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Q9Z247 (FKBP9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP9

Short name=PPIase FKBP9
EC=5.2.1.8
Alternative name(s):
63 kDa FK506-binding protein
Short name=63 kDa FKBP
Short name=FKBP-63
FK506-binding protein 9
Short name=FKBP-9
FKBP65RS
Rotamase
Gene names
Name:Fkbp9
Synonyms:Fkbp60, Fkbp63
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins during protein synthesis.

Catalytic activity

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

Enzyme regulation

Inhibited by FK506. Ref.1

Subcellular location

Endoplasmic reticulum lumen Ref.1.

Tissue specificity

Predominantly expressed in heart, skeletal muscle, lung, liver and kidney. Lower levels found in brain, spleen and testis. Ref.1 Ref.2

Developmental stage

Expressed in all developmental stages. Ref.1

Post-translational modification

Phosphorylated.

Sequence similarities

Contains 2 EF-hand domains.

Contains 4 PPIase FKBP-type domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 570546Peptidyl-prolyl cis-trans isomerase FKBP9
PRO_0000025516

Regions

Domain54 – 14289PPIase FKBP-type 1
Domain166 – 25489PPIase FKBP-type 2
Domain278 – 36588PPIase FKBP-type 3
Domain389 – 47789PPIase FKBP-type 4
Domain488 – 52336EF-hand 1
Domain533 – 56836EF-hand 2
Calcium binding501 – 512121 Potential
Calcium binding546 – 557122 Potential
Motif567 – 5704Prevents secretion from ER Potential

Amino acid modifications

Glycosylation1741N-linked (GlcNAc...) Ref.5
Glycosylation2861N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation3971N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict401Q → R in AAH26133. Ref.3
Sequence conflict1491H → Q in AAH26133. Ref.3
Sequence conflict234 – 2363DGK → NGE in AAF79215. Ref.2
Sequence conflict3211G → S in BAB25071. Ref.4
Sequence conflict3511G → A in AAF79215. Ref.2
Sequence conflict3531A → T in BAB25071. Ref.4
Sequence conflict3611V → F in AAF79215. Ref.2
Sequence conflict3641F → V in AAF79215. Ref.2
Sequence conflict3781K → N in AAF79215. Ref.2
Sequence conflict3861S → I in AAF79215. Ref.2
Sequence conflict4751E → D in AAF79215. Ref.2
Sequence conflict5481N → S in AAH43129. Ref.3
Sequence conflict5501D → N in AAF79215. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Z247 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: DFE8B8F2F6A0F1DA

FASTA57062,995
        10         20         30         40         50         60 
MALGARGWRR RSLLLLLLWV TGQAAPVLGL AVSSELQIQQ SFVPDECPRT VHSGDFVRYH 

        70         80         90        100        110        120 
YVGTFLDGQK FDSSYDRDST FNVFVGKGQL IAGMDQALVG MCVNERRLVT IPPNLAYGSE 

       130        140        150        160        170        180 
GVSGVIPPNS VLHFDVLLVD IWNSEDQVHI QTYFKPPSCP RTIQVSDFVR YHYNGTFLDG 

       190        200        210        220        230        240 
TLFDSSHNRM KTYDTYVGIG WLIPGMDKGL LGMCVGEKRI ITVPPFLAYG EEGDGKDIPG 

       250        260        270        280        290        300 
QASLVFDVAL LDLHNPKDTI SIENKVVPEN CERRSQSGDF LRYHYNGTLL DGTLFDSSYS 

       310        320        330        340        350        360 
RNHTFDTYIG QGYVIPGMDE GLLGVCIGER RRIVVPPHLG YGEKGRGSIP GSAVLVFDIH 

       370        380        390        400        410        420 
VIDFHNPSDS ISITSHYKPP DCSVLSKKGD YLKYHYNASL LDGTLLDSTW NLGKTYNIVL 

       430        440        450        460        470        480 
GSGQVVLGMD MGLREMCVGE KRTVIIPPHL GYGEAGVDGE VPGSAVLVFD IELLELVSGL 

       490        500        510        520        530        540 
PEGYMFIWNG EVSPNLFEEI DRDGNGEVLL EEFSEYIHAQ VATGKGKLAP GFNAEMIVKN 

       550        560        570 
MFTNQDRNGD GKVTAEEFKL KDQEAKHDEL 

« Hide

References

« Hide 'large scale' references
[1]"Biochemical analysis of mouse FKBP60, a novel member of the FKBP family."
Shadidy M., Caubit X., Olsen R., Seternes O.M., Moens U., Krauss S.
Biochim. Biophys. Acta 1446:295-307(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, CALCIUM-BINDING.
[2]"Identification and genetic mapping of the mouse Fkbp9 gene encoding a new member of FK506-binding protein family."
Jo D., Lyu M.S., Cho E.-G., Park D., Kozak C.A., Kim M.G.
Mol. Cells 12:272-275(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Thymus.
[3]"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/6 and Czech II.
Tissue: Fetal brain and Mammary tumor.
[4]"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. expand/collapse author list , 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] OF 155-570.
Strain: C57BL/6J.
Tissue: Pancreas.
[5]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF090334 mRNA. Translation: AAC72964.1.
AF279263 mRNA. Translation: AAF79215.1.
BC026133 mRNA. Translation: AAH26133.1.
BC043129 mRNA. Translation: AAH43129.1.
AK007499 mRNA. Translation: BAB25071.1.
RefSeqNP_036186.2. NM_012056.2.
UniGeneMm.20943.

3D structure databases

ProteinModelPortalQ9Z247.
SMRQ9Z247. Positions 50-477, 495-559.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205110. 1 interaction.
IntActQ9Z247. 3 interactions.
MINTMINT-4095122.
STRING10090.ENSMUSP00000031795.

Proteomic databases

PaxDbQ9Z247.
PRIDEQ9Z247.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031795; ENSMUSP00000031795; ENSMUSG00000029781.
GeneID27055.
KEGGmmu:27055.
UCSCuc009cbp.2. mouse.

Organism-specific databases

CTD11328.
MGIMGI:1350921. Fkbp9.

Phylogenomic databases

eggNOGCOG0545.
GeneTreeENSGT00530000062784.
HOGENOMHOG000230960.
HOVERGENHBG051620.
InParanoidQ9Z247.
KOK09575.
OMAEMIVKNM.
OrthoDBEOG7T1R9S.
PhylomeDBQ9Z247.
TreeFamTF105296.

Enzyme and pathway databases

ReactomeREACT_93132. Metabolism of proteins.

Gene expression databases

BgeeQ9Z247.
CleanExMM_FKBP9.
GenevestigatorQ9Z247.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 4 hits.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS00014. ER_TARGET. 1 hit.
PS50059. FKBP_PPIASE. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFKBP9. mouse.
NextBio304999.
PROQ9Z247.
SOURCESearch...

Entry information

Entry nameFKBP9_MOUSE
AccessionPrimary (citable) accession number: Q9Z247
Secondary accession number(s): Q80ZZ6 expand/collapse secondary AC list , Q8R386, Q9CVM0, Q9JHX5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot