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P60468

- SC61B_HUMAN

UniProt

P60468 - SC61B_HUMAN

Protein

Protein transport protein Sec61 subunit beta

Gene

SEC61B

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

    Necessary for protein translocation in the endoplasmic reticulum.

    GO - Molecular functioni

    1. epidermal growth factor binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. ribosome binding Source: Ensembl

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    3. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    4. cellular protein metabolic process Source: Reactome
    5. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    6. gene expression Source: Reactome
    7. protein import into nucleus, translocation Source: UniProtKB
    8. retrograde protein transport, ER to cytosol Source: UniProtKB
    9. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    10. translation Source: Reactome

    Keywords - Biological processi

    Protein transport, Translocation, Transport

    Enzyme and pathway databases

    ReactomeiREACT_111178. ER-Phagosome pathway.
    REACT_115902. SRP-dependent cotranslational protein targeting to membrane.

    Protein family/group databases

    TCDBi3.A.5.9.1. the general secretory pathway (sec) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein transport protein Sec61 subunit beta
    Gene namesi
    Name:SEC61B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:16993. SEC61B.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: HPA
    2. endoplasmic reticulum Sec complex Source: UniProtKB
    3. integral component of membrane Source: UniProtKB
    4. membrane Source: MGI

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi39 – 391C → S: Abolishes S-acylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA134888963.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 9695Protein transport protein Sec61 subunit betaPRO_0000157254Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylproline1 Publication
    Modified residuei7 – 71Phosphoserine1 Publication
    Modified residuei13 – 131Phosphoserine1 Publication
    Modified residuei14 – 141Phosphoserine1 Publication
    Modified residuei17 – 171Phosphoserine3 Publications
    Lipidationi39 – 391S-palmitoyl cysteine1 Publication

    Keywords - PTMi

    Acetylation, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP60468.
    PaxDbiP60468.
    PeptideAtlasiP60468.
    PRIDEiP60468.

    PTM databases

    PhosphoSiteiP60468.

    Expressioni

    Gene expression databases

    BgeeiP60468.
    CleanExiHS_SEC61B.
    GenevestigatoriP60468.

    Organism-specific databases

    HPAiHPA049407.

    Interactioni

    Subunit structurei

    Heterotrimeric complex composed of SEC61-alpha, SEC61-beta and SEC61-gamma. Part of a complex composed of SEC61, SEC62 and SEC63. Interacts with SEC62.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCAP31P515727EBI-1788819,EBI-77683

    Protein-protein interaction databases

    BioGridi116152. 25 interactions.
    DIPiDIP-40997N.
    IntActiP60468. 9 interactions.
    MINTiMINT-106933.
    STRINGi9606.ENSP00000223641.

    Structurei

    3D structure databases

    ProteinModelPortaliP60468.
    SMRiP60468. Positions 61-96.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 7069CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei71 – 9121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SEC61-beta family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG248540.
    HOGENOMiHOG000211109.
    HOVERGENiHBG061281.
    InParanoidiP60468.
    KOiK09481.
    OMAiHILAKIT.
    OrthoDBiEOG77M8RR.
    PhylomeDBiP60468.
    TreeFamiTF313144.

    Family and domain databases

    InterProiIPR016482. SecG/Sec61-beta/Sbh1.
    [Graphical view]
    PANTHERiPTHR13509. PTHR13509. 1 hit.
    PfamiPF03911. Sec61_beta. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006398. Sec61_beta_euk. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P60468-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGPTPSGTN VGSSGRSPSK AVAARAAGST VRQRKNASCG TRSAGRTTSA   50
    GTGGMWRFYT EDSPGLKVGP VPVLVMSLLF IASVFMLHIW GKYTRS 96
    Length:96
    Mass (Da):9,974
    Last modified:January 23, 2007 - v2
    Checksum:i5FAFF4197A62FA49
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25085 mRNA. Translation: AAA19706.1.
    CR456883 mRNA. Translation: CAG33164.1.
    AL137067 Genomic DNA. Translation: CAC08000.1.
    BC001734 mRNA. Translation: AAH01734.1.
    CCDSiCCDS6741.1.
    PIRiS42410.
    RefSeqiNP_006799.1. NM_006808.2.
    UniGeneiHs.191887.

    Genome annotation databases

    EnsembliENST00000223641; ENSP00000223641; ENSG00000106803.
    GeneIDi10952.
    KEGGihsa:10952.
    UCSCiuc004azh.3. human.

    Polymorphism databases

    DMDMi42560366.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25085 mRNA. Translation: AAA19706.1 .
    CR456883 mRNA. Translation: CAG33164.1 .
    AL137067 Genomic DNA. Translation: CAC08000.1 .
    BC001734 mRNA. Translation: AAH01734.1 .
    CCDSi CCDS6741.1.
    PIRi S42410.
    RefSeqi NP_006799.1. NM_006808.2.
    UniGenei Hs.191887.

    3D structure databases

    ProteinModelPortali P60468.
    SMRi P60468. Positions 61-96.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116152. 25 interactions.
    DIPi DIP-40997N.
    IntActi P60468. 9 interactions.
    MINTi MINT-106933.
    STRINGi 9606.ENSP00000223641.

    Protein family/group databases

    TCDBi 3.A.5.9.1. the general secretory pathway (sec) family.

    PTM databases

    PhosphoSitei P60468.

    Polymorphism databases

    DMDMi 42560366.

    Proteomic databases

    MaxQBi P60468.
    PaxDbi P60468.
    PeptideAtlasi P60468.
    PRIDEi P60468.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000223641 ; ENSP00000223641 ; ENSG00000106803 .
    GeneIDi 10952.
    KEGGi hsa:10952.
    UCSCi uc004azh.3. human.

    Organism-specific databases

    CTDi 10952.
    GeneCardsi GC09P101984.
    HGNCi HGNC:16993. SEC61B.
    HPAi HPA049407.
    MIMi 609214. gene.
    neXtProti NX_P60468.
    PharmGKBi PA134888963.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248540.
    HOGENOMi HOG000211109.
    HOVERGENi HBG061281.
    InParanoidi P60468.
    KOi K09481.
    OMAi HILAKIT.
    OrthoDBi EOG77M8RR.
    PhylomeDBi P60468.
    TreeFami TF313144.

    Enzyme and pathway databases

    Reactomei REACT_111178. ER-Phagosome pathway.
    REACT_115902. SRP-dependent cotranslational protein targeting to membrane.

    Miscellaneous databases

    GeneWikii SEC61B.
    GenomeRNAii 10952.
    NextBioi 41613.
    PROi P60468.
    SOURCEi Search...

    Gene expression databases

    Bgeei P60468.
    CleanExi HS_SEC61B.
    Genevestigatori P60468.

    Family and domain databases

    InterProi IPR016482. SecG/Sec61-beta/Sbh1.
    [Graphical view ]
    PANTHERi PTHR13509. PTHR13509. 1 hit.
    Pfami PF03911. Sec61_beta. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006398. Sec61_beta_euk. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Evolutionary conservation of components of the protein translocation complex."
      Hartmann E., Sommer T., Prehn S., Goerlich D., Jentsch S., Rapoport T.A.
      Nature 367:654-657(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Brain.
    5. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-20, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    6. Cited for: IDENTIFICATION IN A COMPLEX WITH SEC62 AND SEC63, INTERACTION WITH SEC62.
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-14 AND SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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 SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Site-specific analysis of protein S-acylation by resin-assisted capture."
      Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A., Stamler J.S., Casey P.J.
      J. Lipid Res. 52:393-398(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-39, PALMITOYLATION AT CYS-39.
    14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT PRO-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSC61B_HUMAN
    AccessioniPrimary (citable) accession number: P60468
    Secondary accession number(s): P38390, P38391, Q6IBC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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

    External Data

    Dasty 3