KHDR1_RAT - dbPTM
KHDR1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KHDR1_RAT
UniProt AC Q91V33
Protein Name KH domain-containing, RNA-binding, signal transduction-associated protein 1
Gene Name Khdrbs1 {ECO:0000312|RGD:621459}
Organism Rattus norvegicus (Rat).
Sequence Length 443
Subcellular Localization Nucleus . Cytoplasm . Membrane . Predominantly located in the nucleus but also located partially in the cytoplasm.
Protein Description Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. May not be involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species. RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner. In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1. Can regulate alternative splicing of NRXN1 and NRXN3 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. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (By similarity)..
Protein Sequence MQRRDDPAARLTRSSGRSCSKDPSGAHPSVRLTPSRPSPLPHRSRGGGGGPRGGARASPATQPPPLLPPSNPGPDATVVGSAPTPLLPPSATAAAKMEPENKYLPELMAEKDSLDPSFTHAMQLLSVEIEKIQKGESKKDDEENYLDLFSHKNMKLKERVLIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKGGDPKYAHLNMDLHVFIEVFGPPCEAYALMAHAMEEVKKFLVPDMMDDICQEQFLELSYLNGVPEPSRGRGVSVRGRGAAPPPPPVPRGRGVGPPRGALVRGTPVRGSITRGATVTRGVPPPPTVRGAPTPRARTAGIQRIPLPPTPAPETYEDYGYDDSYAEQSYEGYEGYYSQSQGESEYYDYGHGELQDSYEAYGQDDWNGTRPSLKAPPARPVKGAYREHPYGRY
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 Orthologous
Protein Cluster
12PhosphorylationDDPAARLTRSSGRSC
CCHHHHHHHCCCCCC
23.9718779572
14PhosphorylationPAARLTRSSGRSCSK
HHHHHHHCCCCCCCC
31.7327097102
15PhosphorylationAARLTRSSGRSCSKD
HHHHHHCCCCCCCCC
34.6327097102
18PhosphorylationLTRSSGRSCSKDPSG
HHHCCCCCCCCCCCC
26.6928432305
20PhosphorylationRSSGRSCSKDPSGAH
HCCCCCCCCCCCCCC
41.1427097102
21AcetylationSSGRSCSKDPSGAHP
CCCCCCCCCCCCCCC
77.36-
24PhosphorylationRSCSKDPSGAHPSVR
CCCCCCCCCCCCCCC
59.7627097102
29PhosphorylationDPSGAHPSVRLTPSR
CCCCCCCCCCCCCCC
15.2525403869
33PhosphorylationAHPSVRLTPSRPSPL
CCCCCCCCCCCCCCC
14.5127097102
35PhosphorylationPSVRLTPSRPSPLPH
CCCCCCCCCCCCCCC
52.1427097102
38PhosphorylationRLTPSRPSPLPHRSR
CCCCCCCCCCCCCCC
37.6527097102
45Asymmetric dimethylarginineSPLPHRSRGGGGGPR
CCCCCCCCCCCCCCC
47.97-
45MethylationSPLPHRSRGGGGGPR
CCCCCCCCCCCCCCC
47.97-
52Asymmetric dimethylarginineRGGGGGPRGGARASP
CCCCCCCCCCCCCCC
60.49-
52MethylationRGGGGGPRGGARASP
CCCCCCCCCCCCCCC
60.49-
58PhosphorylationPRGGARASPATQPPP
CCCCCCCCCCCCCCC
14.9829779826
61PhosphorylationGARASPATQPPPLLP
CCCCCCCCCCCCCCC
45.0227097102
70PhosphorylationPPPLLPPSNPGPDAT
CCCCCCCCCCCCCCE
54.4327097102
77PhosphorylationSNPGPDATVVGSAPT
CCCCCCCEEECCCCC
24.0927097102
81PhosphorylationPDATVVGSAPTPLLP
CCCEEECCCCCCCCC
21.3325575281
84PhosphorylationTVVGSAPTPLLPPSA
EEECCCCCCCCCCCC
26.70-
96AcetylationPSATAAAKMEPENKY
CCCCHHHHCCCCHHC
38.7822902405
113PhosphorylationELMAEKDSLDPSFTH
HHHHCCCCCCCHHHH
45.82-
137PhosphorylationEKIQKGESKKDDEEN
HHHHCCCCCCCCCCC
54.3928432305
150PhosphorylationENYLDLFSHKNMKLK
CCHHHHHHHCCCCCH
40.6323984901
165AcetylationERVLIPVKQYPKFNF
HEEEEEHHHCCCCCE
38.4713582855
169AcetylationIPVKQYPKFNFVGKI
EEHHHCCCCCEEHHH
48.2622902405
175AcetylationPKFNFVGKILGPQGN
CCCCEEHHHHCCCCH
29.4722902405
183PhosphorylationILGPQGNTIKRLQEE
HHCCCCHHHHHHHHH
34.4023984901
202PhosphorylationISVLGKGSMRDKAKE
EEEECCCHHHHHHHH
17.7123984901
282MethylationNGVPEPSRGRGVSVR
CCCCCCCCCCCCCCC
49.93-
284MethylationVPEPSRGRGVSVRGR
CCCCCCCCCCCCCCC
41.03-
291MethylationRGVSVRGRGAAPPPP
CCCCCCCCCCCCCCC
22.48-
304Asymmetric dimethylargininePPPVPRGRGVGPPRG
CCCCCCCCCCCCCCC
37.59-
304MethylationPPPVPRGRGVGPPRG
CCCCCCCCCCCCCCC
37.59-
310MethylationGRGVGPPRGALVRGT
CCCCCCCCCCEECCC
46.26-
315MethylationPPRGALVRGTPVRGS
CCCCCEECCCCCCCC
44.08-
320MethylationLVRGTPVRGSITRGA
EECCCCCCCCEECCC
34.05-
325MethylationPVRGSITRGATVTRG
CCCCCEECCCEEECC
30.9513582883
331Asymmetric dimethylarginineTRGATVTRGVPPPPT
ECCCEEECCCCCCCC
39.51-
331MethylationTRGATVTRGVPPPPT
ECCCEEECCCCCCCC
39.5126494635
340MethylationVPPPPTVRGAPTPRA
CCCCCCCCCCCCCCC
37.73-
346MethylationVRGAPTPRARTAGIQ
CCCCCCCCCCCCCCC
38.90-
387PhosphorylationYEGYEGYYSQSQGES
CCCCCCCCCCCCCCC
15.87-
390PhosphorylationYEGYYSQSQGESEYY
CCCCCCCCCCCCEEE
33.92-
435PhosphorylationARPVKGAYREHPYGR
CCCCCCCCCCCCCCC
25.79-
440PhosphorylationGAYREHPYGRY----
CCCCCCCCCCC----
19.01-
443PhosphorylationREHPYGRY-------
CCCCCCCC-------
20.67-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
84TPhosphorylationKinaseMAPK1P63086
Uniprot
435YPhosphorylationKinasePTK6-Uniprot
440YPhosphorylationKinasePTK6-Uniprot
443YPhosphorylationKinasePTK6-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KHDR1_RAT !!

Disease-associated PTM Sites based on SAP

* 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 KHDR1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCAB2_RATKcnab2physical
15062979

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KHDR1_RAT

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Related Literatures of Post-Translational Modification

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