FKB11_HUMAN
ID FKB11_HUMAN Reviewed; 201 AA.
AC Q9NYL4; B4DWB7;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP11;
DE Short=PPIase FKBP11;
DE EC=5.2.1.8;
DE AltName: Full=19 kDa FK506-binding protein;
DE Short=19 kDa FKBP;
DE Short=FKBP-19;
DE AltName: Full=FK506-binding protein 11;
DE Short=FKBP-11;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP11; Synonyms=FKBP19; ORFNames=UNQ336/PRO535;
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 [MRNA] (ISOFORM 1).
RA Rulten S., Kay J.E., Robinson C.;
RT "Identification of novel FKBP genes.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Synovium;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas, and Spleen;
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 [6]
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: PPIases accelerate the folding of proteins during protein
CC synthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBUNIT: Interacts with IFITM5. {ECO:0000250|UniProtKB:Q9D1M7}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NYL4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYL4-2; Sequence=VSP_043037;
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; AF238079; AAF63478.1; -; mRNA.
DR EMBL; AY358998; AAQ89357.1; -; mRNA.
DR EMBL; AK301455; BAG62979.1; -; mRNA.
DR EMBL; AC073610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027973; AAH27973.1; -; mRNA.
DR CCDS; CCDS44871.1; -. [Q9NYL4-2]
DR CCDS; CCDS8773.1; -. [Q9NYL4-1]
DR RefSeq; NP_001137253.1; NM_001143781.1.
DR RefSeq; NP_001137254.1; NM_001143782.1. [Q9NYL4-2]
DR RefSeq; NP_057678.1; NM_016594.2. [Q9NYL4-1]
DR AlphaFoldDB; Q9NYL4; -.
DR SMR; Q9NYL4; -.
DR BioGRID; 119454; 15.
DR IntAct; Q9NYL4; 6.
DR STRING; 9606.ENSP00000449751; -.
DR GlyGen; Q9NYL4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NYL4; -.
DR PhosphoSitePlus; Q9NYL4; -.
DR BioMuta; FKBP11; -.
DR DMDM; 23396601; -.
DR EPD; Q9NYL4; -.
DR jPOST; Q9NYL4; -.
DR MassIVE; Q9NYL4; -.
DR MaxQB; Q9NYL4; -.
DR PaxDb; Q9NYL4; -.
DR PeptideAtlas; Q9NYL4; -.
DR PRIDE; Q9NYL4; -.
DR ProteomicsDB; 83249; -. [Q9NYL4-1]
DR ProteomicsDB; 83250; -. [Q9NYL4-2]
DR Antibodypedia; 25734; 200 antibodies from 24 providers.
DR DNASU; 51303; -.
DR Ensembl; ENST00000453172.2; ENSP00000396874.2; ENSG00000134285.11. [Q9NYL4-2]
DR Ensembl; ENST00000550765.6; ENSP00000449751.1; ENSG00000134285.11. [Q9NYL4-1]
DR GeneID; 51303; -.
DR KEGG; hsa:51303; -.
DR MANE-Select; ENST00000550765.6; ENSP00000449751.1; NM_016594.3; NP_057678.1.
DR UCSC; uc001rsp.4; human. [Q9NYL4-1]
DR CTD; 51303; -.
DR DisGeNET; 51303; -.
DR GeneCards; FKBP11; -.
DR HGNC; HGNC:18624; FKBP11.
DR HPA; ENSG00000134285; Tissue enhanced (pancreas).
DR MIM; 610571; gene.
DR neXtProt; NX_Q9NYL4; -.
DR OpenTargets; ENSG00000134285; -.
DR PharmGKB; PA38607; -.
DR VEuPathDB; HostDB:ENSG00000134285; -.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000159521; -.
DR HOGENOM; CLU_013615_8_2_1; -.
DR InParanoid; Q9NYL4; -.
DR OMA; VFTCGLA; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; Q9NYL4; -.
DR TreeFam; TF105296; -.
DR PathwayCommons; Q9NYL4; -.
DR SignaLink; Q9NYL4; -.
DR BioGRID-ORCS; 51303; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; FKBP11; human.
DR GenomeRNAi; 51303; -.
DR Pharos; Q9NYL4; Tbio.
DR PRO; PR:Q9NYL4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NYL4; protein.
DR Bgee; ENSG00000134285; Expressed in body of pancreas and 171 other tissues.
DR ExpressionAtlas; Q9NYL4; baseline and differential.
DR Genevisible; Q9NYL4; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR044609; FKBP2/11.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR45779; PTHR45779; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isomerase; Membrane; Reference proteome; Rotamase;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..201
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP11"
FT /id="PRO_0000025519"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 57..144
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT VAR_SEQ 130..201
FT /note="ADAVVQYDVELIALIRANYWLKLVKGILPLVGMAMVPALLGLIGYHLYRKAN
FT RPKVSKKKLKEEKRNKSKKK -> GTKDNLMRPPGMTSSSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043037"
SQ SEQUENCE 201 AA; 22180 MW; 586E430B9D2DC0A2 CRC64;
MTLRPSLLPL HLLLLLLLSA AVCRAEAGLE TESPVRTLQV ETLVEPPEPC AEPAAFGDTL
HIHYTGSLVD GRIIDTSLTR DPLVIELGQK QVIPGLEQSL LDMCVGEKRR AIIPSHLAYG
KRGFPPSVPA DAVVQYDVEL IALIRANYWL KLVKGILPLV GMAMVPALLG LIGYHLYRKA
NRPKVSKKKL KEEKRNKSKK K
