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P60468 (SC61B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein transport protein Sec61 subunit beta
Gene names
Name:SEC61B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length96 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Necessary for protein translocation in the endoplasmic reticulum.

Subunit structure

Heterotrimeric complex composed of SEC61-alpha, SEC61-beta and SEC61-gamma. Part of a complex composed of SEC61, SEC62 and SEC63. Interacts with SEC62. Ref.6

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein.

Sequence similarities

Belongs to the SEC61-beta family.

Ontologies

Keywords
   Biological processProtein transport
Translocation
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   PTMAcetylation
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 8945469. Source: UniProtKB

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

protein import into nucleus, translocation

Inferred from mutant phenotype PubMed 17215517. Source: UniProtKB

retrograde protein transport, ER to cytosol

Inferred from mutant phenotype PubMed 17215517. Source: UniProtKB

translation

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum

Inferred from direct assay. Source: HPA

endoplasmic reticulum Sec complex

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Non-traceable author statement Ref.1. Source: UniProtKB

membrane

Inferred from direct assay PubMed 22375059. Source: MGI

   Molecular_functionepidermal growth factor binding

Inferred from physical interaction PubMed 19602593. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

ribosome binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BCAP31P515727EBI-1788819,EBI-77683

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.14
Chain2 – 9695Protein transport protein Sec61 subunit beta
PRO_0000157254

Regions

Topological domain2 – 7069Cytoplasmic Potential
Transmembrane71 – 9121Helical; Potential

Amino acid modifications

Modified residue21N-acetylproline Ref.14
Modified residue71Phosphoserine Ref.5
Modified residue131Phosphoserine Ref.8
Modified residue141Phosphoserine Ref.8
Modified residue171Phosphoserine Ref.8 Ref.11 Ref.14
Lipidation391S-palmitoyl cysteine Probable

Experimental info

Mutagenesis391C → S: Abolishes S-acylation. Ref.13

Sequences

Sequence LengthMass (Da)Tools
P60468 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5FAFF4197A62FA49

FASTA969,974
        10         20         30         40         50         60 
MPGPTPSGTN VGSSGRSPSK AVAARAAGST VRQRKNASCG TRSAGRTTSA GTGGMWRFYT 

        70         80         90 
EDSPGLKVGP VPVLVMSLLF IASVFMLHIW GKYTRS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Mammalian Sec61 is associated with Sec62 and Sec63."
Meyer H.-A., Grau H., Kraft R., Kostka S., Prehn S., Kalies K.-U., Hartmann E.
J. Biol. Chem. 275:14550-14557(2000) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L25085 mRNA. Translation: AAA19706.1.
CR456883 mRNA. Translation: CAG33164.1.
AL137067 Genomic DNA. Translation: CAC08000.1.
BC001734 mRNA. Translation: AAH01734.1.
PIRS42410.
RefSeqNP_006799.1. NM_006808.2.
UniGeneHs.191887.

3D structure databases

ProteinModelPortalP60468.
SMRP60468. Positions 61-96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116152. 25 interactions.
DIPDIP-40997N.
IntActP60468. 9 interactions.
MINTMINT-106933.
STRING9606.ENSP00000223641.

Protein family/group databases

TCDB3.A.5.9.1. the general secretory pathway (sec) family.

PTM databases

PhosphoSiteP60468.

Polymorphism databases

DMDM42560366.

Proteomic databases

PaxDbP60468.
PeptideAtlasP60468.
PRIDEP60468.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000223641; ENSP00000223641; ENSG00000106803.
GeneID10952.
KEGGhsa:10952.
UCSCuc004azh.3. human.

Organism-specific databases

CTD10952.
GeneCardsGC09P101984.
HGNCHGNC:16993. SEC61B.
HPAHPA049407.
MIM609214. gene.
neXtProtNX_P60468.
PharmGKBPA134888963.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248540.
HOGENOMHOG000211109.
HOVERGENHBG061281.
InParanoidP60468.
KOK09481.
OMAHILAKIT.
OrthoDBEOG77M8RR.
PhylomeDBP60468.
TreeFamTF313144.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

BgeeP60468.
CleanExHS_SEC61B.
GenevestigatorP60468.

Family and domain databases

InterProIPR016482. SecG/Sec61-beta/Sbh1.
[Graphical view]
PANTHERPTHR13509. PTHR13509. 1 hit.
PfamPF03911. Sec61_beta. 1 hit.
[Graphical view]
PIRSFPIRSF006398. Sec61_beta_euk. 1 hit.
ProtoNetSearch...

Other

GeneWikiSEC61B.
GenomeRNAi10952.
NextBio41613.
PROP60468.
SOURCESearch...

Entry information

Entry nameSC61B_HUMAN
AccessionPrimary (citable) accession number: P60468
Secondary accession number(s): P38390, P38391, Q6IBC1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM