KSR2_HUMAN - dbPTM
KSR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KSR2_HUMAN
UniProt AC Q6VAB6
Protein Name Kinase suppressor of Ras 2
Gene Name KSR2
Organism Homo sapiens (Human).
Sequence Length 950
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein.
Protein Description Location-regulated scaffold connecting MEK to RAF. Has very low protein kinase activity and can phosphorylate MAP2K1 at several Ser and Thr residues with very low efficiency (in vitro). Interaction with BRAF enhances KSR2-mediated phosphorylation of MAP2K1 (in vitro). Blocks MAP3K8 kinase activity and MAP3K8-mediated signaling. Acts as a negative regulator of MAP3K3-mediated activation of ERK, JNK and NF-kappa-B pathways, inhibiting MAP3K3-mediated interleukin-8 production..
Protein Sequence MDEENMTKSEEQQPLSLQKALQQCELVQNMIDLSISNLEGLRTKCATSNDLTQKEIRTLESKLVKYFSRQLSCKKKVALQERNAELDGFPQLRHWFRIVDVRKEVLEEISPGQLSLEDLLEMTDEQVCETVEKYGANREECARLNASLSCLRNVHMSGGNLSKQDWTIQWPTTETGKENNPVCPPEPTPWIRTHLSQSPRVPSKCVQHYCHTSPTPGAPVYTHVDRLTVDAYPGLCPPPPLESGHRSLPPSPRQRHAVRTPPRTPNIVTTVTPPGTPPMRKKNKLKPPGTPPPSSRKLIHLIPGFTALHRSKSHEFQLGHRVDEAHTPKAKKKSKPLNLKIHSSVGSCENIPSQQRSPLLSERSLRSFFVGHAPFLPSTPPVHTEANFSANTLSVPRWSPQIPRRDLGNSIKHRFSTKYWMSQTCTVCGKGMLFGLKCKNCKLKCHNKCTKEAPPCHLLIIHRGDPARLVRTESVPCDINNPLRKPPRYSDLHISQTLPKTNKINKDHIPVPYQPDSSSNPSSTTSSTPSSPAPPLPPSATPPSPLHPSPQCTRQQKNFNLPASHYYKYKQQFIFPDVVPVPETPTRAPQVILHPVTSNPILEGNPLLQIEVEPTSENEEVHDEAEESEDDFEEMNLSLLSARSFPRKASQTSIFLQEWDIPFEQLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFSISGVLQAGRREDKLRIQNGWLCHLAPEIIRQLSPDTEEDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKLPKRNRRLSHPGHFWKSAEL
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
15UbiquitinationKSEEQQPLSLQKALQ
CCHHHCCCHHHHHHH		7.49-
16PhosphorylationSEEQQPLSLQKALQQ
CHHHCCCHHHHHHHH		35.1224719451
34PhosphorylationVQNMIDLSISNLEGL
HHHHHHHHHHCHHHH		21.88-
149PhosphorylationARLNASLSCLRNVHM
HHHHHHHHHHHCEEC		14.4924719451
231PhosphorylationVDRLTVDAYPGLCPP
CCCEEECCCCCCCCC		14.21-
240PhosphorylationPGLCPPPPLESGHRS
CCCCCCCCCCCCCCC		55.31-
247PhosphorylationPLESGHRSLPPSPRQ
CCCCCCCCCCCCHHH		39.28-
251PhosphorylationGHRSLPPSPRQRHAV
CCCCCCCCHHHCCCC		30.6723312004
260PhosphorylationRQRHAVRTPPRTPNI
HHCCCCCCCCCCCCE		30.9223312004
261PhosphorylationQRHAVRTPPRTPNIV
HCCCCCCCCCCCCEE		13.0524719451
264PhosphorylationAVRTPPRTPNIVTTV
CCCCCCCCCCEEEEC		26.85-
269PhosphorylationPRTPNIVTTVTPPGT
CCCCCEEEECCCCCC		16.2622322096
270PhosphorylationRTPNIVTTVTPPGTP
CCCCEEEECCCCCCC		16.1024076635
272PhosphorylationPNIVTTVTPPGTPPM
CCEEEECCCCCCCCC		22.9828985074
276PhosphorylationTTVTPPGTPPMRKKN
EECCCCCCCCCCCCC		29.9622322096
277PhosphorylationTVTPPGTPPMRKKNK
ECCCCCCCCCCCCCC		26.9724719451
281AcetylationPGTPPMRKKNKLKPP
CCCCCCCCCCCCCCC		55.227977241
282PhosphorylationGTPPMRKKNKLKPPG
CCCCCCCCCCCCCCC		49.2824719451
284PhosphorylationPPMRKKNKLKPPGTP
CCCCCCCCCCCCCCC		67.7627251275
290PhosphorylationNKLKPPGTPPPSSRK
CCCCCCCCCCCCHHH		38.0928188228
294PhosphorylationPPGTPPPSSRKLIHL
CCCCCCCCHHHHHHH		48.85-
306PhosphorylationIHLIPGFTALHRSKS
HHHCCCCCEECCCCC		33.9424719451
311PhosphorylationGFTALHRSKSHEFQL
CCCEECCCCCCCCCC		27.9723312004
313PhosphorylationTALHRSKSHEFQLGH
CEECCCCCCCCCCCC		29.5126657352
315PhosphorylationLHRSKSHEFQLGHRV
ECCCCCCCCCCCCCC		42.0327251275
318PhosphorylationSKSHEFQLGHRVDEA
CCCCCCCCCCCCCCC		8.29-
327PhosphorylationHRVDEAHTPKAKKKS
CCCCCCCCCCCCCCC		33.2728985074
334PhosphorylationTPKAKKKSKPLNLKI
CCCCCCCCCCCCCEE		48.6724719451
343PhosphorylationPLNLKIHSSVGSCEN
CCCCEEECCCCCCCC		30.1423312004
344PhosphorylationLNLKIHSSVGSCENI
CCCEEECCCCCCCCC		19.1423312004
347PhosphorylationKIHSSVGSCENIPSQ
EEECCCCCCCCCCHH		18.9930624053
367PhosphorylationLSERSLRSFFVGHAP
CCHHHHHHHHCCCCC		28.4728270605
370PhosphorylationRSLRSFFVGHAPFLP
HHHHHHHCCCCCCCC		5.3124719451
378PhosphorylationGHAPFLPSTPPVHTE
CCCCCCCCCCCCCCC		56.5528270605
379PhosphorylationHAPFLPSTPPVHTEA
CCCCCCCCCCCCCCC		29.6728270605
384PhosphorylationPSTPPVHTEANFSAN
CCCCCCCCCCCCCCC		36.7128270605
389PhosphorylationVHTEANFSANTLSVP
CCCCCCCCCCCCCCC		22.0328270605
392PhosphorylationEANFSANTLSVPRWS
CCCCCCCCCCCCCCC		21.8128270605
394PhosphorylationNFSANTLSVPRWSPQ
CCCCCCCCCCCCCCC		28.2128270605
399PhosphorylationTLSVPRWSPQIPRRD
CCCCCCCCCCCCHHH		14.2728188228
445PhosphorylationCKNCKLKCHNKCTKE
ECCCCCEECCCCCCC		6.5724719451
472PhosphorylationDPARLVRTESVPCDI
CHHHEEECCCCCCCC		25.7328111955
474PhosphorylationARLVRTESVPCDINN
HHEEECCCCCCCCCC		30.6527050516
490PhosphorylationLRKPPRYSDLHISQT
CCCCCCCCCCCCCCC		34.67-
495PhosphorylationRYSDLHISQTLPKTN
CCCCCCCCCCCCCCC		13.3323403867
497PhosphorylationSDLHISQTLPKTNKI
CCCCCCCCCCCCCCC		37.9323403867
566PhosphorylationFNLPASHYYKYKQQF
CCCCHHHHHHCEEEE		10.1227642862
569PhosphorylationPASHYYKYKQQFIFP
CHHHHHHCEEEEECC		9.6327273156
584PhosphorylationDVVPVPETPTRAPQV
CCCCCCCCCCCCCEE		24.7227273156
641PhosphorylationEMNLSLLSARSFPRK
HHHHHHHHHHCCCCC		27.2524719451
765PhosphorylationLDVNKTRQIAQEIVK
ECCCHHHHHHHHHHH		40.37-
773PhosphorylationIAQEIVKGMGYLHAK
HHHHHHHCCCHHHHH		12.12-
779PhosphorylationKGMGYLHAKGILHKD
HCCCHHHHHCCCCCC		14.80-
794PhosphorylationLKSKNVFYDNGKVVI
CCCCCEEEECCEEEE		12.2927251275
802PhosphorylationDNGKVVITDFGLFSI
ECCEEEEEECCHHEE		17.4227251275
808PhosphorylationITDFGLFSISGVLQA
EEECCHHEEHHHHHC		22.3827251275
894UbiquitinationGTGMKPNLSQIGMGK
CCCCCCCHHHHCCCH		5.60-
910PhosphorylationISDILLFCWAFEQEE
HHHHHHHHHHHCCCC		2.3027251275
923UbiquitinationEERPTFTKLMDMLEK
CCCCHHHHHHHHHHH		37.31-
939PhosphorylationPKRNRRLSHPGHFWK
HHCCCCCCCCCCCHH		26.3128152594
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
474SPhosphorylationKinaseMARK3P27448
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
474SPhosphorylation

-
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 KSR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M3K8_HUMANMAP3K8physical
12975377
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 KSR2_HUMAN

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Related Literatures of Post-Translational Modification

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