PKN1_HUMAN - dbPTM
PKN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKN1_HUMAN
UniProt AC Q16512
Protein Name Serine/threonine-protein kinase N1
Gene Name PKN1
Organism Homo sapiens (Human).
Sequence Length 942
Subcellular Localization Cytoplasm . Nucleus . Endosome . Cell membrane
Peripheral membrane protein . Cleavage furrow . Midbody . Associates with chromatin in a ligand-dependent manner. Localization to endosomes is mediated via its interaction with RHOB. Association to the
Protein Description PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro..
Protein Sequence MASDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRREIRKELKLKEGAENLRRATTDLGRSLGPVELLLRGSSRRLDLLHQQLQELHAHVVLPDPAATHDGPQSPGAGGPTCSATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQAGQLENQAAPDDTQGSPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGELPADHPKGRLLREELAAASSAAFSTRLAGPFPATHYSTLCKPAPLTGTLEVRVVGCRDLPETIPWNPTPSMGGPGTPDSRPPFLSRPARGLYSRSGSLSGRSSLKAEAENTSEVSTVLKLDNTVVGQTSWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPVIERIPRLRRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPNATGTGTFSPGASPGSEARTTGDISVEKLNLGTDSDSSPQKSSRDPPSSPSSLSSPIQESTAPELPSETQETPGPALCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLDFDFVAGGC
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
2Acetylation------MASDAVQSE
------CCCHHHCCC
19.0022814378
3Phosphorylation-----MASDAVQSEP
-----CCCHHHCCCC
25.46-
8PhosphorylationMASDAVQSEPRSWSL
CCCHHHCCCCCHHHH
42.8625850435
12PhosphorylationAVQSEPRSWSLLEQL
HHCCCCCHHHHHHHH
31.5624719451
14PhosphorylationQSEPRSWSLLEQLGL
CCCCCHHHHHHHHCC
25.0727251275
18 (in isoform 2)Phosphorylation-40.5824719451
51UbiquitinationREIRKELKLKEGAEN
HHHHHHHHHHHHHHH
59.6124816145
53UbiquitinationIRKELKLKEGAENLR
HHHHHHHHHHHHHHH
53.14-
57UbiquitinationLKLKEGAENLRRATT
HHHHHHHHHHHHHHH
68.5924816145
59 (in isoform 2)Ubiquitination-2.70-
63PhosphorylationAENLRRATTDLGRSL
HHHHHHHHHHHHHHH
21.0223403867
63UbiquitinationAENLRRATTDLGRSL
HHHHHHHHHHHHHHH
21.0224816145
64PhosphorylationENLRRATTDLGRSLG
HHHHHHHHHHHHHHC
28.3910467162
69PhosphorylationATTDLGRSLGPVELL
HHHHHHHHHCHHHHH
35.5622617229
75 (in isoform 2)Phosphorylation-5.7824719451
80PhosphorylationVELLLRGSSRRLDLL
HHHHHCCCHHHHHHH
17.7823186163
81PhosphorylationELLLRGSSRRLDLLH
HHHHCCCHHHHHHHH
25.0123186163
86 (in isoform 2)Phosphorylation-5.6427251275
106PhosphorylationVLPDPAATHDGPQSP
ECCCCCCCCCCCCCC
23.7028464451
112PhosphorylationATHDGPQSPGAGGPT
CCCCCCCCCCCCCCC
28.5628464451
118 (in isoform 2)Phosphorylation-29.3427251275
119PhosphorylationSPGAGGPTCSATNLS
CCCCCCCCCCCCCHH
23.5122210691
121PhosphorylationGAGGPTCSATNLSRV
CCCCCCCCCCCHHHH
40.3828122231
123PhosphorylationGGPTCSATNLSRVAG
CCCCCCCCCHHHHCC
22.0228122231
126PhosphorylationTCSATNLSRVAGLEK
CCCCCCHHHHCCCCH
27.1228122231
167 (in isoform 2)Ubiquitination-24.79-
173PhosphorylationAQQMLQDSKTKIDII
HHHHHHCCCCHHHHH
29.3022210691
175PhosphorylationQMLQDSKTKIDIIRM
HHHHCCCCHHHHHHH
36.8622210691
202PhosphorylationNQAAPDDTQGSPDLG
CCCCCCCCCCCCCCC
42.0628450419
205PhosphorylationAPDDTQGSPDLGAVE
CCCCCCCCCCCCCEE
12.8621712546
233UbiquitinationHAVAEGAKNVLRLLS
HHHHHHHHHHHHHHH
59.4524816145
239UbiquitinationAKNVLRLLSAAKAPD
HHHHHHHHHHCCCCC
2.3724816145
240PhosphorylationKNVLRLLSAAKAPDR
HHHHHHHHHCCCCCH
30.6719664994
243AcetylationLRLLSAAKAPDRKAV
HHHHHHCCCCCHHHH
61.2325953088
243UbiquitinationLRLLSAAKAPDRKAV
HHHHHHCCCCCHHHH
61.2324816145
245UbiquitinationLLSAAKAPDRKAVSE
HHHHCCCCCHHHHHH
41.0324816145
246 (in isoform 2)Phosphorylation-70.3624719451
249UbiquitinationAKAPDRKAVSEAQEK
CCCCCHHHHHHHHHH
15.8024816145
255UbiquitinationKAVSEAQEKLTESNQ
HHHHHHHHHHHHHHH
58.0224816145
256UbiquitinationAVSEAQEKLTESNQK
HHHHHHHHHHHHHHH
48.9429967540
262UbiquitinationEKLTESNQKLGLLRE
HHHHHHHHHHHHHHH
52.1829967540
263UbiquitinationKLTESNQKLGLLREA
HHHHHHHHHHHHHHH
49.0922817900
263 (in isoform 1)Ubiquitination-49.0921890473
263UbiquitinationKLTESNQKLGLLREA
HHHHHHHHHHHHHHH
49.0921890473
269UbiquitinationQKLGLLREALERRLG
HHHHHHHHHHHHHHC
58.5421890473
269 (in isoform 2)Ubiquitination-58.5421890473
275UbiquitinationREALERRLGELPADH
HHHHHHHHCCCCCCC
8.6121890473
301PhosphorylationAASSAAFSTRLAGPF
HHHHHHHHHHHCCCC
14.11-
311PhosphorylationLAGPFPATHYSTLCK
HCCCCCCCCCCCCCC
22.9120873877
313PhosphorylationGPFPATHYSTLCKPA
CCCCCCCCCCCCCCC
10.0522210691
314PhosphorylationPFPATHYSTLCKPAP
CCCCCCCCCCCCCCC
13.8020873877
315PhosphorylationFPATHYSTLCKPAPL
CCCCCCCCCCCCCCC
29.0720873877
317 (in isoform 2)Phosphorylation-5.1327251275
323PhosphorylationLCKPAPLTGTLEVRV
CCCCCCCCCEEEEEE
27.3622210691
345PhosphorylationETIPWNPTPSMGGPG
CCCCCCCCCCCCCCC
25.4526074081
347PhosphorylationIPWNPTPSMGGPGTP
CCCCCCCCCCCCCCC
32.3226074081
353PhosphorylationPSMGGPGTPDSRPPF
CCCCCCCCCCCCCCC
27.3617192257
356PhosphorylationGGPGTPDSRPPFLSR
CCCCCCCCCCCCCCC
48.1426074081
357MethylationGPGTPDSRPPFLSRP
CCCCCCCCCCCCCCC
50.74115386671
359 (in isoform 2)Phosphorylation-41.5224719451
362PhosphorylationDSRPPFLSRPARGLY
CCCCCCCCCCCCCCC
36.2828122231
366MethylationPFLSRPARGLYSRSG
CCCCCCCCCCCCCCC
38.0354558023
370PhosphorylationRPARGLYSRSGSLSG
CCCCCCCCCCCCCCC
25.6424719451
372PhosphorylationARGLYSRSGSLSGRS
CCCCCCCCCCCCCCH
27.1328176443
374PhosphorylationGLYSRSGSLSGRSSL
CCCCCCCCCCCCHHH
22.1710467162
376PhosphorylationYSRSGSLSGRSSLKA
CCCCCCCCCCHHHHE
33.5828450419
379PhosphorylationSGSLSGRSSLKAEAE
CCCCCCCHHHHEECC
43.4828450419
380PhosphorylationGSLSGRSSLKAEAEN
CCCCCCHHHHEECCC
32.3110467162
382UbiquitinationLSGRSSLKAEAENTS
CCCCHHHHEECCCCC
46.2432015554
386 (in isoform 2)Phosphorylation-53.1724719451
388PhosphorylationLKAEAENTSEVSTVL
HHEECCCCCCCCEEE
20.1227251275
388UbiquitinationLKAEAENTSEVSTVL
HHEECCCCCCCCEEE
20.1232015554
389PhosphorylationKAEAENTSEVSTVLK
HEECCCCCCCCEEEE
47.8127251275
392PhosphorylationAENTSEVSTVLKLDN
CCCCCCCCEEEEECC
14.5627251275
393PhosphorylationENTSEVSTVLKLDNT
CCCCCCCEEEEECCE
34.7327251275
445AcetylationQRGLCALKFLKLEDF
CCCCCHHEEECHHHH
30.0825953088
445UbiquitinationQRGLCALKFLKLEDF
CCCCCHHEEECHHHH
30.08-
448AcetylationLCALKFLKLEDFLDN
CCHHEEECHHHHHCC
53.6219608861
451 (in isoform 2)Ubiquitination-60.90-
454AcetylationLKLEDFLDNERHEVQ
ECHHHHHCCCCCEEE
55.7419608861
495PhosphorylationRRQKKIFSKQQGKAF
HHHHHHCHHHHHHHH
32.7823401153
496UbiquitinationRQKKIFSKQQGKAFQ
HHHHHCHHHHHHHHH
35.57-
501PhosphorylationFSKQQGKAFQRARQM
CHHHHHHHHHHHHHC
16.7832645325
501 (in isoform 2)Phosphorylation-16.7824719451
527PhosphorylationRRLIPNATGTGTFSP
HHHCCCCCCCCCCCC
41.7528555341
529PhosphorylationLIPNATGTGTFSPGA
HCCCCCCCCCCCCCC
28.7927134283
531PhosphorylationPNATGTGTFSPGASP
CCCCCCCCCCCCCCC
22.3029255136
533PhosphorylationATGTGTFSPGASPGS
CCCCCCCCCCCCCCC
23.4329255136
535 (in isoform 2)Phosphorylation-37.1724719451
537PhosphorylationGTFSPGASPGSEART
CCCCCCCCCCCCCCC
35.3929255136
539PhosphorylationFSPGASPGSEARTTG
CCCCCCCCCCCCCCC
35.3132142685
539 (in isoform 2)Phosphorylation-35.3124719451
540PhosphorylationSPGASPGSEARTTGD
CCCCCCCCCCCCCCC
31.3129255136
543PhosphorylationASPGSEARTTGDISV
CCCCCCCCCCCCCCE
28.8632142685
543 (in isoform 2)Phosphorylation-28.8624719451
544PhosphorylationSPGSEARTTGDISVE
CCCCCCCCCCCCCEE
42.0223312004
545PhosphorylationPGSEARTTGDISVEK
CCCCCCCCCCCCEEE
27.5723312004
549PhosphorylationARTTGDISVEKLNLG
CCCCCCCCEEECCCC
29.0321815630
557PhosphorylationVEKLNLGTDSDSSPQ
EEECCCCCCCCCCCC
35.1822167270
559O-linked_GlycosylationKLNLGTDSDSSPQKS
ECCCCCCCCCCCCCC
38.9529351928
559PhosphorylationKLNLGTDSDSSPQKS
ECCCCCCCCCCCCCC
38.9522167270
561O-linked_GlycosylationNLGTDSDSSPQKSSR
CCCCCCCCCCCCCCC
48.1229351928
561PhosphorylationNLGTDSDSSPQKSSR
CCCCCCCCCCCCCCC
48.1229255136
562PhosphorylationLGTDSDSSPQKSSRD
CCCCCCCCCCCCCCC
36.0219664994
565UbiquitinationDSDSSPQKSSRDPPS
CCCCCCCCCCCCCCC
54.5024816145
565 (in isoform 2)Phosphorylation-54.5027251275
566PhosphorylationSDSSPQKSSRDPPSS
CCCCCCCCCCCCCCC
25.9223403867
567PhosphorylationDSSPQKSSRDPPSSP
CCCCCCCCCCCCCCC
47.9719413330
568 (in isoform 2)Phosphorylation-68.4924719451
571UbiquitinationQKSSRDPPSSPSSLS
CCCCCCCCCCCHHCC
52.2924816145
572PhosphorylationKSSRDPPSSPSSLSS
CCCCCCCCCCHHCCC
61.3423401153
573PhosphorylationSSRDPPSSPSSLSSP
CCCCCCCCCHHCCCC
34.2830278072
575PhosphorylationRDPPSSPSSLSSPIQ
CCCCCCCHHCCCCCC
45.9523401153
576PhosphorylationDPPSSPSSLSSPIQE
CCCCCCHHCCCCCCC
35.3430278072
577UbiquitinationPPSSPSSLSSPIQES
CCCCCHHCCCCCCCC
7.4424816145
578PhosphorylationPSSPSSLSSPIQEST
CCCCHHCCCCCCCCC
35.7023898821
579PhosphorylationSSPSSLSSPIQESTA
CCCHHCCCCCCCCCC
31.1730278072
579 (in isoform 2)Phosphorylation-31.1727251275
584PhosphorylationLSSPIQESTAPELPS
CCCCCCCCCCCCCCC
17.3130108239
585PhosphorylationSSPIQESTAPELPSE
CCCCCCCCCCCCCCC
45.5430206219
591PhosphorylationSTAPELPSETQETPG
CCCCCCCCCCCCCCC
66.9428450419
593PhosphorylationAPELPSETQETPGPA
CCCCCCCCCCCCCCC
35.7228464451
596PhosphorylationLPSETQETPGPALCS
CCCCCCCCCCCCCCC
24.5928450419
603PhosphorylationTPGPALCSPLRKSPL
CCCCCCCCCCCCCCC
28.0227050516
607UbiquitinationALCSPLRKSPLTLED
CCCCCCCCCCCCHHH
65.2029967540
608PhosphorylationLCSPLRKSPLTLEDF
CCCCCCCCCCCHHHH
20.7828348404
611PhosphorylationPLRKSPLTLEDFKFL
CCCCCCCCHHHHHHH
31.3326074081
613UbiquitinationRKSPLTLEDFKFLAV
CCCCCCHHHHHHHHE
57.0529967540
613 (in isoform 2)Ubiquitination-57.05-
614 (in isoform 2)Phosphorylation-55.9727251275
644UbiquitinationSGELFAIKALKKGDI
CCCEEEEEEHHHCCE
44.2129967540
650UbiquitinationIKALKKGDIVARDEV
EEEHHHCCEEEHHHH
40.8629967540
650 (in isoform 2)Ubiquitination-40.86-
661SulfoxidationRDEVESLMCEKRILA
HHHHHHHHCHHHHHH
3.7421406390
664UbiquitinationVESLMCEKRILAAVT
HHHHHCHHHHHHHHH
39.5524816145
670UbiquitinationEKRILAAVTSAGHPF
HHHHHHHHHHCCCCC
3.4624816145
670 (in isoform 2)Ubiquitination-3.46-
676UbiquitinationAVTSAGHPFLVNLFG
HHHHCCCCCEEHHHC
24.2924816145
742UbiquitinationKIVYRDLKLDNLLLD
CEEECCCCCCCEEEC
59.0722817900
748UbiquitinationLKLDNLLLDTEGYVK
CCCCCEEECCCCCEE
9.6122817900
754UbiquitinationLLDTEGYVKIADFGL
EECCCCCEEHHHCCC
5.4822817900
763UbiquitinationIADFGLCKEGMGYGD
HHHCCCCCCCCCCCC
63.45-
768PhosphorylationLCKEGMGYGDRTSTF
CCCCCCCCCCCCCCC
13.6322322096
772PhosphorylationGMGYGDRTSTFCGTP
CCCCCCCCCCCCCCC
36.5423401153
773PhosphorylationMGYGDRTSTFCGTPE
CCCCCCCCCCCCCCH
22.0022322096
774PhosphorylationGYGDRTSTFCGTPEF
CCCCCCCCCCCCCHH
23.4910467162
778PhosphorylationRTSTFCGTPEFLAPE
CCCCCCCCCHHHCCH
22.3321712546
778 (in isoform 2)Phosphorylation-22.3324719451
779PhosphorylationTSTFCGTPEFLAPEV
CCCCCCCCHHHCCHH
18.6732142685
779 (in isoform 2)Phosphorylation-18.6727251275
780PhosphorylationSTFCGTPEFLAPEVL
CCCCCCCHHHCCHHH
53.8032142685
784PhosphorylationGTPEFLAPEVLTDTS
CCCHHHCCHHHCCCC
34.0832142685
788PhosphorylationFLAPEVLTDTSYTRA
HHCCHHHCCCCCHHH
42.2723403867
790PhosphorylationAPEVLTDTSYTRAVD
CCHHHCCCCCHHHHH
20.5623403867
791PhosphorylationPEVLTDTSYTRAVDW
CHHHCCCCCHHHHHH
27.5823403867
792PhosphorylationEVLTDTSYTRAVDWW
HHHCCCCCHHHHHHH
11.4423403867
793PhosphorylationVLTDTSYTRAVDWWG
HHCCCCCHHHHHHHH
16.3623403867
847DimethylationAEAIGIMRRLLRRNP
HHHHHHHHHHHHHCH
24.95-
847MethylationAEAIGIMRRLLRRNP
HHHHHHHHHHHHHCH
24.95115372699
869UbiquitinationERDAEDVKKQPFFRT
CCCHHHHHHCHHHHH
59.0024816145
875UbiquitinationVKKQPFFRTLGWEAL
HHHCHHHHHHCHHHH
29.4424816145
875 (in isoform 2)Ubiquitination-29.44-
881UbiquitinationFRTLGWEALLARRLP
HHHHCHHHHHHHCCC
11.0224816145
896PhosphorylationPPFVPTLSGRTDVSN
CCCCCCCCCCCCCCC
28.8026074081
899PhosphorylationVPTLSGRTDVSNFDE
CCCCCCCCCCCCCCH
44.2523403867
902PhosphorylationLSGRTDVSNFDEEFT
CCCCCCCCCCCHHHC
34.2928176443
909PhosphorylationSNFDEEFTGEAPTLS
CCCCHHHCCCCCCCC
37.0728176443
914PhosphorylationEFTGEAPTLSPPRDA
HHCCCCCCCCCCCCC
47.0929255136
916PhosphorylationTGEAPTLSPPRDARP
CCCCCCCCCCCCCCC
35.0219664994
922PhosphorylationLSPPRDARPLTAAEQ
CCCCCCCCCCCHHHH
30.9332142685
922 (in isoform 2)Phosphorylation-30.9324719451
925PhosphorylationPRDARPLTAAEQAAF
CCCCCCCCHHHHHHH
26.8926074081

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
533SPhosphorylationKinaseCDK1P06493
PSP
537SPhosphorylationKinaseCDK1P06493
PSP
562SPhosphorylationKinaseCDK1P06493
PSP
773SPhosphorylationKinasePDPK1O15530
GPS
774TPhosphorylationKinasePDK1Q15118
GPS
774TPhosphorylationKinasePDK1O15530
PSP
774TPhosphorylationKinasePKN1Q16512
PSP
916SPhosphorylationKinaseCDK1P06493
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKN1_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 PKN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC85B_HUMANCCDC85Bphysical
16189514
RHOA_HUMANRHOAphysical
9535835
NFL_HUMANNEFLphysical
8621664
NFH_HUMANNEFHphysical
8621664
ACTN1_HUMANACTN1physical
11802708
PLD1_HUMANPLD1physical
11259428
VIME_HUMANVIMphysical
9175763
NDF2_HUMANNEUROD2physical
10640683
RHOA_HUMANRHOAphysical
9446575
AKAP9_HUMANAKAP9physical
10358086
PDPK1_HUMANPDPK1physical
10764742
CDR2_HUMANCDR2physical
9637778
HDAC5_HUMANHDAC5physical
20188095
HDAC6_HUMANHDAC6physical
19036992
H32_HUMANHIST2H3Cphysical
18066052
ZN282_HUMANZNF282physical
21900206
SPR2D_HUMANSPRR2Dphysical
21900206
TBA1A_HUMANTUBA1Aphysical
12716939
TBB5_HUMANTUBBphysical
12716939
TRAF2_HUMANTRAF2physical
14741690
PKN1_HUMANPKN1physical
14741690
TM1L1_HUMANTOM1L1physical
22939629
TAU_HUMANMAPTphysical
11104762
TRAF1_HUMANTRAF1physical
18429822
TNR1B_HUMANTNFRSF1Bphysical
18429822
MK12_HUMANMAPK12physical
12761180
MK11_HUMANMAPK11physical
12761180
MP2K3_HUMANMAP2K3physical
12761180
MP2K6_HUMANMAP2K6physical
12761180
RHOA_HUMANRHOAphysical
10619026
MARCS_HUMANMARCKSphysical
8557118
MPIP3_HUMANCDC25Cphysical
15791647
MBP_HUMANMBPphysical
15791647
BUD23_HUMANWBSCR22physical
21988832
H11_HUMANHIST1H1Aphysical
21357687
VIME_HUMANVIMphysical
25416956
HOME3_HUMANHOMER3physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
CE57L_HUMANCEP57L1physical
25416956
WDR5_HUMANWDR5physical
24793694
KMT2A_HUMANKMT2Aphysical
24793694
RBBP5_HUMANRBBP5physical
24793694
ASH2L_HUMANASH2Lphysical
24793694
PPM1A_HUMANPPM1Aphysical
26344197
PPM1G_HUMANPPM1Gphysical
26344197
HOME3_HUMANHOMER3physical
21516116

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 PKN1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-533; SER-537; SER-559; SER-561; SER-562 ANDSER-916, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-448, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-533; SER-537;SER-559; SER-562; THR-914 AND SER-916, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-533; SER-537; SER-559; SER-561; SER-562 ANDSER-916, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-537; SER-559;SER-562 AND SER-916, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; THR-353; SER-533;SER-537; SER-559 AND SER-916, AND MASS SPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562 AND SER-916, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-778, AND MASSSPECTROMETRY.
"Phosphorylation of protein kinase N by phosphoinositide-dependentprotein kinase-1 mediates insulin signals to the actin cytoskeleton.";
Dong L.Q., Landa L.R., Wick M.J., Zhu L., Mukai H., Ono Y., Liu F.;
Proc. Natl. Acad. Sci. U.S.A. 97:5089-5094(2000).
Cited for: PHOSPHORYLATION AT THR-774 BY PDPK1, AND INTERACTION WITH PDPK1.

TOP