dbPTM

PKN1_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PKN1_RAT
UniProt AC	Q63433
Protein Name	Serine/threonine-protein kinase N1
Gene Name	Pkn1
Organism	Rattus norvegicus (Rat).
Sequence Length	946
Subcellular Localization	Cytoplasm . Nucleus . Endosome . Cell membrane Peripheral membrane protein . Cleavage furrow . Midbody . Associates with chromatin in a ligand-dependent manner (By similarity). Localization to endosomes is mediated via its interaction with RHOB. Ac
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. [PubMed: 8051089]
Protein Sequence	MAGDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLKREIRKELKLKEGAENLRRATTDLGRSLAPVELLLRGSARRLDLLHQQLQELHAHVVLPDPTAGSDAPQSLAEGSPVCSSTNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQALQAGQLESQAAPDEAHGDPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLRESLERRLGELPADHPKGRLLREELTAASSAAFSAILPGPFPATHYSTLSKPAPLTGTLEVRVVGCKNLPETIPWSPPPSVGASGTPDSRTPFLSRPARGLYNRSGSLSGRSSLKGEAENSTEVSTVLKLDNTVVGQTAWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPIIERIPRLQRQKKIFSKQQGQTFQRARQMNIDVATWVRLLRRLIPNAVATGSFSPNASPGSEIRSTGDISMEKLNLGADSDSSSQKSPAGLPSTSCSLSSPTHESTTSPELPSETQETPGPGLCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFHSSGELFAIKALKKGDIVARDEVESLMCEKRILATVTRAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAVFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSTERDAEDVKKQPFFRTLDWDALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFRDFDFVAGGY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGDAVQSE ------CCCHHHCCC	25.27	-
64	Phosphorylation	ENLRRATTDLGRSLA HHHHHHHHHHCCCCH	28.39	8943281
69	Phosphorylation	ATTDLGRSLAPVELL HHHHHCCCCHHHHHH	27.38	-
375	Phosphorylation	ARGLYNRSGSLSGRS CCCCCCCCCCCCCCC	29.15	25575281
377	Phosphorylation	GLYNRSGSLSGRSSL CCCCCCCCCCCCCCC	22.17	15375078
379	Phosphorylation	YNRSGSLSGRSSLKG CCCCCCCCCCCCCCC	33.58	25575281
382	Phosphorylation	SGSLSGRSSLKGEAE CCCCCCCCCCCCCCC	43.48	25575281
383	Phosphorylation	GSLSGRSSLKGEAEN CCCCCCCCCCCCCCC	32.51	25575281
451	Acetylation	LCALKFLKLEDFLDN CCHHEEECHHHHHCC	53.62	-
504	Phosphorylation	FSKQQGQTFQRARQM HHHHHHHHHHHHHHC	28.67	8943281
532	Phosphorylation	LIPNAVATGSFSPNA HCCCCCCCCCCCCCC	27.10	28432305
534	Phosphorylation	PNAVATGSFSPNASP CCCCCCCCCCCCCCC	20.42	27097102
536	Phosphorylation	AVATGSFSPNASPGS CCCCCCCCCCCCCCC	20.95	28432305
540	Phosphorylation	GSFSPNASPGSEIRS CCCCCCCCCCCCCCC	36.11	28432305
543	Phosphorylation	SPNASPGSEIRSTGD CCCCCCCCCCCCCCC	32.98	28432305
562	Phosphorylation	KLNLGADSDSSSQKS CCCCCCCCCCCCCCC	38.57	27097102
564	Phosphorylation	NLGADSDSSSQKSPA CCCCCCCCCCCCCCC	35.52	27097102
565	Phosphorylation	LGADSDSSSQKSPAG CCCCCCCCCCCCCCC	41.60	27097102
566	Phosphorylation	GADSDSSSQKSPAGL CCCCCCCCCCCCCCC	45.65	27097102
569	Phosphorylation	SDSSSQKSPAGLPST CCCCCCCCCCCCCCC	16.61	27097102
575	Phosphorylation	KSPAGLPSTSCSLSS CCCCCCCCCCCCCCC	37.69	27097102
576	Phosphorylation	SPAGLPSTSCSLSSP CCCCCCCCCCCCCCC	31.64	27097102
577	Phosphorylation	PAGLPSTSCSLSSPT CCCCCCCCCCCCCCC	13.17	27097102
579	Phosphorylation	GLPSTSCSLSSPTHE CCCCCCCCCCCCCCC	30.93	27097102
581	Phosphorylation	PSTSCSLSSPTHEST CCCCCCCCCCCCCCC	20.27	27097102
582	Phosphorylation	STSCSLSSPTHESTT CCCCCCCCCCCCCCC	38.83	27097102
584	Phosphorylation	SCSLSSPTHESTTSP CCCCCCCCCCCCCCC	39.98	27097102
587	Phosphorylation	LSSPTHESTTSPELP CCCCCCCCCCCCCCC	29.40	27097102
588	Phosphorylation	SSPTHESTTSPELPS CCCCCCCCCCCCCCC	28.45	27097102
589	Phosphorylation	SPTHESTTSPELPSE CCCCCCCCCCCCCCC	52.11	27097102
590	Phosphorylation	PTHESTTSPELPSET CCCCCCCCCCCCCCC	19.23	27097102
595	Phosphorylation	TTSPELPSETQETPG CCCCCCCCCCCCCCC	66.94	27097102
597	Phosphorylation	SPELPSETQETPGPG CCCCCCCCCCCCCCC	35.72	27097102
612	Phosphorylation	LCSPLRKSPLTLEDF CCCCCCCCCCCHHHH	20.78	8943281
776	Phosphorylation	GMGYGDRTSTFCGTP CCCCCCCCCCCCCCC	36.54	21738781
777	Phosphorylation	MGYGDRTSTFCGTPE CCCCCCCCCCCCCCH	22.00	27097102
778	Phosphorylation	GYGDRTSTFCGTPEF CCCCCCCCCCCCCHH	23.49	27097102
782	Phosphorylation	RTSTFCGTPEFLAPE CCCCCCCCCHHHCCH	22.33	21738781
913	Phosphorylation	SNFDEEFTGEAPTLS CCCCHHHCCCCCCCC	37.07	30181290
918	Phosphorylation	EFTGEAPTLSPPRDA HHCCCCCCCCCCCCC	47.09	27097102
920	Phosphorylation	TGEAPTLSPPRDARP CCCCCCCCCCCCCCC	35.02	23712012

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
64	T	Phosphorylation	Kinase	PKN1	Q63433	PSP
377	S	Phosphorylation	Kinase	PKN1	Q63433	PSP
504	T	Phosphorylation	Kinase	PKN1	Q63433	PSP
534	S	Phosphorylation	Kinase	PKN1	Q63433	PSP
577	S	Phosphorylation	Kinase	PKN1	Q63433	PSP
579	S	Phosphorylation	Kinase	PKN1	Q63433	PSP
612	S	Phosphorylation	Kinase	PKN1	Q63433	PSP
778	T	Phosphorylation	Kinase	PDK1	O55173	GPS
778	T	Phosphorylation	Kinase	PKN1	Q63433	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PKN1_RAT !!

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
ZFAN6_MOUSE	Zfand6	physical	11054541

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PKN1_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Signaling via a novel integral plasma membrane pool of aserine/threonine protein kinase PRK1 in mammalian cells."; Zhu Y., Stolz D.B., Guo F., Ross M.A., Watkins S.C., Tan B.J.,Qi R.Z., Manser E., Li Q.T., Bay B.H., Teo T.S., Duan W.; FASEB J. 18:1722-1724(2004). Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-377.	15375078 [Abstract]