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Q5T1M5 (FKB15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 16, 2012. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FK506-binding protein 15
Short name=FKBP-15
Alternative name(s):
133 kDa FK506-binding protein
Short name=133 kDa FKBP
Short name=FKBP-133
WASP and FKBP-like
Short name=WAFL
Gene names
Name:FKBP15
Synonyms:KIAA0674
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length1219 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase By similarity. Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. Ref.10

Subunit structure

Interacts with WIP and actin. Ref.10

Subcellular location

Cytoplasm By similarity. Cell projection › axon By similarity. Early endosome. Note: Present in axons and neuronal growth cones By similarity. Ref.10

Domain

The PPIase FKBP-type domain seems to be inactive both for FK506-binding and enzymatic activity By similarity.

The central coiled-coil region is responsible for association with early endosomes.

Sequence similarities

Belongs to the FKBP-type PPIase family.

Contains 1 PPIase FKBP-type domain.

Sequence caution

The sequence AAH09609.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA31649.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI10963.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI10964.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processEndocytosis
Transport
   Cellular componentCell projection
Cytoplasm
Endosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processendocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of phosphatase activity

Inferred from direct assay PubMed 19389623. Source: UniProtKB

protein folding

Inferred from electronic annotation. Source: InterPro

   Cellular componentaxon

Inferred from electronic annotation. Source: UniProtKB-SubCell

early endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionactin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5T1M5-1)

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.
Isoform 2 (identifier: Q5T1M5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     629-638: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q5T1M5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     462-472: PYAGMQAYAYP → VTFYNRINYIL
     473-1219: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12191219FK506-binding protein 15
PRO_0000299556

Regions

Domain197 – 29094PPIase FKBP-type
Region72 – 16998Important for function in growth cone organization By similarity
Coiled coil522 – 789268 Potential
Coiled coil818 – 87861 Potential
Coiled coil925 – 95127 Potential
Compositional bias1208 – 12169Poly-Asp

Amino acid modifications

Modified residue921N6-acetyllysine Ref.12
Modified residue3071Phosphoserine By similarity
Modified residue3111Phosphoserine Ref.5
Modified residue3261Phosphoserine Ref.11
Modified residue3441Phosphoserine Ref.7
Modified residue3461Phosphoserine Ref.7 Ref.9
Modified residue3561Phosphoserine Ref.7 Ref.9 Ref.11
Modified residue9391Phosphoserine Ref.7
Modified residue9401Phosphoserine Ref.7
Modified residue9411Phosphoserine Ref.7
Modified residue9561Phosphoserine Ref.5 Ref.7
Modified residue9791Phosphoserine Ref.7
Modified residue10941Phosphothreonine Ref.7
Modified residue10971Phosphoserine Ref.7
Modified residue10991Phosphothreonine By similarity
Modified residue11141Phosphoserine Ref.4 Ref.7 Ref.11
Modified residue11611Phosphoserine Ref.6 Ref.8
Modified residue11621Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9
Modified residue11641Phosphoserine Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11
Modified residue11951Phosphoserine By similarity

Natural variations

Alternative sequence462 – 47211PYAGMQAYAYP → VTFYNRINYIL in isoform 3.
VSP_027756
Alternative sequence473 – 1219747Missing in isoform 3.
VSP_027757
Alternative sequence629 – 63810Missing in isoform 2.
VSP_027758
Natural variant1061A → T.
Corresponds to variant rs1133618 [ dbSNP | Ensembl ].
VAR_034851
Natural variant4131H → Q. Ref.1 Ref.3
Corresponds to variant rs10435864 [ dbSNP | Ensembl ].
VAR_034852
Natural variant4341L → F.
Corresponds to variant rs10465129 [ dbSNP | Ensembl ].
VAR_034853
Natural variant8471A → S.
Corresponds to variant rs1128116 [ dbSNP | Ensembl ].
VAR_061543
Natural variant9931P → T.
Corresponds to variant rs57348436 [ dbSNP | Ensembl ].
VAR_061544

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: 86563D82B540B51D

FASTA1,219133,630
        10         20         30         40         50         60 
MFGAGDEDDT DFLSPSGGAR LASLFGLDQA AAGHGNEFFQ YTAPKQPKKG QGTAATGNQA 

        70         80         90        100        110        120 
TPKTAPATMS TPTILVATAV HAYRYTNGQY VKQGKFGAAV LGNHTAREYR ILLYISQQQP 

       130        140        150        160        170        180 
VTVARIHVNF ELMVRPNNYS TFYDDQRQNW SIMFESEKAA VEFNKQVCIA KCNSTSSLDA 

       190        200        210        220        230        240 
VLSQDLIVAD GPAVEVGDSL EVAYTGWLFQ NHVLGQVFDS TANKDKLLRL KLGSGKVIKG 

       250        260        270        280        290        300 
WEDGMLGMKK GGKRLLIVPP ACAVGSEGVI GWTQATDSIL VFEVEVRRVK FARDSGSDGH 

       310        320        330        340        350        360 
SVSSRDSAAP SPIPGADNLS ADPVVSPPTS IPFKSGEPAL RTKSNSLSEQ LAINTSPDAV 

       370        380        390        400        410        420 
KAKLISRMAK MGQPMLPILP PQLDSNDSEI EDVNTLQGGG QPVVTPSVQP SLHPAHPALP 

       430        440        450        460        470        480 
QMTSQAPQPS VTGLQAPSAA LMQVSSLDSH SAVSGNAQSF QPYAGMQAYA YPQASAVTSQ 

       490        500        510        520        530        540 
LQPVRPLYPA PLSQPPHFQG SGDMASFLMT EARQHNTEIR MAVSKVADKM DHLMTKVEEL 

       550        560        570        580        590        600 
QKHSAGNSML IPSMSVTMET SMIMSNIQRI IQENERLKQE ILEKSNRIEE QNDKISELIE 

       610        620        630        640        650        660 
RNQRYVEQSN LMMEKRNNSL QTATENTQAR VLHAEQEKAK VTEELAAATA QVSHLQLKMT 

       670        680        690        700        710        720 
AHQKKETELQ MQLTESLKET DLLRGQLTKV QAKLSELQET SEQAQSKFKS EKQNRKQLEL 

       730        740        750        760        770        780 
KVTSLEEELT DLRVEKESLE KNLSERKKKS AQERSQAEEE IDEIRKSYQE ELDKLRQLLK 

       790        800        810        820        830        840 
KTRVSTDQAA AEQLSLVQAE LQTQWEAKCE HLLASAKDEH LQQYQEVCAQ RDAYQQKLVQ 

       850        860        870        880        890        900 
LQEKCLALQA QITALTKQNE QHIKELEKNK SQMSGVEAAA SDPSEKVKKI MNQVFQSLRR 

       910        920        930        940        950        960 
EFELEESYNG RTILGTIMNT IKMVTLQLLN QQEQEKEESS SEEEEEKAEE RPRRPSQEQS 

       970        980        990       1000       1010       1020 
ASASSGQPQA PLNRERPESP MVPSEQVVEE AVPLPPQALT TSQDGHRRKG DSEAEALSEI 

      1030       1040       1050       1060       1070       1080 
KDGSLPPELS CIPSHRVLGP PTSIPPEPLG PVSMDSECEE SLAASPMAAK PDNPSGKVCV 

      1090       1100       1110       1120       1130       1140 
REVAPDGPLQ ESSTRLSLTS DPEEGDPLAL GPESPGEPQP PQLKKDDVTS STGPHKELSS 

      1150       1160       1170       1180       1190       1200 
TEAGSTVAGA ALRPSHHSQR SSLSGDEEDE LFKGATLKAL RPKAQPEEED EDEVSMKGRP 

      1210 
PPTPLFGDDD DDDDIDWLG

« Hide

Isoform 2 [UniParc].

Checksum: AD3F9C4AA1FD65A6
Show »

FASTA1,209132,467
Isoform 3 [UniParc].

Checksum: 2112364B487D6E69
Show »

FASTA47250,330

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed: 9734811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-413.
Tissue: Brain.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed: 15164053] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 548-1219 (ISOFORM 2), VARIANT GLN-413.
Tissue: Eye and Prostate.
[4]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1114 AND SER-1164, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[5]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 AND SER-956, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1161; SER-1162 AND SER-1164, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344; SER-346; SER-356; SER-939; SER-940; SER-941; SER-956; SER-979; THR-1094; SER-1097; SER-1114; SER-1162 AND SER-1164, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1161; SER-1162 AND SER-1164, MASS SPECTROMETRY.
Tissue: Liver.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346; SER-356; SER-1162 AND SER-1164, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[10]"WAFL, a new protein involved in regulation of early endocytic transport at the intersection of actin and microtubule dynamics."
Viklund I.-M., Aspenstroem P., Meas-Yedid V., Zhang B., Kopec J., Agren D., Schneider G., D'Amato M., Olivo-Marin J.-C., Sansonetti P., Van Nhieu G.T., Pettersson S.
Exp. Cell Res. 315:1040-1052(2009) [PubMed: 19121306] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ACTIN AND WIP.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-356; SER-1114 AND SER-1164, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, MASS SPECTROMETRY.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB014574 mRNA. Translation: BAA31649.1. Different initiation.
AL449305 Genomic DNA. Translation: CAI10963.1. Different initiation.
AL449305, AL449105 Genomic DNA. Translation: CAI10964.1. Different initiation.
AL449105, AL449305 Genomic DNA. Translation: CAI95402.1.
BC009609 mRNA. Translation: AAH09609.1. Different initiation.
BC077732 mRNA. Translation: AAH77732.1.
IPIIPI00646791.
IPI00853400.
IPI00855962.
PIRT00363.
RefSeqNP_056073.1. NM_015258.1.
UniGeneHs.522351.

3D structure databases

HSSPHSSP built from PDB template 1U79 based on UniProtKB Q9SCY2.
ProteinModelPortalQ5T1M5.
SMRQ5T1M5. Positions 180-289.
ModBaseSearch...

Protein-protein interaction databases

IntActQ5T1M5. 1 interaction.
STRINGQ5T1M5.

PTM databases

PhosphoSiteQ5T1M5.

Polymorphism databases

DMDM158563913.

Proteomic databases

PRIDEQ5T1M5.

Protocols and materials databases

DNASU23307.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238256; ENSP00000238256; ENSG00000119321.
ENST00000446284; ENSP00000416158; ENSG00000119321.
GeneID23307.
KEGGhsa:23307.
UCSCuc004bgr.2. human.
uc004bgs.2. human.
uc004bgt.2. human.

Organism-specific databases

CTD23307.
GeneCardsGC09M115923.
H-InvDBHIX0008300.
HIX0153287.
HGNCHGNC:23397. FKBP15.
HPAHPA007979.
neXtProtNX_Q5T1M5.
PharmGKBPA162388608.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0545.
GeneTreeENSGT00530000064286.
HOGENOMHOG000112601.
HOVERGENHBG067251.
InParanoidQ5T1M5.
OrthoDBEOG4CNQQ8.

Gene expression databases

ArrayExpressQ5T1M5.
BgeeQ5T1M5.
CleanExHS_FKBP15.
GenevestigatorQ5T1M5.

Family and domain databases

InterProIPR001179. PPIase_FKBP_dom.
[Graphical view]
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio45162.

Entry information

Entry nameFKB15_HUMAN
AccessionPrimary (citable) accession number: Q5T1M5
Secondary accession number(s): Q05DK8 expand/collapse secondary AC list , Q5T1M2, Q6DD85, Q9Y4D0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: May 16, 2012
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 9

Human chromosome 9: 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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents