KPCD2_MOUSE - dbPTM
KPCD2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KPCD2_MOUSE
UniProt AC Q8BZ03
Protein Name Serine/threonine-protein kinase D2
Gene Name Prkd2
Organism Mus musculus (Mouse).
Sequence Length 875
Subcellular Localization Cytoplasm . Cell membrane . Golgi apparatus, trans-Golgi network . Translocation to the cell membrane is required for kinase activation. Accumulates in the nucleus upon CK1-mediated phosphorylation after activation of G-protein-coupled receptors. Nuc
Protein Description Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. [PubMed: 17226786]
Protein Sequence MAAAPSHPAGLPGSPGPGSPPPPGGLDLQSPPPLLPQIPAPGSGVSFHIQIGLTREFVLLPAASELAHVKQLACSIVDQKFPECGFYGLYDKILLFKHDPTSANLLQLVRSAADIQEGDLVEVVLSASATFEDFQIRPHALTVHSYRAPAFCDHCGEMLFGLVRQGLKCDGCGLNYHKRCAFSIPNNCSGARKRRLSSTSLASGHSVRLGSSESLPCTAEELSRSTTDLLPRRPPSSSSSSSSSSFYTGRPIELDKMLMSKVKVPHTFLIHSYTRPTVCQACKKLLKGLFRQGLQCKDCKFNCHKRCATRVPNDCLGEALINGDVPMEEAADYSEADKSSISDELEDSGVIPGSHSESALHASEEEEGEGHKAQSSLGYIPLMRVVQSVRHTTRKSSTTLREGWVVHYSNKDTLRKRHYWRLDCKCITLFQNNTTNRYYKEIPLSEILAVEPAQNFSLVPPGTNPHCFEIITANVTYFVGETPGGAPGGPSGQGTEAVRGWETAIRQALMPVILQDAPSAPGHTPHRQASLSISVSNSQIQENVDIATVYQIFPDEVLGSGQFGVVYGGKHRKTGRDVAVKVIDKLRFPTKQESQLRNEVAILQSLRHPGIVNLECMFETPEKVFVVMEKLHGDMLEMILSSEKGRLPERLTKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLLNQGYNRSLDMWSVGVIMYVSLSGTFPFNEDEDINDQIQNAAFMYPASPWSHISSGAIDLINNLLQVKMRKRYSVDKSLSHPWLQEYQTWLDLRELEGKMGERYITHESDDARWDQFVAERHGTPAEGDLGGACLPQDHEMQGLAERISIL
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
30PhosphorylationPGGLDLQSPPPLLPQ
CCCCCCCCCCCCCCC		46.82-
87PhosphorylationKFPECGFYGLYDKIL
CCCCCCEEEEECEEE		7.48-
197PhosphorylationGARKRRLSSTSLASG
CCCCCCCCCCCCCCC		29.7426824392
198PhosphorylationARKRRLSSTSLASGH
CCCCCCCCCCCCCCC		26.9726824392
199PhosphorylationRKRRLSSTSLASGHS
CCCCCCCCCCCCCCC		25.1227742792
200PhosphorylationKRRLSSTSLASGHSV
CCCCCCCCCCCCCCE		24.7227742792
203PhosphorylationLSSTSLASGHSVRLG
CCCCCCCCCCCEECC		42.1925168779
206PhosphorylationTSLASGHSVRLGSSE
CCCCCCCCEECCCCC		16.6827149854
211PhosphorylationGHSVRLGSSESLPCT
CCCEECCCCCCCCCC		35.2125521595
212PhosphorylationHSVRLGSSESLPCTA
CCEECCCCCCCCCCH		29.4325521595
214PhosphorylationVRLGSSESLPCTAEE
EECCCCCCCCCCHHH		39.2927742792
218PhosphorylationSSESLPCTAEELSRS
CCCCCCCCHHHHHHC		34.8525619855
223PhosphorylationPCTAEELSRSTTDLL
CCCHHHHHHCCCCCC		27.7125619855
225PhosphorylationTAEELSRSTTDLLPR
CHHHHHHCCCCCCCC		32.0825521595
226PhosphorylationAEELSRSTTDLLPRR
HHHHHHCCCCCCCCC		24.1828833060
227PhosphorylationEELSRSTTDLLPRRP
HHHHHCCCCCCCCCC		26.3728833060
236PhosphorylationLLPRRPPSSSSSSSS
CCCCCCCCCCCCCCC		45.6028833060
237PhosphorylationLPRRPPSSSSSSSSS
CCCCCCCCCCCCCCC		39.7628833060
238PhosphorylationPRRPPSSSSSSSSSS
CCCCCCCCCCCCCCC		38.2828833060
239PhosphorylationRRPPSSSSSSSSSSF
CCCCCCCCCCCCCCC		35.8728833060
240PhosphorylationRPPSSSSSSSSSSFY
CCCCCCCCCCCCCCC		35.8728833060
241PhosphorylationPPSSSSSSSSSSFYT
CCCCCCCCCCCCCCC		35.8728833060
242PhosphorylationPSSSSSSSSSSFYTG
CCCCCCCCCCCCCCC		35.8728833060
243PhosphorylationSSSSSSSSSSFYTGR
CCCCCCCCCCCCCCC		31.7628833060
244PhosphorylationSSSSSSSSSFYTGRP
CCCCCCCCCCCCCCC		26.8128833060
245PhosphorylationSSSSSSSSFYTGRPI
CCCCCCCCCCCCCCE		24.9928833060
247PhosphorylationSSSSSSFYTGRPIEL
CCCCCCCCCCCCEEH		15.3829514104
287UbiquitinationQACKKLLKGLFRQGL
HHHHHHHHHHHHCCC		65.09-
348PhosphorylationISDELEDSGVIPGSH
CCHHHHHCCCCCCCC		26.1125338131
363PhosphorylationSESALHASEEEEGEG
CCCCCCCCHHCCCCC		34.4925338131
375PhosphorylationGEGHKAQSSLGYIPL
CCCCCCCHHHCHHHH		32.1828833060
376PhosphorylationEGHKAQSSLGYIPLM
CCCCCCHHHCHHHHH		17.4628833060
379PhosphorylationKAQSSLGYIPLMRVV
CCCHHHCHHHHHHHH		12.5028833060
388PhosphorylationPLMRVVQSVRHTTRK
HHHHHHHHHHCCCCC		14.9822817900
396PhosphorylationVRHTTRKSSTTLREG
HHCCCCCCCCCCCCE		29.6223737553
397PhosphorylationRHTTRKSSTTLREGW
HCCCCCCCCCCCCEE		28.5728507225
398PhosphorylationHTTRKSSTTLREGWV
CCCCCCCCCCCCEEE		36.6223737553
399PhosphorylationTTRKSSTTLREGWVV
CCCCCCCCCCCEEEE		26.2623737553
408PhosphorylationREGWVVHYSNKDTLR
CCEEEEEECCCHHCC		11.43-
413PhosphorylationVHYSNKDTLRKRHYW
EEECCCHHCCHHEEE		30.03-
434PhosphorylationITLFQNNTTNRYYKE
EEEEECCCCCCEEEC		32.7528494245
435PhosphorylationTLFQNNTTNRYYKEI
EEEECCCCCCEEECC		21.5928494245
439PhosphorylationNNTTNRYYKEIPLSE
CCCCCCEEECCCHHH		10.02-
519PhosphorylationVILQDAPSAPGHTPH
HHHCCCCCCCCCCCC		49.1422817900
524PhosphorylationAPSAPGHTPHRQASL
CCCCCCCCCCCCEEE		27.0618846507
706UbiquitinationFARIIGEKSFRRSVV
CCEECCCCCHHCCCC		50.08-
707PhosphorylationARIIGEKSFRRSVVG
CEECCCCCHHCCCCC		21.4920819079
711PhosphorylationGEKSFRRSVVGTPAY
CCCCHHCCCCCCHHH		19.5220819079
715PhosphorylationFRRSVVGTPAYLAPE
HHCCCCCCHHHHCHH		7.9828833060
718PhosphorylationSVVGTPAYLAPEVLL
CCCCCHHHHCHHHHH		12.4729550500
833PhosphorylationERYITHESDDARWDQ
CCEECCCCCCHHHHH		32.94-
873PhosphorylationQGLAERISIL-----
CHHHHHHHCC-----		24.8620819079
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
244SPhosphorylationKinaseCSNK1DQ9DC28
Uniprot
244SPhosphorylationKinaseCSNK1EQ9JMK2
Uniprot
439YPhosphorylationKinaseABL1P00520
Uniprot
707SPhosphorylationKinasePKC-FAMILY-GPS
707SPhosphorylationKinasePKC-Uniprot
711SPhosphorylationKinasePRKD2Q8BZ03
GPS
718YPhosphorylationKinaseABL1P00520
Uniprot
873SPhosphorylationKinasePRKD1Q62101
PSP
873SPhosphorylationKinasePRKD2Q8BZ03
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
244SPhosphorylation

-
244SPhosphorylation

-
707SOxidation

20819079
707SPhosphorylation

20819079
707SPhosphorylation

20819079
707SPhosphorylation

20819079
711SOxidation

20819079
711SPhosphorylation

20819079
711SPhosphorylation

20819079
873SPhosphorylation

20819079
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 KPCD2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of KPCD2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KPCD2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Unique functions for protein kinase D1 and protein kinase D2 inmammalian cells.";
Matthews S.A., Navarro M.N., Sinclair L.V., Emslie E.,Feijoo-Carnero C., Cantrell D.A.;
Biochem. J. 432:153-163(2010).
Cited for: FUNCTION IN T-CELLS, PHOSPHORYLATION AT SER-707; SER-711 AND SER-873,AND MUTAGENESIS OF SER-707 AND SER-711.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-211; SER-212AND SER-214, AND MASS SPECTROMETRY.

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