ID SEC62_HUMAN Reviewed; 399 AA. AC Q99442; D3DNQ0; O00682; O00729; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 10-JUN-2026, entry version 190. DE RecName: Full=Translocation protein SEC62; DE AltName: Full=Translocation protein 1; DE Short=TP-1; DE Short=hTP-1; GN Name=SEC62; Synonyms=TLOC1; 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]. RX PubMed=9020021; DOI=10.1006/bbrc.1996.5892; RA Daimon M., Susa S., Suzuki K., Kato T., Yamatani K., Sasaki H.; RT "Identification of a human cDNA homologue to the Drosophila translocation RT protein 1 (Dtrp-1)."; RL Biochem. Biophys. Res. Commun. 230:100-104(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10683767; DOI=10.1080/713803565; RA Daimon M., Susa S., Kato T.; RT "Fine structure of the human translocation protein 1 (HTP1/TLOC1) gene."; RL IUBMB Life 48:619-624(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10799540; DOI=10.1074/jbc.275.19.14550; RA Meyer H.-A., Grau H., Kraft R., Kostka S., Prehn S., Kalies K.-U., RA Hartmann E.; RT "Mammalian Sec61 is associated with Sec62 and Sec63."; RL J. Biol. Chem. 275:14550-14557(2000). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland; 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-158, 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-375, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-158, 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 [9] 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-356, 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 [11] RP FUNCTION. RX PubMed=22375059; DOI=10.1242/jcs.096727; RA Lang S., Benedix J., Fedeles S.V., Schorr S., Schirra C., Schaeuble N., RA Jalal C., Greiner M., Hassdenteufel S., Tatzelt J., Kreutzer B., RA Edelmann L., Krause E., Rettig J., Somlo S., Zimmermann R., Dudek J.; RT "Different effects of Sec61alpha, Sec62 and Sec63 depletion on transport of RT polypeptides into the endoplasmic reticulum of mammalian cells."; RL J. Cell Sci. 125:1958-1969(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341; SER-356 AND THR-375, AND RP IDENTIFICATION BY 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, 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 [14] 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 [15] RP FUNCTION. RX PubMed=29719251; DOI=10.1016/j.celrep.2018.03.122; RA Hassdenteufel S., Johnson N., Paton A.W., Paton J.C., High S., RA Zimmermann R.; RT "Chaperone-Mediated Sec61 Channel Gating during ER Import of Small RT Precursor Proteins Overcomes Sec61 Inhibitor-Reinforced Energy Barrier."; RL Cell Rep. 23:1373-1386(2018). RN [16] {ECO:0007744|PDB:7BRT} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 361-376 IN CHIMERIC CONSTRUCT RP WITH GABARAP. RX PubMed=32620754; DOI=10.1038/s41467-020-17163-y; RA Mochida K., Yamasaki A., Matoba K., Kirisako H., Noda N.N., Nakatogawa H.; RT "Super-assembly of ER-phagy receptor Atg40 induces local ER remodeling at RT contacts with forming autophagosomal membranes."; RL Nat. Commun. 11:3306-3306(2020). CC -!- FUNCTION: Mediates post-translational transport of precursor CC polypeptides across endoplasmic reticulum (ER). Proposed to act as a CC targeting receptor for small presecretory proteins containing short and CC apolar signal peptides. Targets and properly positions newly CC synthesized presecretory proteins into the SEC61 channel-forming CC translocon complex, triggering channel opening for polypeptide CC translocation to the ER lumen. {ECO:0000269|PubMed:22375059, CC ECO:0000269|PubMed:29719251}. CC -!- SUBUNIT: The ER translocon complex that consists of channel-forming CC core components SEC61A1, SEC61B and SEC61G and different auxiliary CC components such as SEC62 and SEC63. Interacts with SEC61B. CC {ECO:0000250|UniProtKB:P82009}. CC -!- INTERACTION: CC Q99442; O95166: GABARAP; NbExp=3; IntAct=EBI-949221, EBI-712001; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; CC Multi-pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the SEC62 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; D87127; BAA13254.1; -; mRNA. DR EMBL; AB024586; BAB12685.1; -; Genomic_DNA. DR EMBL; U93239; AAB51391.1; -; mRNA. DR EMBL; CH471052; EAW78530.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78531.1; -; Genomic_DNA. DR EMBL; BC012035; AAH12035.1; -; mRNA. DR CCDS; CCDS3210.1; -. DR PIR; JC5279; JC5279. DR RefSeq; NP_003253.1; NM_003262.4. DR PDB; 7BRT; X-ray; 2.00 A; A/B=361-376. DR PDBsum; 7BRT; -. DR AlphaFoldDB; Q99442; -. DR SMR; Q99442; -. DR BioGRID; 112950; 545. DR FunCoup; Q99442; 2695. DR IntAct; Q99442; 159. DR MINT; Q99442; -. DR NDEx; IQUERY-CP-SEC62; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000337688; -. DR ChEMBL; CHEMBL6067372; -. DR TCDB; 1.A.15.1.6; the non-selective cation channel-2 (nscc2) family. DR GlyGen; Q99442; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99442; -. DR PhosphoSitePlus; Q99442; -. DR SwissPalm; Q99442; -. DR BioMuta; SEC62; -. DR DMDM; 74732781; -. DR jPOST; Q99442; -. DR MassIVE; Q99442; -. DR PaxDb; 9606-ENSP00000337688; -. DR PeptideAtlas; Q99442; -. DR ProteomicsDB; 78271; -. DR Pumba; Q99442; -. DR TopDownProteomics; Q99442; -. DR Antibodypedia; 2978; 130 antibodies from 28 providers. DR DNASU; 7095; -. DR Ensembl; ENST00000337002.9; ENSP00000337688.4; ENSG00000008952.18. DR Ensembl; ENST00000480708.5; ENSP00000420331.1; ENSG00000008952.18. DR GeneID; 7095; -. DR KEGG; hsa:7095; -. DR MANE-Select; ENST00000337002.9; ENSP00000337688.4; NM_003262.4; NP_003253.1. DR UCSC; uc003fgg.4; human. DR AGR; HGNC:11846; -. DR ClinPGx; PA162402849; -. DR CTD; 7095; -. DR DisGeNET; 7095; -. DR GeneCards; SEC62; -. DR HGNC; HGNC:11846; SEC62. DR HPA; ENSG00000008952; Low tissue specificity. DR MIM; 602173; gene. DR OpenTargets; ENSG00000008952; -. DR VEuPathDB; HostDB:ENSG00000008952; -. DR eggNOG; KOG2927; Eukaryota. DR GeneTree; ENSGT00390000002757; -. DR HOGENOM; CLU_051910_0_0_1; -. DR InParanoid; Q99442; -. DR OMA; CLLESPW; -. DR OrthoDB; 200187at2759; -. DR PAN-GO; Q99442; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q99442; -. DR PathwayCommons; Q99442; -. DR SignaLink; Q99442; -. DR SIGNOR; Q99442; -. DR Agora; ENSG00000008952; -. DR BioGRID-ORCS; 7095; 259 hits in 1165 CRISPR screens. DR ChiTaRS; SEC62; human. DR GeneWiki; SEC62; -. DR GenomeRNAi; 7095; -. DR Pharos; Q99442; Tbio. DR PRO; PR:Q99442; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q99442; protein. DR Bgee; ENSG00000008952; Expressed in endothelial cell and 218 other cell types or tissues. DR ExpressionAtlas; Q99442; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0006613; P:cotranslational protein targeting to membrane; TAS:ProtInc. DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IMP:MGI. DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IMP:UniProtKB. DR GO; GO:0061709; P:reticulophagy; IMP:MGI. DR InterPro; IPR004728; Sec62. DR PANTHER; PTHR12443; TRANSLOCATION PROTEIN SEC62; 1. DR PANTHER; PTHR12443:SF9; TRANSLOCATION PROTEIN SEC62; 1. DR Pfam; PF03839; Sec62; 1. PE 1: Evidence at protein level; KW 3D-structure; Endoplasmic reticulum; Membrane; Phosphoprotein; KW Protein transport; Proteomics identification; Reference proteome; KW Translocation; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..399 FT /note="Translocation protein SEC62" FT /id="PRO_0000206616" FT TOPO_DOM 1..196 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 197..217 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 218..234 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 235..255 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 256..399 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 108..167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 289..399 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 108..155 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 289..324 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 325..335 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 336..354 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 372..389 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 390..399 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 158 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 335 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 341 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 353 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 356 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 375 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:23186163" FT HELIX 363..366 FT /evidence="ECO:0007829|PDB:7BRT" FT HELIX 368..375 FT /evidence="ECO:0007829|PDB:7BRT" SQ SEQUENCE 399 AA; 45862 MW; CACBF4F02E2D0AE5 CRC64; MAERRRHKKR IQEVGEPSKE EKAVAKYLRF NCPTKSTNMM GHRVDYFIAS KAVDCLLDSK WAKAKKGEEA LFTTRESVVD YCNRLLKKQF FHRALKVMKM KYDKDIKKEK DKGKAESGKE EDKKSKKENI KDEKTKKEKE KKKDGEKEES KKEETPGTPK KKETKKKFKL EPHDDQVFLD GNEVYVWIYD PVHFKTFVMG LILVIAVIAA TLFPLWPAEM RVGVYYLSVG AGCFVASILL LAVARCILFL IIWLITGGRH HFWFLPNLTA DVGFIDSFRP LYTHEYKGPK ADLKKDEKSE TKKQQKSDSE EKSDSEKKED EEGKVGPGNH GTEGSGGERH SDTDSDRRED DRSQHSSGNG NDFEMITKEE LEQQTDGDCE EDEEEENDGE TPKSSHEKS //