DEUP1_HUMAN - dbPTM
DEUP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DEUP1_HUMAN
UniProt AC Q05D60
Protein Name Deuterosome assembly protein 1 {ECO:0000312|HGNC:HGNC:26344}
Gene Name DEUP1 {ECO:0000312|HGNC:HGNC:26344}
Organism Homo sapiens (Human).
Sequence Length 604
Subcellular Localization Cytoplasm. Localizes to the deuterosome..
Protein Description Key structural component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells and can generate more than 100 centrioles. Probably sufficient for the specification and formation of the deuterosome inner core. Interacts with CEP152 and recruits PLK4 to activate centriole biogenesis (By similarity)..
Protein Sequence MENQAHNTMGTSPCEAELQELMEQIDIMVSNKKMDWERKMRALETRLDLRDQELANAQTCLDQKGQEVGLLRQKLDSLEKCNLAMTQNYEGQLQSLKAQFSKLTNNFEKLRLHQMKQNKVPRKELPHLKEEIPFELSNLNQKLEEFRAKSREWDKQEILYQTHLISLDAQQKLLSEKCNQFQKQAQSYQTQLNGKKQCLEDSSSEIPRLICDPDPNCEINERDEFIIEKLKSAVNEIALSRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLRIIEMERLQLHRELLKIGECQNAQGNKTRLESSYLPSIKEPERKIKELFSVMQDQPNHEKELNKIRSQLQQVEEYHNSEQERMRNEISDLTEELHQKEITIATVTKKAALLEKQLKMELEIKEKMLAKQKVSDMKYKAVRTENTHLKGMMGDLDPGEYMSMDFTNREQSRHTSINKLQYENERLRNDLAKLHVNGKSTWTNQNTYEETGRYAYQSQIKVEQNEERLSHDCEPNRSTMPPLPPSTFQAKEMTSPLVSDDDVFPLSPPDMSFPASLAAQHFLLEEEKRAKELEKLLNTHIDELQRHTEFTLNKYSKLKQNRHI
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
150PhosphorylationLEEFRAKSREWDKQE
HHHHHHHCCCCHHHH
-
175PhosphorylationDAQQKLLSEKCNQFQ
HHHHHHHHHHHHHHH
24719451
187PhosphorylationQFQKQAQSYQTQLNG
HHHHHHHHHHHHHHC
30619164
188PhosphorylationFQKQAQSYQTQLNGK
HHHHHHHHHHHHHCC
30619164
190PhosphorylationKQAQSYQTQLNGKKQ
HHHHHHHHHHHCCHH
30619164
240PhosphorylationAVNEIALSRNKLQDE
HHHHHHHHHHHCHHH
24719451
270PhosphorylationQAMEAGLSEVKSELQ
HHHHHCHHHHHHHHH
29083192
315PhosphorylationGNKTRLESSYLPSIK
CCCCCCCHHCCCCCC
23403867
316PhosphorylationNKTRLESSYLPSIKE
CCCCCCHHCCCCCCC
23403867
317PhosphorylationKTRLESSYLPSIKEP
CCCCCHHCCCCCCCH
23403867
320PhosphorylationLESSYLPSIKEPERK
CCHHCCCCCCCHHHH
23403867
333PhosphorylationRKIKELFSVMQDQPN
HHHHHHHHHHCCCCC
25159151
419PhosphorylationQKVSDMKYKAVRTEN
HCCCCCCHHHHHCCC
-
547PhosphorylationDDDVFPLSPPDMSFP
CCCCCCCCCCCCCCC
-

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 DEUP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DEUP1_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 DEUP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DEUP1_HUMANCCDC67physical
25416956
TXLNB_HUMANTXLNBphysical
25416956
TXLNA_HUMANTXLNAphysical
25416956
GOGA3_HUMANGOLGA3physical
26186194
HIP1_HUMANHIP1physical
26186194
DGKH_HUMANDGKHphysical
26186194
SPAG5_HUMANSPAG5physical
26186194
ANX13_HUMANANXA13physical
26186194
IFT20_HUMANIFT20physical
26186194
TRAF7_HUMANTRAF7physical
26186194
SKAP_HUMANKNSTRNphysical
26186194
TRAF6_HUMANTRAF6physical
26186194
MAFF_HUMANMAFFphysical
26186194
MAFG_HUMANMAFGphysical
26186194
JUN_HUMANJUNphysical
26186194
FP100_HUMANC17orf70physical
26186194
IFT20_HUMANIFT20physical
24613305
CEP85_HUMANCEP85physical
24613305
CCHCR_HUMANCCHCR1physical
24613305
CCD57_HUMANCCDC57physical
24613305
CE152_HUMANCEP152physical
24613305
SPAG5_HUMANSPAG5physical
24613305
OFD1_HUMANOFD1physical
24613305
CSPP1_HUMANCSPP1physical
24613305
PRP4B_HUMANPRPF4Bphysical
24613305
NKTR_HUMANNKTRphysical
24613305
CE128_HUMANCEP128physical
24613305
MPP9_HUMANMPHOSPH9physical
24613305
K1671_HUMANKIAA1671physical
24613305
TBG1_HUMANTUBG1physical
24613305
PCNT_HUMANPCNTphysical
24613305
MAGD1_HUMANMAGED1physical
24613305
CP131_HUMANCEP131physical
24613305
CEP63_HUMANCEP63physical
24613305
HIP1_HUMANHIP1physical
28514442
IFT20_HUMANIFT20physical
28514442
MAFG_HUMANMAFGphysical
28514442
ANX13_HUMANANXA13physical
28514442
TRAF6_HUMANTRAF6physical
28514442
SPAG5_HUMANSPAG5physical
28514442
GOGA3_HUMANGOLGA3physical
28514442
DGKH_HUMANDGKHphysical
28514442
FP100_HUMANC17orf70physical
28514442
SKAP_HUMANKNSTRNphysical
28514442
TRAF7_HUMANTRAF7physical
28514442
JUN_HUMANJUNphysical
28514442
MAFF_HUMANMAFFphysical
28514442

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 DEUP1_HUMAN

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Related Literatures of Post-Translational Modification

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