DTL_HUMAN - dbPTM
DTL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DTL_HUMAN
UniProt AC Q9NZJ0
Protein Name Denticleless protein homolog
Gene Name DTL
Organism Homo sapiens (Human).
Sequence Length 730
Subcellular Localization Nucleus. Nucleus membrane
Peripheral membrane protein
Nucleoplasmic side. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome. Nuclear matrix-associated protein. Translocates from the interphase nucleus to the metaphase c
Protein Description Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2. [PubMed: 16861906]
Protein Sequence MLFNSVLRQPQLGVLRNGWSSQYPLQSLLTGYQCSGNDEHTSYGETGVPVPPFGCTFSSAPNMEHVLAVANEEGFVRLYNTESQSFRKKCFKEWMAHWNAVFDLAWVPGELKLVTAAGDQTAKFWDVKAGELIGTCKGHQCSLKSVAFSKFEKAVFCTGGRDGNIMVWDTRCNKKDGFYRQVNQISGAHNTSDKQTPSKPKKKQNSKGLAPSVDFQQSVTVVLFQDENTLVSAGAVDGIIKVWDLRKNYTAYRQEPIASKSFLYPGSSTRKLGYSSLILDSTGSTLFANCTDDNIYMFNMTGLKTSPVAIFNGHQNSTFYVKSSLSPDDQFLVSGSSDEAAYIWKVSTPWQPPTVLLGHSQEVTSVCWCPSDFTKIATCSDDNTLKIWRLNRGLEEKPGGDKLSTVGWASQKKKESRPGLVTVTSSQSTPAKAPRAKCNPSNSSPSSAACAPSCAGDLPLPSNTPTFSIKTSPAKARSPINRRGSVSSVSPKPPSSFKMSIRNWVTRTPSSSPPITPPASETKIMSPRKALIPVSQKSSQAEACSESRNRVKRRLDSSCLESVKQKCVKSCNCVTELDGQVENLHLDLCCLAGNQEDLSKDSLGPTKSSKIEGAGTSISEPPSPISPYASESCGTLPLPLRPCGEGSEMVGKENSSPENKNWLLAMAAKRKAENPSPRSPSSQTPNSRRQSGKKLPSPVTITPSSMRKICTYFHRKSQEDFCGPEHSTEL
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-------MLFNSVLR
-------CCCCHHCC		9.7022223895
79PhosphorylationEEGFVRLYNTESQSF
CCCEEEEEECCCHHH		14.9629496907
81 (in isoform 2)Ubiquitination-24.3721906983
83PhosphorylationVRLYNTESQSFRKKC
EEEEECCCHHHHHHH		29.1420873877
85PhosphorylationLYNTESQSFRKKCFK
EEECCCHHHHHHHHH		35.9820873877
121PhosphorylationVTAAGDQTAKFWDVK
EEECCCCCEEEEEEC		36.2320068231
123UbiquitinationAAGDQTAKFWDVKAG
ECCCCCEEEEEECCC		50.8321906983
123 (in isoform 1)Ubiquitination-50.8321890473
128SumoylationTAKFWDVKAGELIGT
CEEEEEECCCEEEEE		48.47-
128SumoylationTAKFWDVKAGELIGT
CEEEEEECCCEEEEE		48.47-
128UbiquitinationTAKFWDVKAGELIGT
CEEEEEECCCEEEEE		48.47-
137SumoylationGELIGTCKGHQCSLK
CEEEEECCCCCCCCC		60.30-
137SumoylationGELIGTCKGHQCSLK
CEEEEECCCCCCCCC		60.30-
137UbiquitinationGELIGTCKGHQCSLK
CEEEEECCCCCCCCC		60.30-
144UbiquitinationKGHQCSLKSVAFSKF
CCCCCCCCHHCCCCC		26.96-
150UbiquitinationLKSVAFSKFEKAVFC
CCHHCCCCCCEEEEE		51.60-
153UbiquitinationVAFSKFEKAVFCTGG
HCCCCCCEEEEECCC		53.64-
175SumoylationWDTRCNKKDGFYRQV
EECCCCCCCCCHHHH		49.44-
175SumoylationWDTRCNKKDGFYRQV
EECCCCCCCCCHHHH		49.44-
175UbiquitinationWDTRCNKKDGFYRQV
EECCCCCCCCCHHHH		49.44-
179PhosphorylationCNKKDGFYRQVNQIS
CCCCCCCHHHHHHCC		12.9826074081
186PhosphorylationYRQVNQISGAHNTSD
HHHHHHCCCCCCCCC		21.8430576142
191PhosphorylationQISGAHNTSDKQTPS
HCCCCCCCCCCCCCC		28.5625159151
192PhosphorylationISGAHNTSDKQTPSK
CCCCCCCCCCCCCCC		48.4025159151
194UbiquitinationGAHNTSDKQTPSKPK
CCCCCCCCCCCCCCC		56.70-
196PhosphorylationHNTSDKQTPSKPKKK
CCCCCCCCCCCCCCC		34.9623401153
198PhosphorylationTSDKQTPSKPKKKQN
CCCCCCCCCCCCCCC		66.0521955146
199UbiquitinationSDKQTPSKPKKKQNS
CCCCCCCCCCCCCCC		63.16-
201UbiquitinationKQTPSKPKKKQNSKG
CCCCCCCCCCCCCCC		76.08-
247UbiquitinationIKVWDLRKNYTAYRQ
EEEEECCCCCEEECC		62.70-
249PhosphorylationVWDLRKNYTAYRQEP
EEECCCCCEEECCCC		8.86-
260UbiquitinationRQEPIASKSFLYPGS
CCCCCCCCCCCCCCC		35.8821890473
260UbiquitinationRQEPIASKSFLYPGS
CCCCCCCCCCCCCCC		35.8821890473
260 (in isoform 1)Ubiquitination-35.8821890473
375UbiquitinationWCPSDFTKIATCSDD
ECCCCCCEEEECCCC		30.27-
386UbiquitinationCSDDNTLKIWRLNRG
CCCCCCEEEEEECCC		37.88-
397SumoylationLNRGLEEKPGGDKLS
ECCCCCCCCCCCCCC		39.32-
397SumoylationLNRGLEEKPGGDKLS
ECCCCCCCCCCCCCC		39.32-
397UbiquitinationLNRGLEEKPGGDKLS
ECCCCCCCCCCCCCC		39.32-
402SumoylationEEKPGGDKLSTVGWA
CCCCCCCCCCCCCHH		47.84-
402SumoylationEEKPGGDKLSTVGWA
CCCCCCCCCCCCCHH		47.84-
402UbiquitinationEEKPGGDKLSTVGWA
CCCCCCCCCCCCCHH		47.84-
410PhosphorylationLSTVGWASQKKKESR
CCCCCHHCCCCCCCC		35.7025159151
412UbiquitinationTVGWASQKKKESRPG
CCCHHCCCCCCCCCC		64.42-
414UbiquitinationGWASQKKKESRPGLV
CHHCCCCCCCCCCEE		68.88-
416PhosphorylationASQKKKESRPGLVTV
HCCCCCCCCCCEEEE		53.2920068231
422PhosphorylationESRPGLVTVTSSQST
CCCCCEEEEECCCCC		24.1022199227
424PhosphorylationRPGLVTVTSSQSTPA
CCCEEEEECCCCCCC		17.1925159151
425PhosphorylationPGLVTVTSSQSTPAK
CCEEEEECCCCCCCC		23.2623927012
426PhosphorylationGLVTVTSSQSTPAKA
CEEEEECCCCCCCCC		20.8417525332
428PhosphorylationVTVTSSQSTPAKAPR
EEEECCCCCCCCCCC		38.0030266825
429PhosphorylationTVTSSQSTPAKAPRA
EEECCCCCCCCCCCC		21.4530266825
432UbiquitinationSSQSTPAKAPRAKCN
CCCCCCCCCCCCCCC		61.1921890473
432SumoylationSSQSTPAKAPRAKCN
CCCCCCCCCCCCCCC		61.19-
432AcetylationSSQSTPAKAPRAKCN
CCCCCCCCCCCCCCC		61.1925953088
432SumoylationSSQSTPAKAPRAKCN
CCCCCCCCCCCCCCC		61.19-
432UbiquitinationSSQSTPAKAPRAKCN
CCCCCCCCCCCCCCC		61.1921890473
432 (in isoform 1)Ubiquitination-61.1921890473
437UbiquitinationPAKAPRAKCNPSNSS
CCCCCCCCCCCCCCC		35.51-
441PhosphorylationPRAKCNPSNSSPSSA
CCCCCCCCCCCCCCC		35.0430576142
443PhosphorylationAKCNPSNSSPSSAAC
CCCCCCCCCCCCCCC		48.2230576142
444PhosphorylationKCNPSNSSPSSAACA
CCCCCCCCCCCCCCC		32.8130278072
446PhosphorylationNPSNSSPSSAACAPS
CCCCCCCCCCCCCCC		34.2630278072
447PhosphorylationPSNSSPSSAACAPSC
CCCCCCCCCCCCCCC		24.2230576142
453PhosphorylationSSAACAPSCAGDLPL
CCCCCCCCCCCCCCC		9.7030278072
462PhosphorylationAGDLPLPSNTPTFSI
CCCCCCCCCCCCEEE		62.1028450419
464PhosphorylationDLPLPSNTPTFSIKT
CCCCCCCCCCEEEEC		28.2228450419
466PhosphorylationPLPSNTPTFSIKTSP
CCCCCCCCEEEECCC		28.1628450419
468PhosphorylationPSNTPTFSIKTSPAK
CCCCCCEEEECCCCC		26.1728450419
471PhosphorylationTPTFSIKTSPAKARS
CCCEEEECCCCCCCC		37.9728450419
472PhosphorylationPTFSIKTSPAKARSP
CCEEEECCCCCCCCC		20.1928450419
478PhosphorylationTSPAKARSPINRRGS
CCCCCCCCCCCCCCC		34.6823882029
485PhosphorylationSPINRRGSVSSVSPK
CCCCCCCCCCCCCCC		19.6023927012
487PhosphorylationINRRGSVSSVSPKPP
CCCCCCCCCCCCCCC		27.0730266825
488PhosphorylationNRRGSVSSVSPKPPS
CCCCCCCCCCCCCCC		25.1830266825
490PhosphorylationRGSVSSVSPKPPSSF
CCCCCCCCCCCCCHH		29.2023927012
495PhosphorylationSVSPKPPSSFKMSIR
CCCCCCCCHHCEEEE		57.8630266825
496PhosphorylationVSPKPPSSFKMSIRN
CCCCCCCHHCEEEEE		34.3630266825
498UbiquitinationPKPPSSFKMSIRNWV
CCCCCHHCEEEEECC		33.41-
506PhosphorylationMSIRNWVTRTPSSSP
EEEEECCCCCCCCCC		22.0528450419
508PhosphorylationIRNWVTRTPSSSPPI
EEECCCCCCCCCCCC		20.3930266825
510PhosphorylationNWVTRTPSSSPPITP
ECCCCCCCCCCCCCC		42.7230266825
511PhosphorylationWVTRTPSSSPPITPP
CCCCCCCCCCCCCCC		48.3325159151
512PhosphorylationVTRTPSSSPPITPPA
CCCCCCCCCCCCCCC		38.7525159151
516PhosphorylationPSSSPPITPPASETK
CCCCCCCCCCCCCCC		29.0625159151
520PhosphorylationPPITPPASETKIMSP
CCCCCCCCCCCCCCC		52.1230278072
522PhosphorylationITPPASETKIMSPRK
CCCCCCCCCCCCCCE		24.3125159151
523SumoylationTPPASETKIMSPRKA
CCCCCCCCCCCCCEE		32.15-
523SumoylationTPPASETKIMSPRKA
CCCCCCCCCCCCCEE		32.15-
526PhosphorylationASETKIMSPRKALIP
CCCCCCCCCCEEEEE		25.6520068231
529SumoylationTKIMSPRKALIPVSQ
CCCCCCCEEEEECCC		51.43-
529SumoylationTKIMSPRKALIPVSQ
CCCCCCCEEEEECCC		51.43-
529UbiquitinationTKIMSPRKALIPVSQ
CCCCCCCEEEEECCC		51.43-
535PhosphorylationRKALIPVSQKSSQAE
CEEEEECCCCCHHHH		26.9125159151
537UbiquitinationALIPVSQKSSQAEAC
EEEECCCCCHHHHHH		44.56-
538PhosphorylationLIPVSQKSSQAEACS
EEECCCCCHHHHHHH		21.7526074081
539PhosphorylationIPVSQKSSQAEACSE
EECCCCCHHHHHHHH		40.2120068231
545PhosphorylationSSQAEACSESRNRVK
CHHHHHHHHHHHHHH		45.7320068231
547PhosphorylationQAEACSESRNRVKRR
HHHHHHHHHHHHHHH		20.6820068231
552UbiquitinationSESRNRVKRRLDSSC
HHHHHHHHHHHCHHH		28.67-
557PhosphorylationRVKRRLDSSCLESVK
HHHHHHCHHHHHHHH		27.7823401153
558PhosphorylationVKRRLDSSCLESVKQ
HHHHHCHHHHHHHHH		23.5330266825
562PhosphorylationLDSSCLESVKQKCVK
HCHHHHHHHHHHHHH		22.9729255136
564UbiquitinationSSCLESVKQKCVKSC
HHHHHHHHHHHHHHC		54.01-
607UbiquitinationKDSLGPTKSSKIEGA
CCCCCCCCCCCCCCC		56.73-
616PhosphorylationSKIEGAGTSISEPPS
CCCCCCCCCCCCCCC		23.5025137130
617PhosphorylationKIEGAGTSISEPPSP
CCCCCCCCCCCCCCC		24.1725137130
619PhosphorylationEGAGTSISEPPSPIS
CCCCCCCCCCCCCCC		43.7629116813
623PhosphorylationTSISEPPSPISPYAS
CCCCCCCCCCCCCCC		45.6525159151
626PhosphorylationSEPPSPISPYASESC
CCCCCCCCCCCCCCC		18.4225159151
628PhosphorylationPPSPISPYASESCGT
CCCCCCCCCCCCCCC		18.9029978859
630PhosphorylationSPISPYASESCGTLP
CCCCCCCCCCCCCCC		24.9729978859
632PhosphorylationISPYASESCGTLPLP
CCCCCCCCCCCCCCC		18.4925137130
635PhosphorylationYASESCGTLPLPLRP
CCCCCCCCCCCCCCC		29.5425137130
647PhosphorylationLRPCGEGSEMVGKEN
CCCCCCCCCCCCCCC		20.4427080861
655PhosphorylationEMVGKENSSPENKNW
CCCCCCCCCHHHHHH		48.6530266825
656PhosphorylationMVGKENSSPENKNWL
CCCCCCCCHHHHHHH		48.0630266825
660SumoylationENSSPENKNWLLAMA
CCCCHHHHHHHHHHH		48.08-
660SumoylationENSSPENKNWLLAMA
CCCCHHHHHHHHHHH		48.08-
660UbiquitinationENSSPENKNWLLAMA
CCCCHHHHHHHHHHH		48.08-
676PhosphorylationKRKAENPSPRSPSSQ
HHHCCCCCCCCCCCC		44.5225159151
679PhosphorylationAENPSPRSPSSQTPN
CCCCCCCCCCCCCCC		32.3023401153
681PhosphorylationNPSPRSPSSQTPNSR
CCCCCCCCCCCCCCC		36.0023927012
682PhosphorylationPSPRSPSSQTPNSRR
CCCCCCCCCCCCCCC		41.2723927012
684PhosphorylationPRSPSSQTPNSRRQS
CCCCCCCCCCCCCCC		26.7823927012
687PhosphorylationPSSQTPNSRRQSGKK
CCCCCCCCCCCCCCC		30.0030576142
691PhosphorylationTPNSRRQSGKKLPSP
CCCCCCCCCCCCCCC		51.2523882029
697PhosphorylationQSGKKLPSPVTITPS
CCCCCCCCCCEECHH		42.3019664995
700PhosphorylationKKLPSPVTITPSSMR
CCCCCCCEECHHHHH		23.6330266825
702PhosphorylationLPSPVTITPSSMRKI
CCCCCEECHHHHHHH		14.0419664995
704PhosphorylationSPVTITPSSMRKICT
CCCEECHHHHHHHHH		28.2829523821
705PhosphorylationPVTITPSSMRKICTY
CCEECHHHHHHHHHH		24.6629523821
708SumoylationITPSSMRKICTYFHR
ECHHHHHHHHHHHHH		33.23-
708SumoylationITPSSMRKICTYFHR
ECHHHHHHHHHHHHH		33.23-
708UbiquitinationITPSSMRKICTYFHR
ECHHHHHHHHHHHHH		33.23-
717PhosphorylationCTYFHRKSQEDFCGP
HHHHHHHCHHHHCCC		38.4725159151
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
464TPhosphorylationKinaseCDK1P06493
Uniprot
464TPhosphorylationKinaseCDK2P24941
Uniprot
-KUbiquitinationE3 ubiquitin ligaseFBXO11Q86XK2
PMID:23478441
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
48Kubiquitylation

23478441
464TPhosphorylation

23478441
464TPhosphorylation

23478441
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 DTL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDN1A_HUMANCDKN1Aphysical
18794347
DDB1_HUMANDDB1physical
16949367
CUL4B_HUMANCUL4Bphysical
16949367
WDR5_HUMANWDR5physical
17041588
DDB1_HUMANDDB1physical
17041588
KMT5A_HUMANSETD8physical
20932471
KMT5A_HUMANSETD8physical
21035370
PCNA_HUMANPCNAphysical
21725088
MSH6_HUMANMSH6physical
21725088
MSH2_HUMANMSH2physical
21725088
P53_HUMANTP53physical
16861890
MDM2_HUMANMDM2physical
16861890
AURKB_HUMANAURKBphysical
18542055
TOB1_HUMANTOB1physical
23066029
TBG1_HUMANTUBG1physical
17106265
CDN1A_HUMANCDKN1Aphysical
23213251
CHK1_HUMANCHEK1physical
23533280
CUL4B_HUMANCUL4Bphysical
23555860
CUL4A_HUMANCUL4Aphysical
23555860
SHPRH_HUMANSHPRHphysical
23555860
HLTF_HUMANHLTFphysical
23555860
RAD18_HUMANRAD18physical
23555860
FBX11_HUMANFBXO11physical
23478441
CUL4A_HUMANCUL4Aphysical
23478441
DDB1_HUMANDDB1physical
23478441
CDT1_HUMANCDT1physical
24906324
FBH1_HUMANFBXO18physical
23677613
TDG_HUMANTDGphysical
24962565
1433E_HUMANYWHAEphysical
25154416
1433T_HUMANYWHAQphysical
25154416
1433Z_HUMANYWHAZphysical
25154416
1433B_HUMANYWHABphysical
25154416
1433G_HUMANYWHAGphysical
25154416
1433F_HUMANYWHAHphysical
25154416
1433S_HUMANSFNphysical
25154416
FBX11_HUMANFBXO11physical
25154416
CUL4A_HUMANCUL4Aphysical
16949367
CHK1_HUMANCHEK1physical
23109433
PCNA_HUMANPCNAphysical
20129063
UB2D1_HUMANUBE2D1physical
20129063
KAT2A_HUMANKAT2Aphysical
21987584
UBE2N_HUMANUBE2Nphysical
23533280
NSD2_HUMANWHSC1physical
26771714
DDB1_HUMANDDB1physical
21628527
CUL4A_HUMANCUL4Aphysical
21628527
CUL4B_HUMANCUL4Bphysical
21628527
CSN4_HUMANCOPS4physical
21628527
RBX1_HUMANRBX1physical
21628527
UB2E2_HUMANUBE2E2physical
21628527
UB2E3_HUMANUBE2E3physical
21628527
UB2E1_HUMANUBE2E1physical
21628527
CDN1A_HUMANCDKN1Aphysical
21628527
DPOD4_HUMANPOLD4physical
24022480
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 DTL_HUMAN

loading...

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-512 AND THR-516, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512 AND THR-516, ANDMASS 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-485; SER-490; SER-495;SER-510; SER-512; THR-516; SER-557; SER-676; SER-679; SER-681; SER-682AND THR-684, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory