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   10-JUN-2026, entry version 202.
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   -!- INTERACTION:
CC       Q9Y5M8; Q96JB5: CDK5RAP3; NbExp=3; IntAct=EBI-355393, EBI-718818;
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_001366242.1; NM_001379313.1.
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   EMDB; EMD-12303; -.
DR   SMR; Q9Y5M8; -.
DR   BioGRID; 121810; 382.
DR   ComplexPortal; CPX-630; Signal recognition particle receptor complex.
DR   DIP; DIP-50218N; -.
DR   ELM; Q9Y5M8; -.
DR   FunCoup; Q9Y5M8; 1507.
DR   IntAct; Q9Y5M8; 219.
DR   MINT; Q9Y5M8; -.
DR   NDEx; IQUERY-CP-SRPRB; 4 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000418401; -.
DR   ChEMBL; CHEMBL4295993; -.
DR   GlyCosmos; Q9Y5M8; 1 site, 1 glycan.
DR   GlyGen; Q9Y5M8; 5 sites, 2 O-linked glycans (5 sites).
DR   iPTMnet; Q9Y5M8; -.
DR   PhosphoSitePlus; Q9Y5M8; -.
DR   SwissPalm; Q9Y5M8; -.
DR   BioMuta; SRPRB; -.
DR   DMDM; 31340540; -.
DR   jPOST; Q9Y5M8; -.
DR   MassIVE; Q9Y5M8; -.
DR   PaxDb; 9606-ENSP00000418401; -.
DR   PeptideAtlas; Q9Y5M8; -.
DR   ProteomicsDB; 86446; -.
DR   Pumba; Q9Y5M8; -.
DR   TopDownProteomics; Q9Y5M8; -.
DR   Antibodypedia; 2504; 363 antibodies from 24 providers.
DR   DNASU; 58477; -.
DR   Ensembl; ENST00000466490.7; ENSP00000418401.1; ENSG00000144867.14.
DR   Ensembl; ENST00000678299.1; ENSP00000503923.1; ENSG00000144867.14.
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   AGR; HGNC:24085; -.
DR   ClinPGx; PA128394701; -.
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   OpenTargets; ENSG00000144867; -.
DR   VEuPathDB; HostDB:ENSG00000144867; -.
DR   eggNOG; KOG0090; Eukaryota.
DR   GeneTree; ENSGT00940000154388; -.
DR   HOGENOM; CLU_046625_2_0_1; -.
DR   InParanoid; Q9Y5M8; -.
DR   OMA; MNGVKVT; -.
DR   OrthoDB; 41266at2759; -.
DR   PAN-GO; Q9Y5M8; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9Y5M8; -.
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   Agora; ENSG00000144867; -.
DR   BioGRID-ORCS; 58477; 470 hits in 1162 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
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 202 other cell types or tissues.
DR   ExpressionAtlas; Q9Y5M8; baseline and differential.
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: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; NAS:ComplexPortal.
DR   CDD; cd04105; SR_beta; 1.
DR   FunFam; 3.40.50.300:FF:001173; signal recognition particle receptor subunit beta; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR024156; Small_GTPase_ARF.
DR   InterPro; IPR019009; SRP_receptor_beta_su.
DR   PANTHER; PTHR45909; ADP-RIBOSYLATION FACTOR-RELATED PROTEIN 1; 1.
DR   PANTHER; PTHR45909:SF1; ADP-RIBOSYLATION FACTOR-RELATED PROTEIN 1; 1.
DR   Pfam; PF09439; SRPRB; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Endoplasmic reticulum; GTP-binding; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Proteomics identification; Receptor;
KW   Reference proteome; 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"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   HELIX           77..83
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   STRAND          99..104
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   STRAND          106..109
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   STRAND          112..117
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   TURN            122..124
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   HELIX           125..132
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   STRAND          137..145
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   HELIX           152..167
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   STRAND          169..171
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   STRAND          174..180
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   HELIX           190..206
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   TURN            234..236
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   STRAND          241..245
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   HELIX           251..254
FT                   /evidence="ECO:0007829|PDB:7NFX"
FT   HELIX           262..270
FT                   /evidence="ECO:0007829|PDB:7NFX"
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
//