Q5T1M5 (FKB15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1219 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Endocytosis Transport
Cellular component	Cell projection Cytoplasm Endosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	endocytosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of phosphatase activity Inferred from direct assay. Source: UniProtKB protein folding Inferred from electronic annotation. Source: InterPro
Cellular component	axon Inferred from electronic annotation. Source: UniProtKB-SubCell early endosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1219	1219	FK506-binding protein 15		PRO_0000299556
Regions
	Domain	197 – 290	94	PPIase FKBP-type
	Region	72 – 169	98	Important for function in growth cone organization By similarity
	Coiled coil	522 – 789	268	Potential
	Coiled coil	818 – 878	61	Potential
	Coiled coil	925 – 951	27	Potential
	Compositional bias	1208 – 1216	9	Poly-Asp
Amino acid modifications
	Modified residue	92	1	N6-acetyllysine Ref.12
	Modified residue	307	1	Phosphoserine By similarity
	Modified residue	311	1	Phosphoserine Ref.5
	Modified residue	326	1	Phosphoserine Ref.11
	Modified residue	344	1	Phosphoserine Ref.7
	Modified residue	346	1	Phosphoserine Ref.7 Ref.9
	Modified residue	356	1	Phosphoserine Ref.7 Ref.9 Ref.11
	Modified residue	939	1	Phosphoserine Ref.7
	Modified residue	940	1	Phosphoserine Ref.7
	Modified residue	941	1	Phosphoserine Ref.7
	Modified residue	956	1	Phosphoserine Ref.5 Ref.7
	Modified residue	979	1	Phosphoserine Ref.7
	Modified residue	1094	1	Phosphothreonine Ref.7
	Modified residue	1097	1	Phosphoserine Ref.7
	Modified residue	1099	1	Phosphothreonine By similarity
	Modified residue	1114	1	Phosphoserine Ref.4 Ref.7 Ref.11
	Modified residue	1161	1	Phosphoserine Ref.6 Ref.8
	Modified residue	1162	1	Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9
	Modified residue	1164	1	Phosphoserine Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11
	Modified residue	1195	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	462 – 472	11	PYAGMQAYAYP → VTFYNRINYIL in isoform 3.		VSP_027756
	Alternative sequence	473 – 1219	747	Missing in isoform 3.		VSP_027757
	Alternative sequence	629 – 638	10	Missing in isoform 2.		VSP_027758
	Natural variant	106	1	A → T. Corresponds to variant rs1133618 [ dbSNP | Ensembl ].		VAR_034851
	Natural variant	413	1	H → Q. Ref.1 Ref.3 Corresponds to variant rs10435864 [ dbSNP | Ensembl ].		VAR_034852
	Natural variant	434	1	L → F. Corresponds to variant rs10465129 [ dbSNP | Ensembl ].		VAR_034853
	Natural variant	847	1	A → S. Corresponds to variant rs1128116 [ dbSNP | Ensembl ].		VAR_061543
	Natural variant	993	1	P → T. Corresponds to variant rs57348436 [ dbSNP | Ensembl ].		VAR_061544

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: 86563D82B540B51D	FASTA	1,219	133,630
	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
	Isoform 2 [UniParc]. Checksum: AD3F9C4AA1FD65A6	FASTA	1,209	132,467
	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 QTATENTQAK VTEELAAATA QVSHLQLKMT AHQKKETELQ 670 680 690 700 710 720 MQLTESLKET DLLRGQLTKV QAKLSELQET SEQAQSKFKS EKQNRKQLEL KVTSLEEELT 730 740 750 760 770 780 DLRVEKESLE KNLSERKKKS AQERSQAEEE IDEIRKSYQE ELDKLRQLLK KTRVSTDQAA 790 800 810 820 830 840 AEQLSLVQAE LQTQWEAKCE HLLASAKDEH LQQYQEVCAQ RDAYQQKLVQ LQEKCLALQA 850 860 870 880 890 900 QITALTKQNE QHIKELEKNK SQMSGVEAAA SDPSEKVKKI MNQVFQSLRR EFELEESYNG 910 920 930 940 950 960 RTILGTIMNT IKMVTLQLLN QQEQEKEESS SEEEEEKAEE RPRRPSQEQS ASASSGQPQA 970 980 990 1000 1010 1020 PLNRERPESP MVPSEQVVEE AVPLPPQALT TSQDGHRRKG DSEAEALSEI KDGSLPPELS 1030 1040 1050 1060 1070 1080 CIPSHRVLGP PTSIPPEPLG PVSMDSECEE SLAASPMAAK PDNPSGKVCV REVAPDGPLQ 1090 1100 1110 1120 1130 1140 ESSTRLSLTS DPEEGDPLAL GPESPGEPQP PQLKKDDVTS STGPHKELSS TEAGSTVAGA 1150 1160 1170 1180 1190 1200 ALRPSHHSQR SSLSGDEEDE LFKGATLKAL RPKAQPEEED EDEVSMKGRP PPTPLFGDDD DDDDIDWLG
	Isoform 3 [UniParc]. Checksum: 2112364B487D6E69	FASTA	472	50,330
	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 QMTSQAPQPS VTGLQAPSAA LMQVSSLDSH SAVSGNAQSF QVTFYNRINY IL

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00646791. IPI00853400. IPI00855962.
PIR	T00363.
RefSeq	NP_056073.1. NM_015258.1.
UniGene	Hs.522351.
3D structure databases
HSSP	HSSP built from PDB template 1U79 based on UniProtKB Q9SCY2.
ProteinModelPortal	Q5T1M5.
SMR	Q5T1M5. Positions 180-289.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5T1M5.
PTM databases
PhosphoSite	Q5T1M5.
Polymorphism databases
DMDM	158563913.
Proteomic databases
PRIDE	Q5T1M5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000238256; ENSP00000238256; ENSG00000119321. ENST00000446284; ENSP00000416158; ENSG00000119321.
GeneID	23307.
KEGG	hsa:23307.
UCSC	uc004bgs.2. human. uc004bgt.2. human.
Organism-specific databases
CTD	23307.
GeneCards	GC09M115923.
H-InvDB	HIX0008300. HIX0153287.
HGNC	HGNC:23397. FKBP15.
HPA	HPA007979.
neXtProt	NX_Q5T1M5.
PharmGKB	PA162388608.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12978.
GeneTree	ENSGT00530000064286.
HOGENOM	HBG447023.
HOVERGEN	HBG067251.
InParanoid	Q5T1M5.
OrthoDB	EOG4CNQQ8.
Gene expression databases
ArrayExpress	Q5T1M5.
Bgee	Q5T1M5.
CleanEx	HS_FKBP15.
Genevestigator	Q5T1M5.
Family and domain databases
InterPro	IPR001179. PPIase_FKBP_dom. [Graphical view]
Pfam	PF00254. FKBP_C. 1 hit. [Graphical view]
PROSITE	PS50059. FKBP_PPIASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	45162.

Entry information

Entry name

FKB15_HUMAN

Accession

Primary (citable) accession number: Q5T1M5
Secondary accession number(s): Q05DK8 , Q5T1M2, Q6DD85, Q9Y4D0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	January 25, 2012
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.