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Protein

Translocation protein SEC62

Gene

SEC62

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for preprotein translocation.By similarity

GO - Molecular functioni

  • protein transporter activity Source: InterPro
  • receptor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

ReactomeiR-HSA-381038. XBP1(S) activates chaperone genes.

Protein family/group databases

TCDBi1.A.15.2.1. the non-selective cation channel-2 (nscc2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Translocation protein SEC62
Alternative name(s):
Translocation protein 1
Short name:
TP-1
Short name:
hTP-1
Gene namesi
Name:SEC62
Synonyms:TLOC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:11846. SEC62.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 196196CytoplasmicSequence analysisAdd
BLAST
Transmembranei197 – 21721HelicalSequence analysisAdd
BLAST
Topological domaini218 – 23417LumenalSequence analysisAdd
BLAST
Transmembranei235 – 25521HelicalSequence analysisAdd
BLAST
Topological domaini256 – 399144CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • aggresome Source: HPA
  • cytosol Source: Reactome
  • endoplasmic reticulum Source: HPA
  • endoplasmic reticulum membrane Source: Reactome
  • integral component of membrane Source: ProtInc
  • intermediate filament cytoskeleton Source: HPA
  • membrane Source: MGI
  • rough endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162402849.

Polymorphism and mutation databases

BioMutaiSEC62.
DMDMi74732781.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 399399Translocation protein SEC62PRO_0000206616Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei158 – 1581PhosphothreonineCombined sources
Modified residuei335 – 3351PhosphoserineCombined sources
Modified residuei353 – 3531PhosphoserineCombined sources
Modified residuei356 – 3561PhosphoserineCombined sources
Modified residuei375 – 3751PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ99442.
MaxQBiQ99442.
PaxDbiQ99442.
PeptideAtlasiQ99442.
PRIDEiQ99442.
TopDownProteomicsiQ99442.

PTM databases

iPTMnetiQ99442.
PhosphoSiteiQ99442.
SwissPalmiQ99442.

Expressioni

Gene expression databases

BgeeiQ99442.
CleanExiHS_SEC62.
ExpressionAtlasiQ99442. baseline and differential.
GenevisibleiQ99442. HS.

Organism-specific databases

HPAiHPA014059.
HPA061450.

Interactioni

Subunit structurei

Part of a complex that contains SEC61, SEC62 and SEC63. Interacts with SEC61B.1 Publication

Protein-protein interaction databases

BioGridi112950. 22 interactions.
IntActiQ99442. 11 interactions.
MINTiMINT-2863594.
STRINGi9606.ENSP00000337688.

Structurei

3D structure databases

ProteinModelPortaliQ99442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SEC62 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2927. Eukaryota.
COG5232. LUCA.
GeneTreeiENSGT00390000002757.
HOGENOMiHOG000016701.
HOVERGENiHBG055550.
InParanoidiQ99442.
KOiK12275.
OMAiSNGNDFE.
OrthoDBiEOG70W3FT.
PhylomeDBiQ99442.
TreeFamiTF314944.

Family and domain databases

InterProiIPR004728. Sec62.
[Graphical view]
PANTHERiPTHR12443. PTHR12443. 1 hit.
PfamiPF03839. Sec62. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99442-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAERRRHKKR IQEVGEPSKE EKAVAKYLRF NCPTKSTNMM GHRVDYFIAS
60 70 80 90 100
KAVDCLLDSK WAKAKKGEEA LFTTRESVVD YCNRLLKKQF FHRALKVMKM
110 120 130 140 150
KYDKDIKKEK DKGKAESGKE EDKKSKKENI KDEKTKKEKE KKKDGEKEES
160 170 180 190 200
KKEETPGTPK KKETKKKFKL EPHDDQVFLD GNEVYVWIYD PVHFKTFVMG
210 220 230 240 250
LILVIAVIAA TLFPLWPAEM RVGVYYLSVG AGCFVASILL LAVARCILFL
260 270 280 290 300
IIWLITGGRH HFWFLPNLTA DVGFIDSFRP LYTHEYKGPK ADLKKDEKSE
310 320 330 340 350
TKKQQKSDSE EKSDSEKKED EEGKVGPGNH GTEGSGGERH SDTDSDRRED
360 370 380 390
DRSQHSSGNG NDFEMITKEE LEQQTDGDCE EDEEEENDGE TPKSSHEKS
Length:399
Mass (Da):45,862
Last modified:May 1, 1997 - v1
Checksum:iCACBF4F02E2D0AE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87127 mRNA. Translation: BAA13254.1.
AB024586 Genomic DNA. Translation: BAB12685.1.
U93239 mRNA. Translation: AAB51391.1.
CH471052 Genomic DNA. Translation: EAW78530.1.
CH471052 Genomic DNA. Translation: EAW78531.1.
BC012035 mRNA. Translation: AAH12035.1.
CCDSiCCDS3210.1.
PIRiJC5279.
RefSeqiNP_003253.1. NM_003262.3.
UniGeneiHs.744859.

Genome annotation databases

EnsembliENST00000337002; ENSP00000337688; ENSG00000008952.
ENST00000480708; ENSP00000420331; ENSG00000008952.
GeneIDi7095.
KEGGihsa:7095.
UCSCiuc003fgg.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87127 mRNA. Translation: BAA13254.1.
AB024586 Genomic DNA. Translation: BAB12685.1.
U93239 mRNA. Translation: AAB51391.1.
CH471052 Genomic DNA. Translation: EAW78530.1.
CH471052 Genomic DNA. Translation: EAW78531.1.
BC012035 mRNA. Translation: AAH12035.1.
CCDSiCCDS3210.1.
PIRiJC5279.
RefSeqiNP_003253.1. NM_003262.3.
UniGeneiHs.744859.

3D structure databases

ProteinModelPortaliQ99442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112950. 22 interactions.
IntActiQ99442. 11 interactions.
MINTiMINT-2863594.
STRINGi9606.ENSP00000337688.

Protein family/group databases

TCDBi1.A.15.2.1. the non-selective cation channel-2 (nscc2) family.

PTM databases

iPTMnetiQ99442.
PhosphoSiteiQ99442.
SwissPalmiQ99442.

Polymorphism and mutation databases

BioMutaiSEC62.
DMDMi74732781.

Proteomic databases

EPDiQ99442.
MaxQBiQ99442.
PaxDbiQ99442.
PeptideAtlasiQ99442.
PRIDEiQ99442.
TopDownProteomicsiQ99442.

Protocols and materials databases

DNASUi7095.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337002; ENSP00000337688; ENSG00000008952.
ENST00000480708; ENSP00000420331; ENSG00000008952.
GeneIDi7095.
KEGGihsa:7095.
UCSCiuc003fgg.4. human.

Organism-specific databases

CTDi7095.
GeneCardsiSEC62.
HGNCiHGNC:11846. SEC62.
HPAiHPA014059.
HPA061450.
MIMi602173. gene.
neXtProtiNX_Q99442.
PharmGKBiPA162402849.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2927. Eukaryota.
COG5232. LUCA.
GeneTreeiENSGT00390000002757.
HOGENOMiHOG000016701.
HOVERGENiHBG055550.
InParanoidiQ99442.
KOiK12275.
OMAiSNGNDFE.
OrthoDBiEOG70W3FT.
PhylomeDBiQ99442.
TreeFamiTF314944.

Enzyme and pathway databases

ReactomeiR-HSA-381038. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSiSEC62. human.
GeneWikiiSEC62.
GenomeRNAii7095.
NextBioi27755.
PROiQ99442.
SOURCEiSearch...

Gene expression databases

BgeeiQ99442.
CleanExiHS_SEC62.
ExpressionAtlasiQ99442. baseline and differential.
GenevisibleiQ99442. HS.

Family and domain databases

InterProiIPR004728. Sec62.
[Graphical view]
PANTHERiPTHR12443. PTHR12443. 1 hit.
PfamiPF03839. Sec62. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a human cDNA homologue to the Drosophila translocation protein 1 (Dtrp-1)."
    Daimon M., Susa S., Suzuki K., Kato T., Yamatani K., Sasaki H.
    Biochem. Biophys. Res. Commun. 230:100-104(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Fine structure of the human translocation protein 1 (HTP1/TLOC1) gene."
    Daimon M., Susa S., Kato T.
    IUBMB Life 48:619-624(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A COMPLEX WITH SEC61 AND SEC63, INTERACTION WITH SEC61B.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSEC62_HUMAN
AccessioniPrimary (citable) accession number: Q99442
Secondary accession number(s): D3DNQ0, O00682, O00729
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: May 1, 1997
Last modified: April 13, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.