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Protein

Translocon-associated protein subunit beta

Gene

SSR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_115902. 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
Synonyms:TRAPB
ORF Names:HSD25
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11324. SSR2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 149132LumenalSequence AnalysisAdd
BLAST
Transmembranei150 – 16920HelicalSequence AnalysisAdd
BLAST
Topological domaini170 – 18314CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: ProtInc
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36148.

Polymorphism and mutation databases

BioMutaiSSR2.
DMDMi1174451.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717By similarityAdd
BLAST
Chaini18 – 183166Translocon-associated protein subunit betaPRO_0000033290Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP43308.
PaxDbiP43308.
PRIDEiP43308.

PTM databases

PhosphoSiteiP43308.

Expressioni

Gene expression databases

BgeeiP43308.
CleanExiHS_SSR2.
ExpressionAtlasiP43308. baseline and differential.
GenevisibleiP43308. HS.

Organism-specific databases

HPAiHPA037787.

Interactioni

Subunit structurei

Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma. Interacts with TMEM173/STING.1 Publication

Protein-protein interaction databases

BioGridi112624. 2 interactions.
DIPiDIP-60652N.
IntActiP43308. 1 interaction.
STRINGi9606.ENSP00000295702.

Structurei

3D structure databases

ProteinModelPortaliP43308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TRAP-beta family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG292722.
GeneTreeiENSGT00390000005125.
HOVERGENiHBG000858.
InParanoidiP43308.
KOiK13250.
OMAiIVNLNEY.
OrthoDBiEOG7X0VK4.
PhylomeDBiP43308.
TreeFamiTF314461.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

P43308-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLSFVVLA LFAVTQAEEG 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 SKRKYDTPKT KKN
Length:183
Mass (Da):20,135
Last modified:November 1, 1995 - v1
Checksum:i575715449B8586D8
GO

Sequence cautioni

The sequence CAH72631.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAH72632.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461I → T in BAD96320 (Ref. 6) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74104 mRNA. Translation: CAA52207.1.
D37991 mRNA. Translation: BAA07206.1.
AY251536 mRNA. Translation: AAP20059.1.
CR456973 mRNA. Translation: CAG33254.1.
AK222600 mRNA. Translation: BAD96320.1.
AK313821 mRNA. Translation: BAG36556.1.
AL355388 Genomic DNA. Translation: CAH72631.1. Sequence problems.
AL355388 Genomic DNA. Translation: CAH72632.1. Sequence problems.
CH471121 Genomic DNA. Translation: EAW53010.1.
CH471121 Genomic DNA. Translation: EAW53011.1.
BC000341 mRNA. Translation: AAH00341.2.
CCDSiCCDS1126.1.
PIRiS41063.
RefSeqiNP_003136.1. NM_003145.3.
XP_011508226.1. XM_011509924.1.
UniGeneiHs.74564.

Genome annotation databases

EnsembliENST00000295702; ENSP00000295702; ENSG00000163479.
ENST00000480567; ENSP00000434306; ENSG00000163479.
GeneIDi6746.
KEGGihsa:6746.
UCSCiuc001fmx.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74104 mRNA. Translation: CAA52207.1.
D37991 mRNA. Translation: BAA07206.1.
AY251536 mRNA. Translation: AAP20059.1.
CR456973 mRNA. Translation: CAG33254.1.
AK222600 mRNA. Translation: BAD96320.1.
AK313821 mRNA. Translation: BAG36556.1.
AL355388 Genomic DNA. Translation: CAH72631.1. Sequence problems.
AL355388 Genomic DNA. Translation: CAH72632.1. Sequence problems.
CH471121 Genomic DNA. Translation: EAW53010.1.
CH471121 Genomic DNA. Translation: EAW53011.1.
BC000341 mRNA. Translation: AAH00341.2.
CCDSiCCDS1126.1.
PIRiS41063.
RefSeqiNP_003136.1. NM_003145.3.
XP_011508226.1. XM_011509924.1.
UniGeneiHs.74564.

3D structure databases

ProteinModelPortaliP43308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112624. 2 interactions.
DIPiDIP-60652N.
IntActiP43308. 1 interaction.
STRINGi9606.ENSP00000295702.

PTM databases

PhosphoSiteiP43308.

Polymorphism and mutation databases

BioMutaiSSR2.
DMDMi1174451.

Proteomic databases

MaxQBiP43308.
PaxDbiP43308.
PRIDEiP43308.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295702; ENSP00000295702; ENSG00000163479.
ENST00000480567; ENSP00000434306; ENSG00000163479.
GeneIDi6746.
KEGGihsa:6746.
UCSCiuc001fmx.3. human.

Organism-specific databases

CTDi6746.
GeneCardsiGC01M155989.
HGNCiHGNC:11324. SSR2.
HPAiHPA037787.
MIMi600867. gene.
neXtProtiNX_P43308.
PharmGKBiPA36148.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG292722.
GeneTreeiENSGT00390000005125.
HOVERGENiHBG000858.
InParanoidiP43308.
KOiK13250.
OMAiIVNLNEY.
OrthoDBiEOG7X0VK4.
PhylomeDBiP43308.
TreeFamiTF314461.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.

Miscellaneous databases

ChiTaRSiSSR2. human.
GeneWikiiSSR2.
GenomeRNAii6746.
NextBioi26314.
PROiP43308.
SOURCEiSearch...

Gene expression databases

BgeeiP43308.
CleanExiHS_SSR2.
ExpressionAtlasiP43308. baseline and differential.
GenevisibleiP43308. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of the beta subunit of the human translocon-associated protein."
    Bodescot M., Brison O.
    Biochim. Biophys. Acta 1217:101-102(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Colon carcinoma.
  2. "Isolation and mapping of the human beta-signal sequence receptor gene (SSR2)."
    Chinen K., Sudo K., Takahashi E., Nakamura Y.
    Cytogenet. Cell Genet. 70:215-217(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  3. "A new spermatogenesis-related gene."
    Wu N., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  4. "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].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Coronary artery.
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Lung.
  10. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
    Zhang H., Li X.-J., Martin D.B., Aebersold R.
    Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-88 AND ASN-104.
  11. "STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling."
    Ishikawa H., Barber G.N.
    Nature 455:674-678(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM173.
  12. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88 AND ASN-104.
    Tissue: Liver.

Entry informationi

Entry nameiSSRB_HUMAN
AccessioniPrimary (citable) accession number: P43308
Secondary accession number(s): B2R9K9
, D3DVA7, Q53HI0, Q5VY95, Q5VY96, Q6IB31, Q9BWE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 22, 2015
This is version 127 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 1
    Human chromosome 1: 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

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.