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Q9Y680

- FKBP7_HUMAN

UniProt

Q9Y680 - FKBP7_HUMAN

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Protein

Peptidyl-prolyl cis-trans isomerase FKBP7

Gene

FKBP7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 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 bindingi195 – 206121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi239 – 250122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: Ensembl
  2. FK506 binding Source: RefGenome
  3. 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

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP7 (EC:5.2.1.8)
Short name:
PPIase FKBP7
Alternative name(s):
23 kDa FK506-binding protein
Short name:
23 kDa FKBP
Short name:
FKBP-23
FK506-binding protein 7
Short name:
FKBP-7
Rotamase
Gene namesi
Name:FKBP7
Synonyms:FKBP23
ORF Names:UNQ670/PRO1304
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:3723. FKBP7.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28164.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 259236Peptidyl-prolyl cis-trans isomerase FKBP7PRO_0000025513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9Y680.
PaxDbiQ9Y680.
PRIDEiQ9Y680.

PTM databases

PhosphoSiteiQ9Y680.

Expressioni

Gene expression databases

BgeeiQ9Y680.
CleanExiHS_FKBP7.
ExpressionAtlasiQ9Y680. baseline and differential.
GenevestigatoriQ9Y680.

Organism-specific databases

HPAiHPA008707.

Interactioni

Protein-protein interaction databases

BioGridi119666. 7 interactions.
IntActiQ9Y680. 4 interactions.
MINTiMINT-4723228.
STRINGi9606.ENSP00000413152.

Structurei

3D structure databases

ProteinModelPortaliQ9Y680.
SMRiQ9Y680. Positions 34-258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 182130PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST
Domaini182 – 21736EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini226 – 25934EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi256 – 2594Prevents 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.
InParanoidiQ9Y680.
KOiK09573.
OMAiRPENCSK.
OrthoDBiEOG7T1R9S.
PhylomeDBiQ9Y680.
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. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS00014. ER_TARGET. 1 hit.
PS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y680-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPKTMHFLFR FIVFFYLWGL FTAQRQKKEE STEEVKIEVL HRPENCSKTS
60 70 80 90 100
KKGDLLNAHY DGYLAKDGSK FYCSRTQNEG HPKWFVLGVG QVIKGLDIAM
110 120 130 140 150
TDMCPGEKRK VVIPPSFAYG KEGYGSLEEV FLLQNILVSC HRTTLHVLKC
160 170 180 190 200
MYLLVLNNNT CAEGKIPPDA TLIFEIELYA VTKGPRSIET FKQIDMDNDR
210 220 230 240 250
QLSKAEINLY LQREFEKDEK PRDKSYQDAV LEDIFKKNDH DGDGFISPKE

YNVYQHDEL
Length:259
Mass (Da):30,009
Last modified:November 1, 1999 - v1
Checksum:i886A1F3F5ACB9E78
GO
Isoform 2 (identifier: Q9Y680-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     125-161: Missing.

Show »
Length:222
Mass (Da):25,794
Checksum:i362957BAD3C5C2A6
GO
Isoform 3 (identifier: Q9Y680-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     125-162: Missing.

Show »
Length:221
Mass (Da):25,723
Checksum:i7A00D79506D301BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241Y → H in AAD40379. (PubMed:10931946)Curated
Sequence conflicti237 – 2371K → M in AAQ57208. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei125 – 16238Missing in isoform 3. 1 PublicationVSP_041018Add
BLAST
Alternative sequencei125 – 16137Missing in isoform 2. 5 PublicationsVSP_005187Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF092137 mRNA. Translation: AAD40379.1.
AF100751 mRNA. Translation: AAD43015.1.
AY359015 mRNA. Translation: AAQ89374.1.
AK292145 mRNA. Translation: BAF84834.1.
BT007122 mRNA. Translation: AAP35786.1.
AY353086 mRNA. Translation: AAQ57208.1.
AC009948 Genomic DNA. Translation: AAX88883.1.
BC009711 mRNA. Translation: AAH09711.1.
CCDSiCCDS2280.1. [Q9Y680-2]
CCDS46462.1. [Q9Y680-3]
RefSeqiNP_001128684.1. NM_001135212.1. [Q9Y680-3]
NP_851939.1. NM_181342.2. [Q9Y680-2]
UniGeneiHs.410378.

Genome annotation databases

EnsembliENST00000424785; ENSP00000413152; ENSG00000079150. [Q9Y680-2]
ENST00000434643; ENSP00000415486; ENSG00000079150. [Q9Y680-3]
GeneIDi51661.
KEGGihsa:51661.
UCSCiuc002umk.3. human. [Q9Y680-2]
uc002umm.3. human. [Q9Y680-3]

Polymorphism databases

DMDMi23396602.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF092137 mRNA. Translation: AAD40379.1 .
AF100751 mRNA. Translation: AAD43015.1 .
AY359015 mRNA. Translation: AAQ89374.1 .
AK292145 mRNA. Translation: BAF84834.1 .
BT007122 mRNA. Translation: AAP35786.1 .
AY353086 mRNA. Translation: AAQ57208.1 .
AC009948 Genomic DNA. Translation: AAX88883.1 .
BC009711 mRNA. Translation: AAH09711.1 .
CCDSi CCDS2280.1. [Q9Y680-2 ]
CCDS46462.1. [Q9Y680-3 ]
RefSeqi NP_001128684.1. NM_001135212.1. [Q9Y680-3 ]
NP_851939.1. NM_181342.2. [Q9Y680-2 ]
UniGenei Hs.410378.

3D structure databases

ProteinModelPortali Q9Y680.
SMRi Q9Y680. Positions 34-258.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119666. 7 interactions.
IntActi Q9Y680. 4 interactions.
MINTi MINT-4723228.
STRINGi 9606.ENSP00000413152.

PTM databases

PhosphoSitei Q9Y680.

Polymorphism databases

DMDMi 23396602.

Proteomic databases

MaxQBi Q9Y680.
PaxDbi Q9Y680.
PRIDEi Q9Y680.

Protocols and materials databases

DNASUi 51661.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000424785 ; ENSP00000413152 ; ENSG00000079150 . [Q9Y680-2 ]
ENST00000434643 ; ENSP00000415486 ; ENSG00000079150 . [Q9Y680-3 ]
GeneIDi 51661.
KEGGi hsa:51661.
UCSCi uc002umk.3. human. [Q9Y680-2 ]
uc002umm.3. human. [Q9Y680-3 ]

Organism-specific databases

CTDi 51661.
GeneCardsi GC02M179328.
H-InvDB HIX0002629.
HGNCi HGNC:3723. FKBP7.
HPAi HPA008707.
MIMi 607062. gene.
neXtProti NX_Q9Y680.
PharmGKBi PA28164.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0545.
GeneTreei ENSGT00530000062784.
HOGENOMi HOG000154887.
HOVERGENi HBG051623.
InParanoidi Q9Y680.
KOi K09573.
OMAi RPENCSK.
OrthoDBi EOG7T1R9S.
PhylomeDBi Q9Y680.
TreeFami TF105296.

Miscellaneous databases

GenomeRNAii 51661.
NextBioi 55642.
PROi Q9Y680.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y680.
CleanExi HS_FKBP7.
ExpressionAtlasi Q9Y680. baseline and differential.
Genevestigatori Q9Y680.

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. 2 hits.
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 [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Pituitary and Pituitary tumor.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. "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] (ISOFORM 2).
    Tissue: Synovial cell.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. Li H., Zhong G., Yu R., Shen C., Zhou G., Li M., Xiao W., Lin L., Yang S.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 2).
    Tissue: Lung.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFKBP7_HUMAN
AccessioniPrimary (citable) accession number: Q9Y680
Secondary accession number(s): Q4ZG70
, Q6V3B2, Q86U65, Q96DA4, Q9Y6B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 138 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

Miscellaneous

Binds calcium.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3