ID SERP1_HUMAN Reviewed; 66 AA. AC Q9Y6X1; D3DNI6; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 10-JUN-2026, entry version 169. DE RecName: Full=Stress-associated endoplasmic reticulum protein 1; DE AltName: Full=Ribosome-attached membrane protein 4; GN Name=SERP1; Synonyms=RAMP4; 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]. RA Yamaguchi A., Hori O., Ogawa S.; RT "Human SERP1."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Adrenal gland; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; 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). CC -!- FUNCTION: Interacts with target proteins during their translocation CC into the lumen of the endoplasmic reticulum. Protects unfolded target CC proteins against degradation during ER stress. May facilitate CC glycosylation of target proteins after termination of ER stress. May CC modulate the use of N-glycosylation sites on target proteins. CC {ECO:0000250|UniProtKB:Q9R2C1}. CC -!- SUBUNIT: Interacts with SEC61B, SEC61A1 and the SEC61 complex. CC Interacts with CANX. {ECO:0000250|UniProtKB:Q9R2C1}. CC -!- INTERACTION: CC Q9Y6X1; Q92685: ALG3; NbExp=3; IntAct=EBI-10329948, EBI-2848814; CC Q9Y6X1; Q96BI3: APH1A; NbExp=3; IntAct=EBI-10329948, EBI-2606935; CC Q9Y6X1; Q13520: AQP6; NbExp=3; IntAct=EBI-10329948, EBI-13059134; CC Q9Y6X1; O94778: AQP8; NbExp=3; IntAct=EBI-10329948, EBI-19124986; CC Q9Y6X1; Q13323: BIK; NbExp=3; IntAct=EBI-10329948, EBI-700794; CC Q9Y6X1; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-10329948, EBI-11532900; CC Q9Y6X1; P04233-2: CD74; NbExp=3; IntAct=EBI-10329948, EBI-12222807; CC Q9Y6X1; P11912: CD79A; NbExp=3; IntAct=EBI-10329948, EBI-7797864; CC Q9Y6X1; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-10329948, EBI-17233035; CC Q9Y6X1; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-10329948, EBI-8637742; CC Q9Y6X1; Q15125: EBP; NbExp=3; IntAct=EBI-10329948, EBI-3915253; CC Q9Y6X1; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-10329948, EBI-18636064; CC Q9Y6X1; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10329948, EBI-18304435; CC Q9Y6X1; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-10329948, EBI-18938272; CC Q9Y6X1; A2A2Y4: FRMD3; NbExp=3; IntAct=EBI-10329948, EBI-6911547; CC Q9Y6X1; O75712: GJB3; NbExp=3; IntAct=EBI-10329948, EBI-3908586; CC Q9Y6X1; O95377: GJB5; NbExp=3; IntAct=EBI-10329948, EBI-3909454; CC Q9Y6X1; Q9NS71: GKN1; NbExp=3; IntAct=EBI-10329948, EBI-3933251; CC Q9Y6X1; O60883: GPR37L1; NbExp=3; IntAct=EBI-10329948, EBI-2927498; CC Q9Y6X1; Q8TED1: GPX8; NbExp=3; IntAct=EBI-10329948, EBI-11721746; CC Q9Y6X1; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-10329948, EBI-18053395; CC Q9Y6X1; P26951: IL3RA; NbExp=3; IntAct=EBI-10329948, EBI-1757512; CC Q9Y6X1; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-10329948, EBI-10266796; CC Q9Y6X1; Q9H3M0: KCNF1; NbExp=4; IntAct=EBI-10329948, EBI-6918743; CC Q9Y6X1; Q8N743: KIR3DL3; NbExp=3; IntAct=EBI-10329948, EBI-17272405; CC Q9Y6X1; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-10329948, EBI-2820517; CC Q9Y6X1; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-10329948, EBI-373355; CC Q9Y6X1; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-10329948, EBI-3923617; CC Q9Y6X1; Q8TBJ4: PLPPR1; NbExp=3; IntAct=EBI-10329948, EBI-18063495; CC Q9Y6X1; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-10329948, EBI-7545592; CC Q9Y6X1; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-10329948, EBI-3920694; CC Q9Y6X1; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-10329948, EBI-2855401; CC Q9Y6X1; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-10329948, EBI-18159983; CC Q9Y6X1; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-10329948, EBI-17295964; CC Q9Y6X1; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-10329948, EBI-17280858; CC Q9Y6X1; Q16623: STX1A; NbExp=3; IntAct=EBI-10329948, EBI-712466; CC Q9Y6X1; P32856-2: STX2; NbExp=3; IntAct=EBI-10329948, EBI-11956649; CC Q9Y6X1; Q12846: STX4; NbExp=3; IntAct=EBI-10329948, EBI-744942; CC Q9Y6X1; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-10329948, EBI-12947623; CC Q9Y6X1; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-10329948, EBI-8638294; CC Q9Y6X1; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-10329948, EBI-18178701; CC Q9Y6X1; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-10329948, EBI-8649725; CC Q9Y6X1; Q07011: TNFRSF9; NbExp=3; IntAct=EBI-10329948, EBI-12945620; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9R2C1}; Single- CC pass membrane protein {ECO:0000250|UniProtKB:Q9R2C1}. Endoplasmic CC reticulum membrane {ECO:0000250|UniProtKB:Q9R2C1}; Single-pass membrane CC protein {ECO:0000250|UniProtKB:Q9R2C1}. CC -!- SIMILARITY: Belongs to the RAMP4 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB022427; BAA81895.1; -; mRNA. DR EMBL; AF136975; AAG49436.1; -; mRNA. DR EMBL; AL136807; CAB66741.1; -; mRNA. DR EMBL; CR533472; CAG38503.1; -; mRNA. DR EMBL; CH471052; EAW78834.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78835.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78836.1; -; Genomic_DNA. DR EMBL; BC108314; AAI08315.1; -; mRNA. DR EMBL; BC112364; AAI12365.1; -; mRNA. DR EMBL; BC112365; AAI12366.1; -; mRNA. DR CCDS; CCDS3150.1; -. DR RefSeq; NP_055260.1; NM_014445.4. DR PDB; 9N9J; EM; 3.20 A; G=1-66. DR PDB; 9YGY; EM; 4.10 A; G=1-66. DR PDBsum; 9N9J; -. DR PDBsum; 9YGY; -. DR AlphaFoldDB; Q9Y6X1; -. DR EMDB; EMD-49171; -. DR EMDB; EMD-72945; -. DR SMR; Q9Y6X1; -. DR BioGRID; 118079; 69. DR FunCoup; Q9Y6X1; 1041. DR IntAct; Q9Y6X1; 44. DR STRING; 9606.ENSP00000420076; -. DR iPTMnet; Q9Y6X1; -. DR PhosphoSitePlus; Q9Y6X1; -. DR BioMuta; SERP1; -. DR DMDM; 74721555; -. DR jPOST; Q9Y6X1; -. DR MassIVE; Q9Y6X1; -. DR PaxDb; 9606-ENSP00000420076; -. DR PeptideAtlas; Q9Y6X1; -. DR ProteomicsDB; 86809; -. DR TopDownProteomics; Q9Y6X1; -. DR Antibodypedia; 46738; 108 antibodies from 24 providers. DR DNASU; 27230; -. DR Ensembl; ENST00000239944.7; ENSP00000239944.2; ENSG00000120742.12. DR Ensembl; ENST00000479209.1; ENSP00000420076.1; ENSG00000120742.12. DR GeneID; 27230; -. DR KEGG; hsa:27230; -. DR MANE-Select; ENST00000239944.7; ENSP00000239944.2; NM_014445.4; NP_055260.1. DR UCSC; uc003exy.4; human. DR AGR; HGNC:10759; -. DR ClinPGx; PA162402942; -. DR CTD; 27230; -. DR DisGeNET; 27230; -. DR GeneCards; SERP1; -. DR HGNC; HGNC:10759; SERP1. DR HPA; ENSG00000120742; Low tissue specificity. DR MIM; 617674; gene. DR OpenTargets; ENSG00000120742; -. DR VEuPathDB; HostDB:ENSG00000120742; -. DR eggNOG; KOG3491; Eukaryota. DR GeneTree; ENSGT00940000161729; -. DR HOGENOM; CLU_160944_3_0_1; -. DR InParanoid; Q9Y6X1; -. DR OMA; WIRMANE; -. DR OrthoDB; 16679at2759; -. DR PAN-GO; Q9Y6X1; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q9Y6X1; -. DR PathwayCommons; Q9Y6X1; -. DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes. DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. DR SignaLink; Q9Y6X1; -. DR Agora; ENSG00000120742; -. DR BioGRID-ORCS; 27230; 24 hits in 1146 CRISPR screens. DR ChiTaRS; SERP1; human. DR GeneWiki; SERP1; -. DR GenomeRNAi; 27230; -. DR Pharos; Q9Y6X1; Tbio. DR PRO; PR:Q9Y6X1; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9Y6X1; protein. DR Bgee; ENSG00000120742; Expressed in parotid gland and 207 other cell types or tissues. DR ExpressionAtlas; Q9Y6X1; baseline and differential. DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005840; C:ribosome; TAS:ProtInc. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central. DR GO; GO:0009101; P:glycoprotein biosynthetic process; TAS:ProtInc. DR GO; GO:0007009; P:plasma membrane organization; TAS:ProtInc. DR GO; GO:0036211; P:protein modification process; TAS:ProtInc. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR010580; ER_stress-assoc. DR PANTHER; PTHR15601; STRESS ASSOCIATED ENDOPLASMIC RETICULUM PROTEIN SERP1/RAMP4; 1. DR PANTHER; PTHR15601:SF14; STRESS-ASSOCIATED ENDOPLASMIC RETICULUM PROTEIN 1; 1. DR Pfam; PF06624; RAMP4; 1. PE 1: Evidence at protein level; KW 3D-structure; Endoplasmic reticulum; Membrane; Protein transport; KW Proteomics identification; Reference proteome; Translocation; KW Transmembrane; Transmembrane helix; Transport; Unfolded protein response. FT CHAIN 1..66 FT /note="Stress-associated endoplasmic reticulum protein 1" FT /id="PRO_0000274794" FT TRANSMEM 39..59 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 17..30 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 66 AA; 7374 MW; DC15C0143AAE0D91 CRC64; MVAKQRIRMA NEKHSKNITQ RGNVAKTSRN APEEKASVGP WLLALFIFVV CGSAIFQIIQ SIRMGM //