CTBL1_HUMAN - dbPTM
CTBL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTBL1_HUMAN
UniProt AC Q8WYA6
Protein Name Beta-catenin-like protein 1
Gene Name CTNNBL1
Organism Homo sapiens (Human).
Sequence Length 563
Subcellular Localization Isoform 1: Nucleus.
Isoform 2: Cytoplasm .
Protein Description Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. Participates in AID/AICDA-mediated Ig class switching recombination (CSR). May induce apoptosis..
Protein Sequence MDVGELLSYQPNRGTKRPRDDEEEEQKMRRKQTGTRERGRYREEEMTVVEEADDDKKRLLQIIDRDGEEEEEEEEPLDESSVKKMILTFEKRSYKNQELRIKFPDNPEKFMESELDLNDIIQEMHVVATMPDLYHLLVELNAVQSLLGLLGHDNTDVSIAVVDLLQELTDIDTLHESEEGAEVLIDALVDGQVVALLVQNLERLDESVKEEADGVHNTLAIVENMAEFRPEMCTEGAQQGLLQWLLKRLKAKMPFDANKLYCSEVLAILLQDNDENRELLGELDGIDVLLQQLSVFKRHNPSTAEEQEMMENLFDSLCSCLMLSSNRERFLKGEGLQLMNLMLREKKISRSSALKVLDHAMIGPEGTDNCHKFVDILGLRTIFPLFMKSPRKIKKVGTTEKEHEEHVCSILASLLRNLRGQQRTRLLNKFTENDSEKVDRLMELHFKYLGAMQVADKKIEGEKHDMVRRGEIIDNDTEEEFYLRRLDAGLFVLQHICYIMAEICNANVPQIRQRVHQILNMRGSSIKIVRHIIKEYAENIGDGRSPEFRENEQKRILGLLENF
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
1Acetylation-------MDVGELLS
-------CCHHHHHC
9.4522223895
8PhosphorylationMDVGELLSYQPNRGT
CCHHHHHCCCCCCCC
34.0529083192
9PhosphorylationDVGELLSYQPNRGTK
CHHHHHCCCCCCCCC
28.1427642862
13MethylationLLSYQPNRGTKRPRD
HHCCCCCCCCCCCCC
61.92-
15PhosphorylationSYQPNRGTKRPRDDE
CCCCCCCCCCCCCCH
22.2029083192
29UbiquitinationEEEEQKMRRKQTGTR
HHHHHHHHHHHHCCC
50.0824816145
47PhosphorylationRYREEEMTVVEEADD
CCCHHHCEEEEECCC
25.3621601212
56UbiquitinationVEEADDDKKRLLQII
EEECCCCHHHHHHHH
46.9524816145
56AcetylationVEEADDDKKRLLQII
EEECCCCHHHHHHHH
46.9524471233
64AcetylationKRLLQIIDRDGEEEE
HHHHHHHCCCCCCHH
44.2219608861
65MethylationRLLQIIDRDGEEEEE
HHHHHHCCCCCCHHH
43.34-
68UbiquitinationQIIDRDGEEEEEEEE
HHHCCCCCCHHHCCC
67.5329967540
75UbiquitinationEEEEEEEEPLDESSV
CCHHHCCCCCCHHHH
55.2129967540
80PhosphorylationEEEPLDESSVKKMIL
CCCCCCHHHHHHHHH
39.8530266825
81PhosphorylationEEPLDESSVKKMILT
CCCCCHHHHHHHHHH
35.5930266825
83AcetylationPLDESSVKKMILTFE
CCCHHHHHHHHHHHC
38.2726051181
88PhosphorylationSVKKMILTFEKRSYK
HHHHHHHHHCCCCCC
20.8730108239
91AcetylationKMILTFEKRSYKNQE
HHHHHHCCCCCCCCE
42.3119608861
91UbiquitinationKMILTFEKRSYKNQE
HHHHHHCCCCCCCCE
42.3119608861
95AcetylationTFEKRSYKNQELRIK
HHCCCCCCCCEEEEE
54.0925953088
95UbiquitinationTFEKRSYKNQELRIK
HHCCCCCCCCEEEEE
54.0929967540
102AcetylationKNQELRIKFPDNPEK
CCCEEEEECCCCHHH
44.3925953088
102UbiquitinationKNQELRIKFPDNPEK
CCCEEEEECCCCHHH
44.3929967540
222UbiquitinationVHNTLAIVENMAEFR
HHHHHHHHHHHHHHC
3.4622505724
225UbiquitinationTLAIVENMAEFRPEM
HHHHHHHHHHHCHHH
2.0929967540
252AcetylationLLKRLKAKMPFDANK
HHHHHHCCCCCCCCH
45.5825953088
252UbiquitinationLLKRLKAKMPFDANK
HHHHHHCCCCCCCCH
45.5829967540
305UbiquitinationRHNPSTAEEQEMMEN
HHCCCHHHHHHHHHH
61.3722505724
305UbiquitinationRHNPSTAEEQEMMEN
HHCCCHHHHHHHHHH
61.37-
319UbiquitinationNLFDSLCSCLMLSSN
HHHHHHHHHHHHCCC
18.6424816145
328UbiquitinationLMLSSNRERFLKGEG
HHHCCCHHHHHCHHH
52.6229967540
328UbiquitinationLMLSSNRERFLKGEG
HHHCCCHHHHHCHHH
52.62-
332UbiquitinationSNRERFLKGEGLQLM
CCHHHHHCHHHHHHH
52.8022505724
345UbiquitinationLMNLMLREKKISRSS
HHHHHHHCCCCCHHH
55.53-
349PhosphorylationMLREKKISRSSALKV
HHHCCCCCHHHHHHH
34.6820068231
351PhosphorylationREKKISRSSALKVLD
HCCCCCHHHHHHHHH
17.1120068231
352PhosphorylationEKKISRSSALKVLDH
CCCCCHHHHHHHHHH
36.1920068231
355UbiquitinationISRSSALKVLDHAMI
CCHHHHHHHHHHHHC
40.2329967540
361UbiquitinationLKVLDHAMIGPEGTD
HHHHHHHHCCCCCCC
3.06-
368UbiquitinationMIGPEGTDNCHKFVD
HCCCCCCCCHHHHHH
67.62-
372AcetylationEGTDNCHKFVDILGL
CCCCCHHHHHHHHCH
49.6525953088
372UbiquitinationEGTDNCHKFVDILGL
CCCCCHHHHHHHHCH
49.65-
388UbiquitinationTIFPLFMKSPRKIKK
HHHHHHHCCCCCCCC
50.39-
389PhosphorylationIFPLFMKSPRKIKKV
HHHHHHCCCCCCCCC
20.3922617229
395UbiquitinationKSPRKIKKVGTTEKE
CCCCCCCCCCCCHHH
49.74-
398PhosphorylationRKIKKVGTTEKEHEE
CCCCCCCCCHHHHHH
34.47-
399PhosphorylationKIKKVGTTEKEHEEH
CCCCCCCCHHHHHHH
38.85-
401AcetylationKKVGTTEKEHEEHVC
CCCCCCHHHHHHHHH
63.3826051181
402UbiquitinationKVGTTEKEHEEHVCS
CCCCCHHHHHHHHHH
50.7524816145
402UbiquitinationKVGTTEKEHEEHVCS
CCCCCHHHHHHHHHH
50.75-
409O-linked_GlycosylationEHEEHVCSILASLLR
HHHHHHHHHHHHHHH
21.3930379171
410UbiquitinationHEEHVCSILASLLRN
HHHHHHHHHHHHHHH
2.93-
429UbiquitinationQRTRLLNKFTENDSE
HHHHHHHHCCCCCHH
54.3424816145
429AcetylationQRTRLLNKFTENDSE
HHHHHHHHCCCCCHH
54.3425953088
430UbiquitinationRTRLLNKFTENDSEK
HHHHHHHCCCCCHHH
11.4433845483
430AcetylationRTRLLNKFTENDSEK
HHHHHHHCCCCCHHH
11.44-
430UbiquitinationRTRLLNKFTENDSEK
HHHHHHHCCCCCHHH
11.44-
431UbiquitinationTRLLNKFTENDSEKV
HHHHHHCCCCCHHHH
35.17-
431O-linked_GlycosylationTRLLNKFTENDSEKV
HHHHHHCCCCCHHHH
35.1730379171
437UbiquitinationFTENDSEKVDRLMEL
CCCCCHHHHHHHHHH
54.08-
457UbiquitinationGAMQVADKKIEGEKH
CHHHHHCCCCCCCCC
46.0133845483
457AcetylationGAMQVADKKIEGEKH
CHHHHHCCCCCCCCC
46.0123236377
458UbiquitinationAMQVADKKIEGEKHD
HHHHHCCCCCCCCCC
46.68-
4632-HydroxyisobutyrylationDKKIEGEKHDMVRRG
CCCCCCCCCCCCCCC
56.62-
463AcetylationDKKIEGEKHDMVRRG
CCCCCCCCCCCCCCC
56.6225953088
469MethylationEKHDMVRRGEIIDND
CCCCCCCCCCCCCCC
35.37-
477PhosphorylationGEIIDNDTEEEFYLR
CCCCCCCCCHHHHHH
52.10-
500UbiquitinationLQHICYIMAEICNAN
HHHHHHHHHHHHCCC
0.81-
500AcetylationLQHICYIMAEICNAN
HHHHHHHHHHHHCCC
0.81-
507UbiquitinationMAEICNANVPQIRQR
HHHHHCCCHHHHHHH
31.8229967540
507AcetylationMAEICNANVPQIRQR
HHHHHCCCHHHHHHH
31.82-
518PhosphorylationIRQRVHQILNMRGSS
HHHHHHHHHHCCCHH
1.4932142685
527UbiquitinationNMRGSSIKIVRHIIK
HCCCHHHHHHHHHHH
36.78-
527AcetylationNMRGSSIKIVRHIIK
HCCCHHHHHHHHHHH
36.7823749302
534UbiquitinationKIVRHIIKEYAENIG
HHHHHHHHHHHHHCC
44.0329967540
534MalonylationKIVRHIIKEYAENIG
HHHHHHHHHHHHHCC
44.0326320211
534AcetylationKIVRHIIKEYAENIG
HHHHHHHHHHHHHCC
44.0323236377
536PhosphorylationVRHIIKEYAENIGDG
HHHHHHHHHHHCCCC
17.7623927012
545PhosphorylationENIGDGRSPEFRENE
HHCCCCCCHHHHHHH
34.0229255136

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 CTBL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTBL1_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 CTBL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC5L_HUMANCDC5Lphysical
21385873
PRP19_HUMANPRPF19physical
21385873
HSP74_HUMANHSPA4physical
21385873
PRP31_HUMANPRPF31physical
21385873
IMA1_HUMANKPNA2physical
21385873
DDX21_HUMANDDX21physical
21385873
PLRG1_HUMANPLRG1physical
21385873
ANM5_HUMANPRMT5physical
21385873
ACTS_HUMANACTA1physical
21385873
NPM_HUMANNPM1physical
21385873
RBM39_HUMANRBM39physical
21385873
STAT1_HUMANSTAT1physical
21385873
MEP50_HUMANWDR77physical
21385873
IMA5_HUMANKPNA1physical
21385873
CWC15_HUMANCWC15physical
20176811
CDC5L_HUMANCDC5Lphysical
20176811
SR140_HUMANU2SURPphysical
22365833
PRPF3_HUMANPRPF3physical
22365833
CWC15_HUMANCWC15physical
22365833
WBP11_HUMANWBP11physical
22365833
SNW1_HUMANSNW1physical
22365833
BUD31_HUMANBUD31physical
22365833
RED_HUMANIKphysical
22365833
PP1R8_HUMANPPP1R8physical
22365833
HNRPK_HUMANHNRNPKphysical
22365833
NSRP1_HUMANNSRP1physical
22365833
ZCH10_HUMANZCCHC10physical
22365833
SRPK2_HUMANSRPK2physical
22365833
LUC7L_HUMANLUC7Lphysical
22365833
ZHANG_HUMANCREBZFphysical
25416956
CATIP_HUMANCATIPphysical
25416956
CTBL1_HUMANCTNNBL1physical
24598747
SPF27_HUMANBCAS2physical
26344197

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 CTBL1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-389, AND MASSSPECTROMETRY.

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