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SSRB_MOUSE
ID   SSRB_MOUSE              Reviewed;         183 AA.
AC   Q9CPW5; Q91Z43; Q9CR94; Q9CX54;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Translocon-associated protein subunit beta;
DE            Short=TRAP-beta;
DE   AltName: Full=Signal sequence receptor subunit beta;
DE            Short=SSR-beta;
DE   Flags: Precursor;
GN   Name=Ssr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Embryonic heart, Embryonic stem cell, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88.
RC   TISSUE=Epidermis;
RX   PubMed=16170054; DOI=10.1074/mcp.m500203-mcp200;
RA   Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K.,
RA   Nishimura S.;
RT   "High throughput quantitative glycomics and glycoform-focused proteomics of
RT   murine dermis and epidermis.";
RL   Mol. Cell. Proteomics 4:1977-1989(2005).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: TRAP proteins are part of a complex whose function is to bind
CC       calcium to the ER membrane and thereby regulate the retention of ER
CC       resident proteins.
CC   -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-
CC       gamma. Interacts with STING1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAP-beta family. {ECO:0000305}.
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DR   EMBL; AK005340; BAB23962.1; -; mRNA.
DR   EMBL; AK007538; BAB25097.1; -; mRNA.
DR   EMBL; AK007720; BAB25211.1; -; mRNA.
DR   EMBL; AK010565; BAB27030.1; -; mRNA.
DR   EMBL; AK020145; BAB32009.1; -; mRNA.
DR   EMBL; AK050505; BAC34295.1; -; mRNA.
DR   EMBL; AK084530; BAC39212.1; -; mRNA.
DR   EMBL; BC010214; AAH10214.1; -; mRNA.
DR   CCDS; CCDS17480.1; -.
DR   RefSeq; NP_079724.1; NM_025448.3.
DR   RefSeq; XP_006501941.1; XM_006501878.2.
DR   AlphaFoldDB; Q9CPW5; -.
DR   STRING; 10090.ENSMUSP00000045456; -.
DR   GlyConnect; 2780; 7 N-Linked glycans (2 sites).
DR   GlyGen; Q9CPW5; 2 sites, 6 N-linked glycans (2 sites).
DR   iPTMnet; Q9CPW5; -.
DR   PhosphoSitePlus; Q9CPW5; -.
DR   MaxQB; Q9CPW5; -.
DR   PaxDb; Q9CPW5; -.
DR   PeptideAtlas; Q9CPW5; -.
DR   PRIDE; Q9CPW5; -.
DR   ProteomicsDB; 257080; -.
DR   TopDownProteomics; Q9CPW5; -.
DR   Antibodypedia; 20426; 185 antibodies from 24 providers.
DR   DNASU; 66256; -.
DR   Ensembl; ENSMUST00000035785; ENSMUSP00000045456; ENSMUSG00000041355.
DR   Ensembl; ENSMUST00000195014; ENSMUSP00000141441; ENSMUSG00000041355.
DR   GeneID; 66256; -.
DR   KEGG; mmu:66256; -.
DR   UCSC; uc008pvs.1; mouse.
DR   CTD; 6746; -.
DR   MGI; MGI:1913506; Ssr2.
DR   VEuPathDB; HostDB:ENSMUSG00000041355; -.
DR   eggNOG; KOG3317; Eukaryota.
DR   GeneTree; ENSGT00390000005125; -.
DR   HOGENOM; CLU_102025_1_0_1; -.
DR   InParanoid; Q9CPW5; -.
DR   OMA; ILWHSSK; -.
DR   OrthoDB; 1286165at2759; -.
DR   PhylomeDB; Q9CPW5; -.
DR   TreeFam; TF314461; -.
DR   BioGRID-ORCS; 66256; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Ssr2; mouse.
DR   PRO; PR:Q9CPW5; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9CPW5; protein.
DR   Bgee; ENSMUSG00000041355; Expressed in yolk sac and 277 other tissues.
DR   ExpressionAtlas; Q9CPW5; baseline and differential.
DR   Genevisible; Q9CPW5; MM.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   InterPro; IPR008856; TRAP_beta.
DR   PIRSF; PIRSF016400; TRAP_beta; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000250"
FT   CHAIN           18..183
FT                   /note="Translocon-associated protein subunit beta"
FT                   /id="PRO_0000033291"
FT   TOPO_DOM        18..146
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        168..183
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16170054,
FT                   ECO:0000269|PubMed:19349973"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        132
FT                   /note="G -> E (in Ref. 1; BAB32009)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="I -> M (in Ref. 2; AAH10214)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   183 AA;  20019 MW;  EFC743A84F02A4AF CRC64;
     MRLLAVVVLA LLAVSQAEEG ARLLASKSLL NRYAVEGRDL TLQYNIYNVG SSAALDVELS
     DDSFPPEDFG IVSGMLNVKW DRIAPASNVS HTVVLRPLKA GYFNFTSATI TYLAQEDGPV
     VIGSTSAPGQ GGILAQREFD RRFSPHFLDW AAFGVMTLPS IGIPLLLWYS SKRKYDTPKP
     KKN
 
 
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