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 27-MAR-2024, entry version 167. 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). RN [14] RP INTERACTION WITH ROTAVIRUS A NON-STRUCTURAL PROTEIN 2 (MICROBIAL RP INFECTION), AND INTERACTION WITH ROTAVIRUS A NON-STRUCTURAL PROTEIN 5 RP (MICROBIAL INFECTION). RX PubMed=30258011; DOI=10.1128/jvi.01363-18; RA Dhillon P., Rao C.D.; RT "Rotavirus Induces Formation of Remodeled Stress Granules and P Bodies and RT Their Sequestration in Viroplasms To Promote Progeny Virus Production."; RL J. Virol. 92:0-0(2018). 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 -!- SUBUNIT: (Microbial infection) Interacts with rotavirus A non- CC structural protein 2; this interaction probably plays a role in the CC sequestration of DCP1B in viral factories (PubMed:30258011). Interacts CC with rotavirus A non-structural protein 5; this interaction probably CC plays a role in its sequestration in viral factories (PubMed:30258011). CC {ECO:0000269|PubMed:30258011}. 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=9; 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; AAH15368.3; -; 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. DR AlphaFoldDB; Q8IZD4; -. DR SMR; Q8IZD4; -. DR BioGRID; 128216; 108. DR ComplexPortal; CPX-7341; RNA decapping and exonuclease complex, DCP1B variant. DR DIP; DIP-31289N; -. DR IntAct; Q8IZD4; 49. DR MINT; Q8IZD4; -. DR STRING; 9606.ENSP00000280665; -. DR GlyCosmos; Q8IZD4; 3 sites, 2 glycans. 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; 9606-ENSP00000280665; -. DR PeptideAtlas; Q8IZD4; -. DR ProteomicsDB; 4941; -. DR ProteomicsDB; 71329; -. [Q8IZD4-1] DR Pumba; Q8IZD4; -. DR Antibodypedia; 22113; 199 antibodies from 26 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 AGR; HGNC:24451; -. 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; IHPVGET; -. DR OrthoDB; 385293at2759; -. 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; 15 hits in 1156 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 103 other cell types or tissues. DR ExpressionAtlas; Q8IZD4; baseline and differential. 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:0140933; F:5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity; IEA:RHEA. DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro. 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 CDD; cd09804; Dcp1; 1. DR Gene3D; 6.10.140.2030; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR010334; Dcp1. DR InterPro; IPR031953; mRNA_decap_C. DR InterPro; IPR011993; PH-like_dom_sf. DR PANTHER; PTHR16290:SF5; MRNA-DECAPPING ENZYME 1B; 1. DR PANTHER; PTHR16290; TRANSCRIPTION FACTOR SMIF DECAPPING ENZYME DCP1; 1. DR Pfam; PF06058; DCP1; 1. DR Pfam; PF16741; mRNA_decap_C; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR Genevisible; Q8IZD4; HS. 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 //