DIP2B_HUMAN
ID DIP2B_HUMAN Reviewed; 1576 AA.
AC Q9P265; Q6B011; Q8N1L5; Q8NB38;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Disco-interacting protein 2 homolog B;
DE Short=DIP2 homolog B;
GN Name=DIP2B; Synonyms=KIAA1463;
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 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-372 AND 764-1576.
RC TISSUE=Brain, and Synovium;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-372.
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 411-1576, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=17236128; DOI=10.1086/510800;
RA Winnepenninckx B., Debacker K., Ramsay J., Smeets D., Smits A.,
RA FitzPatrick D.R., Kooy R.F.;
RT "CGG-repeat expansion in the DIP2B gene is associated with the fragile site
RT FRA12A on chromosome 12q13.1.";
RL Am. J. Hum. Genet. 80:221-231(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-53; THR-71; SER-100;
RP THR-140; SER-146 AND SER-148, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND SER-100, AND
RP 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-53; SER-100; SER-178;
RP SER-193; SER-203 AND SER-259, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
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).
CC -!- FUNCTION: Negatively regulates axonal outgrowth and is essential for
CC normal synaptic transmission. Not required for regulation of axon
CC polarity. Promotes acetylation of alpha-tubulin.
CC {ECO:0000250|UniProtKB:Q3UH60}.
CC -!- SUBUNIT: Interacts with alpha-tubulin. {ECO:0000250|UniProtKB:Q3UH60}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q3UH60}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q3UH60}. Perikaryon
CC {ECO:0000250|UniProtKB:Q3UH60}.
CC -!- TISSUE SPECIFICITY: Moderately expressed in adult brain, placenta,
CC skeletal muscle, heart, kidney, pancreas, lung, spleen and colon.
CC Expression was weaker in adult liver, kidney, spleen, and ovary, and in
CC fetal brain and liver. In the brain, it is expressed in the cerebral
CC cortex; the frontal, parietal, occipital and temporal lobes; the
CC paracentral gyrus; the pons; the corpus callosum and the hippocampus.
CC Highest expression levels in the brain were found in the cerebral
CC cortex and the frontal and parietal lobes.
CC {ECO:0000269|PubMed:10819331, ECO:0000269|PubMed:17236128}.
CC -!- SIMILARITY: Belongs to the DIP2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH75027.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC Sequence=BAC03705.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC Sequence=BAC05025.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW58149.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC078818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58149.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK091597; BAC03705.1; ALT_SEQ; mRNA.
DR EMBL; AK097369; BAC05025.1; ALT_INIT; mRNA.
DR EMBL; BC075027; AAH75027.1; ALT_SEQ; mRNA.
DR EMBL; AB040896; BAA95987.2; -; mRNA.
DR CCDS; CCDS31799.1; -.
DR RefSeq; NP_775873.2; NM_173602.2.
DR AlphaFoldDB; Q9P265; -.
DR SMR; Q9P265; -.
DR BioGRID; 121656; 48.
DR IntAct; Q9P265; 12.
DR STRING; 9606.ENSP00000301180; -.
DR iPTMnet; Q9P265; -.
DR PhosphoSitePlus; Q9P265; -.
DR BioMuta; DIP2B; -.
DR DMDM; 172044681; -.
DR EPD; Q9P265; -.
DR jPOST; Q9P265; -.
DR MassIVE; Q9P265; -.
DR MaxQB; Q9P265; -.
DR PaxDb; Q9P265; -.
DR PeptideAtlas; Q9P265; -.
DR PRIDE; Q9P265; -.
DR ProteomicsDB; 83736; -.
DR Antibodypedia; 55127; 39 antibodies from 14 providers.
DR DNASU; 57609; -.
DR Ensembl; ENST00000301180.10; ENSP00000301180.5; ENSG00000066084.13.
DR GeneID; 57609; -.
DR KEGG; hsa:57609; -.
DR MANE-Select; ENST00000301180.10; ENSP00000301180.5; NM_173602.3; NP_775873.2.
DR UCSC; uc001rwv.4; human.
DR CTD; 57609; -.
DR DisGeNET; 57609; -.
DR GeneCards; DIP2B; -.
DR HGNC; HGNC:29284; DIP2B.
DR HPA; ENSG00000066084; Tissue enhanced (brain).
DR MalaCards; DIP2B; -.
DR MIM; 611379; gene.
DR neXtProt; NX_Q9P265; -.
DR OpenTargets; ENSG00000066084; -.
DR PharmGKB; PA143485449; -.
DR VEuPathDB; HostDB:ENSG00000066084; -.
DR eggNOG; KOG3628; Eukaryota.
DR GeneTree; ENSGT00950000182997; -.
DR HOGENOM; CLU_001345_0_0_1; -.
DR InParanoid; Q9P265; -.
DR OMA; VPVCTAT; -.
DR OrthoDB; 539697at2759; -.
DR PhylomeDB; Q9P265; -.
DR TreeFam; TF312871; -.
DR PathwayCommons; Q9P265; -.
DR SignaLink; Q9P265; -.
DR BioGRID-ORCS; 57609; 21 hits in 1075 CRISPR screens.
DR ChiTaRS; DIP2B; human.
DR GenomeRNAi; 57609; -.
DR Pharos; Q9P265; Tdark.
DR PRO; PR:Q9P265; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9P265; protein.
DR Bgee; ENSG00000066084; Expressed in inferior vagus X ganglion and 189 other tissues.
DR ExpressionAtlas; Q9P265; baseline and differential.
DR Genevisible; Q9P265; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:2000758; P:positive regulation of peptidyl-lysine acetylation; ISS:UniProtKB.
DR CDD; cd05905; Dip2; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.12780; -; 2.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR037337; Dip2-like_dom.
DR InterPro; IPR010506; DMAP1-bd.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF06464; DMAP_binding; 1.
DR SMART; SM01137; DMAP_binding; 1.
DR PROSITE; PS51912; DMAP1_BIND; 1.
PE 1: Evidence at protein level;
KW Cell projection; Neurogenesis; Phosphoprotein; Reference proteome.
FT CHAIN 1..1576
FT /note="Disco-interacting protein 2 homolog B"
FT /id="PRO_0000318736"
FT DOMAIN 12..131
FT /note="DMAP1-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT REGION 31..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH60"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 792
FT /note="I -> V (in dbSNP:rs11169525)"
FT /id="VAR_038861"
FT CONFLICT 216
FT /note="F -> L (in Ref. 3; BAC03705)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="S -> P (in Ref. 3; BAC03705)"
FT /evidence="ECO:0000305"
FT CONFLICT 1432
FT /note="W -> R (in Ref. 3; BAC05025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1576 AA; 171492 MW; 351AC2C3E4B72E31 CRC64;
MAERGLEPSP AAVAALPPEV RAQLAELELE LSEGDITQKG YEKKRSKLLS PYSPQTQETD
SAVQKELRNQ TPAPSAAQTS APSKYHRTRS GGARDERYRS DIHTEAVQAA LAKHKEQKMA
LPMPTKRRST FVQSPADACT PPDTSSASED EGSLRRQAAL SAALQQSLQN AESWINRSIQ
GSSTSSSASS TLSHGEVKGT SGSLADVFAN TRIENFSAPP DVTTTTSSSS SSSSIRPANI
DLPPSGIVKG MHKGSNRSSL MDTADGVPVS SRVSTKIQQL LNTLKRPKRP PLKEFFVDDS
EEIVEVPQPD PNQPKPEGRQ MTPVKGEPLG VICNWPPALE SALQRWGTTQ AKCSCLTALD
MTGKPVYTLT YGKLWSRSLK LAYTLLNKLG TKNEPVLKPG DRVALVYPNN DPVMFMVAFY
GCLLAEVIPV PIEVPLTRKD AGGQQIGFLL GSCGIALALT SEVCLKGLPK TQNGEIVQFK
GWPRLKWVVT DSKYLSKPPK DWQPHISPAG TEPAYIEYKT SKEGSVMGVT VSRLAMLSHC
QALSQACNYS EGETIVNVLD FKKDAGLWHG MFANVMNKMH TISVPYSVMK TCPLSWVQRV
HAHKAKVALV KCRDLHWAMM AHRDQRDVSL SSLRMLIVTD GANPWSVSSC DAFLSLFQSH
GLKPEAICPC ATSAEAMTVA IRRPGVPGAP LPGRAILSMN GLSYGVIRVN TEDKNSALTV
QDVGHVMPGG MMCIVKPDGP PQLCKTDEIG EICVSSRTGG MMYFGLAGVT KNTFEVIPVN
SAGSPVGDVP FIRSGLLGFV GPGSLVFVVG KMDGLLMVSG RRHNADDIVA TGLAVESIKT
VYRGRIAVFS VSVFYDERIV VVAEQRPDAS EEDSFQWMSR VLQAIDSIHQ VGVYCLALVP
ANTLPKTPLG GIHISQTKQL FLEGSLHPCN ILMCPHTCVT NLPKPRQKQP GVGPASVMVG
NLVAGKRIAQ AAGRDLGQIE ENDLVRKHQF LAEILQWRAQ ATPDHVLFML LNAKGTTVCT
ASCLQLHKRA ERIASVLGDK GHLNAGDNVV LLYPPGIELI AAFYGCLYAG CIPVTVRPPH
AQNLTATLPT VRMIVDVSKA ACILTSQTLM RLLRSREAAA AVDVKTWPTI IDTDDLPRKR
LPQLYKPPTP EMLAYLDFSV STTGMLTGVK MSHSAVNALC RAIKLQCELY SSRQIAICLD
PYCGLGFALW CLCSVYSGHQ SVLIPPMELE NNLFLWLSTV NQYKIRDTFC SYSVMELCTK
GLGNQVEVLK TRGINLSCVR TCVVVAEERP RVALQQSFSK LFKDIGLSPR AVSTTFGSRV
NVAICLQGTS GPDPTTVYVD LKSLRHDRVR LVERGAPQSL LLSESGKILP GVKVVIVNPE
TKGPVGDSHL GEIWVNSPHT ASGYYTIYDS ETLQADHFNT RLSFGDAAQT LWARTGYLGF
VRRTELTAAT GERHDALYVV GALDETLELR GLRYHPIDIE TSVSRIHRSI AECAVFTWTN
LLVVVVELCG SEQEALDLVP LVTNVVLEEH YLIVGVVVVV DPGVIPINSR GEKQRMHLRD
SFLADQLDPI YVAYNM
