UniProt ID | ELOA2_HUMAN | |
---|---|---|
UniProt AC | Q8IYF1 | |
Protein Name | Elongin-A2 | |
Gene Name | ELOA2 {ECO:0000312|HGNC:HGNC:30771} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 753 | |
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 A2 is transcriptionally active but its transcription activity is not enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).. | |
Protein Sequence | MAAGSTTLHAVEKLQVRLATKTEPKKLEKYLQKLSALPMTADILAETGIRKTVKRLRKHQHVGDFARDLAARWKKLVLVDRNTRPGPQDPEESASRQRFGEALQDQEKAWGFPENATAPRSPSHSPEHRRTARRTPPGQQRPHPRSHSREPRAERKCPRIAPADSGRYRASPTRTAPLRMPEGPEPAAPGKQPGRGHTHAAQGGPLLCPGCQGQPQGKAVVSHSKGHKSSRQEKRPLCAQGDWHSPTLIREKSCGACLREETPRMPSWASARDRQPSDFKTDKEGGQAGSGQRVPALEEAPDSHQKRPQHSHSNKKRPSLDGRDPGNGTHGLSPEEKEQLSNDRETQEGKPPTAHLDRTSVSSLSEVEEVDMAEEFEQPTLSCEKYLTYDQLRKQKKKTGKSATTALGDKQRKANESKGTRESWDSAKKLPPVQESQSERLQAAGADSAGPKTVPSHVFSELWDLSEAWMQANYDPLSDSDSMTSQAKPEALSSPKFREEAAFPGRRVNAKMPVYSGSRPACQLQVPTLRQQCAQVLRNNPDALSDVGEVPYWVLEPVLEGWRPDQLYRRKKDNHALVRETDELRRNHCFQDFKEEKPQENKTWREQYLRLPDAPEQRLRVMTTNIRSARGNNPNGREAKMICFKSVAKTPYDTSRRQEKSAGDADPENGEIKPASKPAGSSHTPSSQSSSGGGRDSSSSILRWLPEKRANPCLSSSNEHAAPAAKTRKQAAKKVAPLMAKAIRDYKRRFSRR | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
21 | Acetylation | LQVRLATKTEPKKLE HHHHHHCCCCHHHHH | 45.33 | - | |
26 | "N6,N6-dimethyllysine" | ATKTEPKKLEKYLQK HCCCCHHHHHHHHHH | 73.01 | - | |
26 | Methylation | ATKTEPKKLEKYLQK HCCCCHHHHHHHHHH | 73.01 | - | |
270 | Phosphorylation | PRMPSWASARDRQPS CCCCCHHHHCCCCCC | 19.99 | - | |
386 | Phosphorylation | PTLSCEKYLTYDQLR CCCCHHHCCCHHHHH | 5.08 | 28102081 | |
388 | Phosphorylation | LSCEKYLTYDQLRKQ CCHHHCCCHHHHHHH | 23.20 | 28102081 | |
389 | Phosphorylation | SCEKYLTYDQLRKQK CHHHCCCHHHHHHHH | 10.09 | 28102081 | |
480 | Phosphorylation | NYDPLSDSDSMTSQA CCCCCCCCCCCCCCC | 28.36 | 21601212 | |
603 | Phosphorylation | EKPQENKTWREQYLR HCCCCCCCHHHHHHC | 41.14 | 26074081 | |
608 | Phosphorylation | NKTWREQYLRLPDAP CCCHHHHHHCCCCCH | 6.77 | 26074081 | |
628 | Phosphorylation | VMTTNIRSARGNNPN HHHHHHHHHCCCCCC | 20.65 | 23403867 | |
676 | Phosphorylation | NGEIKPASKPAGSSH CCCCCCCCCCCCCCC | 47.93 | - | |
699 | Phosphorylation | GGGRDSSSSILRWLP CCCCCCHHHHHHHCC | 25.91 | - | |
700 | Phosphorylation | GGRDSSSSILRWLPE CCCCCHHHHHHHCCH | 27.82 | 24719451 |
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 ELOA2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ELOA2_HUMAN !! |
* 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 ELOA2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
KXDL1_HUMAN | KXD1 | physical | 16189514 | |
SOLH2_HUMAN | SOHLH2 | physical | 16189514 | |
CEP70_HUMAN | CEP70 | physical | 16189514 | |
KR412_HUMAN | KRTAP4-12 | physical | 16189514 | |
ELOB_HUMAN | TCEB2 | physical | 10692460 | |
ELOC_HUMAN | TCEB1 | physical | 10692460 | |
ZCH10_HUMAN | ZCCHC10 | physical | 25416956 |
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. |
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