TNK1_HUMAN - dbPTM
TNK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNK1_HUMAN
UniProt AC Q13470
Protein Name Non-receptor tyrosine-protein kinase TNK1
Gene Name TNK1 {ECO:0000312|EMBL:AAC99412.1}
Organism Homo sapiens (Human).
Sequence Length 666
Subcellular Localization Cytoplasm . Membrane
Peripheral membrane protein .
Protein Description Involved in negative regulation of cell growth. Has tumor suppressor properties. Plays a negative regulatory role in the Ras-MAPK pathway. May function in signaling pathways utilized broadly during fetal development and more selectively in adult tissues and in cells of the lymphohematopoietic system. Could specifically be involved in phospholipid signal transduction..
Protein Sequence MLPEAGSLWLLKLLRDIQLAQFYWPILEELNVTRPEHFDFVKPEDLDGIGMGRPAQRRLSEALKRLRSGPKSKNWVYKILGGFAPEHKEPTLPSDSPRHLPEPEGGLKCLIPEGAVCRGELLGSGCFGVVHRGLWTLPSGKSVPVAVKSLRVGPEGPMGTELGDFLREVSVMMNLEHPHVLRLHGLVLGQPLQMVMELAPLGSLHARLTAPAPTPPLLVALLCLFLRQLAGAMAYLGARGLVHRDLATRNLLLASPRTIKVADFGLVRPLGGARGRYVMGGPRPIPYAWCAPESLRHGAFSSASDVWMFGVTLWEMFSGGEEPWAGVPPYLILQRLEDRARLPRPPLCSRALYSLALRCWAPHPADRPSFSHLEGLLQEAGPSEACCVRDVTEPGALRMETGDPITVIEGSSSFHSPDSTIWKGQNGRTFKVGSFPASAVTLADAGGLPATRPVHRGTPARGDQHPGSIDGDRKKANLWDAPPARGQRRNMPLERMKGISRSLESVLSLGPRPTGGGSSPPEIRQARAVPQGPPGLPPRPPLSSSSPQPSQPSRERLPWPKRKPPHNHPMGMPGARKAAALSGGLLSDPELQRKIMEVELSVHGVTHQECQTALGATGGDVVSAIRNLKVDQLFHLSSRSRADCWRILEHYQWDLSAASRYVLARP
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
60PhosphorylationRPAQRRLSEALKRLR
HHHHHHHHHHHHHHH		21.0017192257
68PhosphorylationEALKRLRSGPKSKNW
HHHHHHHCCCCCCCH		65.1320068231
73UbiquitinationLRSGPKSKNWVYKIL
HHCCCCCCCHHHHHH		62.0429967540
77PhosphorylationPKSKNWVYKILGGFA
CCCCCHHHHHHCCCC		5.5020090780
88UbiquitinationGGFAPEHKEPTLPSD
CCCCCCCCCCCCCCC		64.8227667366
91PhosphorylationAPEHKEPTLPSDSPR
CCCCCCCCCCCCCCC		53.0128857561
94PhosphorylationHKEPTLPSDSPRHLP
CCCCCCCCCCCCCCC		54.5618691976
96PhosphorylationEPTLPSDSPRHLPEP
CCCCCCCCCCCCCCC		28.3325159151
103UbiquitinationSPRHLPEPEGGLKCL
CCCCCCCCCCCCEEE		43.5222817900
108UbiquitinationPEPEGGLKCLIPEGA
CCCCCCCEEECCCCC		30.2129967540
139PhosphorylationRGLWTLPSGKSVPVA
CCEEECCCCCCCCEE		63.0624719451
141 (in isoform 2)Ubiquitination-53.2521890473
141 (in isoform 1)Ubiquitination-53.2521890473
141UbiquitinationLWTLPSGKSVPVAVK
EEECCCCCCCCEEEE		53.2527667366
160PhosphorylationGPEGPMGTELGDFLR
CCCCCCCCCHHHHHH		23.0630257219
209PhosphorylationGSLHARLTAPAPTPP
CCEEEHHCCCCCCHH		25.66-
214PhosphorylationRLTAPAPTPPLLVAL
HHCCCCCCHHHHHHH		39.38-
235PhosphorylationQLAGAMAYLGARGLV
HHHHHHHHHHHCCHH		7.8120090780
248PhosphorylationLVHRDLATRNLLLAS
HHCHHHHHHHHHHCC		27.6421712546
255PhosphorylationTRNLLLASPRTIKVA
HHHHHHCCCCEEEEE		18.1922617229
258PhosphorylationLLLASPRTIKVADFG
HHHCCCCEEEEECEE		28.65-
260UbiquitinationLASPRTIKVADFGLV
HCCCCEEEEECEECE		30.6622817900
260 (in isoform 1)Ubiquitination-30.6621890473
260 (in isoform 2)Ubiquitination-30.6621890473
261UbiquitinationASPRTIKVADFGLVR
CCCCEEEEECEECEE		5.6623503661
277PhosphorylationLGGARGRYVMGGPRP
CCCCCCCEECCCCCC		9.5220090780
287PhosphorylationGGPRPIPYAWCAPES
CCCCCCCCEEECCHH		17.2920090780
313UbiquitinationVWMFGVTLWEMFSGG
HHHHEEEEHHHHCCC		3.2027667366
353PhosphorylationPLCSRALYSLALRCW
CHHHHHHHHHHHHHH		10.7220090780
354PhosphorylationLCSRALYSLALRCWA
HHHHHHHHHHHHHHC		14.1724719451
406PhosphorylationMETGDPITVIEGSSS
ECCCCCEEEEECCCC		22.3322817900
411PhosphorylationPITVIEGSSSFHSPD
CEEEEECCCCCCCCC		15.2618691976
411 (in isoform 2)Phosphorylation-15.2617192257
418 (in isoform 2)Ubiquitination-62.5221890473
418UbiquitinationSSSFHSPDSTIWKGQ
CCCCCCCCCCEEECC		62.5223503661
423UbiquitinationSPDSTIWKGQNGRTF
CCCCCEEECCCCCEE		46.9323503661
458PhosphorylationTRPVHRGTPARGDQH
CCCCCCCCCCCCCCC		17.4628555341
468PhosphorylationRGDQHPGSIDGDRKK
CCCCCCCCCCCCCHH		23.2025159151
470UbiquitinationDQHPGSIDGDRKKAN
CCCCCCCCCCCHHCC		55.4227667366
475MethylationSIDGDRKKANLWDAP
CCCCCCHHCCCCCCC		43.32115979821
475UbiquitinationSIDGDRKKANLWDAP
CCCCCCHHCCCCCCC		43.3227667366
497PhosphorylationNMPLERMKGISRSLE
CCCHHHHHHHCHHHH		60.3533259812
500PhosphorylationLERMKGISRSLESVL
HHHHHHHCHHHHHHH		25.2030576142
502PhosphorylationRMKGISRSLESVLSL
HHHHHCHHHHHHHCC		29.6919664994
505PhosphorylationGISRSLESVLSLGPR
HHCHHHHHHHCCCCC		33.3822167270
508PhosphorylationRSLESVLSLGPRPTG
HHHHHHHCCCCCCCC		29.1730278072
514PhosphorylationLSLGPRPTGGGSSPP
HCCCCCCCCCCCCCH		50.1422167270
518PhosphorylationPRPTGGGSSPPEIRQ
CCCCCCCCCCHHHHH		42.8422167270
519PhosphorylationRPTGGGSSPPEIRQA
CCCCCCCCCHHHHHH		47.9919664994
543PhosphorylationLPPRPPLSSSSPQPS
CCCCCCCCCCCCCCC		33.6718691976
544PhosphorylationPPRPPLSSSSPQPSQ
CCCCCCCCCCCCCCC		42.3826657352
545PhosphorylationPRPPLSSSSPQPSQP
CCCCCCCCCCCCCCC		42.5330576142
546PhosphorylationRPPLSSSSPQPSQPS
CCCCCCCCCCCCCCC		29.5126657352
550PhosphorylationSSSSPQPSQPSRERL
CCCCCCCCCCCHHCC		49.8518669648
553PhosphorylationSPQPSQPSRERLPWP
CCCCCCCCHHCCCCC		38.8523312004
558UbiquitinationQPSRERLPWPKRKPP
CCCHHCCCCCCCCCC		52.0929967540
563UbiquitinationRLPWPKRKPPHNHPM
CCCCCCCCCCCCCCC		69.8629967540
572UbiquitinationPHNHPMGMPGARKAA
CCCCCCCCCHHHHHH		1.9429967540
577UbiquitinationMGMPGARKAAALSGG
CCCCHHHHHHHHHCC		41.6729967540
582PhosphorylationARKAAALSGGLLSDP
HHHHHHHHCCCCCCH		26.5321082442
587PhosphorylationALSGGLLSDPELQRK
HHHCCCCCCHHHHHH		57.0420068231
612PhosphorylationVTHQECQTALGATGG
CCHHHHHHHHCCCCH		35.19-
651PhosphorylationCWRILEHYQWDLSAA
HHHHHHHHCCCHHHH		11.2627642862
659PhosphorylationQWDLSAASRYVLARP
CCCHHHHHHHHHCCC		24.70-
661PhosphorylationDLSAASRYVLARP--
CHHHHHHHHHCCC--		9.4123911959
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
502SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNK1_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 TNK1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TNK1_HUMANTNK1physical
10873601
DDX5_HUMANDDX5physical
25852190
ILF3_HUMANILF3physical
25852190
1433S_HUMANSFNphysical
25852190
1433B_HUMANYWHABphysical
25852190
1433E_HUMANYWHAEphysical
25852190
1433G_HUMANYWHAGphysical
25852190
1433F_HUMANYWHAHphysical
25852190
1433T_HUMANYWHAQphysical
25852190
1433Z_HUMANYWHAZphysical
25852190
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 TNK1_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-96; SER-255; SER-411;SER-502; THR-514; SER-518 AND SER-543, AND MASS SPECTROMETRY.
"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-502; SER-508; THR-514;SER-519 AND TYR-661, AND MASS SPECTROMETRY.
"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-60; SER-96; SER-255;TYR-277; SER-468; SER-502; THR-514; SER-519; SER-582 AND TYR-661, ANDMASS SPECTROMETRY.

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