UniProt ID | SF3B5_HUMAN | |
---|---|---|
UniProt AC | Q9BWJ5 | |
Protein Name | Splicing factor 3B subunit 5 | |
Gene Name | SF3B5 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 86 | |
Subcellular Localization | Nucleus . | |
Protein Description | Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex, a constituent of the spliceosome. [PubMed: 27720643] | |
Protein Sequence | MTDRYTIHSQLEHLQSKYIGTGHADTTKWEWLVNQHRDSYCSYMGHFDLLNYFAIAENESKARVRFNLMEKMLQPCGPPADKPEEN | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MTDRYTIHS ------CCCCEEHHH | 29.23 | 20068231 | |
2 | Acetylation | ------MTDRYTIHS ------CCCCEEHHH | 29.23 | 19413330 | |
5 | Phosphorylation | ---MTDRYTIHSQLE ---CCCCEEHHHHHH | 16.92 | 29978859 | |
6 | Phosphorylation | --MTDRYTIHSQLEH --CCCCEEHHHHHHH | 17.07 | 26074081 | |
9 | Phosphorylation | TDRYTIHSQLEHLQS CCCEEHHHHHHHHHH | 32.39 | 17525332 | |
16 | Phosphorylation | SQLEHLQSKYIGTGH HHHHHHHHCCCCCCC | 33.51 | 27080861 | |
17 | Acetylation | QLEHLQSKYIGTGHA HHHHHHHCCCCCCCC | 28.11 | 19608861 | |
17 | Ubiquitination | QLEHLQSKYIGTGHA HHHHHHHCCCCCCCC | 28.11 | 22053931 | |
18 | Phosphorylation | LEHLQSKYIGTGHAD HHHHHHCCCCCCCCC | 15.16 | 28152594 | |
18 | Nitration | LEHLQSKYIGTGHAD HHHHHHCCCCCCCCC | 15.16 | - | |
28 | Acetylation | TGHADTTKWEWLVNQ CCCCCHHHHHHHHHH | 45.25 | 25825284 | |
28 | Ubiquitination | TGHADTTKWEWLVNQ CCCCCHHHHHHHHHH | 45.25 | 22817900 | |
69 | Sulfoxidation | ARVRFNLMEKMLQPC HHHHHHHHHHHHCCC | 4.96 | 21406390 | |
71 | Ubiquitination | VRFNLMEKMLQPCGP HHHHHHHHHHCCCCC | 30.83 | 21963094 | |
71 | Acetylation | VRFNLMEKMLQPCGP HHHHHHHHHHCCCCC | 30.83 | 26051181 | |
72 | Sulfoxidation | RFNLMEKMLQPCGPP HHHHHHHHHCCCCCC | 2.40 | 21406390 | |
76 | Glutathionylation | MEKMLQPCGPPADKP HHHHHCCCCCCCCCC | 9.13 | 22555962 | |
82 | Acetylation | PCGPPADKPEEN--- CCCCCCCCCCCC--- | 57.33 | 26822725 | |
82 | Ubiquitination | PCGPPADKPEEN--- CCCCCCCCCCCC--- | 57.33 | - |
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 SF3B5_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SF3B5_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 SF3B5_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SMD1_HUMAN | SNRPD1 | physical | 22939629 | |
SPF30_HUMAN | SMNDC1 | physical | 22939629 | |
SNRPA_HUMAN | SNRPA | physical | 22939629 | |
SIM20_HUMAN | SMIM20 | physical | 22939629 | |
SPEB_HUMAN | AGMAT | physical | 22939629 | |
VRK1_HUMAN | VRK1 | physical | 22939629 | |
STRN_HUMAN | STRN | physical | 22939629 | |
TOX4_HUMAN | TOX4 | physical | 22939629 |
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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Acetylation | |
Reference | PubMed |
"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-17, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"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-9, AND MASSSPECTROMETRY. |