TACC1_HUMAN - dbPTM
TACC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TACC1_HUMAN
UniProt AC O75410
Protein Name Transforming acidic coiled-coil-containing protein 1
Gene Name TACC1
Organism Homo sapiens (Human).
Sequence Length 805
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Midbody . Nucleus during interphase. Weakly concentrated at centrosomes during mitosis and colocalizes with AURKC at the midbody during cytokinesis.
Isoform 5
Protein Description Likely involved in the processes that promote cell division prior to the formation of differentiated tissues..
Protein Sequence MAFSPWQILSPVQWAKWTWSAVRGGAAGEDEAGGPEGDPEEEDSQAETKSLSFSSDSEGNFETPEAETPIRSPFKESCDPSLGLAGPGAKSQESQEADEQLVAEVVEKCSSKTCSKPSENEVPQQAIDSHSVKNFREEPEHDFSKISIVRPFSIETKDSTDISAVLGTKAAHGCVTAVSGKALPSSPPDALQDEAMTEGSMGVTLEASAEADLKAGNSCPELVPSRRSKLRKPKPVPLRKKAIGGEFSDTNAAVEGTPLPKASYHFSPEELDENTSPLLGDARFQKSPPDLKETPGTLSSDTNDSGVELGEESRSSPLKLEFDFTEDTGNIEARKALPRKLGRKLGSTLTPKIQKDGISKSAGLEQPTDPVARDGPLSQTSSKPDPSQWESPSFNPFGSHSVLQNSPPLSSEGSYHFDPDNFDESMDPFKPTTTLTSSDFCSPTGNHVNEILESPKKAKSRLITSGCKVKKHETQSLALDACSRDEGAVISQISDISNRDGHATDEEKLASTSCGQKSAGAEVKGEPEEDLEYFECSNVPVSTINHAFSSSEAGIEKETCQKMEEDGSTVLGLLESSAEKAPVSVSCGGESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKTD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAFSPWQIL
------CCCCCCCEE
17.3920068231
2 (in isoform 5)Myristoylation-17.3925807930
4Phosphorylation----MAFSPWQILSP
----CCCCCCCEECH
18.7222199227
4 (in isoform 4)Phosphorylation-18.7224043423
4 (in isoform 5)Phosphorylation-18.7224043423
6 (in isoform 4)Phosphorylation-9.1724043423
6 (in isoform 5)Phosphorylation-9.1724043423
8 (in isoform 4)Phosphorylation-3.4822468782
8 (in isoform 5)Phosphorylation-3.4822468782
10PhosphorylationFSPWQILSPVQWAKW
CCCCCEECHHHHHHH
25.3425159151
20PhosphorylationQWAKWTWSAVRGGAA
HHHHHHHHHHCCCCC
14.9828555341
44PhosphorylationGDPEEEDSQAETKSL
CCCHHHCCCCCHHCC
34.2723401153
48PhosphorylationEEDSQAETKSLSFSS
HHCCCCCHHCCCCCC
29.0222167270
50PhosphorylationDSQAETKSLSFSSDS
CCCCCHHCCCCCCCC
36.3430278072
52PhosphorylationQAETKSLSFSSDSEG
CCCHHCCCCCCCCCC
30.1230278072
54PhosphorylationETKSLSFSSDSEGNF
CHHCCCCCCCCCCCC
29.8425159151
55PhosphorylationTKSLSFSSDSEGNFE
HHCCCCCCCCCCCCC
43.0530278072
57PhosphorylationSLSFSSDSEGNFETP
CCCCCCCCCCCCCCC
49.7225159151
63PhosphorylationDSEGNFETPEAETPI
CCCCCCCCCCCCCCC
23.4528464451
68PhosphorylationFETPEAETPIRSPFK
CCCCCCCCCCCCCCH
30.9424173317
75MethylationTPIRSPFKESCDPSL
CCCCCCCHHHCCCCC
52.69115980249
75UbiquitinationTPIRSPFKESCDPSL
CCCCCCCHHHCCCCC
52.69-
81PhosphorylationFKESCDPSLGLAGPG
CHHHCCCCCCCCCCC
23.0917081983
91PhosphorylationLAGPGAKSQESQEAD
CCCCCCCCHHCHHHH
38.3523663014
94PhosphorylationPGAKSQESQEADEQL
CCCCCHHCHHHHHHH
26.1930266825
118PhosphorylationSKTCSKPSENEVPQQ
CCCCCCCCCCCCCHH
57.7125137130
129PhosphorylationVPQQAIDSHSVKNFR
CCHHHHHHHCCCCHH
16.1423403867
131PhosphorylationQQAIDSHSVKNFREE
HHHHHHHCCCCHHHC
38.4426657352
132 (in isoform 8)Ubiquitination-5.0021906983
144PhosphorylationEEPEHDFSKISIVRP
HCCCCCCCCEEEEEC
34.8325137130
147PhosphorylationEHDFSKISIVRPFSI
CCCCCCEEEEECEEE
20.8325159151
153PhosphorylationISIVRPFSIETKDST
EEEEECEEEECCCCC
23.3828102081
156PhosphorylationVRPFSIETKDSTDIS
EECEEEECCCCCCCH
38.1823403867
168PhosphorylationDISAVLGTKAAHGCV
CCHHHHCCHHHCCCE
17.2220058876
169UbiquitinationISAVLGTKAAHGCVT
CHHHHCCHHHCCCEE
41.60-
179PhosphorylationHGCVTAVSGKALPSS
CCCEEEECCCCCCCC
31.9220058876
218PhosphorylationADLKAGNSCPELVPS
HHHHCCCCCCCCCCC
30.0826657352
225PhosphorylationSCPELVPSRRSKLRK
CCCCCCCCHHHHCCC
32.6130108239
228PhosphorylationELVPSRRSKLRKPKP
CCCCCHHHHCCCCCC
34.6321531210
234AcetylationRSKLRKPKPVPLRKK
HHHCCCCCCCCCCCC
62.7812429785
240AcetylationPKPVPLRKKAIGGEF
CCCCCCCCCCCCCCC
54.9912429797
248PhosphorylationKAIGGEFSDTNAAVE
CCCCCCCCCCCCCCC
38.9430266825
250PhosphorylationIGGEFSDTNAAVEGT
CCCCCCCCCCCCCCC
26.0930266825
257PhosphorylationTNAAVEGTPLPKASY
CCCCCCCCCCCCCCC
14.2429255136
263PhosphorylationGTPLPKASYHFSPEE
CCCCCCCCCCCCHHH
25.8519690332
264PhosphorylationTPLPKASYHFSPEEL
CCCCCCCCCCCHHHH
16.2530266825
267PhosphorylationPKASYHFSPEELDEN
CCCCCCCCHHHHCCC
20.3530266825
275PhosphorylationPEELDENTSPLLGDA
HHHHCCCCCCCCCCH
29.6723401153
276PhosphorylationEELDENTSPLLGDAR
HHHCCCCCCCCCCHH
25.7325159151
286UbiquitinationLGDARFQKSPPDLKE
CCCHHHCCCCCCHHC
63.32-
287PhosphorylationGDARFQKSPPDLKET
CCHHHCCCCCCHHCC
30.7730108239
294PhosphorylationSPPDLKETPGTLSSD
CCCCHHCCCCCCCCC
25.9830624053
297PhosphorylationDLKETPGTLSSDTND
CHHCCCCCCCCCCCC
25.3523403867
299PhosphorylationKETPGTLSSDTNDSG
HCCCCCCCCCCCCCC
26.4623403867
300PhosphorylationETPGTLSSDTNDSGV
CCCCCCCCCCCCCCC
52.1223403867
302PhosphorylationPGTLSSDTNDSGVEL
CCCCCCCCCCCCCCC
42.7623403867
305PhosphorylationLSSDTNDSGVELGEE
CCCCCCCCCCCCCCC
46.9725159151
313PhosphorylationGVELGEESRSSPLKL
CCCCCCCCCCCCEEE
32.9122199227
315PhosphorylationELGEESRSSPLKLEF
CCCCCCCCCCEEEEE
45.6630266825
316PhosphorylationLGEESRSSPLKLEFD
CCCCCCCCCEEEEEE
32.8930266825
345 (in isoform 5)Ubiquitination-6.7121906983
347PhosphorylationKLGRKLGSTLTPKIQ
HHHHCCCCCCCHHHC
30.5823401153
348PhosphorylationLGRKLGSTLTPKIQK
HHHCCCCCCCHHHCC
32.6222199227
350PhosphorylationRKLGSTLTPKIQKDG
HCCCCCCCHHHCCCC
23.7121815630
357 (in isoform 4)Ubiquitination-32.8621906983
359PhosphorylationKIQKDGISKSAGLEQ
HHCCCCCCCCCCCCC
26.5323312004
360UbiquitinationIQKDGISKSAGLEQP
HCCCCCCCCCCCCCC
42.26-
361PhosphorylationQKDGISKSAGLEQPT
CCCCCCCCCCCCCCC
22.3030108239
373 (in isoform 6)Ubiquitination-50.0521906983
381PhosphorylationDGPLSQTSSKPDPSQ
CCCCCCCCCCCCHHH
28.82-
406PhosphorylationSHSVLQNSPPLSSEG
CCHHHCCCCCCCCCC
18.2222468782
454PhosphorylationHVNEILESPKKAKSR
CHHHHHHCHHHHHHH
38.2825159151
464PhosphorylationKAKSRLITSGCKVKK
HHHHHHHCCCCCCCC
24.5328102081
465PhosphorylationAKSRLITSGCKVKKH
HHHHHHCCCCCCCCC
34.8928102081
468UbiquitinationRLITSGCKVKKHETQ
HHHCCCCCCCCCCCC
61.69-
471UbiquitinationTSGCKVKKHETQSLA
CCCCCCCCCCCCCHH
50.05-
474PhosphorylationCKVKKHETQSLALDA
CCCCCCCCCCHHHHH
24.1523312004
476PhosphorylationVKKHETQSLALDACS
CCCCCCCCHHHHHCC
24.0323312004
477 (in isoform 2)Phosphorylation-3.8428270605
483PhosphorylationSLALDACSRDEGAVI
CHHHHHCCCCCCCEE
44.48-
491PhosphorylationRDEGAVISQISDISN
CCCCCEEEEEHHCCC
18.1828450419
494PhosphorylationGAVISQISDISNRDG
CCEEEEEHHCCCCCC
22.6628450419
497PhosphorylationISQISDISNRDGHAT
EEEEHHCCCCCCCCC
30.7030576142
504PhosphorylationSNRDGHATDEEKLAS
CCCCCCCCCHHHHHC
37.9623401153
511PhosphorylationTDEEKLASTSCGQKS
CCHHHHHCCCCCCCC
31.1523927012
512PhosphorylationDEEKLASTSCGQKSA
CHHHHHCCCCCCCCC
23.5623927012
513PhosphorylationEEKLASTSCGQKSAG
HHHHHCCCCCCCCCC
17.4723927012
517UbiquitinationASTSCGQKSAGAEVK
HCCCCCCCCCCCCCC
27.79-
518PhosphorylationSTSCGQKSAGAEVKG
CCCCCCCCCCCCCCC
24.8526074081
533PhosphorylationEPEEDLEYFECSNVP
CCHHHHCCEECCCCC
16.3928796482
537PhosphorylationDLEYFECSNVPVSTI
HHCCEECCCCCHHHH
33.3928796482
542PhosphorylationECSNVPVSTINHAFS
ECCCCCHHHHHHHCC
19.9427251275
543PhosphorylationCSNVPVSTINHAFSS
CCCCCHHHHHHHCCC
26.4927251275
549PhosphorylationSTINHAFSSSEAGIE
HHHHHHCCCCCCCCC
33.4627251275
550PhosphorylationTINHAFSSSEAGIEK
HHHHHCCCCCCCCCH
26.2427251275
551PhosphorylationINHAFSSSEAGIEKE
HHHHCCCCCCCCCHH
30.2127251275
568PhosphorylationQKMEEDGSTVLGLLE
HHHHCCCCHHHHHHH
27.8822199227
569PhosphorylationKMEEDGSTVLGLLES
HHHCCCCHHHHHHHH
25.8622199227
576PhosphorylationTVLGLLESSAEKAPV
HHHHHHHHCCCCCCE
34.5122199227
577PhosphorylationVLGLLESSAEKAPVS
HHHHHHHCCCCCCEE
30.9522199227
588 (in isoform 3)Ubiquitination-35.0821906983
591PhosphorylationSVSCGGESPLDGICL
EEECCCCCCCCCEEC
33.7510470851
616PhosphorylationLIREEIITKEIEANE
HHHHHHHHHHHHHHH
28.4324670416
617UbiquitinationIREEIITKEIEANEW
HHHHHHHHHHHHHHH
46.41-
640AcetylationQEVLEMRKIVAEYEK
HHHHHHHHHHHHHHH
39.987965395
640UbiquitinationQEVLEMRKIVAEYEK
HHHHHHHHHHHHHHH
39.98-
647AcetylationKIVAEYEKTIAQMIE
HHHHHHHHHHHHHHH
44.317965407
647UbiquitinationKIVAEYEKTIAQMIE
HHHHHHHHHHHHHHH
44.31-
660PhosphorylationIEDEQRTSMTSQKSF
HHHHHHHHHHCHHHH
23.4222468782
665UbiquitinationRTSMTSQKSFQQLTM
HHHHHCHHHHHHHHH
53.67-
666PhosphorylationTSMTSQKSFQQLTME
HHHHCHHHHHHHHHH
22.2022468782
687PhosphorylationDLNSVERSLSDLFRR
HHHHHHHHHHHHHHH
20.7922468782
689PhosphorylationNSVERSLSDLFRRYE
HHHHHHHHHHHHHHH
33.2522468782
714UbiquitinationKNEEALKKCAQDYLA
HCHHHHHHHHHHHHH
35.34-
730PhosphorylationVKQEEQRYQALKIHA
HHHHHHHHHHHHHHH
9.6120068231
734UbiquitinationEQRYQALKIHAEEKL
HHHHHHHHHHHHHHH
35.15-
740AcetylationLKIHAEEKLDKANEE
HHHHHHHHHHHHHHH
54.1925953088
754AcetylationEIAQVRTKAKAESAA
HHHHHHHHHHHHHHH
37.0119824175
756UbiquitinationAQVRTKAKAESAALH
HHHHHHHHHHHHHHH
55.00-
759PhosphorylationRTKAKAESAALHAGL
HHHHHHHHHHHHHHH
24.57-
783UbiquitinationLERALQQKNQEIEEL
HHHHHHHHHHHHHHH
47.872190698
783 (in isoform 1)Ubiquitination-47.8721906983
792UbiquitinationQEIEELTKICDELIA
HHHHHHHHHHHHHHH
54.70-
795 (in isoform 2)Ubiquitination-58.1521906983
800UbiquitinationICDELIAKLGKTD--
HHHHHHHHHCCCC--
51.26-

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
228SPhosphorylationKinaseAURCQ9UQB9
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TACC1_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 TACC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YETS4_HUMANYEATS4physical
11903063
AURKB_HUMANAURKBphysical
15064709
AURKA_HUMANAURKAphysical
15064709
LSM7_HUMANLSM7physical
14603251
TDRD7_HUMANTDRD7physical
14603251
CKAP5_HUMANCKAP5physical
14603251
AURKA_HUMANAURKAphysical
14603251
CKAP5_HUMANCKAP5physical
11903063
LSM7_HUMANLSM7physical
12165861
RUXG_HUMANSNRPGphysical
12165861
BARD1_HUMANBARD1physical
19176389
KAT2A_HUMANKAT2Aphysical
14767476
KDM1A_HUMANKDM1Aphysical
23455924
FBW1A_HUMANBTRCphysical
25416956
MEMO1_HUMANMEMO1physical
25416956
SH24A_HUMANSH2D4Aphysical
25416956
LYST_HUMANLYSTphysical
26496610
BRD3_HUMANBRD3physical
26496610
RBCC1_HUMANRB1CC1physical
26496610
TACC2_HUMANTACC2physical
26496610
BI2L1_HUMANBAIAP2L1physical
26496610
TACC2_HUMANTACC2physical
28514442
RNF41_HUMANRNF41physical
28514442
SKAP_HUMANKNSTRNphysical
28514442
FBW1A_HUMANBTRCphysical
28514442
FBW1B_HUMANFBXW11physical
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 TACC1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-276, AND MASSSPECTROMETRY.
"Aurora-C interacts with and phosphorylates the transforming acidiccoiled-coil 1 protein.";
Gabillard J.C., Ulisse S., Baldini E., Sorrenti S., Cremet J.Y.,Coccaro C., Prigent C., D'Armiento M., Arlot-Bonnemains Y.;
Biochem. Biophys. Res. Commun. 408:647-653(2011).
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AURKC, PHOSPHORYLATION ATSER-228 BY AURKC, AND MUTAGENESIS OF SER-228.
"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-44, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-52; SER-54;SER-55 AND SER-57, AND MASS SPECTROMETRY.
"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-533, AND MASSSPECTROMETRY.

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