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Reviewed, UniProtKB/Swiss-Prot Q96AY3 (FKB10_HUMAN)

Last modified June 16, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    FK506-binding protein 10
    EC=5.2.1.8
Alternative name(s):
    Peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
      Short name=Rotamase
    Immunophilin FKBP65
    65 kDa FK506-binding protein
    FKBP65
Gene names
Name: FKBP10
Synonyms: FKBP65
ORF Names: PSEC0056
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length582 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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 both FK506 and rapamycin, but not by cyclosporin A By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity.

Post-translational modification

Glycosylated and phosphorylated By similarity.

Sequence similarities

Contains 2 EF-hand domains.

Contains 4 PPIase FKBP-type domains.

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Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
   LigandCalcium
   Molecular functionIsomerase
Rotamase
   PTMGlycoprotein
Phosphoprotein
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 582556FK506-binding protein 10
PRO_0000025517

Regions

Domain62 – 15089PPIase FKBP-type 1
Domain174 – 26289PPIase FKBP-type 2
Domain286 – 37489PPIase FKBP-type 3
Domain399 – 48688PPIase FKBP-type 4
Domain497 – 53236EF-hand 1
Domain542 – 57736EF-hand 2
Calcium binding510 – 521121 Potential
Calcium binding555 – 566122 Potential
Motif579 – 5824Prevents secretion from ER Potential

Amino acid modifications

Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Ref.6
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3101N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Potential
Glycosylation3931N-linked (GlcNAc...) Potential
Glycosylation4071N-linked (GlcNAc...) Ref.6

Natural variations

Natural variant1971K → R: dbSNP rs34764749.
VAR_050625

Experimental info

Sequence conflict1901S → F in BAB20974. Ref.2
Sequence conflict4561V → L in CAD97695. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Q96AY3-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 98257459158407C2

FASTA58264,245
        10         20         30         40         50         60 
MFPAGPPSHS LLRLPLLQLL LLVVQAVGRG LGRASPAGGP LEDVVIERYH IPRACPREVQ 

        70         80         90        100        110        120 
MGDFVRYHYN GTFEDGKKFD SSYDRNTLVA IVVGVGRLIT GMDRGLMGMC VNERRRLIVP 

       130        140        150        160        170        180 
PHLGYGSIGL AGLIPPDATL YFDVVLLDVW NKEDTVQVST LLRPPHCPRM VQDGDFVRYH 

       190        200        210        220        230        240 
YNGTLLDGTS FDTSYSKGGT YDTYVGSGWL IKGMDQGLLG MCPGERRKII IPPFLAYGEK 

       250        260        270        280        290        300 
GYGTVIPPQA SLVFHVLLID VHNPKDAVQL ETLELPPGCV RRAGAGDFMR YHYNGSLMDG 

       310        320        330        340        350        360 
TLFDSSYSRN HTYNTYIGQG YIIPGMDQGL QGACMGERRR ITIPPHLAYG ENGTGDKIPG 

       370        380        390        400        410        420 
SAVLIFNVHV IDFHNPADVV EIRTLSRPSE TCNETTKLGD FVRYHYNCSL LDGTQLFTSH 

       430        440        450        460        470        480 
DYGAPQEATL GANKVIEGLD TGLQGMCVGE RRQLIVPPHL AHGESGARGV PGSAVLLFEV 

       490        500        510        520        530        540 
ELVSREDGLP TGYLFVWHKD PPANLFEDMD LNKDGEVPPE EFSTFIKAQV SEGKGRLMPG 

       550        560        570        580 
QDPEKTIGDM FQNQDRNQDG KITVDELKLK SDEDEERVHE EL

« Hide

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References

« Hide 'large scale' references
[1]"The human FK506-binding protein repertoire."
Rulten S., Kinloch R.A., Robinson C., Gettins L., Kay J.E.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"HRI human cDNA sequencing project."
Ota T., Nishikawa T., Kawai Y., Suzuki Y., Ishii S., Saito K., Yamamoto J., Sugano S., Isogai T.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Teratocarcinoma.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Endometrial tumor and Uterus.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-582.
[6]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed: 12754519] [Abstract]
Cited for: GLYCOSYLATION AT ASN-182 AND ASN-407.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-182, MASS SPECTROMETRY.
Tissue: Liver.

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Cross-references

Sequence databases

AF337909 mRNA. Translation: AAM15770.1.
AB045981 mRNA. Translation: BAB20974.1.
BX537452 mRNA. Translation: CAD97695.1. Different initiation.
AL133116 mRNA. Translation: CAB61418.1.
BC016467 mRNA. Translation: AAH16467.1.
AK025694 mRNA. Translation: BAB15220.1. Different initiation.
IPIIPI00303300.
PIRT42709.
RefSeqNP_068758.3.
UniGeneHs.463035

3D structure databases

HSSPHSSP built from PDB template 1YAT based on UniProtKB P20081.
ModBaseSearch...

Proteomic databases

PeptideAtlasQ96AY3.
PRIDEQ96AY3.

Genome annotation databases

EnsemblENSG00000141756. Homo sapiens. [Contig view]
GeneID60681.
KEGGhsa:60681.

Organism-specific databases

GeneCardsGC17P037222.
H-InvDBHIX0013820.
HGNCHGNC:18169. FKBP10.
MIM607063. gene.
PharmGKBPA28152.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ96AY3.
HOVERGENQ96AY3.
OMAQ96AY3. DRGLMGM.

Enzyme and pathway databases

BRENDA5.2.1.8. 247.

Gene expression databases

ArrayExpressQ96AY3.
BgeeQ96AY3.
CleanExHS_FKBP10.
GermOnlineENSG00000141756. Homo sapiens.

Family and domain databases

InterProIPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR000886. ER_targeting_sequence.
IPR001179. PPIase_FKBP.
[Graphical view]
PANTHERPTHR10516. PPIase_FKBP. 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 Resources

NextBio65504.
SOURCESearch...

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Entry information

Entry nameFKB10_HUMAN
AccessionPrimary (citable) accession number: Q96AY3
Secondary accession number(s): Q7Z3R4 expand/collapse secondary AC list , Q9H3N3, Q9H6N5, Q9UF89
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: December 1, 2001
Last modified: June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents