ID CD37L_HUMAN Reviewed; 337 AA. AC Q7L3B6; B1AL70; Q9NWS3; Q9NX16; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 28-JUN-2023, entry version 105. DE RecName: Full=Hsp90 co-chaperone Cdc37-like 1; DE AltName: Full=Hsp90-associating relative of Cdc37; GN Name=CDC37L1; Synonyms=CDC37B, HARC; 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 [LARGE SCALE MRNA]. RC TISSUE=Signet-ring cell carcinoma; 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 [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., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., 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., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., 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., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [5] RP INTERACTION WITH FKBP4; HSP70; HSP90; PPID AND STIP1, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND PHOSPHORYLATION. RX PubMed=11413142; DOI=10.1074/jbc.m103889200; RA Scholz G.M., Cartledge K., Hall N.E.; RT "Identification and characterization of Harc, a novel Hsp90-associating RT relative of Cdc37."; RL J. Biol. Chem. 276:30971-30979(2001). RN [6] RP SELF-ASSOCIATION, AND INTERACTION WITH CDC37 AND HSP90. RX PubMed=15850399; DOI=10.1021/bi047406z; RA Roiniotis J., Masendycz P., Ho S., Scholz G.M.; RT "Domain-mediated dimerization of the Hsp90 cochaperones Harc and Cdc37."; RL Biochemistry 44:6662-6669(2005). RN [7] RP SELF-ASSOCIATION, AND INTERACTION WITH HSP70; HSP90 AND STIP1. RX PubMed=18052042; DOI=10.1021/bi701041p; RA Cartledge K., Elsegood C., Roiniotis J., Hamilton J.A., Scholz G.M.; RT "Importance of the C-terminal domain of harc for binding to hsp70 and hop RT as well as its response to heat shock."; RL Biochemistry 46:15144-15152(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [10] 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). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY RP MASS 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). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Co-chaperone that binds to numerous proteins and promotes CC their interaction with Hsp70 and Hsp90. {ECO:0000250}. CC -!- SUBUNIT: Self-associates. Forms complexes with Hsp70 and Hsp90. CC Interacts with CDC37, FKBP4, PPID and STIP1. CC {ECO:0000269|PubMed:11413142, ECO:0000269|PubMed:15850399, CC ECO:0000269|PubMed:18052042}. CC -!- INTERACTION: CC Q7L3B6; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-2841876, EBI-2837444; CC Q7L3B6; P07900: HSP90AA1; NbExp=2; IntAct=EBI-2841876, EBI-296047; CC Q7L3B6; P08238: HSP90AB1; NbExp=5; IntAct=EBI-2841876, EBI-352572; CC Q7L3B6; Q6PK50: HSP90AB1; NbExp=2; IntAct=EBI-2841876, EBI-9356629; CC Q7L3B6; P31948: STIP1; NbExp=2; IntAct=EBI-2841876, EBI-1054052; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11413142}. CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, placenta CC and skeletal muscle. {ECO:0000269|PubMed:11413142}. CC -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91206.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK000497; BAA91206.1; ALT_SEQ; mRNA. DR EMBL; AK000646; BAA91304.1; -; mRNA. DR EMBL; AL136231; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471071; EAW58782.1; -; Genomic_DNA. DR EMBL; BC014133; AAH14133.1; -; mRNA. DR CCDS; CCDS6454.1; -. DR RefSeq; NP_060383.2; NM_017913.3. DR AlphaFoldDB; Q7L3B6; -. DR SMR; Q7L3B6; -. DR BioGRID; 120796; 31. DR IntAct; Q7L3B6; 26. DR STRING; 9606.ENSP00000371278; -. DR GlyGen; Q7L3B6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q7L3B6; -. DR PhosphoSitePlus; Q7L3B6; -. DR BioMuta; CDC37L1; -. DR DMDM; 182705252; -. DR EPD; Q7L3B6; -. DR jPOST; Q7L3B6; -. DR MassIVE; Q7L3B6; -. DR MaxQB; Q7L3B6; -. DR PaxDb; Q7L3B6; -. DR PeptideAtlas; Q7L3B6; -. DR ProteomicsDB; 68770; -. DR Antibodypedia; 24046; 230 antibodies from 29 providers. DR DNASU; 55664; -. DR Ensembl; ENST00000381854.4; ENSP00000371278.3; ENSG00000106993.12. DR GeneID; 55664; -. DR KEGG; hsa:55664; -. DR MANE-Select; ENST00000381854.4; ENSP00000371278.3; NM_017913.4; NP_060383.2. DR UCSC; uc003zio.4; human. DR AGR; HGNC:17179; -. DR CTD; 55664; -. DR DisGeNET; 55664; -. DR GeneCards; CDC37L1; -. DR HGNC; HGNC:17179; CDC37L1. DR HPA; ENSG00000106993; Tissue enhanced (skeletal). DR MIM; 610346; gene. DR neXtProt; NX_Q7L3B6; -. DR OpenTargets; ENSG00000106993; -. DR PharmGKB; PA134982210; -. DR VEuPathDB; HostDB:ENSG00000106993; -. DR eggNOG; KOG2260; Eukaryota. DR GeneTree; ENSGT00390000013443; -. DR HOGENOM; CLU_046495_1_0_1; -. DR InParanoid; Q7L3B6; -. DR OMA; GKWTKDD; -. DR OrthoDB; 297041at2759; -. DR PhylomeDB; Q7L3B6; -. DR TreeFam; TF101059; -. DR PathwayCommons; Q7L3B6; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR SignaLink; Q7L3B6; -. DR BioGRID-ORCS; 55664; 16 hits in 1158 CRISPR screens. DR ChiTaRS; CDC37L1; human. DR GenomeRNAi; 55664; -. DR Pharos; Q7L3B6; Tbio. DR PRO; PR:Q7L3B6; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q7L3B6; protein. DR Bgee; ENSG00000106993; Expressed in gastrocnemius and 198 other tissues. DR ExpressionAtlas; Q7L3B6; baseline and differential. DR Genevisible; Q7L3B6; HS. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0031089; C:platelet dense granule lumen; TAS:Reactome. DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central. DR GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central. DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central. DR Gene3D; 1.20.58.610; Cdc37, Hsp90 binding domain; 1. DR InterPro; IPR004918; Cdc37. DR InterPro; IPR013874; Cdc37_Hsp90-bd. DR InterPro; IPR038189; Cdc37_Hsp90-bd_sf. DR PANTHER; PTHR12800; CDC37-RELATED; 1. DR PANTHER; PTHR12800:SF2; HSP90 CO-CHAPERONE CDC37-LIKE 1; 1. DR Pfam; PF08565; CDC37_M; 1. DR SMART; SM01070; CDC37_M; 1. DR SUPFAM; SSF101391; Hsp90 co-chaperone CDC37; 1. PE 1: Evidence at protein level; KW Chaperone; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome. FT CHAIN 1..337 FT /note="Hsp90 co-chaperone Cdc37-like 1" FT /id="PRO_0000318521" FT REGION 1..40 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..171 FT /note="Self-association" FT REGION 147..277 FT /note="Self-association and interaction with Hsp90" FT REGION 267..337 FT /note="Interaction with Hsp70" FT REGION 278..337 FT /note="Required for interaction with STIP1" FT COILED 84..122 FT /evidence="ECO:0000255" FT MOD_RES 32 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 88 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VARIANT 291 FT /note="S -> F (in dbSNP:rs7036014)" FT /id="VAR_038755" FT CONFLICT 17 FT /note="E -> G (in Ref. 1; BAA91304)" FT /evidence="ECO:0000305" FT CONFLICT 159 FT /note="M -> V (in Ref. 1; BAA91206)" FT /evidence="ECO:0000305" FT CONFLICT 305 FT /note="N -> S (in Ref. 1; BAA91304)" FT /evidence="ECO:0000305" SQ SEQUENCE 337 AA; 38835 MW; 46ACDDCE5D07B587 CRC64; MEQPWPPPGP WSLPRAEGEA EEESDFDVFP SSPRCPQLPG GGAQMYSHGI ELACQKQKEF VKSSVACKWN LAEAQQKLGS LALHNSESLD QEHAKAQTAV SELRQREEEW RQKEEALVQR EKMCLWSTDA ISKDVFNKSF INQDKRKDTE DEDKSESFMQ KYEQKIRHFG MLSRWDDSQR FLSDHPYLVC EETAKYLILW CFHLEAEKKG ALMEQIAHQA VVMQFIMEMA KNCNVDPRGC FRLFFQKAKA EEEGYFEAFK NELEAFKSRV RLYSQSQSFQ PMTVQNHVPH SGVGSIGLLE SLPQNPDYLQ YSISTALCSL NSVVHKEDDE PKMMDTV //