CTNL1_HUMAN - dbPTM
CTNL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTNL1_HUMAN
UniProt AC Q9UBT7
Protein Name Alpha-catulin
Gene Name CTNNAL1
Organism Homo sapiens (Human).
Sequence Length 734
Subcellular Localization Cytoplasm, cytoskeleton . Cell membrane
Peripheral membrane protein .
Protein Description May modulate the Rho pathway signaling by providing a scaffold for the Lbc Rho guanine nucleotide exchange factor (ARHGEF1)..
Protein Sequence MAASPGPAGVGGAGAVYGSGSSGFALDSGLEIKTRSVEQTLLPLVSQITTLINHKDNTKKSDKTLQAIQRVGQAVNLAVGRFVKVGEAIANENWDLKEEINIACIEAKQAGETIAALTDITNLNHLESDGQITIFTDKTGVIKAARLLLSSVTKVLLLADRVVIKQIITSRNKVLATMERLEKVNSFQEFVQIFSQFGNEMVEFAHLSGDRQNDLKDEKKKAKMAAARAVLEKCTMMLLTASKTCLRHPNCESAHKNKEGVFDRMKVALDKVIEIVTDCKPNGETDISSISIFTGIKEFKMNIEALRENLYFQSKENLSVTLEVILERMEDFTDSAYTSHEHRERILELSTQARMELQQLISVWIQAQSKKTKSIAEELELSILKISHSLNELKKELHSTATQLAADLLKYHADHVVLKALKLTGVEGNLEALAEYACKLSEQKEQLVETCRLLRHISGTEPLEITCIHAEETFQVTGQQIISAAETLTLHPSSKIAKENLDVFCEAWESQISDMSTLLREINDVFEGRRGEKYGYLSLPKPMKNNANLKSLKPDKPDSEEQAKIAKLGLKLGLLTSDADCEIEKWEDQENEIVQYGRNMSSMAYSLYLFTRGEGPLKTSQDLIHQLEVFAAEGLKLTSSVQAFSKQLKDDDKLMLLLEINKLIPLCHQLQTVTKTSLQNKVFLKVDKCITKTRSMMALLVQLLSLCYKLLKKLQMENNGWVSVTNKDTMDSKT
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
4Phosphorylation----MAASPGPAGVG
----CCCCCCCCCCC		22.3523532336
17PhosphorylationVGGAGAVYGSGSSGF
CCCCCCCCCCCCCCC		12.6825867546
19PhosphorylationGAGAVYGSGSSGFAL
CCCCCCCCCCCCCCC		20.1525867546
21PhosphorylationGAVYGSGSSGFALDS
CCCCCCCCCCCCCCC		29.0525867546
22PhosphorylationAVYGSGSSGFALDSG
CCCCCCCCCCCCCCC		41.2625867546
28PhosphorylationSSGFALDSGLEIKTR
CCCCCCCCCCEEEEC		46.2425867546
40PhosphorylationKTRSVEQTLLPLVSQ
EECCHHHHHHHHHHH		19.43-
61PhosphorylationHKDNTKKSDKTLQAI
CCCCCCCCHHHHHHH		45.9917494752
84UbiquitinationLAVGRFVKVGEAIAN
HHHHCHHHHHHHHHC		41.64-
154 (in isoform 3)Ubiquitination-28.8221906983
154 (in isoform 2)Ubiquitination-28.8221906983
154 (in isoform 1)Ubiquitination-28.8221906983
154UbiquitinationLLLSSVTKVLLLADR
HHHHHHHHHHHHHCH		28.822190698
161MethylationKVLLLADRVVIKQII
HHHHHHCHHHHHHHH		20.99-
169PhosphorylationVVIKQIITSRNKVLA
HHHHHHHHCCHHHHH		24.2224719451
170PhosphorylationVIKQIITSRNKVLAT
HHHHHHHCCHHHHHH		24.3724719451
177PhosphorylationSRNKVLATMERLEKV
CCHHHHHHHHHHHHH		18.5324043423
240PhosphorylationKCTMMLLTASKTCLR
HHHHHHHHCCHHHHH		25.56-
242PhosphorylationTMMLLTASKTCLRHP
HHHHHHCCHHHHHCC		24.22-
258UbiquitinationCESAHKNKEGVFDRM
CHHHHCCCCCHHHHH		61.73-
315AcetylationENLYFQSKENLSVTL
HHCHHCCCCCCEEEH		39.5811795023
319PhosphorylationFQSKENLSVTLEVIL
HCCCCCCEEEHHHHH		25.3323403867
321PhosphorylationSKENLSVTLEVILER
CCCCCEEEHHHHHHH		17.5223403867
335PhosphorylationRMEDFTDSAYTSHEH
HHHHCCCCCCCCHHH		21.8121130716
337PhosphorylationEDFTDSAYTSHEHRE
HHCCCCCCCCHHHHH		16.8421130716
338PhosphorylationDFTDSAYTSHEHRER
HCCCCCCCCHHHHHH		24.2721130716
350PhosphorylationRERILELSTQARMEL
HHHHHHHHHHHHHHH		14.7527732954
351PhosphorylationERILELSTQARMELQ
HHHHHHHHHHHHHHH		38.5827732954
372PhosphorylationIQAQSKKTKSIAEEL
HHHCCCCCHHHHHHH		33.4923898821
373UbiquitinationQAQSKKTKSIAEELE
HHCCCCCHHHHHHHH		49.06-
374PhosphorylationAQSKKTKSIAEELEL
HCCCCCHHHHHHHHH		32.0619664994
382PhosphorylationIAEELELSILKISHS
HHHHHHHHHHHHHHH		19.2524719451
394UbiquitinationSHSLNELKKELHSTA
HHHHHHHHHHHHHHH		37.71-
402PhosphorylationKELHSTATQLAADLL
HHHHHHHHHHHHHHH		24.9722210691
419UbiquitinationHADHVVLKALKLTGV
HHHHHHHHHHHHHCC		39.81-
436PhosphorylationNLEALAEYACKLSEQ
CHHHHHHHHHHHHHH		16.2222817900
439UbiquitinationALAEYACKLSEQKEQ
HHHHHHHHHHHHHHH		47.04-
444UbiquitinationACKLSEQKEQLVETC
HHHHHHHHHHHHHHH		43.29-
534PhosphorylationEGRRGEKYGYLSLPK
CCCCCCCCCCCCCCC		13.5021945579
536PhosphorylationRRGEKYGYLSLPKPM
CCCCCCCCCCCCCCC		7.0521945579
538PhosphorylationGEKYGYLSLPKPMKN
CCCCCCCCCCCCCCC		33.8619664994
605PhosphorylationRNMSSMAYSLYLFTR
CHHHHHHHHHHHHHC		7.2022210691
606PhosphorylationNMSSMAYSLYLFTRG
HHHHHHHHHHHHHCC		10.8622210691
608PhosphorylationSSMAYSLYLFTRGEG
HHHHHHHHHHHCCCC		8.2022210691
640PhosphorylationEGLKLTSSVQAFSKQ
HCCCCHHHHHHHHHH		17.02-
672PhosphorylationPLCHQLQTVTKTSLQ
HHHHHCCCCCHHHHC		38.4429978859
674PhosphorylationCHQLQTVTKTSLQNK
HHHCCCCCHHHHCCC		31.8029978859
676PhosphorylationQLQTVTKTSLQNKVF
HCCCCCHHHHCCCCE		25.8829978859
677PhosphorylationLQTVTKTSLQNKVFL
CCCCCHHHHCCCCEE		29.5229978859
681UbiquitinationTKTSLQNKVFLKVDK
CHHHHCCCCEEEHHH		22.77-
693PhosphorylationVDKCITKTRSMMALL
HHHHHHHHHHHHHHH		21.2321964256
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 CTNL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTNL1_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 CTNL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKP13_HUMANAKAP13physical
12270917
PCGF2_HUMANPCGF2physical
21988832
USH1C_HUMANUSH1Cphysical
25416956
CS057_HUMANC19orf57physical
25416956
RN135_HUMANRNF135physical
25416956
SPERT_HUMANSPERTphysical
25416956
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 CTNL1_HUMAN

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Related Literatures of Post-Translational Modification
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-538, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-534, AND MASSSPECTROMETRY.

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