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Reviewed, UniProtKB/Swiss-Prot P23284 (PPIB_HUMAN)

Last modified July 7, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase B
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin B
    S-cyclophilin
      Short name=SCYLP
    CYP-S1
Gene names
Name: PPIB
Synonyms: CYPB
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Cyclosporin A (CsA) inhibits CYPB.

Subcellular location

Endoplasmic reticulum lumen. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.12 Ref.13

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase B subfamily.

Contains 1 PPIase cyclophilin-type domain.

Caution

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

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum Ref.8

Traceable author statement. Source: ProtInc

endoplasmic reticulum lumen Ref.12

Non-traceable author statement. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpeptide binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity Ref.8

Non-traceable author statement. Source: UniProtKB

unfolded protein binding Ref.8

Traceable author statement. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Ref.8
Chain34 – 216183Peptidyl-prolyl cis-trans isomerase B
PRO_0000025479

Regions

Domain47 – 204158PPIase cyclophilin-type
Motif213 – 2164Prevents secretion from ER

Amino acid modifications

Glycosylation1481N-linked (GlcNAc...) Potential

Natural variations

Natural variant601V → L: dbSNP rs11558595.
VAR_047711

Experimental info

Sequence conflict51S → R in AAA52150. Ref.8
Sequence conflict2161E → D in CAG33110. Ref.3

Secondary structure

................................ 216
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23284-1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 2D0410A07AA9E420

FASTA21623,743
        10         20         30         40         50         60 
MLRLSERNMK VLLAAALIAG SVFFLLLPGP SAADEKKKGP KVTVKVYFDL RIGDEDVGRV 

        70         80         90        100        110        120 
IFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF MIQGGDFTRG DGTGGKSIYG 

       130        140        150        160        170        180 
ERFPDENFKL KHYGPGWVSM ANAGKDTNGS QFFITTVKTA WLDGKHVVFG KVLEGMEVVR 

       190        200        210 
KVESTKTDSR DKPLKDVIIA DCGKIEVEKP FAIAKE 

« Hide

References

« Hide 'large scale' references
[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: 2040592] [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. expand/collapse author list , 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: 14702039] [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. expand/collapse author list , 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: 16572171] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: 15489334] [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: 2000394] [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: 1710767] [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, 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: 1286667] [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: 1530944] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]"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: 8197205] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 39-216.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

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.
IPIIPI00646304.
PIRCSHUB. A39118.
RefSeqNP_000933.1.
UniGeneHs.434937

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CYNX-ray1.85A39-216[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP23284. 11 interactions.

PTM databases

PhosphoSiteP23284.

2-D gel databases

SWISS-2DPAGEP23284.
Aarhus/Ghent-2DPAGE117. NEPHGE.
OGPP23284.
REPRODUCTION-2DPAGEIPI00646304.

Proteomic databases

PRIDEP23284.

Genome annotation databases

EnsemblENSG00000166794. Homo sapiens. [Contig view]
GeneID5479.
KEGGhsa:5479.
UCSCuc002and.1. human.

Organism-specific databases

GeneCardsGC15M062235.
H-InvDBHIX0012337.
HGNCHGNC:9255. PPIB.
HPAHPA012720.
MIM123841. gene.
PharmGKBPA33580.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP23284.
OMAP23284. GPSTADE.

Enzyme and pathway databases

BRENDA5.2.1.8. 247.
Pathway_Interaction_DBsyndecan_1_pathway. Syndecan-1-mediated signaling events.

Gene expression databases

BgeeP23284.
CleanExHS_PPIB.
GermOnlineENSG00000166794. Homo sapiens.

Family and domain databases

InterProIPR002130. PPIase_cyclophilin.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00172. L-Proline.
NextBio21210.
SOURCESearch...

Entry information

Entry namePPIB_HUMAN
AccessionPrimary (citable) accession number: P23284
Secondary accession number(s): A8K534, Q6IBH5, Q9BVK5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 25, 2008
Last modified: July 7, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents