dbPTM

PKN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PKN2_HUMAN
UniProt AC	Q16513
Protein Name	Serine/threonine-protein kinase N2
Gene Name	PKN2
Organism	Homo sapiens (Human).
Sequence Length	984
Subcellular Localization	Cytoplasm . Nucleus . Membrane . Cell projection, lamellipodium . Cytoplasm, cytoskeleton . Cleavage furrow . Midbody . Cell junction . Colocalizes with PTPN13 in lamellipodia-like structures, regions of large actin turnover. Accumulates during telop
Protein Description	PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Phosphorylates HCV NS5B leading to stimulation of HCV RNA replication. Involved in the negative regulation of ciliogenesis. [PubMed: 27104747]
Protein Sequence	MASNPERGEILLTELQGDSRSLPFSENVSAVQKLDFSDTMVQQKLDDIKDRIKREIRKELKIKEGAENLRKVTTDKKSLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDITDCPRTPDTPNNDPRCSTSNNRLKALQKQLDIELKVKQGAENMIQMYSNGSSKDRKLHGTAQQLLQDSKTKIEVIRMQILQAVQTNELAFDNAKPVISPLELRMEELRHHFRIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNEVPKNHPKSRIIIEELSLVAASPTLSPRQSMISTQNQYSTLSKPAALTGTLEVRLMGCQDILENVPGRSKATSVALPGWSPSETRSSFMSRTSKSKSGSSRNLLKTDDLSNDVCAVLKLDNTVVGQTSWKPISNQSWDQKFTLELDRSRELEISVYWRDWRSLCAVKFLRLEDFLDNQRHGMCLYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPTVNHSGTFSPQAPVPTTVPVVDVRIPQLAPPASDSTVTKLDFDLEPEPPPAPPRASSLGEIDESSELRVLDIPGQDSETVFDIQNDRNSILPKSQSEYKPDTPQSGLEYSGIQELEDRRSQQRFQFNLQDFRCCAVLGRGHFGKVLLAEYKNTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHTDVFSEPRAVFYAACVVLGLQYLHEHKIVYRDLKLDNLLLDTEGFVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNPERRLGASEKDAEDVKKHPFFRLIDWSALMDKKVKPPFIPTIRGREDVSNFDDEFTSEAPILTPPREPRILSEEEQEMFRDFDYIADWC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASNPERGE ------CCCCCCCCC	20.29	-
3	Phosphorylation	-----MASNPERGEI -----CCCCCCCCCE	52.17	25159151
10 (in isoform 4)	Phosphorylation	-	4.21	22210691
21	Phosphorylation	ELQGDSRSLPFSENV EECCCCCCCCCCCCC	44.33	30266825
25	Phosphorylation	DSRSLPFSENVSAVQ CCCCCCCCCCCCHHE	26.73	30266825
27	Ubiquitination	RSLPFSENVSAVQKL CCCCCCCCCCHHEEC	31.67	29967540
29	Phosphorylation	LPFSENVSAVQKLDF CCCCCCCCHHEECCC	34.01	25159151
39	Phosphorylation	QKLDFSDTMVQQKLD EECCCCHHHHHHHHH	20.31	28857561
40	Sulfoxidation	KLDFSDTMVQQKLDD ECCCCHHHHHHHHHH	2.84	21406390
44	Ubiquitination	SDTMVQQKLDDIKDR CHHHHHHHHHHHHHH	36.47	32015554
58	Acetylation	RIKREIRKELKIKEG HHHHHHHHHCCHHHH	73.41	7266301
59	Ubiquitination	IKREIRKELKIKEGA HHHHHHHHCCHHHHH	45.51	21963094
77	Acetylation	RKVTTDKKSLAYVDN HHHCCCHHHHHHHHH	54.21	25953088
77	Ubiquitination	RKVTTDKKSLAYVDN HHHCCCHHHHHHHHH	54.21	19413330
78	Phosphorylation	KVTTDKKSLAYVDNI HHCCCHHHHHHHHHH	24.79	28152594
81	Phosphorylation	TDKKSLAYVDNILKK CCHHHHHHHHHHHHH	17.40	28152594
84	Ubiquitination	KSLAYVDNILKKSNK HHHHHHHHHHHHCCH	31.29	29967540
90	Ubiquitination	DNILKKSNKKLEELH HHHHHHCCHHHHHHH	55.12	32015554
110	Phosphorylation	LNAHIVVSDPEDITD HCCCEEECCHHHCCC	36.23	30266825
110	Ubiquitination	LNAHIVVSDPEDITD HCCCEEECCHHHCCC	36.23	29967540
115	Ubiquitination	VVSDPEDITDCPRTP EECCHHHCCCCCCCC	3.14	32015554
116	Phosphorylation	VSDPEDITDCPRTPD ECCHHHCCCCCCCCC	43.82	30576142
118	Glutathionylation	DPEDITDCPRTPDTP CHHHCCCCCCCCCCC	1.51	22555962
121	Phosphorylation	DITDCPRTPDTPNND HCCCCCCCCCCCCCC	15.62	25159151
124	Phosphorylation	DCPRTPDTPNNDPRC CCCCCCCCCCCCCCC	29.17	25159151
127	Ubiquitination	RTPDTPNNDPRCSTS CCCCCCCCCCCCCCC	62.96	24816145
143	Ubiquitination	NRLKALQKQLDIELK HHHHHHHHHHCCEEH	54.39	-
162	Phosphorylation	AENMIQMYSNGSSKD HHHHHHHHHCCCHHH	5.21	20068231
163	Phosphorylation	ENMIQMYSNGSSKDR HHHHHHHHCCCHHHH	29.40	25159151
166	Phosphorylation	IQMYSNGSSKDRKLH HHHHHCCCHHHHHHH	38.16	20068231
167	Phosphorylation	QMYSNGSSKDRKLHG HHHHCCCHHHHHHHH	39.72	25159151
171	Malonylation	NGSSKDRKLHGTAQQ CCCHHHHHHHHHHHH	55.77	26320211
171	Ubiquitination	NGSSKDRKLHGTAQQ CCCHHHHHHHHHHHH	55.77	29967540
183	Phosphorylation	AQQLLQDSKTKIEVI HHHHHHCCCHHHHHH	29.30	20873877
184	Ubiquitination	QQLLQDSKTKIEVIR HHHHHCCCHHHHHHH	63.23	29967540
193	Ubiquitination	KIEVIRMQILQAVQT HHHHHHHHHHHHHHC	24.32	29967540
228	Ubiquitination	ELRHHFRIEFAVAEG HHHHHHHHHHHHHHH	5.09	21963094
239	Ubiquitination	VAEGAKNVMKLLGSG HHHHHHHHHHHHCCC	3.36	21963094
241	Ubiquitination	EGAKNVMKLLGSGKV HHHHHHHHHHCCCCC	35.96	29967540
247	Acetylation	MKLLGSGKVTDRKAL HHHHCCCCCCCHHHH	43.59	27452117
247	Ubiquitination	MKLLGSGKVTDRKAL HHHHCCCCCCCHHHH	43.59	32015554
253	Ubiquitination	GKVTDRKALSEAQAR CCCCCHHHHHHHHHH	19.74	29967540
255	Phosphorylation	VTDRKALSEAQARFN CCCHHHHHHHHHHHH	35.43	20068231
264	Phosphorylation	AQARFNESSQKLDLL HHHHHHHHHHHHHHH	38.89	20873877
265	Phosphorylation	QARFNESSQKLDLLK HHHHHHHHHHHHHHH	25.75	28857561
267	2-Hydroxyisobutyrylation	RFNESSQKLDLLKYS HHHHHHHHHHHHHHH	46.01	-
267	Ubiquitination	RFNESSQKLDLLKYS HHHHHHHHHHHHHHH	46.01	29967540
272	Acetylation	SQKLDLLKYSLEQRL HHHHHHHHHHHHHHH	39.84	20167786
272	Ubiquitination	SQKLDLLKYSLEQRL HHHHHHHHHHHHHHH	39.84	32015554
273	Phosphorylation	QKLDLLKYSLEQRLN HHHHHHHHHHHHHHH	20.61	17494752
274	Phosphorylation	KLDLLKYSLEQRLNE HHHHHHHHHHHHHHH	24.68	17494752
284	Ubiquitination	QRLNEVPKNHPKSRI HHHHHCCCCCCCCCE	73.41	24816145
289	Phosphorylation	VPKNHPKSRIIIEEL CCCCCCCCCEEEEEH	32.91	20068231
297	Phosphorylation	RIIIEELSLVAASPT CEEEEEHHHHHCCCC	24.87	20873877
302	Phosphorylation	ELSLVAASPTLSPRQ EHHHHHCCCCCCHHH	14.53	29255136
304	Phosphorylation	SLVAASPTLSPRQSM HHHHCCCCCCHHHHH	37.06	30266825
306	Phosphorylation	VAASPTLSPRQSMIS HHCCCCCCHHHHHCC	22.10	30266825
310	Phosphorylation	PTLSPRQSMISTQNQ CCCCHHHHHCCCCCH	21.26	30576142
313	Phosphorylation	SPRQSMISTQNQYST CHHHHHCCCCCHHHC	18.46	29449344
314	Phosphorylation	PRQSMISTQNQYSTL HHHHHCCCCCHHHCC	22.18	29449344
318	Phosphorylation	MISTQNQYSTLSKPA HCCCCCHHHCCCCCC	15.92	23917254
323	Ubiquitination	NQYSTLSKPAALTGT CHHHCCCCCCHHCCC	41.61	-
338	Glutathionylation	LEVRLMGCQDILENV EEEEEECHHHHHHCC	1.73	22555962
345	Ubiquitination	CQDILENVPGRSKAT HHHHHHCCCCCCCCC	3.77	32015554
349	Phosphorylation	LENVPGRSKATSVAL HHCCCCCCCCCEEEC	32.34	-
350	Ubiquitination	ENVPGRSKATSVALP HCCCCCCCCCEEECC	55.08	29967540
352	Phosphorylation	VPGRSKATSVALPGW CCCCCCCCEEECCCC	27.72	23403867
353	Phosphorylation	PGRSKATSVALPGWS CCCCCCCEEECCCCC	15.39	23403867
360	Phosphorylation	SVALPGWSPSETRSS EEECCCCCCHHHHHH	25.18	19664994
360 (in isoform 2)	Phosphorylation	-	25.18	25159151
362	Phosphorylation	ALPGWSPSETRSSFM ECCCCCCHHHHHHHH	46.19	25159151
362 (in isoform 2)	Phosphorylation	-	46.19	25159151
364	Phosphorylation	PGWSPSETRSSFMSR CCCCCHHHHHHHHHC	39.94	25159151
364 (in isoform 2)	Phosphorylation	-	39.94	25159151
366	Phosphorylation	WSPSETRSSFMSRTS CCCHHHHHHHHHCCC	35.03	25159151
366 (in isoform 2)	Phosphorylation	-	35.03	25159151
367	Phosphorylation	SPSETRSSFMSRTSK CCHHHHHHHHHCCCC	22.98	25159151
367 (in isoform 2)	Phosphorylation	-	22.98	25159151
370	Phosphorylation	ETRSSFMSRTSKSKS HHHHHHHHCCCCCCC	30.32	25159151
370 (in isoform 2)	Phosphorylation	-	30.32	25159151
372	Phosphorylation	RSSFMSRTSKSKSGS HHHHHHCCCCCCCCC	32.95	29514088
373	Phosphorylation	SSFMSRTSKSKSGSS HHHHHCCCCCCCCCC	33.55	29514088
374	Ubiquitination	SFMSRTSKSKSGSSR HHHHCCCCCCCCCCC	62.38	29967540
375	Phosphorylation	FMSRTSKSKSGSSRN HHHCCCCCCCCCCCC	31.64	29038488
376	Methylation	MSRTSKSKSGSSRNL HHCCCCCCCCCCCCC	63.67	116252779
377	Phosphorylation	SRTSKSKSGSSRNLL HCCCCCCCCCCCCCC	51.50	29038488
379	Phosphorylation	TSKSKSGSSRNLLKT CCCCCCCCCCCCCCC	32.96	25159151
380	Phosphorylation	SKSKSGSSRNLLKTD CCCCCCCCCCCCCCC	28.81	29038488
385	Ubiquitination	GSSRNLLKTDDLSND CCCCCCCCCCCCCCC	53.74	21963094
394	Ubiquitination	DDLSNDVCAVLKLDN CCCCCCEEEEEEECC	2.12	29967540
402	Phosphorylation	AVLKLDNTVVGQTSW EEEEECCCEEEEECC	19.08	20873877
407	Phosphorylation	DNTVVGQTSWKPISN CCCEEEEECCEECCC	30.53	20873877
408	Phosphorylation	NTVVGQTSWKPISNQ CCEEEEECCEECCCC	25.80	20873877
408	Ubiquitination	NTVVGQTSWKPISNQ CCEEEEECCEECCCC	25.80	21963094
410	Ubiquitination	VVGQTSWKPISNQSW EEEEECCEECCCCCC	32.04	29967540
413	Phosphorylation	QTSWKPISNQSWDQK EECCEECCCCCCCCE	37.03	20873877
416	Phosphorylation	WKPISNQSWDQKFTL CEECCCCCCCCEEEE	36.55	20873877
426	Phosphorylation	QKFTLELDRSRELEI CEEEEEECCCCEEEE	36.81	32142685
428	Phosphorylation	FTLELDRSRELEISV EEEEECCCCEEEEEE	29.76	26091039
454	Ubiquitination	KFLRLEDFLDNQRHG EEEEHHHHHHCCCCE	7.24	32015554
458	Ubiquitination	LEDFLDNQRHGMCLY HHHHHHCCCCEEEEE	38.11	22817900
462	Ubiquitination	LDNQRHGMCLYLEPQ HHCCCCEEEEEECCC	0.86	29967540
468	Ubiquitination	GMCLYLEPQGTLFAE EEEEEECCCCEEEEE	34.99	29967540
486	Ubiquitination	FNPVIERRPKLQRQK CCHHHHCCHHHHHHH	21.66	32015554
497	Phosphorylation	QRQKKIFSKQQGKTF HHHHHHHHHHCCCCH	32.78	23401153
498	Ubiquitination	RQKKIFSKQQGKTFL HHHHHHHHHCCCCHH	35.57	-
501	Ubiquitination	KIFSKQQGKTFLRAP HHHHHHCCCCHHCCC	28.60	21963094
502	Ubiquitination	IFSKQQGKTFLRAPQ HHHHHCCCCHHCCCC	31.59	32015554
503	Phosphorylation	FSKQQGKTFLRAPQM HHHHCCCCHHCCCCC	34.42	27251275
503	Ubiquitination	FSKQQGKTFLRAPQM HHHHCCCCHHCCCCC	34.42	21963094
516	Phosphorylation	QMNINIATWGRLVRR CCCEEHHHHHHHHHH	25.34	30576142
517	Ubiquitination	MNINIATWGRLVRRA CCEEHHHHHHHHHHH	4.85	21963094
520	Ubiquitination	NIATWGRLVRRAIPT EHHHHHHHHHHHCCC	2.87	29967540
527	Phosphorylation	LVRRAIPTVNHSGTF HHHHHCCCCCCCCCC	28.03	28176443
531	Phosphorylation	AIPTVNHSGTFSPQA HCCCCCCCCCCCCCC	34.03	30266825
533	Phosphorylation	PTVNHSGTFSPQAPV CCCCCCCCCCCCCCC	24.77	30266825
535	Phosphorylation	VNHSGTFSPQAPVPT CCCCCCCCCCCCCCC	18.88	30266825
542	Phosphorylation	SPQAPVPTTVPVVDV CCCCCCCCCCEEEEE	40.43	24732914
543	Phosphorylation	PQAPVPTTVPVVDVR CCCCCCCCCEEEEEE	19.42	24732914
549	Ubiquitination	TTVPVVDVRIPQLAP CCCEEEEEECCCCCC	3.95	21963094
559	Phosphorylation	PQLAPPASDSTVTKL CCCCCCCCCCCCEEE	37.56	15822905
561	Phosphorylation	LAPPASDSTVTKLDF CCCCCCCCCCEEECC	23.45	15822905
562	Phosphorylation	APPASDSTVTKLDFD CCCCCCCCCEEECCC	36.87	23828894
564	Phosphorylation	PASDSTVTKLDFDLE CCCCCCCEEECCCCC	26.44	26074081
565	Ubiquitination	ASDSTVTKLDFDLEP CCCCCCEEECCCCCC	41.54	21963094
567	Phosphorylation	DSTVTKLDFDLEPEP CCCCEEECCCCCCCC	36.25	32142685
571	Ubiquitination	TKLDFDLEPEPPPAP EEECCCCCCCCCCCC	49.84	29967540
577	Ubiquitination	LEPEPPPAPPRASSL CCCCCCCCCCCCCCC	32.29	29967540
582	Phosphorylation	PPAPPRASSLGEIDE CCCCCCCCCCCCCCC	27.63	29255136
583	Phosphorylation	PAPPRASSLGEIDES CCCCCCCCCCCCCCC	39.13	29255136
590	Phosphorylation	SLGEIDESSELRVLD CCCCCCCCCCEEEEE	25.93	25159151
591	Phosphorylation	LGEIDESSELRVLDI CCCCCCCCCEEEEEC	38.31	23927012
603	Phosphorylation	LDIPGQDSETVFDIQ EECCCCCCCEEEEEC	27.55	20873877
603	Ubiquitination	LDIPGQDSETVFDIQ EECCCCCCCEEEEEC	27.55	29967540
604	Ubiquitination	DIPGQDSETVFDIQN ECCCCCCCEEEEECC	58.23	27667366
605	Phosphorylation	IPGQDSETVFDIQND CCCCCCCEEEEECCC	30.35	29978859
609	Ubiquitination	DSETVFDIQNDRNSI CCCEEEEECCCCCCC	2.54	29967540
613	Methylation	VFDIQNDRNSILPKS EEEECCCCCCCCCCC	46.47	115487703
615	Phosphorylation	DIQNDRNSILPKSQS EECCCCCCCCCCCCC	26.79	20068231
619	Ubiquitination	DRNSILPKSQSEYKP CCCCCCCCCCCCCCC	58.65	29967540
620	Phosphorylation	RNSILPKSQSEYKPD CCCCCCCCCCCCCCC	36.68	29978859
622	Phosphorylation	SILPKSQSEYKPDTP CCCCCCCCCCCCCCC	50.40	29978859
624	Phosphorylation	LPKSQSEYKPDTPQS CCCCCCCCCCCCCCC	32.82	28796482
625	Ubiquitination	PKSQSEYKPDTPQSG CCCCCCCCCCCCCCC	32.16	29967540
627	Ubiquitination	SQSEYKPDTPQSGLE CCCCCCCCCCCCCCC	67.86	22817900
628	Phosphorylation	QSEYKPDTPQSGLEY CCCCCCCCCCCCCCC	31.58	25159151
629	Ubiquitination	SEYKPDTPQSGLEYS CCCCCCCCCCCCCCC	33.45	29967540
631	Phosphorylation	YKPDTPQSGLEYSGI CCCCCCCCCCCCCCC	46.69	30175587
635	Phosphorylation	TPQSGLEYSGIQELE CCCCCCCCCCCHHHH	19.76	21712546
636	Phosphorylation	PQSGLEYSGIQELED CCCCCCCCCCHHHHH	21.75	21712546
646	Phosphorylation	QELEDRRSQQRFQFN HHHHHHHHHHCCEEC	31.40	30576142
658	Phosphorylation	QFNLQDFRCCAVLGR EECCHHHHHHEEECC	23.93	32142685
658	Ubiquitination	QFNLQDFRCCAVLGR EECCHHHHHHEEECC	23.93	29901268
659	Phosphorylation	FNLQDFRCCAVLGRG ECCHHHHHHEEECCC	1.44	32142685
661	Ubiquitination	LQDFRCCAVLGRGHF CHHHHHHEEECCCCC	11.82	29967540
663	Phosphorylation	DFRCCAVLGRGHFGK HHHHHEEECCCCCHH	1.74	32142685
676	Phosphorylation	GKVLLAEYKNTNEMF HHHEEEECCCCCCCC	12.16	28102081
677	Ubiquitination	KVLLAEYKNTNEMFA HHEEEECCCCCCCCH	49.12	29967540
686	Acetylation	TNEMFAIKALKKGDI CCCCCHHHHHHHCCE	44.21	19820183
690	Ubiquitination	FAIKALKKGDIVARD CHHHHHHHCCEEEHH	63.77	29901268
701	Phosphorylation	VARDEVDSLMCEKRI EEHHHHHHHHHHHHH	24.15	30576142
706	2-Hydroxyisobutyrylation	VDSLMCEKRIFETVN HHHHHHHHHHHHHHH	45.96	-
706	Acetylation	VDSLMCEKRIFETVN HHHHHHHHHHHHHHH	45.96	26051181
706	Ubiquitination	VDSLMCEKRIFETVN HHHHHHHHHHHHHHH	45.96	29901268
720	Ubiquitination	NSVRHPFLVNLFACF HHCCCCHHHHHHHHC	2.69	22817900
722	Ubiquitination	VRHPFLVNLFACFQT CCCCHHHHHHHHCCC	31.43	22817900
729	Phosphorylation	NLFACFQTKEHVCFV HHHHHCCCCCEEEEE	20.39	24719451
736	Ubiquitination	TKEHVCFVMEYAAGG CCCEEEEEEEECCCC	2.11	22817900
767	Phosphorylation	VFYAACVVLGLQYLH HHHHHHHHHHHHHHH	3.36	32142685
768	Phosphorylation	FYAACVVLGLQYLHE HHHHHHHHHHHHHHH	2.56	32142685
768	Ubiquitination	FYAACVVLGLQYLHE HHHHHHHHHHHHHHH	2.56	22817900
771	Ubiquitination	ACVVLGLQYLHEHKI HHHHHHHHHHHHCCE	36.62	29967540
772	Phosphorylation	CVVLGLQYLHEHKIV HHHHHHHHHHHCCEE	18.31	32142685
773	Ubiquitination	VVLGLQYLHEHKIVY HHHHHHHHHHCCEEE	2.17	32015554
784	Ubiquitination	KIVYRDLKLDNLLLD CEEECCCCCCCEEEC	59.07	21906983
792	Phosphorylation	LDNLLLDTEGFVKIA CCCEEECCCCCEEHH	37.67	27251275
799	Phosphorylation	TEGFVKIADFGLCKE CCCCEEHHHCCCCCC	10.60	32142685
800	Phosphorylation	EGFVKIADFGLCKEG CCCEEHHHCCCCCCC	41.44	32142685
801	Phosphorylation	GFVKIADFGLCKEGM CCEEHHHCCCCCCCC	6.26	32645325
804	Phosphorylation	KIADFGLCKEGMGYG EHHHCCCCCCCCCCC	3.74	32142685
805	Ubiquitination	IADFGLCKEGMGYGD HHHCCCCCCCCCCCC	63.45	-
810	Phosphorylation	LCKEGMGYGDRTSTF CCCCCCCCCCCCCCC	13.63	22322096
814	Phosphorylation	GMGYGDRTSTFCGTP CCCCCCCCCCCCCCC	36.54	22322096
815	Phosphorylation	MGYGDRTSTFCGTPE CCCCCCCCCCCCCCC	22.00	22322096
816	Phosphorylation	GYGDRTSTFCGTPEF CCCCCCCCCCCCCCC	23.49	22322096
820	Phosphorylation	RTSTFCGTPEFLAPE CCCCCCCCCCCCCHH	22.33	21712546
832	Phosphorylation	APEVLTETSYTRAVD CHHHHCCCCCCCCHH	23.07	28985074
834	Phosphorylation	EVLTETSYTRAVDWW HHHCCCCCCCCHHHH	13.99	28985074
866	Ubiquitination	GDDEEEVFDSIVNDE CCCHHHHHHHHHCCC	7.44	27667366
868	Ubiquitination	DEEEVFDSIVNDEVR CHHHHHHHHHCCCCC	19.57	27667366
880	Ubiquitination	EVRYPRFLSTEAISI CCCCCCCCCHHHHHH	6.99	29967540
882	Phosphorylation	RYPRFLSTEAISIMR CCCCCCCHHHHHHHH	31.42	20860994
882	Ubiquitination	RYPRFLSTEAISIMR CCCCCCCHHHHHHHH	31.42	32015554
903	Phosphorylation	PERRLGASEKDAEDV HHHCCCCCCCCHHHH	43.30	23403867
910	Phosphorylation	SEKDAEDVKKHPFFR CCCCHHHHHHCCHHH	7.19	32645325
912	Ubiquitination	KDAEDVKKHPFFRLI CCHHHHHHCCHHHCC	57.25	29967540
914	Ubiquitination	AEDVKKHPFFRLIDW HHHHHHCCHHHCCCH	38.66	32015554
928	Ubiquitination	WSALMDKKVKPPFIP HHHHCCCCCCCCCCC	51.75	29967540
930	Ubiquitination	ALMDKKVKPPFIPTI HHCCCCCCCCCCCCC	56.72	32015554
942	Phosphorylation	PTIRGREDVSNFDDE CCCCCCCCCCCCCCC	48.02	32645325
944	Phosphorylation	IRGREDVSNFDDEFT CCCCCCCCCCCCCCC	44.06	20873877
951	Phosphorylation	SNFDDEFTSEAPILT CCCCCCCCCCCCCCC	24.49	23927012
952	Phosphorylation	NFDDEFTSEAPILTP CCCCCCCCCCCCCCC	36.76	22167270
958	Phosphorylation	TSEAPILTPPREPRI CCCCCCCCCCCCCCC	31.78	29255136
967	Phosphorylation	PREPRILSEEEQEMF CCCCCCCCHHHHHHH	40.36	26074081

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
535	S	Phosphorylation	Kinase	CDK1	P06493	PSP
816	T	Phosphorylation	Kinase	PDK1	Q15118	GPS
816	T	Phosphorylation	Kinase	PDK1	O15530	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PKN2_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 PKN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTN13_HUMAN	PTPN13	physical	11356191
AKT1_HUMAN	AKT1	physical	10926925
RHOA_HUMAN	RHOA	physical	9446575
PDPK1_HUMAN	PDPK1	physical	10764742
PKN2_HUMAN	PKN2	physical	10818102
HDAC5_HUMAN	HDAC5	physical	20188095
CC136_HUMAN	CCDC136	physical	21900206
SCG1_HUMAN	CHGB	physical	21900206
MYO9B_HUMAN	MYO9B	physical	21900206
F193B_HUMAN	FAM193B	physical	21900206
EIF3G_HUMAN	EIF3G	physical	21900206
EF1A1_HUMAN	EEF1A1	physical	21900206
GCP60_HUMAN	ACBD3	physical	26344197
LSM2_HUMAN	LSM2	physical	26344197
LSM3_HUMAN	LSM3	physical	26344197
LSM4_HUMAN	LSM4	physical	26344197
LSM6_HUMAN	LSM6	physical	26344197
LSM7_HUMAN	LSM7	physical	26344197
PPM1B_HUMAN	PPM1B	physical	26344197
RPE_HUMAN	RPE	physical	26344197
AT2A2_HUMAN	ATP2A2	physical	26496610
BTF3_HUMAN	BTF3	physical	26496610
SYDC_HUMAN	DARS	physical	26496610
EF1D_HUMAN	EEF1D	physical	26496610
EF1G_HUMAN	EEF1G	physical	26496610
SYEP_HUMAN	EPRS	physical	26496610
SYIC_HUMAN	IARS	physical	26496610
SYK_HUMAN	KARS	physical	26496610
KTN1_HUMAN	KTN1	physical	26496610
SYMC_HUMAN	MARS	physical	26496610
SYRC_HUMAN	RARS	physical	26496610
SOAT1_HUMAN	SOAT1	physical	26496610
SYVC_HUMAN	VARS	physical	26496610
SGPL1_HUMAN	SGPL1	physical	26496610
VAPB_HUMAN	VAPB	physical	26496610
MCA3_HUMAN	EEF1E1	physical	26496610
ERLN1_HUMAN	ERLIN1	physical	26496610
CKAP4_HUMAN	CKAP4	physical	26496610
TRAM1_HUMAN	TRAM1	physical	26496610
SYLC_HUMAN	LARS	physical	26496610
WDR74_HUMAN	WDR74	physical	26496610
MBOA7_HUMAN	MBOAT7	physical	26496610
TRM1L_HUMAN	TRMT1L	physical	26496610
TMUB1_HUMAN	TMUB1	physical	26496610
RABL3_HUMAN	RABL3	physical	26496610

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 PKN2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-360 AND SER-583, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582; SER-583 ANDTHR-814, AND MASS SPECTROMETRY.	19369195 [Abstract]
"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-360 AND SER-583, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-110; THR-121; THR-124;SER-302; SER-306; SER-360; SER-362; SER-535; THR-628; SER-631 ANDTHR-958, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-302; SER-306; SER-360;SER-535; SER-583 AND THR-958, AND MASS SPECTROMETRY.	18691976 [Abstract]
"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 SER-360; SER-531 ANDSER-535, AND MASS SPECTROMETRY.	18220336 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-531 AND SER-535, ANDMASS SPECTROMETRY.	17924679 [Abstract]
"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-302; SER-306 ANDSER-360, AND MASS SPECTROMETRY.	16964243 [Abstract]
"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-289; SER-583 ANDTHR-958, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Phosphoproteomic analysis of synaptosomes from human cerebralcortex."; DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P.,Pant H.C., Dosemeci A.; J. Proteome Res. 4:306-315(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 AND SER-561, ANDMASS SPECTROMETRY.	15822905 [Abstract]
"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-582 AND THR-816, ANDMASS SPECTROMETRY.	15302935 [Abstract]
"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-816 BY PDPK1, AND INTERACTION WITH PDPK1.	10792047 [Abstract]