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Protein

Peptidyl-prolyl cis-trans isomerase FKBP11

Gene

Fkbp11

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins during protein synthesis.

Catalytic activityi

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

GO - Molecular functioni

  1. FK506 binding Source: GO_Central
  2. peptidyl-prolyl cis-trans isomerase activity Source: GO_Central

GO - Biological processi

  1. chaperone-mediated protein folding Source: GO_Central
  2. protein peptidyl-prolyl isomerization Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP11 (EC:5.2.1.8)
Short name:
PPIase FKBP11
Alternative name(s):
19 kDa FK506-binding protein
Short name:
19 kDa FKBP
Short name:
FKBP-19
FK506-binding protein 11
Short name:
FKBP-11
Rotamase
Gene namesi
Name:Fkbp11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1913370. Fkbp11.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei156 – 17621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: GO_Central
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 201174Peptidyl-prolyl cis-trans isomerase FKBP11PRO_0000025520Add
BLAST

Proteomic databases

MaxQBiQ9D1M7.
PaxDbiQ9D1M7.
PRIDEiQ9D1M7.

PTM databases

PhosphoSiteiQ9D1M7.

Expressioni

Gene expression databases

BgeeiQ9D1M7.
CleanExiMM_FKBP11.
GenevestigatoriQ9D1M7.

Interactioni

Subunit structurei

Interacts with IFITM5.1 Publication

Structurei

3D structure databases

SMRiQ9D1M7. Positions 38-145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 14488PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the FKBP-type PPIase family.Curated
Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0545.
GeneTreeiENSGT00530000062784.
HOGENOMiHOG000154887.
HOVERGENiHBG051623.
InParanoidiQ9D1M7.
KOiK09576.
OMAiMCRAEAG.
OrthoDBiEOG7V1FTB.
PhylomeDBiQ9D1M7.
TreeFamiTF105296.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D1M7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLSPLLLPL QLLLLLLFSG AVCRAEAGPE TESPVRTLQV ETLVQPPESC
60 70 80 90 100
TESAAIGDTL HIHYTGSLVD GRIIDTSLTR DPLVIELGQK QVIPGLEQSL
110 120 130 140 150
LDMCVGEKRR AVIPSHLAYG KRGYPPSIPA DAVVQYDVEL IALIRANYWQ
160 170 180 190 200
KLLKSILPLV GIAMVPALLG LIGYHLYRKA SRPKVSKKKL KEEKRNKSKK

K
Length:201
Mass (Da):22,137
Last modified:June 1, 2001 - v1
Checksum:i94D955C57264BD82
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531S → F in BAB31559 (PubMed:16141072).Curated
Sequence conflicti198 – 1981S → R in BAB31559 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003331 mRNA. Translation: BAB22719.1.
AK019132 mRNA. Translation: BAB31559.1.
BC037596 mRNA. Translation: AAH37596.1.
CCDSiCCDS27803.1.
RefSeqiNP_077131.2. NM_024169.3.
UniGeneiMm.30729.

Genome annotation databases

EnsembliENSMUST00000003445; ENSMUSP00000003445; ENSMUSG00000003355.
GeneIDi66120.
KEGGimmu:66120.
UCSCiuc007xnm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003331 mRNA. Translation: BAB22719.1.
AK019132 mRNA. Translation: BAB31559.1.
BC037596 mRNA. Translation: AAH37596.1.
CCDSiCCDS27803.1.
RefSeqiNP_077131.2. NM_024169.3.
UniGeneiMm.30729.

3D structure databases

SMRiQ9D1M7. Positions 38-145.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9D1M7.

Proteomic databases

MaxQBiQ9D1M7.
PaxDbiQ9D1M7.
PRIDEiQ9D1M7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003445; ENSMUSP00000003445; ENSMUSG00000003355.
GeneIDi66120.
KEGGimmu:66120.
UCSCiuc007xnm.1. mouse.

Organism-specific databases

CTDi51303.
MGIiMGI:1913370. Fkbp11.

Phylogenomic databases

eggNOGiCOG0545.
GeneTreeiENSGT00530000062784.
HOGENOMiHOG000154887.
HOVERGENiHBG051623.
InParanoidiQ9D1M7.
KOiK09576.
OMAiMCRAEAG.
OrthoDBiEOG7V1FTB.
PhylomeDBiQ9D1M7.
TreeFamiTF105296.

Miscellaneous databases

NextBioi320690.
PROiQ9D1M7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1M7.
CleanExiMM_FKBP11.
GenevestigatoriQ9D1M7.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. "Characterization of the osteoblast-specific transmembrane protein IFITM5 and analysis of IFITM5-deficient mice."
    Hanagata N., Li X., Morita H., Takemura T., Li J., Minowa T.
    J. Bone Miner. Metab. 29:279-290(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IFITM5.

Entry informationi

Entry nameiFKB11_MOUSE
AccessioniPrimary (citable) accession number: Q9D1M7
Secondary accession number(s): Q9CRE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.