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Q9D1M7

- FKB11_MOUSE

UniProt

Q9D1M7 - FKB11_MOUSE

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Protein

Peptidyl-prolyl cis-trans isomerase FKBP11

Gene

Fkbp11

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript 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: RefGenome
  2. peptidyl-prolyl cis-trans isomerase activity Source: RefGenome

GO - Biological processi

  1. chaperone-mediated protein folding Source: RefGenome
  2. protein peptidyl-prolyl isomerization Source: RefGenome
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: Chromosome 15

Organism-specific databases

MGIiMGI:1913370. Fkbp11.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: RefGenome
  2. integral component of membrane Source: UniProtKB-KW
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.

Structurei

3D structure databases

ProteinModelPortaliQ9D1M7.
SMRiQ9D1M7. Positions 57-145.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

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

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.
OMAiSRPKVSK.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK003331 mRNA. Translation: BAB22719.1 .
AK019132 mRNA. Translation: BAB31559.1 .
BC037596 mRNA. Translation: AAH37596.1 .
CCDSi CCDS27803.1.
RefSeqi NP_077131.2. NM_024169.3.
UniGenei Mm.30729.

3D structure databases

ProteinModelPortali Q9D1M7.
SMRi Q9D1M7. Positions 57-145.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9D1M7.

Proteomic databases

MaxQBi Q9D1M7.
PaxDbi Q9D1M7.
PRIDEi Q9D1M7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000003445 ; ENSMUSP00000003445 ; ENSMUSG00000003355 .
GeneIDi 66120.
KEGGi mmu:66120.
UCSCi uc007xnm.1. mouse.

Organism-specific databases

CTDi 51303.
MGIi MGI:1913370. Fkbp11.

Phylogenomic databases

eggNOGi COG0545.
GeneTreei ENSGT00530000062784.
HOGENOMi HOG000154887.
HOVERGENi HBG051623.
InParanoidi Q9D1M7.
KOi K09576.
OMAi SRPKVSK.
OrthoDBi EOG7V1FTB.
PhylomeDBi Q9D1M7.
TreeFami TF105296.

Miscellaneous databases

NextBioi 320690.
PROi Q9D1M7.
SOURCEi Search...

Gene expression databases

Bgeei Q9D1M7.
CleanExi MM_FKBP11.
Genevestigatori Q9D1M7.

Family and domain databases

InterProi IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view ]
PANTHERi PTHR10516. PTHR10516. 1 hit.
Pfami PF00254. FKBP_C. 1 hit.
[Graphical view ]
PROSITEi PS50059. FKBP_PPIASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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: October 1, 2014
This is version 95 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