dbPTM

TBB6_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB6_MOUSE
UniProt AC	Q922F4
Protein Name	Tubulin beta-6 chain
Gene Name	Tubb6
Organism	Mus musculus (Mouse).
Sequence Length	447
Subcellular Localization	Cytoplasm, cytoskeleton.
Protein Description	Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain..
Protein Sequence	MREIVHIQAGQCGNQIGTKFWEVISDEHGIDQAGGYVGDSALQLERISVYYNESSSKKYVPRAALVDLEPGTMDSVRSGPFGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDSVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVATVFRGPMSMKEVDEQMLAIQNKNSSYFVEWIPNNVKVAVCDIPPRGLKMASTFIGNSTAIQELFKRISEQFSAMFRRKAFLHWFTGEGMDEMEFTEAESNMNDLVSEYQQYQDATVNDGEEAFEDEDEEEINE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	S-nitrosocysteine	VHIQAGQCGNQIGTK EEEECCCCCCCCCHH	5.60	-
12	S-nitrosylation	VHIQAGQCGNQIGTK EEEECCCCCCCCCHH	5.60	20925432
12	Glutathionylation	VHIQAGQCGNQIGTK EEEECCCCCCCCCHH	5.60	24333276
50	Phosphorylation	QLERISVYYNESSSK EEEEEEEEECCCCCC	8.19	29895711
54	Phosphorylation	ISVYYNESSSKKYVP EEEEECCCCCCCCCC	35.95	29895711
55	Phosphorylation	SVYYNESSSKKYVPR EEEECCCCCCCCCCC	39.74	29514104
56	Phosphorylation	VYYNESSSKKYVPRA EEECCCCCCCCCCCE	42.31	29895711
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCCCCCCC	28.64	29514104
75	Phosphorylation	LEPGTMDSVRSGPFG CCCCCCCCCCCCCCC	14.49	29514104
78	Phosphorylation	GTMDSVRSGPFGQLF CCCCCCCCCCCCCCC	48.97	26239621
103	Methylation	GAGNNWAKGHYTEGA CCCCCCCCCCCCCHH	37.52	-
105	Methylation	GNNWAKGHYTEGAEL CCCCCCCCCCCHHHH	26.15	4207447
106	Phosphorylation	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	12692561
107	Phosphorylation	NWAKGHYTEGAELVD CCCCCCCCCHHHHHH	23.44	12692561
115	Phosphorylation	EGAELVDSVLDVVRK CHHHHHHHHHHHHHH	19.66	27600695
166	Phosphorylation	YPDRIMNTFSVMPSP CCCCCCHHEECCCCC	10.41	-
168	Phosphorylation	DRIMNTFSVMPSPKV CCCCHHEECCCCCCC	18.57	-
172	Phosphorylation	NTFSVMPSPKVSDTV HHEECCCCCCCCCCE	21.18	19737024
208	Phosphorylation	CIDNEALYDICFRTL EECHHHHHHHHHHEE	15.43	18563927
218	Phosphorylation	CFRTLKLTTPTYGDL HHHEECCCCCCCHHH	29.19	19060867
219	Phosphorylation	FRTLKLTTPTYGDLN HHEECCCCCCCHHHH	24.86	22817900
221	Phosphorylation	TLKLTTPTYGDLNHL EECCCCCCCHHHHHH	37.74	19060867
222	Phosphorylation	LKLTTPTYGDLNHLV ECCCCCCCHHHHHHH	15.17	-
230	Phosphorylation	GDLNHLVSATMSGVT HHHHHHHHHHHCCCC	25.12	26643407
232	Phosphorylation	LNHLVSATMSGVTTS HHHHHHHHHCCCCCC	12.36	26643407
234	Phosphorylation	HLVSATMSGVTTSLR HHHHHHHCCCCCCCC	26.25	26643407
237	Phosphorylation	SATMSGVTTSLRFPG HHHHCCCCCCCCCCC	17.75	26643407
238	Phosphorylation	ATMSGVTTSLRFPGQ HHHCCCCCCCCCCCC	24.29	26643407
239	Phosphorylation	TMSGVTTSLRFPGQL HHCCCCCCCCCCCCC	14.26	26643407
252	Acetylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	8664883
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
274	Phosphorylation	MPGFAPLTARGSQQY CCCCCCCCCCCCHHH	17.16	22817900
278	Phosphorylation	APLTARGSQQYRALT CCCCCCCCHHHEEEE	14.46	29899451
285	Phosphorylation	SQQYRALTVPELTQQ CHHHEEEEHHHHHHH	32.79	-
297	Ubiquitination	TQQMFDAKNMMAACD HHHHHCCCHHHHHCC	47.42	-
312	Phosphorylation	PRHGRYLTVATVFRG CCCCCEEEEEEEEEC	10.12	18779572
315	Phosphorylation	GRYLTVATVFRGPMS CCEEEEEEEEECCCC	18.81	18779572
338	Phosphorylation	LAIQNKNSSYFVEWI HHHHCCCCCCEEEEC	28.20	26745281
339	Phosphorylation	AIQNKNSSYFVEWIP HHHCCCCCCEEEECC	31.80	26745281
340	Phosphorylation	IQNKNSSYFVEWIPN HHCCCCCCEEEECCC	16.09	22324799
362	Ubiquitination	DIPPRGLKMASTFIG CCCCCCHHHHHHHHC	34.93	-
379	Acetylation	TAIQELFKRISEQFS HHHHHHHHHHHHHHH	62.54	156603
438	5-glutamyl polyglutamate	NDGEEAFEDEDEEEI CCCHHHCCCCCHHHH	68.49	-
438	Formation of an isopeptide bond	NDGEEAFEDEDEEEI CCCHHHCCCCCHHHH	68.49	-

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
172	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
172	S	Phosphorylation		-
Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase.

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 TBB6_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TBB6_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of TBB6_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-106, AND MASSSPECTROMETRY.	18034455 [Abstract]

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