ELOA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ELOA1_MOUSE
• UniProt AC: Q8CB77
• Protein Name: Elongin-A
• Gene Name: Eloa {ECO:0000312|MGI:MGI:1351315}
• Organism: Mus musculus (Mouse).
• Sequence Length: 773
• 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: MAAESALQVVEKLQARLAANPDPKKLLKYLKKLSILPITVDILVETGVGKTVNSFRKHEQVGNFARDLVAQWKKLVPVERNSEAEDQDFEKNNSRKRPRDALQREEELEGNYQESWKPSGSRSYSPEHRQKKHKKLSEPERPHKVAHSHEKRDERKRCHKVSPPYSSDPESSDYGHVQSPPPSSPHQMYTDLSRSPEEDQEPIISHQKPGKVHSNTFQDRLGVSHLGEQGKGAVSHHKQHRSSHKEKHPADAREDEKISAVSREKSHKASSKEESRRLLSGDSAKEKLPSSVVKKDKDREGSSLKKKFSPALDVASDNHFKKPKHKDSEKAKSDKNKQSVDGVDSGRGTGDPLPKAKEKVPNHLKAQEGKVRTNADGKSAGPLHPKAEETDVDDEFERPTMSFESYLSYDQPRKKKKKVVKTSSTALGEKGLKKKDSKSTSKNLNSAQKLPKVNENKSEKLQPAGAEPTRPRKVPTDVLPALPDIPLPAIHANYRPLPSLELIPSFQPKRKAFSSPQEEEEAGFTGRRMNSKMQVYSGSKCAYLPKMMTLHQQCIRVLKNNIDSIFEVGGVPYSVLEPVLERCTPDQLYRIEECNHVLIEETDQLWKVHCHRDFKEERPEEYESWREMYLRLQDAREQRLRLLTNNIRSAHANKPKGRQAKMAFVNSVAKPPRDVRRRQEKFGTGGAAVPEKVRIKPAPYTTGSSHVPASNSSSNFHSSPEELAYDGPSTSSAHLAPVASSSVSYDPRKPAVKKIAPMMAKTIKAFKNRFSRR

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
34	Phosphorylation	LKYLKKLSILPITVD HHHHHHCCCCEEEEE	30.84	-
82	Phosphorylation	LVPVERNSEAEDQDF HCCCCCCCHHHHCCH	44.39	25521595
112	Phosphorylation	EEELEGNYQESWKPS HHHHCCCCCCCCCCC	25.23	25159016
121	Phosphorylation	ESWKPSGSRSYSPEH CCCCCCCCCCCCHHH	23.53	20469934
123	Phosphorylation	WKPSGSRSYSPEHRQ CCCCCCCCCCHHHHH	31.49	21743459
124	Phosphorylation	KPSGSRSYSPEHRQK CCCCCCCCCHHHHHH	27.43	25195567
125	Phosphorylation	PSGSRSYSPEHRQKK CCCCCCCCHHHHHHH	25.67	26824392
137	Phosphorylation	QKKHKKLSEPERPHK HHHHHCCCCCCCCHH	61.04	25159016
165	Phosphorylation	CHKVSPPYSSDPESS HCCCCCCCCCCCCCC	24.96	25338131
171	Phosphorylation	PYSSDPESSDYGHVQ CCCCCCCCCCCCCCC	33.62	25338131
179	Phosphorylation	SDYGHVQSPPPSSPH CCCCCCCCCCCCCCC	37.98	25338131
184	Phosphorylation	VQSPPPSSPHQMYTD CCCCCCCCCCCCCCC	31.98	25338131
195	Phosphorylation	MYTDLSRSPEEDQEP CCCCCCCCCHHHCCC	33.03	25521595
205	Phosphorylation	EDQEPIISHQKPGKV HHCCCCCCCCCCCCC	22.15	25777480
224	Phosphorylation	FQDRLGVSHLGEQGK HHHHHCCCCCCCCCC	15.93	28066266
259	Phosphorylation	AREDEKISAVSREKS HHHHHHHHHHHHHHH	33.41	23737553
262	Phosphorylation	DEKISAVSREKSHKA HHHHHHHHHHHHCCC	34.14	23737553
266	Phosphorylation	SAVSREKSHKASSKE HHHHHHHHCCCCCHH	26.01	-
280	Phosphorylation	EESRRLLSGDSAKEK HHHHHHHCCCHHHHH	45.18	26060331
283	Phosphorylation	RRLLSGDSAKEKLPS HHHHCCCHHHHHCCH	44.78	29176673
290	Phosphorylation	SAKEKLPSSVVKKDK HHHHHCCHHHCCCCC	46.32	28066266
291	Phosphorylation	AKEKLPSSVVKKDKD HHHHCCHHHCCCCCC	29.05	28066266
309	Phosphorylation	SSLKKKFSPALDVAS CCCHHHCCHHHHHHC	20.38	25521595
330	Acetylation	PKHKDSEKAKSDKNK CCCCCHHHHHCCCCC	66.13	7631041
332	Acetylation	HKDSEKAKSDKNKQS CCCHHHHHCCCCCCC	70.97	7631051
335	Acetylation	SEKAKSDKNKQSVDG HHHHHCCCCCCCCCC	73.47	7631061
379	Phosphorylation	RTNADGKSAGPLHPK CCCCCCCCCCCCCCC	43.94	-
390	Phosphorylation	LHPKAEETDVDDEFE CCCCCHHCCCCCCCC	32.59	26239621
422	Phosphorylation	KKKKVVKTSSTALGE CCCCEEECCCHHHHH	19.12	30635358
423	Phosphorylation	KKKVVKTSSTALGEK CCCEEECCCHHHHHH	21.70	30635358
424	Phosphorylation	KKVVKTSSTALGEKG CCEEECCCHHHHHHC	23.96	30635358
425	Phosphorylation	KVVKTSSTALGEKGL CEEECCCHHHHHHCC	26.18	30635358
430	Acetylation	SSTALGEKGLKKKDS CCHHHHHHCCCCCCC	68.68	23806337
505	Phosphorylation	PSLELIPSFQPKRKA CCCCCCCCCCCCCCC	29.53	24719451
514	Phosphorylation	QPKRKAFSSPQEEEE CCCCCCCCCCHHHHH	46.07	26239621
515	Phosphorylation	PKRKAFSSPQEEEEA CCCCCCCCCHHHHHH	24.93	25521595
536	Phosphorylation	MNSKMQVYSGSKCAY CCCCEEEECCCCHHH	7.16	28576409
537	Phosphorylation	NSKMQVYSGSKCAYL CCCEEEECCCCHHHH	37.42	24719451
684	Phosphorylation	RRQEKFGTGGAAVPE HHHHHHCCCCCCCCC	35.26	25777480
710	Phosphorylation	GSSHVPASNSSSNFH CCCCCCCCCCCCCCC	31.04	25338131
712	Phosphorylation	SHVPASNSSSNFHSS CCCCCCCCCCCCCCC	32.42	25338131
718	Phosphorylation	NSSSNFHSSPEELAY CCCCCCCCCHHHHCC	43.37	25338131
719	Phosphorylation	SSSNFHSSPEELAYD CCCCCCCCHHHHCCC	27.97	25338131

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ELOA1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ELOA1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ELOA1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FOXB1_MOUSE	Foxb1	physical	20211142
RPB1_MOUSE	Polr2a	physical	19037258

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-195, AND MASSSPECTROMETRY.
PubMed: 19144319

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195 AND SER-309, ANDMASS SPECTROMETRY.
PubMed: 19367708