dbPTM

TBG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBG2_HUMAN
UniProt AC	Q9NRH3
Protein Name	Tubulin gamma-2 chain
Gene Name	TUBG2
Organism	Homo sapiens (Human).
Sequence Length	451
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome .
Protein Description	Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation (By similarity)..
Protein Sequence	MPREIITLQLGQCGNQIGFEFWKQLCAEHGISPEGIVEEFATEGTDRKDVFFYQADDEHYIPRAVLLDLEPRVIHSILNSPYAKLYNPENIYLSEHGGGAGNNWASGFSQGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPYQDEMSDVVVQPYNSLLTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLMTGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVSTGRDRQTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFESSCQQFDKLRKRDAFLEQFRKEDMFKDNFDEMDRSREVVQELIDEYHAATQPDYISWGTQEQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	Phosphorylation	LCAEHGISPEGIVEE HHHHCCCCCCHHHHH	22.84	28509920
42	Phosphorylation	GIVEEFATEGTDRKD HHHHHHHCCCCCCCC	40.02	28509920
45	Phosphorylation	EEFATEGTDRKDVFF HHHHCCCCCCCCEEE	26.80	28509920
48	Ubiquitination	ATEGTDRKDVFFYQA HCCCCCCCCEEEEEC	62.14	21890473
80	Phosphorylation	VIHSILNSPYAKLYN HHHHHHCCCCHHHCC	18.82	25159151
82	Phosphorylation	HSILNSPYAKLYNPE HHHHCCCCHHHCCHH	19.05	23186163
84	Ubiquitination	ILNSPYAKLYNPENI HHCCCCHHHCCHHHE	45.74	21906983
113	Ubiquitination	SGFSQGEKIHEDIFD CCCCCCCCHHHHHHH	57.07	-
129	Phosphorylation	IDREADGSDSLEGFV HCCCCCCCCCCCEEE	25.27	22067460
131	Phosphorylation	READGSDSLEGFVLC CCCCCCCCCCEEEEE	29.98	22817900
169	Phosphorylation	PKKLVQTYSVFPYQD CCCCEEEEECCCCCC	5.92	-
186	Phosphorylation	SDVVVQPYNSLLTLK CCCEEEECCHHHHHH	10.57	-
201	Glutathionylation	RLTQNADCVVVLDNT HHHCCCCEEEEECCH	2.02	22555962
249	Sulfoxidation	TLRYPGYMNNDLIGL CCCCCCCCCCCHHHH	4.72	28183972
263	Phosphorylation	LIASLIPTPRLHFLM HHHHHCCCCCEEEEC	17.66	28060719
274	Phosphorylation	HFLMTGYTPLTTDQS EEECCCCCCCCCCCH	17.11	24719451
277	Phosphorylation	MTGYTPLTTDQSVAS CCCCCCCCCCCHHHH	29.54	23403867
278	Phosphorylation	TGYTPLTTDQSVASV CCCCCCCCCCHHHHC	39.46	30576142
281	Phosphorylation	TPLTTDQSVASVRKT CCCCCCCHHHHCCHH	23.59	23403867
284	Phosphorylation	TTDQSVASVRKTTVL CCCCHHHHCCHHHHH	21.94	28348404
287	Ubiquitination	QSVASVRKTTVLDVM CHHHHCCHHHHHHHH	46.52	-
295	Methylation	TTVLDVMRRLLQPKN HHHHHHHHHHHCCCC	26.41	-
301	Ubiquitination	MRRLLQPKNVMVSTG HHHHHCCCCEEEECC	49.57	21890473
306	Phosphorylation	QPKNVMVSTGRDRQT CCCCEEEECCCCCCC	13.67	-
307	Phosphorylation	PKNVMVSTGRDRQTN CCCEEEECCCCCCCC	25.48	-
336	Phosphorylation	DPTQVHKSLQRIRER CHHHHHHHHHHHHHH	18.17	27251275
344	Ubiquitination	LQRIRERKLANFIPW HHHHHHHHHHHCCCC	47.39	-
363	Ubiquitination	IQVALSRKSPYLPSA HHHHHHCCCCCCCCH	53.02	-
364	Phosphorylation	QVALSRKSPYLPSAH HHHHHCCCCCCCCHH	20.05	22067460
382	Phosphorylation	GLMMANHTSISSLFE CCCCCCCCCHHHHHH	27.80	22210691
383	Phosphorylation	LMMANHTSISSLFES CCCCCCCCHHHHHHH	16.96	22210691
390	Phosphorylation	SISSLFESSCQQFDK CHHHHHHHHHHHHHH	29.13	-
391	Phosphorylation	ISSLFESSCQQFDKL HHHHHHHHHHHHHHH	14.56	-
410	Ubiquitination	AFLEQFRKEDMFKDN HHHHHHHHHHHHHCC	60.39	21890473
415	Ubiquitination	FRKEDMFKDNFDEMD HHHHHHHHCCHHHHH	45.16	21890473

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
80	S	Phosphorylation	Kinase	CDK2	P24941	PSP
131	S	Phosphorylation	Kinase	BRSK1	Q8TDC3	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
131	S	Phosphorylation		-
Phosphorylation at Ser-131 by BRSK1 regulates centrosome duplication, possibly by mediating relocation of gamma-tubulin and its associated proteins from the cytoplasm to the centrosome.

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 TBG2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GCP5_HUMAN	TUBGCP5	physical	28514442
MZT2A_HUMAN	MZT2A	physical	28514442
GCP4_HUMAN	TUBGCP4	physical	28514442
GCP6_HUMAN	TUBGCP6	physical	28514442
TBG1_HUMAN	TUBG1	physical	28514442
GCP3_HUMAN	TUBGCP3	physical	28514442
MZT2B_HUMAN	MZT2B	physical	28514442
GCP2_HUMAN	TUBGCP2	physical	28514442
NDK7_HUMAN	NME7	physical	28514442
TCPG_HUMAN	CCT3	physical	28514442
TCPB_HUMAN	CCT2	physical	28514442
TCPD_HUMAN	CCT4	physical	28514442
PHLP_HUMAN	PDCL	physical	28514442
TCPA_HUMAN	TCP1	physical	28514442
TCPW_HUMAN	CCT6B	physical	28514442
TCPZ_HUMAN	CCT6A	physical	28514442
TXND9_HUMAN	TXNDC9	physical	28514442
TCPH_HUMAN	CCT7	physical	28514442

Drug and Disease Associations

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

Regulatory Network of TBG2_HUMAN

Related Literatures of Post-Translational Modification

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