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UniProtKB/Swiss-Prot entry P23284


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PPIB_HUMAN
Primary accession number P23284
Secondary accession numbers A8K534 Q6IBH5 Q9BVK5
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on November 25, 2008 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 99)
Name and origin of the protein
Protein name Peptidyl-prolyl cis-trans isomerase B [Precursor]
Synonyms PPIase
Rotamase
EC 5.2.1.8
Cyclophilin B
S-cyclophilin
SCYLP
CYP-S1
Gene name
Name: PPIB
Synonyms: CYPB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2040592 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A novel secreted cyclophilin-like protein (SCYLP).";
J. Biol. Chem. 266:10735-10738(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04601; PubMed=16572171 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Analysis of the DNA sequence and duplication history of human chromosome 15.";
Nature 440:671-675(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Prostate, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-216, AND PROTEIN SEQUENCE OF 34-48.
DOI=10.1073/pnas.88.5.1903; PubMed=2000394 [NCBI, ExPASy, EBI, Israel, Japan]
Price E.R., Zydowsky L.D., Jin M., Hunter C.H., McKeon F.D., Walsh C.T.;
"Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence.";
Proc. Natl. Acad. Sci. U.S.A. 88:1903-1907(1991).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-216.
PubMed=1710767 [NCBI, ExPASy, EBI, Israel, Japan]
Hasel K.W., Glass J.R., Godbout M., Sutcliffe J.G.;
"An endoplasmic reticulum-specific cyclophilin.";
Mol. Cell. Biol. 11:3484-3491(1991).
[10]
PROTEIN SEQUENCE OF 52-59; 64-76; 91-101; 138-150; 164-172 AND 197-207, AND MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[11]
PROTEIN SEQUENCE OF 72-84 AND 159-165.
DOI=10.1002/elps.11501301199; PubMed=1286667 [NCBI, ExPASy, EBI, Israel, Japan]
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[12]
SUBCELLULAR LOCATION.
DOI=10.1083/jcb.116.1.113; PubMed=1530944 [NCBI, ExPASy, EBI, Israel, Japan]
Arber S., Krause K.-H., Caroni P.;
"S-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin.";
J. Cell Biol. 116:113-125(1992).
[13]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[14]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[15]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 39-216.
DOI=10.1073/pnas.91.11.5183; PubMed=8197205 [NCBI, ExPASy, EBI, Israel, Japan]
Mikol V., Kallen J., Walkinshaw M.D.;
"X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain.";
Proc. Natl. Acad. Sci. U.S.A. 91:5183-5186(1994).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M63573; AAA36601.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291149; BAF83838.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456829; CAG33110.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY962310; AAX44050.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC100840; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
CH471082; EAW77669.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001125; AAH01125.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008848; AAH08848.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020800; AAH20800.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032138; AAH32138.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60857; AAA52150.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60457; AAA35733.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00646304; -.
PIR A39118; CSHUB.
RefSeq NP_000933.1; -.
UniGene Hs.434937
3D structure databases
PDB
1CYN; X-ray; 1.85 A; A=39-216.[ExPASy / RCSB / EBI]
PDBsum 1CYN; -.
ModBase P23284.
Protein-protein interaction databases
IntAct P23284; 11.
PTM databases
PhosphoSite P23284; -.
Enzyme and pathway databases
BRENDA 5.2.1.8; 247.
Pathway_Interaction_DB syndecan_1_pathway; Syndecan-1-mediated signaling events.
2D gel databases
SWISS-2DPAGE P23284; -.
Aarhus/Ghent-2DPAGE 117; NEPHGE.
OGP P23284; -.
REPRODUCTION-2DPAGE IPI00646304; -.
Organism-specific databases
GeneCards GC15M062235; -.
H-InvDB HIX0012337; -.
HGNC HGNC:9255; PPIB.
GenAtlas PPIB.
HPA HPA012720; -.
MIM 123841; gene. [NCBI / EBI]
PharmGKB PA33580; -.
Gene expression databases
Bgee P23284; -.
CleanEx HS_PPIB; -.
GermOnline ENSG00000166794; Homo sapiens.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (traceable author statement from ProtInc).
GO:0005788; Cellular component: endoplasmic reticulum lumen (non-traceable author statement from UniProtKB).
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0042277; Molecular function: peptide binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003755; Molecular function: peptidyl-prolyl cis-trans isomerase activity (non-traceable author statement from UniProtKB).
GO:0051082; Molecular function: unfolded protein binding (traceable author statement from ProtInc).
GO:0006457; Biological process: protein folding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002130; PPIase_cyclophilin.
Graphical view of domain structure.
Gene3D G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
Pfam PF00160; Pro_isomerase; 1.
Pfam graphical view of domain structure.
PRINTS PR00153; CSAPPISMRASE.
PROSITE PS00170; CSA_PPIASE_1; 1.
PS50072; CSA_PPIASE_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P23284; -.
Genome annotation databases
Ensembl ENSG00000166794; Homo sapiens. [Contig view]
GeneID 5479; -.
KEGG hsa:5479; -.
Phylogenomic databases
HOVERGEN P23284; -.
OMA P23284; GPSTADE.
Other
DrugBank DB00172; L-Proline.
NextBio 21210; -.
SOURCE PPIB; Homo sapiens.
ProtoNet P23284.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cyclosporin; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Isomerase; Polymorphism; Rotamase; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    33  33      
CHAIN   34   216  183     Peptidyl-prolyl cis-trans isomerase B. PRO_0000025479
DOMAIN   47   204  158     PPIase cyclophilin-type. 
MOTIF   213   216  4     Prevents secretion from ER. 
CARBOHYD   148   148        N-linked (GlcNAc...) (Potential). 
VARIANT   60    60  1     V -> L (in dbSNP:rs11558595 [NCBI]). VAR_047711 [3D]
CONFLICT   5     5        S -> R (in Ref. 8; AAA52150). 
CONFLICT   216   216        E -> D (in Ref. 3; CAG33110). 
STRAND   41    52  12      
STRAND   55    64  10      
TURN   66    68  3      
HELIX   70    81  12      
TURN   82    84  3      
STRAND   92    97  6      
TURN   98   100  3      
STRAND   101   104  4      
TURN   107   109  3      
STRAND   110   113  4      
STRAND   137   140  4      
STRAND   152   157  6      
HELIX   160   162  3      
TURN   163   165  3      
STRAND   168   174  7      
HELIX   176   183  8      
STRAND   193   195  3      
STRAND   197   212  16      
Sequence information
Length: 216 AA [This is the length of the unprocessed precursor] Molecular weight: 23743 Da [This is the MW of the unprocessed precursor] CRC64: 2D0410A07AA9E420 [This is a checksum on the sequence]
        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 

P23284 in FASTA format

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