Full text data of FKBP15
FKBP15
(KIAA0674)
[Confidence: low (only semi-automatic identification from reviews)]
FK506-binding protein 15; FKBP-15 (133 kDa FK506-binding protein; 133 kDa FKBP; FKBP-133; WASP and FKBP-like; WAFL)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
FK506-binding protein 15; FKBP-15 (133 kDa FK506-binding protein; 133 kDa FKBP; FKBP-133; WASP and FKBP-like; WAFL)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q5T1M5
ID FKB15_HUMAN Reviewed; 1219 AA.
AC Q5T1M5; Q05DK8; Q5T1M2; Q6DD85; Q9Y4D0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-SEP-2007, sequence version 2.
DT 22-JAN-2014, entry version 86.
DE RecName: Full=FK506-binding protein 15;
DE Short=FKBP-15;
DE AltName: Full=133 kDa FK506-binding protein;
DE Short=133 kDa FKBP;
DE Short=FKBP-133;
DE AltName: Full=WASP and FKBP-like;
DE Short=WAFL;
GN Name=FKBP15; Synonyms=KIAA0674;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP GLN-413.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 548-1219 (ISOFORM 2), AND VARIANT
RP GLN-413.
RC TISSUE=Eye, and Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-956, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1161 AND SER-1162, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346; SER-356; SER-939;
RP SER-940; SER-941; SER-956; SER-979; SER-1114 AND SER-1164, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ACTIN AND WIP.
RX PubMed=19121306; DOI=10.1016/j.yexcr.2008.12.004;
RA Viklund I.-M., Aspenstroem P., Meas-Yedid V., Zhang B., Kopec J.,
RA Agren D., Schneider G., D'Amato M., Olivo-Marin J.-C., Sansonetti P.,
RA Van Nhieu G.T., Pettersson S.;
RT "WAFL, a new protein involved in regulation of early endocytic
RT transport at the intersection of actin and microtubule dynamics.";
RL Exp. Cell Res. 315:1040-1052(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-356; SER-1114;
RP SER-1164; SER-1195 AND THR-1203, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-14; SER-956; SER-1114 AND SER-1164, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1164, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be involved in the cytoskeletal organization of
CC neuronal growth cones. Seems to be inactive as a PPIase (By
CC similarity). Involved in the transport of early endosomes at the
CC level of transition between microfilament-based and microtubule-
CC based movement.
CC -!- SUBUNIT: Interacts with WIP and actin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell projection,
CC axon (By similarity). Early endosome. Note=Present in axons and
CC neuronal growth cones (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5T1M5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T1M5-2; Sequence=VSP_027758;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q5T1M5-3; Sequence=VSP_027756, VSP_027757;
CC -!- DOMAIN: The PPIase FKBP-type domain seems to be inactive both for
CC FK506-binding and enzymatic activity (By similarity).
CC -!- DOMAIN: The central coiled-coil region is responsible for
CC association with early endosomes.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09609.1; Type=Erroneous initiation;
CC Sequence=BAA31649.1; Type=Erroneous initiation;
CC Sequence=CAI10963.1; Type=Erroneous initiation;
CC Sequence=CAI10964.1; Type=Erroneous initiation;
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DR EMBL; AB014574; BAA31649.1; ALT_INIT; mRNA.
DR EMBL; AL449305; CAI10963.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL449305; CAI10964.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL449105; CAI10964.1; JOINED; Genomic_DNA.
DR EMBL; AL449105; CAI95402.1; -; Genomic_DNA.
DR EMBL; AL449305; CAI95402.1; JOINED; Genomic_DNA.
DR EMBL; BC009609; AAH09609.1; ALT_INIT; mRNA.
DR EMBL; BC077732; AAH77732.1; -; mRNA.
DR PIR; T00363; T00363.
DR RefSeq; NP_056073.1; NM_015258.1.
DR UniGene; Hs.522351; -.
DR ProteinModelPortal; Q5T1M5; -.
DR SMR; Q5T1M5; 184-286.
DR IntAct; Q5T1M5; 2.
DR STRING; 9606.ENSP00000238256; -.
DR PhosphoSite; Q5T1M5; -.
DR DMDM; 158563913; -.
DR PaxDb; Q5T1M5; -.
DR PRIDE; Q5T1M5; -.
DR DNASU; 23307; -.
DR Ensembl; ENST00000238256; ENSP00000238256; ENSG00000119321.
DR GeneID; 23307; -.
DR KEGG; hsa:23307; -.
DR UCSC; uc004bgs.2; human.
DR CTD; 23307; -.
DR GeneCards; GC09M115923; -.
DR H-InvDB; HIX0008300; -.
DR H-InvDB; HIX0153287; -.
DR HGNC; HGNC:23397; FKBP15.
DR HPA; HPA007979; -.
DR neXtProt; NX_Q5T1M5; -.
DR PharmGKB; PA162388608; -.
DR eggNOG; COG0545; -.
DR HOGENOM; HOG000112601; -.
DR HOVERGEN; HBG067251; -.
DR InParanoid; Q5T1M5; -.
DR KO; K17478; -.
DR OrthoDB; EOG75XGKG; -.
DR ChiTaRS; FKBP15; human.
DR GenomeRNAi; 23307; -.
DR NextBio; 45162; -.
DR PRO; PR:Q5T1M5; -.
DR ArrayExpress; Q5T1M5; -.
DR Bgee; Q5T1M5; -.
DR CleanEx; HS_FKBP15; -.
DR Genevestigator; Q5T1M5; -.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell projection;
KW Coiled coil; Complete proteome; Cytoplasm; Endocytosis; Endosome;
KW Phosphoprotein; Polymorphism; Reference proteome; Transport.
FT CHAIN 1 1219 FK506-binding protein 15.
FT /FTId=PRO_0000299556.
FT DOMAIN 197 290 PPIase FKBP-type.
FT REGION 72 169 Important for function in growth cone
FT organization (By similarity).
FT COILED 522 789 Potential.
FT COILED 818 878 Potential.
FT COILED 925 951 Potential.
FT COMPBIAS 1208 1216 Poly-Asp.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 92 92 N6-acetyllysine.
FT MOD_RES 326 326 Phosphoserine.
FT MOD_RES 346 346 Phosphoserine.
FT MOD_RES 356 356 Phosphoserine.
FT MOD_RES 939 939 Phosphoserine.
FT MOD_RES 940 940 Phosphoserine.
FT MOD_RES 941 941 Phosphoserine.
FT MOD_RES 956 956 Phosphoserine.
FT MOD_RES 979 979 Phosphoserine.
FT MOD_RES 1097 1097 Phosphoserine (By similarity).
FT MOD_RES 1099 1099 Phosphothreonine (By similarity).
FT MOD_RES 1114 1114 Phosphoserine.
FT MOD_RES 1161 1161 Phosphoserine.
FT MOD_RES 1162 1162 Phosphoserine.
FT MOD_RES 1164 1164 Phosphoserine.
FT MOD_RES 1195 1195 Phosphoserine.
FT MOD_RES 1203 1203 Phosphothreonine.
FT VAR_SEQ 462 472 PYAGMQAYAYP -> VTFYNRINYIL (in isoform
FT 3).
FT /FTId=VSP_027756.
FT VAR_SEQ 473 1219 Missing (in isoform 3).
FT /FTId=VSP_027757.
FT VAR_SEQ 629 638 Missing (in isoform 2).
FT /FTId=VSP_027758.
FT VARIANT 106 106 A -> T (in dbSNP:rs1133618).
FT /FTId=VAR_034851.
FT VARIANT 413 413 H -> Q (in dbSNP:rs10435864).
FT /FTId=VAR_034852.
FT VARIANT 434 434 L -> F (in dbSNP:rs10465129).
FT /FTId=VAR_034853.
FT VARIANT 847 847 A -> S (in dbSNP:rs1128116).
FT /FTId=VAR_061543.
FT VARIANT 993 993 P -> T (in dbSNP:rs57348436).
FT /FTId=VAR_061544.
SQ SEQUENCE 1219 AA; 133630 MW; 86563D82B540B51D CRC64;
MFGAGDEDDT DFLSPSGGAR LASLFGLDQA AAGHGNEFFQ YTAPKQPKKG QGTAATGNQA
TPKTAPATMS TPTILVATAV HAYRYTNGQY VKQGKFGAAV LGNHTAREYR ILLYISQQQP
VTVARIHVNF ELMVRPNNYS TFYDDQRQNW SIMFESEKAA VEFNKQVCIA KCNSTSSLDA
VLSQDLIVAD GPAVEVGDSL EVAYTGWLFQ NHVLGQVFDS TANKDKLLRL KLGSGKVIKG
WEDGMLGMKK GGKRLLIVPP ACAVGSEGVI GWTQATDSIL VFEVEVRRVK FARDSGSDGH
SVSSRDSAAP SPIPGADNLS ADPVVSPPTS IPFKSGEPAL RTKSNSLSEQ LAINTSPDAV
KAKLISRMAK MGQPMLPILP PQLDSNDSEI EDVNTLQGGG QPVVTPSVQP SLHPAHPALP
QMTSQAPQPS VTGLQAPSAA LMQVSSLDSH SAVSGNAQSF QPYAGMQAYA YPQASAVTSQ
LQPVRPLYPA PLSQPPHFQG SGDMASFLMT EARQHNTEIR MAVSKVADKM DHLMTKVEEL
QKHSAGNSML IPSMSVTMET SMIMSNIQRI IQENERLKQE ILEKSNRIEE QNDKISELIE
RNQRYVEQSN LMMEKRNNSL QTATENTQAR VLHAEQEKAK VTEELAAATA QVSHLQLKMT
AHQKKETELQ MQLTESLKET DLLRGQLTKV QAKLSELQET SEQAQSKFKS EKQNRKQLEL
KVTSLEEELT DLRVEKESLE KNLSERKKKS AQERSQAEEE IDEIRKSYQE ELDKLRQLLK
KTRVSTDQAA AEQLSLVQAE LQTQWEAKCE HLLASAKDEH LQQYQEVCAQ RDAYQQKLVQ
LQEKCLALQA QITALTKQNE QHIKELEKNK SQMSGVEAAA SDPSEKVKKI MNQVFQSLRR
EFELEESYNG RTILGTIMNT IKMVTLQLLN QQEQEKEESS SEEEEEKAEE RPRRPSQEQS
ASASSGQPQA PLNRERPESP MVPSEQVVEE AVPLPPQALT TSQDGHRRKG DSEAEALSEI
KDGSLPPELS CIPSHRVLGP PTSIPPEPLG PVSMDSECEE SLAASPMAAK PDNPSGKVCV
REVAPDGPLQ ESSTRLSLTS DPEEGDPLAL GPESPGEPQP PQLKKDDVTS STGPHKELSS
TEAGSTVAGA ALRPSHHSQR SSLSGDEEDE LFKGATLKAL RPKAQPEEED EDEVSMKGRP
PPTPLFGDDD DDDDIDWLG
//
ID FKB15_HUMAN Reviewed; 1219 AA.
AC Q5T1M5; Q05DK8; Q5T1M2; Q6DD85; Q9Y4D0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-SEP-2007, sequence version 2.
DT 22-JAN-2014, entry version 86.
DE RecName: Full=FK506-binding protein 15;
DE Short=FKBP-15;
DE AltName: Full=133 kDa FK506-binding protein;
DE Short=133 kDa FKBP;
DE Short=FKBP-133;
DE AltName: Full=WASP and FKBP-like;
DE Short=WAFL;
GN Name=FKBP15; Synonyms=KIAA0674;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP GLN-413.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 548-1219 (ISOFORM 2), AND VARIANT
RP GLN-413.
RC TISSUE=Eye, and Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-956, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1161 AND SER-1162, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346; SER-356; SER-939;
RP SER-940; SER-941; SER-956; SER-979; SER-1114 AND SER-1164, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ACTIN AND WIP.
RX PubMed=19121306; DOI=10.1016/j.yexcr.2008.12.004;
RA Viklund I.-M., Aspenstroem P., Meas-Yedid V., Zhang B., Kopec J.,
RA Agren D., Schneider G., D'Amato M., Olivo-Marin J.-C., Sansonetti P.,
RA Van Nhieu G.T., Pettersson S.;
RT "WAFL, a new protein involved in regulation of early endocytic
RT transport at the intersection of actin and microtubule dynamics.";
RL Exp. Cell Res. 315:1040-1052(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-356; SER-1114;
RP SER-1164; SER-1195 AND THR-1203, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-14; SER-956; SER-1114 AND SER-1164, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1164, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be involved in the cytoskeletal organization of
CC neuronal growth cones. Seems to be inactive as a PPIase (By
CC similarity). Involved in the transport of early endosomes at the
CC level of transition between microfilament-based and microtubule-
CC based movement.
CC -!- SUBUNIT: Interacts with WIP and actin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell projection,
CC axon (By similarity). Early endosome. Note=Present in axons and
CC neuronal growth cones (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5T1M5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T1M5-2; Sequence=VSP_027758;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q5T1M5-3; Sequence=VSP_027756, VSP_027757;
CC -!- DOMAIN: The PPIase FKBP-type domain seems to be inactive both for
CC FK506-binding and enzymatic activity (By similarity).
CC -!- DOMAIN: The central coiled-coil region is responsible for
CC association with early endosomes.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09609.1; Type=Erroneous initiation;
CC Sequence=BAA31649.1; Type=Erroneous initiation;
CC Sequence=CAI10963.1; Type=Erroneous initiation;
CC Sequence=CAI10964.1; Type=Erroneous initiation;
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DR EMBL; AB014574; BAA31649.1; ALT_INIT; mRNA.
DR EMBL; AL449305; CAI10963.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL449305; CAI10964.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL449105; CAI10964.1; JOINED; Genomic_DNA.
DR EMBL; AL449105; CAI95402.1; -; Genomic_DNA.
DR EMBL; AL449305; CAI95402.1; JOINED; Genomic_DNA.
DR EMBL; BC009609; AAH09609.1; ALT_INIT; mRNA.
DR EMBL; BC077732; AAH77732.1; -; mRNA.
DR PIR; T00363; T00363.
DR RefSeq; NP_056073.1; NM_015258.1.
DR UniGene; Hs.522351; -.
DR ProteinModelPortal; Q5T1M5; -.
DR SMR; Q5T1M5; 184-286.
DR IntAct; Q5T1M5; 2.
DR STRING; 9606.ENSP00000238256; -.
DR PhosphoSite; Q5T1M5; -.
DR DMDM; 158563913; -.
DR PaxDb; Q5T1M5; -.
DR PRIDE; Q5T1M5; -.
DR DNASU; 23307; -.
DR Ensembl; ENST00000238256; ENSP00000238256; ENSG00000119321.
DR GeneID; 23307; -.
DR KEGG; hsa:23307; -.
DR UCSC; uc004bgs.2; human.
DR CTD; 23307; -.
DR GeneCards; GC09M115923; -.
DR H-InvDB; HIX0008300; -.
DR H-InvDB; HIX0153287; -.
DR HGNC; HGNC:23397; FKBP15.
DR HPA; HPA007979; -.
DR neXtProt; NX_Q5T1M5; -.
DR PharmGKB; PA162388608; -.
DR eggNOG; COG0545; -.
DR HOGENOM; HOG000112601; -.
DR HOVERGEN; HBG067251; -.
DR InParanoid; Q5T1M5; -.
DR KO; K17478; -.
DR OrthoDB; EOG75XGKG; -.
DR ChiTaRS; FKBP15; human.
DR GenomeRNAi; 23307; -.
DR NextBio; 45162; -.
DR PRO; PR:Q5T1M5; -.
DR ArrayExpress; Q5T1M5; -.
DR Bgee; Q5T1M5; -.
DR CleanEx; HS_FKBP15; -.
DR Genevestigator; Q5T1M5; -.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell projection;
KW Coiled coil; Complete proteome; Cytoplasm; Endocytosis; Endosome;
KW Phosphoprotein; Polymorphism; Reference proteome; Transport.
FT CHAIN 1 1219 FK506-binding protein 15.
FT /FTId=PRO_0000299556.
FT DOMAIN 197 290 PPIase FKBP-type.
FT REGION 72 169 Important for function in growth cone
FT organization (By similarity).
FT COILED 522 789 Potential.
FT COILED 818 878 Potential.
FT COILED 925 951 Potential.
FT COMPBIAS 1208 1216 Poly-Asp.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 92 92 N6-acetyllysine.
FT MOD_RES 326 326 Phosphoserine.
FT MOD_RES 346 346 Phosphoserine.
FT MOD_RES 356 356 Phosphoserine.
FT MOD_RES 939 939 Phosphoserine.
FT MOD_RES 940 940 Phosphoserine.
FT MOD_RES 941 941 Phosphoserine.
FT MOD_RES 956 956 Phosphoserine.
FT MOD_RES 979 979 Phosphoserine.
FT MOD_RES 1097 1097 Phosphoserine (By similarity).
FT MOD_RES 1099 1099 Phosphothreonine (By similarity).
FT MOD_RES 1114 1114 Phosphoserine.
FT MOD_RES 1161 1161 Phosphoserine.
FT MOD_RES 1162 1162 Phosphoserine.
FT MOD_RES 1164 1164 Phosphoserine.
FT MOD_RES 1195 1195 Phosphoserine.
FT MOD_RES 1203 1203 Phosphothreonine.
FT VAR_SEQ 462 472 PYAGMQAYAYP -> VTFYNRINYIL (in isoform
FT 3).
FT /FTId=VSP_027756.
FT VAR_SEQ 473 1219 Missing (in isoform 3).
FT /FTId=VSP_027757.
FT VAR_SEQ 629 638 Missing (in isoform 2).
FT /FTId=VSP_027758.
FT VARIANT 106 106 A -> T (in dbSNP:rs1133618).
FT /FTId=VAR_034851.
FT VARIANT 413 413 H -> Q (in dbSNP:rs10435864).
FT /FTId=VAR_034852.
FT VARIANT 434 434 L -> F (in dbSNP:rs10465129).
FT /FTId=VAR_034853.
FT VARIANT 847 847 A -> S (in dbSNP:rs1128116).
FT /FTId=VAR_061543.
FT VARIANT 993 993 P -> T (in dbSNP:rs57348436).
FT /FTId=VAR_061544.
SQ SEQUENCE 1219 AA; 133630 MW; 86563D82B540B51D CRC64;
MFGAGDEDDT DFLSPSGGAR LASLFGLDQA AAGHGNEFFQ YTAPKQPKKG QGTAATGNQA
TPKTAPATMS TPTILVATAV HAYRYTNGQY VKQGKFGAAV LGNHTAREYR ILLYISQQQP
VTVARIHVNF ELMVRPNNYS TFYDDQRQNW SIMFESEKAA VEFNKQVCIA KCNSTSSLDA
VLSQDLIVAD GPAVEVGDSL EVAYTGWLFQ NHVLGQVFDS TANKDKLLRL KLGSGKVIKG
WEDGMLGMKK GGKRLLIVPP ACAVGSEGVI GWTQATDSIL VFEVEVRRVK FARDSGSDGH
SVSSRDSAAP SPIPGADNLS ADPVVSPPTS IPFKSGEPAL RTKSNSLSEQ LAINTSPDAV
KAKLISRMAK MGQPMLPILP PQLDSNDSEI EDVNTLQGGG QPVVTPSVQP SLHPAHPALP
QMTSQAPQPS VTGLQAPSAA LMQVSSLDSH SAVSGNAQSF QPYAGMQAYA YPQASAVTSQ
LQPVRPLYPA PLSQPPHFQG SGDMASFLMT EARQHNTEIR MAVSKVADKM DHLMTKVEEL
QKHSAGNSML IPSMSVTMET SMIMSNIQRI IQENERLKQE ILEKSNRIEE QNDKISELIE
RNQRYVEQSN LMMEKRNNSL QTATENTQAR VLHAEQEKAK VTEELAAATA QVSHLQLKMT
AHQKKETELQ MQLTESLKET DLLRGQLTKV QAKLSELQET SEQAQSKFKS EKQNRKQLEL
KVTSLEEELT DLRVEKESLE KNLSERKKKS AQERSQAEEE IDEIRKSYQE ELDKLRQLLK
KTRVSTDQAA AEQLSLVQAE LQTQWEAKCE HLLASAKDEH LQQYQEVCAQ RDAYQQKLVQ
LQEKCLALQA QITALTKQNE QHIKELEKNK SQMSGVEAAA SDPSEKVKKI MNQVFQSLRR
EFELEESYNG RTILGTIMNT IKMVTLQLLN QQEQEKEESS SEEEEEKAEE RPRRPSQEQS
ASASSGQPQA PLNRERPESP MVPSEQVVEE AVPLPPQALT TSQDGHRRKG DSEAEALSEI
KDGSLPPELS CIPSHRVLGP PTSIPPEPLG PVSMDSECEE SLAASPMAAK PDNPSGKVCV
REVAPDGPLQ ESSTRLSLTS DPEEGDPLAL GPESPGEPQP PQLKKDDVTS STGPHKELSS
TEAGSTVAGA ALRPSHHSQR SSLSGDEEDE LFKGATLKAL RPKAQPEEED EDEVSMKGRP
PPTPLFGDDD DDDDIDWLG
//