TRAD1_HUMAN
ID TRAD1_HUMAN Reviewed; 582 AA.
AC O14545; A8K5L6; B4DI89;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=TRAF-type zinc finger domain-containing protein 1;
DE AltName: Full=Protein FLN29;
GN Name=TRAFD1; Synonyms=FLN29;
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).
RC TISSUE=Brain;
RA Nezu J.;
RT "TRAF interacting Zn finger protein.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus, and Tongue;
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=Skin;
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 FUNCTION, AND INTERACTION WITH TRAF6.
RX PubMed=16221674; DOI=10.1074/jbc.m508221200;
RA Mashima R., Saeki K., Aki D., Minoda Y., Takaki H., Sanada T.,
RA Kobayashi T., Aburatani H., Yamanashi Y., Yoshimura A.;
RT "FLN29, a novel interferon- and LPS-inducible gene acting as a negative
RT regulator of toll-like receptor signaling.";
RL J. Biol. Chem. 280:41289-41297(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-415 AND SER-470, 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-415, 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-327 AND SER-415, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-278; SER-327;
RP SER-409; SER-415 AND SER-430, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-327; SER-409 AND
RP SER-415, AND 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 [19]
RP STRUCTURE BY NMR OF 78-139 IN COMPLEX WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZF-TRAF domain of FLN29 gene product.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Negative feedback regulator that controls excessive innate
CC immune responses. Regulates both Toll-like receptor 4 (TLR4) and
CC DDX58/RIG1-like helicases (RLH) pathways. May inhibit the LTR pathway
CC by direct interaction with TRAF6 and attenuation of NF-kappa-B
CC activation. May negatively regulate the RLH pathway downstream from
CC MAVS and upstream of NF-kappa-B and IRF3 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16221674}.
CC -!- SUBUNIT: Interacts with MAVS, TICAM1, TRAF1, TRAF2, TRAF3 (By
CC similarity). Interacts with TRAF6. {ECO:0000250,
CC ECO:0000269|PubMed:16221674, ECO:0000269|Ref.19}.
CC -!- INTERACTION:
CC O14545; P42858: HTT; NbExp=5; IntAct=EBI-1396921, EBI-466029;
CC O14545; Q96IV0: NGLY1; NbExp=7; IntAct=EBI-1396921, EBI-6165879;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14545-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14545-2; Sequence=VSP_056085, VSP_056086;
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DR EMBL; AB007447; BAA22541.1; -; mRNA.
DR EMBL; AK291331; BAF84020.1; -; mRNA.
DR EMBL; AK295474; BAG58401.1; -; mRNA.
DR EMBL; AC073575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003553; AAH03553.1; -; mRNA.
DR CCDS; CCDS9160.1; -. [O14545-1]
DR RefSeq; NP_001137378.1; NM_001143906.1. [O14545-1]
DR RefSeq; NP_006691.1; NM_006700.2. [O14545-1]
DR PDB; 2D9K; NMR; -; A=78-139.
DR PDBsum; 2D9K; -.
DR AlphaFoldDB; O14545; -.
DR BMRB; O14545; -.
DR SMR; O14545; -.
DR BioGRID; 116112; 66.
DR IntAct; O14545; 38.
DR MINT; O14545; -.
DR STRING; 9606.ENSP00000257604; -.
DR GlyGen; O14545; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O14545; -.
DR PhosphoSitePlus; O14545; -.
DR BioMuta; TRAFD1; -.
DR EPD; O14545; -.
DR jPOST; O14545; -.
DR MassIVE; O14545; -.
DR MaxQB; O14545; -.
DR PaxDb; O14545; -.
DR PeptideAtlas; O14545; -.
DR PRIDE; O14545; -.
DR ProteomicsDB; 4284; -.
DR ProteomicsDB; 48080; -. [O14545-1]
DR Antibodypedia; 18647; 221 antibodies from 26 providers.
DR DNASU; 10906; -.
DR Ensembl; ENST00000257604.9; ENSP00000257604.5; ENSG00000135148.12. [O14545-1]
DR Ensembl; ENST00000412615.7; ENSP00000396526.2; ENSG00000135148.12. [O14545-1]
DR Ensembl; ENST00000552890.5; ENSP00000447340.1; ENSG00000135148.12. [O14545-2]
DR GeneID; 10906; -.
DR KEGG; hsa:10906; -.
DR MANE-Select; ENST00000412615.7; ENSP00000396526.2; NM_006700.3; NP_006691.1.
DR UCSC; uc001tto.4; human. [O14545-1]
DR CTD; 10906; -.
DR DisGeNET; 10906; -.
DR GeneCards; TRAFD1; -.
DR HGNC; HGNC:24808; TRAFD1.
DR HPA; ENSG00000135148; Low tissue specificity.
DR MIM; 613197; gene.
DR neXtProt; NX_O14545; -.
DR OpenTargets; ENSG00000135148; -.
DR PharmGKB; PA142670704; -.
DR VEuPathDB; HostDB:ENSG00000135148; -.
DR eggNOG; ENOG502QQRU; Eukaryota.
DR GeneTree; ENSGT00530000063869; -.
DR HOGENOM; CLU_034057_0_0_1; -.
DR InParanoid; O14545; -.
DR OMA; AHQSSEC; -.
DR PhylomeDB; O14545; -.
DR TreeFam; TF331416; -.
DR PathwayCommons; O14545; -.
DR SignaLink; O14545; -.
DR BioGRID-ORCS; 10906; 8 hits in 1078 CRISPR screens.
DR ChiTaRS; TRAFD1; human.
DR EvolutionaryTrace; O14545; -.
DR GeneWiki; TRAFD1; -.
DR GenomeRNAi; 10906; -.
DR Pharos; O14545; Tbio.
DR PRO; PR:O14545; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O14545; protein.
DR Bgee; ENSG00000135148; Expressed in secondary oocyte and 196 other tissues.
DR ExpressionAtlas; O14545; baseline and differential.
DR Genevisible; O14545; HS.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045824; P:negative regulation of innate immune response; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..582
FT /note="TRAF-type zinc finger domain-containing protein 1"
FT /id="PRO_0000278457"
FT ZN_FING 27..103
FT /note="TRAF-type"
FT REGION 217..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 134..164
FT /note="VCGREGEEKRNEVAIPPNAYDESWGQDGIWI -> LKNKRGRKGIEANSPPK
FT RVVKRVQTWTSCWP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056085"
FT VAR_SEQ 165..582
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056086"
FT CONFLICT 138
FT /note="E -> V (in Ref. 2; BAF84020)"
FT /evidence="ECO:0000305"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:2D9K"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:2D9K"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2D9K"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2D9K"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2D9K"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2D9K"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:2D9K"
SQ SEQUENCE 582 AA; 64841 MW; 4937682988851AC0 CRC64;
MAEFLDDQET RLCDNCKKEI PVFNFTIHEI HCQRNIGMCP TCKEPFPKSD METHMAAEHC
QVTCKCNKKL EKRLLKKHEE TECPLRLAVC QHCDLELSIL KLKEHEDYCG ARTELCGNCG
RNVLVKDLKT HPEVCGREGE EKRNEVAIPP NAYDESWGQD GIWIASQLLR QIEALDPPMR
LPRRPLRAFE SDVFHNRTTN QRNITAQVSI QNNLFEEQER QERNRGQQPP KEGGEESANL
DFMLALSLQN EGQASSVAEQ DFWRAVCEAD QSHGGPRSLS DIKGAADEIM LPCEFCEELY
PEELLIDHQT SCNPSRALPS LNTGSSSPRG VEEPDVIFQN FLQQAASNQL DSLMGLSNSH
PVEESIIIPC EFCGVQLEEE VLFHHQDQCD QRPATATNHV TEGIPRLDSQ PQETSPELPR
RRVRHQGDLS SGYLDDTKQE TANGPTSCLP PSRPINNMTA TYNQLSRSTS GPRPGCQPSS
PCVPKLSNSD SQDIQGRNRD SQNGAIAPGH VSVIRPPQNL YPENIVPSFS PGPSGRYGAS
GRSEGGRNSR VTPAAANYRS RTAKAKPSKQ QGAGDAEEEE EE
