dbPTM

TBB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB1_HUMAN
UniProt AC	Q9H4B7
Protein Name	Tubulin beta-1 chain
Gene Name	TUBB1
Organism	Homo sapiens (Human).
Sequence Length	451
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 (By similarity)..
Protein Sequence	MREIVHIQIGQCGNQIGAKFWEMIGEEHGIDLAGSDRGASALQLERISVYYNEAYGRKYVPRAVLVDLEPGTMDSIRSSKLGALFQPDSFVHGNSGAGNNWAKGHYTEGAELIENVLEVVRHESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRIMNSFSVMPSPKVSDTVVEPYNAVLSIHQLIENADACFCIDNEALYDICFRTLKLTTPTYGDLNHLVSLTMSGITTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNTMAACDLRRGRYLTVACIFRGKMSTKEVDQQLLSVQTRNSSCFVEWIPNNVKVAVCDIPPRGLSMAATFIGNNTAIQEIFNRVSEHFSAMFKRKAFVHWYTSEGMDINEFGEAENNIHDLVSEYQQFQDAKAVLEEDEEVTEEAEMEPEDKGH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
35	Phosphorylation	HGIDLAGSDRGASAL HCCCCCCCCCCCCHH	20.66	27535140
40	Phosphorylation	AGSDRGASALQLERI CCCCCCCCHHHHEEE	32.13	28270605
55	Phosphorylation	SVYYNEAYGRKYVPR EEEEEHHCCCCCCCE	15.98	-
58	Acetylation	YNEAYGRKYVPRAVL EEHHCCCCCCCEEEE	46.35	50084403
72	Phosphorylation	LVDLEPGTMDSIRSS EEECCCCCHHHHHHC	28.64	23532336
75	Phosphorylation	LEPGTMDSIRSSKLG CCCCCHHHHHHCCCC	14.74	27535140
78	Phosphorylation	GTMDSIRSSKLGALF CCHHHHHHCCCCCCC	30.10	27535140
79	Phosphorylation	TMDSIRSSKLGALFQ CHHHHHHCCCCCCCC	23.27	28270605
81	Ubiquitination	DSIRSSKLGALFQPD HHHHHCCCCCCCCCC	5.39	22817900
89	Phosphorylation	GALFQPDSFVHGNSG CCCCCCCCEECCCCC	35.53	28270605
95	Phosphorylation	DSFVHGNSGAGNNWA CCEECCCCCCCCCCC	34.31	28270605
103	Ubiquitination	GAGNNWAKGHYTEGA CCCCCCCCCCCCHHH	37.52	22817900
138	Phosphorylation	QGFQIVHSLGGGTGS CCEEEEEECCCCCCC	20.16	25332170
143	Phosphorylation	VHSLGGGTGSGMGTL EEECCCCCCCHHHHH	31.30	28270605
145	Phosphorylation	SLGGGTGSGMGTLLM ECCCCCCCHHHHHHH	25.99	28270605
149	Phosphorylation	GTGSGMGTLLMNKIR CCCCHHHHHHHHHHH	14.07	28270605
154	Ubiquitination	MGTLLMNKIREEYPD HHHHHHHHHHHHCCC	29.22	-
159	Phosphorylation	MNKIREEYPDRIMNS HHHHHHHCCCHHHHC	12.99	28152594
166	Phosphorylation	YPDRIMNSFSVMPSP CCCHHHHCCCCCCCC	11.08	20860994
168	Phosphorylation	DRIMNSFSVMPSPKV CHHHHCCCCCCCCCC	19.82	-
172	Phosphorylation	NSFSVMPSPKVSDTV HCCCCCCCCCCCCCC	21.18	16371510
194	Ubiquitination	LSIHQLIENADACFC HHHHHHHHCCCEEEE	55.76	22817900
208	Phosphorylation	CIDNEALYDICFRTL EECHHHHHHHHHHCC	15.43	25884760
216	Ubiquitination	DICFRTLKLTTPTYG HHHHHCCCCCCCCCC	43.08	21890473
218	Phosphorylation	CFRTLKLTTPTYGDL HHHCCCCCCCCCCCH	29.19	-
219	Phosphorylation	FRTLKLTTPTYGDLN HHCCCCCCCCCCCHH	24.86	-
221	Phosphorylation	TLKLTTPTYGDLNHL CCCCCCCCCCCHHHH	37.74	-
222	Phosphorylation	LKLTTPTYGDLNHLV CCCCCCCCCCHHHHH	15.17	-
230	Ubiquitination	GDLNHLVSLTMSGIT CCHHHHHHEECCCCC	25.20	23000965
238	Phosphorylation	LTMSGITTSLRFPGQ EECCCCCCCCCCCCC	24.68	23532336
239	Phosphorylation	TMSGITTSLRFPGQL ECCCCCCCCCCCCCC	14.64	23532336
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	23000965
252	Acetylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	15821807
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
274	Phosphorylation	MPGFAPLTAQGSQQY CCCCCCCCCCCHHHH	18.84	28270605
278	Phosphorylation	APLTAQGSQQYRALS CCCCCCCHHHHHHHH	11.30	21406692
281	Phosphorylation	TAQGSQQYRALSVAE CCCCHHHHHHHHHHH	7.10	28270605
285	Phosphorylation	SQQYRALSVAELTQQ HHHHHHHHHHHHHHH	20.49	23532336
324	Acetylation	FRGKMSTKEVDQQLL ECCCCCHHHHHHHHH	48.73	50084399
328	Ubiquitination	MSTKEVDQQLLSVQT CCHHHHHHHHHHHHC	40.78	23503661
338	Phosphorylation	LSVQTRNSSCFVEWI HHHHCCCCCCEEEEC	25.78	28270605
339	Phosphorylation	SVQTRNSSCFVEWIP HHHCCCCCCEEEECC	18.34	28270605
350	Ubiquitination	EWIPNNVKVAVCDIP EECCCCEEEEEECCC	26.97	23503661
390	Acetylation	EHFSAMFKRKAFVHW HHHHHHHHCCCCEEE	39.65	30593151
439	Phosphorylation	LEEDEEVTEEAEMEP HHCCHHHHHHHHCCC	31.24	20058876
440	5-glutamyl polyglutamate	EEDEEVTEEAEMEPE HCCHHHHHHHHCCCC	61.46	-
440	Formation of an isopeptide bond	EEDEEVTEEAEMEPE HCCHHHHHHHHCCCC	61.46	-

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	P06493	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
172	S	Phosphorylation		16371510
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
278	Phosphorylation	287 (9)	A ⇒ V	rs139473150	Platelet distribution width	27863252

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYUA_HUMAN	SNCA	physical	16216085
SC6A3_HUMAN	SLC6A3	physical	16216085
TBA1B_HUMAN	TUBA1B	physical	16216085
THIL_HUMAN	ACAT1	physical	22939629
TOIP2_HUMAN	TOR1AIP2	physical	28514442
IFG15_HUMAN	TOR1AIP2	physical	28514442
DNLZ_HUMAN	DNLZ	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613112	Macrothrombocytopenia, autosomal dominant, TUBB1-related (MAD-TUBB1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB06772	Cabazitaxel
DB01394	Colchicine
DB01248	Docetaxel
DB01229	Paclitaxel
DB00309	Vindesine

Regulatory Network of TBB1_HUMAN

Related Literatures of Post-Translational Modification

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