CPEB4_HUMAN
ID CPEB4_HUMAN Reviewed; 729 AA.
AC Q17RY0; B7ZLQ7; Q7Z310; Q8N405; Q9C0J0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 4;
DE Short=CPE-BP4;
DE Short=CPE-binding protein 4;
DE Short=hCPEB-4;
GN Name=CPEB4; Synonyms=KIAA1673;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, and Lymphoma;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252; SER-255 AND THR-326, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252; SER-255; SER-330 AND
RP SER-332, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP INTERACTION WITH TOB1.
RX PubMed=21336257; DOI=10.1038/emboj.2011.37;
RA Hosoda N., Funakoshi Y., Hirasawa M., Yamagishi R., Asano Y., Miyagawa R.,
RA Ogami K., Tsujimoto M., Hoshino S.;
RT "Anti-proliferative protein Tob negatively regulates CPEB3 target by
RT recruiting Caf1 deadenylase.";
RL EMBO J. 30:1311-1323(2011).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22138752; DOI=10.1038/nm.2540;
RA Ortiz-Zapater E., Pineda D., Martinez-Bosch N., Fernandez-Miranda G.,
RA Iglesias M., Alameda F., Moreno M., Eliscovich C., Eyras E., Real F.X.,
RA Mendez R., Navarro P.;
RT "Key contribution of CPEB4-mediated translational control to cancer
RT progression.";
RL Nat. Med. 18:83-90(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-99 AND SER-332, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-99 AND SER-137, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP FUNCTION.
RX PubMed=26398195; DOI=10.1371/journal.pone.0138794;
RA Giangarra V., Igea A., Castellazzi C.L., Bava F.A., Mendez R.;
RT "Global analysis of CPEBs reveals sequential and non-redundant functions in
RT mitotic cell cycle.";
RL PLoS ONE 10:E0138794-E0138794(2015).
RN [12]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=27857118; DOI=10.1038/ncomms13418;
RA Perez-Guijarro E., Karras P., Cifdaloz M., Martinez-Herranz R., Canon E.,
RA Grana O., Horcajada-Reales C., Alonso-Curbelo D., Calvo T.G.,
RA Gomez-Lopez G., Bellora N., Riveiro-Falkenbach E., Ortiz-Romero P.L.,
RA Rodriguez-Peralto J.L., Maestre L., Roncador G., de Agustin Asensio J.C.,
RA Goding C.R., Eyras E., Megias D., Mendez R., Soengas M.S.;
RT "Lineage-specific roles of the cytoplasmic polyadenylation factor CPEB4 in
RT the regulation of melanoma drivers.";
RL Nat. Commun. 7:13418-13418(2016).
RN [13]
RP FUNCTION, STRUCTURE BY NMR OF 460-662 ALONE OR IN COMPLEX WITH RNA AND
RP ZINC, AND DOMAIN.
RX PubMed=24990967; DOI=10.1101/gad.241133.114;
RA Afroz T., Skrisovska L., Belloc E., Guillen-Boixet J., Mendez R.,
RA Allain F.H.;
RT "A fly trap mechanism provides sequence-specific RNA recognition by CPEB
RT proteins.";
RL Genes Dev. 28:1498-1514(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 379-393.
RX PubMed=26349033; DOI=10.7554/elife.10034;
RA Fung H.Y., Fu S.C., Brautigam C.A., Chook Y.M.;
RT "Structural determinants of nuclear export signal orientation in binding to
RT exportin CRM1.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: Sequence-specific RNA-binding protein that binds to the
CC cytoplasmic polyadenylation element (CPE), an uridine-rich sequence
CC element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR
CC (PubMed:24990967). RNA binding results in a clear conformational change
CC analogous to the Venus fly trap mechanism (PubMed:24990967). Regulates
CC activation of unfolded protein response (UPR) in the process of
CC adaptation to ER stress in liver, by maintaining translation of CPE-
CC regulated mRNAs in conditions in which global protein synthesis is
CC inhibited (By similarity). Required for cell cycle progression,
CC specifically for cytokinesis and chromosomal segregation
CC (PubMed:26398195). Plays a role as an oncogene promoting tumor growth
CC and progression by positively regulating translation of t-plasminogen
CC activator/PLAT (PubMed:22138752). Stimulates proliferation of
CC melanocytes (PubMed:27857118). In contrast to CPEB1 and CPEB3, does not
CC play role in synaptic plasticity, learning and memory (By similarity).
CC {ECO:0000250|UniProtKB:Q7TN98, ECO:0000269|PubMed:22138752,
CC ECO:0000269|PubMed:24990967, ECO:0000269|PubMed:26398195,
CC ECO:0000269|PubMed:27857118}.
CC -!- SUBUNIT: Interacts with TOB1. {ECO:0000269|PubMed:21336257}.
CC -!- INTERACTION:
CC Q17RY0; P50616: TOB1; NbExp=2; IntAct=EBI-2848203, EBI-723281;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7TN98}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:Q7TN98}. Cell projection,
CC dendritic spine {ECO:0000250|UniProtKB:Q7TN98}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q7TN98}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q7TN98}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q7TN98}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q17RY0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q17RY0-2; Sequence=VSP_022041;
CC Name=3;
CC IsoId=Q17RY0-3; Sequence=VSP_022040, VSP_022042;
CC -!- TISSUE SPECIFICITY: Expressed in pancreas in islets and ductal cells
CC (at protein level) (PubMed:22138752). Expressed in melanocytes
CC (PubMed:27857118). {ECO:0000269|PubMed:22138752,
CC ECO:0000269|PubMed:27857118}.
CC -!- DOMAIN: The 2 RRM domains and the C-terminal region mediate interaction
CC with CPE-containing RNA (PubMed:24990967). The interdomain linker (564-
CC 579) acts as a hinge to fix the relative orientation of the 2 RRMs
CC (PubMed:24990967). The ZZ domain (509-566) coordinates 2 Zn ions and is
CC probably implicated in mediating interactions with other proteins in
CC addition to increasing the affinity of the RRMs for the CPEs (By
CC similarity). Unlike in CPEB1, a continuous polar interface is formed
CC between the 2 RRMs (PubMed:24990967). {ECO:0000250|UniProtKB:Q9BZB8,
CC ECO:0000269|PubMed:24990967}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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DR EMBL; AB051460; BAB21764.1; -; mRNA.
DR EMBL; BX538213; CAD98072.1; -; mRNA.
DR EMBL; CH471062; EAW61392.1; -; Genomic_DNA.
DR EMBL; BC036899; AAH36899.1; -; mRNA.
DR EMBL; BC117150; AAI17151.1; -; mRNA.
DR EMBL; BC143958; AAI43959.1; -; mRNA.
DR CCDS; CCDS4390.1; -. [Q17RY0-1]
DR CCDS; CCDS78086.1; -. [Q17RY0-2]
DR CCDS; CCDS83044.1; -. [Q17RY0-3]
DR RefSeq; NP_001295118.1; NM_001308189.1. [Q17RY0-2]
DR RefSeq; NP_001295120.1; NM_001308191.1.
DR RefSeq; NP_001295121.1; NM_001308192.1.
DR RefSeq; NP_001295122.1; NM_001308193.1. [Q17RY0-3]
DR RefSeq; NP_085130.2; NM_030627.3. [Q17RY0-1]
DR PDB; 2MKI; NMR; -; A=460-662.
DR PDB; 2MKJ; NMR; -; A=460-662.
DR PDB; 5DIF; X-ray; 2.09 A; D=379-393.
DR PDBsum; 2MKI; -.
DR PDBsum; 2MKJ; -.
DR PDBsum; 5DIF; -.
DR AlphaFoldDB; Q17RY0; -.
DR BMRB; Q17RY0; -.
DR SMR; Q17RY0; -.
DR BioGRID; 123228; 142.
DR IntAct; Q17RY0; 8.
DR MINT; Q17RY0; -.
DR STRING; 9606.ENSP00000265085; -.
DR iPTMnet; Q17RY0; -.
DR PhosphoSitePlus; Q17RY0; -.
DR BioMuta; CPEB4; -.
DR DMDM; 119368635; -.
DR EPD; Q17RY0; -.
DR jPOST; Q17RY0; -.
DR MassIVE; Q17RY0; -.
DR MaxQB; Q17RY0; -.
DR PaxDb; Q17RY0; -.
DR PeptideAtlas; Q17RY0; -.
DR PRIDE; Q17RY0; -.
DR ProteomicsDB; 61171; -. [Q17RY0-1]
DR ProteomicsDB; 61172; -. [Q17RY0-2]
DR ProteomicsDB; 61173; -. [Q17RY0-3]
DR Antibodypedia; 28980; 160 antibodies from 24 providers.
DR DNASU; 80315; -.
DR Ensembl; ENST00000265085.10; ENSP00000265085.5; ENSG00000113742.14. [Q17RY0-1]
DR Ensembl; ENST00000334035.9; ENSP00000334533.5; ENSG00000113742.14. [Q17RY0-2]
DR Ensembl; ENST00000517880.1; ENSP00000427990.1; ENSG00000113742.14. [Q17RY0-3]
DR GeneID; 80315; -.
DR KEGG; hsa:80315; -.
DR MANE-Select; ENST00000265085.10; ENSP00000265085.5; NM_030627.4; NP_085130.2.
DR UCSC; uc003mcs.5; human. [Q17RY0-1]
DR CTD; 80315; -.
DR DisGeNET; 80315; -.
DR GeneCards; CPEB4; -.
DR HGNC; HGNC:21747; CPEB4.
DR HPA; ENSG00000113742; Low tissue specificity.
DR MIM; 610607; gene.
DR neXtProt; NX_Q17RY0; -.
DR OpenTargets; ENSG00000113742; -.
DR PharmGKB; PA134869176; -.
DR VEuPathDB; HostDB:ENSG00000113742; -.
DR eggNOG; KOG0129; Eukaryota.
DR GeneTree; ENSGT00940000154998; -.
DR HOGENOM; CLU_014948_2_1_1; -.
DR InParanoid; Q17RY0; -.
DR OMA; AENDTMK; -.
DR OrthoDB; 1075356at2759; -.
DR PhylomeDB; Q17RY0; -.
DR TreeFam; TF317658; -.
DR PathwayCommons; Q17RY0; -.
DR SignaLink; Q17RY0; -.
DR BioGRID-ORCS; 80315; 20 hits in 1090 CRISPR screens.
DR ChiTaRS; CPEB4; human.
DR GenomeRNAi; 80315; -.
DR Pharos; Q17RY0; Tbio.
DR PRO; PR:Q17RY0; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q17RY0; protein.
DR Bgee; ENSG00000113742; Expressed in adrenal tissue and 190 other tissues.
DR ExpressionAtlas; Q17RY0; baseline and differential.
DR Genevisible; Q17RY0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0036294; P:cellular response to decreased oxygen levels; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.640.40; -; 1.
DR InterPro; IPR032296; CEBP_ZZ.
DR InterPro; IPR038446; CEBP_ZZ_sf.
DR InterPro; IPR034819; CPEB.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR12566; PTHR12566; 1.
DR Pfam; PF16366; CEBP_ZZ; 1.
DR Pfam; PF16367; RRM_7; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW Endoplasmic reticulum; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Synapse; Zinc.
FT CHAIN 1..729
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 4"
FT /id="PRO_0000269264"
FT DOMAIN 472..563
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 580..662
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 20..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..543
FT /note="RNA-binding"
FT /evidence="ECO:0007744|PDB:5DIF"
FT COMPBIAS 33..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 667
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 684
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 689
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 694
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 697
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 702
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT SITE 473
FT /note="RNA-binding"
FT /evidence="ECO:0007744|PDB:5DIF"
FT SITE 561
FT /note="Important for the positionning of RRM1 relative to
FT RRM2"
FT /evidence="ECO:0000269|PubMed:24990967"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..382
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022040"
FT VAR_SEQ 403..419
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11214970,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022041"
FT VAR_SEQ 404..428
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022042"
FT CONFLICT 228
FT /note="P -> L (in Ref. 2; CAD98072)"
FT /evidence="ECO:0000305"
FT HELIX 384..391
FT /evidence="ECO:0007829|PDB:5DIF"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:2MKI"
FT HELIX 485..491
FT /evidence="ECO:0007829|PDB:2MKI"
FT HELIX 492..495
FT /evidence="ECO:0007829|PDB:2MKI"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:2MKI"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:2MKJ"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:2MKI"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:2MKI"
FT HELIX 527..533
FT /evidence="ECO:0007829|PDB:2MKI"
FT STRAND 534..538
FT /evidence="ECO:0007829|PDB:2MKI"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:2MKI"
FT STRAND 556..560
FT /evidence="ECO:0007829|PDB:2MKI"
FT STRAND 563..572
FT /evidence="ECO:0007829|PDB:2MKI"
FT STRAND 580..586
FT /evidence="ECO:0007829|PDB:2MKI"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:2MKJ"
FT HELIX 593..603
FT /evidence="ECO:0007829|PDB:2MKI"
FT STRAND 607..615
FT /evidence="ECO:0007829|PDB:2MKI"
FT TURN 616..619
FT /evidence="ECO:0007829|PDB:2MKI"
FT STRAND 620..631
FT /evidence="ECO:0007829|PDB:2MKI"
FT HELIX 632..638
FT /evidence="ECO:0007829|PDB:2MKI"
FT STRAND 639..643
FT /evidence="ECO:0007829|PDB:2MKI"
FT STRAND 645..648
FT /evidence="ECO:0007829|PDB:2MKJ"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:2MKJ"
FT STRAND 656..659
FT /evidence="ECO:0007829|PDB:2MKI"
SQ SEQUENCE 729 AA; 80152 MW; B71AAB0650E8CB13 CRC64;
MGDYGFGVLV QSNTGNKSAF PVRFHPHLQP PHHHQNATPS PAAFINNNTA ANGSSAGSAW
LFPAPATHNI QDEILGSEKA KSQQQEQQDP LEKQQLSPSP GQEAGILPET EKAKSEENQG
DNSSENGNGK EKIRIESPVL TGFDYQEATG LGTSTQPLTS SASSLTGFSN WSAAIAPSSS
TIINEDASFF HQGGVPAASA NNGALLFQNF PHHVSPGFGG SFSPQIGPLS QHHPHHPHFQ
HHHSQHQQQR RSPASPHPPP FTHRNAAFNQ LPHLANNLNK PPSPWSSYQS PSPTPSSSWS
PGGGGYGGWG GSQGRDHRRG LNGGITPLNS ISPLKKNFAS NHIQLQKYAR PSSAFAPKSW
MEDSLNRADN IFPFPDRPRT FDMHSLESSL IDIMRAENDT IKGRLNYSYP GSDSSLLINA
RTYGRRRGQS SLFPMEDGFL DDGRGDQPLH SGLGSPHCFS HQNGERVERY SRKVFVGGLP
PDIDEDEITA SFRRFGPLIV DWPHKAESKS YFPPKGYAFL LFQDESSVQA LIDACIEEDG
KLYLCVSSPT IKDKPVQIRP WNLSDSDFVM DGSQPLDPRK TIFVGGVPRP LRAVELAMIM
DRLYGGVCYA GIDTDPELKY PKGAGRVAFS NQQSYIAAIS ARFVQLQHGE IDKRVEVKPY
VLDDQLCDEC QGARCGGKFA PFFCANVTCL QYYCEYCWAA IHSRAGREFH KPLVKEGGDR
PRHISFRWN
