Ser13

Site Information
VWDHIEVsDDEDETH SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 450034

In vivo Characterization
Methods used to characterize site in vivo:	immunoprecipitation ( 1 , 6 ) , mass spectrometry ( 1 , 2 , 7 , 9 , 10 , 13 , 14 , 15 , 16 , 17 , 18 , 20 , 21 , 22 , 23 , 24 , 25 , 26 ) , mutation of modification site ( 1 , 6 ) , phospho-antibody ( 1 , 5 , 7 , 11 , 12 , 28 ) , western blotting ( 1 , 6 , 7 , 11 , 12 , 28 )
Disease tissue studied:	brain cancer ( 7 ) , glioblastoma ( 7 ) , glioma ( 7 ) , breast cancer ( 5 , 6 , 9 , 14 , 17 ) , breast ductal carcinoma ( 14 ) , breast cancer, triple negative ( 14 ) , cervical cancer ( 24 , 28 ) , cervical adenocarcinoma ( 24 ) , cervical squamous cell carcinoma ( 28 ) , colorectal cancer ( 5 ) , colorectal carcinoma ( 5 ) , kidney cancer ( 1 ) , leukemia ( 20 ) , acute myelogenous leukemia ( 20 ) , lung cancer ( 17 ) , non-small cell lung cancer ( 17 ) , lymphoma ( 11 ) , B cell lymphoma ( 11 ) , non-Hodgkin's lymphoma ( 11 ) , follicular lymphoma ( 11 )
Relevant cell line - cell type - tissue:	'muscle, skeletal' ( 21 ) , 293 (epithelial) ( 1 , 25 ) , 786-O (renal) [VHL (human), transfection] ( 10 ) , 786-O (renal) ( 1 , 10 ) , A498 (renal) ( 1 , 23 ) , A549 (pulmonary) ( 15 ) , breast ( 14 ) , BT-20 (breast cell) ( 17 ) , BT-474 (breast cell) ( 5 , 9 ) , BT-549 (breast cell) ( 17 ) , Caki-1 (renal) ( 1 ) , Calu 6 (pulmonary) ( 17 ) , COS (fibroblast) ( 28 ) , E.coli (bacterial) ( 1 ) , Flp-In T-Rex-293 (epithelial) [PRKD1 (human), genetic knockin] ( 18 ) , Flp-In T-Rex-293 (epithelial) ( 18 ) , glial-brain ( 7 ) , H2009 (pulmonary) ( 17 ) , H2077 (pulmonary) ( 17 ) , H2887 (pulmonary) ( 17 ) , H322M (pulmonary) ( 17 ) , HCC1359 (pulmonary) ( 17 ) , HCC1937 (breast cell) ( 17 ) , HCC2279 (pulmonary) ( 17 ) , HCC366 (pulmonary) ( 17 ) , HCC4006 (pulmonary) ( 17 ) , HCC78 (pulmonary) ( 17 ) , HCT116 (intestinal) ( 5 ) , HeLa (cervical) ( 2 , 13 ) , HeLa S3 (cervical) ( 24 ) , HOP62 (pulmonary) ( 17 ) , HUES-9 ('stem, embryonic') ( 22 ) , Jurkat (T lymphocyte) ( 16 ) , KB (squamous) ( 28 ) , KG-1 (myeloid) ( 20 ) , LOU-NH91 (squamous) ( 17 ) , MCF-7 (breast cell) ( 6 , 9 , 17 ) , MDA-MB-231 (breast cell) ( 17 ) , MDA-MB-468 (breast cell) ( 17 ) , NCI-H1395 (pulmonary) ( 17 ) , NCI-H1648 (pulmonary) ( 17 ) , NCI-H2030 (pulmonary) ( 17 ) , NCI-H2172 (pulmonary) ( 17 ) , NCI-H322 (pulmonary) ( 17 ) , NCI-H460 (pulmonary) ( 17 ) , OCI-ly1 (B lymphocyte) ( 11 ) , OCI-ly10 (B lymphocyte) ( 11 ) , OCI-ly3 (B lymphocyte) ( 11 ) , SUM149 (breast cell) ( 5 ) , WM115 (melanocyte) ( 26 )

Upstream Regulation
Putative in vivo kinases:	CK2A2 (human) ( 28 )
Kinases, in vitro:	CK2A1 (human) ( 29 )
Phosphatases, in vitro:	PPP5C (human) ( 1 )
Treatments:	anisomycin ( 28 ) , IGF-1 ( 28 ) , OSU-03012 ( 7 ) , serum ( 28 ) , sildenafil ( 7 ) , silmitasertib ( 11 ) , tanespimycin ( 8 ) , TBB ( 28 ) , UV ( 28 )

Downstream Regulation
Effects of modification on CDC37:	molecular association, regulation ( 6 , 29 )
Induce interaction with:	HRI (human) ( 29 ) , HSP90A (human) ( 29 )

Disease / Diagnostics Relevance
Relevant diseases:	B cell lymphoma ( 11 ) , lymphoplasmacytic lymphoma ( 11 ) , non-Hodgkin's lymphoma ( 11 ) , follicular lymphoma ( 11 )

References
1	Dushukyan N, et al. (2017) Phosphorylation and Ubiquitination Regulate Protein Phosphatase 5 Activity and Its Prosurvival Role in Kidney Cancer. Cell Rep 21, 1883-1895 29141220 Curated Info
2	Huang H, et al. (2016) Simultaneous Enrichment of Cysteine-containing Peptides and Phosphopeptides Using a Cysteine-specific Phosphonate Adaptable Tag (CysPAT) in Combination with titanium dioxide (TiO2) Chromatography. Mol Cell Proteomics 15, 3282-3296 27281782 Curated Info
3	Mertins P, et al. (2016) Proteogenomics connects somatic mutations to signalling in breast cancer. Nature 534, 55-62 27251275 Curated Info
4	Boeing S, et al. (2016) Multiomic Analysis of the UV-Induced DNA Damage Response. Cell Rep 15, 1597-1610 27184836 Curated Info
5	Booth L, et al. (2016) [Pemetrexed + Sorafenib] lethality is increased by inhibition of ERBB1/2/3-PI3K-NFκB compensatory survival signaling. Oncotarget 7, 23608-32 27015562 Curated Info
6	Keramisanou D, et al. (2016) Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37. Mol Cell 62, 260-71 27105117 Curated Info
7	Booth L, et al. (2016) Multi-kinase inhibitors can associate with heat shock proteins through their NH2-termini by which they suppress chaperone function. Oncotarget 7, 12975-96 26887051 Curated Info
8	Jin J, et al. (2016) Mutational Analysis of Glycogen Synthase Kinase 3β Protein Kinase Together with Kinome-Wide Binding and Stability Studies Suggests Context-Dependent Recognition of Kinases by the Chaperone Heat Shock Protein 90. Mol Cell Biol 36, 1007-18 26755559 Curated Info
9	Carrier M, et al. (2016) Phosphoproteome and Transcriptome of RA-Responsive and RA-Resistant Breast Cancer Cell Lines. PLoS One 11, e0157290 27362937 Curated Info
10	Malec V, Coulson JM, Urbé S, Clague MJ (2015) Combined Analyses of the VHL and Hypoxia Signaling Axes in an Isogenic Pairing of Renal Clear Cell Carcinoma Cells. J Proteome Res 14, 5263-72 26506913 Curated Info
11	Pizzi M, et al. (2015) Protein kinase CK2 is widely expressed in follicular, Burkitt and diffuse large B-cell lymphomas and propels malignant B-cell growth. Oncotarget 6, 6544-52 25788269 Curated Info
12	Smith JR, et al. (2015) Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins. Oncogene 34, 15-26 24292678 Curated Info
13	Sharma K, et al. (2014) Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling. Cell Rep 8, 1583-94 25159151 Curated Info
14	Mertins P, et al. (2014) Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels. Mol Cell Proteomics 13, 1690-704 24719451 Curated Info
15	Kim JY, et al. (2013) Dissection of TBK1 signaling via phosphoproteomics in lung cancer cells. Proc Natl Acad Sci U S A 110, 12414-9 23836654 Curated Info
16	Mertins P, et al. (2013) Integrated proteomic analysis of post-translational modifications by serial enrichment. Nat Methods 10, 634-7 23749302 Curated Info
17	Klammer M, et al. (2012) Phosphosignature predicts dasatinib response in non-small cell lung cancer. Mol Cell Proteomics 11, 651-68 22617229 Curated Info
18	Franz-Wachtel M, et al. (2012) Global detection of protein kinase D-dependent phosphorylation events in nocodazole-treated human cells. Mol Cell Proteomics 11, 160-70 22496350 Curated Info
19	Beli P, et al. (2012) Proteomic Investigations Reveal a Role for RNA Processing Factor THRAP3 in the DNA Damage Response. Mol Cell 46, 212-25 22424773 Curated Info
20	Weber C, Schreiber TB, Daub H (2012) Dual phosphoproteomics and chemical proteomics analysis of erlotinib and gefitinib interference in acute myeloid leukemia cells. J Proteomics 75, 1343-56 22115753 Curated Info
21	Lundby A, et al. (2012) Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat Commun 3, 876 22673903 Curated Info
22	Rigbolt KT, et al. (2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal 4, rs3 21406692 Curated Info
23	Schreiber TB, et al. (2010) An integrated phosphoproteomics work flow reveals extensive network regulation in early lysophosphatidic acid signaling. Mol Cell Proteomics 9, 1047-62 20071362 Curated Info
24	Olsen JV, et al. (2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal 3, ra3 20068231 Curated Info
25	Gauci S, et al. (2009) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem 81, 4493-501 19413330 Curated Info
26	Old WM, et al. (2009) Functional proteomics identifies targets of phosphorylation by B-Raf signaling in melanoma. Mol Cell 34, 115-31 19362540 Curated Info
27	Vaughan CK, et al. (2008) Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37. Mol Cell 31, 886-95 18922470 Curated Info
28	Miyata Y, Nishida E (2008) Evaluating CK2 activity with the antibody specific for the CK2-phosphorylated form of a kinase-targeting cochaperone Cdc37. Mol Cell Biochem 316, 127-34 18566753 Curated Info
29	Shao J, Prince T, Hartson SD, Matts RL (2003) Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. J Biol Chem 278, 38117-20 12930845 Curated Info