DCP1B_HUMAN
ID DCP1B_HUMAN Reviewed; 617 AA.
AC Q8IZD4; B4DRD1; Q86XH9; Q96BP8; Q96MZ8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=mRNA-decapping enzyme 1B;
DE EC=3.6.1.62 {ECO:0000250|UniProtKB:Q9NPI6};
GN Name=DCP1B;
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), AND INTERACTION WITH DCP1A.
RX PubMed=12417715; DOI=10.1128/mcb.22.23.8114-8121.2002;
RA Lykke-Andersen J.;
RT "Identification of a human decapping complex associated with hUpf proteins
RT in nonsense-mediated decay.";
RL Mol. Cell. Biol. 22:8114-8121(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis, and Uterus;
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 SUBCELLULAR LOCATION, AND INTERACTION WITH DCP1A.
RX PubMed=15067023; DOI=10.1083/jcb.200309008;
RA Cougot N., Babajko S., Seraphin B.;
RT "Cytoplasmic foci are sites of mRNA decay in human cells.";
RL J. Cell Biol. 165:31-40(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-191, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-511, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; SER-275; THR-392;
RP SER-448 AND SER-511, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: May play a role in the degradation of mRNAs, both in normal
CC mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7-
CC methyl guanine cap structure from mRNA molecules, yielding a 5'-
CC phosphorylated mRNA fragment and 7m-GDP (By similarity).
CC {ECO:0000250|UniProtKB:Q9NPI6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) +
CC N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692,
CC Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChEBI:CHEBI:156461;
CC EC=3.6.1.62; Evidence={ECO:0000250|UniProtKB:Q9NPI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC Evidence={ECO:0000250|UniProtKB:Q9NPI6};
CC -!- SUBUNIT: Interacts with DCP1A. {ECO:0000269|PubMed:12417715,
CC ECO:0000269|PubMed:15067023}.
CC -!- INTERACTION:
CC Q8IZD4; O95429: BAG4; NbExp=2; IntAct=EBI-521595, EBI-2949658;
CC Q8IZD4; Q9NPI6: DCP1A; NbExp=8; IntAct=EBI-521595, EBI-374238;
CC Q8IZD4; Q8IU60: DCP2; NbExp=3; IntAct=EBI-521595, EBI-521577;
CC Q8IZD4; Q96F86: EDC3; NbExp=8; IntAct=EBI-521595, EBI-997311;
CC Q8IZD4; Q92636: NSMAF; NbExp=2; IntAct=EBI-521595, EBI-2947053;
CC Q8IZD4; F4HZB2: SPI; Xeno; NbExp=2; IntAct=EBI-521595, EBI-3386960;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15067023}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NPI6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IZD4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZD4-2; Sequence=VSP_056044;
CC -!- SIMILARITY: Belongs to the DCP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15368.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY146652; AAN62764.1; -; mRNA.
DR EMBL; AK056200; BAB71118.1; -; mRNA.
DR EMBL; AK299203; BAG61243.1; -; mRNA.
DR EMBL; AC005342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015368; AAH15368.2; ALT_INIT; mRNA.
DR EMBL; BC043437; AAH43437.1; -; mRNA.
DR CCDS; CCDS31727.1; -. [Q8IZD4-1]
DR RefSeq; NP_689853.3; NM_152640.4. [Q8IZD4-1]
DR RefSeq; XP_011519229.1; XM_011520927.2. [Q8IZD4-2]
DR AlphaFoldDB; Q8IZD4; -.
DR SMR; Q8IZD4; -.
DR BioGRID; 128216; 93.
DR DIP; DIP-31289N; -.
DR IntAct; Q8IZD4; 39.
DR MINT; Q8IZD4; -.
DR STRING; 9606.ENSP00000280665; -.
DR GlyGen; Q8IZD4; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q8IZD4; -.
DR PhosphoSitePlus; Q8IZD4; -.
DR BioMuta; DCP1B; -.
DR DMDM; 317373353; -.
DR EPD; Q8IZD4; -.
DR jPOST; Q8IZD4; -.
DR MassIVE; Q8IZD4; -.
DR MaxQB; Q8IZD4; -.
DR PaxDb; Q8IZD4; -.
DR PeptideAtlas; Q8IZD4; -.
DR PRIDE; Q8IZD4; -.
DR ProteomicsDB; 4941; -.
DR ProteomicsDB; 71329; -. [Q8IZD4-1]
DR Antibodypedia; 22113; 171 antibodies from 25 providers.
DR DNASU; 196513; -.
DR Ensembl; ENST00000280665.11; ENSP00000280665.6; ENSG00000151065.14. [Q8IZD4-1]
DR Ensembl; ENST00000647122.2; ENSP00000494635.1; ENSG00000284850.2. [Q8IZD4-1]
DR GeneID; 196513; -.
DR KEGG; hsa:196513; -.
DR MANE-Select; ENST00000280665.11; ENSP00000280665.6; NM_152640.5; NP_689853.3.
DR UCSC; uc001qjx.2; human. [Q8IZD4-1]
DR CTD; 196513; -.
DR DisGeNET; 196513; -.
DR GeneCards; DCP1B; -.
DR HGNC; HGNC:24451; DCP1B.
DR HPA; ENSG00000151065; Low tissue specificity.
DR MIM; 609843; gene.
DR neXtProt; NX_Q8IZD4; -.
DR OpenTargets; ENSG00000151065; -.
DR PharmGKB; PA134889143; -.
DR VEuPathDB; HostDB:ENSG00000151065; -.
DR eggNOG; KOG2868; Eukaryota.
DR GeneTree; ENSGT00940000158409; -.
DR HOGENOM; CLU_030030_2_0_1; -.
DR InParanoid; Q8IZD4; -.
DR OMA; GHQAHGK; -.
DR OrthoDB; 1509316at2759; -.
DR PhylomeDB; Q8IZD4; -.
DR TreeFam; TF320504; -.
DR PathwayCommons; Q8IZD4; -.
DR Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
DR SignaLink; Q8IZD4; -.
DR BioGRID-ORCS; 196513; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; DCP1B; human.
DR GeneWiki; DCP1B; -.
DR GenomeRNAi; 196513; -.
DR Pharos; Q8IZD4; Tdark.
DR PRO; PR:Q8IZD4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8IZD4; protein.
DR Bgee; ENSG00000151065; Expressed in muscle layer of sigmoid colon and 101 other tissues.
DR ExpressionAtlas; Q8IZD4; baseline and differential.
DR Genevisible; Q8IZD4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010334; Dcp1.
DR InterPro; IPR031953; mRNA_decap_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16290; PTHR16290; 1.
DR Pfam; PF06058; DCP1; 1.
DR Pfam; PF16741; mRNA_decap_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Hydrolase;
KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..617
FT /note="mRNA-decapping enzyme 1B"
FT /id="PRO_0000402799"
FT REGION 195..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 191
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 392
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..107
FT /note="MAAVAAGGLVGKGRDISLAALQRHDPYINRIVDVASQVALYTFGHRANEWEK
FT TDVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQLQDPFLLYRNARL ->
FT MQIKV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056044"
FT VARIANT 195
FT /note="N -> D (in dbSNP:rs12423058)"
FT /id="VAR_047395"
FT VARIANT 216
FT /note="N -> S (in dbSNP:rs34730825)"
FT /id="VAR_047396"
FT VARIANT 301
FT /note="S -> T (in dbSNP:rs2470449)"
FT /id="VAR_047397"
FT VARIANT 344
FT /note="R -> H (in dbSNP:rs715146)"
FT /id="VAR_047398"
FT CONFLICT 251
FT /note="H -> HQ (in Ref. 1; AAN62764, 2; BAB71118 and 4;
FT AAH15368/AAH43437)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="Q -> R (in Ref. 2; BAB71118)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="P -> A (in Ref. 4; AAH43437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 67723 MW; 00B9D9592BAC3B64 CRC64;
MAAVAAGGLV GKGRDISLAA LQRHDPYINR IVDVASQVAL YTFGHRANEW EKTDVEGTLF
VYTRSASPKH GFTIMNRLSM ENRTEPITKD LDFQLQDPFL LYRNARLSIY GIWFYDKEEC
QRIAELMKNL TQYEQLKAHQ GTGAGISPVI LNSGEGKEVD ILRMLIKAKD EYTKCKTCSE
PKKITSSSAI YDNPNLIKPI PVKPSENQQQ RIPQPNQTLD PEPQHLSLTA LFGKQDKATC
QETVEPPQTL HQQQQQQQQQ QEKLPIRQGV VRSLSYEEPR RHSPPIEKQL CPAIQKLMVR
SADLHPLSEL PENRPCENGS THSAGEFFTG PVQPGSPHNI GTSRGVQNAS RTQNLFEKLQ
STPGAANKCD PSTPAPASSA ALNRSRAPTS VTPVAPGKGL AQPPQAYFNG SLPPQTVGHQ
AHGREQSTLP RQTLPISGSQ TGSSGVISPQ ELLKKLQIVQ QEQQLHASNR PALAAKFPVL
AQSSGTGKPL ESWINKTPNT EQQTPLFQVI SPQRIPATAA PSLLMSPMVF AQPTSVPPKE
RESGLLPVGG QEPPAAATSL LLPIQSPEPS VITSSPLTKL QLQEALLYLI QNDDNFLNII
YEAYLFSMTQ AAMKKTM
