CDR2L_HUMAN - dbPTM
CDR2L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDR2L_HUMAN
UniProt AC Q86X02
Protein Name Cerebellar degeneration-related protein 2-like
Gene Name CDR2L
Organism Homo sapiens (Human).
Sequence Length 465
Subcellular Localization
Protein Description
Protein Sequence MRRAAGMEDFSAEEEESWYDQQDLEQDLHLAAELGKTLLERNKELEGSLQQMYSTNEEQVQEIEYLTKQLDTLRHVNEQHAKVYEQLDLTARDLELTNHRLVLESKAAQQKIHGLTETIERLQAQVEELQAQVEQLRGLEQLRVLREKRERRRTIHTFPCLKELCTSPRCKDAFRLHSSSLELGPRPLEQENERLQTLVGALRSQVSQERQRKERAEREYTAVLQEYSELERQLCEMEACRLRVQELEAELLELQQMKQAKTYLLGPDDHLAEALLAPLTQAPEADDPQPGRGDDLGAQDGVSSPAASPGHVVRKSCSDTALNAIVAKDPASRHAGNLTLHANSVRKRGMSILREVDEQYHALLEKYEELLSKCRQHGAGVRHAGVQTSRPISRDSSWRDLRGGEEGQGEVKAGEKSLSQHVEAVDKRLEQSQPEYKALFKEIFSRIQKTKADINATKVKTHSSK
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
19PhosphorylationAEEEESWYDQQDLEQ
HHHHHCCCCHHHHHH
17.1027642862
84PhosphorylationNEQHAKVYEQLDLTA
HHHHHHHHHHHCCCH
9.3927642862
106UbiquitinationHRLVLESKAAQQKIH
CHHHHCHHHHHHHHH
38.06-
154PhosphorylationEKRERRRTIHTFPCL
HHHHHHHCCCHHHHH
18.4627273156
157PhosphorylationERRRTIHTFPCLKEL
HHHHCCCHHHHHHHH
25.9730266825
166PhosphorylationPCLKELCTSPRCKDA
HHHHHHCCCCCCCHH
55.1627794612
167PhosphorylationCLKELCTSPRCKDAF
HHHHHCCCCCCCHHH
14.8921815630
178PhosphorylationKDAFRLHSSSLELGP
CHHHHHCCCCCCCCC
26.6430266825
179PhosphorylationDAFRLHSSSLELGPR
HHHHHCCCCCCCCCC
28.3523401153
180PhosphorylationAFRLHSSSLELGPRP
HHHHCCCCCCCCCCC
28.9530266825
303PhosphorylationLGAQDGVSSPAASPG
CCCCCCCCCCCCCCC
35.8130266825
304PhosphorylationGAQDGVSSPAASPGH
CCCCCCCCCCCCCCC
19.0230266825
308PhosphorylationGVSSPAASPGHVVRK
CCCCCCCCCCCEEEC
33.2630266825
316PhosphorylationPGHVVRKSCSDTALN
CCCEEECCCCHHHHH
14.3225159151
318PhosphorylationHVVRKSCSDTALNAI
CEEECCCCHHHHHHH
45.1225159151
320PhosphorylationVRKSCSDTALNAIVA
EECCCCHHHHHHHHC
19.4229978859
339PhosphorylationSRHAGNLTLHANSVR
HCCCCCEEEEHHHHH
22.0924117733
344PhosphorylationNLTLHANSVRKRGMS
CEEEEHHHHHHHCHH
24.8825159151
351PhosphorylationSVRKRGMSILREVDE
HHHHHCHHHHHHHHH
22.6923090842
388PhosphorylationVRHAGVQTSRPISRD
CCCCCCCCCCCCCCC
25.0523403867
389PhosphorylationRHAGVQTSRPISRDS
CCCCCCCCCCCCCCC
20.9723403867
393PhosphorylationVQTSRPISRDSSWRD
CCCCCCCCCCCCCCC
32.4927794612
396PhosphorylationSRPISRDSSWRDLRG
CCCCCCCCCCCCCCC
30.5922964224
397PhosphorylationRPISRDSSWRDLRGG
CCCCCCCCCCCCCCC
30.3522964224
417PhosphorylationEVKAGEKSLSQHVEA
CCCCCCCCHHHHHHH
29.0225159151
419PhosphorylationKAGEKSLSQHVEAVD
CCCCCCHHHHHHHHH
25.9029214152
458AcetylationKADINATKVKTHSSK
HCHHHCCCCCCCCCC
39.057265689

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 CDR2L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDR2L_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 CDR2L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDR2_HUMANCDR2physical
27173435

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 CDR2L_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-179; SER-304AND SER-308, AND MASS SPECTROMETRY.

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