SRPRB_HUMAN
ID SRPRB_HUMAN Reviewed; 271 AA.
AC Q9Y5M8; Q6P595; Q8N2D8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Signal recognition particle receptor subunit beta;
DE Short=SR-beta;
DE AltName: Full=Protein APMCF1;
GN Name=SRPRB; ORFNames=PSEC0230;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary carcinoma;
RA Yan W., Zhu F., Chai Y., Zhao Z., Li Q., Wang C.;
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-9.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-9.
RC TISSUE=Colon, and Eye;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND THR-214, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9] {ECO:0007744|PDB:7NFX}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF SIGNAL RECOGNITION
RP PARTICLE IN COMPLEX WITH RIBOSOME NASCENT CHAIN COMPLEX AND THE SRP
RP RECEPTOR.
RX PubMed=34020957; DOI=10.1126/sciadv.abg0942;
RA Lee J.H., Jomaa A., Jomaa A., Chung S., Hwang Fu Y.H., Qian R., Sun X.,
RA Hsieh H.H., Chandrasekar S., Bi X., Mattei S., Boehringer D., Weiss S.,
RA Ban N., Shan S.O.;
RT "Receptor compaction and GTPase rearrangement drive SRP-mediated
RT cotranslational protein translocation into the ER.";
RL Sci. Adv. 7:942-942(2021).
CC -!- FUNCTION: Component of the signal recognition particle (SRP) complex
CC receptor (SR) (By similarity). Ensures, in conjunction with the SRP
CC complex, the correct targeting of the nascent secretory proteins to the
CC endoplasmic reticulum membrane system (By similarity). May mediate the
CC membrane association of SR (By similarity).
CC {ECO:0000250|UniProtKB:P47758}.
CC -!- SUBUNIT: Heterodimer with SRPRA. {ECO:0000250|UniProtKB:P47758}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O13950}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SRP receptor beta subunit family.
CC {ECO:0000305}.
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DR EMBL; AF141882; AAD34888.3; -; mRNA.
DR EMBL; AK027525; BAB55176.1; -; mRNA.
DR EMBL; AK075531; BAC11675.1; -; mRNA.
DR EMBL; BC063001; AAH63001.1; -; mRNA.
DR EMBL; BC065299; AAH65299.1; -; mRNA.
DR CCDS; CCDS3081.1; -.
DR RefSeq; NP_067026.3; NM_021203.3.
DR PDB; 7NFX; EM; 3.20 A; v=1-271.
DR PDBsum; 7NFX; -.
DR AlphaFoldDB; Q9Y5M8; -.
DR SMR; Q9Y5M8; -.
DR BioGRID; 121810; 283.
DR ComplexPortal; CPX-630; Signal recognition particle receptor complex.
DR DIP; DIP-50218N; -.
DR ELM; Q9Y5M8; -.
DR IntAct; Q9Y5M8; 119.
DR MINT; Q9Y5M8; -.
DR STRING; 9606.ENSP00000418401; -.
DR ChEMBL; CHEMBL4295993; -.
DR GlyGen; Q9Y5M8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y5M8; -.
DR PhosphoSitePlus; Q9Y5M8; -.
DR SwissPalm; Q9Y5M8; -.
DR BioMuta; SRPRB; -.
DR DMDM; 31340540; -.
DR EPD; Q9Y5M8; -.
DR jPOST; Q9Y5M8; -.
DR MassIVE; Q9Y5M8; -.
DR MaxQB; Q9Y5M8; -.
DR PaxDb; Q9Y5M8; -.
DR PeptideAtlas; Q9Y5M8; -.
DR PRIDE; Q9Y5M8; -.
DR ProteomicsDB; 86446; -.
DR TopDownProteomics; Q9Y5M8; -.
DR Antibodypedia; 2504; 365 antibodies from 24 providers.
DR DNASU; 58477; -.
DR Ensembl; ENST00000466490.7; ENSP00000418401.1; ENSG00000144867.13.
DR Ensembl; ENST00000678299.1; ENSP00000503923.1; ENSG00000144867.13.
DR GeneID; 58477; -.
DR KEGG; hsa:58477; -.
DR MANE-Select; ENST00000678299.1; ENSP00000503923.1; NM_001379313.1; NP_001366242.1.
DR UCSC; uc003epx.2; human.
DR CTD; 58477; -.
DR DisGeNET; 58477; -.
DR GeneCards; SRPRB; -.
DR HGNC; HGNC:24085; SRPRB.
DR HPA; ENSG00000144867; Low tissue specificity.
DR MIM; 616883; gene.
DR neXtProt; NX_Q9Y5M8; -.
DR OpenTargets; ENSG00000144867; -.
DR PharmGKB; PA128394701; -.
DR VEuPathDB; HostDB:ENSG00000144867; -.
DR eggNOG; KOG0090; Eukaryota.
DR GeneTree; ENSGT00940000154388; -.
DR HOGENOM; CLU_046625_2_0_1; -.
DR InParanoid; Q9Y5M8; -.
DR OMA; NKQDVAM; -.
DR OrthoDB; 1503159at2759; -.
DR PhylomeDB; Q9Y5M8; -.
DR TreeFam; TF106190; -.
DR BRENDA; 3.6.5.4; 2681.
DR PathwayCommons; Q9Y5M8; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q9Y5M8; -.
DR SIGNOR; Q9Y5M8; -.
DR BioGRID-ORCS; 58477; 444 hits in 1083 CRISPR screens.
DR ChiTaRS; SRPRB; human.
DR GeneWiki; SRPRB; -.
DR GenomeRNAi; 58477; -.
DR Pharos; Q9Y5M8; Tbio.
DR PRO; PR:Q9Y5M8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y5M8; protein.
DR Bgee; ENSG00000144867; Expressed in body of pancreas and 200 other tissues.
DR ExpressionAtlas; Q9Y5M8; baseline and differential.
DR Genevisible; Q9Y5M8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005785; C:signal recognition particle receptor complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
DR GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; IC:ComplexPortal.
DR CDD; cd04105; SR_beta; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019009; SRP_receptor_beta_su.
DR PANTHER; PTHR11485:SF34; PTHR11485:SF34; 1.
DR Pfam; PF09439; SRPRB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; GTP-binding; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..271
FT /note="Signal recognition particle receptor subunit beta"
FT /id="PRO_0000101227"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 71..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 92..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 9
FT /note="V -> L (in dbSNP:rs1107413)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_057335"
FT CONFLICT 137
FT /note="R -> G (in Ref. 2; BAB55176)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="D -> Y (in Ref. 2; BAB55176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 29702 MW; EC8DBCE9EE01B2B6 CRC64;
MASADSRRVA DGGGAGGTFQ PYLDTLRQEL QQTDPTLLSV VVAVLAVLLT LVFWKLIRSR
RSSQRAVLLV GLCDSGKTLL FVRLLTGLYR DTQTSITDSC AVYRVNNNRG NSLTLIDLPG
HESLRLQFLE RFKSSARAIV FVVDSAAFQR EVKDVAEFLY QVLIDSMGLK NTPSFLIACN
KQDIAMAKSA KLIQQQLEKE LNTLRVTRSA APSTLDSSST APAQLGKKGK EFEFSQLPLK
VEFLECSAKG GRGDVGSADI QDLEKWLAKI A
