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P23284

- PPIB_HUMAN

UniProt

P23284 - PPIB_HUMAN

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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

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 complex binding Source: UniProt
  5. 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
Complete GO annotation...

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: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. macromolecular complex Source: UniProt
  6. membrane Source: UniProtKB
  7. nucleus Source: UniProt
Complete GO annotation...

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.
ExpressionAtlasiP23284. baseline and differential.
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.
GeneTreeiENSGT00760000119072.
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

        10         20         30         40         50
MLRLSERNMK VLLAAALIAG SVFFLLLPGP SAADEKKKGP KVTVKVYFDL
60 70 80 90 100
RIGDEDVGRV IFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF
110 120 130 140 150
MIQGGDFTRG DGTGGKSIYG ERFPDENFKL KHYGPGWVSM ANAGKDTNGS
160 170 180 190 200
QFFITTVKTA WLDGKHVVFG KVLEGMEVVR KVESTKTDSR DKPLKDVIIA
210
DCGKIEVEKP FAIAKE
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.
GeneTreei ENSGT00760000119072.
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.
ExpressionAtlasi P23284. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 156 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