NUAK2_HUMAN - dbPTM
NUAK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUAK2_HUMAN
UniProt AC Q9H093
Protein Name NUAK family SNF1-like kinase 2
Gene Name NUAK2 {ECO:0000312|EMBL:AAH17306.1}
Organism Homo sapiens (Human).
Sequence Length 628
Subcellular Localization
Protein Description Stress-activated kinase involved in tolerance to glucose starvation. Induces cell-cell detachment by increasing F-actin conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required for the increased motility and invasiveness of CD95-activated tumor cells. Able to phosphorylate 'Ser-464' of LATS1..
Protein Sequence MESLVFARRSGPTPSAAELARPLAEGLIKSPKPLMKKQAVKRHHHKHNLRHRYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLMHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLYDYISERQQLSEREARHFFRQIVSAVHYCHQNRVVHRDLKLENILLDANGNIKIADFGLSNLYHQGKFLQTFCGSPLYASPEIVNGKPYTGPEVDSWSLGVLLYILVHGTMPFDGHDHKILVKQISNGAYREPPKPSDACGLIRWLLMVNPTRRATLEDVASHWWVNWGYATRVGEQEAPHEGGHPGSDSARASMADWLRRSSRPLLENGAKVCSFFKQHAPGGGSTTPGLERQHSLKKSRKENDMAQSLHSDTADDTAHRPGKSNLKLPKGILKKKVSASAEGVQEDPPELSPIPASPGQAAPLLPKKGILKKPRQRESGYYSSPEPSESGELLDAGDVFVSGDPKEQKPPQASGLLLHRKGILKLNGKFSQTALELAAPTTFGSLDELAPPRPLARASRPSGAVSEDSILSSESFDQLDLPERLPEPPLRGCVSVDNLTGLEEPPSEGPGSCLRRWRQDPLGDSCFSLTDCQEVTATYRQALRVCSKLT
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
1Acetylation-------MESLVFAR
-------CCCCEECC		7.7222814378
30PhosphorylationLAEGLIKSPKPLMKK
HHHHHCCCCHHHHCH		31.0330576142
58PhosphorylationHRYEFLETLGKGTYG
HHHHHHHHHCCCCCC		42.85-
64PhosphorylationETLGKGTYGKVKKAR
HHHCCCCCCCHHHHH		24.5020049867
73PhosphorylationKVKKARESSGRLVAI
CHHHHHHCCCCEEEE		32.3229038488
74PhosphorylationVKKARESSGRLVAIK
HHHHHHCCCCEEEEE		24.1529038488
125UbiquitinationVFENSSKIVIVMEYA
HHHCCCEEEEEEEEC		2.49-
131PhosphorylationKIVIVMEYASRGDLY
EEEEEEEECCCCCHH		7.5622817900
133PhosphorylationVIVMEYASRGDLYDY
EEEEEECCCCCHHHH		35.5725072903
138PhosphorylationYASRGDLYDYISERQ
ECCCCCHHHHHHHHH		16.0825072903
140PhosphorylationSRGDLYDYISERQQL
CCCCHHHHHHHHHHC		7.8725072903
142PhosphorylationGDLYDYISERQQLSE
CCHHHHHHHHHHCCH		22.0925072903
208PhosphorylationHQGKFLQTFCGSPLY
HCCCHHHHHCCCCCC		24.0414976552
252PhosphorylationHGTMPFDGHDHKILV
HCCCCCCCCCCEEEE		28.6214976552
267PhosphorylationKQISNGAYREPPKPS
EEECCCCCCCCCCHH		19.5319702290
289PhosphorylationWLLMVNPTRRATLED
HHHHHCCCCCCCHHH		27.8128270605
311PhosphorylationNWGYATRVGEQEAPH
CCCCEEEECCCCCCC		9.57-
355AcetylationAKVCSFFKQHAPGGG
HHHHHHHHHHCCCCC		38.8826051181
416PhosphorylationGILKKKVSASAEGVQ
CHHHHHHCCCCCCCC		25.9425627689
418PhosphorylationLKKKVSASAEGVQED
HHHHHCCCCCCCCCC		21.2425627689
430PhosphorylationQEDPPELSPIPASPG
CCCCCCCCCCCCCCC		21.0825627689
435PhosphorylationELSPIPASPGQAAPL
CCCCCCCCCCCCCCC		24.9822817900
457PhosphorylationKKPRQRESGYYSSPE
CCCCCCCCCCCCCCC		33.9920071362
461PhosphorylationQRESGYYSSPEPSES
CCCCCCCCCCCCCCC		30.8229802988
462PhosphorylationRESGYYSSPEPSESG
CCCCCCCCCCCCCCC		19.7022817900
466PhosphorylationYYSSPEPSESGELLD
CCCCCCCCCCCCCCC		42.6128348404
468PhosphorylationSSPEPSESGELLDAG
CCCCCCCCCCCCCCC		41.7429759185
479PhosphorylationLDAGDVFVSGDPKEQ
CCCCCEEECCCCHHC		6.67-
506PhosphorylationKGILKLNGKFSQTAL
CCEEEECCEECHHHH		42.70-
519PhosphorylationALELAAPTTFGSLDE
HHHHHCCCCCCCHHH		29.9920071362
520PhosphorylationLELAAPTTFGSLDEL
HHHHCCCCCCCHHHC		25.5828348404
523PhosphorylationAAPTTFGSLDELAPP
HCCCCCCCHHHCCCC		28.5822817900
531UbiquitinationLDELAPPRPLARASR
HHHCCCCCCCCCCCC		37.49-
540PhosphorylationLARASRPSGAVSEDS
CCCCCCCCCCCCCCC		37.9719369195
544PhosphorylationSRPSGAVSEDSILSS
CCCCCCCCCCCCCCC		34.8422817900
547PhosphorylationSGAVSEDSILSSESF
CCCCCCCCCCCCCCC		22.7522817900
550PhosphorylationVSEDSILSSESFDQL
CCCCCCCCCCCCCCC		30.3219369195
553PhosphorylationDSILSSESFDQLDLP
CCCCCCCCCCCCCCC		35.7522817900
567PhosphorylationPERLPEPPLRGCVSV
CHHCCCCCCCCCEEE		32.78-
573PhosphorylationPPLRGCVSVDNLTGL
CCCCCCEEECCCCCC		28.0328348404
588PhosphorylationEEPPSEGPGSCLRRW
CCCCCCCCCHHHHHH		27.72-
591PhosphorylationPSEGPGSCLRRWRQD
CCCCCCHHHHHHCCC		4.20-
597PhosphorylationSCLRRWRQDPLGDSC
HHHHHHCCCCCCCCC		50.11-
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
208TPhosphorylationKinaseSTK11Q15831
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
208TPhosphorylation

14976552
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 NUAK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
LATS1_HUMANLATS1physical
19927127
LZTR1_HUMANLZTR1physical
28514442
MYPT1_HUMANPPP1R12Aphysical
28514442
MARK3_HUMANMARK3physical
28514442
UBXN7_HUMANUBXN7physical
28514442
FLNC_HUMANFLNCphysical
28514442
FBW1A_HUMANBTRCphysical
28514442
SAHH3_HUMANAHCYL2physical
28514442
MARK2_HUMANMARK2physical
28514442
FBW1B_HUMANFBXW11physical
28514442
DCAF5_HUMANDCAF5physical
28514442
UBP7_HUMANUSP7physical
28514442
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 NUAK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-435; SER-462; SER-523;SER-540; SER-544; SER-547; SER-550 AND SER-553, AND MASS SPECTROMETRY.
"LKB1 is a master kinase that activates 13 kinases of the AMPKsubfamily, including MARK/PAR-1.";
Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A.,Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G.,Alessi D.R.;
EMBO J. 23:833-843(2004).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 205-224, FUNCTION,ENZYME REGULATION, PHOSPHORYLATION AT THR-208, AND MUTAGENESIS OFTHR-208.

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