SEC62_HUMAN
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 03-AUG-2022, entry version 172.
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).
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEC62 family. {ECO:0000305}.
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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_003262.3.
DR PDB; 7BRT; X-ray; 2.00 A; A/B=361-376.
DR PDBsum; 7BRT; -.
DR AlphaFoldDB; Q99442; -.
DR SMR; Q99442; -.
DR BioGRID; 112950; 498.
DR IntAct; Q99442; 24.
DR MINT; Q99442; -.
DR STRING; 9606.ENSP00000337688; -.
DR TCDB; 1.A.15.1.6; the non-selective cation channel-2 (nscc2) family.
DR iPTMnet; Q99442; -.
DR PhosphoSitePlus; Q99442; -.
DR SwissPalm; Q99442; -.
DR BioMuta; SEC62; -.
DR DMDM; 74732781; -.
DR EPD; Q99442; -.
DR jPOST; Q99442; -.
DR MassIVE; Q99442; -.
DR MaxQB; Q99442; -.
DR PaxDb; Q99442; -.
DR PeptideAtlas; Q99442; -.
DR PRIDE; Q99442; -.
DR ProteomicsDB; 78271; -.
DR TopDownProteomics; Q99442; -.
DR Antibodypedia; 2978; 134 antibodies from 28 providers.
DR DNASU; 7095; -.
DR Ensembl; ENST00000337002.9; ENSP00000337688.4; ENSG00000008952.17.
DR Ensembl; ENST00000480708.5; ENSP00000420331.1; ENSG00000008952.17.
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 CTD; 7095; -.
DR DisGeNET; 7095; -.
DR GeneCards; SEC62; -.
DR HGNC; HGNC:11846; SEC62.
DR HPA; ENSG00000008952; Low tissue specificity.
DR MIM; 602173; gene.
DR neXtProt; NX_Q99442; -.
DR OpenTargets; ENSG00000008952; -.
DR PharmGKB; PA162402849; -.
DR VEuPathDB; HostDB:ENSG00000008952; -.
DR eggNOG; KOG2927; Eukaryota.
DR GeneTree; ENSGT00390000002757; -.
DR HOGENOM; CLU_051910_0_0_1; -.
DR InParanoid; Q99442; -.
DR OMA; HQEQSFN; -.
DR OrthoDB; 1474000at2759; -.
DR PhylomeDB; Q99442; -.
DR TreeFam; TF314944; -.
DR PathwayCommons; Q99442; -.
DR SignaLink; Q99442; -.
DR SIGNOR; Q99442; -.
DR BioGRID-ORCS; 7095; 254 hits in 1087 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 216 other tissues.
DR ExpressionAtlas; Q99442; baseline and differential.
DR Genevisible; Q99442; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
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 InterPro; IPR004728; Sec62.
DR PANTHER; PTHR12443; PTHR12443; 1.
DR Pfam; PF03839; Sec62; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW 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 289..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="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 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
