dbPTM

TBCB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBCB_HUMAN
UniProt AC	Q99426
Protein Name	Tubulin-folding cofactor B
Gene Name	TBCB
Organism	Homo sapiens (Human).
Sequence Length	244
Subcellular Localization	Cytoplasm . Cytoplasm, cytoskeleton . Colocalizes with microtubules. In differentiated neurons, located in the cytoplasm. In differentiating neurons, accumulates at the growth cone.
Protein Description	Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer. [PubMed: 9265649 Involved in regulation of tubulin heterodimer dissociation. May function as a negative regulator of axonal growth (By similarity]
Protein Sequence	MEVTGVSAPTVTVFISSSLNTFRSEKRYSRSLTIAEFKCKLELLVGSPASCMELELYGVDDKFYSKLDQEDALLGSYPVDDGCRIHVIDHSGARLGEYEDVSRVEKYTISQEAYDQRQDTVRSFLKRSKLGRYNEEERAQQEAEAAQRLAEEKAQASSIPVGSRCEVRAAGQSPRRGTVMYVGLTDFKPGYWIGVRYDEPLGKNDGSVNGKRYFECQAKYGAFVKPAVVTVGDFPEEDYGLDEI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEVTGVSA -------CCCCCCCC	9.37	22223895
15	Ubiquitination	APTVTVFISSSLNTF CCEEEEEEECCCCHH	3.20	32015554
29	Phosphorylation	FRSEKRYSRSLTIAE HCCCCCCCCCEEHHE	21.30	29514088
31	Phosphorylation	SEKRYSRSLTIAEFK CCCCCCCCEEHHEEE	24.75	30266825
33	Phosphorylation	KRYSRSLTIAEFKCK CCCCCCEEHHEEEEE	21.27	30266825
38	Ubiquitination	SLTIAEFKCKLELLV CEEHHEEEEEEEEEC	23.20	33845483
55	Ubiquitination	PASCMELELYGVDDK CCCCEEEEEECCCHH	27.00	23000965
62	Ubiquitination	ELYGVDDKFYSKLDQ EEECCCHHHHHCCCH	41.56	32015554
65	Phosphorylation	GVDDKFYSKLDQEDA CCCHHHHHCCCHHHC	29.85	15831477
66	Ubiquitination	VDDKFYSKLDQEDAL CCHHHHHCCCHHHCC	44.71	32015554
91	Phosphorylation	RIHVIDHSGARLGEY EEEEECCCCCCCCCC	30.33	20068231
98	Phosphorylation	SGARLGEYEDVSRVE CCCCCCCCCCHHHEE	18.68	21945579
102	Phosphorylation	LGEYEDVSRVEKYTI CCCCCCHHHEEEEEC	42.82	21945579
102	Ubiquitination	LGEYEDVSRVEKYTI CCCCCCHHHEEEEEC	42.82	32142685
106	Ubiquitination	EDVSRVEKYTISQEA CCHHHEEEEECCHHH	44.85	21890473
106	2-Hydroxyisobutyrylation	EDVSRVEKYTISQEA CCHHHEEEEECCHHH	44.85	-
106	Ubiquitination	EDVSRVEKYTISQEA CCHHHEEEEECCHHH	44.85	23000965
107	Phosphorylation	DVSRVEKYTISQEAY CHHHEEEEECCHHHH	8.87	28796482
108	Phosphorylation	VSRVEKYTISQEAYD HHHEEEEECCHHHHH	25.81	28152594
110	Phosphorylation	RVEKYTISQEAYDQR HEEEEECCHHHHHHH	17.73	17525332
114	Phosphorylation	YTISQEAYDQRQDTV EECCHHHHHHHHHHH	16.32	28674151
120	Phosphorylation	AYDQRQDTVRSFLKR HHHHHHHHHHHHHHH	14.96	23312004
123	Phosphorylation	QRQDTVRSFLKRSKL HHHHHHHHHHHHHHH	30.51	24719451
128	Phosphorylation	VRSFLKRSKLGRYNE HHHHHHHHHHCCCCH	30.55	15831477
133	Phosphorylation	KRSKLGRYNEEERAQ HHHHHCCCCHHHHHH	25.73	-
137	Ubiquitination	LGRYNEEERAQQEAE HCCCCHHHHHHHHHH	47.33	32015554
152	Neddylation	AAQRLAEEKAQASSI HHHHHHHHHHHHHCC	48.35	32015554
152	Ubiquitination	AAQRLAEEKAQASSI HHHHHHHHHHHHHCC	48.35	22817900
153	Acetylation	AQRLAEEKAQASSIP HHHHHHHHHHHHCCC	36.99	23954790
153	2-Hydroxyisobutyrylation	AQRLAEEKAQASSIP HHHHHHHHHHHHCCC	36.99	-
153	Malonylation	AQRLAEEKAQASSIP HHHHHHHHHHHHCCC	36.99	26320211
153	Ubiquitination	AQRLAEEKAQASSIP HHHHHHHHHHHHCCC	36.99	21906983
168	Ubiquitination	VGSRCEVRAAGQSPR CCCCCEEEECCCCCC	9.09	-
168	Acetylation	VGSRCEVRAAGQSPR CCCCCEEEECCCCCC	9.09	19608861
168	Ubiquitination	VGSRCEVRAAGQSPR CCCCCEEEECCCCCC	9.09	23000965
173	Phosphorylation	EVRAAGQSPRRGTVM EEEECCCCCCCCEEE	21.32	20068231
174	Ubiquitination	VRAAGQSPRRGTVMY EEECCCCCCCCEEEE	23.31	23000965
178	Phosphorylation	GQSPRRGTVMYVGLT CCCCCCCEEEEEECC	10.57	26074081
181	Phosphorylation	PRRGTVMYVGLTDFK CCCCEEEEEECCCCC	6.24	26074081
185	Phosphorylation	TVMYVGLTDFKPGYW EEEEEECCCCCCCEE	33.20	26074081
188	Ubiquitination	YVGLTDFKPGYWIGV EEECCCCCCCEEEEE	40.10	32015554
203	Ubiquitination	RYDEPLGKNDGSVNG EECCCCCCCCCCCCC	60.59	21906983
203	Malonylation	RYDEPLGKNDGSVNG EECCCCCCCCCCCCC	60.59	26320211
203	Neddylation	RYDEPLGKNDGSVNG EECCCCCCCCCCCCC	60.59	32015554
211	Ubiquitination	NDGSVNGKRYFECQA CCCCCCCEEEEEEEH	38.43	-
219	Ubiquitination	RYFECQAKYGAFVKP EEEEEEHCCCCEECC	20.52	23000965
219	Acetylation	RYFECQAKYGAFVKP EEEEEEHCCCCEECC	20.52	19608861
219	Ubiquitination	RYFECQAKYGAFVKP EEEEEEHCCCCEECC	20.52	21890473
220	Phosphorylation	YFECQAKYGAFVKPA EEEEEHCCCCEECCE	19.39	26356563
225	Ubiquitination	AKYGAFVKPAVVTVG HCCCCEECCEEEEEC	22.32	23000965
230	Phosphorylation	FVKPAVVTVGDFPEE EECCEEEEECCCCHH	16.51	26356563
239	Phosphorylation	GDFPEEDYGLDEI-- CCCCHHHCCCCCC--	23.91	28674151

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
65	S	Phosphorylation	Kinase	PAK1	Q13153	Uniprot
128	S	Phosphorylation	Kinase	PAK1	Q13153	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	GAN	Q9H2C0	PMID:16303566

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TBCB_HUMAN !!

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 TBCB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GAN_HUMAN	GAN	physical	16303566
TXND5_HUMAN	TXNDC5	physical	22939629
TCTP_HUMAN	TPT1	physical	22939629
AL7A1_HUMAN	ALDH7A1	physical	22863883
ASNS_HUMAN	ASNS	physical	22863883
CPNS1_HUMAN	CAPNS1	physical	22863883
KCRB_HUMAN	CKB	physical	22863883
ISOC1_HUMAN	ISOC1	physical	22863883
MARE1_HUMAN	MAPRE1	physical	22863883
PDIA4_HUMAN	PDIA4	physical	22863883
PP1A_HUMAN	PPP1CA	physical	22863883
PLPHP_HUMAN	PROSC	physical	22863883
RISC_HUMAN	SCPEP1	physical	22863883
RUXF_HUMAN	SNRPF	physical	22863883
STK24_HUMAN	STK24	physical	22863883
UBFD1_HUMAN	UBFD1	physical	22863883
VINC_HUMAN	VCL	physical	22863883
1433E_HUMAN	YWHAE	physical	22863883
1433F_HUMAN	YWHAH	physical	22863883
ANXA6_HUMAN	ANXA6	physical	26344197
D2HDH_HUMAN	D2HGDH	physical	26344197
HXK2_HUMAN	HK2	physical	26344197
LGSN_HUMAN	LGSN	physical	26344197
PLBL2_HUMAN	PLBD2	physical	26344197
PP14B_HUMAN	PPP1R14B	physical	26344197
XPP1_HUMAN	XPNPEP1	physical	26344197
TBA4A_HUMAN	TUBA4A	physical	28514442

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 TBCB_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-219, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASSSPECTROMETRY.	17525332 [Abstract]
"p21-activated kinase 1 regulates microtubule dynamics byphosphorylating tubulin cofactor B."; Vadlamudi R.K., Barnes C.J., Rayala S., Li F., Balasenthil S.,Marcus S., Goodson H.V., Sahin A.A., Kumar R.; Mol. Cell. Biol. 25:3726-3736(2005). Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-65 AND SER-128, ANDMUTAGENESIS OF SER-65 AND SER-128.	15831477 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98 AND TYR-114, AND MASSSPECTROMETRY.	15592455 [Abstract]