DCLK2_HUMAN - dbPTM
DCLK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCLK2_HUMAN
UniProt AC Q8N568
Protein Name Serine/threonine-protein kinase DCLK2
Gene Name DCLK2
Organism Homo sapiens (Human).
Sequence Length 766
Subcellular Localization Cytoplasm, cytoskeleton. Colocalizes with microtubules..
Protein Description Protein kinase with a significantly reduced C(a2+)/CAM affinity and dependence compared to other members of the CaMK family. May play a role in the down-regulation of CRE-dependent gene activation probably by phosphorylation of the CREB coactivator CRTC2/TORC2 and the resulting retention of TORC2 in the cytoplasm (By similarity)..
Protein Sequence MASTRSIELEHFEERDKRPRPGSRRGAPSSSGGSSSSGPKGNGLIPSPAHSAHCSFYRTRTLQALSSEKKAKKARFYRNGDRYFKGLVFAISSDRFRSFDALLIELTRSLSDNVNLPQGVRTIYTIDGSRKVTSLDELLEGESYVCASNEPFRKVDYTKNINPNWSVNIKGGTSRALAAASSVKSEVKESKDFIKPKLVTVIRSGVKPRKAVRILLNKKTAHSFEQVLTDITEAIKLDSGVVKRLCTLDGKQVTCLQDFFGDDDVFIACGPEKFRYAQDDFVLDHSECRVLKSSYSRSSAVKYSGSKSPGPSRRSKSPASVNGTPSSQLSTPKSTKSSSSSPTSPGSFRGLKQISAHGRSSSNVNGGPELDRCISPEGVNGNRCSESSTLLEKYKIGKVIGDGNFAVVKECIDRSTGKEFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLVEEMETATELFLVMELVKGGDLFDAITSSTKYTERDGSAMVYNLANALRYLHGLSIVHRDIKPENLLVCEYPDGTKSLKLGDFGLATVVEGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQILAGKLEFPAPYWDNITDSAKELISQMLQVNVEARCTAGQILSHPWVSDDASQENNMQAEVTGKLKQHFNNALPKQNSTTTGVSVIMNTALDKEGQIFCSKHCQDSGRPGMEPISPVPPSVEEIPVPGEAVPAPTPPESPTPHPPPAAPGGERAGTWRRHRD
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
6Phosphorylation--MASTRSIELEHFE
--CCCCCCEEHHHHH
22.0922617229
29PhosphorylationGSRRGAPSSSGGSSS
CCCCCCCCCCCCCCC
36.2822210691
30PhosphorylationSRRGAPSSSGGSSSS
CCCCCCCCCCCCCCC
31.7621955146
31PhosphorylationRRGAPSSSGGSSSSG
CCCCCCCCCCCCCCC
52.0621955146
34PhosphorylationAPSSSGGSSSSGPKG
CCCCCCCCCCCCCCC
30.4921955146
35PhosphorylationPSSSGGSSSSGPKGN
CCCCCCCCCCCCCCC
31.6222210691
36PhosphorylationSSSGGSSSSGPKGNG
CCCCCCCCCCCCCCC
40.8021955146
37PhosphorylationSSGGSSSSGPKGNGL
CCCCCCCCCCCCCCC
62.1521955146
47PhosphorylationKGNGLIPSPAHSAHC
CCCCCCCCCCHHHCC
27.9428555341
51PhosphorylationLIPSPAHSAHCSFYR
CCCCCCHHHCCCHHH
23.0921955146
55PhosphorylationPAHSAHCSFYRTRTL
CCHHHCCCHHHHHHH
18.5521955146
57PhosphorylationHSAHCSFYRTRTLQA
HHHCCCHHHHHHHHH
8.5221955146
59PhosphorylationAHCSFYRTRTLQALS
HCCCHHHHHHHHHHC
19.3428857561
61PhosphorylationCSFYRTRTLQALSSE
CCHHHHHHHHHHCCH
23.7025884760
66PhosphorylationTRTLQALSSEKKAKK
HHHHHHHCCHHHHHH
39.1928674419
83PhosphorylationFYRNGDRYFKGLVFA
HHCCCCHHCCCEEEE
17.87-
93PhosphorylationGLVFAISSDRFRSFD
CEEEEECCCCCCCHH
27.05-
98PhosphorylationISSDRFRSFDALLIE
ECCCCCCCHHHHHHH
25.4324719451
166PhosphorylationKNINPNWSVNIKGGT
CCCCCCCEEEECCHH
16.3624076635
173PhosphorylationSVNIKGGTSRALAAA
EEEECCHHHHHHHHH
24.57-
182PhosphorylationRALAAASSVKSEVKE
HHHHHHHHCHHHHHH
28.9228857561
184UbiquitinationLAAASSVKSEVKESK
HHHHHHCHHHHHHCC
42.7330230243
185PhosphorylationAAASSVKSEVKESKD
HHHHHCHHHHHHCCC
45.5328857561
190PhosphorylationVKSEVKESKDFIKPK
CHHHHHHCCCCCCHH
31.6322964224
220PhosphorylationRILLNKKTAHSFEQV
HHHCCCCCCCCHHHH
31.0827732954
223PhosphorylationLNKKTAHSFEQVLTD
CCCCCCCCHHHHHHH
28.1927732954
293PhosphorylationSECRVLKSSYSRSSA
HHHEEEECCCCCCCC
30.2822210691
294PhosphorylationECRVLKSSYSRSSAV
HHEEEECCCCCCCCC
26.0722210691
295PhosphorylationCRVLKSSYSRSSAVK
HEEEECCCCCCCCCC
18.3929449344
296PhosphorylationRVLKSSYSRSSAVKY
EEEECCCCCCCCCCC
27.8629449344
298PhosphorylationLKSSYSRSSAVKYSG
EECCCCCCCCCCCCC
19.4022964224
299PhosphorylationKSSYSRSSAVKYSGS
ECCCCCCCCCCCCCC
35.6529449344
303PhosphorylationSRSSAVKYSGSKSPG
CCCCCCCCCCCCCCC
16.2122912867
304PhosphorylationRSSAVKYSGSKSPGP
CCCCCCCCCCCCCCC
30.7629449344
306PhosphorylationSAVKYSGSKSPGPSR
CCCCCCCCCCCCCCC
24.8222964224
308PhosphorylationVKYSGSKSPGPSRRS
CCCCCCCCCCCCCCC
36.4622912867
312PhosphorylationGSKSPGPSRRSKSPA
CCCCCCCCCCCCCCC
46.3629449344
315PhosphorylationSPGPSRRSKSPASVN
CCCCCCCCCCCCCCC
36.0520363803
317PhosphorylationGPSRRSKSPASVNGT
CCCCCCCCCCCCCCC
27.2625159151
320PhosphorylationRRSKSPASVNGTPSS
CCCCCCCCCCCCCHH
21.3522210691
324PhosphorylationSPASVNGTPSSQLST
CCCCCCCCCHHHCCC
18.1320363803
326PhosphorylationASVNGTPSSQLSTPK
CCCCCCCHHHCCCCC
30.4727251275
327PhosphorylationSVNGTPSSQLSTPKS
CCCCCCHHHCCCCCC
36.0227251275
330PhosphorylationGTPSSQLSTPKSTKS
CCCHHHCCCCCCCCC
34.7228985074
331PhosphorylationTPSSQLSTPKSTKSS
CCHHHCCCCCCCCCC
43.24-
334PhosphorylationSQLSTPKSTKSSSSS
HHCCCCCCCCCCCCC
42.1222210691
335PhosphorylationQLSTPKSTKSSSSSP
HCCCCCCCCCCCCCC
40.8622210691
336 (in isoform 3)Phosphorylation-56.2722210691
337PhosphorylationSTPKSTKSSSSSPTS
CCCCCCCCCCCCCCC
35.2230576142
338PhosphorylationTPKSTKSSSSSPTSP
CCCCCCCCCCCCCCC
35.4822199227
339PhosphorylationPKSTKSSSSSPTSPG
CCCCCCCCCCCCCCC
41.7630576142
340PhosphorylationKSTKSSSSSPTSPGS
CCCCCCCCCCCCCCC
42.1430576142
341 (in isoform 3)Phosphorylation-33.8628985074
341PhosphorylationSTKSSSSSPTSPGSF
CCCCCCCCCCCCCCC
33.8622199227
343PhosphorylationKSSSSSPTSPGSFRG
CCCCCCCCCCCCCCC
49.8822199227
344PhosphorylationSSSSSPTSPGSFRGL
CCCCCCCCCCCCCCC
30.5522199227
347 (in isoform 2)Phosphorylation-18.3628842319
347PhosphorylationSSPTSPGSFRGLKQI
CCCCCCCCCCCCEEE
18.3620886841
348 (in isoform 3)Phosphorylation-9.9624076635
355PhosphorylationFRGLKQISAHGRSSS
CCCCEEEECCCCCCC
16.2423312004
358PhosphorylationLKQISAHGRSSSNVN
CEEEECCCCCCCCCC
30.7724719451
360PhosphorylationQISAHGRSSSNVNGG
EEECCCCCCCCCCCC
42.5921955146
361PhosphorylationISAHGRSSSNVNGGP
EECCCCCCCCCCCCC
25.2728450419
362PhosphorylationSAHGRSSSNVNGGPE
ECCCCCCCCCCCCCC
46.1525159151
364PhosphorylationHGRSSSNVNGGPELD
CCCCCCCCCCCCCCC
8.3327251275
372PhosphorylationNGGPELDRCISPEGV
CCCCCCCCCCCCCCC
32.0924719451
375PhosphorylationPELDRCISPEGVNGN
CCCCCCCCCCCCCCC
22.1128450419
377PhosphorylationLDRCISPEGVNGNRC
CCCCCCCCCCCCCCC
69.8227251275
379PhosphorylationRCISPEGVNGNRCSE
CCCCCCCCCCCCCCC
8.7027251275
392PhosphorylationSESSTLLEKYKIGKV
CCCCHHHHHHCCCEE
58.4127251275
398UbiquitinationLEKYKIGKVIGDGNF
HHHHCCCEEECCCCE
33.8730230243
409UbiquitinationDGNFAVVKECIDRST
CCCEEEEEHHHHCCC
40.0229967540
415UbiquitinationVKECIDRSTGKEFAL
EEHHHHCCCCCCHHH
37.4530230243
426UbiquitinationEFALKIIDKAKCCGK
CHHHHHHHHHHHCCC
48.6229967540
486UbiquitinationDAITSSTKYTERDGS
HHHHCCCCCCCCCCC
52.7230230243
503UbiquitinationVYNLANALRYLHGLS
HHHHHHHHHHHHCCC
3.5730230243
505PhosphorylationNLANALRYLHGLSIV
HHHHHHHHHHCCCEE
12.1425884760
647PhosphorylationCTAGQILSHPWVSDD
CCCCCHHCCCCCCCC
29.18-
666PhosphorylationNNMQAEVTGKLKQHF
CCHHHHHHHHHHHHH
21.80-
682PhosphorylationNALPKQNSTTTGVSV
HCCCCCCCCCCCCEE
25.3321712546
683PhosphorylationALPKQNSTTTGVSVI
CCCCCCCCCCCCEEE
35.6128348404
684PhosphorylationLPKQNSTTTGVSVIM
CCCCCCCCCCCEEEE
22.7528348404
685PhosphorylationPKQNSTTTGVSVIMN
CCCCCCCCCCEEEEC
35.3627251275
702PhosphorylationLDKEGQIFCSKHCQD
CCCCCCEEECHHCCC
2.7127251275

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 DCLK2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCLK2_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 DCLK2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
T22D3_HUMANTSC22D3physical
21988832

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 DCLK2_HUMAN

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Related Literatures of Post-Translational Modification

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