CD37L_HUMAN - dbPTM
CD37L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD37L_HUMAN
UniProt AC Q7L3B6
Protein Name Hsp90 co-chaperone Cdc37-like 1
Gene Name CDC37L1
Organism Homo sapiens (Human).
Sequence Length 337
Subcellular Localization Cytoplasm .
Protein Description Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90..
Protein Sequence MEQPWPPPGPWSLPRAEGEAEEESDFDVFPSSPRCPQLPGGGAQMYSHGIELACQKQKEFVKSSVACKWNLAEAQQKLGSLALHNSESLDQEHAKAQTAVSELRQREEEWRQKEEALVQREKMCLWSTDAISKDVFNKSFINQDKRKDTEDEDKSESFMQKYEQKIRHFGMLSRWDDSQRFLSDHPYLVCEETAKYLILWCFHLEAEKKGALMEQIAHQAVVMQFIMEMAKNCNVDPRGCFRLFFQKAKAEEEGYFEAFKNELEAFKSRVRLYSQSQSFQPMTVQNHVPHSGVGSIGLLESLPQNPDYLQYSISTALCSLNSVVHKEDDEPKMMDTV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
24PhosphorylationEGEAEEESDFDVFPS
CCCCCCCCCCCCCCC
47.0229396449
31PhosphorylationSDFDVFPSSPRCPQL
CCCCCCCCCCCCCCC
41.3225159151
32PhosphorylationDFDVFPSSPRCPQLP
CCCCCCCCCCCCCCC
19.3219664994
46PhosphorylationPGGGAQMYSHGIELA
CCCCCHHHHHHHHHH
5.8527642862
62MethylationQKQKEFVKSSVACKW
HHHHHHHHHHHHHHC
42.19-
62UbiquitinationQKQKEFVKSSVACKW
HHHHHHHHHHHHHHC
42.19-
77UbiquitinationNLAEAQQKLGSLALH
CHHHHHHHHHHHHHH
42.6129967540
80PhosphorylationEAQQKLGSLALHNSE
HHHHHHHHHHHHCCC
22.3928857561
86PhosphorylationGSLALHNSESLDQEH
HHHHHHCCCCCCHHH
20.1527050516
88PhosphorylationLALHNSESLDQEHAK
HHHHCCCCCCHHHHH
36.7522617229
95UbiquitinationSLDQEHAKAQTAVSE
CCCHHHHHHHHHHHH
42.8229967540
98PhosphorylationQEHAKAQTAVSELRQ
HHHHHHHHHHHHHHH
33.6117924679
101PhosphorylationAKAQTAVSELRQREE
HHHHHHHHHHHHHHH
28.5717924679
113UbiquitinationREEEWRQKEEALVQR
HHHHHHHHHHHHHHH
49.2829967540
138UbiquitinationISKDVFNKSFINQDK
CCHHHCCHHHCCCCC
34.9729967540
139PhosphorylationSKDVFNKSFINQDKR
CHHHCCHHHCCCCCC
32.2528857561
260UbiquitinationEGYFEAFKNELEAFK
CCHHHHHHHHHHHHH
57.4729967540

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CD37L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD37L_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CD37L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90B_HUMANHSP90AB1physical
21988832
NIBAN_HUMANFAM129Aphysical
22863883
K1468_HUMANKIAA1468physical
22863883
UBAP1_HUMANUBAP1physical
22863883
UBP25_HUMANUSP25physical
22863883
HS90B_HUMANHSP90AB1physical
25036637
HS90A_HUMANHSP90AA1physical
25036637
PPP5_HUMANPPP5Cphysical
25036637
FKBP4_HUMANFKBP4physical
25036637
TOM34_HUMANTOMM34physical
25036637
UBP19_HUMANUSP19physical
25036637
CDC37_HUMANCDC37physical
25036637
RS7_HUMANRPS7physical
25036637
CHIP_HUMANSTUB1physical
25036637
TTC4_HUMANTTC4physical
25036637
CHRD1_HUMANCHORDC1physical
25036637
FKBP5_HUMANFKBP5physical
25036637
RS17_HUMANRPS17physical
25036637
GLMN_HUMANGLMNphysical
25036637
TMOD4_HUMANTMOD4physical
25036637
STIP1_HUMANSTIP1physical
25036637
XPO1_HUMANXPO1physical
25036637
HS90A_HUMANHSP90AA1physical
11413142
STIP1_HUMANSTIP1physical
11413142

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CD37L_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-98 AND SER-101, AND MASSSPECTROMETRY.

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