dbPTM

TCEA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TCEA2_HUMAN
UniProt AC	Q15560
Protein Name	Transcription elongation factor A protein 2
Gene Name	TCEA2
Organism	Homo sapiens (Human).
Sequence Length	299
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	MMGKEEEIARIARRLDKMVTKKSAEGAMDLLRELKAMPITLHLLQSTRVGMSVNALRKQSSDEEVIALAKSLIKSWKKLLDASDAKARERGRGMPLPTSSRDASEAPDPSRKRPELPRAPSTPRITTFPPVPVTCDAVRNKCREMLTAALQTDHDHVAIGADCERLSAQIEECIFRDVGNTDMKYKNRVRSRISNLKDAKNPDLRRNVLCGAITPQQIAVMTSEEMASDELKEIRKAMTKEAIREHQMARTGGTQTDLFTCGKCRKKNCTYTQVQTRSSDEPMTTFVVCNECGNRWKFC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Phosphorylation	RRLDKMVTKKSAEGA HHHHHHHCHHCHHHH	29.29	20068231
23	Phosphorylation	DKMVTKKSAEGAMDL HHHHCHHCHHHHHHH	32.86	20068231
40	Phosphorylation	ELKAMPITLHLLQST HHHHCCHHHHHHHHC	11.40	28509920
52	Phosphorylation	QSTRVGMSVNALRKQ HHCCCCCCHHHHHHC	13.29	28509920
58	Ubiquitination	MSVNALRKQSSDEEV CCHHHHHHCCCHHHH	56.21	18655026
60	Phosphorylation	VNALRKQSSDEEVIA HHHHHHCCCHHHHHH	42.67	28122231
61	Phosphorylation	NALRKQSSDEEVIAL HHHHHCCCHHHHHHH	46.69	28122231
70	Ubiquitination	EEVIALAKSLIKSWK HHHHHHHHHHHHHHH	46.79	-
70	Acetylation	EEVIALAKSLIKSWK HHHHHHHHHHHHHHH	46.79	30592865
71	Phosphorylation	EVIALAKSLIKSWKK HHHHHHHHHHHHHHH	29.71	24719451
83	Phosphorylation	WKKLLDASDAKARER HHHHHCHHHHHHHHH	37.45	20068231
92	Methylation	AKARERGRGMPLPTS HHHHHHCCCCCCCCC	44.45	97770755
98	Phosphorylation	GRGMPLPTSSRDASE CCCCCCCCCCCCHHH	47.20	20068231
99	Phosphorylation	RGMPLPTSSRDASEA CCCCCCCCCCCHHHC	22.80	20068231
100	Phosphorylation	GMPLPTSSRDASEAP CCCCCCCCCCHHHCC	36.34	20068231
104	Phosphorylation	PTSSRDASEAPDPSR CCCCCCHHHCCCCCC	38.28	20068231
110	Phosphorylation	ASEAPDPSRKRPELP HHHCCCCCCCCCCCC	58.79	20068231
121	Phosphorylation	PELPRAPSTPRITTF CCCCCCCCCCCCCCC	50.49	-
122	Phosphorylation	ELPRAPSTPRITTFP CCCCCCCCCCCCCCC	18.61	20562096
126	Phosphorylation	APSTPRITTFPPVPV CCCCCCCCCCCCCCC	24.54	-
134	Phosphorylation	TFPPVPVTCDAVRNK CCCCCCCCCHHHHHH	9.90	20068231
184	Ubiquitination	DVGNTDMKYKNRVRS CCCCCCHHHHHHHHH	56.75	-
184	Acetylation	DVGNTDMKYKNRVRS CCCCCCHHHHHHHHH	56.75	26051181
194	Phosphorylation	NRVRSRISNLKDAKN HHHHHHHHCCHHCCC	34.69	28787133
197	Acetylation	RSRISNLKDAKNPDL HHHHHCCHHCCCCCH	60.95	-
240	Ubiquitination	EIRKAMTKEAIREHQ HHHHHHHHHHHHHHH	31.87	-
260	Phosphorylation	GTQTDLFTCGKCRKK CCCCCCEECCCCCCC	27.87	25159151
270	Phosphorylation	KCRKKNCTYTQVQTR CCCCCCCEEEEEEEC	38.71	28796482
271	Phosphorylation	CRKKNCTYTQVQTRS CCCCCCEEEEEEECC	9.44	28796482
272	Phosphorylation	RKKNCTYTQVQTRSS CCCCCEEEEEEECCC	12.24	28796482
276	Phosphorylation	CTYTQVQTRSSDEPM CEEEEEEECCCCCCC	33.39	28152594

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 TCEA2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TCEA2_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 TCEA2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRAF2_HUMAN	TRAF2	physical	16189514
AKTS1_HUMAN	AKT1S1	physical	16169070
FBF1_HUMAN	FBF1	physical	16169070
CENPT_HUMAN	CENPT	physical	16169070
WDR47_HUMAN	WDR47	physical	16169070
CCSE2_HUMAN	CCSER2	physical	16169070
RFA1_HUMAN	RPA1	physical	16169070
SH3G2_HUMAN	SH3GL2	physical	16169070
TX1B3_HUMAN	TAX1BP3	physical	16169070
MARK3_HUMAN	MARK3	physical	16169070
CAMKV_HUMAN	CAMKV	physical	16169070
MCM2_HUMAN	MCM2	physical	12392551
CAND1_HUMAN	CAND1	physical	17643375
HNRPK_HUMAN	HNRNPK	physical	17643375
TNPO1_HUMAN	TNPO1	physical	17643375
PININ_HUMAN	PNN	physical	17643375
IF4A3_HUMAN	EIF4A3	physical	17643375
TCEA1_HUMAN	TCEA1	physical	17643375
SNW1_HUMAN	SNW1	physical	17643375
NELFA_HUMAN	NELFA	physical	17643375
PARP1_HUMAN	PARP1	physical	17643375
KLC4_HUMAN	KLC4	physical	17643375
MAGD2_HUMAN	MAGED2	physical	17643375
A4_HUMAN	APP	physical	21832049
ITF2_HUMAN	TCF4	physical	25416956
TFCP2_HUMAN	TFCP2	physical	25416956
TRAF2_HUMAN	TRAF2	physical	25416956
MKRN3_HUMAN	MKRN3	physical	25416956
TAXB1_HUMAN	TAX1BP1	physical	25416956
TNIP1_HUMAN	TNIP1	physical	25416956
TRIM1_HUMAN	MID2	physical	25416956
EXOS8_HUMAN	EXOSC8	physical	25416956
GPKOW_HUMAN	GPKOW	physical	25416956
ATL4_HUMAN	ADAMTSL4	physical	25416956
THAP1_HUMAN	THAP1	physical	25416956
TRI54_HUMAN	TRIM54	physical	25416956
CC136_HUMAN	CCDC136	physical	25416956
TSG10_HUMAN	TSGA10	physical	25416956
CEP44_HUMAN	CEP44	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
K1958_HUMAN	KIAA1958	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
BRCA1_HUMAN	BRCA1	physical	25184681
KXDL1_HUMAN	KXD1	physical	21516116

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 TCEA2_HUMAN

Related Literatures of Post-Translational Modification

Ubiquitylation
Reference	PubMed
"Proteomic analysis of ubiquitinated proteins in normal hepatocytecell line Chang liver cells."; Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E.,Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.; Proteomics 8:2885-2896(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-58, AND MASSSPECTROMETRY.	18655026 [Abstract]