UniProt ID | KHDR2_HUMAN | |
---|---|---|
UniProt AC | Q5VWX1 | |
Protein Name | KH domain-containing, RNA-binding, signal transduction-associated protein 2 | |
Gene Name | KHDRBS2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 349 | |
Subcellular Localization | Nucleus . | |
Protein Description | RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds both poly(A) and poly(U) homopolymers. Phosphorylation by PTK6 inhibits its RNA-binding ability (By similarity). Induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer. Can regulate alternative splicing of NRXN1 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. Regulates cell-type specific alternative splicing of NRXN1 at AS4 and acts synergystically with SAM68 in exon skipping. In contrast acts antagonistically with SAM68 in NRXN3 exon skipping at AS4. Its phosphorylation by FYN inhibits its ability to regulate splice site selection. May function as an adapter protein for Src kinases during mitosis.. | |
Protein Sequence | MEEEKYLPELMAEKDSLDPSFVHASRLLAEEIEKFQGSDGKKEDEEKKYLDVISNKNIKLSERVLIPVKQYPKFNFVGKLLGPRGNSLKRLQEETGAKMSILGKGSMRDKAKEEELRKSGEAKYAHLSDELHVLIEVFAPPGEAYSRMSHALEEIKKFLVPDYNDEIRQEQLRELSYLNGSEDSGRGRGIRGRGIRIAPTAPSRGRGGAIPPPPPPGRGVLTPRGSTVTRGALPVPPVARGVPTPRARGAPTVPGYRAPPPPAHEAYEEYGYDDGYGGEYDDQTYETYDNSYATQTQSVPEYYDYGHGVSEDAYDSYAPEEWATTRSSLKAPPQRSARGGYREHPYGRY | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
6 | Phosphorylation | --MEEEKYLPELMAE --CCHHHHHHHHHHC | 30.67 | 20068231 | |
16 | Phosphorylation | ELMAEKDSLDPSFVH HHHHCCCCCCHHHHH | 45.82 | 26074081 | |
20 | Phosphorylation | EKDSLDPSFVHASRL CCCCCCHHHHHHHHH | 39.30 | 24719451 | |
25 | Phosphorylation | DPSFVHASRLLAEEI CHHHHHHHHHHHHHH | 14.48 | 26074081 | |
54 | O-linked_Glycosylation | KKYLDVISNKNIKLS HHHHHHHHCCCCCCC | 41.42 | 30379171 | |
56 | Acetylation | YLDVISNKNIKLSER HHHHHHCCCCCCCCC | 53.94 | 30589657 | |
69 | Acetylation | ERVLIPVKQYPKFNF CCEEEEHHHCCCCCC | 38.47 | 163895 | |
69 | Ubiquitination | ERVLIPVKQYPKFNF CCEEEEHHHCCCCCC | 38.47 | 21890473 | |
73 | Ubiquitination | IPVKQYPKFNFVGKL EEHHHCCCCCCHHHH | 48.26 | 73 | |
73 | Acetylation | IPVKQYPKFNFVGKL EEHHHCCCCCCHHHH | 48.26 | 22647397 | |
79 | Methylation | PKFNFVGKLLGPRGN CCCCCHHHHHCCCCH | 34.93 | 72622551 | |
79 | Acetylation | PKFNFVGKLLGPRGN CCCCCHHHHHCCCCH | 34.93 | 72622551 | |
95 | Phosphorylation | LKRLQEETGAKMSIL HHHHHHHHCCCEEHH | 41.51 | 20068231 | |
100 | Phosphorylation | EETGAKMSILGKGSM HHHCCCEEHHCCCHH | 17.60 | 20068231 | |
106 | Phosphorylation | MSILGKGSMRDKAKE EEHHCCCHHHHHHHH | 17.71 | 20068231 | |
112 | Acetylation | GSMRDKAKEEELRKS CHHHHHHHHHHHHHH | 71.98 | 19818047 | |
117 | Methylation | KAKEEELRKSGEAKY HHHHHHHHHHCCHHH | 34.08 | - | |
119 | Phosphorylation | KEEELRKSGEAKYAH HHHHHHHHCCHHHHC | 35.12 | 24719451 | |
128 | Phosphorylation | EAKYAHLSDELHVLI CHHHHCHHHCCEEEE | 21.12 | 24719451 | |
146 | Phosphorylation | APPGEAYSRMSHALE CCCCHHHHHHHHHHH | 28.67 | 24719451 | |
163 | Phosphorylation | KKFLVPDYNDEIRQE HHHHCCCCCHHHHHH | 20.60 | - | |
230 | Methylation | PRGSTVTRGALPVPP CCCCCCCCCCCCCCC | 24.85 | - | |
240 | Methylation | LPVPPVARGVPTPRA CCCCCCCCCCCCCCC | 47.04 | - | |
244 | Phosphorylation | PVARGVPTPRARGAP CCCCCCCCCCCCCCC | 24.01 | 24719451 | |
346 | Phosphorylation | GGYREHPYGRY---- CCCCCCCCCCC---- | 19.01 | - | |
348 | Methylation | YREHPYGRY------ CCCCCCCCC------ | 28.30 | - | |
349 | Phosphorylation | REHPYGRY------- CCCCCCCC------- | 20.67 | 28112733 |
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 KHDR2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KHDR2_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 KHDR2_HUMAN !! |
Kegg Disease | ||||||
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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-73, AND MASS SPECTROMETRY. |