ID ERP29_HUMAN Reviewed; 261 AA. AC P30040; C9J183; Q3MJC3; Q6FHT4; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 4. DT 23-MAY-2018, entry version 189. DE RecName: Full=Endoplasmic reticulum resident protein 29; DE Short=ERp29; DE AltName: Full=Endoplasmic reticulum resident protein 28; DE Short=ERp28; DE AltName: Full=Endoplasmic reticulum resident protein 31; DE Short=ERp31; DE Flags: Precursor; GN Name=ERP29; Synonyms=C12orf8, ERP28; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION. RC TISSUE=Liver; RX PubMed=9738895; DOI=10.1046/j.1432-1327.1998.2550570.x; RA Ferrari D.M., van Nguyen P., Kratzin H.D., Soeling H.D.; RT "ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of RT the protein disulfide isomerase family but lacks a CXXC thioredoxin- RT box motif."; RL Eur. J. Biochem. 255:570-579(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; RA Hillier L., Clark N., Dubuque T., Elliston K., Hawkins M., Holman M., RA Hultman M., Kucaba T., Le M., Lennon G., Marra M., Parsons J., RA Rifkin L., Rohlfing T., Soares M., Tan F., Trevaskis E., Waterston R., RA Williamson A., Wohldmann P., Wilson R.; RT "The WashU-Merck EST project."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] 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 [4] 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., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA 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., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA 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., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 33-52. RC TISSUE=Liver; RX PubMed=8313870; DOI=10.1002/elps.11501401181; RA Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., RA Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.; RT "Human liver protein map: update 1993."; RL Electrophoresis 14:1216-1222(1993). RN [7] RP PRELIMINARY PROTEIN SEQUENCE OF 33-42. RC TISSUE=Liver; RX PubMed=1286669; DOI=10.1002/elps.11501301201; RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., RA Appel R.D., Hughes G.J.; RT "Human liver protein map: a reference database established by RT microsequencing and gel comparison."; RL Electrophoresis 13:992-1001(1992). RN [8] RP PROTEIN SEQUENCE OF 113-122, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Vishwanath V.; RL Submitted (MAR-2007) to UniProtKB. RN [9] RP PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RA Hubbard M.J.; RL Submitted (DEC-1998) to UniProtKB. RN [10] RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION. RC TISSUE=Liver; RX PubMed=11271497; RX DOI=10.1002/1522-2683(200011)21:17<3785::AID-ELPS3785>3.0.CO;2-2; RA Hubbard M.J., McHugh N.J.; RT "Human ERp29: isolation, primary structural characterisation and two- RT dimensional gel mapping."; RL Electrophoresis 21:3785-3796(2000). RN [11] RP COMPONENT OF A CHAPERONE COMPLEX. RX PubMed=12475965; DOI=10.1091/mbc.E02-05-0311; RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.; RT "A subset of chaperones and folding enzymes form multiprotein RT complexes in endoplasmic reticulum to bind nascent proteins."; RL Mol. Biol. Cell 13:4456-4469(2002). RN [12] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=12643545; DOI=10.1021/pr025562r; RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., RA Hearing V.J., Hunt D.F., Appella E.; RT "Proteomic analysis of early melanosomes: identification of novel RT melanosomal proteins."; RL J. Proteome Res. 2:69-79(2003). RN [13] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [14] 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation 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., RA Buerckstuemmer T., 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 AT TYR-64 AND TYR-66. RX PubMed=25171405; DOI=10.1016/j.cell.2014.06.048; RA Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr., RA Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L., RA Asara J.M., Dixon J.E., Yeo C.Y., Whitman M.; RT "A secreted tyrosine kinase acts in the extracellular environment."; RL Cell 158:1033-1044(2014). RN [17] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-32, AND 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., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Does not seem to be a disulfide isomerase. Plays an CC important role in the processing of secretory proteins within the CC endoplasmic reticulum (ER), possibly by participating in the CC folding of proteins in the ER. CC -!- SUBUNIT: Homodimer. Part of a large chaperone multiprotein complex CC comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, CC PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or CC at very low levels, CALR nor CANX. CC -!- INTERACTION: CC P52555:Erp29 (xeno); NbExp=2; IntAct=EBI-8762218, EBI-917740; CC Q9UMX0:UBQLN1; NbExp=4; IntAct=EBI-946830, EBI-741480; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome. CC Note=Identified by mass spectrometry in melanosome fractions from CC stage I to stage IV. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P30040-1; Sequence=Displayed; CC Name=2; CC IsoId=P30040-2; Sequence=VSP_045680, VSP_045681; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Ubiquitous. Mostly expressed in secretory CC tissues. 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; X94910; CAA64397.1; -; mRNA. DR EMBL; AA412124; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CR541667; CAG46468.1; -; mRNA. DR EMBL; AC073575; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC101493; AAI01494.1; -; mRNA. DR EMBL; BC101495; AAI01496.1; -; mRNA. DR CCDS; CCDS44977.1; -. [P30040-2] DR CCDS; CCDS9158.1; -. [P30040-1] DR PIR; T09549; T09549. DR RefSeq; NP_001029197.1; NM_001034025.1. [P30040-2] DR RefSeq; NP_006808.1; NM_006817.3. [P30040-1] DR UniGene; Hs.75841; -. DR PDB; 2QC7; X-ray; 2.90 A; A/B=34-261. DR PDB; 5V8Z; X-ray; 2.10 A; A/C=158-261. DR PDB; 5V90; X-ray; 3.25 A; A/C=158-261. DR PDBsum; 2QC7; -. DR PDBsum; 5V8Z; -. DR PDBsum; 5V90; -. DR ProteinModelPortal; P30040; -. DR SMR; P30040; -. DR BioGrid; 116160; 20. DR IntAct; P30040; 15. DR STRING; 9606.ENSP00000261735; -. DR iPTMnet; P30040; -. DR PhosphoSitePlus; P30040; -. DR SwissPalm; P30040; -. DR BioMuta; ERP29; -. DR DMDM; 6015110; -. DR OGP; P30040; -. DR REPRODUCTION-2DPAGE; IPI00024911; -. DR SWISS-2DPAGE; P30040; -. DR EPD; P30040; -. DR PaxDb; P30040; -. DR PeptideAtlas; P30040; -. DR PRIDE; P30040; -. DR TopDownProteomics; P30040-1; -. [P30040-1] DR Ensembl; ENST00000261735; ENSP00000261735; ENSG00000089248. [P30040-1] DR Ensembl; ENST00000455836; ENSP00000412083; ENSG00000089248. [P30040-2] DR GeneID; 10961; -. DR KEGG; hsa:10961; -. DR UCSC; uc001ttl.1; human. [P30040-1] DR CTD; 10961; -. DR DisGeNET; 10961; -. DR EuPathDB; HostDB:ENSG00000089248.6; -. DR GeneCards; ERP29; -. DR HGNC; HGNC:13799; ERP29. DR HPA; HPA039363; -. DR HPA; HPA039456; -. DR MIM; 602287; gene. DR neXtProt; NX_P30040; -. DR OpenTargets; ENSG00000089248; -. DR PharmGKB; PA25509; -. DR eggNOG; ENOG410IX2F; Eukaryota. DR eggNOG; ENOG4111I8S; LUCA. DR GeneTree; ENSGT00390000018566; -. DR HOGENOM; HOG000169611; -. DR HOVERGEN; HBG051508; -. DR InParanoid; P30040; -. DR KO; K09586; -. DR OMA; DGCIKEF; -. DR OrthoDB; EOG091G0NH4; -. DR PhylomeDB; P30040; -. DR TreeFam; TF324701; -. DR ChiTaRS; ERP29; human. DR EvolutionaryTrace; P30040; -. DR GeneWiki; ERP29; -. DR GenomeRNAi; 10961; -. DR PRO; PR:P30040; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; ENSG00000089248; -. DR CleanEx; HS_ERP29; -. DR ExpressionAtlas; P30040; baseline and differential. DR Genevisible; P30040; HS. DR GO; GO:0009986; C:cell surface; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL. DR GO; GO:0005788; C:endoplasmic reticulum lumen; NAS:ParkinsonsUK-UCL. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISS:ParkinsonsUK-UCL. DR GO; GO:0030133; C:transport vesicle; ISS:ParkinsonsUK-UCL. DR GO; GO:0051087; F:chaperone binding; ISS:ParkinsonsUK-UCL. DR GO; GO:0042803; F:protein homodimerization activity; ISS:ParkinsonsUK-UCL. DR GO; GO:0000187; P:activation of MAPK activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0010629; P:negative regulation of gene expression; IDA:ParkinsonsUK-UCL. DR GO; GO:0050709; P:negative regulation of protein secretion; IDA:ParkinsonsUK-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ParkinsonsUK-UCL. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ParkinsonsUK-UCL. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR GO; GO:0043335; P:protein unfolding; NAS:ParkinsonsUK-UCL. DR GO; GO:1902235; P:regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl. DR CDD; cd00238; ERp29c; 1. DR CDD; cd03007; PDI_a_ERp29_N; 1. DR Gene3D; 1.20.1150.12; -; 1. DR InterPro; IPR016855; ERp29. DR InterPro; IPR011679; ERp29_C. DR InterPro; IPR036356; ERp29_C_sf. DR InterPro; IPR012883; ERp29_N. DR InterPro; IPR036249; Thioredoxin-like_sf. DR Pfam; PF07749; ERp29; 1. DR Pfam; PF07912; ERp29_N; 1. DR PIRSF; PIRSF027352; ER_p29; 1. DR SUPFAM; SSF47933; SSF47933; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00014; ER_TARGET; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; KW Direct protein sequencing; Endoplasmic reticulum; Phosphoprotein; KW Reference proteome; Signal. FT SIGNAL 1 32 {ECO:0000244|PubMed:25944712, FT ECO:0000269|PubMed:8313870}. FT CHAIN 33 261 Endoplasmic reticulum resident protein FT 29. FT /FTId=PRO_0000021197. FT MOTIF 258 261 Prevents secretion from ER. FT {ECO:0000255|PROSITE-ProRule:PRU10138}. FT MOD_RES 64 64 Phosphotyrosine; by PKDCC. FT {ECO:0000269|PubMed:25171405}. FT MOD_RES 66 66 Phosphotyrosine; by PKDCC. FT {ECO:0000269|PubMed:25171405}. FT VAR_SEQ 49 53 VIPKS -> IMVTS (in isoform 2). FT {ECO:0000303|Ref.2}. FT /FTId=VSP_045680. FT VAR_SEQ 54 261 Missing (in isoform 2). FT {ECO:0000303|Ref.2}. FT /FTId=VSP_045681. FT HELIX 45 49 {ECO:0000244|PDB:2QC7}. FT HELIX 50 52 {ECO:0000244|PDB:2QC7}. FT STRAND 54 60 {ECO:0000244|PDB:2QC7}. FT HELIX 68 80 {ECO:0000244|PDB:2QC7}. FT STRAND 86 91 {ECO:0000244|PDB:2QC7}. FT STRAND 96 98 {ECO:0000244|PDB:2QC7}. FT HELIX 102 107 {ECO:0000244|PDB:2QC7}. FT HELIX 112 114 {ECO:0000244|PDB:2QC7}. FT STRAND 116 122 {ECO:0000244|PDB:2QC7}. FT HELIX 138 147 {ECO:0000244|PDB:2QC7}. FT HELIX 159 170 {ECO:0000244|PDB:5V8Z}. FT HELIX 174 187 {ECO:0000244|PDB:5V8Z}. FT HELIX 188 190 {ECO:0000244|PDB:5V8Z}. FT HELIX 193 195 {ECO:0000244|PDB:5V8Z}. FT HELIX 196 212 {ECO:0000244|PDB:5V8Z}. FT HELIX 216 230 {ECO:0000244|PDB:5V8Z}. FT HELIX 235 249 {ECO:0000244|PDB:5V8Z}. SQ SEQUENCE 261 AA; 28993 MW; 76145006433A1983 CRC64; MAAAVPRAAF LSPLLPLLLG FLLLSAPHGG SGLHTKGALP LDTVTFYKVI PKSKFVLVKF DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL NMELSEKYKL DKESYPVFYL FRDGDFENPV PYTGAVKVGA IQRWLKGQGV YLGMPGCLPV YDALAGEFIR ASGVEARQAL LKQGQDNLSS VKETQKKWAE QYLKIMGKIL DQGEDFPASE MTRIARLIEK NKMSDGKKEE LQKSLNILTA FQKKGAEKEE L //