ID TRAM1_HUMAN Reviewed; 374 AA. AC Q15629; B4E0K2; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 188. DE RecName: Full=Translocating chain-associated membrane protein 1 {ECO:0000303|PubMed:19121997}; DE Short=Protein TRAM1 {ECO:0000303|PubMed:19121997}; GN Name=TRAM1 {ECO:0000312|HGNC:HGNC:20568}; GN Synonyms=TRAM {ECO:0000303|PubMed:8616892}; 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), FUNCTION, SUBCELLULAR LOCATION, AND RP GLYCOSYLATION. RX PubMed=1315422; DOI=10.1038/357047a0; RA Goerlich D., Hartmann E., Prehn S., Rapoport T.A.; RT "A protein of the endoplasmic reticulum involved early in polypeptide RT translocation."; RL Nature 357:47-52(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Thymus; 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=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Kidney; 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 SUBCELLULAR LOCATION. RX PubMed=8616892; DOI=10.1016/s0092-8674(00)81115-0; RA Do H., Falcone D., Lin J., Andrews D.W., Johnson A.E.; RT "The cotranslational integration of membrane proteins into the phospholipid RT bilayer is a multistep process."; RL Cell 85:369-378(1996). RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=9506517; DOI=10.1016/s0092-8674(00)81130-7; RA Hegde R.S., Voigt S., Rapoport T.A., Lingappa V.R.; RT "TRAM regulates the exposure of nascent secretory proteins to the cytosol RT during translocation into the endoplasmic reticulum."; RL Cell 92:621-631(1998). RN [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12475939; DOI=10.1091/mbc.e02-04-0198; RA Meacock S.L., Lecomte F.J., Crawshaw S.G., High S.; RT "Different transmembrane domains associate with distinct endoplasmic RT reticulum components during membrane integration of a polytopic protein."; RL Mol. Biol. Cell 13:4114-4129(2002). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY RP 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY RP 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 [11] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SEC61B AND DERL1, RP INTERACTION WITH HHV-5 PROTEINS US2 AND US11 (MICROBIAL INFECTION), AND RP GLYCOSYLATION. RX PubMed=19121997; DOI=10.1074/jbc.m807568200; RA Oresic K., Ng C.L., Tortorella D.; RT "TRAM1 participates in human cytomegalovirus US2- and US11-mediated RT dislocation of an endoplasmic reticulum membrane glycoprotein."; RL J. Biol. Chem. 284:5905-5914(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, 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 FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY ER STRESS. RX PubMed=20430023; DOI=10.1016/j.yexcr.2010.04.010; RA Ng C.L., Oresic K., Tortorella D.; RT "TRAM1 is involved in disposal of ER membrane degradation substrates."; RL Exp. Cell Res. 316:2113-2122(2010). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY RP 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 [15] 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY RP 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 [17] RP FUNCTION. RX PubMed=32013668; DOI=10.1080/19336950.2020.1724759; RA Klein M.C., Lerner M., Nguyen D., Pfeffer S., Dudek J., Foerster F., RA Helms V., Lang S., Zimmermann R.; RT "TRAM1 protein may support ER protein import by modulating the phospholipid RT bilayer near the lateral gate of the Sec61-channel."; RL Channels 14:28-44(2020). CC -!- FUNCTION: Involved in the translocation of nascent protein chains into CC or through the endoplasmic reticulum (ER) membrane by facilitating the CC proper chain positioning at the SEC61 channel (PubMed:1315422, CC PubMed:8616892, PubMed:9506517, PubMed:12475939, PubMed:32013668). CC Regulates the exposure of nascent secretory protein chain to the CC cytosol during translocation into the ER (PubMed:9506517). May affect CC the phospholipid bilayer in the vicinity of the lateral gate of the CC SEC61 channel, thereby facilitating ER protein transport CC (PubMed:32013668). Intimately associates with transmembrane (TM) domain CC of nascent membrane proteins during the entire integration process into CC the ER membrane (PubMed:8616892). Associates with the second TM domain CC of G-protein-coupled receptor opsin/OPSD nascent chain in the ER CC membrane, which may facilitate its integration into the membrane CC (PubMed:12475939). Under conditions of ER stress, participates in the CC disposal of misfolded ER membrane proteins during the unfolded protein CC response (UPR), an integrated stress response (ISR) pathway, by CC selectively retrotranslocating misfolded ER-membrane proteins from the CC ER into the cytosol where they are ubiquitinated and degraded by the CC proteasome (PubMed:20430023). {ECO:0000269|PubMed:12475939, CC ECO:0000269|PubMed:1315422, ECO:0000269|PubMed:20430023, CC ECO:0000269|PubMed:32013668, ECO:0000269|PubMed:8616892, CC ECO:0000269|PubMed:9506517, ECO:0000303|PubMed:32013668}. CC -!- FUNCTION: (Microbial infection) In case of cytomegalovirus infection, CC participates in US2- and US11-mediated ER-to-cytosol retrotranslocation CC and subsequent degradation of major histocompatibility complex (MHC) CC class I heavy chains, thereby decreasing the immune detection by CC cytotoxic T-cells. {ECO:0000269|PubMed:19121997}. CC -!- SUBUNIT: Interacts with SEC61B (PubMed:19121997). May interact with CC Derlin-1/DERL1 (PubMed:19121997). {ECO:0000269|PubMed:19121997}. CC -!- SUBUNIT: (Microbial infection) Interacts with human CC cytomegalovirus/HHV-5 proteins US2 and US11. CC {ECO:0000269|PubMed:19121997}. CC -!- INTERACTION: CC Q15629; P51572: BCAP31; NbExp=5; IntAct=EBI-1788852, EBI-77683; CC Q15629; Q02747: GUCA2A; NbExp=3; IntAct=EBI-1788852, EBI-12244272; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:12475939, ECO:0000269|PubMed:1315422, CC ECO:0000269|PubMed:20430023, ECO:0000269|PubMed:8616892, CC ECO:0000269|PubMed:9506517}; Multi-pass membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q15629-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15629-2; Sequence=VSP_056213; CC -!- INDUCTION: Up-regulated upon endoplasmic reticulum stress. CC {ECO:0000269|PubMed:20430023}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:1315422, CC ECO:0000269|PubMed:19121997}. CC -!- SIMILARITY: Belongs to the TRAM 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; X63679; CAA45218.1; -; mRNA. DR EMBL; AK303411; BAG64464.1; -; mRNA. DR EMBL; AC022731; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC120194; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000687; AAH00687.1; -; mRNA. DR EMBL; BC037738; AAH37738.1; -; mRNA. DR CCDS; CCDS6207.1; -. [Q15629-1] DR PIR; S30034; S30034. DR RefSeq; NP_001304733.1; NM_001317804.1. [Q15629-2] DR RefSeq; NP_001304734.1; NM_001317805.1. DR RefSeq; NP_055109.1; NM_014294.5. [Q15629-1] DR AlphaFoldDB; Q15629; -. DR BioGRID; 117032; 72. DR DIP; DIP-45978N; -. DR IntAct; Q15629; 31. DR MINT; Q15629; -. DR STRING; 9606.ENSP00000262213; -. DR TCDB; 9.B.311.2.1; the 6-7 tms tram-lag (tram-lag) family. DR GlyConnect; 1838; 1 N-Linked glycan (1 site). DR GlyCosmos; Q15629; 2 sites, 1 glycan. DR GlyGen; Q15629; 3 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q15629; -. DR PhosphoSitePlus; Q15629; -. DR SwissPalm; Q15629; -. DR BioMuta; TRAM1; -. DR DMDM; 18202507; -. DR EPD; Q15629; -. DR jPOST; Q15629; -. DR MassIVE; Q15629; -. DR MaxQB; Q15629; -. DR PaxDb; 9606-ENSP00000262213; -. DR PeptideAtlas; Q15629; -. DR ProteomicsDB; 5680; -. DR ProteomicsDB; 60664; -. [Q15629-1] DR Pumba; Q15629; -. DR TopDownProteomics; Q15629-1; -. [Q15629-1] DR Antibodypedia; 12213; 171 antibodies from 28 providers. DR DNASU; 23471; -. DR Ensembl; ENST00000262213.7; ENSP00000262213.2; ENSG00000067167.8. [Q15629-1] DR GeneID; 23471; -. DR KEGG; hsa:23471; -. DR MANE-Select; ENST00000262213.7; ENSP00000262213.2; NM_014294.6; NP_055109.1. DR AGR; HGNC:20568; -. DR CTD; 23471; -. DR DisGeNET; 23471; -. DR GeneCards; TRAM1; -. DR HGNC; HGNC:20568; TRAM1. DR HPA; ENSG00000067167; Low tissue specificity. DR MIM; 605190; gene. DR neXtProt; NX_Q15629; -. DR OpenTargets; ENSG00000067167; -. DR PharmGKB; PA134955644; -. DR VEuPathDB; HostDB:ENSG00000067167; -. DR eggNOG; KOG1608; Eukaryota. DR GeneTree; ENSGT00510000046470; -. DR HOGENOM; CLU_062830_0_0_1; -. DR InParanoid; Q15629; -. DR OMA; CAVFFYF; -. DR OrthoDB; 5402309at2759; -. DR PhylomeDB; Q15629; -. DR TreeFam; TF314319; -. DR PathwayCommons; Q15629; -. DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane. DR SignaLink; Q15629; -. DR BioGRID-ORCS; 23471; 17 hits in 1155 CRISPR screens. DR ChiTaRS; TRAM1; human. DR GenomeRNAi; 23471; -. DR Pharos; Q15629; Tbio. DR PRO; PR:Q15629; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q15629; Protein. DR Bgee; ENSG00000067167; Expressed in choroid plexus epithelium and 216 other cell types or tissues. DR ExpressionAtlas; Q15629; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0006613; P:cotranslational protein targeting to membrane; IDA:UniProtKB. DR GO; GO:0045048; P:protein insertion into ER membrane; IDA:UniProtKB. DR GO; GO:0006986; P:response to unfolded protein; IMP:UniProtKB. DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IEA:InterPro. DR InterPro; IPR006634; TLC-dom. DR InterPro; IPR016447; Translocation_assoc_membrane. DR PANTHER; PTHR12371:SF3; TRANSLOCATING CHAIN-ASSOCIATED MEMBRANE PROTEIN 1; 1. DR PANTHER; PTHR12371; TRANSLOCATION ASSOCIATED MEMBRANE PROTEIN; 1. DR Pfam; PF03798; TRAM_LAG1_CLN8; 1. DR PIRSF; PIRSF005449; Translocation_assoc_membrane; 1. DR SMART; SM00724; TLC; 1. DR PROSITE; PS50922; TLC; 1. DR Genevisible; Q15629; HS. PE 1: Evidence at protein level; KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; KW Host-virus interaction; Membrane; Phosphoprotein; Protein transport; KW Reference proteome; Translocation; Transmembrane; Transmembrane helix; KW Transport; Unfolded protein response. FT CHAIN 1..374 FT /note="Translocating chain-associated membrane protein 1" FT /id="PRO_0000185530" FT TOPO_DOM 1..29 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q91V04" FT TRANSMEM 30..50 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 51..76 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q91V04" FT TRANSMEM 77..97 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 98..121 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q91V04" FT TRANSMEM 122..142 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 143..159 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q91V04" FT TRANSMEM 160..180 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 181..192 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q91V04" FT TRANSMEM 193..213 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 214..217 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q91V04" FT TRANSMEM 218..238 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 239..251 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q91V04" FT TRANSMEM 252..272 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 273..297 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q91V04" FT TRANSMEM 298..318 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 319..374 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q91V04" FT DOMAIN 117..326 FT /note="TLC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205" FT REGION 334..374 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 345..364 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 365 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT CARBOHYD 56 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..31 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056213" SQ SEQUENCE 374 AA; 43072 MW; 9232ADA33DE20076 CRC64; MAIRKKSTKS PPVLSHEFVL QNHADIVSCV AMVFLLGLMF EITAKASIIF VTLQYNVTLP ATEEQATESV SLYYYGIKDL ATVFFYMLVA IIIHAVIQEY MLDKINRRMH FSKTKHSKFN ESGQLSAFYL FACVWGTFIL ISENYISDPT ILWRAYPHNL MTFQMKFFYI SQLAYWLHAF PELYFQKTKK EDIPRQLVYI GLYLFHIAGA YLLNLNHLGL VLLVLHYFVE FLFHISRLFY FSNEKYQKGF SLWAVLFVLG RLLTLILSVL TVGFGLARAE NQKLDFSTGN FNVLAVRIAV LASICVTQAF MMWKFINFQL RRWREHSAFQ APAVKKKPTV TKGRSSKKGT ENGVNGTLTS NVADSPRNKK EKSS //