TCEA1_HUMAN - dbPTM
TCEA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCEA1_HUMAN
UniProt AC P23193
Protein Name Transcription elongation factor A protein 1
Gene Name TCEA1
Organism Homo sapiens (Human).
Sequence Length 301
Subcellular Localization Nucleus.
Protein Description Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus..
Protein Sequence MEDEVVRFAKKMDKMVQKKNAAGALDLLKELKNIPMTLELLQSTRIGMSVNAIRKQSTDEEVTSLAKSLIKSWKKLLDGPSTEKDLDEKKKEPAITSQNSPEAREESTSSGNVSNRKDETNARDTYVSSFPRAPSTSDSVRLKCREMLAAALRTGDDYIAIGADEEELGSQIEEAIYQEIRNTDMKYKNRVRSRISNLKDAKNPNLRKNVLCGNIPPDLFARMTAEEMASDELKEMRKNLTKEAIREHQMAKTGGTQTDLFTCGKCKKKNCTYTQVQTRSADEPMTTFVVCNECGNRWKFC
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
1Acetylation-------MEDEVVRF
-------CHHHHHHH		15.3522814378
192-HydroxyisobutyrylationMDKMVQKKNAAGALD
HHHHHHHCCHHHHHH		34.43-
19UbiquitinationMDKMVQKKNAAGALD
HHHHHHHCCHHHHHH		34.43-
22 (in isoform 2)Phosphorylation-17.1217287340
28 (in isoform 2)Phosphorylation-3.9617287340
292-HydroxyisobutyrylationAGALDLLKELKNIPM
HHHHHHHHHHCCCCC		69.19-
29AcetylationAGALDLLKELKNIPM
HHHHHHHHHHCCCCC		69.1927452117
29 (in isoform 1)Ubiquitination-69.1921890473
29UbiquitinationAGALDLLKELKNIPM
HHHHHHHHHHCCCCC		69.1921890473
36 (in isoform 2)Phosphorylation-6.2229116813
46 (in isoform 2)Ubiquitination-5.7121890473
47 (in isoform 2)Phosphorylation-10.0617287340
48SulfoxidationLQSTRIGMSVNAIRK
HHHCCCCCCHHHHHH		3.6321406390
49PhosphorylationQSTRIGMSVNAIRKQ
HHCCCCCCHHHHHHC		13.65-
57PhosphorylationVNAIRKQSTDEEVTS
HHHHHHCCCHHHHHH		40.6427273156
58PhosphorylationNAIRKQSTDEEVTSL
HHHHHCCCHHHHHHH		44.9626657352
63PhosphorylationQSTDEEVTSLAKSLI
CCCHHHHHHHHHHHH		22.6923312004
64PhosphorylationSTDEEVTSLAKSLIK
CCHHHHHHHHHHHHH		31.3523312004
67UbiquitinationEEVTSLAKSLIKSWK
HHHHHHHHHHHHHHH		51.6021890473
67 (in isoform 1)Ubiquitination-51.6021890473
68PhosphorylationEVTSLAKSLIKSWKK
HHHHHHHHHHHHHHH		29.7121712546
75MalonylationSLIKSWKKLLDGPST
HHHHHHHHHHCCCCC		48.2826320211
75UbiquitinationSLIKSWKKLLDGPST
HHHHHHHHHHCCCCC		48.28-
81PhosphorylationKKLLDGPSTEKDLDE
HHHHCCCCCHHCHHH		55.5230266825
82PhosphorylationKLLDGPSTEKDLDEK
HHHCCCCCHHCHHHH		50.6230266825
84AcetylationLDGPSTEKDLDEKKK
HCCCCCHHCHHHHHH		64.7723954790
84SuccinylationLDGPSTEKDLDEKKK
HCCCCCHHCHHHHHH		64.7723954790
84UbiquitinationLDGPSTEKDLDEKKK
HCCCCCHHCHHHHHH		64.7719608861
96PhosphorylationKKKEPAITSQNSPEA
HHHCCCCCCCCCHHH		26.7720201521
97PhosphorylationKKEPAITSQNSPEAR
HHCCCCCCCCCHHHH		22.6620201521
100PhosphorylationPAITSQNSPEAREES
CCCCCCCCHHHHHHH		19.2419664994
107PhosphorylationSPEAREESTSSGNVS
CHHHHHHHCCCCCCC		28.9224732914
108PhosphorylationPEAREESTSSGNVSN
HHHHHHHCCCCCCCC		30.1423927012
109PhosphorylationEAREESTSSGNVSNR
HHHHHHCCCCCCCCC		45.5924732914
110PhosphorylationAREESTSSGNVSNRK
HHHHHCCCCCCCCCC		34.1825159151
114PhosphorylationSTSSGNVSNRKDETN
HCCCCCCCCCCCCCC		34.6124732914
120PhosphorylationVSNRKDETNARDTYV
CCCCCCCCCCCHHCH		44.2923828894
125PhosphorylationDETNARDTYVSSFPR
CCCCCCHHCHHCCCC		21.9228442448
126PhosphorylationETNARDTYVSSFPRA
CCCCCHHCHHCCCCC		11.5625159151
126NitrationETNARDTYVSSFPRA
CCCCCHHCHHCCCCC		11.56-
128PhosphorylationNARDTYVSSFPRAPS
CCCHHCHHCCCCCCC		18.8228634120
129PhosphorylationARDTYVSSFPRAPST
CCHHCHHCCCCCCCC		29.2628450419
135PhosphorylationSSFPRAPSTSDSVRL
HCCCCCCCCCHHHHH		39.2925159151
136PhosphorylationSFPRAPSTSDSVRLK
CCCCCCCCCHHHHHH		35.1825262027
137PhosphorylationFPRAPSTSDSVRLKC
CCCCCCCCHHHHHHH		32.0225262027
139PhosphorylationRAPSTSDSVRLKCRE
CCCCCCHHHHHHHHH		14.6528450419
170PhosphorylationADEEELGSQIEEAIY
CCHHHHHHHHHHHHH		40.3825338102
177PhosphorylationSQIEEAIYQEIRNTD
HHHHHHHHHHHHCCC		13.7227642862
186AcetylationEIRNTDMKYKNRVRS
HHHCCCHHHHHHHHH		56.7525953088
196PhosphorylationNRVRSRISNLKDAKN
HHHHHHHHCCCCCCC		34.6928787133
199SuccinylationRSRISNLKDAKNPNL
HHHHHCCCCCCCCCC		60.9523954790
199AcetylationRSRISNLKDAKNPNL
HHHHHCCCCCCCCCC		60.9523749302
202UbiquitinationISNLKDAKNPNLRKN
HHCCCCCCCCCCCCC		80.98-
223SulfoxidationPPDLFARMTAEEMAS
CHHHHHHHCHHHHCH		3.6021406390
224PhosphorylationPDLFARMTAEEMASD
HHHHHHHCHHHHCHH		25.9330624053
230PhosphorylationMTAEEMASDELKEMR
HCHHHHCHHHHHHHH		30.2428258704
234UbiquitinationEMASDELKEMRKNLT
HHCHHHHHHHHHHHH		47.63-
242MethylationEMRKNLTKEAIREHQ
HHHHHHHHHHHHHHH		48.6054424997
242UbiquitinationEMRKNLTKEAIREHQ
HHHHHHHHHHHHHHH		48.60-
252AcetylationIREHQMAKTGGTQTD
HHHHHHHHCCCCCCC		42.2225953088
252UbiquitinationIREHQMAKTGGTQTD
HHHHHHHHCCCCCCC		42.22-
253PhosphorylationREHQMAKTGGTQTDL
HHHHHHHCCCCCCCC		31.1628555341
262PhosphorylationGTQTDLFTCGKCKKK
CCCCCCEECCCCCCC		27.8725159151
265UbiquitinationTDLFTCGKCKKKNCT
CCCEECCCCCCCCCE		45.06-
265AcetylationTDLFTCGKCKKKNCT
CCCEECCCCCCCCCE		45.0625953088
267UbiquitinationLFTCGKCKKKNCTYT
CEECCCCCCCCCEEE		70.98-
272PhosphorylationKCKKKNCTYTQVQTR
CCCCCCCEEEEEECC		38.7128796482
273PhosphorylationCKKKNCTYTQVQTRS
CCCCCCEEEEEECCC		9.4428796482
273NitrationCKKKNCTYTQVQTRS
CCCCCCEEEEEECCC		9.44-
274PhosphorylationKKKNCTYTQVQTRSA
CCCCCEEEEEECCCC		12.2428796482
278PhosphorylationCTYTQVQTRSADEPM
CEEEEEECCCCCCCC		27.9528152594
285SulfoxidationTRSADEPMTTFVVCN
CCCCCCCCEEEEEEC		5.3321406390
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

Oops, there are no upstream regulatory protein records of TCEA1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCEA1_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 TCEA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPB1_HUMANPOLR2Aphysical
9765293
TF2H1_HUMANGTF2H1physical
9765293
CTDP1_HUMANCTDP1physical
9765293
RPB1_HUMANPOLR2Aphysical
9305922
CDK8_HUMANCDK8physical
9305922
T2FA_HUMANGTF2F1physical
9305922
CDK7_HUMANCDK7physical
9305922
TBP_HUMANTBPphysical
9305922
T2EA_HUMANGTF2E1physical
9305922
T2FB_HUMANGTF2F2physical
9305922
TF2B_HUMANGTF2Bphysical
9305922
TF2H1_HUMANGTF2H1physical
9305922
UBR5_HUMANUBR5physical
17643375
SPT6H_HUMANSUPT6Hphysical
17643375
RPB1_HUMANPOLR2Aphysical
17643375
SF3B2_HUMANSF3B2physical
17643375
TCEA2_HUMANTCEA2physical
17643375
SF3B3_HUMANSF3B3physical
17643375
SF3A1_HUMANSF3A1physical
17643375
INT1_HUMANINTS1physical
17643375
RPB2_HUMANPOLR2Bphysical
17643375
DDX5_HUMANDDX5physical
17643375
U520_HUMANSNRNP200physical
17643375
DDX46_HUMANDDX46physical
17643375
LEO1_HUMANLEO1physical
20178742
PAF1_HUMANPAF1physical
20178742
CTR9_HUMANCTR9physical
20178742
CDC73_HUMANCDC73physical
20178742
RTF1_HUMANRTF1physical
20178742
WDR61_HUMANWDR61physical
20178742
RPB1_HUMANPOLR2Aphysical
20178742
UBR5_HUMANUBR5physical
21127351
CDK9_HUMANCDK9physical
21127351
PAF1_HUMANPAF1physical
21596312
A4_HUMANAPPphysical
21832049
UBAC1_HUMANUBAC1physical
22939629
MED26_HUMANMED26physical
21729782
T2EA_HUMANGTF2E1physical
10454562
CDK8_HUMANCDK8physical
10454562
TBP_HUMANTBPphysical
10454562
TF2H1_HUMANGTF2H1physical
10454562
T2FA_HUMANGTF2F1physical
10454562
TF2B_HUMANGTF2Bphysical
10454562
MCM2_HUMANMCM2physical
10454562
MCM3_HUMANMCM3physical
10454562
MCM5_HUMANMCM5physical
10454562
BCCIP_HUMANBCCIPphysical
22863883
CHRD1_HUMANCHORDC1physical
22863883
XPO2_HUMANCSE1Lphysical
22863883
LDHA_HUMANLDHAphysical
22863883
6PGD_HUMANPGDphysical
22863883
DHSO_HUMANSORDphysical
22863883
DUS3L_HUMANDUS3Lphysical
26344197
NF2IP_HUMANNFATC2IPphysical
26344197
ZMAT2_HUMANZMAT2physical
26344197
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 TCEA1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-97 AND SER-100, AND MASS SPECTROMETRY.
"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-84, AND MASS SPECTROMETRY.
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-100, AND MASSSPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-97 AND SER-100, AND MASS SPECTROMETRY.
"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-97 AND SER-100, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASSSPECTROMETRY.
"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-97 AND SER-100, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-100; THR-108;SER-110 AND TYR-126, AND MASS SPECTROMETRY.
"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-100, AND MASSSPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASSSPECTROMETRY.
"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-100, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-96, AND MASSSPECTROMETRY.

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