dbPTM

TACC3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TACC3_HUMAN
UniProt AC	Q9Y6A5
Protein Name	Transforming acidic coiled-coil-containing protein 3
Gene Name	TACC3
Organism	Homo sapiens (Human).
Sequence Length	838
Subcellular Localization	Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Cytoplasm, cytoskeleton, spindle pole . In complex with CKAP5 localized to microtubule plus-ends in mitosis and interphase. In complex
Protein Description	Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors (By similarity). Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension. [PubMed: 21297582]
Protein Sequence	MSLQVLNDKNVSNEKNTENCDFLFSPPEVTGRSSVLRVSQKENVPPKNLAKAMKVTFQTPLRDPQTHRILSPSMASKLEAPFTQDDTLGLENSHPVWTQKENQQLIKEVDAKTTHGILQKPVEADTDLLGDASPAFGSGSSSESGPGALADLDCSSSSQSPGSSENQMVSPGKVSGSPEQAVEENLSSYSLDRRVTPASETLEDPCRTESQHKAETPHGAEEECKAETPHGAEEECRHGGVCAPAAVATSPPGAIPKEACGGAPLQGLPGEALGCPAGVGTPVPADGTQTLTCAHTSAPESTAPTNHLVAGRAMTLSPQEEVAAGQMASSSRSGPVKLEFDVSDGATSKRAPPPRRLGERSGLKPPLRKAAVRQQKAPQEVEEDDGRSGAGEDPPMPASRGSYHLDWDKMDDPNFIPFGGDTKSGCSEAQPPESPETRLGQPAAEQLHAGPATEEPGPCLSQQLHSASAEDTPVVQLAAETPTAESKERALNSASTSLPTSCPGSEPVPTHQQGQPALELKEESFRDPAEVLGTGAEVDYLEQFGTSSFKESALRKQSLYLKFDPLLRDSPGRPVPVATETSSMHGANETPSGRPREAKLVEFDFLGALDIPVPGPPPGVPAPGGPPLSTGPIVDLLQYSQKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSLQVLNDK ------CCCCCCCCC	27.75	19413330
2	Phosphorylation	------MSLQVLNDK ------CCCCCCCCC	27.75	19413330
9	Acetylation	SLQVLNDKNVSNEKN CCCCCCCCCCCCCCC	59.17	25953088
9	Ubiquitination	SLQVLNDKNVSNEKN CCCCCCCCCCCCCCC	59.17	29967540
12	Phosphorylation	VLNDKNVSNEKNTEN CCCCCCCCCCCCCCC	48.98	21712546
17	Phosphorylation	NVSNEKNTENCDFLF CCCCCCCCCCCCCCC	39.38	28450419
25	Phosphorylation	ENCDFLFSPPEVTGR CCCCCCCCCCCCCCC	41.51	30266825
30	Phosphorylation	LFSPPEVTGRSSVLR CCCCCCCCCCCCEEE	25.80	28450419
32	Methylation	SPPEVTGRSSVLRVS CCCCCCCCCCEEEHH	19.18	115389615
33	Phosphorylation	PPEVTGRSSVLRVSQ CCCCCCCCCEEEHHH	26.58	26074081
34	Phosphorylation	PEVTGRSSVLRVSQK CCCCCCCCEEEHHHC	24.66	28450419
39	Phosphorylation	RSSVLRVSQKENVPP CCCEEEHHHCCCCCC	29.15	25159151
51	Trimethylation	VPPKNLAKAMKVTFQ CCCHHHHHHHCEEEC	52.78	-
51	Methylation	VPPKNLAKAMKVTFQ CCCHHHHHHHCEEEC	52.78	-
54	Trimethylation	KNLAKAMKVTFQTPL HHHHHHHCEEECCCC	42.87	-
54	Acetylation	KNLAKAMKVTFQTPL HHHHHHHCEEECCCC	42.87	25953088
54	Methylation	KNLAKAMKVTFQTPL HHHHHHHCEEECCCC	42.87	-
56	Phosphorylation	LAKAMKVTFQTPLRD HHHHHCEEECCCCCC	12.42	29255136
59	Phosphorylation	AMKVTFQTPLRDPQT HHCEEECCCCCCCCC	21.79	23401153
66	Phosphorylation	TPLRDPQTHRILSPS CCCCCCCCCCCCCHH	20.64	23403867
71	Phosphorylation	PQTHRILSPSMASKL CCCCCCCCHHHHHHC	16.74	29255136
73	Phosphorylation	THRILSPSMASKLEA CCCCCCHHHHHHCCC	24.49	30266825
76	Phosphorylation	ILSPSMASKLEAPFT CCCHHHHHHCCCCCC	29.18	29255136
77	Acetylation	LSPSMASKLEAPFTQ CCHHHHHHCCCCCCC	40.59	25953088
83	Phosphorylation	SKLEAPFTQDDTLGL HHCCCCCCCCCCCCC	29.99	22199227
87	Phosphorylation	APFTQDDTLGLENSH CCCCCCCCCCCCCCC	30.89	28122231
100	Ubiquitination	SHPVWTQKENQQLIK CCCCCCHHHHHHHHH	51.78	29967540
170	Phosphorylation	SSENQMVSPGKVSGS CCCCCCCCCCCCCCC	23.69	26074081
175	Phosphorylation	MVSPGKVSGSPEQAV CCCCCCCCCCHHHHH	36.72	30266825
177	Phosphorylation	SPGKVSGSPEQAVEE CCCCCCCCHHHHHHH	20.11	25159151
187	Phosphorylation	QAVEENLSSYSLDRR HHHHHHHHHCCCCCC	38.52	29978859
188	Phosphorylation	AVEENLSSYSLDRRV HHHHHHHHCCCCCCC	23.16	29978859
189	Phosphorylation	VEENLSSYSLDRRVT HHHHHHHCCCCCCCC	15.18	29978859
190	Phosphorylation	EENLSSYSLDRRVTP HHHHHHCCCCCCCCC	26.24	29978859
190	Ubiquitination	EENLSSYSLDRRVTP HHHHHHCCCCCCCCC	26.24	22817900
196	Phosphorylation	YSLDRRVTPASETLE CCCCCCCCCCHHHCC	16.01	21815630
196	Ubiquitination	YSLDRRVTPASETLE CCCCCCCCCCHHHCC	16.01	23503661
199	Phosphorylation	DRRVTPASETLEDPC CCCCCCCHHHCCCCC	32.11	21815630
202	Ubiquitination	VTPASETLEDPCRTE CCCCHHHCCCCCCCH	6.53	21890473
208	Phosphorylation	TLEDPCRTESQHKAE HCCCCCCCHHHHHCC	46.86	28555341
210	Phosphorylation	EDPCRTESQHKAETP CCCCCCHHHHHCCCC	36.65	28555341
216	Phosphorylation	ESQHKAETPHGAEEE HHHHHCCCCCCCHHH	25.99	28985074
228	Phosphorylation	EEECKAETPHGAEEE HHHHCCCCCCCCCHH	25.99	25159151
249	Phosphorylation	CAPAAVATSPPGAIP ECCCHHCCCCCCCCC	34.86	23401153
250	Phosphorylation	APAAVATSPPGAIPK CCCHHCCCCCCCCCH	21.25	29255136
281	Phosphorylation	GCPAGVGTPVPADGT CCCCCCCCCCCCCCC	20.78	30576142
315	Phosphorylation	LVAGRAMTLSPQEEV EECCCCCCCCHHHHH	24.09	29255136
317	Phosphorylation	AGRAMTLSPQEEVAA CCCCCCCCHHHHHHH	18.51	29255136
318	Ubiquitination	GRAMTLSPQEEVAAG CCCCCCCHHHHHHHH	49.03	21890473
329	Phosphorylation	VAAGQMASSSRSGPV HHHHCCCCCCCCCCE	24.41	29396449
330	Phosphorylation	AAGQMASSSRSGPVK HHHCCCCCCCCCCEE	21.89	29396449
331	Phosphorylation	AGQMASSSRSGPVKL HHCCCCCCCCCCEEE	28.15	29396449
342	Ubiquitination	PVKLEFDVSDGATSK CEEEEEECCCCCCCC	7.35	27667366
347	Phosphorylation	FDVSDGATSKRAPPP EECCCCCCCCCCCCC	40.07	28555341
348	Phosphorylation	DVSDGATSKRAPPPR ECCCCCCCCCCCCCC	21.43	28555341
361	Phosphorylation	PRRLGERSGLKPPLR CCCCCCCCCCCHHHH	44.14	29214152
376	Ubiquitination	KAAVRQQKAPQEVEE HHHHHCCCCCCCCCC	54.41	24816145
391	Ubiquitination	DDGRSGAGEDPPMPA CCCCCCCCCCCCCCC	43.28	24816145
396	Sulfoxidation	GAGEDPPMPASRGSY CCCCCCCCCCCCCEE	5.43	21406390
399	Phosphorylation	EDPPMPASRGSYHLD CCCCCCCCCCEEECC	31.16	30576142
402	Phosphorylation	PMPASRGSYHLDWDK CCCCCCCEEECCHHH	14.31	23401153
403	Phosphorylation	MPASRGSYHLDWDKM CCCCCCEEECCHHHC	14.82	30576142
423	Acetylation	IPFGGDTKSGCSEAQ CCCCCCCCCCCCCCC	49.98	7680221
424	O-linked_Glycosylation	PFGGDTKSGCSEAQP CCCCCCCCCCCCCCC	47.31	23301498
424	Phosphorylation	PFGGDTKSGCSEAQP CCCCCCCCCCCCCCC	47.31	26552605
427	Phosphorylation	GDTKSGCSEAQPPES CCCCCCCCCCCCCCC	39.22	26552605
434	Phosphorylation	SEAQPPESPETRLGQ CCCCCCCCCCCCCCC	33.53	19664994
437	Phosphorylation	QPPESPETRLGQPAA CCCCCCCCCCCCCHH	34.28	30266825
461	Ubiquitination	EEPGPCLSQQLHSAS CCCCCCHHHHHHHCC	23.69	24816145
481	Phosphorylation	VVQLAAETPTAESKE CCEEEECCCCHHHHH	22.63	28464451
496	Phosphorylation	RALNSASTSLPTSCP HHHHHCCCCCCCCCC	33.72	25159151
497	Phosphorylation	ALNSASTSLPTSCPG HHHHCCCCCCCCCCC	29.83	25627689
500	Phosphorylation	SASTSLPTSCPGSEP HCCCCCCCCCCCCCC	48.53	25627689
501	Phosphorylation	ASTSLPTSCPGSEPV CCCCCCCCCCCCCCC	19.17	25627689
505	Phosphorylation	LPTSCPGSEPVPTHQ CCCCCCCCCCCCCCC	24.70	25159151
524	Phosphorylation	ALELKEESFRDPAEV CHHHCHHHHCCHHHH	27.03	25159151
534	Phosphorylation	DPAEVLGTGAEVDYL CHHHHCCCCCCCCHH	29.11	27732954
540	Phosphorylation	GTGAEVDYLEQFGTS CCCCCCCHHHHHCCC	19.81	28796482
550	Ubiquitination	QFGTSSFKESALRKQ HHCCCCHHHHHHHHC	53.35	21906983
552	Phosphorylation	GTSSFKESALRKQSL CCCCHHHHHHHHCCE	32.94	20068231
556	Ubiquitination	FKESALRKQSLYLKF HHHHHHHHCCEEEEC	45.12	23503661
558	Phosphorylation	ESALRKQSLYLKFDP HHHHHHCCEEEECCH	23.24	23401153
560	Phosphorylation	ALRKQSLYLKFDPLL HHHHCCEEEECCHHH	17.06	29396449
562	Ubiquitination	RKQSLYLKFDPLLRD HHCCEEEECCHHHCC	33.88	21890473
562	Ubiquitination	RKQSLYLKFDPLLRD HHCCEEEECCHHHCC	33.88	22817900
570	Phosphorylation	FDPLLRDSPGRPVPV CCHHHCCCCCCCCCE	23.87	25159151
579	Phosphorylation	GRPVPVATETSSMHG CCCCCEEEECCCCCC	39.78	25850435
581	Phosphorylation	PVPVATETSSMHGAN CCCEEEECCCCCCCC	23.03	29449344
582	Phosphorylation	VPVATETSSMHGANE CCEEEECCCCCCCCC	21.31	22496350
583	Phosphorylation	PVATETSSMHGANET CEEEECCCCCCCCCC	23.40	26330541
590	Phosphorylation	SMHGANETPSGRPRE CCCCCCCCCCCCCCE	23.67	25159151
592	Phosphorylation	HGANETPSGRPREAK CCCCCCCCCCCCEEE	55.65	23917254
649	Ubiquitination	KDLDAVVKATQEENR HHHHHHHHHHHHHHH	38.83	21906983
668	Ubiquitination	RCEELHGKNLELGKI HHHHHHCCCCCHHHH	47.84	29967540
674	Ubiquitination	GKNLELGKIMDRFEE CCCCCHHHHHHHHHH	47.70	21890473
674	Ubiquitination	GKNLELGKIMDRFEE CCCCCHHHHHHHHHH	47.70	21906983
678	Ubiquitination	ELGKIMDRFEEVVYQ CHHHHHHHHHHHHHH	24.40	21890473
684	Phosphorylation	DRFEEVVYQAMEEVQ HHHHHHHHHHHHHHH	8.84	27642862
698	Ubiquitination	QKQKELSKAEIQKVL HHHHHHCHHHHHHHH	63.76	27667366
702	Ubiquitination	ELSKAEIQKVLKEKD HHCHHHHHHHHHHHH	22.70	27667366
703	Ubiquitination	LSKAEIQKVLKEKDQ HCHHHHHHHHHHHHH	56.02	29967540
708	2-Hydroxyisobutyrylation	IQKVLKEKDQLTTDL HHHHHHHHHHHHHHH	49.54	-
712	Phosphorylation	LKEKDQLTTDLNSME HHHHHHHHHHHHHHH	16.78	28270605
713	Phosphorylation	KEKDQLTTDLNSMEK HHHHHHHHHHHHHHH	47.27	28270605
717	Phosphorylation	QLTTDLNSMEKSFSD HHHHHHHHHHHHHHH	35.30	28270605
720	Ubiquitination	TDLNSMEKSFSDLFK HHHHHHHHHHHHHHH	48.43	29967540
723	Phosphorylation	NSMEKSFSDLFKRFE HHHHHHHHHHHHHHH	40.26	23186163
739	Phosphorylation	QKEVIEGYRKNEESL HHHHHHHHHCCHHHH	12.96	20068231
745	Phosphorylation	GYRKNEESLKKCVED HHHCCHHHHHHHHHH	39.03	24702127
747	Ubiquitination	RKNEESLKKCVEDYL HCCHHHHHHHHHHHH	54.10	24816145
748	Ubiquitination	KNEESLKKCVEDYLA CCHHHHHHHHHHHHH	49.13	29967540
751	Ubiquitination	ESLKKCVEDYLARIT HHHHHHHHHHHHHHH	50.86	24816145
768	Ubiquitination	GQRYQALKAHAEEKL HHHHHHHHHHHHHHH	40.93	29967540
774	2-Hydroxyisobutyrylation	LKAHAEEKLQLANEE HHHHHHHHHHHCHHH	32.79	-
774	Acetylation	LKAHAEEKLQLANEE HHHHHHHHHHHCHHH	32.79	26822725
788	Ubiquitination	EIAQVRSKAQAEALA HHHHHHHHHHHHHHH	33.67	29967540
799	Phosphorylation	EALALQASLRKEQMR HHHHHHHHHHHHHHH	18.75	25159151
817	Ubiquitination	LEKTVEQKTKENEEL HHHHHHHHHHHHHHH	48.32	24816145
819	Ubiquitination	KTVEQKTKENEELTR HHHHHHHHHHHHHHH	66.63	-
821	Ubiquitination	VEQKTKENEELTRIC HHHHHHHHHHHHHHH	49.99	24816145
834	Ubiquitination	ICDDLISKMEKI--- HHHHHHHHHHCC---	44.05	32015554

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
558	S	Phosphorylation	Kinase	AURA	O14965	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TACC3_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 TACC3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AKAP9_HUMAN	AKAP9	physical	12015314
NDEL1_HUMAN	NDEL1	physical	17060449
MBD2_HUMAN	MBD2	physical	16410616
KAT2A_HUMAN	KAT2A	physical	14767476
VP37C_HUMAN	VPS37C	physical	25416956
TB22B_HUMAN	TBC1D22B	physical	25416956
KIZ_HUMAN	KIZ	physical	25416956
ASPC1_HUMAN	ASPSCR1	physical	25416956
CIB3_HUMAN	CIB3	physical	25416956
SNX20_HUMAN	SNX20	physical	25416956
FZR1_HUMAN	FZR1	physical	19823035
MRE11_HUMAN	MRE11A	physical	26344197
DSRAD_HUMAN	ADAR	physical	26496610
CALD1_HUMAN	CALD1	physical	26496610
CUX1_HUMAN	CUX1	physical	26496610
CASP_HUMAN	CUX1	physical	26496610
KIF11_HUMAN	KIF11	physical	26496610
PCDH7_HUMAN	PCDH7	physical	26496610
VASP_HUMAN	VASP	physical	26496610
SLBP_HUMAN	SLBP	physical	26496610
NFS1_HUMAN	NFS1	physical	26496610
XPR1_HUMAN	XPR1	physical	26496610
CKAP5_HUMAN	CKAP5	physical	26496610
DHRS2_HUMAN	DHRS2	physical	26496610
ZER1_HUMAN	ZER1	physical	26496610
ORC3_HUMAN	ORC3	physical	26496610
ENAH_HUMAN	ENAH	physical	26496610
SLAI2_HUMAN	SLAIN2	physical	26496610
MET14_HUMAN	METTL14	physical	26496610
RN123_HUMAN	RNF123	physical	26496610
DEFM_HUMAN	PDF	physical	26496610
PANK2_HUMAN	PANK2	physical	26496610
RN135_HUMAN	RNF135	physical	26496610
M3K21_HUMAN	KIAA1804	physical	26496610
ANM9_HUMAN	PRMT9	physical	26496610
DEPD7_HUMAN	DEPDC7	physical	26496610
RN168_HUMAN	RNF168	physical	26496610
WDR90_HUMAN	WDR90	physical	26496610
CB069_HUMAN	C2orf69	physical	26496610
PR14L_HUMAN	PRR14L	physical	26496610
FRYL_HUMAN	FRYL	physical	26496610
F111B_HUMAN	FAM111B	physical	26496610
TGO1_HUMAN	MIA3	physical	26496610
FZR1_HUMAN	FZR1	physical	25375378
CDC27_HUMAN	CDC27	physical	25375378

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 TACC3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND SER-434, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-71; SER-317;SER-434 AND SER-558, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-317, AND MASSSPECTROMETRY.	18220336 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-434, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59, AND MASSSPECTROMETRY.	17924679 [Abstract]