ID PPIB_HUMAN Reviewed; 216 AA. AC P23284; A8K534; Q6IBH5; Q9BVK5; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 28-JAN-2026, entry version 236. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase B; DE Short=PPIase B; DE EC=5.2.1.8 {ECO:0000269|PubMed:20676357}; DE AltName: Full=CYP-S1; DE AltName: Full=Cyclophilin B; DE AltName: Full=Rotamase B; DE AltName: Full=S-cyclophilin; DE Short=SCYLP; DE Flags: Precursor; GN Name=PPIB; Synonyms=CYPB; 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]. RX PubMed=2040592; DOI=10.1016/s0021-9258(18)99078-2; RA Spik G., Haendler B., Delmas O., Mariller C., Chamoux M., Maes P., RA Tartar A., Montreuil J., Stedman K., Kocher H.P., Keller R., Hiestand P.C., RA Movva N.R.; RT "A novel secreted cyclophilin-like protein (SCYLP)."; RL J. Biol. Chem. 266:10735-10738(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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]. 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [6] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Prostate, and Skin; 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-216, AND PROTEIN SEQUENCE OF 34-48. RX PubMed=2000394; DOI=10.1073/pnas.88.5.1903; RA Price E.R., Zydowsky L.D., Jin M., Hunter C.H., McKeon F.D., Walsh C.T.; RT "Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl RT isomerase with a signal sequence."; RL Proc. Natl. Acad. Sci. U.S.A. 88:1903-1907(1991). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-216. RX PubMed=1710767; DOI=10.1128/mcb.11.7.3484-3491.1991; RA Hasel K.W., Glass J.R., Godbout M., Sutcliffe J.G.; RT "An endoplasmic reticulum-specific cyclophilin."; RL Mol. Cell. Biol. 11:3484-3491(1991). RN [10] RP COMPONENT OF A CHAPERONE COMPLEX. RX PubMed=12475965; DOI=10.1091/mbc.e02-05-0311; RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.; RT "A subset of chaperones and folding enzymes form multiprotein complexes in RT endoplasmic reticulum to bind nascent proteins."; RL Mol. Biol. Cell 13:4456-4469(2002). RN [11] RP PROTEIN SEQUENCE OF 52-59; 64-76; 91-101; 138-150; 164-172 AND 197-207, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [12] RP PROTEIN SEQUENCE OF 72-84 AND 159-165. RX PubMed=1286667; DOI=10.1002/elps.11501301199; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein RT database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [13] RP SUBCELLULAR LOCATION. RX PubMed=1530944; DOI=10.1083/jcb.116.1.113; RA Arber S., Krause K.-H., Caroni P.; RT "S-cyclophilin is retained intracellularly via a unique COOH-terminal RT sequence and colocalizes with the calcium storage protein calreticulin."; RL J. Cell Biol. 116:113-125(1992). RN [14] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [15] RP INVOLVEMENT IN OI9. RX PubMed=19781681; DOI=10.1016/j.ajhg.2009.09.001; RA van Dijk F.S., Nesbitt I.M., Zwikstra E.H., Nikkels P.G., Piersma S.R., RA Fratantoni S.A., Jimenez C.R., Huizer M., Morsman A.C., Cobben J.M., RA van Roij M.H., Elting M.W., Verbeke J.I., Wijnaendts L.C., Shaw N.J., RA Hogler W., McKeown C., Sistermans E.A., Dalton A., Meijers-Heijboer H., RA Pals G.; RT "PPIB mutations cause severe osteogenesis imperfecta."; RL Am. J. Hum. Genet. 85:521-527(2009). RN [16] RP INTERACTION WITH MEASLES VIRUS NUCLEOPROTEIN (MICROBIAL INFECTION), AND RP SUBCELLULAR LOCATION (MICROBIAL INFECTION). RX PubMed=20147391; DOI=10.1128/jvi.02168-09; RA Watanabe A., Yoneda M., Ikeda F., Terao-Muto Y., Sato H., Kai C.; RT "CD147/EMMPRIN acts as a functional entry receptor for measles virus on RT epithelial cells."; RL J. Virol. 84:4183-4193(2010). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=20676357; DOI=10.1371/journal.pbio.1000439; RA Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J., Paramanathan R., RA Bernstein G., MacKenzie F., Tempel W., Ouyang H., Lee W.H., RA Eisenmesser E.Z., Dhe-Paganon S.; RT "Structural and biochemical characterization of the human cyclophilin RT family of peptidyl-prolyl isomerases."; RL PLoS Biol. 8:E1000439-E1000439(2010). RN [18] 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 [19] RP INTERACTION WITH DYM. RX PubMed=21280149; DOI=10.1002/humu.21413; RA Denais C., Dent C.L., Southgate L., Hoyle J., Dafou D., Trembath R.C., RA Machado R.D.; RT "Dymeclin, the gene underlying Dyggve-Melchior-Clausen syndrome, encodes a RT protein integral to extracellular matrix and Golgi organization and is RT associated with protein secretion pathways critical in bone development."; RL Hum. Mutat. 32:231-239(2011). RN [20] 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 [21] 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 [22] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 39-216. RX PubMed=8197205; DOI=10.1073/pnas.91.11.5183; RA Mikol V., Kallen J., Walkinshaw M.D.; RT "X-ray structure of a cyclophilin B/cyclosporin complex: comparison with RT cyclophilin A and delineation of its calcineurin-binding domain."; RL Proc. Natl. Acad. Sci. U.S.A. 91:5183-5186(1994). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 34-216 IN COMPLEX WITH CLGN, RP MUTAGENESIS OF LYS-129, AND INTERACTION WITH CALR; CANX AND CLGN. RX PubMed=20801878; DOI=10.1074/jbc.m110.160101; RA Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F., RA Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.; RT "Structural basis of cyclophilin B binding by the calnexin/calreticulin P- RT domain."; RL J. Biol. Chem. 285:35551-35557(2010). RN [24] RP VARIANT OI9 ARG-9. RX PubMed=20089953; DOI=10.1056/nejmoa0907705; RA Barnes A.M., Carter E.M., Cabral W.A., Weis M., Chang W., Makareeva E., RA Leikin S., Rotimi C.N., Eyre D.R., Raggio C.L., Marini J.C.; RT "Lack of cyclophilin B in osteogenesis imperfecta with normal collagen RT folding."; RL N. Engl. J. Med. 362:521-528(2010). CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline CC imidic peptide bonds in oligopeptides and may therefore assist protein CC folding. {ECO:0000269|PubMed:20676357}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-peptidylproline (omega=180) = [protein]- CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, CC ChEBI:CHEBI:83834; EC=5.2.1.8; CC Evidence={ECO:0000269|PubMed:20676357}; CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA). CC {ECO:0000305|PubMed:20676357}. CC -!- SUBUNIT: Interacts with DYM. Interacts with CALR, CLGN and CANX. Part CC of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, CC HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small CC amounts of ERP29, but not, or at very low levels, CALR nor CANX CC (PubMed:12475965). {ECO:0000269|PubMed:12475965, CC ECO:0000269|PubMed:20801878, ECO:0000269|PubMed:21280149}. CC -!- SUBUNIT: (Microbial infection) Interacts with measles virus CC nucleoprotein. {ECO:0000269|PubMed:20147391}. CC -!- INTERACTION: CC P23284; Q8N9N5: BANP; NbExp=3; IntAct=EBI-359252, EBI-744695; CC P23284; Q7Z7K6: CENPV; NbExp=3; IntAct=EBI-359252, EBI-1210604; CC P23284; Q7RTS9: DYM; NbExp=4; IntAct=EBI-359252, EBI-2871106; CC P23284; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-359252, EBI-618189; CC P23284; O43292-2: GPAA1; NbExp=3; IntAct=EBI-359252, EBI-25884370; CC P23284; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-359252, EBI-11959863; CC P23284; P09017: HOXC4; NbExp=3; IntAct=EBI-359252, EBI-3923226; CC P23284; P17066: HSPA6; NbExp=3; IntAct=EBI-359252, EBI-355106; CC P23284; Q02363: ID2; NbExp=3; IntAct=EBI-359252, EBI-713450; CC P23284; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-359252, EBI-743960; CC P23284; Q9Y4X4: KLF12; NbExp=3; IntAct=EBI-359252, EBI-750750; CC P23284; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-359252, EBI-25835523; CC P23284; P13667: PDIA4; NbExp=2; IntAct=EBI-359252, EBI-1054653; CC P23284; P40855: PEX19; NbExp=6; IntAct=EBI-359252, EBI-594747; CC P23284; Q9NWS8-3: RMND1; NbExp=3; IntAct=EBI-359252, EBI-25884400; CC P23284; O43765: SGTA; NbExp=6; IntAct=EBI-359252, EBI-347996; CC P23284; Q96EQ0: SGTB; NbExp=4; IntAct=EBI-359252, EBI-744081; CC P23284; Q13586: STIM1; NbExp=3; IntAct=EBI-359252, EBI-448878; CC P23284; Q13061-2: TRDN; NbExp=3; IntAct=EBI-359252, EBI-17257686; CC P23284; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-359252, EBI-741480; CC P23284; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-359252, EBI-10173939; CC P23284; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-359252, EBI-947187; CC P23284; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-359252, EBI-12040603; CC P23284; A0A087WZY1; NbExp=3; IntAct=EBI-359252, EBI-13387614; CC P23284; PRO_0000037552 [Q9WMX2]; Xeno; NbExp=7; IntAct=EBI-359252, EBI-9005440; CC PRO_0000025479; P13667: PDIA4; NbExp=3; IntAct=EBI-8771982, EBI-1054653; CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:20147391}. CC Note=(Microbial infection). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen CC {ECO:0000269|PubMed:1530944}. Melanosome {ECO:0000269|PubMed:17081065}. CC Note=Identified by mass spectrometry in melanosome fractions from stage CC I to stage IV (PubMed:17081065). {ECO:0000269|PubMed:17081065}. CC -!- DISEASE: Osteogenesis imperfecta 9 (OI9) [MIM:259440]: A form of CC osteogenesis imperfecta, a disorder of bone formation characterized by CC low bone mass, bone fragility and susceptibility to fractures after CC minimal trauma. Disease severity ranges from very mild forms without CC fractures to intrauterine fractures and perinatal lethality. CC Extraskeletal manifestations, which affect a variable number of CC patients, are dentinogenesis imperfecta, hearing loss, and blue CC sclerae. OI9 is a severe autosomal recessive form of the disorder. CC {ECO:0000269|PubMed:19781681, ECO:0000269|PubMed:20089953}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B CC subfamily. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA52150.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database; Note=The CC PPIB gene homepage; CC URL="https://www.LOVD.nl/PPIB"; 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; M63573; AAA36601.1; -; mRNA. DR EMBL; AK291149; BAF83838.1; -; mRNA. DR EMBL; CR456829; CAG33110.1; -; mRNA. DR EMBL; AY962310; AAX44050.1; -; Genomic_DNA. DR EMBL; AC100840; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471082; EAW77669.1; -; Genomic_DNA. DR EMBL; BC001125; AAH01125.1; -; mRNA. DR EMBL; BC008848; AAH08848.1; -; mRNA. DR EMBL; BC020800; AAH20800.1; -; mRNA. DR EMBL; BC032138; AAH32138.1; -; mRNA. DR EMBL; M60857; AAA52150.1; ALT_INIT; mRNA. DR EMBL; M60457; AAA35733.1; -; mRNA. DR CCDS; CCDS10191.1; -. DR PIR; A39118; CSHUB. DR RefSeq; NP_000933.1; NM_000942.5. DR PDB; 1CYN; X-ray; 1.85 A; A=39-216. DR PDB; 3ICH; X-ray; 1.20 A; A=34-216. DR PDB; 3ICI; X-ray; 1.70 A; A/B=34-216. DR PDB; 8K0F; EM; 3.37 A; C=1-216. DR PDB; 8K0I; EM; 3.62 A; C/c=1-216. DR PDB; 8K0M; EM; 3.17 A; C=1-216. DR PDB; 8K17; EM; 3.18 A; C=1-216. DR PDB; 8KC9; EM; 3.75 A; C=1-216. DR PDBsum; 1CYN; -. DR PDBsum; 3ICH; -. DR PDBsum; 3ICI; -. DR PDBsum; 8K0F; -. DR PDBsum; 8K0I; -. DR PDBsum; 8K0M; -. DR PDBsum; 8K17; -. DR PDBsum; 8KC9; -. DR AlphaFoldDB; P23284; -. DR BMRB; P23284; -. DR EMDB; EMD-36763; -. DR EMDB; EMD-36765; -. DR EMDB; EMD-36774; -. DR EMDB; EMD-36787; -. DR EMDB; EMD-37097; -. DR SMR; P23284; -. DR BioGRID; 111475; 374. DR FunCoup; P23284; 2026. DR IntAct; P23284; 151. DR MINT; P23284; -. DR STRING; 9606.ENSP00000300026; -. DR BindingDB; P23284; -. DR ChEMBL; CHEMBL2075; -. DR DrugBank; DB04447; 1,4-Dithiothreitol. DR DrugBank; DB00172; Proline. DR DrugCentral; P23284; -. DR GlyConnect; 2943; 1 N-Linked glycan (1 site). DR GlyCosmos; P23284; 1 site, 2 glycans. DR GlyGen; P23284; 2 sites, 7 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P23284; -. DR MetOSite; P23284; -. DR PhosphoSitePlus; P23284; -. DR SwissPalm; P23284; -. DR BioMuta; PPIB; -. DR DMDM; 215273869; -. DR OGP; P23284; -. DR REPRODUCTION-2DPAGE; IPI00646304; -. DR jPOST; P23284; -. DR MassIVE; P23284; -. DR PaxDb; 9606-ENSP00000300026; -. DR PeptideAtlas; P23284; -. DR PRIDE; P23284; -. DR ProteomicsDB; 54078; -. DR Pumba; P23284; -. DR TopDownProteomics; P23284; -. DR Antibodypedia; 2584; 521 antibodies from 35 providers. DR DNASU; 5479; -. DR Ensembl; ENST00000300026.4; ENSP00000300026.4; ENSG00000166794.8. DR GeneID; 5479; -. DR KEGG; hsa:5479; -. DR MANE-Select; ENST00000300026.4; ENSP00000300026.4; NM_000942.5; NP_000933.1. DR UCSC; uc002and.4; human. DR AGR; HGNC:9255; -. DR ClinPGx; PA33580; -. DR CTD; 5479; -. DR DisGeNET; 5479; -. DR GeneCards; PPIB; -. DR HGNC; HGNC:9255; PPIB. DR HPA; ENSG00000166794; Low tissue specificity. DR MalaCards; PPIB; -. DR MIM; 123841; gene. DR MIM; 259440; phenotype. DR OpenTargets; ENSG00000166794; -. DR Orphanet; 216804; Osteogenesis imperfecta type 2. DR Orphanet; 216812; Osteogenesis imperfecta type 3. DR Orphanet; 216820; Osteogenesis imperfecta type 4. DR VEuPathDB; HostDB:ENSG00000166794; -. DR eggNOG; KOG0880; Eukaryota. DR GeneTree; ENSGT00940000158007; -. DR HOGENOM; CLU_012062_4_2_1; -. DR InParanoid; P23284; -. DR OMA; ENHEITH; -. DR OrthoDB; 193499at2759; -. DR PAN-GO; P23284; 6 GO annotations based on evolutionary models. DR PhylomeDB; P23284; -. DR BioCyc; MetaCyc:HS09452-MONOMER; -. DR BRENDA; 5.2.1.8; 2681. DR PathwayCommons; P23284; -. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses. DR SignaLink; P23284; -. DR Agora; ENSG00000166794; -. DR BioGRID-ORCS; 5479; 16 hits in 1159 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; PPIB; human. DR EvolutionaryTrace; P23284; -. DR GeneWiki; PPIB; -. DR GenomeRNAi; 5479; -. DR Pharos; P23284; Tchem. DR PRO; PR:P23284; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; P23284; protein. DR Bgee; ENSG00000166794; Expressed in stromal cell of endometrium and 213 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase. DR GO; GO:0032991; C:protein-containing complex; ISS:CAFA. DR GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0070063; F:RNA polymerase binding; IPI:AgBase. DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc. DR GO; GO:0060348; P:bone development; IMP:UniProtKB. DR GO; GO:0044829; P:host-mediated activation of viral genome replication; IMP:AgBase. DR GO; GO:0044794; P:host-mediated activation of viral process; IMP:AgBase. DR GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:UniProtKB. DR GO; GO:0006457; P:protein folding; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB. DR CDD; cd01926; cyclophilin_ABH_like; 1. DR FunFam; 2.40.100.10:FF:000001; Peptidyl-prolyl cis-trans isomerase; 1. DR Gene3D; 2.40.100.10; Cyclophilin-like; 1. DR InterPro; IPR029000; Cyclophilin-like_dom_sf. DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS. DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom. DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1. DR PANTHER; PTHR11071:SF477; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE B; 1. DR Pfam; PF00160; Pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR SUPFAM; SSF50891; Cyclophilin-like; 1. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant; KW Dwarfism; Endoplasmic reticulum; Glycoprotein; Isomerase; KW Osteogenesis imperfecta; Proteomics identification; Reference proteome; KW Rotamase; S-nitrosylation; Signal; Virion. FT SIGNAL 1..33 FT /evidence="ECO:0000269|PubMed:2000394" FT CHAIN 34..216 FT /note="Peptidyl-prolyl cis-trans isomerase B" FT /id="PRO_0000025479" FT DOMAIN 47..204 FT /note="PPIase cyclophilin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156" FT MOTIF 213..216 FT /note="Prevents secretion from ER" FT MOD_RES 84 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99KR7" FT MOD_RES 165 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99KR7" FT MOD_RES 202 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:Q99KR7" FT MOD_RES 209 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P24369" FT MOD_RES 209 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P24369" FT CARBOHYD 148 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 9 FT /note="M -> R (in OI9; patients have white sclerae, normal FT dentition, no rhizomelia or severe deformity of long bones; FT dbSNP:rs137853864)" FT /evidence="ECO:0000269|PubMed:20089953" FT /id="VAR_063436" FT VARIANT 60 FT /note="V -> L (in dbSNP:rs11558595)" FT /id="VAR_047711" FT MUTAGEN 129 FT /note="K->A: Impairs interaction with CLGN and CANX." FT /evidence="ECO:0000269|PubMed:20801878" FT CONFLICT 5 FT /note="S -> R (in Ref. 8; AAA52150)" FT /evidence="ECO:0000305" FT CONFLICT 216 FT /note="E -> D (in Ref. 3; CAG33110)" FT /evidence="ECO:0000305" FT STRAND 41..52 FT /evidence="ECO:0007829|PDB:3ICH" FT STRAND 55..64 FT /evidence="ECO:0007829|PDB:3ICH" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:3ICH" FT HELIX 70..81 FT /evidence="ECO:0007829|PDB:3ICH" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:3ICH" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:3ICH" FT TURN 98..100 FT /evidence="ECO:0007829|PDB:3ICH" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:3ICH" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:3ICH" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:3ICH" FT STRAND 118..121 FT /evidence="ECO:0007829|PDB:8K0M" FT STRAND 137..140 FT /evidence="ECO:0007829|PDB:3ICH" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:1CYN" FT STRAND 152..157 FT /evidence="ECO:0007829|PDB:3ICH" FT HELIX 160..162 FT /evidence="ECO:0007829|PDB:3ICH" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:3ICH" FT STRAND 168..174 FT /evidence="ECO:0007829|PDB:3ICH" FT HELIX 176..183 FT /evidence="ECO:0007829|PDB:3ICH" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:3ICH" FT STRAND 197..212 FT /evidence="ECO:0007829|PDB:3ICH" SQ SEQUENCE 216 AA; 23743 MW; 2D0410A07AA9E420 CRC64; MLRLSERNMK VLLAAALIAG SVFFLLLPGP SAADEKKKGP KVTVKVYFDL RIGDEDVGRV IFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF MIQGGDFTRG DGTGGKSIYG ERFPDENFKL KHYGPGWVSM ANAGKDTNGS QFFITTVKTA WLDGKHVVFG KVLEGMEVVR KVESTKTDSR DKPLKDVIIA DCGKIEVEKP FAIAKE //