dbPTM

TBB8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB8_HUMAN
UniProt AC	Q3ZCM7
Protein Name	Tubulin beta-8 chain {ECO:0000305}
Gene Name	TUBB8 {ECO:0000312\|HGNC:HGNC:20773}
Organism	Homo sapiens (Human).
Sequence Length	444
Subcellular Localization	Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, spindle .
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). TUBB8 has a key role in meiotic spindle assembly and oocyte maturation. [PubMed: 26789871]
Protein Sequence	MREIVLTQIGQCGNQIGAKFWEVISDEHAIDSAGTYHGDSHLQLERINVYYNEASGGRYVPRAVLVDLEPGTMDSVRSGPFGQVFRPDNFIFGQCGAGNNWAKGHYTEGAELMESVMDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLLSKIREEYPDRIINTFSILPSPKVSDTVVEPYNATLSVHQLIENADETFCIDNEALYDICSKTLKLPTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVAELTQQMFDAKNMMAACDPRHGRYLTAAAIFRGRMPMREVDEQMFNIQDKNSSYFADWLPNNVKTAVCDIPPRGLKMSATFIGNNTAIQELFKRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDEEYAEEEVA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MREIVLTQIGQCGN -CCEEEEEEEHHCCC	13.77	-
10	Ubiquitination	EIVLTQIGQCGNQIG EEEEEEEHHCCCHHH	13.60	21963094
31	Ubiquitination	ISDEHAIDSAGTYHG HCCCCCCCCCCCCCC	32.97	22817900
40	Phosphorylation	AGTYHGDSHLQLERI CCCCCCCCCEEEEEE	30.59	-
42	Ubiquitination	TYHGDSHLQLERINV CCCCCCCEEEEEEEE	7.82	21963094
50	Ubiquitination	QLERINVYYNEASGG EEEEEEEEEECCCCC	8.97	21963094
59	Phosphorylation	NEASGGRYVPRAVLV ECCCCCCCCCEEEEE	20.34	-
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCCCCCCC	28.64	20873877
75	Phosphorylation	LEPGTMDSVRSGPFG CCCCCCCCCCCCCCC	14.49	28555341
78	Phosphorylation	GTMDSVRSGPFGQVF CCCCCCCCCCCCCCC	48.97	29083192
82	Ubiquitination	SVRSGPFGQVFRPDN CCCCCCCCCCCCCCC	26.35	21963094
99	Ubiquitination	FGQCGAGNNWAKGHY EEECCCCCCCCCCCC	40.09	23000965
103	Ubiquitination	GAGNNWAKGHYTEGA CCCCCCCCCCCHHHH	37.52	22817900
106	Phosphorylation	NNWAKGHYTEGAELM CCCCCCCCHHHHHHH	18.37	23403867
107	Phosphorylation	NWAKGHYTEGAELME CCCCCCCHHHHHHHH	23.44	23403867
115	Phosphorylation	EGAELMESVMDVVRK HHHHHHHHHHHHHHH	14.58	23403867
122	Ubiquitination	SVMDVVRKEAESCDC HHHHHHHHHHHHCCC	50.06	21906983
122	Acetylation	SVMDVVRKEAESCDC HHHHHHHHHHHHCCC	50.06	26051181
126	Phosphorylation	VVRKEAESCDCLQGF HHHHHHHHCCCCCEE	23.46	30108239
136	Phosphorylation	CLQGFQLTHSLGGGT CCCEEEEEECCCCCC	9.91	30108239
138	Phosphorylation	QGFQLTHSLGGGTGS CEEEEEECCCCCCCC	24.39	23663014
140	Ubiquitination	FQLTHSLGGGTGSGM EEEEECCCCCCCCCH	35.18	23000965
143	Phosphorylation	THSLGGGTGSGMGTL EECCCCCCCCCHHHH	31.30	30108239
144	Ubiquitination	HSLGGGTGSGMGTLL ECCCCCCCCCHHHHH	26.02	22817900
145	Phosphorylation	SLGGGTGSGMGTLLL CCCCCCCCCHHHHHH	25.99	27486199
149	Phosphorylation	GTGSGMGTLLLSKIR CCCCCHHHHHHHHHH	12.82	30108239
153	Phosphorylation	GMGTLLLSKIREEYP CHHHHHHHHHHHHCC	26.46	27486199
154	Ubiquitination	MGTLLLSKIREEYPD HHHHHHHHHHHHCCC	45.83	21963094
154	Acetylation	MGTLLLSKIREEYPD HHHHHHHHHHHHCCC	45.83	25953088
159	Phosphorylation	LSKIREEYPDRIINT HHHHHHHCCCCEEEE	12.99	28152594
168	Phosphorylation	DRIINTFSILPSPKV CCEEEEECCCCCCCC	22.60	-
172	Phosphorylation	NTFSILPSPKVSDTV EEECCCCCCCCCCCE	33.63	16371510
180	Ubiquitination	PKVSDTVVEPYNATL CCCCCCEECCCCCCE	7.14	23000965
183	Phosphorylation	SDTVVEPYNATLSVH CCCEECCCCCCEEHH	12.15	25884760
185	Ubiquitination	TVVEPYNATLSVHQL CEECCCCCCEEHHHH	12.22	22817900
209	Ubiquitination	IDNEALYDICSKTLK ECHHHHHHHHHCCCC	35.95	22817900
216	Ubiquitination	DICSKTLKLPTPTYG HHHHCCCCCCCCCCH	58.62	21906983
219	Phosphorylation	SKTLKLPTPTYGDLN HCCCCCCCCCCHHHH	38.40	21082442
221	Phosphorylation	TLKLPTPTYGDLNHL CCCCCCCCCHHHHHH	42.48	21082442
222	Phosphorylation	LKLPTPTYGDLNHLV CCCCCCCCHHHHHHH	15.17	21082442
225	Ubiquitination	PTPTYGDLNHLVSAT CCCCCHHHHHHHHHH	3.65	22817900
230	Phosphorylation	GDLNHLVSATMSGVT HHHHHHHHHHHCCCH	25.12	22817900
234	Phosphorylation	HLVSATMSGVTTCLR HHHHHHHCCCHHHHH	26.25	-
250	Ubiquitination	PGQLNADLRKLAVNM CCCCCHHHHHHHHHC	4.90	22817900
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	27667366
267	Sulfoxidation	FPRLHFFMPGFAPLT CCCCCEECCCCCCCC	2.87	28183972
274	Phosphorylation	MPGFAPLTSRGSQQY CCCCCCCCCCCHHHH	18.47	22617229
275	Phosphorylation	PGFAPLTSRGSQQYR CCCCCCCCCCHHHHH	42.18	22617229
276	Methylation	GFAPLTSRGSQQYRA CCCCCCCCCHHHHHE	43.47	-
278	Phosphorylation	APLTSRGSQQYRALT CCCCCCCHHHHHEEH	17.01	22617229
281	Phosphorylation	TSRGSQQYRALTVAE CCCCHHHHHEEHHHH	7.10	28787133
285	Phosphorylation	SQQYRALTVAELTQQ HHHHHEEHHHHHHHH	19.38	-
290	Ubiquitination	ALTVAELTQQMFDAK EEHHHHHHHHHHCCC	14.30	22817900
290	Phosphorylation	ALTVAELTQQMFDAK EEHHHHHHHHHHCCC	14.30	-
297	Ubiquitination	TQQMFDAKNMMAACD HHHHHCCCHHHHHCC	47.42	22817900
303	S-palmitoylation	AKNMMAACDPRHGRY CCHHHHHCCCCCCCH	5.55	29575903
318	Methylation	LTAAAIFRGRMPMRE HHHHHHHCCCCCCHH	26.20	-
339	Phosphorylation	NIQDKNSSYFADWLP CCCCCCCHHHCCCCC	33.39	-
340	Phosphorylation	IQDKNSSYFADWLPN CCCCCCHHHCCCCCC	11.56	-
351	Phosphorylation	WLPNNVKTAVCDIPP CCCCCCCEEECCCCC	21.75	-
354	S-palmitoylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	29575903
362	Ubiquitination	DIPPRGLKMSATFIG CCCCCCCCEEEEEEC	33.36	22817900
380	Methylation	AIQELFKRVSEQFTA HHHHHHHHHHHHHHH	29.84	24390987
392	Ubiquitination	FTAMFRRKAFLHWYT HHHHHHHHHHHHHHC	38.95	-
399	Phosphorylation	KAFLHWYTGEGMDEM HHHHHHHCCCCCCHH	24.46	24275569
409	Phosphorylation	GMDEMEFTEAESNMN CCCHHCCCHHHHHHH	22.45	12631274
420	Phosphorylation	SNMNDLVSEYQQYQD HHHHHHHHHHHHHHH	37.57	12631274
422	Phosphorylation	MNDLVSEYQQYQDAT HHHHHHHHHHHHHCC	8.07	22817900
425	Phosphorylation	LVSEYQQYQDATAEE HHHHHHHHHHCCCCH	7.88	22817900
429	Phosphorylation	YQQYQDATAEEEEDE HHHHHHCCCCHHHHH	42.78	-
436	5-glutamyl polyglutamate	TAEEEEDEEYAEEEV CCCHHHHHHHHHHHH	57.07	-
436	Formation of an isopeptide bond	TAEEEEDEEYAEEEV CCCHHHHHHHHHHHH	57.07	-

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
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
Oops, there are no SNP-PTM records of TBB8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TBA1C_HUMAN	TUBA1C	physical	22863883
TBB2A_HUMAN	TUBB2A	physical	22863883

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 TBB8_HUMAN

Related Literatures of Post-Translational Modification

show