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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MDVGELLS -------CCHHHHHC | 9.45 | 22223895 | |
8 | Phosphorylation | MDVGELLSYQPNRGT CCHHHHHCCCCCCCC | 34.05 | 29083192 | |
9 | Phosphorylation | DVGELLSYQPNRGTK CHHHHHCCCCCCCCC | 28.14 | 27642862 | |
13 | Methylation | LLSYQPNRGTKRPRD HHCCCCCCCCCCCCC | 61.92 | - | |
15 | Phosphorylation | SYQPNRGTKRPRDDE CCCCCCCCCCCCCCH | 22.20 | 29083192 | |
29 | Ubiquitination | EEEEQKMRRKQTGTR HHHHHHHHHHHHCCC | 50.08 | 24816145 | |
47 | Phosphorylation | RYREEEMTVVEEADD CCCHHHCEEEEECCC | 25.36 | 21601212 | |
56 | Ubiquitination | VEEADDDKKRLLQII EEECCCCHHHHHHHH | 46.95 | 24816145 | |
56 | Acetylation | VEEADDDKKRLLQII EEECCCCHHHHHHHH | 46.95 | 24471233 | |
64 | Acetylation | KRLLQIIDRDGEEEE HHHHHHHCCCCCCHH | 44.22 | 19608861 | |
65 | Methylation | RLLQIIDRDGEEEEE HHHHHHCCCCCCHHH | 43.34 | - | |
68 | Ubiquitination | QIIDRDGEEEEEEEE HHHCCCCCCHHHCCC | 67.53 | 29967540 | |
75 | Ubiquitination | EEEEEEEEPLDESSV CCHHHCCCCCCHHHH | 55.21 | 29967540 | |
80 | Phosphorylation | EEEPLDESSVKKMIL CCCCCCHHHHHHHHH | 39.85 | 30266825 | |
81 | Phosphorylation | EEPLDESSVKKMILT CCCCCHHHHHHHHHH | 35.59 | 30266825 | |
83 | Acetylation | PLDESSVKKMILTFE CCCHHHHHHHHHHHC | 38.27 | 26051181 | |
88 | Phosphorylation | SVKKMILTFEKRSYK HHHHHHHHHCCCCCC | 20.87 | 30108239 | |
91 | Acetylation | KMILTFEKRSYKNQE HHHHHHCCCCCCCCE | 42.31 | 19608861 | |
91 | Ubiquitination | KMILTFEKRSYKNQE HHHHHHCCCCCCCCE | 42.31 | 19608861 | |
95 | Acetylation | TFEKRSYKNQELRIK HHCCCCCCCCEEEEE | 54.09 | 25953088 | |
95 | Ubiquitination | TFEKRSYKNQELRIK HHCCCCCCCCEEEEE | 54.09 | 29967540 | |
102 | Acetylation | KNQELRIKFPDNPEK CCCEEEEECCCCHHH | 44.39 | 25953088 | |
102 | Ubiquitination | KNQELRIKFPDNPEK CCCEEEEECCCCHHH | 44.39 | 29967540 | |
222 | Ubiquitination | VHNTLAIVENMAEFR HHHHHHHHHHHHHHC | 3.46 | 22505724 | |
225 | Ubiquitination | TLAIVENMAEFRPEM HHHHHHHHHHHCHHH | 2.09 | 29967540 | |
252 | Acetylation | LLKRLKAKMPFDANK HHHHHHCCCCCCCCH | 45.58 | 25953088 | |
252 | Ubiquitination | LLKRLKAKMPFDANK HHHHHHCCCCCCCCH | 45.58 | 29967540 | |
305 | Ubiquitination | RHNPSTAEEQEMMEN HHCCCHHHHHHHHHH | 61.37 | 22505724 | |
305 | Ubiquitination | RHNPSTAEEQEMMEN HHCCCHHHHHHHHHH | 61.37 | - | |
319 | Ubiquitination | NLFDSLCSCLMLSSN HHHHHHHHHHHHCCC | 18.64 | 24816145 | |
328 | Ubiquitination | LMLSSNRERFLKGEG HHHCCCHHHHHCHHH | 52.62 | 29967540 | |
328 | Ubiquitination | LMLSSNRERFLKGEG HHHCCCHHHHHCHHH | 52.62 | - | |
332 | Ubiquitination | SNRERFLKGEGLQLM CCHHHHHCHHHHHHH | 52.80 | 22505724 | |
345 | Ubiquitination | LMNLMLREKKISRSS HHHHHHHCCCCCHHH | 55.53 | - | |
349 | Phosphorylation | MLREKKISRSSALKV HHHCCCCCHHHHHHH | 34.68 | 20068231 | |
351 | Phosphorylation | REKKISRSSALKVLD HCCCCCHHHHHHHHH | 17.11 | 20068231 | |
352 | Phosphorylation | EKKISRSSALKVLDH CCCCCHHHHHHHHHH | 36.19 | 20068231 | |
355 | Ubiquitination | ISRSSALKVLDHAMI CCHHHHHHHHHHHHC | 40.23 | 29967540 | |
361 | Ubiquitination | LKVLDHAMIGPEGTD HHHHHHHHCCCCCCC | 3.06 | - | |
368 | Ubiquitination | MIGPEGTDNCHKFVD HCCCCCCCCHHHHHH | 67.62 | - | |
372 | Acetylation | EGTDNCHKFVDILGL CCCCCHHHHHHHHCH | 49.65 | 25953088 | |
372 | Ubiquitination | EGTDNCHKFVDILGL CCCCCHHHHHHHHCH | 49.65 | - | |
388 | Ubiquitination | TIFPLFMKSPRKIKK HHHHHHHCCCCCCCC | 50.39 | - | |
389 | Phosphorylation | IFPLFMKSPRKIKKV HHHHHHCCCCCCCCC | 20.39 | 22617229 | |
395 | Ubiquitination | KSPRKIKKVGTTEKE CCCCCCCCCCCCHHH | 49.74 | - | |
398 | Phosphorylation | RKIKKVGTTEKEHEE CCCCCCCCCHHHHHH | 34.47 | - | |
399 | Phosphorylation | KIKKVGTTEKEHEEH CCCCCCCCHHHHHHH | 38.85 | - | |
401 | Acetylation | KKVGTTEKEHEEHVC CCCCCCHHHHHHHHH | 63.38 | 26051181 | |
402 | Ubiquitination | KVGTTEKEHEEHVCS CCCCCHHHHHHHHHH | 50.75 | 24816145 | |
402 | Ubiquitination | KVGTTEKEHEEHVCS CCCCCHHHHHHHHHH | 50.75 | - | |
409 | O-linked_Glycosylation | EHEEHVCSILASLLR HHHHHHHHHHHHHHH | 21.39 | 30379171 | |
410 | Ubiquitination | HEEHVCSILASLLRN HHHHHHHHHHHHHHH | 2.93 | - | |
429 | Ubiquitination | QRTRLLNKFTENDSE HHHHHHHHCCCCCHH | 54.34 | 24816145 | |
429 | Acetylation | QRTRLLNKFTENDSE HHHHHHHHCCCCCHH | 54.34 | 25953088 | |
430 | Ubiquitination | RTRLLNKFTENDSEK HHHHHHHCCCCCHHH | 11.44 | 33845483 | |
430 | Acetylation | RTRLLNKFTENDSEK HHHHHHHCCCCCHHH | 11.44 | - | |
430 | Ubiquitination | RTRLLNKFTENDSEK HHHHHHHCCCCCHHH | 11.44 | - | |
431 | Ubiquitination | TRLLNKFTENDSEKV HHHHHHCCCCCHHHH | 35.17 | - | |
431 | O-linked_Glycosylation | TRLLNKFTENDSEKV HHHHHHCCCCCHHHH | 35.17 | 30379171 | |
437 | Ubiquitination | FTENDSEKVDRLMEL CCCCCHHHHHHHHHH | 54.08 | - | |
457 | Ubiquitination | GAMQVADKKIEGEKH CHHHHHCCCCCCCCC | 46.01 | 33845483 | |
457 | Acetylation | GAMQVADKKIEGEKH CHHHHHCCCCCCCCC | 46.01 | 23236377 | |
458 | Ubiquitination | AMQVADKKIEGEKHD HHHHHCCCCCCCCCC | 46.68 | - | |
463 | 2-Hydroxyisobutyrylation | DKKIEGEKHDMVRRG CCCCCCCCCCCCCCC | 56.62 | - | |
463 | Acetylation | DKKIEGEKHDMVRRG CCCCCCCCCCCCCCC | 56.62 | 25953088 | |
469 | Methylation | EKHDMVRRGEIIDND CCCCCCCCCCCCCCC | 35.37 | - | |
477 | Phosphorylation | GEIIDNDTEEEFYLR CCCCCCCCCHHHHHH | 52.10 | - | |
500 | Ubiquitination | LQHICYIMAEICNAN HHHHHHHHHHHHCCC | 0.81 | - | |
500 | Acetylation | LQHICYIMAEICNAN HHHHHHHHHHHHCCC | 0.81 | - | |
507 | Ubiquitination | MAEICNANVPQIRQR HHHHHCCCHHHHHHH | 31.82 | 29967540 | |
507 | Acetylation | MAEICNANVPQIRQR HHHHHCCCHHHHHHH | 31.82 | - | |
518 | Phosphorylation | IRQRVHQILNMRGSS HHHHHHHHHHCCCHH | 1.49 | 32142685 | |
527 | Ubiquitination | NMRGSSIKIVRHIIK HCCCHHHHHHHHHHH | 36.78 | - | |
527 | Acetylation | NMRGSSIKIVRHIIK HCCCHHHHHHHHHHH | 36.78 | 23749302 | |
534 | Ubiquitination | KIVRHIIKEYAENIG HHHHHHHHHHHHHCC | 44.03 | 29967540 | |
534 | Malonylation | KIVRHIIKEYAENIG HHHHHHHHHHHHHCC | 44.03 | 26320211 | |
534 | Acetylation | KIVRHIIKEYAENIG HHHHHHHHHHHHHCC | 44.03 | 23236377 | |
536 | Phosphorylation | VRHIIKEYAENIGDG HHHHHHHHHHHCCCC | 17.76 | 23927012 | |
545 | Phosphorylation | ENIGDGRSPEFRENE HHCCCCCCHHHHHHH | 34.02 | 29255136 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CTBL1_HUMAN !! |
* 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 !! |
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. |
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Acetylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |