ID SSRA_HUMAN Reviewed; 286 AA. AC P43307; A8K685; Q53GX2; Q53H19; Q5TAM3; Q6IB43; Q8NBH9; Q96IA2; Q9TNQ8; AC Q9UN49; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-2002, sequence version 3. DT 18-JUN-2025, entry version 206. DE RecName: Full=Translocon-associated protein subunit alpha; DE Short=TRAP-alpha; DE AltName: Full=Signal sequence receptor subunit alpha; DE Short=SSR-alpha; DE Flags: Precursor; GN Name=SSR1; Synonyms=TRAPA; ORFNames=PSEC0262; 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 VARIANT SER-28. RX PubMed=8050590; DOI=10.1016/0014-5793(94)00693-8; RA Hartmann E., Prehn S.; RT "The N-terminal region of the alpha-subunit of the TRAP complex has a RT conserved cluster of negative charges."; RL FEBS Lett. 349:324-326(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10437777; DOI=10.1016/s0014-5793(99)00885-6; RA Hirama T., Miller C.W., Koeffler H.P.; RT "Translocon-associated protein alpha transcripts are induced by RT granulocyte-macrophage colony-stimulating factor and exhibit complex RT alternative polyadenylation."; RL FEBS Lett. 455:223-227(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-28. RC TISSUE=Liver; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Teratocarcinoma; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=B-cell; 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 [10] RP PROTEIN SEQUENCE OF 19-31. RX PubMed=1557127; DOI=10.1038/356443a0; RA Wei M.L., Cresswell P.; RT "HLA-A2 molecules in an antigen-processing mutant cell contain signal RT sequence-derived peptides."; RL Nature 356:443-446(1992). RN [11] RP GLYCOSYLATION AT ASN-136. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-268, 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 [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136 AND ASN-191. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY RP 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-260 AND SER-268, 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 [19] 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 [20] RP INTERACTION WITH CALNEXIN. RX PubMed=22314232; DOI=10.1038/emboj.2012.15; RA Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic S., Kunz B., Kihara A., RA Dal Peraro M., van der Goot F.G.; RT "Palmitoylated calnexin is a key component of the ribosome-translocon RT complex."; RL EMBO J. 31:1823-1835(2012). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, 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 [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [24] {ECO:0007744|PDB:8B6L} RP STRUCTURE BY ELECTRON MICROSCOPY (7.60 ANGSTROMS) OF THE STT3A-CONTAINING RP OLIGOSACCHARYLTRANSFERASE (OST) AND TRANSLOCON COMPLEXES, AND SUBUNIT. RX PubMed=36697828; DOI=10.1038/s41586-022-05638-5; RA Gemmer M., Chaillet M.L., van Loenhout J., Cuevas Arenas R., Vismpas D., RA Grollers-Mulderij M., Koh F.A., Albanese P., Scheltema R.A., Howes S.C., RA Kotecha A., Fedry J., Forster F.; RT "Visualization of translation and protein biogenesis at the ER membrane."; RL Nature 614:160-167(2023). CC -!- FUNCTION: TRAP proteins are part of a complex whose function is to bind CC calcium to the ER membrane and thereby regulate the retention of ER CC resident proteins. May be involved in the recycling of the CC translocation apparatus after completion of the translocation process CC or may function as a membrane-bound chaperone facilitating folding of CC translocated proteins. CC -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP- CC gamma (PubMed:36697828). Interacts with palmitoylated calnexin (CALX), CC the interaction is required for efficient folding of glycosylated CC proteins (PubMed:22314232). {ECO:0000269|PubMed:22314232, CC ECO:0000269|PubMed:36697828}. CC -!- INTERACTION: CC P43307; P27824: CANX; NbExp=7; IntAct=EBI-714168, EBI-355947; CC P43307; P60468: SEC61B; NbExp=2; IntAct=EBI-714168, EBI-1788819; CC P43307; P01009: SERPINA1; NbExp=4; IntAct=EBI-714168, EBI-986224; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type CC I membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P43307-1; Sequence=Displayed; CC Name=2; CC IsoId=P43307-2; Sequence=VSP_013621; CC -!- DOMAIN: Shows a remarkable charge distribution with the N-terminus CC being highly negatively charged, and the cytoplasmic C-terminus CC positively charged. CC -!- MISCELLANEOUS: Seems to bind calcium. CC -!- SIMILARITY: Belongs to the TRAP-alpha 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; Z12830; CAA78290.1; -; mRNA. DR EMBL; AF156965; AAD48778.1; -; mRNA. DR EMBL; BT007387; AAP36051.1; -; mRNA. DR EMBL; AK291550; BAF84239.1; -; mRNA. DR EMBL; CR456961; CAG33242.1; -; mRNA. DR EMBL; AK222762; BAD96482.1; -; mRNA. DR EMBL; AK222809; BAD96529.1; -; mRNA. DR EMBL; AK075562; BAC11701.1; -; mRNA. DR EMBL; AL139095; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC007710; AAH07710.1; -; mRNA. DR CCDS; CCDS4499.1; -. [P43307-1] DR PIR; I38246; I38246. DR RefSeq; NP_001278937.1; NM_001292008.1. DR RefSeq; NP_003135.2; NM_003144.5. [P43307-1] DR PDB; 8B6L; EM; 7.60 A; E=1-286. DR PDBsum; 8B6L; -. DR AlphaFoldDB; P43307; -. DR EMDB; EMD-15870; -. DR SMR; P43307; -. DR BioGRID; 112623; 464. DR ComplexPortal; CPX-8024; Translocon-associated protein complex. DR FunCoup; P43307; 2831. DR IntAct; P43307; 106. DR MINT; P43307; -. DR STRING; 9606.ENSP00000244763; -. DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family. DR GlyConnect; 1839; 29 N-Linked glycans (2 sites). DR GlyCosmos; P43307; 2 sites, 32 glycans. DR GlyGen; P43307; 8 sites, 53 N-linked glycans (2 sites), 1 O-linked glycan (2 sites). DR iPTMnet; P43307; -. DR MetOSite; P43307; -. DR PhosphoSitePlus; P43307; -. DR BioMuta; SSR1; -. DR DMDM; 22261821; -. DR CPTAC; CPTAC-593; -. DR CPTAC; CPTAC-594; -. DR jPOST; P43307; -. DR MassIVE; P43307; -. DR PaxDb; 9606-ENSP00000244763; -. DR PeptideAtlas; P43307; -. DR ProteomicsDB; 55609; -. [P43307-1] DR ProteomicsDB; 55610; -. [P43307-2] DR Pumba; P43307; -. DR TopDownProteomics; P43307-1; -. [P43307-1] DR TopDownProteomics; P43307-2; -. [P43307-2] DR Antibodypedia; 2405; 270 antibodies from 30 providers. DR DNASU; 6745; -. DR Ensembl; ENST00000244763.9; ENSP00000244763.4; ENSG00000124783.14. [P43307-1] DR GeneID; 6745; -. DR KEGG; hsa:6745; -. DR MANE-Select; ENST00000244763.9; ENSP00000244763.4; NM_003144.5; NP_003135.2. DR UCSC; uc003mxf.6; human. [P43307-1] DR AGR; HGNC:11323; -. DR CTD; 6745; -. DR DisGeNET; 6745; -. DR GeneCards; SSR1; -. DR HGNC; HGNC:11323; SSR1. DR HPA; ENSG00000124783; Low tissue specificity. DR MIM; 600868; gene. DR OpenTargets; ENSG00000124783; -. DR VEuPathDB; HostDB:ENSG00000124783; -. DR eggNOG; KOG1631; Eukaryota. DR GeneTree; ENSGT00400000022103; -. DR HOGENOM; CLU_073618_0_0_1; -. DR InParanoid; P43307; -. DR OMA; TFPYSFT; -. DR OrthoDB; 1926781at2759; -. DR PAN-GO; P43307; 1 GO annotation based on evolutionary models. DR PhylomeDB; P43307; -. DR PathwayCommons; P43307; -. DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane. DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes. DR SignaLink; P43307; -. DR BioGRID-ORCS; 6745; 34 hits in 1167 CRISPR screens. DR ChiTaRS; SSR1; human. DR GeneWiki; SSR1; -. DR GenomeRNAi; 6745; -. DR Pharos; P43307; Tbio. DR PRO; PR:P43307; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P43307; protein. DR Bgee; ENSG00000124783; Expressed in corpus epididymis and 215 other cell types or tissues. DR ExpressionAtlas; P43307; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0006613; P:cotranslational protein targeting to membrane; TAS:ProtInc. DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc. DR InterPro; IPR005595; TRAP_alpha. DR PANTHER; PTHR12924:SF0; TRANSLOCON-ASSOCIATED PROTEIN SUBUNIT ALPHA; 1. DR PANTHER; PTHR12924; TRANSLOCON-ASSOCIATED PROTEIN, ALPHA SUBUNIT; 1. DR Pfam; PF03896; TRAP_alpha; 1. DR neXtProt; NX_P43307; -. DR PharmGKB; PA36147; -. DR TreeFam; TF321074; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Direct protein sequencing; KW Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein; KW Proteomics identification; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:1557127" FT CHAIN 19..286 FT /note="Translocon-associated protein subunit alpha" FT /id="PRO_0000033281" FT TOPO_DOM 19..207 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 208..228 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 229..286 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 39..83 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 261..286 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 39..75 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 268..279 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 247 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 260 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 268 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT CARBOHYD 136 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 191 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT VAR_SEQ 68..94 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16303743" FT /id="VSP_013621" FT VARIANT 28 FT /note="L -> S (in dbSNP:rs10004)" FT /evidence="ECO:0000269|PubMed:8050590, ECO:0000269|Ref.6" FT /id="VAR_022427" FT CONFLICT 6 FT /note="R -> G (in Ref. 7; BAC11701)" FT /evidence="ECO:0000305" FT CONFLICT 37 FT /note="E -> A (in Ref. 6; BAD96529)" FT /evidence="ECO:0000305" FT CONFLICT 130 FT /note="Y -> H (in Ref. 1; CAA78290)" FT /evidence="ECO:0000305" FT CONFLICT 190 FT /note="F -> Y (in Ref. 4; BAF84239)" FT /evidence="ECO:0000305" FT CONFLICT 220 FT /note="L -> P (in Ref. 6; BAD96529)" FT /evidence="ECO:0000305" FT CONFLICT 263 FT /note="Q -> R (in Ref. 4; BAF84239)" FT /evidence="ECO:0000305" FT CONFLICT 286 FT /note="E -> D (in Ref. 5; CAG33242)" FT /evidence="ECO:0000305" SQ SEQUENCE 286 AA; 32235 MW; 2C631DC0CC3EB489 CRC64; MRLLPRLLLL LLLVFPATVL FRGGPRGLLA VAQDLTEDEE TVEDSIIEDE DDEAEVEEDE PTDLVEDKEE EDVSGEPEAS PSADTTILFV KGEDFPANNI VKFLVGFTNK GTEDFIVESL DASFRYPQDY QFYIQNFTAL PLNTVVPPQR QATFEYSFIP AEPMGGRPFG LVINLNYKDL NGNVFQDAVF NQTVTVIERE DGLDGETIFM YMFLAGLGLL VIVGLHQLLE SRKRKRPIQK VEMGTSSQND VDMSWIPQET LNQINKASPR RLPRKRAQKR SVGSDE //