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P23284

- PPIB_HUMAN

UniProt

P23284 - PPIB_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase B

Gene

PPIB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).

    Enzyme regulationi

    Cyclosporin A (CsA) inhibits CYPB.

    GO - Molecular functioni

    1. peptide binding Source: UniProtKB-KW
    2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein complex binding Source: UniProt
    6. unfolded protein binding Source: ProtInc

    GO - Biological processi

    1. bone development Source: UniProt
    2. chaperone-mediated protein folding Source: UniProt
    3. extracellular matrix organization Source: Reactome
    4. positive regulation of multicellular organism growth Source: UniProt
    5. protein peptidyl-prolyl isomerization Source: UniProt
    6. protein stabilization Source: UniProt

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Ligandi

    Cyclosporin

    Enzyme and pathway databases

    ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase B (EC:5.2.1.8)
    Short name:
    PPIase B
    Alternative name(s):
    CYP-S1
    Cyclophilin B
    Rotamase B
    S-cyclophilin
    Short name:
    SCYLP
    Gene namesi
    Name:PPIB
    Synonyms:CYPB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:9255. PPIB.

    Subcellular locationi

    Endoplasmic reticulum lumen. Melanosome
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProt
    2. endoplasmic reticulum lumen Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. macromolecular complex Source: UniProt
    5. melanosome Source: UniProtKB-SubCell
    6. membrane Source: UniProtKB
    7. nucleus Source: UniProt

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Osteogenesis imperfecta 9 (OI9) [MIM:259440]: A form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI9 is a severe autosomal recessive form of the disorder.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91M → R in OI9; patients have white sclerae, normal dentition, no rhizomelia or severe deformity of long bones. 1 Publication
    VAR_063436

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi129 – 1291K → A: Impairs interaction with CLGN and CANX. 1 Publication

    Keywords - Diseasei

    Disease mutation, Dwarfism, Osteogenesis imperfecta

    Organism-specific databases

    MIMi259440. phenotype.
    Orphaneti216804. Osteogenesis imperfecta type 2.
    216812. Osteogenesis imperfecta type 3.
    216820. Osteogenesis imperfecta type 4.
    PharmGKBiPA33580.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 33331 PublicationAdd
    BLAST
    Chaini34 – 216183Peptidyl-prolyl cis-trans isomerase BPRO_0000025479Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence Analysis
    Modified residuei209 – 2091N6-acetyllysine; alternateBy similarity
    Modified residuei209 – 2091N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    MaxQBiP23284.
    PaxDbiP23284.
    PRIDEiP23284.

    2D gel databases

    OGPiP23284.
    REPRODUCTION-2DPAGEIPI00646304.
    SWISS-2DPAGEP23284.

    PTM databases

    PhosphoSiteiP23284.

    Expressioni

    Gene expression databases

    BgeeiP23284.
    CleanExiHS_PPIB.
    GenevestigatoriP23284.

    Organism-specific databases

    HPAiCAB011487.
    HPA012720.

    Interactioni

    Subunit structurei

    Interacts with DYM. Interacts with CALR, CLGN and CANX.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDIA4P136673EBI-8771982,EBI-1054653

    Protein-protein interaction databases

    BioGridi111475. 48 interactions.
    IntActiP23284. 23 interactions.
    MINTiMINT-1142578.
    STRINGi9606.ENSP00000300026.

    Structurei

    Secondary structure

    1
    216
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi41 – 5212
    Beta strandi55 – 6410
    Turni66 – 683
    Helixi70 – 8112
    Turni82 – 843
    Beta strandi95 – 973
    Turni98 – 1003
    Beta strandi101 – 1044
    Turni107 – 1093
    Beta strandi110 – 1134
    Beta strandi137 – 1404
    Beta strandi142 – 1443
    Beta strandi152 – 1576
    Helixi160 – 1623
    Turni163 – 1653
    Beta strandi168 – 1747
    Helixi176 – 1838
    Beta strandi193 – 1953
    Beta strandi197 – 21216

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CYNX-ray1.85A39-216[»]
    3ICHX-ray1.20A34-216[»]
    3ICIX-ray1.70A/B34-216[»]
    ProteinModelPortaliP23284.
    SMRiP23284. Positions 37-216.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23284.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini47 – 204158PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi213 – 2164Prevents secretion from ER

    Sequence similaritiesi

    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0652.
    HOGENOMiHOG000065981.
    HOVERGENiHBG001065.
    InParanoidiP23284.
    KOiK03768.
    OMAiPAYANED.
    OrthoDBiEOG7RFTK4.
    PhylomeDBiP23284.
    TreeFamiTF354259.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view]
    PfamiPF00160. Pro_isomerase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSiPR00153. CSAPPISMRASE.
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P23284-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRLSERNMK VLLAAALIAG SVFFLLLPGP SAADEKKKGP KVTVKVYFDL    50
    RIGDEDVGRV IFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF 100
    MIQGGDFTRG DGTGGKSIYG ERFPDENFKL KHYGPGWVSM ANAGKDTNGS 150
    QFFITTVKTA WLDGKHVVFG KVLEGMEVVR KVESTKTDSR DKPLKDVIIA 200
    DCGKIEVEKP FAIAKE 216
    Length:216
    Mass (Da):23,743
    Last modified:November 25, 2008 - v2
    Checksum:i2D0410A07AA9E420
    GO

    Sequence cautioni

    The sequence AAA52150.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51S → R in AAA52150. (PubMed:2000394)Curated
    Sequence conflicti216 – 2161E → D in CAG33110. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91M → R in OI9; patients have white sclerae, normal dentition, no rhizomelia or severe deformity of long bones. 1 Publication
    VAR_063436
    Natural varianti60 – 601V → L.
    Corresponds to variant rs11558595 [ dbSNP | Ensembl ].
    VAR_047711

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63573 mRNA. Translation: AAA36601.1.
    AK291149 mRNA. Translation: BAF83838.1.
    CR456829 mRNA. Translation: CAG33110.1.
    AY962310 Genomic DNA. Translation: AAX44050.1.
    AC100840 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77669.1.
    BC001125 mRNA. Translation: AAH01125.1.
    BC008848 mRNA. Translation: AAH08848.1.
    BC020800 mRNA. Translation: AAH20800.1.
    BC032138 mRNA. Translation: AAH32138.1.
    M60857 mRNA. Translation: AAA52150.1. Different initiation.
    M60457 mRNA. Translation: AAA35733.1.
    CCDSiCCDS10191.1.
    PIRiA39118. CSHUB.
    RefSeqiNP_000933.1. NM_000942.4.
    UniGeneiHs.434937.

    Genome annotation databases

    EnsembliENST00000300026; ENSP00000300026; ENSG00000166794.
    GeneIDi5479.
    KEGGihsa:5479.
    UCSCiuc002and.3. human.

    Polymorphism databases

    DMDMi215273869.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Osteogenesis imperfecta variant database

    Peptidyl-prolyl cis-trans isomerase B (PPIB)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63573 mRNA. Translation: AAA36601.1 .
    AK291149 mRNA. Translation: BAF83838.1 .
    CR456829 mRNA. Translation: CAG33110.1 .
    AY962310 Genomic DNA. Translation: AAX44050.1 .
    AC100840 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77669.1 .
    BC001125 mRNA. Translation: AAH01125.1 .
    BC008848 mRNA. Translation: AAH08848.1 .
    BC020800 mRNA. Translation: AAH20800.1 .
    BC032138 mRNA. Translation: AAH32138.1 .
    M60857 mRNA. Translation: AAA52150.1 . Different initiation.
    M60457 mRNA. Translation: AAA35733.1 .
    CCDSi CCDS10191.1.
    PIRi A39118. CSHUB.
    RefSeqi NP_000933.1. NM_000942.4.
    UniGenei Hs.434937.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CYN X-ray 1.85 A 39-216 [» ]
    3ICH X-ray 1.20 A 34-216 [» ]
    3ICI X-ray 1.70 A/B 34-216 [» ]
    ProteinModelPortali P23284.
    SMRi P23284. Positions 37-216.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111475. 48 interactions.
    IntActi P23284. 23 interactions.
    MINTi MINT-1142578.
    STRINGi 9606.ENSP00000300026.

    Chemistry

    BindingDBi P23284.
    ChEMBLi CHEMBL2075.
    DrugBanki DB00172. L-Proline.

    PTM databases

    PhosphoSitei P23284.

    Polymorphism databases

    DMDMi 215273869.

    2D gel databases

    OGPi P23284.
    REPRODUCTION-2DPAGE IPI00646304.
    SWISS-2DPAGE P23284.

    Proteomic databases

    MaxQBi P23284.
    PaxDbi P23284.
    PRIDEi P23284.

    Protocols and materials databases

    DNASUi 5479.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300026 ; ENSP00000300026 ; ENSG00000166794 .
    GeneIDi 5479.
    KEGGi hsa:5479.
    UCSCi uc002and.3. human.

    Organism-specific databases

    CTDi 5479.
    GeneCardsi GC15M064448.
    HGNCi HGNC:9255. PPIB.
    HPAi CAB011487.
    HPA012720.
    MIMi 123841. gene.
    259440. phenotype.
    neXtProti NX_P23284.
    Orphaneti 216804. Osteogenesis imperfecta type 2.
    216812. Osteogenesis imperfecta type 3.
    216820. Osteogenesis imperfecta type 4.
    PharmGKBi PA33580.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0652.
    HOGENOMi HOG000065981.
    HOVERGENi HBG001065.
    InParanoidi P23284.
    KOi K03768.
    OMAi PAYANED.
    OrthoDBi EOG7RFTK4.
    PhylomeDBi P23284.
    TreeFami TF354259.

    Enzyme and pathway databases

    Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.

    Miscellaneous databases

    ChiTaRSi PPIB. human.
    EvolutionaryTracei P23284.
    GeneWikii PPIB.
    GenomeRNAii 5479.
    NextBioi 21210.
    PROi P23284.
    SOURCEi Search...

    Gene expression databases

    Bgeei P23284.
    CleanExi HS_PPIB.
    Genevestigatori P23284.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel secreted cyclophilin-like protein (SCYLP)."
      Spik G., Haendler B., Delmas O., Mariller C., Chamoux M., Maes P., Tartar A., Montreuil J., Stedman K., Kocher H.P., Keller R., Hiestand P.C., Movva N.R.
      J. Biol. Chem. 266:10735-10738(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. NIEHS SNPs program
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain, Prostate and Skin.
    8. "Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence."
      Price E.R., Zydowsky L.D., Jin M., Hunter C.H., McKeon F.D., Walsh C.T.
      Proc. Natl. Acad. Sci. U.S.A. 88:1903-1907(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-216, PROTEIN SEQUENCE OF 34-48.
    9. "An endoplasmic reticulum-specific cyclophilin."
      Hasel K.W., Glass J.R., Godbout M., Sutcliffe J.G.
      Mol. Cell. Biol. 11:3484-3491(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-216.
    10. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 52-59; 64-76; 91-101; 138-150; 164-172 AND 197-207, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    11. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 72-84 AND 159-165.
    12. "S-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin."
      Arber S., Krause K.-H., Caroni P.
      J. Cell Biol. 116:113-125(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    14. Cited for: INVOLVEMENT IN OI9.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Dymeclin, the gene underlying Dyggve-Melchior-Clausen syndrome, encodes a protein integral to extracellular matrix and Golgi organization and is associated with protein secretion pathways critical in bone development."
      Denais C., Dent C.L., Southgate L., Hoyle J., Dafou D., Trembath R.C., Machado R.D.
      Hum. Mutat. 32:231-239(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DYM.
    17. "X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain."
      Mikol V., Kallen J., Walkinshaw M.D.
      Proc. Natl. Acad. Sci. U.S.A. 91:5183-5186(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 39-216.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 34-216 IN COMPLEX WITH CLGN, MUTAGENESIS OF LYS-129, INTERACTION WITH CALR; CANX AND CLGN.
    19. Cited for: VARIANT OI9 ARG-9.

    Entry informationi

    Entry nameiPPIB_HUMAN
    AccessioniPrimary (citable) accession number: P23284
    Secondary accession number(s): A8K534, Q6IBH5, Q9BVK5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 155 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    It is uncertain whether Met-1 or Met-9 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3