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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
 
 
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