR HGNC; HGNC:15569; CABYR.
DR HPA; ENSG00000154040; Tissue enriched (testis).
DR MIM; 612135; gene.
DR neXtProt; NX_O75952; -.
DR OpenTargets; ENSG00000154040; -.
DR PharmGKB; PA26005; -.
DR VEuPathDB; HostDB:ENSG00000154040; -.
DR eggNOG; ENOG502S1NF; Eukaryota.
DR GeneTree; ENSGT00390000000444; -.
DR HOGENOM; CLU_061187_0_0_1; -.
DR InParanoid; O75952; -.
DR OMA; VHISSIY; -.
DR OrthoDB; 919811at2759; -.
DR PhylomeDB; O75952; -.
DR TreeFam; TF332959; -.
DR PathwayCommons; O75952; -.
DR SignaLink; O75952; -.
DR SIGNOR; O75952; -.
DR BioGRID-ORCS; 26256; 5 hits in 1071 CRISPR screens.
DR ChiTaRS; CABYR; human.
DR GeneWiki; CABYR; -.
DR GenomeRNAi; 26256; -.
DR Pharos; O75952; Tbio.
DR PRO; PR:O75952; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; O75952; protein.
DR Bgee; ENSG00000154040; Expressed in sperm and 126 other tissues.
DR ExpressionAtlas; O75952; baseline and differential.
DR Genevisible; O75952; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0031514; C:motile cilium; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0035686; C:sperm fibrous sheath; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0017124; F:SH3 domain binding; NAS:BHF-UCL.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; NAS:BHF-UCL.
DR GO; GO:0048240; P:sperm capacitation; NAS:BHF-UCL.
DR InterPro; IPR038848; CABYR.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR PANTHER; PTHR15494; PTHR15494; 2.
DR Pfam; PF02197; RIIa; 1.
DR SMART; SM00394; RIIa; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Flagellum; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..493
FT /note="Calcium-binding tyrosine phosphorylation-regulated
FT protein"
FT /id="PRO_0000089268"
FT DOMAIN 12..49
FT /note="RIIa"
FT REGION 85..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:15752768"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:15752768"
FT VAR_SEQ 1..201
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11820818"
FT /id="VSP_016245"
FT VAR_SEQ 1..98
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11820818"
FT /id="VSP_016246"
FT VAR_SEQ 49..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11820818,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_016247"
FT VAR_SEQ 181..379
FT /note="GKVSSIHSDQSDVLMVDVATSMPVVIKEVPSSEAAEDVMVAAPLVCSGKVLE
FT VQVVNQTSVHVDLGSQPKENEAEPSTASSVPLQDEQEPPAYDQAPEVTLQADIEVMSTV
FT HISSVYNDVPVTEGVVYIEQLPEQIVIPFTDQVACLKENEQSKENEQSPRVSPKSVVEK
FT TTSGMSKKSVESVKLAQLEENAKYSSVYM -> AMATSERGQPPPCSNMWTLYCLTDKN
FT QQGHPSPPPAPGPFPQATLYLPNPKDPQFQQHPPKVTFPTYVMGDTKKTSAPPFILVGS
FT NVQEAQGWKPLPGHAVVSQSDVLRYVAMQVPIAVPADEKYQKHTLSPQNANPPSGQDVP
FT RPKSPVFLSVAFPVEDVAKKSSGSGDKCAPFGSYGIAGEVTVTTAHKRRKAETEN (in
FT isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11820818,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016248"
FT VAR_SEQ 181..221
FT /note="GKVSSIHSDQSDVLMVDVATSMPVVIKEVPSSEAAEDVMVA -> EDVAKKS
FT SGSGDKCAPFGSYGIAGEVTVTTAHKRRKAETEN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11820818"
FT /id="VSP_016249"
FT VAR_SEQ 222..493
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11820818"
FT /id="VSP_016250"
FT VAR_SEQ 380..493
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11820818,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016251"
FT VARIANT 74
FT /note="T -> M (in dbSNP:rs3786417)"
FT /id="VAR_030040"
FT VARIANT 186
FT /note="I -> V (in dbSNP:rs35118855)"
FT /id="VAR_050709"
FT VARIANT 448
FT /note="K -> R (in dbSNP:rs1049682)"
FT /evidence="ECO:0000269|PubMed:11820818"
FT /id="VAR_030041"
FT VARIANT 490
FT /note="S -> A (in dbSNP:rs1049683)"
FT /evidence="ECO:0000269|PubMed:11820818"
FT /id="VAR_023818"
FT MUTAGEN 146
FT /note="T->A: Does not affect phosphorylation."
FT /evidence="ECO:0000269|PubMed:15752768"
FT MUTAGEN 151
FT /note="T->A: Decreases phosphorylation. Abolishes
FT phosphorylation; when associated with A-155."
FT /evidence="ECO:0000269|PubMed:15752768"
FT MUTAGEN 154
FT /note="S->A: Does not affect phosphorylation. Does not
FT affect phosphorylation; when associated with A-159."
FT /evidence="ECO:0000269|PubMed:15752768"
FT MUTAGEN 155
FT /note="S->A: Decreases phosphorylation and interaction with
FT GSK3B. Abolishes phosphorylation and decreases interaction
FT with GSK3B; when associated with A-151."
FT /evidence="ECO:0000269|PubMed:15752768"
FT MUTAGEN 159
FT /note="T->A: Does not affect phosphorylation. Does not
FT affect phosphorylation; when associated with A-154."
FT /evidence="ECO:0000269|PubMed:15752768"
FT CONFLICT 423
FT /note="I -> V (in Ref. 1; AAC35373/AAL56051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 52774 MW; 42F97605262C8199 CRC64;
MISSKPRLVV PYGLKTLLEG ISRAVLKTNP SNINQFAAAY FQELTMYRGN TTMDIKDLVK
QFHQIKVEKW SEGTTPQKKL ECLKEPGKTS VESKVPTQME KSTDTDEDNV TRTEYSDKTT
QFPSVYAVPG TEQTEAVGGL SSKPATPKTT TPPSSPPPTA VSPEFAYVPA DPAQLAAQML
GKVSSIHSDQ SDVLMVDVAT SMPVVIKEVP SSEAAEDVMV AAPLVCSGKV LEVQVVNQTS
VHVDLGSQPK ENEAEPSTAS SVPLQDEQEP PAYDQAPEVT LQADIEVMST VHISSVYNDV
PVTEGVVYIE QLPEQIVIPF TDQVACLKEN EQSKENEQSP RVSPKSVVEK TTSGMSKKSV
ESVKLAQLEE NAKYSSVYME AEATALLSDT SLKGQPEVPA QLLDAEGAIK IGSEKSLHLE
VEITSIVSDN TGQEESGENS VPQEMEGKPV LSGEAAEAVH SGTSVKSSSG PFPPAPEGLT
APEIEPEGES TAE