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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 number Q9BVK5
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on November 1, 1991 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 89)
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], AND PROTEIN SEQUENCE OF 26-40.
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).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Rieder M.J., Rajkumar N., Downing T.K., Olson A.N., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-208.
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).
[6]
PROTEIN SEQUENCE OF 64-76 AND 151-157.
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).
[7]
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).
[8]
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).
[9]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-208.
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
M60857; AAA52150.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63573; AAA36601.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY962310; AAX44050.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001125; AAH01125.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008848; AAH08848.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020800; AAH20800.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032138; AAH32138.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60457; AAA35733.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39118; CSHUB.
RefSeq NP_000933.1; -.
UniGene Hs.434937
3D structure databases
PDB
1CYN; X-ray; 1.85 A; A=31-208.[ExPASy / RCSB / EBI]
PDBsum 1CYN; -.
ModBase P23284.
Protein-protein interaction databases
IntAct P23284; -.
PTM databases
PhosphoSite P23284; -.
Polymorphism databases
NIEHS-SNPs PPIB.
2D gel databases
SWISS-2DPAGE P23284; -.
Aarhus/Ghent-2DPAGE 117; NEPHGE.
OGP P23284; -.
REPRODUCTION-2DPAGE IPI00646304; -.
Organism-specific databases
H-InvDB HIX0012337; -.
HGNC HGNC:9255; PPIB.
GenAtlas PPIB.
HPA CAB011487; -.
HPA012720; -.
MIM 123841; gene. [NCBI / EBI]
PharmGKB PA33580; -.
GeneCards P23284.
Gene expression databases
CleanEx HS_PPIB; -.
GermOnline ENSG00000166794; Homo sapiens.
Ontologies
GO
GO:0005788; Cellular component: endoplasmic reticulum lumen (non-traceable author statement from UniProtKB).
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).
QuickGo view.
Family and domain databases
InterPro IPR002130; PPIase_cyclophilin.
Graphical view of domain structure.
Gene3D G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
PANTHER PTHR11071; 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).
BLOCKS P23284.
Genome annotation databases
Ensembl ENSG00000166794; Homo sapiens. [Contig view]
GeneID 5479; -.
KEGG hsa:5479; -.
Phylogenomic databases
HOVERGEN P23284; -.
Other
DrugBank DB00172; L-Proline.
LinkHub P23284; -.
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; Isomerase; Rotamase; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    25  25      
CHAIN   26   208  183     Peptidyl-prolyl cis-trans isomerase B. PRO_0000025479
DOMAIN   39   196  158     PPIase cyclophilin-type. 
MOTIF   205   208  4     Prevents secretion from ER. 
STRAND   33    44  12      
STRAND   47    56  10      
TURN   58    60  3      
HELIX   62    73  12      
TURN   74    76  3      
STRAND   84    89  6      
TURN   90    92  3      
STRAND   93    96  4      
TURN   99   101  3      
STRAND   102   105  4      
STRAND   129   132  4      
STRAND   144   149  6      
HELIX   152   154  3      
TURN   155   157  3      
STRAND   160   166  7      
HELIX   168   175  8      
STRAND   185   187  3      
STRAND   189   204  16      
Sequence information
Length: 208 AA [This is the length of the unprocessed precursor] Molecular weight: 22742 Da [This is the MW of the unprocessed precursor] CRC64: A814481B7EBD4579 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKVLLAAALI AGSVFFLLLP GPSAADEKKK GPKVTVKVYF DLRIGDEDVG RVIFGLFGKT 

        70         80         90        100        110        120 
VPKTVDNFVA LATGEKGFGY KNSKFHRVIK DFMIQGGDFT RGDGTGGKSI YGERFPDENF 

       130        140        150        160        170        180 
KLKHYGPGWV SMANAGKDTN GSQFFITTVK TAWLDGKHVV FGKVLEGMEV VRKVESTKTD 

       190        200 
SRDKPLKDVI IADCGKIEVE KPFAIAKE 

P23284 in FASTA format

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