TopFIND 4.0

P24368: Peptidyl-prolyl cis-trans isomerase B

General Information

Protein names
- Peptidyl-prolyl cis-trans isomerase B
- PPIase B
- 5.2.1.8 {ECO:0000250|UniProtKB:P23284}
- CYP-S1
- Cyclophilin B
- Rotamase B
- S-cyclophilin
- SCYLP

Gene names Ppib
Organism Rattus norvegicus
Protease Family
Protease ID
Chromosome location
UniProt ID P24368

1

N-termini

1

C-termini

0

Cleavages

0

Substrates

Sequence

        10         20         30         40         50         60 
MLRLSERNMK VLFAAALIVG SVVFLLLPGP SVANDKKKGP KVTVKVYFDF QIGDEPVGRV 
        70         80         90        100        110        120 
TFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF MIQGGDFTRG DGTGGKSIYG 
       130        140        150        160        170        180 
ERFPDENFKL KHYGPGWVSM ANAGKDTNGS QFFITTVKTS WLDGKHVVFG KVLEGMDVVR 
       190        200        210    
KVENTKTDSR DKPLKDVIIV DCGKIEVEKP FAIAKE

Isoforms



Sequence View



Filter Information:


(REFRESH)

Directness:


Physiological Relevance:


Evidence Codes:


Methodology:


Perturbation of System:


Biological System:


Protease Assignment Confidence:


Evidence Names:


Database:


Lab:



Protein Neighborhood

Domains & Features

1 N-termini - 1 C-termini - 0 Cleavages - 0 Substrates

N-termini

    Name Sequence Position Modification Evidence type Method Source (database) Source (Lab) Evidence name Publications (PMID)
    P24368-34-unknown NDKKKG... 34 inferred from electronic annotation electronic annotation UniProtKB inferred from uniprot

C-termini

    Name Sequence Position Evidence type Method Source (database) Source (Lab) Evidence name Publications (PMIDs)
    ...AIAKE 216 inferred from electronic annotation electronic annotation UniProtKB inferred from uniprot

Cleavages

    Protease Position Sequence Evidence type Method Source (database) Source (Lab) Evidence name Publications (PMIDs)

Substrates

    Substrate Position Sequence Evidence type Method Source (database) Source (Lab) Evidence name Publications (PMIDs)