Skip Header

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

Peptidyl-prolyl cis-trans isomerase FKBP14

Gene

FKBP14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 159121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi192 – 203122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi5.2.1.8. 2681.
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 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:18625. FKBP14.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Ehlers-Danlos syndrome, with progressive kyphoscoliosis, myopathy, and hearing loss (EDSKMH)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:614557

Keywords - Diseasei

Deafness, Ehlers-Danlos syndrome

Organism-specific databases

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

Polymorphism and mutation databases

BioMutaiFKBP14.
DMDMi23821568.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 211192Peptidyl-prolyl cis-trans isomerase FKBP14PRO_0000025521Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9NWM8.
PaxDbiQ9NWM8.
PRIDEiQ9NWM8.

PTM databases

PhosphoSiteiQ9NWM8.

Expressioni

Gene expression databases

BgeeiQ9NWM8.
CleanExiHS_FKBP14.
ExpressionAtlasiQ9NWM8. baseline and differential.
GenevisibleiQ9NWM8. HS.

Organism-specific databases

HPAiHPA013329.
HPA026829.

Interactioni

Protein-protein interaction databases

BioGridi120362. 14 interactions.
IntActiQ9NWM8. 3 interactions.
MINTiMINT-8247492.
STRINGi9606.ENSP00000222803.

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 213Combined sources
Beta strandi28 – 336Combined sources
Beta strandi47 – 5610Combined sources
Turni57 – 593Combined sources
Beta strandi62 – 654Combined sources
Helixi66 – 694Combined sources
Turni70 – 723Combined sources
Beta strandi75 – 784Combined sources
Turni79 – 824Combined sources
Helixi86 – 916Combined sources
Beta strandi100 – 1056Combined sources
Helixi107 – 1093Combined sources
Turni110 – 1145Combined sources
Beta strandi125 – 13511Combined sources
Helixi141 – 1477Combined sources
Beta strandi152 – 1565Combined sources
Helixi157 – 17014Combined sources
Helixi177 – 19115Combined sources
Beta strandi196 – 2005Combined sources
Helixi201 – 2055Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 13591PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST
Domaini135 – 17036EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini179 – 21133EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi208 – 2114Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG0545.
GeneTreeiENSGT00530000062784.
HOGENOMiHOG000154887.
HOVERGENiHBG051623.
InParanoidiQ9NWM8.
KOiK09577.
OMAiNDTQHDA.
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

        10         20         30         40         50
MRLFLWNAVL TLFVTSLIGA LIPEPEVKIE VLQKPFICHR KTKGGDLMLV
60 70 80 90 100
HYEGYLEKDG SLFHSTHKHN NGQPIWFTLG ILEALKGWDQ GLKGMCVGEK
110 120 130 140 150
RKLIIPPALG YGKEGKGKIP PESTLIFNID LLEIRNGPRS HESFQEMDLN
160 170 180 190 200
DDWKLSKDEV KAYLKKEFEK HGAVVNESHH DALVEDIFDK EDEDKDGFIS
210
AREFTYKHDE L
Length:211
Mass (Da):24,172
Last modified:October 1, 2000 - v1
Checksum:i858184954FE10029
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120362. 14 interactions.
IntActiQ9NWM8. 3 interactions.
MINTiMINT-8247492.
STRINGi9606.ENSP00000222803.

Chemistry

BindingDBiQ9NWM8.
ChEMBLiCHEMBL2342.

PTM databases

PhosphoSiteiQ9NWM8.

Polymorphism and mutation databases

BioMutaiFKBP14.
DMDMi23821568.

Proteomic databases

MaxQBiQ9NWM8.
PaxDbiQ9NWM8.
PRIDEiQ9NWM8.

Protocols and materials databases

DNASUi55033.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi55033.
GeneCardsiGC07M030050.
HGNCiHGNC:18625. FKBP14.
HPAiHPA013329.
HPA026829.
MIMi614505. gene.
614557. phenotype.
neXtProtiNX_Q9NWM8.
Orphaneti300179. Ehlers-Danlos syndrome, kyphoscoliotic and deafness type.
PharmGKBiPA38608.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0545.
GeneTreeiENSGT00530000062784.
HOGENOMiHOG000154887.
HOVERGENiHBG051623.
InParanoidiQ9NWM8.
KOiK09577.
OMAiNDTQHDA.
OrthoDBiEOG7T1R9S.
PhylomeDBiQ9NWM8.
TreeFamiTF105296.

Enzyme and pathway databases

BRENDAi5.2.1.8. 2681.
ReactomeiREACT_18273. XBP1(S) activates chaperone genes.

Miscellaneous databases

GenomeRNAii55033.
NextBioi58455.
PROiQ9NWM8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NWM8.
CleanExiHS_FKBP14.
ExpressionAtlasiQ9NWM8. baseline and differential.
GenevisibleiQ9NWM8. HS.

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]
ProtoNetiSearch...

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: July 22, 2015
This is version 137 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

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.