NEK6_HUMAN - dbPTM
NEK6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NEK6_HUMAN
UniProt AC Q9HC98
Protein Name Serine/threonine-protein kinase Nek6
Gene Name NEK6
Organism Homo sapiens (Human).
Sequence Length 313
Subcellular Localization Cytoplasm. Nucleus. Nucleus speckle. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Colocalizes with APBB1 at the nuclear speckles. Colocalizes with PIN1 in the nucleus. Colocalizes with ATF
Protein Description Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence..
Protein Sequence MAGQPGHMPHGGSSNNLCHTLGPVHPPDPQRHPNTLSFRCSLADFQIEKKIGRGQFSEVYKATCLLDRKTVALKKVQIFEMMDAKARQDCVKEIGLLKQLNHPNIIKYLDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSETTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPGEHYSEKLRELVSMCICPDPHQRPDIGYVHQVAKQMHIWMSST
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-------MAGQPGHM
-------CCCCCCCC		9.49-
13PhosphorylationGHMPHGGSSNNLCHT
CCCCCCCCCCCCCCC		34.1930108239
14PhosphorylationHMPHGGSSNNLCHTL
CCCCCCCCCCCCCCC		32.7728857561
20PhosphorylationSSNNLCHTLGPVHPP
CCCCCCCCCCCCCCC		32.2028857561
35PhosphorylationDPQRHPNTLSFRCSL
CCCCCCCCEEEEEEH		28.3830108239
37PhosphorylationQRHPNTLSFRCSLAD
CCCCCCEEEEEEHHH		14.4930108239
41PhosphorylationNTLSFRCSLADFQIE
CCEEEEEEHHHHHHH		23.4927251275
49UbiquitinationLADFQIEKKIGRGQF
HHHHHHHHHHCCCCC		51.85-
57PhosphorylationKIGRGQFSEVYKATC
HHCCCCCHHHHHHHH		20.4726074081
60PhosphorylationRGQFSEVYKATCLLD
CCCCHHHHHHHHHHC		7.2826074081
61UbiquitinationGQFSEVYKATCLLDR
CCCHHHHHHHHHHCC		42.25-
63PhosphorylationFSEVYKATCLLDRKT
CHHHHHHHHHHCCCE		10.2626074081
75PhosphorylationRKTVALKKVQIFEMM
CCEEEEEEEHHHHHC		39.9827251275
85UbiquitinationIFEMMDAKARQDCVK
HHHHCCHHHHHHHHH		39.58-
92UbiquitinationKARQDCVKEIGLLKQ
HHHHHHHHHHHHHHH		50.36-
98UbiquitinationVKEIGLLKQLNHPNI
HHHHHHHHHCCCCCH		58.75-
108PhosphorylationNHPNIIKYLDSFIED
CCCCHHHHHHHHHHC		12.8219941817
152PhosphorylationPERTVWKYFVQLCSA
CHHHHHHHHHHHHHH		8.02-
158PhosphorylationKYFVQLCSAVEHMHS
HHHHHHHHHHHHHHH		43.89-
165PhosphorylationSAVEHMHSRRVMHRD
HHHHHHHHCCCCCCC		17.76-
174UbiquitinationRVMHRDIKPANVFIT
CCCCCCCCCCCEEEE		42.2221890473
181PhosphorylationKPANVFITATGVVKL
CCCCEEEEECEEEEE		13.50-
183PhosphorylationANVFITATGVVKLGD
CCEEEEECEEEEECC		23.12-
187UbiquitinationITATGVVKLGDLGLG
EEECEEEEECCCCCC		44.33-
198PhosphorylationLGLGRFFSSETTAAH
CCCCCCCCCCCHHHH		25.2622115753
199UbiquitinationGLGRFFSSETTAAHS
CCCCCCCCCCHHHHH		33.5321890473
199PhosphorylationGLGRFFSSETTAAHS
CCCCCCCCCCHHHHH		33.5321712546
201PhosphorylationGRFFSSETTAAHSLV
CCCCCCCCHHHHHCC		24.5521945579
202PhosphorylationRFFSSETTAAHSLVG
CCCCCCCHHHHHCCC		20.1421945579
206PhosphorylationSETTAAHSLVGTPYY
CCCHHHHHCCCCCCC		21.7421945579
208 (in isoform 2)Ubiquitination-10.07-
210PhosphorylationAAHSLVGTPYYMSPE
HHHHCCCCCCCCCHH		10.7121945579
212PhosphorylationHSLVGTPYYMSPERI
HHCCCCCCCCCHHHH		16.1921945579
213PhosphorylationSLVGTPYYMSPERIH
HCCCCCCCCCHHHHH		7.7221945579
215PhosphorylationVGTPYYMSPERIHEN
CCCCCCCCHHHHHHC		13.9021945579
224PhosphorylationERIHENGYNFKSDIW
HHHHHCCCCCHHHHH		29.0729496907
235PhosphorylationSDIWSLGCLLYEMAA
HHHHHHHHHHHHHHH		2.6127251275
236PhosphorylationDIWSLGCLLYEMAAL
HHHHHHHHHHHHHHH		5.6027251275
240PhosphorylationLGCLLYEMAALQSPF
HHHHHHHHHHHHCCC		1.3427251275
277UbiquitinationPGEHYSEKLRELVSM
CCCCCHHHHHHHHHH		47.07-
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
206SPhosphorylationKinaseNEK9Q8TD19
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
206SPhosphorylation

12840024
210TPhosphorylation

17512906
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 NEK6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC85B_HUMANCCDC85Bphysical
16189514
NECA2_HUMANNECAB2physical
16189514
NEK9_HUMANNEK9physical
17353931
EMAL3_HUMANEML3physical
17353931
USP9X_HUMANUSP9Xphysical
17353931
CCAR2_HUMANCCAR2physical
17353931
IPO4_HUMANIPO4physical
17353931
NEK7_HUMANNEK7physical
17353931
LPPRC_HUMANLRPPRCphysical
17353931
SMC3_HUMANSMC3physical
17353931
MCM7_HUMANMCM7physical
17353931
EMAL2_HUMANEML2physical
17353931
DYL1_HUMANDYNLL1physical
17353931
AAAT_HUMANSLC1A5physical
17353931
NUP93_HUMANNUP93physical
17353931
XPO5_HUMANXPO5physical
17353931
HACD3_HUMANPTPLAD1physical
17353931
FANCI_HUMANFANCIphysical
17353931
GCN1_HUMANGCN1L1physical
17353931
PCID2_HUMANPCID2physical
17353931
EMAL4_HUMANEML4physical
17353931
ERD21_HUMANKDELR1physical
17353931
CDC37_HUMANCDC37physical
17353931
RUVB2_HUMANRUVBL2physical
17353931
PSMD2_HUMANPSMD2physical
17353931
MYO1C_HUMANMYO1Cphysical
17353931
NEK9_HUMANNEK9physical
12840024
NEK9_HUMANNEK9physical
12101123
PAK6_HUMANPAK6physical
21988832
PHF1_HUMANPHF1physical
20873783
PRDX3_HUMANPRDX3physical
20873783
PRAM_HUMANPRAM1physical
20873783
PTN_HUMANPTNphysical
20873783
RBBP6_HUMANRBBP6physical
20873783
RHG33_HUMANARHGAP33physical
20873783
TRIP4_HUMANTRIP4physical
20873783
RS7_HUMANRPS7physical
20873783
RELB_HUMANRELBphysical
20873783
CIR1_HUMANCIR1physical
20873783
CDC42_HUMANCDC42physical
20873783
ER6L2_HUMANERCC6L2physical
20873783
ATF4_HUMANATF4physical
20873783
ANRA2_HUMANANKRA2physical
20873783
NEK9_HUMANNEK9physical
20873783
NEK6_HUMANNEK6physical
20873783
IKZF3_HUMANIKZF3physical
25416956
DHB14_HUMANHSD17B14physical
25416956
NECA2_HUMANNECAB2physical
25416956
F208B_HUMANFAM208Bphysical
25416956
LZTS2_HUMANLZTS2physical
25416956
LNX1_HUMANLNX1physical
25416956
K1C40_HUMANKRT40physical
25416956
IHO1_HUMANCCDC36physical
25416956
INCA1_HUMANINCA1physical
25416956
NEK7_HUMANNEK7physical
26186194
NEK9_HUMANNEK9physical
26186194
NEK7_HUMANNEK7physical
28514442
NEK9_HUMANNEK9physical
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 NEK6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Characterization of hNek6 interactome reveals an important role forits short N-terminal domain and colocalization with proteins at thecentrosome.";
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C.,Santana Bernachi J., Paes Leme A.F., Kobarg J.;
J. Proteome Res. 9:6298-6316(2010).
Cited for: FUNCTION, INTERACTION WITH ANKRA2; ATF4; ARHGAP33; CDC42; CIR1; NEK9;PRAM1; PTN; PRDX3; RAD26L; RBBP6; RPS7 AND TRIP4, PHOSPHORYLATION ATSER-206, AND AUTOPHOSPHORYLATION.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND MASSSPECTROMETRY.
"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 THR-35; SER-198; SER-199;THR-201; THR-202 AND SER-206, AND MASS SPECTROMETRY.
"A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates theNek6 and Nek7 kinases.";
Belham C., Roig J., Caldwell J.A., Aoyama Y., Kemp B.E., Comb M.,Avruch J.;
J. Biol. Chem. 278:34897-34909(2003).
Cited for: PHOSPHORYLATION AT SER-37; THR-202 AND SER-206.
"Human NIMA-related kinase 6 is one of the Fe65 WW domain bindingproteins.";
Lee E.J., Hyun S.H., Chun J., Kang S.S.;
Biochem. Biophys. Res. Commun. 358:783-788(2007).
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH APBB1, AND PHOSPHORYLATION ATTHR-210.

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