dbPTM

KHDR1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KHDR1_MOUSE
UniProt AC	Q60749
Protein Name	KH domain-containing, RNA-binding, signal transduction-associated protein 1
Gene Name	Khdrbs1 {ECO:0000312\|MGI:MGI:893579}
Organism	Mus musculus (Mouse).
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). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (By similarity). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner. 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. [PubMed: 12478298]
Protein Sequence	MQRRDDPASRLTRSSGRSCSKDPSGAHPSVRLTPSRPSPLPHRPRGGGGGPRGGARASPATQPPPLLPPSTPGPDATVVGSAPTPLLPPSATAAVKMEPENKYLPELMAEKDSLDPSFTHAMQLLSVEIEKIQKGESKKDDEENYLDLFSHKNMKLKERVLIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKGGDPKYAHLNMDLHVFIEVFGPPCEAYALMAHAMEEVKKFLVPDMMDDICQEQFLELSYLNGVPEPSRGRGVSVRGRGAAPPPPPVPRGRGVGPPRGALVRGTPVRGSITRGATVTRGVPPPPTVRGAPTPRARTAGIQRIPLPPTPAPETYEDYGYDDTYAEQSYEGYEGYYSQSQGESEYYDYGHGELQDSYEAYGQDDWNGTRPSLKAPPARPVKGAYREHPYGRY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	QRRDDPASRLTRSSG CCCCCHHHHHHHCCC	32.96	18779572
14	Phosphorylation	PASRLTRSSGRSCSK HHHHHHHCCCCCCCC	31.73	25777480
15	Phosphorylation	ASRLTRSSGRSCSKD HHHHHHCCCCCCCCC	34.63	25777480
18	Phosphorylation	LTRSSGRSCSKDPSG HHHCCCCCCCCCCCC	26.69	26824392
19	S-nitrosocysteine	TRSSGRSCSKDPSGA HHCCCCCCCCCCCCC	5.89	-
19	Glutathionylation	TRSSGRSCSKDPSGA HHCCCCCCCCCCCCC	5.89	24333276
19	S-nitrosylation	TRSSGRSCSKDPSGA HHCCCCCCCCCCCCC	5.89	21278135
19	S-palmitoylation	TRSSGRSCSKDPSGA HHCCCCCCCCCCCCC	5.89	26165157
20	Phosphorylation	RSSGRSCSKDPSGAH HCCCCCCCCCCCCCC	41.14	26824392
21	Acetylation	SSGRSCSKDPSGAHP CCCCCCCCCCCCCCC	77.36	23806337
21	Malonylation	SSGRSCSKDPSGAHP CCCCCCCCCCCCCCC	77.36	26320211
24	Phosphorylation	RSCSKDPSGAHPSVR CCCCCCCCCCCCCCC	59.76	25619855
29	Phosphorylation	DPSGAHPSVRLTPSR CCCCCCCCCCCCCCC	15.25	25619855
33	Phosphorylation	AHPSVRLTPSRPSPL CCCCCCCCCCCCCCC	14.51	26824392
35	Phosphorylation	PSVRLTPSRPSPLPH CCCCCCCCCCCCCCC	52.14	21743459
36	Methylation	SVRLTPSRPSPLPHR CCCCCCCCCCCCCCC	36.60	16187431
38	Phosphorylation	RLTPSRPSPLPHRPR CCCCCCCCCCCCCCC	37.65	21743459
43	Methylation	RPSPLPHRPRGGGGG CCCCCCCCCCCCCCC	22.22	18958399
45	Methylation	SPLPHRPRGGGGGPR CCCCCCCCCCCCCCC	57.24	16187111
45	Asymmetric dimethylarginine	SPLPHRPRGGGGGPR CCCCCCCCCCCCCCC	57.24	-
52	Asymmetric dimethylarginine	RGGGGGPRGGARASP CCCCCCCCCCCCCCC	60.49	-
52	Methylation	RGGGGGPRGGARASP CCCCCCCCCCCCCCC	60.49	16187117
56	Methylation	GGPRGGARASPATQP CCCCCCCCCCCCCCC	38.58	18958409
58	Phosphorylation	PRGGARASPATQPPP CCCCCCCCCCCCCCC	14.98	27087446
61	Phosphorylation	GARASPATQPPPLLP CCCCCCCCCCCCCCC	45.02	22942356
70	Phosphorylation	PPPLLPPSTPGPDAT CCCCCCCCCCCCCCE	45.34	25159016
71	Phosphorylation	PPLLPPSTPGPDATV CCCCCCCCCCCCCEE	37.73	25159016
77	Phosphorylation	STPGPDATVVGSAPT CCCCCCCEEECCCCC	24.09	25159016
81	Phosphorylation	PDATVVGSAPTPLLP CCCEEECCCCCCCCC	21.33	24453211
84	Phosphorylation	TVVGSAPTPLLPPSA EEECCCCCCCCCCCC	26.70	25619855
90	Phosphorylation	PTPLLPPSATAAVKM CCCCCCCCCCEEEEC	35.99	25159016
92	Phosphorylation	PLLPPSATAAVKMEP CCCCCCCCEEEECCC	21.35	25159016
96	Acetylation	PSATAAVKMEPENKY CCCCEEEECCCCCCC	32.59	23236377
102	Ubiquitination	VKMEPENKYLPELMA EECCCCCCCHHHHHH	46.64	22790023
102	Acetylation	VKMEPENKYLPELMA EECCCCCCCHHHHHH	46.64	23236377
113	Phosphorylation	ELMAEKDSLDPSFTH HHHHCCCCCCCHHHH	45.82	22817900
137	Phosphorylation	EKIQKGESKKDDEEN HHHHCCCCCCCCCCC	54.39	21082442
150	Phosphorylation	ENYLDLFSHKNMKLK CCHHHHHHHCCCCCH	40.63	-
152	Ubiquitination	YLDLFSHKNMKLKER HHHHHHHCCCCCHHE	58.50	22790023
165	Ubiquitination	ERVLIPVKQYPKFNF HEEEEEHHHCCCCCE	38.47	22790023
169	Ubiquitination	IPVKQYPKFNFVGKI EEHHHCCCCCEEHHH	48.26	22790023
175	Ubiquitination	PKFNFVGKILGPQGN CCCCEEHHHHCCCCH	29.47	22790023
175	Acetylation	PKFNFVGKILGPQGN CCCCEEHHHHCCCCH	29.47	23236377
183	Phosphorylation	ILGPQGNTIKRLQEE HHCCCCHHHHHHHHH	34.40	29176673
185	Ubiquitination	GPQGNTIKRLQEETG CCCCHHHHHHHHHHC	45.04	22790023
194	Ubiquitination	LQEETGAKISVLGKG HHHHHCCCEEEECCC	36.54	22790023
200	Ubiquitination	AKISVLGKGSMRDKA CCEEEECCCHHHHHH	43.59	27667366
202	Phosphorylation	ISVLGKGSMRDKAKE EEEECCCHHHHHHHH	17.71	29176673
282	Methylation	NGVPEPSRGRGVSVR CCCCCCCCCCCCCCC	49.93	24129315
284	Dimethylation	VPEPSRGRGVSVRGR CCCCCCCCCCCCCCC	41.03	-
284	Methylation	VPEPSRGRGVSVRGR CCCCCCCCCCCCCCC	41.03	24129315
289	Methylation	RGRGVSVRGRGAAPP CCCCCCCCCCCCCCC	22.91	54559027
289	Dimethylation	RGRGVSVRGRGAAPP CCCCCCCCCCCCCCC	22.91	-
291	Dimethylation	RGVSVRGRGAAPPPP CCCCCCCCCCCCCCC	22.48	-
291	Methylation	RGVSVRGRGAAPPPP CCCCCCCCCCCCCCC	22.48	24129315
302	Dimethylation	PPPPPVPRGRGVGPP CCCCCCCCCCCCCCC	47.91	-
302	Methylation	PPPPPVPRGRGVGPP CCCCCCCCCCCCCCC	47.91	54559011
304	Methylation	PPPVPRGRGVGPPRG CCCCCCCCCCCCCCC	37.59	25057783
304	Asymmetric dimethylarginine	PPPVPRGRGVGPPRG CCCCCCCCCCCCCCC	37.59	-
310	Dimethylation	GRGVGPPRGALVRGT CCCCCCCCCCEECCC	46.26	-
310	Methylation	GRGVGPPRGALVRGT CCCCCCCCCCEECCC	46.26	137995
315	Methylation	PPRGALVRGTPVRGS CCCCCEECCCCCCCC	44.08	137999
315	Dimethylation	PPRGALVRGTPVRGS CCCCCEECCCCCCCC	44.08	-
317	Phosphorylation	RGALVRGTPVRGSIT CCCEECCCCCCCCEE	14.19	20139300
320	Methylation	LVRGTPVRGSITRGA EECCCCCCCCEECCC	34.05	138003
320	Dimethylation	LVRGTPVRGSITRGA EECCCCCCCCEECCC	34.05	-
322	Phosphorylation	RGTPVRGSITRGATV CCCCCCCCEECCCEE	15.38	28507225
325	Methylation	PVRGSITRGATVTRG CCCCCEECCCEEECC	30.95	136697
325	Dimethylation	PVRGSITRGATVTRG CCCCCEECCCEEECC	30.95	-
331	Asymmetric dimethylarginine	TRGATVTRGVPPPPT ECCCEEECCCCCCCC	39.51	-
331	Methylation	TRGATVTRGVPPPPT ECCCEEECCCCCCCC	39.51	24129315
340	Dimethylation	VPPPPTVRGAPTPRA CCCCCCCCCCCCCCC	37.73	-
340	Methylation	VPPPPTVRGAPTPRA CCCCCCCCCCCCCCC	37.73	136701
346	Dimethylation	VRGAPTPRARTAGIQ CCCCCCCCCCCCCCC	38.90	-
346	Methylation	VRGAPTPRARTAGIQ CCCCCCCCCCCCCCC	38.90	54559019
348	Dimethylation	GAPTPRARTAGIQRI CCCCCCCCCCCCCCC	26.79	-
348	Methylation	GAPTPRARTAGIQRI CCCCCCCCCCCCCCC	26.79	54559035
387	Phosphorylation	YEGYEGYYSQSQGES CCCCCCCCCCCCCCC	15.87	-
390	Phosphorylation	YEGYYSQSQGESEYY CCCCCCCCCCCCEEE	33.92	-
396	Phosphorylation	QSQGESEYYDYGHGE CCCCCCEEECCCCCC	15.77	22817900
397	Phosphorylation	SQGESEYYDYGHGEL CCCCCEEECCCCCCC	9.91	22817900
432	Ubiquitination	APPARPVKGAYREHP CCCCCCCCCCCCCCC	40.27	22790023
435	Phosphorylation	ARPVKGAYREHPYGR CCCCCCCCCCCCCCC	25.79	22817900
440	Phosphorylation	GAYREHPYGRY---- CCCCCCCCCCC----	19.01	16179349
443	Phosphorylation	REHPYGRY------- CCCCCCCC-------	20.67	16179349

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
58	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
58	S	Phosphorylation	Kinase	MK01	P63085	PhosphoELM
71	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
71	T	Phosphorylation	Kinase	MK01	P63085	PhosphoELM
84	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
84	T	Phosphorylation	Kinase	MK01	P63085	PhosphoELM
435	Y	Phosphorylation	Kinase	PTK6	Q13882	GPS
435	Y	Phosphorylation	Kinase	PTK6	Q64434	Uniprot
440	Y	Phosphorylation	Kinase	PTK6	Q13882	GPS
440	Y	Phosphorylation	Kinase	PTK6	Q64434	Uniprot
443	Y	Phosphorylation	Kinase	PTK6	Q13882	GPS
443	Y	Phosphorylation	Kinase	PTK6	Q64434	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
58	S	Phosphorylation	12478298
Phosphorylation by MAPK1 at Ser-58, Thr-71 and Thr-84 regulates CD44 alternative splicing by promoting CD44 exon v5 inclusion.
71	T	Phosphorylation	12478298
Phosphorylation by MAPK1 at Ser-58, Thr-71 and Thr-84 regulates CD44 alternative splicing by promoting CD44 exon v5 inclusion.
84	T	Phosphorylation	12478298
Phosphorylation by MAPK1 at Ser-58, Thr-71 and Thr-84 regulates CD44 alternative splicing by promoting CD44 exon v5 inclusion.

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KHDR1_MOUSE	Khdrbs1	physical	20211142
T2EB_MOUSE	Gtf2e2	physical	20211142
RBM39_MOUSE	Rbm39	physical	20211142
NCOA5_MOUSE	Ncoa5	physical	20211142
RIPK1_MOUSE	Ripk1	physical	21620750
RASA1_HUMAN	RASA1	physical	1374686

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KHDR1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A target for Src in mitosis."; Fumagalli S., Totty N.F., Hsuan J.J., Courtneidge S.A.; Nature 368:871-874(1994). Cited for: PROTEIN SEQUENCE OF 57-71; 103-131; 139-152; 158-165; 222-230; 273-282AND 433-443, FUNCTION, PHOSPHORYLATION AT SER-113, AND INTERACTIONWITH SRC.	7512695 [Abstract]

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