dbPTM

TBB5_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB5_RAT
UniProt AC	P69897
Protein Name	Tubulin beta-5 chain
Gene Name	Tubb5
Organism	Rattus norvegicus (Rat).
Sequence Length	444
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	MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDFGEEAEEEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	S-nitrosocysteine	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	-
12	S-nitrosylation	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	16418269
25	Phosphorylation	AKFWEVISDEHGIDP HHHHEHHHCCCCCCC	41.96	23984901
33	Phosphorylation	DEHGIDPTGTYHGDS CCCCCCCCCCCCCCC	38.11	23984901
35	Phosphorylation	HGIDPTGTYHGDSDL CCCCCCCCCCCCCCC	18.15	23984901
36	Phosphorylation	GIDPTGTYHGDSDLQ CCCCCCCCCCCCCCE	12.73	23984901
40	Phosphorylation	TGTYHGDSDLQLDRI CCCCCCCCCCEEEEE	44.83	30240740
48	Phosphorylation	DLQLDRISVYYNEAT CCEEEEEEEEEECCC	12.64	30181290
50	Phosphorylation	QLDRISVYYNEATGG EEEEEEEEEECCCCC	8.19	25403869
51	Phosphorylation	LDRISVYYNEATGGK EEEEEEEEECCCCCC	12.36	25403869
55	Phosphorylation	SVYYNEATGGKYVPR EEEEECCCCCCCCCE	40.04	27097102
58	Ubiquitination	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	-
58	Succinylation	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	-
58	Acetylation	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	22902405
58	Succinylation	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	-
59	Phosphorylation	NEATGGKYVPRAILV ECCCCCCCCCEEEEE	20.97	-
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCCCCCCC	28.64	23984901
75	Phosphorylation	LEPGTMDSVRSGPFG CCCCCCCCCCCCCCC	14.49	27097102
95	Phosphorylation	DNFVFGQSGAGNNWA CCEEECCCCCCCCCC	30.87	23984901
106	Phosphorylation	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	-
115	Phosphorylation	EGAELVDSVLDVVRK CHHHHHHHHHHHHHH	19.66	23984901
126	Phosphorylation	VVRKEAESCDCLQGF HHHHHHHHCCCCCEE	23.46	23984901
136	Phosphorylation	CLQGFQLTHSLGGGT CCCEEEEEEECCCCC	9.91	23984901
138	Phosphorylation	QGFQLTHSLGGGTGS CEEEEEEECCCCCCC	24.39	23984901
143	Phosphorylation	THSLGGGTGSGMGTL EEECCCCCCCCHHHH	31.30	23984901
145	Phosphorylation	SLGGGTGSGMGTLLI ECCCCCCCCHHHHHH	25.99	23984901
149	Phosphorylation	GTGSGMGTLLISKIR CCCCCHHHHHHHHHH	14.97	23984901
153	Phosphorylation	GMGTLLISKIREEYP CHHHHHHHHHHHHCC	23.23	23984901
168	Phosphorylation	DRIMNTFSVVPSPKV CCCCCCEECCCCCCC	21.84	23984901
172	Phosphorylation	NTFSVVPSPKVSDTV CCEECCCCCCCCCCE	26.24	30240740
216	Ubiquitination	DICFRTLKLTTPTYG HHHHHEECCCCCCCC	43.08	-
218	Phosphorylation	CFRTLKLTTPTYGDL HHHEECCCCCCCCCH	29.19	16641100
219	Phosphorylation	FRTLKLTTPTYGDLN HHEECCCCCCCCCHH	24.86	30240740
221	Phosphorylation	TLKLTTPTYGDLNHL EECCCCCCCCCHHHH	37.74	16641100
222	Phosphorylation	LKLTTPTYGDLNHLV ECCCCCCCCCHHHHH	15.17	16641100
239	S-nitrosylation	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	16418269
239	S-nitrosocysteine	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	-
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
274	Phosphorylation	MPGFAPLTSRGSQQY CCCCCCCCCCCCHHE	18.47	25403869
275	Phosphorylation	PGFAPLTSRGSQQYR CCCCCCCCCCCHHEE	42.18	22108457
278	Phosphorylation	APLTSRGSQQYRALT CCCCCCCCHHEEEEE	17.01	23984901
281	Phosphorylation	TSRGSQQYRALTVPE CCCCCHHEEEEEHHH	7.10	23984901
285	Phosphorylation	SQQYRALTVPELTQQ CHHEEEEEHHHHHHH	32.79	23984901
290	Phosphorylation	ALTVPELTQQVFDAK EEEHHHHHHHHHHHH	18.46	23984901
303	S-nitrosocysteine	AKNMMAACDPRHGRY HHHHHHHCCCCCCCE	5.55	-
303	S-nitrosylation	AKNMMAACDPRHGRY HHHHHHHCCCCCCCE	5.55	16418269
312	Phosphorylation	PRHGRYLTVAAVFRG CCCCCEEHHHHHHCC	10.12	23984901
318	Methylation	LTVAAVFRGRMSMKE EHHHHHHCCCCCHHH	25.80	-
322	Phosphorylation	AVFRGRMSMKEVDEQ HHHCCCCCHHHHHHH	25.91	23984901
324	Acetylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	22902405
324	Ubiquitination	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	-
336	Ubiquitination	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	-
338	Phosphorylation	LNVQNKNSSYFVEWI HHCCCCCCCHHEEEC	28.20	27097102
339	Phosphorylation	NVQNKNSSYFVEWIP HCCCCCCCHHEEECC	31.80	23984901
340	Phosphorylation	VQNKNSSYFVEWIPN CCCCCCCHHEEECCC	16.09	27097102
350	Ubiquitination	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	-
354	S-nitrosocysteine	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	-
354	S-nitrosylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	16418269
379	Acetylation	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	22902405
409	Phosphorylation	GMDEMEFTEAESNMN CCCHHCCCHHHHHHH	22.45	12631274
420	Phosphorylation	SNMNDLVSEYQQYQD HHHHHHHHHHHHHHH	37.57	12631274
438	Formation of an isopeptide bond	EEEEDFGEEAEEEA- HHHHHHHHHHHHHC-	54.77	-
438	5-glutamyl polyglutamate	EEEEDFGEEAEEEA- HHHHHHHHHHHHHC-	54.77	-

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	P39951	Uniprot
409	T	Phosphorylation	Kinase	GRK2	P25098	PSP
420	S	Phosphorylation	Kinase	GRK2	P25098	PSP

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 TBB5_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
HDAC6_HUMAN	HDAC6	physical	19961433

Drug and Disease Associations

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

Regulatory Network of TBB5_RAT

Related Literatures of Post-Translational Modification

S-nitrosylation
Reference	PubMed
"SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures."; Hao G., Derakhshan B., Shi L., Campagne F., Gross S.S.; Proc. Natl. Acad. Sci. U.S.A. 103:1012-1017(2006). Cited for: S-NITROSYLATION [LARGE SCALE ANALYSIS] AT CYS-12, AND MASSSPECTROMETRY.	16418269 [Abstract]

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