CD37L_HUMAN
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 03-AUG-2022, entry version 100.
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};
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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; 30.
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 PRIDE; Q7L3B6; -.
DR ProteomicsDB; 68770; -.
DR Antibodypedia; 24046; 206 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 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; 786744at2759; -.
DR PhylomeDB; Q7L3B6; -.
DR TreeFam; TF101059; -.
DR PathwayCommons; Q7L3B6; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q7L3B6; -.
DR BioGRID-ORCS; 55664; 14 hits in 1080 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:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein 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; -; 1.
DR InterPro; IPR004918; Cdc37.
DR InterPro; IPR013874; Cdc37_Hsp90-bd.
DR InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
DR PANTHER; PTHR12800; PTHR12800; 1.
DR Pfam; PF08565; CDC37_M; 1.
DR SMART; SM01070; CDC37_M; 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
