CMTA1_HUMAN - dbPTM
CMTA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CMTA1_HUMAN
UniProt AC Q9Y6Y1
Protein Name Calmodulin-binding transcription activator 1
Gene Name CAMTA1
Organism Homo sapiens (Human).
Sequence Length 1673
Subcellular Localization Nucleus . Cytoplasm.
Protein Description Transcriptional activator. May act as a tumor suppressor..
Protein Sequence MWRAEGKWLPKTSRKSVSQSVFCGTSTYCVLNTVPPIEDDHGNSNSSHVKIFLPKKLLECLPKCSSLPKERHRWNTNEEIAAYLITFEKHEEWLTTSPKTRPQNGSMILYNRKKVKYRKDGYCWKKRKDGKTTREDHMKLKVQGVECLYGCYVHSSIIPTFHRRCYWLLQNPDIVLVHYLNVPAIEDCGKPCGPILCSINTDKKEWAKWTKEELIGQLKPMFHGIKWTCSNGNSSSGFSVEQLVQQILDSHQTKPQPRTHNCLCTGSLGAGGSVHHKCNSAKHRIISPKVEPRTGGYGSHSEVQHNDVSEGKHEHSHSKGSSREKRNGKVAKPVLLHQSSTEVSSTNQVEVPDTTQSSPVSISSGLNSDPDMVDSPVVTGVSGMAVASVMGSLSQSATVFMSEVTNEAVYTMSPTAGPNHHLLSPDASQGLVLAVSSDGHKFAFPTTGSSESLSMLPTNVSEELVLSTTLDGGRKIPETTMNFDPDCFLNNPKQGQTYGGGGLKAEMVSSNIRHSPPGERSFSFTTVLTKEIKTEDTSFEQQMAKEAYSSSAAAVAASSLTLTAGSSLLPSGGGLSPSTTLEQMDFSAIDSNKDYTSSFSQTGHSPHIHQTPSPSFFLQDASKPLPVEQNTHSSLSDSGGTFVMPTVKTEASSQTSSCSGHVETRIESTSSLHLMQFQANFQAMTAEGEVTMETSQAAEGSEVLLKSGELQACSSEHYLQPETNGVIRSAGGVPILPGNVVQGLYPVAQPSLGNASNMELSLDHFDISFSNQFSDLINDFISVEGGSSTIYGHQLVSGDSTALSQSEDGARAPFTQAEMCLPCCSPQQGSLQLSSSEGGASTMAYMHVAEVVSAASAQGTLGMLQQSGRVFMVTDYSPEWSYPEGGVKVLITGPWQEASNNYSCLFDQISVPASLIQPGVLRCYCPAHDTGLVTLQVAFNNQIISNSVVFEYKARALPTLPSSQHDWLSLDDNQFRMSILERLEQMERRMAEMTGSQQHKQASGGGSSGGGSGSGNGGSQAQCASGTGALGSCFESRVVVVCEKMMSRACWAKSKHLIHSKTFRGMTLLHLAAAQGYATLIQTLIKWRTKHADSIDLELEVDPLNVDHFSCTPLMWACALGHLEAAVVLYKWDRRAISIPDSLGRLPLGIARSRGHVKLAECLEHLQRDEQAQLGQNPRIHCPASEEPSTESWMAQWHSEAISSPEIPKGVTVIASTNPELRRPRSEPSNYYSSESHKDYPAPKKHKLNPEYFQTRQEKLLPTALSLEEPNIRKQSPSSKQSVPETLSPSEGVRDFSRELSPPTPETAAFQASGSQPVGKWNSKDLYIGVSTVQVTGNPKGTSVGKEAAPSQVRPREPMSVLMMANREVVNTELGSYRDSAENEECGQPMDDIQVNMMTLAEHIIEATPDRIKQENFVPMESSGLERTDPATISSTMSWLASYLADADCLPSAAQIRSAYNEPLTPSSNTSLSPVGSPVSEIAFEKPNLPSAADWSEFLSASTSEKVENEFAQLTLSDHEQRELYEAARLVQTAFRKYKGRPLREQQEVAAAVIQRCYRKYKQYALYKKMTQAAILIQSKFRSYYEQKKFQQSRRAAVLIQKYYRSYKKCGKRRQARRTAVIVQQKLRSSLLTKKQDQAARKIMRFLRRCRHSPLVDHRLYKRSERIEKGQGT
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
7Ubiquitination-MWRAEGKWLPKTSR
-CCCCCCCCCCCCCC		36.74-
20UbiquitinationSRKSVSQSVFCGTST
CCCCCCCCEECCCCC		15.0623000965
25UbiquitinationSQSVFCGTSTYCVLN
CCCEECCCCCEEEEE		21.0523000965
26UbiquitinationQSVFCGTSTYCVLNT
CCEECCCCCEEEEEC		11.5823000965
27PhosphorylationSVFCGTSTYCVLNTV
CEECCCCCEEEEECC		22.3025332170
33PhosphorylationSTYCVLNTVPPIEDD
CCEEEEECCCCCCCC		30.1725332170
46UbiquitinationDDHGNSNSSHVKIFL
CCCCCCCCCCEEEEC		22.9523000965
50UbiquitinationNSNSSHVKIFLPKKL
CCCCCCEEEECCHHH		23.4723000965
51UbiquitinationSNSSHVKIFLPKKLL
CCCCCEEEECCHHHH		4.1123000965
52UbiquitinationNSSHVKIFLPKKLLE
CCCCEEEECCHHHHH		8.7223000965
55UbiquitinationHVKIFLPKKLLECLP
CEEEECCHHHHHHHH		59.1923000965
56UbiquitinationVKIFLPKKLLECLPK
EEEECCHHHHHHHHH		57.2623000965
100PhosphorylationWLTTSPKTRPQNGSM
HHCCCCCCCCCCCCE		51.4729978859
106PhosphorylationKTRPQNGSMILYNRK
CCCCCCCCEEEEECC		15.3629978859
110PhosphorylationQNGSMILYNRKKVKY
CCCCEEEEECCEEEE		11.2929978859
117PhosphorylationYNRKKVKYRKDGYCW
EECCEEEECCCCCCE		26.3618083107
152PhosphorylationVECLYGCYVHSSIIP
EECCHHCEECCHHHH		9.2418083107
287PhosphorylationSAKHRIISPKVEPRT
CCCCCEECCCCCCCC		19.1224719451
622PhosphorylationSFFLQDASKPLPVEQ
CCCCCCCCCCCCCCC		42.9924719451
653PhosphorylationTVKTEASSQTSSCSG
EEEECCCCCCCCCCC		44.52-
656PhosphorylationTEASSQTSSCSGHVE
ECCCCCCCCCCCCEE		23.01-
665DimethylationCSGHVETRIESTSSL
CCCCEEEEEECCCEE		19.71-
1025PhosphorylationGSQAQCASGTGALGS
CCCCCCCCCCCCCHH		44.5122210691
1032PhosphorylationSGTGALGSCFESRVV
CCCCCCHHHHCCCCC		19.24-
1036PhosphorylationALGSCFESRVVVVCE
CCHHHHCCCCCEEEH		15.3222210691
1060PhosphorylationKSKHLIHSKTFRGMT
HCCCCCCCCCCCHHH		26.79-
1138PhosphorylationKWDRRAISIPDSLGR
HCCCCCCCCCCCCCC		27.3824702127
1142PhosphorylationRAISIPDSLGRLPLG
CCCCCCCCCCCCCCC		27.63-
1216PhosphorylationKGVTVIASTNPELRR
CCCEEEECCCHHHCC		20.0017081983
1247AcetylationYPAPKKHKLNPEYFQ
CCCCCCCCCCHHHHH		59.8620167786
1252PhosphorylationKHKLNPEYFQTRQEK
CCCCCHHHHHHHHHH		11.4021712546
1255PhosphorylationLNPEYFQTRQEKLLP
CCHHHHHHHHHHHHC		25.1521712546
1282PhosphorylationQSPSSKQSVPETLSP
CCCCCCCCCCCCCCC		43.2926657352
1286PhosphorylationSKQSVPETLSPSEGV
CCCCCCCCCCCCCCH		26.8526471730
1288PhosphorylationQSVPETLSPSEGVRD
CCCCCCCCCCCCHHH		33.5226657352
1323PhosphorylationQPVGKWNSKDLYIGV
CCCCCCCCCCEEEEE		26.8222210691
1477PhosphorylationTSLSPVGSPVSEIAF
CCCCCCCCCHHHHHC		23.5127135362
1619PhosphorylationKRRQARRTAVIVQQK
CHHHHHHHHHHHHHH		21.52-
1629PhosphorylationIVQQKLRSSLLTKKQ
HHHHHHHHHHCCHHH		35.46-
1630PhosphorylationVQQKLRSSLLTKKQD
HHHHHHHHHCCHHHH		22.4424719451
1633PhosphorylationKLRSSLLTKKQDQAA
HHHHHHCCHHHHHHH		41.30-
1635UbiquitinationRSSLLTKKQDQAARK
HHHHCCHHHHHHHHH		54.60-
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 CMTA1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CMTA1_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 CMTA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CMTA1_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614756Cerebellar ataxia, non-progressive, with mental retardation (CANPMR)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CMTA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, AND MASSSPECTROMETRY.

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