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Protein

Protein transport protein Sec61 subunit beta

Gene

SEC61B

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Necessary for protein translocation in the endoplasmic reticulum.

GO - Molecular functioni

  • poly(A) RNA binding Source: Ensembl
  • P-P-bond-hydrolysis-driven protein transmembrane transporter activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Protein transport protein Sec61 subunit beta
Gene namesi
Name:SEC61B
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Chromosome 11

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 7069CytoplasmicSequence analysisAdd
BLAST
Transmembranei71 – 9121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity1 Publication
Chaini2 – 9695Protein transport protein Sec61 subunit betaPRO_0000157253Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylprolineBy similarity
Modified residuei7 – 71PhosphoserineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei14 – 141PhosphoserineBy similarity
Modified residuei17 – 171PhosphoserineBy similarity
Lipidationi39 – 391S-palmitoyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP60467.
PRIDEiP60467.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi139931. 1 interaction.
IntActiP60467. 1 interaction.
STRINGi9615.ENSCAFP00000003690.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WWBelectron microscopy6.48C1-96[»]
4CG5electron microscopy7.40C61-96[»]
4CG6electron microscopy7.80C1-96[»]
4CG7electron microscopy6.90C61-96[»]
5A6Uelectron microscopy9.00B61-96[»]
ProteinModelPortaliP60467.
SMRiP60467. Positions 61-96.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60467.

Family & Domainsi

Sequence similaritiesi

Belongs to the SEC61-beta family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3457. Eukaryota.
ENOG4111UAR. LUCA.
GeneTreeiENSGT00390000003561.
HOGENOMiHOG000211109.
HOVERGENiHBG061281.
InParanoidiP60467.
KOiK09481.
OMAiHILAKIT.
OrthoDBiEOG77M8RR.
TreeFamiTF313144.

Family and domain databases

InterProiIPR030671. Sec61-beta/Sbh.
IPR016482. SecG/Sec61-beta/Sbh.
[Graphical view]
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.

P60467-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGPTPSGTN VGSSGRSPSK AVAARAAGST VRQRKNASCG TRSAGRTTSA
60 70 80 90
GTGGMWRFYT EDSPGLKVGP VPVLVMSLLF IASVFMLHIW GKYTRS
Length:96
Mass (Da):9,974
Last modified:January 23, 2007 - v2
Checksum:i5FAFF4197A62FA49
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25052 mRNA. Translation: AAA19639.1.
PIRiS42409.
RefSeqiNP_001003326.1. NM_001003326.1.
UniGeneiCfa.3895.

Genome annotation databases

EnsembliENSCAFT00000003996; ENSCAFP00000003690; ENSCAFG00000002533.
GeneIDi404018.
KEGGicfa:404018.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25052 mRNA. Translation: AAA19639.1.
PIRiS42409.
RefSeqiNP_001003326.1. NM_001003326.1.
UniGeneiCfa.3895.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WWBelectron microscopy6.48C1-96[»]
4CG5electron microscopy7.40C61-96[»]
4CG6electron microscopy7.80C1-96[»]
4CG7electron microscopy6.90C61-96[»]
5A6Uelectron microscopy9.00B61-96[»]
ProteinModelPortaliP60467.
SMRiP60467. Positions 61-96.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi139931. 1 interaction.
IntActiP60467. 1 interaction.
STRINGi9615.ENSCAFP00000003690.

Proteomic databases

PaxDbiP60467.
PRIDEiP60467.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000003996; ENSCAFP00000003690; ENSCAFG00000002533.
GeneIDi404018.
KEGGicfa:404018.

Organism-specific databases

CTDi10952.

Phylogenomic databases

eggNOGiKOG3457. Eukaryota.
ENOG4111UAR. LUCA.
GeneTreeiENSGT00390000003561.
HOGENOMiHOG000211109.
HOVERGENiHBG061281.
InParanoidiP60467.
KOiK09481.
OMAiHILAKIT.
OrthoDBiEOG77M8RR.
TreeFamiTF313144.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP60467.
NextBioi20817505.

Family and domain databases

InterProiIPR030671. Sec61-beta/Sbh.
IPR016482. SecG/Sec61-beta/Sbh.
[Graphical view]
PfamiPF03911. Sec61_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF006398. Sec61_beta_euk. 1 hit.
ProtoNetiSearch...

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], PROTEIN SEQUENCE OF 2-16; 78-81; 83-86 AND 88-97.
    Strain: Cocker spaniel.
    Tissue: Kidney.

Entry informationi

Entry nameiSC61B_CANLF
AccessioniPrimary (citable) accession number: P60467
Secondary accession number(s): P38390, P38391
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.