DET1_HUMAN - dbPTM
DET1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DET1_HUMAN
UniProt AC Q7L5Y6
Protein Name DET1 homolog
Gene Name DET1
Organism Homo sapiens (Human).
Sequence Length 550
Subcellular Localization Nucleus .
Protein Description Component of the E3 ubiquitin ligase DCX DET1-COP1 complex, which is required for ubiquitination and subsequent degradation of target proteins. The complex is involved in JUN ubiquitination and degradation..
Protein Sequence MDHHVSTIKPRRIQNQNVIHRLERRRISSGKAGTHWHQVRVFHQNVFPNFTVVNVEKPPCFLRKFSPDGRYFIAFSSDQTSLEIYEYQGCQAAEDLLQGYEGEILSNGNDQRSVNIRGRLFERFFVLLHITNVAANGEHLNRECSLFTDDCRCVIVGSAAYLPDEPHPPFFEVYRNSESVTPNPRSPLEDYSLHIIDLHTGRLCDTRTFKCDKVVLSHNQGLYLYKNILAILSVQQQTIHVFQVTPEGTFIDVRTIGRFCYEDDLLTVSAVFPEVQRDSQTGMANPFRDPFINSLKHRLLVYLWRRAEQDGSAMAKRRFFQYFDQLRQLRMWKMQLLDENHLFIKYTSEDVVTLRVTDPSQASFFVVYNMVTTEVIAVFENTSDELLELFENFCDLFRNATLHSEVQFPCSASSNNFARQIQRRFKDTIINAKYGGHTEAVRRLLGQLPISAQSYSGSPYLDLSLFSYDDKWVSVMERPKTCGDHPIRFYARDSGLLKFEIQAGLLGRPINHTVRRLVAFTFHPFEPFAISVQRTNAEYVVNFHMRHCCT
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
233PhosphorylationKNILAILSVQQQTIH
HHHHHHHCCCCCEEE
16.2724043423
238PhosphorylationILSVQQQTIHVFQVT
HHCCCCCEEEEEEEC
14.5424043423
245PhosphorylationTIHVFQVTPEGTFID
EEEEEEECCCCCEEE
12.5824043423
249PhosphorylationFQVTPEGTFIDVRTI
EEECCCCCEEEEEEE
18.7624043423
333AcetylationLRQLRMWKMQLLDEN
HHHHHHHHHHHHCCC
13.8730588111
348PhosphorylationHLFIKYTSEDVVTLR
CEEEEEECCCEEEEE
28.80-
353PhosphorylationYTSEDVVTLRVTDPS
EECCCEEEEEECCHH
14.54-
426UbiquitinationRQIQRRFKDTIINAK
HHHHHHHHHHHHHCC
52.75-
437 (in isoform 2)Ubiquitination-19.03-
481PhosphorylationSVMERPKTCGDHPIR
EEECCCCCCCCCCEE
25.1423532336
492PhosphorylationHPIRFYARDSGLLKF
CCEEEEEECCCCEEE
27.5227251275

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 DET1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DET1_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 DET1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDB1_HUMANDDB1physical
14739464
CUL4A_HUMANCUL4Aphysical
14739464
RFWD2_HUMANRFWD2physical
14739464
RBX1_HUMANRBX1physical
14739464
DDA1_HUMANDDA1physical
17452440
DDB1_HUMANDDB1physical
17452440
UB2E3_HUMANUBE2E3physical
17452440
UB2E1_HUMANUBE2E1physical
17452440
DDB1_HUMANDDB1physical
16949367
CUL4A_HUMANCUL4Aphysical
16949367
CUL4B_HUMANCUL4Bphysical
16949367
CUL4A_HUMANCUL4Aphysical
17452440
RFWD2_HUMANRFWD2physical
17452440
MDM2_HUMANMDM2physical
17452440
RNF14_HUMANRNF14physical
17452440
RFWD2_HUMANRFWD2physical
28514442
UB2E2_HUMANUBE2E2physical
28514442
UB2E3_HUMANUBE2E3physical
28514442
CUL4A_HUMANCUL4Aphysical
28514442
STK40_HUMANSTK40physical
28514442
CUL4B_HUMANCUL4Bphysical
28514442
DDA1_HUMANDDA1physical
28514442
DDB1_HUMANDDB1physical
28514442
CSN2_HUMANCOPS2physical
28514442
CSN7B_HUMANCOPS7Bphysical
28514442
UB2E1_HUMANUBE2E1physical
28514442
CSN5_HUMANCOPS5physical
28514442
CSN6_HUMANCOPS6physical
28514442
CSN4_HUMANCOPS4physical
28514442
CSN7A_HUMANCOPS7Aphysical
28514442
CSN1_HUMANGPS1physical
28514442
HSP7C_HUMANHSPA8physical
28514442
CSN3_HUMANCOPS3physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DET1_HUMAN

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Related Literatures of Post-Translational Modification

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