CDA7L_HUMAN - dbPTM
CDA7L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDA7L_HUMAN
UniProt AC Q96GN5
Protein Name Cell division cycle-associated 7-like protein
Gene Name CDCA7L
Organism Homo sapiens (Human).
Sequence Length 454
Subcellular Localization Cytoplasm. Nucleus. Associates with chromatin. Translocates from cytoplasm to nucleus under dexamethasone induction.
Protein Description Plays a role in transcriptional regulation as a repressor that inhibits monoamine oxidase A (MAOA) activity and gene expression by binding to the promoter. Plays an important oncogenic role in mediating the full transforming effect of MYC in medulloblastoma cells. Involved in apoptotic signaling pathways; May act downstream of P38-kinase and BCL-2, but upstream of CASP3/caspase-3 as well as CCND1/cyclin D1 and E2F1..
Protein Sequence MELATRYQIPKEVADIFNAPSDDEEFVGFRDDVPMETLSSEESCDSFDSLESGKQQDVRFHSKYFTEELRRIFIEDTDSETEDFAGFTQSDLNGKTNPEVMVVESDLSDDGKASLVSEEEEDEEEDKATPRRSRSRRSSIGLRVAFQFPTKKLANKPDKNSSSEQLFSSARLQNEKKTILERKKDCRQVIQREDSTSESEDDSRDESQESSDALLKRTMNIKENKAMLAQLLAELNSMPDFFPVRTPTSASRKKTVRRAFSEGQITRRMNPTRSARPPEKFALENFTVSAAKFAEEFYSFRRRKTIGGKCREYRRRHRISSFRPVEDITEEDLENVAITVRDKIYDKVLGNTCHQCRQKTIDTKTVCRNQGCCGVRGQFCGPCLRNRYGEDVRSALLDPDWVCPPCRGICNCSYCRKRDGRCATGILIHLAKFYGYDNVKEYLESLQKELVEDN
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
21PhosphorylationADIFNAPSDDEEFVG
HHHHCCCCCCCCCCC		56.1129255136
37PhosphorylationRDDVPMETLSSEESC
CCCCCHHHCCCHHHC		26.2028111955
39PhosphorylationDVPMETLSSEESCDS
CCCHHHCCCHHHCCC		43.0228111955
40PhosphorylationVPMETLSSEESCDSF
CCHHHCCCHHHCCCC		48.7928111955
43PhosphorylationETLSSEESCDSFDSL
HHCCCHHHCCCCHHH		21.1228111955
46PhosphorylationSSEESCDSFDSLESG
CCHHHCCCCHHHHHC		34.9728111955
49PhosphorylationESCDSFDSLESGKQQ
HHCCCCHHHHHCCCC		31.8428111955
52PhosphorylationDSFDSLESGKQQDVR
CCCHHHHHCCCCCCH		57.4928111955
59 (in isoform 5)Phosphorylation-31.6723663014
62PhosphorylationQQDVRFHSKYFTEEL
CCCCHHHHHHHHHHH		26.75-
62 (in isoform 5)Phosphorylation-26.7523663014
63SumoylationQDVRFHSKYFTEELR
CCCHHHHHHHHHHHH		35.49-
63SumoylationQDVRFHSKYFTEELR
CCCHHHHHHHHHHHH		35.49-
63UbiquitinationQDVRFHSKYFTEELR
CCCHHHHHHHHHHHH		35.49-
63AcetylationQDVRFHSKYFTEELR
CCCHHHHHHHHHHHH		35.4925953088
68 (in isoform 5)Phosphorylation-44.5129116813
77PhosphorylationRRIFIEDTDSETEDF
HHHHCCCCCCCCCCC		28.7421955146
79PhosphorylationIFIEDTDSETEDFAG
HHCCCCCCCCCCCCC		48.8121955146
81PhosphorylationIEDTDSETEDFAGFT
CCCCCCCCCCCCCCC		44.8222617229
88PhosphorylationTEDFAGFTQSDLNGK
CCCCCCCCHHHHCCC		26.6729997176
90PhosphorylationDFAGFTQSDLNGKTN
CCCCCCHHHHCCCCC		40.7926074081
96PhosphorylationQSDLNGKTNPEVMVV
HHHHCCCCCCCEEEE		58.3628634120
105PhosphorylationPEVMVVESDLSDDGK
CCEEEEECCCCCCCC		32.0425159151
108PhosphorylationMVVESDLSDDGKASL
EEEECCCCCCCCCCC		38.3525159151
114PhosphorylationLSDDGKASLVSEEEE
CCCCCCCCCCCHHHC		32.5623401153
117PhosphorylationDGKASLVSEEEEDEE
CCCCCCCCHHHCCHH		44.5829255136
129PhosphorylationDEEEDKATPRRSRSR
CHHHHHCCCCHHHHH		24.0630576142
133PhosphorylationDKATPRRSRSRRSSI
HHCCCCHHHHHHHCH		35.5717081983
135PhosphorylationATPRRSRSRRSSIGL
CCCCHHHHHHHCHHH		33.0430576142
138PhosphorylationRRSRSRRSSIGLRVA
CHHHHHHHCHHHHHE		25.7930266825
139PhosphorylationRSRSRRSSIGLRVAF
HHHHHHHCHHHHHEE		20.9023401153
151AcetylationVAFQFPTKKLANKPD
HEEECCCHHHCCCCC		46.1323749302
151SumoylationVAFQFPTKKLANKPD
HEEECCCHHHCCCCC		46.13-
151SumoylationVAFQFPTKKLANKPD
HEEECCCHHHCCCCC		46.13-
152UbiquitinationAFQFPTKKLANKPDK
EEECCCHHHCCCCCC		56.14-
156SumoylationPTKKLANKPDKNSSS
CCHHHCCCCCCCCCH		49.32-
156SumoylationPTKKLANKPDKNSSS
CCHHHCCCCCCCCCH		49.32-
156UbiquitinationPTKKLANKPDKNSSS
CCHHHCCCCCCCCCH		49.32-
156AcetylationPTKKLANKPDKNSSS
CCHHHCCCCCCCCCH		49.3225953088
159SumoylationKLANKPDKNSSSEQL
HHCCCCCCCCCHHHH		68.22-
159SumoylationKLANKPDKNSSSEQL
HHCCCCCCCCCHHHH		68.22-
159UbiquitinationKLANKPDKNSSSEQL
HHCCCCCCCCCHHHH		68.22-
161PhosphorylationANKPDKNSSSEQLFS
CCCCCCCCCHHHHHH		40.7723401153
162PhosphorylationNKPDKNSSSEQLFSS
CCCCCCCCHHHHHHH		47.4925159151
163PhosphorylationKPDKNSSSEQLFSSA
CCCCCCCHHHHHHHH		29.2321406692
168PhosphorylationSSSEQLFSSARLQNE
CCHHHHHHHHHHHHH		31.5121406692
169PhosphorylationSSEQLFSSARLQNEK
CHHHHHHHHHHHHHH		15.2921406692
176UbiquitinationSARLQNEKKTILERK
HHHHHHHHHHHHHHH		63.87-
177SumoylationARLQNEKKTILERKK
HHHHHHHHHHHHHHH		34.32-
177SumoylationARLQNEKKTILERKK
HHHHHHHHHHHHHHH		34.32-
177UbiquitinationARLQNEKKTILERKK
HHHHHHHHHHHHHHH		34.32-
195PhosphorylationQVIQREDSTSESEDD
HHHHHCCCCCCCCCC		29.1320363803
196PhosphorylationVIQREDSTSESEDDS
HHHHCCCCCCCCCCC		49.1620363803
197PhosphorylationIQREDSTSESEDDSR
HHHCCCCCCCCCCCC		42.9720363803
199PhosphorylationREDSTSESEDDSRDE
HCCCCCCCCCCCCCH		46.2020363803
203PhosphorylationTSESEDDSRDESQES
CCCCCCCCCCHHHHH		54.6921406692
207PhosphorylationEDDSRDESQESSDAL
CCCCCCHHHHHHHHH		43.4620860994
210PhosphorylationSRDESQESSDALLKR
CCCHHHHHHHHHHHH		26.3621406692
211PhosphorylationRDESQESSDALLKRT
CCHHHHHHHHHHHHH		26.5921406692
222UbiquitinationLKRTMNIKENKAMLA
HHHHCCHHHHHHHHH		50.67-
222SumoylationLKRTMNIKENKAMLA
HHHHCCHHHHHHHHH		50.6728112733
225SumoylationTMNIKENKAMLAQLL
HCCHHHHHHHHHHHH		35.94-
225SumoylationTMNIKENKAMLAQLL
HCCHHHHHHHHHHHH		35.9428112733
234UbiquitinationMLAQLLAELNSMPDF
HHHHHHHHHHCCCCC		48.7521890473
234UbiquitinationMLAQLLAELNSMPDF
HHHHHHHHHHCCCCC		48.7521890473
237PhosphorylationQLLAELNSMPDFFPV
HHHHHHHCCCCCCCC		44.2927174698
246PhosphorylationPDFFPVRTPTSASRK
CCCCCCCCCCCCCCH		31.0220068231
246UbiquitinationPDFFPVRTPTSASRK
CCCCCCCCCCCCCCH		31.0221890473
248PhosphorylationFFPVRTPTSASRKKT
CCCCCCCCCCCCHHH		35.9920068231
249PhosphorylationFPVRTPTSASRKKTV
CCCCCCCCCCCHHHH		26.0020068231
251PhosphorylationVRTPTSASRKKTVRR
CCCCCCCCCHHHHHH		44.3820068231
261PhosphorylationKTVRRAFSEGQITRR
HHHHHHHHCCCCCCC		39.5723401153
266PhosphorylationAFSEGQITRRMNPTR
HHHCCCCCCCCCCCC		12.3420068231
274PhosphorylationRRMNPTRSARPPEKF
CCCCCCCCCCCCHHH		30.9820860994
279 (in isoform 2)Ubiquitination-64.5921890473
280SumoylationRSARPPEKFALENFT
CCCCCCHHHHHCCCE		41.53-
280UbiquitinationRSARPPEKFALENFT
CCCCCCHHHHHCCCE		41.5321890473
280SumoylationRSARPPEKFALENFT
CCCCCCHHHHHCCCE		41.53-
280UbiquitinationRSARPPEKFALENFT
CCCCCCHHHHHCCCE		41.5321890473
280 (in isoform 1)Ubiquitination-41.5321890473
299PhosphorylationKFAEEFYSFRRRKTI
HHHHHHHHHHHHCCC		20.00-
301UbiquitinationAEEFYSFRRRKTIGG
HHHHHHHHHHCCCCC		31.3921890473
301UbiquitinationAEEFYSFRRRKTIGG
HHHHHHHHHHCCCCC		31.3921890473
313UbiquitinationIGGKCREYRRRHRIS
CCCHHHHHHHHHCCC		7.0621890473
320PhosphorylationYRRRHRISSFRPVED
HHHHHCCCCCCCCCC		24.3130108239
321PhosphorylationRRRHRISSFRPVEDI
HHHHCCCCCCCCCCC		23.9327273156
329PhosphorylationFRPVEDITEEDLENV
CCCCCCCCHHHHHHC		45.7230108239
345PhosphorylationITVRDKIYDKVLGNT
EEEHHHHHHHHHCCC		18.56-
346 (in isoform 2)Ubiquitination-37.7521890473
347SumoylationVRDKIYDKVLGNTCH
EHHHHHHHHHCCCHH		23.53-
347UbiquitinationVRDKIYDKVLGNTCH
EHHHHHHHHHCCCHH		23.5321890473
347SumoylationVRDKIYDKVLGNTCH
EHHHHHHHHHCCCHH		23.53-
347UbiquitinationVRDKIYDKVLGNTCH
EHHHHHHHHHCCCHH		23.5321890473
347 (in isoform 1)Ubiquitination-23.5321890473
359UbiquitinationTCHQCRQKTIDTKTV
CHHHHHHCCCCCHHH		28.26-
360PhosphorylationCHQCRQKTIDTKTVC
HHHHHHCCCCCHHHH		18.7520860994
363PhosphorylationCRQKTIDTKTVCRNQ
HHHCCCCCHHHHCCC		25.4324505115
364SumoylationRQKTIDTKTVCRNQG
HHCCCCCHHHHCCCC		34.90-
364SumoylationRQKTIDTKTVCRNQG
HHCCCCCHHHHCCCC		34.90-
364UbiquitinationRQKTIDTKTVCRNQG
HHCCCCCHHHHCCCC		34.90-
365PhosphorylationQKTIDTKTVCRNQGC
HCCCCCHHHHCCCCC		27.2520860994
393MethylationNRYGEDVRSALLDPD
HCCCHHHHHHHCCCC		28.65-
407MethylationDWVCPPCRGICNCSY
CCCCCCCCCCCCCHH		43.20-
413PhosphorylationCRGICNCSYCRKRDG
CCCCCCCHHHHCCCC		17.1828152594
414PhosphorylationRGICNCSYCRKRDGR
CCCCCCHHHHCCCCC		9.8528152594
424PhosphorylationKRDGRCATGILIHLA
CCCCCCCHHHHHHHH		28.51-
432UbiquitinationGILIHLAKFYGYDNV
HHHHHHHHHHCCHHH		45.54-
439 (in isoform 2)Ubiquitination-4.5621890473
440UbiquitinationFYGYDNVKEYLESLQ
HHCCHHHHHHHHHHH		47.0721906983
440 (in isoform 1)Ubiquitination-47.0721890473
442PhosphorylationGYDNVKEYLESLQKE
CCHHHHHHHHHHHHH		15.2826074081
445PhosphorylationNVKEYLESLQKELVE
HHHHHHHHHHHHHHH		33.2426074081
447 (in isoform 2)Ubiquitination-46.5921890473
448UbiquitinationEYLESLQKELVEDN-
HHHHHHHHHHHHCC-		59.312190698
448 (in isoform 1)Ubiquitination-59.3121890473
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 CDA7L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDA7L_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 CDA7L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VDR_HUMANVDRphysical
21988832
SUV91_HUMANSUV39H1physical
23455924
CDA7L_HUMANCDCA7Lphysical
25416956
ZN821_HUMANZNF821physical
25416956
CTBL1_HUMANCTNNBL1physical
25416956
SAS10_HUMANUTP3physical
25416956
ZN250_HUMANZNF250physical
25416956
PRD14_HUMANPRDM14physical
25416956
CARD9_HUMANCARD9physical
25416956
CCD33_HUMANCCDC33physical
25416956
CEP70_HUMANCEP70physical
25416956
T3JAM_HUMANTRAF3IP3physical
25416956
ING5_HUMANING5physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
DEDD2_HUMANDEDD2physical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
BEND7_HUMANBEND7physical
25416956
MORN3_HUMANMORN3physical
25416956
TRI42_HUMANTRIM42physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
ZGPAT_HUMANZGPATphysical
21516116
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 CDA7L_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-105; SER-108;SER-117; SER-162 AND SER-261, AND MASS SPECTROMETRY.
"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-117 AND SER-261, ANDMASS SPECTROMETRY.
"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-21, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139; SER-162 ANDSER-261, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-77; SER-79; SER-105;SER-108; SER-114 AND SER-117, AND MASS SPECTROMETRY.

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