NUAK1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NUAK1_MOUSE
• UniProt AC: Q641K5
• Protein Name: NUAK family SNF1-like kinase 1
• Gene Name: Nuak1
• Organism: Mus musculus (Mouse).
• Sequence Length: 658
• Subcellular Localization: Nucleus. Cytoplasm.
• Protein Description: Serine/threonine-protein kinase involved in various processes such as cell adhesion, regulation of cell ploidy and senescence, cell proliferation and tumor progression. Phosphorylates ATM, CASP6, LATS1, PPP1R12A and p53/TP53. Acts as a regulator of cellular senescence and cellular ploidy by mediating phosphorylation of 'Ser-464' of LATS1, thereby controlling its stability. Controls cell adhesion by regulating activity of the myosin protein phosphatase 1 (PP1) complex. Acts by mediating phosphorylation of PPP1R12A subunit of myosin PP1: phosphorylated PPP1R12A then interacts with 14-3-3, leading to reduced dephosphorylation of myosin MLC2 by myosin PP1. May be involved in DNA damage response: phosphorylates p53/TP53 at 'Ser-15' and 'Ser-392' and is recruited to the CDKN1A/WAF1 promoter to participate to transcription activation by p53/TP53. May also act as a tumor malignancy-associated factor by promoting tumor invasion and metastasis under regulation and phosphorylation by AKT1. Suppresses Fas-induced apoptosis by mediating phosphorylation of CASP6, thereby suppressing the activation of the caspase and the subsequent cleavage of CFLAR. Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with STK11, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair..
• Protein Sequence: MEGAAVSAAGDGPAVETGLPGSPLEAVAGATAAPVEPRKPHGVKRHHHKHNLKHRYELQETLGKGTYGKVKRATERFSGRVVAIKSIRKDKIKDELDMVHIRREIEIMSSLNHPHIISIYEVFENKDKIVIIMEYASKGELYDYISERRRLSERETRHFFRQIVSAVHYCHKNGVVHRDLKLENILLDDNCNIKIADFGLSNLYQKDKFLQTFCGSPLYASPEIVNGRPYRGPEVDSWALGVLLYTLIYGTMPFDGFDHKNLIRQISSGEYREPTQPSDARGLIRWMLMVNPDRRATIEDIANHWWVNWGYKSSVCDCDALPDSESPLLARIIDWHHRSTGLQAEAEAKMKGLAKPGASEVVLERQRSLKKSKKENDFPQSGQDSVPESPSKLSSKRPKGILKKRSNSEHRSHSTGFIEGIVSPALPSPFKMEQDLCRTAIPLPSSPEADMSGKLSLKQSATMPKKGILKKTQQRESGYYSSPERSESSELLDSNDVVISGGLSSPPPDPARGTSHSLSCRRKGILKHSSRYSDGGTDPALTRPEMPTLESLSPPGVPSDGISRSYSRPSSIISDDSVLSSDSFDLLELQENRPARQRIRSCVSAENFLQLQDFETPHNRPRPQYLKRLADSSFSLLTDMDDVTQVYKKALEICSKLN

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
1	Acetylation	-------MEGAAVSA -------CCCCCCCC	10.93	-
22	Phosphorylation	VETGLPGSPLEAVAG CCCCCCCCCHHHHCC	25.11	25338131
86	Phosphorylation	GRVVAIKSIRKDKIK CEEEEEEEHHHHHCC	22.85	-
142	Phosphorylation	YASKGELYDYISERR ECCCCCHHHHHHHHH	11.46	-
146	Phosphorylation	GELYDYISERRRLSE CCHHHHHHHHHCCCH	20.87	-
212	Phosphorylation	QKDKFLQTFCGSPLY CCCHHHHHHCCCCCC	24.04	-
326	Phosphorylation	DALPDSESPLLARII CCCCCCCCHHHHHHH	25.46	25521595
368	Phosphorylation	VVLERQRSLKKSKKE HHHHHHHHHHHHHHC	35.88	-
385	Phosphorylation	FPQSGQDSVPESPSK CCCCCCCCCCCCCCC	31.51	28066266
389	Phosphorylation	GQDSVPESPSKLSSK CCCCCCCCCCCCCCC	28.53	26824392
391	Phosphorylation	DSVPESPSKLSSKRP CCCCCCCCCCCCCCC	56.35	28066266
412	Phosphorylation	RSNSEHRSHSTGFIE CCCCCCCCCCCCCCH	24.56	26160508
414	Phosphorylation	NSEHRSHSTGFIEGI CCCCCCCCCCCCHHC	31.32	26160508
415	Phosphorylation	SEHRSHSTGFIEGIV CCCCCCCCCCCHHCC	30.59	26160508
445	Phosphorylation	RTAIPLPSSPEADMS HCCCCCCCCCCCCCC	67.23	28066266
446	Phosphorylation	TAIPLPSSPEADMSG CCCCCCCCCCCCCCC	25.48	25521595
452	Phosphorylation	SSPEADMSGKLSLKQ CCCCCCCCCCCCHHH	33.07	28066266
456	Phosphorylation	ADMSGKLSLKQSATM CCCCCCCCHHHCCCC	36.69	-
553	Phosphorylation	MPTLESLSPPGVPSD CCCCHHCCCCCCCCC	38.02	25338131
563	Phosphorylation	GVPSDGISRSYSRPS CCCCCCCCCCCCCCH	22.24	23737553
565	Phosphorylation	PSDGISRSYSRPSSI CCCCCCCCCCCCHHC	22.22	23737553
566	Phosphorylation	SDGISRSYSRPSSII CCCCCCCCCCCHHCC	13.95	20531401
567	Phosphorylation	DGISRSYSRPSSIIS CCCCCCCCCCHHCCC	38.67	25521595
570	Phosphorylation	SRSYSRPSSIISDDS CCCCCCCHHCCCCCC	32.81	25521595
581	Phosphorylation	SDDSVLSSDSFDLLE CCCCCCCCCCCCHHH	32.87	25521595
601	Phosphorylation	PARQRIRSCVSAENF HHHHHHHHHHCHHHH	19.25	29899451
632	Phosphorylation	YLKRLADSSFSLLTD HHHHHHHCCCCCCCC	27.89	29899451
633	Phosphorylation	LKRLADSSFSLLTDM HHHHHHCCCCCCCCH	21.28	29899451
638	Phosphorylation	DSSFSLLTDMDDVTQ HCCCCCCCCHHHHHH	34.27	-

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
212	T	Phosphorylation	Kinase	LKB1	Q9WTK7	Uniprot
601	S	Phosphorylation	Kinase	AKT1	P31750	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
29	K	Phosphorylation	Ubiquitinated with 'Lys-29'- and 'Lys-33'-linked polyubiquitins which appear to impede LKB1-mediated phosphorylation.	-
29	K	ubiquitylation	Ubiquitinated with 'Lys-29'- and 'Lys-33'-linked polyubiquitins which appear to impede LKB1-mediated phosphorylation.	-
212	T	Phosphorylation	Phosphorylated at Thr-212 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NUAK1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of NUAK1_MOUSE !!

Drug and Disease Associations

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