DYRK4_HUMAN - dbPTM
DYRK4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DYRK4_HUMAN
UniProt AC Q9NR20
Protein Name Dual specificity tyrosine-phosphorylation-regulated kinase 4
Gene Name DYRK4
Organism Homo sapiens (Human).
Sequence Length 520
Subcellular Localization Isoform 1: Cytoplasm .
Isoform 4: Cytoplasm . Nucleus .
Protein Description Possible non-essential role in spermiogenesis..
Protein Sequence MPASELKASEIPFHPSIKTQDPKAEEKSPKKQKVTLTAAEALKLFKNQLSPYEQSEILGYAELWFLGLEAKKLDTAPEKFSKTSFDDEHGFYLKVLHDHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFDSKGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKPQPRPQTLRKSNSFFPSETRKDKVQGCHHSSRKADEITKETTEKTKDSPTKHVQHSGDQQDCLQHGADTVQLPQLVDAPKKSEAAVGAEVSMTSPGQSKNFSLKNTNVLPPIV
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
4Phosphorylation----MPASELKASEI
----CCHHHHCHHCC
37.2825404012
9PhosphorylationPASELKASEIPFHPS
CHHHHCHHCCCCCCC
34.1825404012
16PhosphorylationSEIPFHPSIKTQDPK
HCCCCCCCCCCCCCC
28.3125404012
37PhosphorylationKKQKVTLTAAEALKL
CCCCCCCHHHHHHHH
17.92-
71UbiquitinationWFLGLEAKKLDTAPE
HHHHHHHCCCCCCCH
44.48-
72UbiquitinationFLGLEAKKLDTAPEK
HHHHHHCCCCCCCHH
59.65-
205PhosphorylationNFQGFSLSIVRRFTL
CCCCCCHHHHHHHHH
20.1724719451
211PhosphorylationLSIVRRFTLSVLKCL
HHHHHHHHHHHHHHH
19.1330619164
213PhosphorylationIVRRFTLSVLKCLQM
HHHHHHHHHHHHHHH
23.5030619164
222PhosphorylationLKCLQMLSVEKIIHC
HHHHHHHCCCEEECC
23.92-
262PhosphorylationCYEHQKVYTYIQSRF
HHHHHHHHHHHHHHH
10.8124260401
263PhosphorylationYEHQKVYTYIQSRFY
HHHHHHHHHHHHHHC
19.6927794612
264PhosphorylationEHQKVYTYIQSRFYR
HHHHHHHHHHHHHCC
4.5419664994
267PhosphorylationKVYTYIQSRFYRSPE
HHHHHHHHHHCCCCH
18.1322617229
356PhosphorylationNNRGKKRYPDSKDLT
CCCCCCCCCCCCCCE
21.9222817900
360SumoylationKKRYPDSKDLTMVLK
CCCCCCCCCCEEHHH
65.23-
417UbiquitinationPRPQTLRKSNSFFPS
CCCCCHHCCCCCCCC
58.04-
418PhosphorylationRPQTLRKSNSFFPSE
CCCCHHCCCCCCCCC
31.1324505115
426PhosphorylationNSFFPSETRKDKVQG
CCCCCCCHHHHCCCC
47.5624505115
437PhosphorylationKVQGCHHSSRKADEI
CCCCCCCCHHHHHHH
14.26-
445PhosphorylationSRKADEITKETTEKT
HHHHHHHHHHHHHCC
22.30-
457PhosphorylationEKTKDSPTKHVQHSG
HCCCCCCCCCCCCCC
37.42-

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
264YPhosphorylationKinaseDYRK4Q9NR20
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DYRK4_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 DYRK4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR33_HUMANWDR33physical
23602568
TECR_HUMANTECRphysical
23602568
YMEL1_HUMANYME1L1physical
23602568
RCN1_HUMANRCN1physical
23602568
RBBP4_HUMANRBBP4physical
23602568
HAX1_HUMANHAX1physical
23602568
AT1A1_HUMANATP1A1physical
23602568
UBP11_HUMANUSP11physical
23602568
CALL5_HUMANCALML5physical
28514442

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DYRK4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-264, AND MASSSPECTROMETRY.
"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-264, AND MASSSPECTROMETRY.

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