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Protein

Translocon-associated protein subunit beta

Gene

Ssr2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.

Enzyme and pathway databases

ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Translocon-associated protein subunit beta
Short name:
TRAP-beta
Alternative name(s):
Signal sequence receptor subunit beta
Short name:
SSR-beta
Gene namesi
Name:Ssr2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1913506. Ssr2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 146129LumenalSequence AnalysisAdd
BLAST
Transmembranei147 – 16721HelicalSequence AnalysisAdd
BLAST
Topological domaini168 – 18316CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717By similarityAdd
BLAST
Chaini18 – 183166Translocon-associated protein subunit betaPRO_0000033291Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi88 – 881N-linked (GlcNAc...) (high mannose)2 Publications
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9CPW5.
PRIDEiQ9CPW5.

PTM databases

PhosphoSiteiQ9CPW5.

Expressioni

Gene expression databases

BgeeiQ9CPW5.
CleanExiMM_SSR2.
GenevestigatoriQ9CPW5.

Interactioni

Subunit structurei

Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma. Interacts with TMEM173/STING (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9CPW5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TRAP-beta family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG292722.
GeneTreeiENSGT00390000005125.
HOGENOMiHOG000007980.
HOVERGENiHBG000858.
InParanoidiQ9CPW5.
KOiK13250.
OMAiKMRLLAF.
OrthoDBiEOG7X0VK4.
PhylomeDBiQ9CPW5.
TreeFamiTF314461.

Family and domain databases

InterProiIPR008856. TRAP_beta.
[Graphical view]
PANTHERiPTHR12861. PTHR12861. 1 hit.
PfamiPF05753. TRAP_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF016400. TRAP_beta. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9CPW5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLAVVVLA LLAVSQAEEG ARLLASKSLL NRYAVEGRDL TLQYNIYNVG
60 70 80 90 100
SSAALDVELS DDSFPPEDFG IVSGMLNVKW DRIAPASNVS HTVVLRPLKA
110 120 130 140 150
GYFNFTSATI TYLAQEDGPV VIGSTSAPGQ GGILAQREFD RRFSPHFLDW
160 170 180
AAFGVMTLPS IGIPLLLWYS SKRKYDTPKP KKN
Length:183
Mass (Da):20,019
Last modified:June 1, 2001 - v1
Checksum:iEFC743A84F02A4AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321G → E in BAB32009 (PubMed:16141072).Curated
Sequence conflicti163 – 1631I → M in AAH10214 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005340 mRNA. Translation: BAB23962.1.
AK007538 mRNA. Translation: BAB25097.1.
AK007720 mRNA. Translation: BAB25211.1.
AK010565 mRNA. Translation: BAB27030.1.
AK020145 mRNA. Translation: BAB32009.1.
AK050505 mRNA. Translation: BAC34295.1.
AK084530 mRNA. Translation: BAC39212.1.
BC010214 mRNA. Translation: AAH10214.1.
CCDSiCCDS17480.1.
RefSeqiNP_079724.1. NM_025448.3.
XP_006501941.1. XM_006501878.1.
UniGeneiMm.7091.

Genome annotation databases

EnsembliENSMUST00000035785; ENSMUSP00000045456; ENSMUSG00000041355.
ENSMUST00000195014; ENSMUSP00000141441; ENSMUSG00000041355.
GeneIDi66256.
KEGGimmu:66256.
UCSCiuc008pvs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005340 mRNA. Translation: BAB23962.1.
AK007538 mRNA. Translation: BAB25097.1.
AK007720 mRNA. Translation: BAB25211.1.
AK010565 mRNA. Translation: BAB27030.1.
AK020145 mRNA. Translation: BAB32009.1.
AK050505 mRNA. Translation: BAC34295.1.
AK084530 mRNA. Translation: BAC39212.1.
BC010214 mRNA. Translation: AAH10214.1.
CCDSiCCDS17480.1.
RefSeqiNP_079724.1. NM_025448.3.
XP_006501941.1. XM_006501878.1.
UniGeneiMm.7091.

3D structure databases

ProteinModelPortaliQ9CPW5.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9CPW5.

Proteomic databases

PaxDbiQ9CPW5.
PRIDEiQ9CPW5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035785; ENSMUSP00000045456; ENSMUSG00000041355.
ENSMUST00000195014; ENSMUSP00000141441; ENSMUSG00000041355.
GeneIDi66256.
KEGGimmu:66256.
UCSCiuc008pvs.1. mouse.

Organism-specific databases

CTDi6746.
MGIiMGI:1913506. Ssr2.

Phylogenomic databases

eggNOGiNOG292722.
GeneTreeiENSGT00390000005125.
HOGENOMiHOG000007980.
HOVERGENiHBG000858.
InParanoidiQ9CPW5.
KOiK13250.
OMAiKMRLLAF.
OrthoDBiEOG7X0VK4.
PhylomeDBiQ9CPW5.
TreeFamiTF314461.

Enzyme and pathway databases

ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.

Miscellaneous databases

ChiTaRSiSsr2. mouse.
NextBioi321109.
PROiQ9CPW5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CPW5.
CleanExiMM_SSR2.
GenevestigatoriQ9CPW5.

Family and domain databases

InterProiIPR008856. TRAP_beta.
[Graphical view]
PANTHERiPTHR12861. PTHR12861. 1 hit.
PfamiPF05753. TRAP_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF016400. TRAP_beta. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryonic heart, Embryonic stem cell and Pancreas.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis."
    Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K., Nishimura S.
    Mol. Cell. Proteomics 4:1977-1989(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88.
    Tissue: Epidermis.
  4. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88.

Entry informationi

Entry nameiSSRB_MOUSE
AccessioniPrimary (citable) accession number: Q9CPW5
Secondary accession number(s): Q91Z43, Q9CR94, Q9CX54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.