SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9NWM8

- FKB14_HUMAN

UniProt

Q9NWM8 - FKB14_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Peptidyl-prolyl cis-trans isomerase FKBP14
Gene
FKBP14, FKBP22, UNQ322/PRO381
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi148 – 159121 Reviewed prediction
Add
BLAST
Calcium bindingi192 – 203122 Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. FK506 binding Source: RefGenome
  2. calcium ion binding Source: InterPro
  3. peptidyl-prolyl cis-trans isomerase activity Source: RefGenome

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. chaperone-mediated protein folding Source: RefGenome
  4. endoplasmic reticulum unfolded protein response Source: Reactome
  5. protein peptidyl-prolyl isomerization Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_18273. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP14 (EC:5.2.1.8)
Short name:
PPIase FKBP14
Alternative name(s):
22 kDa FK506-binding protein
Short name:
22 kDa FKBP
Short name:
FKBP-22
FK506-binding protein 14
Short name:
FKBP-14
Rotamase
Gene namesi
Name:FKBP14
Synonyms:FKBP22
ORF Names:UNQ322/PRO381
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:18625. FKBP14.

Subcellular locationi

Endoplasmic reticulum lumen 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
  2. endoplasmic reticulum membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Ehlers-Danlos syndrome, with progressive kyphoscoliosis, myopathy, and hearing loss (EDSKMH) [MIM:614557]: A syndrome with features of Ehlers-Danlos syndrome types VIA and VIB on the one hand, and the collagen VI-related congenital myopathies Ullrich congenital muscular dystrophy and Bethlem myopathy on the other hand. Clinically, this disorder is characterized by the following features: severe generalized hypotonia at birth with marked muscle weakness that improve in infancy; early-onset progressive kyphoscoliosis; joint hypermobility without contractures; hyperelastic skin with follicular hyperkeratosis, easy bruising, and occasional abnormal scarring; myopathy; hearing impairment, which is predominantly sensorineural; normal ratio of lysyl pyridinoline to hydroxylysyl pyridinoline (LP/HP) in urine.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Keywords - Diseasei

Deafness, Ehlers-Danlos syndrome

Organism-specific databases

MIMi614557. phenotype.
Orphaneti300179. Ehlers-Danlos syndrome, kyphoscoliotic and deafness type.
PharmGKBiPA38608.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 Publication
Add
BLAST
Chaini20 – 211192Peptidyl-prolyl cis-trans isomerase FKBP14
PRO_0000025521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi176 – 1761N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9NWM8.
PaxDbiQ9NWM8.
PRIDEiQ9NWM8.

PTM databases

PhosphoSiteiQ9NWM8.

Expressioni

Gene expression databases

ArrayExpressiQ9NWM8.
BgeeiQ9NWM8.
CleanExiHS_FKBP14.
GenevestigatoriQ9NWM8.

Organism-specific databases

HPAiHPA013329.
HPA026829.

Interactioni

Protein-protein interaction databases

BioGridi120362. 5 interactions.
IntActiQ9NWM8. 3 interactions.
MINTiMINT-8247492.
STRINGi9606.ENSP00000222803.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 213
Beta strandi28 – 336
Beta strandi47 – 5610
Turni57 – 593
Beta strandi62 – 654
Helixi66 – 694
Turni70 – 723
Beta strandi75 – 784
Turni79 – 824
Helixi86 – 916
Beta strandi100 – 1056
Helixi107 – 1093
Turni110 – 1145
Beta strandi125 – 13511
Helixi141 – 1477
Beta strandi152 – 1565
Helixi157 – 17014
Helixi177 – 19115
Beta strandi196 – 2005
Helixi201 – 2055

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DIPX-ray1.82A/B/C/D/E/F/G/H/I/J19-138[»]
4MSPX-ray1.90A/B21-211[»]
ProteinModelPortaliQ9NWM8.
SMRiQ9NWM8. Positions 21-209.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 13591PPIase FKBP-type
Add
BLAST
Domaini135 – 17036EF-hand 1
Add
BLAST
Domaini179 – 21133EF-hand 2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi208 – 2114Prevents secretion from ER Reviewed prediction

Sequence similaritiesi

Contains 2 EF-hand domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG0545.
HOGENOMiHOG000154887.
HOVERGENiHBG051623.
InParanoidiQ9NWM8.
KOiK09577.
OMAiMMLVHYE.
OrthoDBiEOG7T1R9S.
PhylomeDBiQ9NWM8.
TreeFamiTF105296.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF13499. EF-hand_7. 1 hit.
PF00254. FKBP_C. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS00014. ER_TARGET. 1 hit.
PS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9NWM8-1 [UniParc]FASTAAdd to Basket

« Hide

MRLFLWNAVL TLFVTSLIGA LIPEPEVKIE VLQKPFICHR KTKGGDLMLV    50
HYEGYLEKDG SLFHSTHKHN NGQPIWFTLG ILEALKGWDQ GLKGMCVGEK 100
RKLIIPPALG YGKEGKGKIP PESTLIFNID LLEIRNGPRS HESFQEMDLN 150
DDWKLSKDEV KAYLKKEFEK HGAVVNESHH DALVEDIFDK EDEDKDGFIS 200
AREFTYKHDE L 211
Length:211
Mass (Da):24,172
Last modified:October 1, 2000 - v1
Checksum:i858184954FE10029
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY358643 mRNA. Translation: AAQ89006.1.
AK000738 mRNA. Translation: BAA91351.1.
BC005206 mRNA. Translation: AAH05206.1.
CCDSiCCDS5423.1.
RefSeqiNP_060416.1. NM_017946.3.
UniGeneiHs.390838.

Genome annotation databases

EnsembliENST00000222803; ENSP00000222803; ENSG00000106080.
GeneIDi55033.
KEGGihsa:55033.
UCSCiuc003tal.2. human.

Polymorphism databases

DMDMi23821568.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY358643 mRNA. Translation: AAQ89006.1 .
AK000738 mRNA. Translation: BAA91351.1 .
BC005206 mRNA. Translation: AAH05206.1 .
CCDSi CCDS5423.1.
RefSeqi NP_060416.1. NM_017946.3.
UniGenei Hs.390838.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4DIP X-ray 1.82 A/B/C/D/E/F/G/H/I/J 19-138 [» ]
4MSP X-ray 1.90 A/B 21-211 [» ]
ProteinModelPortali Q9NWM8.
SMRi Q9NWM8. Positions 21-209.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120362. 5 interactions.
IntActi Q9NWM8. 3 interactions.
MINTi MINT-8247492.
STRINGi 9606.ENSP00000222803.

Chemistry

BindingDBi Q9NWM8.
ChEMBLi CHEMBL2342.

PTM databases

PhosphoSitei Q9NWM8.

Polymorphism databases

DMDMi 23821568.

Proteomic databases

MaxQBi Q9NWM8.
PaxDbi Q9NWM8.
PRIDEi Q9NWM8.

Protocols and materials databases

DNASUi 55033.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222803 ; ENSP00000222803 ; ENSG00000106080 .
GeneIDi 55033.
KEGGi hsa:55033.
UCSCi uc003tal.2. human.

Organism-specific databases

CTDi 55033.
GeneCardsi GC07M030050.
HGNCi HGNC:18625. FKBP14.
HPAi HPA013329.
HPA026829.
MIMi 614505. gene.
614557. phenotype.
neXtProti NX_Q9NWM8.
Orphaneti 300179. Ehlers-Danlos syndrome, kyphoscoliotic and deafness type.
PharmGKBi PA38608.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0545.
HOGENOMi HOG000154887.
HOVERGENi HBG051623.
InParanoidi Q9NWM8.
KOi K09577.
OMAi MMLVHYE.
OrthoDBi EOG7T1R9S.
PhylomeDBi Q9NWM8.
TreeFami TF105296.

Enzyme and pathway databases

Reactomei REACT_18273. XBP1(S) activates chaperone genes.

Miscellaneous databases

GenomeRNAii 55033.
NextBioi 58455.
PROi Q9NWM8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NWM8.
Bgeei Q9NWM8.
CleanExi HS_FKBP14.
Genevestigatori Q9NWM8.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view ]
PANTHERi PTHR10516. PTHR10516. 1 hit.
Pfami PF13499. EF-hand_7. 1 hit.
PF00254. FKBP_C. 1 hit.
[Graphical view ]
SMARTi SM00054. EFh. 2 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS00014. ER_TARGET. 1 hit.
PS50059. FKBP_PPIASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
    Tissue: Kidney.
  4. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-34.
  5. Cited for: INVOLVEMENT IN EDSKMH, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiFKB14_HUMAN
AccessioniPrimary (citable) accession number: Q9NWM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi