ID   FKBPL_HUMAN             Reviewed;         349 AA.
AC   Q9UIM3; A8K5V3; B0UYX8; Q9H5G3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   28-JAN-2026, entry version 181.
DE   RecName: Full=FK506-binding protein-like;
DE   AltName: Full=WAF-1/CIP1 stabilizing protein 39;
DE            Short=WISp39;
GN   Name=FKBPL; Synonyms=DIR1, NG7;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Lung;
RX   PubMed=10521921; DOI=10.2307/3580140;
RA   Robson T., Joiner M.C., Wilson G.D., McCullough W., Price M.E., Logan I.,
RA   Jones H., McKeown S.R., Hirst D.G.;
RT   "A novel human stress response-related gene with a potential role in
RT   induced radioresistance.";
RL   Radiat. Res. 152:451-461(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA   Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-90.
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Ovary;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-203.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-287 AND ARG-291, AND
RP   INTERACTION WITH CDKN1A AND HSP90AB1.
RX   PubMed=15664193; DOI=10.1016/j.molcel.2004.11.049;
RA   Jascur T., Brickner H., Salles-Passador I., Barbier V., El Khissiin A.,
RA   Smith B., Fotedar R., Fotedar A.;
RT   "Regulation of p21(WAF1/CIP1) stability by WISp39, a Hsp90 binding TPR
RT   protein.";
RL   Mol. Cell 17:237-249(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: May be involved in response to X-ray. Regulates p21 protein
CC       stability by binding to Hsp90 and p21. {ECO:0000269|PubMed:15664193}.
CC   -!- SUBUNIT: Forms a ternary complex with CDKN1A/p21 and HSP90AB1/Hsp90.
CC   -!- INTERACTION:
CC       Q9UIM3; Q8WVL7: ANKRD49; NbExp=9; IntAct=EBI-719882, EBI-9381820;
CC       Q9UIM3; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-719882, EBI-739580;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher levels in
CC       testis. {ECO:0000269|PubMed:15664193}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15663.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAG33655.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF139374; AAF67785.1; -; Genomic_DNA.
DR   EMBL; AK027119; BAB15663.1; ALT_FRAME; mRNA.
DR   EMBL; AK291418; BAF84107.1; -; mRNA.
DR   EMBL; U89337; AAF04864.1; -; Genomic_DNA.
DR   EMBL; AL662828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR753803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR925796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03586.1; -; Genomic_DNA.
DR   EMBL; BC004168; AAH04168.1; -; mRNA.
DR   EMBL; BC011966; AAH11966.1; -; mRNA.
DR   EMBL; CR457374; CAG33655.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS4738.1; -.
DR   RefSeq; NP_071393.2; NM_022110.3.
DR   AlphaFoldDB; Q9UIM3; -.
DR   SMR; Q9UIM3; -.
DR   BioGRID; 122007; 31.
DR   CORUM; Q9UIM3; -.
DR   FunCoup; Q9UIM3; 289.
DR   IntAct; Q9UIM3; 70.
DR   STRING; 9606.ENSP00000364298; -.
DR   iPTMnet; Q9UIM3; -.
DR   PhosphoSitePlus; Q9UIM3; -.
DR   BioMuta; FKBPL; -.
DR   DMDM; 74762773; -.
DR   jPOST; Q9UIM3; -.
DR   MassIVE; Q9UIM3; -.
DR   PaxDb; 9606-ENSP00000364298; -.
DR   PeptideAtlas; Q9UIM3; -.
DR   ProteomicsDB; 84550; -.
DR   Pumba; Q9UIM3; -.
DR   Antibodypedia; 28379; 284 antibodies from 29 providers.
DR   DNASU; 63943; -.
DR   Ensembl; ENST00000375156.4; ENSP00000364298.3; ENSG00000204315.5.
DR   Ensembl; ENST00000425378.2; ENSP00000397530.2; ENSG00000230907.2.
DR   Ensembl; ENST00000443350.2; ENSP00000398812.2; ENSG00000223666.2.
DR   Ensembl; ENST00000456854.2; ENSP00000412439.2; ENSG00000224200.2.
DR   GeneID; 63943; -.
DR   KEGG; hsa:63943; -.
DR   MANE-Select; ENST00000375156.4; ENSP00000364298.3; NM_022110.4; NP_071393.2.
DR   UCSC; uc003nzr.4; human.
DR   AGR; HGNC:13949; -.
DR   ClinPGx; PA28167; -.
DR   CTD; 63943; -.
DR   DisGeNET; 63943; -.
DR   GeneCards; FKBPL; -.
DR   HGNC; HGNC:13949; FKBPL.
DR   HPA; ENSG00000204315; Low tissue specificity.
DR   MalaCards; FKBPL; -.
DR   OpenTargets; ENSG00000204315; -.
DR   VEuPathDB; HostDB:ENSG00000204315; -.
DR   eggNOG; KOG1124; Eukaryota.
DR   GeneTree; ENSGT00920000149187; -.
DR   HOGENOM; CLU_013615_13_0_1; -.
DR   InParanoid; Q9UIM3; -.
DR   OMA; WTELTIG; -.
DR   OrthoDB; 433738at2759; -.
DR   PAN-GO; Q9UIM3; 0 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9UIM3; -.
DR   PathwayCommons; Q9UIM3; -.
DR   Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   SignaLink; Q9UIM3; -.
DR   Agora; ENSG00000204315; -.
DR   BioGRID-ORCS; 63943; 138 hits in 1152 CRISPR screens.
DR   ChiTaRS; FKBPL; human.
DR   GeneWiki; FKBPL; -.
DR   GenomeRNAi; 63943; -.
DR   Pharos; Q9UIM3; Tbio.
DR   PRO; PR:Q9UIM3; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9UIM3; protein.
DR   Bgee; ENSG00000204315; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 99 other cell types or tissues.
DR   ExpressionAtlas; Q9UIM3; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:1905553; P:regulation of blood vessel branching; IEA:Ensembl.
DR   GO; GO:0009314; P:response to radiation; NAS:UniProtKB.
DR   FunFam; 1.25.40.10:FF:000251; FK506-binding protein-like isoform X1; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR050754; FKBP4/5/8-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_rpt.
DR   PANTHER; PTHR46512:SF10; FK506-BINDING PROTEIN-LIKE; 1.
DR   PANTHER; PTHR46512; PEPTIDYLPROLYL ISOMERASE; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF13432; TPR_16; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Proteomics identification; Reference proteome; Repeat;
KW   TPR repeat.
FT   CHAIN           1..349
FT                   /note="FK506-binding protein-like"
FT                   /id="PRO_0000289878"
FT   REPEAT          210..243
FT                   /note="TPR 1"
FT   REPEAT          252..285
FT                   /note="TPR 2"
FT   REPEAT          286..319
FT                   /note="TPR 3"
FT   REGION          36..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         3
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         90
FT                   /note="A -> T (in dbSNP:rs28732176)"
FT                   /evidence="ECO:0000269|PubMed:14574404"
FT                   /id="VAR_061546"
FT   MUTAGEN         287
FT                   /note="K->A: Abolishes HSP90AB1 binding; when associated
FT                   with A-291."
FT                   /evidence="ECO:0000269|PubMed:15664193"
FT   MUTAGEN         291
FT                   /note="R->A: Abolishes HSP90AB1 binding; when associated
FT                   with A-287."
FT                   /evidence="ECO:0000269|PubMed:15664193"
FT   CONFLICT        203
FT                   /note="T -> I (in Ref. 7; CAG33655)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   349 AA;  38176 MW;  428EDD70FD9C807C CRC64;
     METPPVNTIG EKDTSQPQQE WEKNLRENLD SVIQIRQQPR DPPTETLELE VSPDPASQIL
     EHTQGAEKLV AELEGDSHKS HGSTSQMPEA LQASDLWYCP DGSFVKKIVI RGHGLDKPKL
     GSCCRVLALG FPFGSGPPEG WTELTMGVGP WREETWGELI EKCLESMCQG EEAELQLPGH
     SGPPVRLTLA SFTQGRDSWE LETSEKEALA REERARGTEL FRAGNPEGAA RCYGRALRLL
     LTLPPPGPPE RTVLHANLAA CQLLLGQPQL AAQSCDRVLE REPGHLKALY RRGVAQAALG
     NLEKATADLK KVLAIDPKNR AAQEELGKVV IQGKNQDAGL AQGLRKMFG
//