Phospho-hnRNP K (Ser216) Antibody - #AF3639
Product: | Phospho-hnRNP K (Ser216) Antibody |
Catalog: | AF3639 |
Description: | Rabbit polyclonal antibody to Phospho-hnRNP K (Ser216) |
Application: | IF/ICC |
Reactivity: | Human, Mouse, Rat |
Mol.Wt.: | 51kD(Calculated). |
Uniprot: | P61978 |
RRID: | AB_2846953 |
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# AF3639, RRID:AB_2846953.
Fold/Unfold
CSBP; dC stretch binding protein; FLJ41122; Heterogeneous nuclear ribonucleoprotein K; hnRNP K; HNRNPK; HNRPK; HNRPK_HUMAN; Transformation up regulated nuclear protein; Transformation up-regulated nuclear protein; Transformation upregulated nuclear protein; TUNP;
Immunogens
A synthesized peptide derived from human hnRNP K around the phosphorylation site of Ser216.
- P61978 HNRPK_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
METEQPEETFPNTETNGEFGKRPAEDMEEEQAFKRSRNTDEMVELRILLQSKNAGAVIGKGGKNIKALRTDYNASVSVPDSSGPERILSISADIETIGEILKKIIPTLEEGLQLPSPTATSQLPLESDAVECLNYQHYKGSDFDCELRLLIHQSLAGGIIGVKGAKIKELRENTQTTIKLFQECCPHSTDRVVLIGGKPDRVVECIKIILDLISESPIKGRAQPYDPNFYDETYDYGGFTMMFDDRRGRPVGFPMRGRGGFDRMPPGRGGRPMPPSRRDYDDMSPRRGPPPPPPGRGGRGGSRARNLPLPPPPPPRGGDLMAYDRRGRPGDRYDGMVGFSADETWDSAIDTWSPSEWQMAYEPQGGSGYDYSYAGGRGSYGDLGGPIITTQVTIPKDLAGSIIGKGGQRIKQIRHESGASIKIDEPLEGSEDRIITITGTQDQIQNAQYLLQNSVKQYSGKFF
PTMs - P61978 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
M1 | Acetylation | Uniprot | |
T3 | Phosphorylation | Uniprot | |
K21 | Acetylation | Uniprot | |
R22 | Methylation | Uniprot | |
K34 | Acetylation | Uniprot | |
K34 | Methylation | Uniprot | |
K34 | Sumoylation | Uniprot | |
K34 | Ubiquitination | Uniprot | |
S36 | Phosphorylation | Uniprot | |
T39 | Phosphorylation | Uniprot | |
R46 | Methylation | Uniprot | |
K52 | Sumoylation | Uniprot | |
K52 | Ubiquitination | Uniprot | |
K60 | Acetylation | Uniprot | |
K60 | Sumoylation | Uniprot | |
K60 | Ubiquitination | Uniprot | |
K63 | Ubiquitination | Uniprot | |
K66 | Ubiquitination | Uniprot | |
Y72 | Phosphorylation | P12931 (SRC) | Uniprot |
S75 | Phosphorylation | Uniprot | |
S77 | Phosphorylation | Uniprot | |
S81 | Phosphorylation | Uniprot | |
S82 | Phosphorylation | Uniprot | |
S89 | Phosphorylation | Uniprot | |
K102 | Ubiquitination | Uniprot | |
K103 | Ubiquitination | Uniprot | |
S116 | Phosphorylation | Uniprot | |
T118 | Phosphorylation | Uniprot | |
T120 | Phosphorylation | Uniprot | |
S121 | Phosphorylation | Uniprot | |
Y135 | Phosphorylation | Uniprot | |
Y138 | Phosphorylation | Uniprot | |
K139 | Methylation | Uniprot | |
K139 | Ubiquitination | Uniprot | |
S141 | Phosphorylation | Uniprot | |
R148 | Methylation | Uniprot | |
S154 | Phosphorylation | Uniprot | |
K163 | Sumoylation | Uniprot | |
K163 | Ubiquitination | Uniprot | |
K166 | Ubiquitination | Uniprot | |
K168 | Ubiquitination | Uniprot | |
K179 | Acetylation | Uniprot | |
K179 | Ubiquitination | Uniprot | |
C184 | S-Nitrosylation | Uniprot | |
C185 | S-Nitrosylation | Uniprot | |
S188 | Phosphorylation | Uniprot | |
R191 | Methylation | Uniprot | |
K198 | Methylation | Uniprot | |
K198 | Ubiquitination | Uniprot | |
R201 | Methylation | Uniprot | |
K207 | Ubiquitination | Uniprot | |
S214 | Phosphorylation | Uniprot | |
S216 | Phosphorylation | P53779 (MAPK10) , P06493 (CDK1) , P24941 (CDK2) , P45983 (MAPK8) | Uniprot |
K219 | Acetylation | Uniprot | |
K219 | Sumoylation | Uniprot | |
K219 | Ubiquitination | Uniprot | |
Y225 | Phosphorylation | P12931 (SRC) | Uniprot |
Y230 | Phosphorylation | P12931 (SRC) | Uniprot |
Y234 | Phosphorylation | P12931 (SRC) | Uniprot |
Y236 | Phosphorylation | P12931 (SRC) | Uniprot |
R246 | Methylation | Uniprot | |
R247 | Methylation | Uniprot | |
R249 | Methylation | Uniprot | |
R256 | Methylation | Uniprot | |
R258 | Methylation | Uniprot | |
R263 | Methylation | Uniprot | |
R268 | Methylation | Uniprot | |
R271 | Methylation | Uniprot | |
S276 | Phosphorylation | Uniprot | |
R277 | Methylation | Uniprot | |
R278 | Methylation | Uniprot | |
Y280 | Phosphorylation | Uniprot | |
S284 | Phosphorylation | P28482 (MAPK1) , P27361 (MAPK3) | Uniprot |
R286 | Methylation | Uniprot | |
R296 | Methylation | Uniprot | |
R299 | Methylation | Uniprot | |
S302 | Phosphorylation | Q05655 (PRKCD) | Uniprot |
R303 | Methylation | Uniprot | |
R305 | Methylation | Uniprot | |
R316 | Methylation | Uniprot | |
Y323 | Phosphorylation | Uniprot | |
R325 | Methylation | Uniprot | |
R326 | Methylation | Uniprot | |
R328 | Methylation | Uniprot | |
Y333 | Phosphorylation | Uniprot | |
S353 | Phosphorylation | P53779 (MAPK10) , P45983 (MAPK8) , P27361 (MAPK3) | Uniprot |
Y361 | Phosphorylation | Uniprot | |
Y369 | Phosphorylation | Uniprot | |
Y371 | Phosphorylation | Uniprot | |
S372 | Phosphorylation | Uniprot | |
Y373 | Phosphorylation | Uniprot | |
R377 | Methylation | Uniprot | |
S379 | Phosphorylation | O14965 (AURKA) | Uniprot |
Y380 | Phosphorylation | P12931 (SRC) | Uniprot |
T389 | Phosphorylation | Uniprot | |
T390 | Phosphorylation | Uniprot | |
T393 | Phosphorylation | Uniprot | |
K396 | Ubiquitination | Uniprot | |
S401 | Phosphorylation | Uniprot | |
K405 | Sumoylation | Uniprot | |
K405 | Ubiquitination | Uniprot | |
S417 | Phosphorylation | Uniprot | |
S420 | Phosphorylation | Uniprot | |
K422 | Acetylation | Uniprot | |
K422 | Sumoylation | Uniprot | |
K422 | Ubiquitination | Uniprot | |
S430 | Phosphorylation | Uniprot | |
R433 | Methylation | Uniprot | |
T436 | Phosphorylation | Uniprot | |
T440 | Phosphorylation | Uniprot | |
Y449 | Phosphorylation | Uniprot | |
S454 | Phosphorylation | Uniprot | |
K456 | Ubiquitination | Uniprot | |
Y458 | Phosphorylation | P12931 (SRC) | Uniprot |
K461 | Acetylation | Uniprot | |
K461 | Ubiquitination | Uniprot |
Research Backgrounds
One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest.
Arg-296 and Arg-299 are dimethylated, probably to asymmetric dimethylarginine.
Sumoylated by CBX4. Sumoylation is increased upon DNA damage, such as that produced by doxorubicin, etoposide, UV light and camptothecin, due to enhanced CBX4 phosphorylation by HIPK2 under these conditions.
Ubiquitinated by MDM2. Doxorubicin treatment does not affect monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination.
O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
Cytoplasm. Nucleus>Nucleoplasm. Cell projection>Podosome.
Note: Recruited to p53/TP53-responsive promoters, in the presence of functional p53/TP53 (PubMed:16360036). In case of ASFV infection, there is a shift in the localization which becomes predominantly nuclear (PubMed:18775702).
Interacts with RBM42 and ZIK1 (By similarity). Interacts with BRDT (By similarity). Identified in the spliceosome C complex. Interacts with ANKRD28. Interacts with ASFV p30 protein. Interacts with DDX1. Interacts with MDM2; this interaction leads to ubiquitination and proteasomal degradation. Interacts with p53/TP53. Interacts with IVNS1ABP.
(Microbial infection) Interacts with HCV core protein.
Research Fields
· Genetic Information Processing > Transcription > Spliceosome.
· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.
· Human Diseases > Cancers: Overview > Viral carcinogenesis.
· Human Diseases > Cancers: Overview > MicroRNAs in cancer.
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