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Protein

Peptidyl-prolyl cis-trans isomerase FKBP14

Gene

FKBP14

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: 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).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi148 – 159121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi192 – 203122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP14 (EC:5.2.1.8)
Short name:
PPIase FKBP14
Alternative name(s):
FK506-binding protein 14
Short name:
FKBP-14
Rotamase
Gene namesi
Name:FKBP14
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595 Componenti: Unplaced

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 211192Peptidyl-prolyl cis-trans isomerase FKBP14PRO_0000025523Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ5R941.

Interactioni

Structurei

3D structure databases

ProteinModelPortaliQ5R941.
SMRiQ5R941. 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

HOVERGENiHBG051623.
InParanoidiQ5R941.
KOiK09577.

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.

Q5R941-1 [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:December 20, 2004 - v1
Checksum:i858184954FE10029
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR859554 mRNA. Translation: CAH91719.1.
RefSeqiNP_001127454.1. NM_001133982.1.
UniGeneiPab.9172.

Genome annotation databases

GeneIDi100174527.
KEGGipon:100174527.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR859554 mRNA. Translation: CAH91719.1.
RefSeqiNP_001127454.1. NM_001133982.1.
UniGeneiPab.9172.

3D structure databases

ProteinModelPortaliQ5R941.
SMRiQ5R941. Positions 21-209.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ5R941.

Proteomic databases

PRIDEiQ5R941.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100174527.
KEGGipon:100174527.

Organism-specific databases

CTDi55033.

Phylogenomic databases

HOVERGENiHBG051623.
InParanoidiQ5R941.
KOiK09577.

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

  1. The German cDNA consortium
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.

Entry informationi

Entry nameiFKB14_PONAB
AccessioniPrimary (citable) accession number: Q5R941
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2005
Last sequence update: December 20, 2004
Last modified: January 6, 2015
This is version 65 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. 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.