dbPTM

ELOA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ELOA1_HUMAN
UniProt AC	Q14241
Protein Name	Elongin-A
Gene Name	ELOA {ECO:0000312\|HGNC:HGNC:11620}
Organism	Homo sapiens (Human).
Sequence Length	798
Subcellular Localization	Nucleus .
Protein Description	SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex)..
Protein Sequence	MHGGRSCGPRTRREPSSGEEAAPVTAMAAESALQVVEKLQARLAANPDPKKLLKYLKKLSTLPITVDILAETGVGKTVNSLRKHEHVGSFARDLVAQWKKLVPVERNAEPDEQDFEKSNSRKRPRDALQKEEEMEGDYQETWKATGSRSYSPDHRQKKHRKLSELERPHKVSHGHERRDERKRCHRMSPTYSSDPESSDYGHVQSPPSCTSPHQMYVDHYRSLEEDQEPIVSHQKPGKGHSNAFQDRLGASQERHLGEPHGKGVVSQNKEHKSSHKDKRPVDAKSDEKASVVSREKSHKALSKEENRRPPSGDNAREKPPSSGVKKEKDREGSSLKKKCLPPSEAASDNHLKKPKHRDPEKAKLDKSKQGLDSFDTGKGAGDLLPKVKEKGSNNLKTPEGKVKTNLDRKSLGSLPKVEETDMEDEFEQPTMSFESYLSYDQPRKKKKKIVKTSATALGDKGLKKNDSKSTGKNLDSVQKLPKVNKTKSEKPAGADLAKLRKVPDVLPVLPDLPLPAIQANYRPLPSLELISSFQPKRKAFSSPQEEEEAGFTGRRMNSKMQVYSGSKCAYLPKMMTLHQQCIRVLKNNIDSIFEVGGVPYSVLEPVLERCTPDQLYRIEEYNHVLIEETDQLWKVHCHRDFKEERPEEYESWREMYLRLQDAREQRLRVLTKNIQFAHANKPKGRQAKMAFVNSVAKPPRDVRRRQEKFGTGGAAVPEKIKIKPAPYPMGSSHASASSISFNPSPEEPAYDGPSTSSAHLAPVVSSTVSYDPRKPTVKKIAPMMAKTIKAFKNRFSRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MHGGRSCGPRTRR --CCCCCCCCCCCCC	27.05	29083192
17	Phosphorylation	RTRREPSSGEEAAPV CCCCCCCCCCCCCHH	62.02	26133373
31	Phosphorylation	VTAMAAESALQVVEK HHHHHHHHHHHHHHH	29.56	20860994
38	Methylation	SALQVVEKLQARLAA HHHHHHHHHHHHHHC	34.00	23644510
72	Phosphorylation	TVDILAETGVGKTVN EHHHHHHHCCCHHHH	31.40	-
83	Ubiquitination	KTVNSLRKHEHVGSF HHHHHHHHCCCHHHH	59.65	29967540
99	Acetylation	RDLVAQWKKLVPVER HHHHHHHHHHCCCCC	24.93	25953088
117	Ubiquitination	PDEQDFEKSNSRKRP CCHHHHHHHHCCCCH	55.73	24816145
118	Phosphorylation	DEQDFEKSNSRKRPR CHHHHHHHHCCCCHH	32.60	26055452
125	Phosphorylation	SNSRKRPRDALQKEE HHCCCCHHHHHHHHH	45.96	17081983
137	Phosphorylation	KEEEMEGDYQETWKA HHHHHHCCHHHHHHH	28.74	17287340
138	Phosphorylation	EEEMEGDYQETWKAT HHHHHCCHHHHHHHH	21.07	28796482
141	Phosphorylation	MEGDYQETWKATGSR HHCCHHHHHHHHCCC	19.42	29978859
145	Phosphorylation	YQETWKATGSRSYSP HHHHHHHHCCCCCCH	31.78	26074081
147	Phosphorylation	ETWKATGSRSYSPDH HHHHHHCCCCCCHHH	17.44	26074081
149	Phosphorylation	WKATGSRSYSPDHRQ HHHHCCCCCCHHHHH	31.49	30266825
150	Phosphorylation	KATGSRSYSPDHRQK HHHCCCCCCHHHHHH	24.10	30266825
151	Phosphorylation	ATGSRSYSPDHRQKK HHCCCCCCHHHHHHH	25.71	23401153
163	Phosphorylation	QKKHRKLSELERPHK HHHHHHHHHCCCCCC	43.07	23401153
170	Ubiquitination	SELERPHKVSHGHER HHCCCCCCCCCCCCC	48.38	29967540
188	Phosphorylation	RKRCHRMSPTYSSDP HHHHHCCCCCCCCCC	17.66	23663014
190	Phosphorylation	RCHRMSPTYSSDPES HHHCCCCCCCCCCCC	28.82	23663014
191	Phosphorylation	CHRMSPTYSSDPESS HHCCCCCCCCCCCCC	15.01	23663014
192	Phosphorylation	HRMSPTYSSDPESSD HCCCCCCCCCCCCCC	30.64	23663014
193	Phosphorylation	RMSPTYSSDPESSDY CCCCCCCCCCCCCCC	46.93	23663014
197	Phosphorylation	TYSSDPESSDYGHVQ CCCCCCCCCCCCCCC	33.62	23663014
198	Phosphorylation	YSSDPESSDYGHVQS CCCCCCCCCCCCCCC	32.94	23663014
200	Phosphorylation	SDPESSDYGHVQSPP CCCCCCCCCCCCCCC	15.87	23663014
205	Phosphorylation	SDYGHVQSPPSCTSP CCCCCCCCCCCCCCC	37.38	23663014
208	Phosphorylation	GHVQSPPSCTSPHQM CCCCCCCCCCCCCCC	33.15	23663014
210	Phosphorylation	VQSPPSCTSPHQMYV CCCCCCCCCCCCCCC	50.02	23663014
211	Phosphorylation	QSPPSCTSPHQMYVD CCCCCCCCCCCCCCH	25.39	23663014
216	Phosphorylation	CTSPHQMYVDHYRSL CCCCCCCCCHHCCCC	8.99	23663014
220	Phosphorylation	HQMYVDHYRSLEEDQ CCCCCHHCCCCCCCC	9.46	23663014
222	Phosphorylation	MYVDHYRSLEEDQEP CCCHHCCCCCCCCCC	32.73	30266825
225	Phosphorylation	DHYRSLEEDQEPIVS HHCCCCCCCCCCCCC	71.00	15302935
232	Phosphorylation	EDQEPIVSHQKPGKG CCCCCCCCCCCCCCC	22.41	25159151
235	Acetylation	EPIVSHQKPGKGHSN CCCCCCCCCCCCCCH	50.76	25953088
235	Ubiquitination	EPIVSHQKPGKGHSN CCCCCCCCCCCCCCH	50.76	29967540
247	Methylation	HSNAFQDRLGASQER CCHHHHHHHCHHHCC	25.00	115918317
251	Phosphorylation	FQDRLGASQERHLGE HHHHHCHHHCCCCCC	30.67	20363803
262	Ubiquitination	HLGEPHGKGVVSQNK CCCCCCCCCCCCCCH	45.56	29967540
266	Phosphorylation	PHGKGVVSQNKEHKS CCCCCCCCCCHHCCC	26.15	29083192
273	Phosphorylation	SQNKEHKSSHKDKRP CCCHHCCCCCCCCCC	39.31	29083192
274	Phosphorylation	QNKEHKSSHKDKRPV CCHHCCCCCCCCCCC	39.08	29083192
285	Phosphorylation	KRPVDAKSDEKASVV CCCCCCCCCHHHHHH	53.36	29214152
293	Phosphorylation	DEKASVVSREKSHKA CHHHHHHCHHHHHHH	32.35	29414761
311	Phosphorylation	EENRRPPSGDNAREK HHHCCCCCCCCCCCC	62.55	21406692
321	Phosphorylation	NAREKPPSSGVKKEK CCCCCCCCCCCCCCC	48.53	17494752
333	Phosphorylation	KEKDREGSSLKKKCL CCCCCCCCCCCHHCC	27.95	28102081
334	Phosphorylation	EKDREGSSLKKKCLP CCCCCCCCCCHHCCC	55.88	28102081
343	Phosphorylation	KKKCLPPSEAASDNH CHHCCCHHHHHCCCC	37.62	17494752
347	Phosphorylation	LPPSEAASDNHLKKP CCHHHHHCCCCCCCC	46.09	17494752
373	Phosphorylation	KSKQGLDSFDTGKGA HHHCCCCCCCCCCCH	30.02	21815630
376	Phosphorylation	QGLDSFDTGKGAGDL CCCCCCCCCCCHHHH	38.49	28102081
392	Phosphorylation	PKVKEKGSNNLKTPE HHHHHCCCCCCCCCC	33.34	29396449
397	Phosphorylation	KGSNNLKTPEGKVKT CCCCCCCCCCCCCCC	29.73	25159151
403	Acetylation	KTPEGKVKTNLDRKS CCCCCCCCCCCCHHC	34.87	25953088
410	Phosphorylation	KTNLDRKSLGSLPKV CCCCCHHCCCCCCCC	38.57	30266825
413	Phosphorylation	LDRKSLGSLPKVEET CCHHCCCCCCCCEEC	46.95	30266825
420	Phosphorylation	SLPKVEETDMEDEFE CCCCCEECCCCCCCC	27.43	27422710
430	Phosphorylation	EDEFEQPTMSFESYL CCCCCCCCCCHHHHH	25.74	29523821
432	Phosphorylation	EFEQPTMSFESYLSY CCCCCCCCHHHHHCC	28.48	29523821
435	Phosphorylation	QPTMSFESYLSYDQP CCCCCHHHHHCCCCC	29.39	28122231
452	Phosphorylation	KKKKIVKTSATALGD HCCHHHHCCHHHHHC	16.82	29396449
453	Phosphorylation	KKKIVKTSATALGDK CCHHHHCCHHHHHCC	20.22	29396449
455	Phosphorylation	KIVKTSATALGDKGL HHHHCCHHHHHCCCC	23.37	29396449
460	Acetylation	SATALGDKGLKKNDS CHHHHHCCCCCCCCC	65.43	25953088
472	Acetylation	NDSKSTGKNLDSVQK CCCCCCCCCHHHHHH	55.19	23749302
476	Phosphorylation	STGKNLDSVQKLPKV CCCCCHHHHHHCCCC	29.61	29214152
479	Ubiquitination	KNLDSVQKLPKVNKT CCHHHHHHCCCCCCC	65.68	29967540
487	Acetylation	LPKVNKTKSEKPAGA CCCCCCCCCCCCCCC	59.22	25953088
488	Phosphorylation	PKVNKTKSEKPAGAD CCCCCCCCCCCCCCC	56.96	29396449
490	Acetylation	VNKTKSEKPAGADLA CCCCCCCCCCCCCHH	47.46	25953088
538	Ubiquitination	SSFQPKRKAFSSPQE HHCCCCCCCCCCCHH	60.97	29967540
541	Phosphorylation	QPKRKAFSSPQEEEE CCCCCCCCCCHHHHH	46.07	30266825
542	Phosphorylation	PKRKAFSSPQEEEEA CCCCCCCCCHHHHHH	24.93	30266825
552	Phosphorylation	EEEEAGFTGRRMNSK HHHHHCCCCCCCCCC	28.94	30266825
558	Phosphorylation	FTGRRMNSKMQVYSG CCCCCCCCCEEEECC	21.84	29978859
559	Acetylation	TGRRMNSKMQVYSGS CCCCCCCCEEEECCC	28.48	25953088
563	Phosphorylation	MNSKMQVYSGSKCAY CCCCEEEECCCCHHH	7.16	29978859
564	Phosphorylation	NSKMQVYSGSKCAYL CCCEEEECCCCHHHH	37.42	29978859
566	Phosphorylation	KMQVYSGSKCAYLPK CEEEECCCCHHHHHH	20.72	30576142
570	Phosphorylation	YSGSKCAYLPKMMTL ECCCCHHHHHHHHHH	32.76	30576142
681	Acetylation	IQFAHANKPKGRQAK CHHHCCCCCCCHHHH	49.22	23749302
694	Phosphorylation	AKMAFVNSVAKPPRD HHHHHHHHCCCCHHH	20.39	28555341
697	Acetylation	AFVNSVAKPPRDVRR HHHHHCCCCHHHHHH	54.09	25953088
711	Phosphorylation	RRQEKFGTGGAAVPE HHHHHHCCCCCCCCC	35.26	25159151
744	Phosphorylation	SSISFNPSPEEPAYD CCCCCCCCCCCCCCC	46.15	28348404
786	Acetylation	KIAPMMAKTIKAFKN HHHHHHHHHHHHHHH	32.65	25953088

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 ELOA1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ELOA1_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 ELOA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NINL_HUMAN	NINL	physical	16189514
ELOB_HUMAN	TCEB2	physical	18187417
ELOC_HUMAN	TCEB1	physical	18187417
ELOB_HUMAN	TCEB2	physical	10692460
ELOC_HUMAN	TCEB1	physical	10692460
ELOC_HUMAN	TCEB1	physical	10449727
ELOB_HUMAN	TCEB2	physical	7660122
ELOC_HUMAN	TCEB1	physical	7660122
FSBP_HUMAN	RAD54B	physical	19060904
RA54B_HUMAN	RAD54B	physical	19060904
MED26_HUMAN	MED26	physical	21729782
PSB9_HUMAN	PSMB9	physical	16957778
RPB1_HUMAN	POLR2A	physical	16957778
RPB2_HUMAN	POLR2B	physical	16957778
RPB3_HUMAN	POLR2C	physical	16957778
RPB4_HUMAN	POLR2D	physical	16957778
RPAB1_HUMAN	POLR2E	physical	16957778
RPAB2_HUMAN	POLR2F	physical	16957778
RPB7_HUMAN	POLR2G	physical	16957778
RPAB3_HUMAN	POLR2H	physical	16957778
RPB9_HUMAN	POLR2I	physical	16957778
RPAB5_HUMAN	POLR2L	physical	16957778
RPB11_HUMAN	POLR2J	physical	16957778
RPAB4_HUMAN	POLR2K	physical	16957778
JKIP2_HUMAN	JAKMIP2	physical	25416956
PLK4_HUMAN	PLK4	physical	25416956
TRIM1_HUMAN	MID2	physical	25416956
TRI54_HUMAN	TRIM54	physical	25416956
HOMEZ_HUMAN	HOMEZ	physical	25416956
GMCL1_HUMAN	GMCL1	physical	25416956
CEP70_HUMAN	CEP70	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
SPERT_HUMAN	SPERT	physical	25416956
CE57L_HUMAN	CEP57L1	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
BRCA1_HUMAN	BRCA1	physical	25184681
RPB1_HUMAN	POLR2A	physical	19037258
CAF1A_HUMAN	CHAF1A	physical	26344197
ELOB_HUMAN	TCEB2	physical	25878247
ELOC_HUMAN	TCEB1	physical	25878247
CUL5_HUMAN	CUL5	physical	25878247
NEDD8_HUMAN	NEDD8	physical	25878247
RHG26_HUMAN	ARHGAP26	physical	27173435
CTR9_HUMAN	CTR9	physical	27173435
CUL3_HUMAN	CUL3	physical	27173435

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 ELOA1_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-410 AND THR-420, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-163, AND MASSSPECTROMETRY.	17287340 [Abstract]
"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-151, AND MASSSPECTROMETRY.	17081983 [Abstract]