HNRPL_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HNRPL_MOUSE
• UniProt AC: Q8R081
• Protein Name: Heterogeneous nuclear ribonucleoprotein L
• Gene Name: Hnrnpl
• Organism: Mus musculus (Mouse).
• Sequence Length: 586
• Subcellular Localization: Nucleus, nucleoplasm . Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodies or stress granules.
• Protein Description: Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. [PubMed: 22523384 Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter.]
• Protein Sequence: MSRRLLPRAEKRRRRLEQRQQPDEQLRRAGAMVKMAAAGGGGGGGRYYGGGNEGGRAPKRLKTENAGDQHGGGGGGGSGAAGGGGGENYDDPHKTPASPVVHIRGLIDGVVEADLVEALQEFGPISYVVVMPKKRQALVEFEDVLGACNAVNYAADNQIYIAGHPAFVNYSTSQKISRPGDSDDSRSVNSVLLFTILNPIYSITTDVLYTICNPCGPVQRIVIFRKNGVQAMVEFDSVQSAQRAKASLNGADIYSGCCTLKIEYAKPTRLNVFKNDQDTWDYTNPNLSGQGDPGSNPNKRQRQPPLLGDHPAEYGGPHGGYHSHYHDEGYGPPPPHYEGRRMGPPVGGHRRGPSRYGPQYGHPPPPPPPPDYGPHADSPVLMVYGLDQSKMNCDRVFNVFCLYGNVEKVKFMKSKPGAAMVEMADGYAVDRAITHLNNNFMFGQKMNVCVSKQPAIMPGQSYGLEDGSCSYKDFSESRNNRFSTPEQAAKNRIQHPSNVLHFFNAPLEVTEENFFEICDELGVKRPTSVKVFSGKSERSSSGLLEWDSKSDALETLGFLNHYQMKNPNGPYPYTLKLCFSTAQHAS

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
34	Ubiquitination	RRAGAMVKMAAAGGG HHHHHHHHHHHCCCC	15.10	-
47	Phosphorylation	GGGGGGRYYGGGNEG CCCCCCCCCCCCCCC	15.10	18563927
59	Acetylation	NEGGRAPKRLKTENA CCCCCCCCCCCCCCC	70.18	88741
62	Ubiquitination	GRAPKRLKTENAGDQ CCCCCCCCCCCCCCC	58.80	-
63	Phosphorylation	RAPKRLKTENAGDQH CCCCCCCCCCCCCCC	38.78	29550500
78	Phosphorylation	GGGGGGGSGAAGGGG CCCCCCCCCCCCCCC	28.65	25159016
89	Phosphorylation	GGGGGENYDDPHKTP CCCCCCCCCCCCCCC	19.88	25159016
94	Ubiquitination	ENYDDPHKTPASPVV CCCCCCCCCCCCCEE	62.69	-
95	Phosphorylation	NYDDPHKTPASPVVH CCCCCCCCCCCCEEE	22.51	25159016
98	Phosphorylation	DPHKTPASPVVHIRG CCCCCCCCCEEEHHH	21.30	25159016
148	Glutathionylation	FEDVLGACNAVNYAA HHHHHHHHHHHHHHC	2.97	24333276
177	Phosphorylation	YSTSQKISRPGDSDD CCCCCCCCCCCCCCC	39.18	25159016
182	Phosphorylation	KISRPGDSDDSRSVN CCCCCCCCCCCCCCH	49.59	25521595
185	Phosphorylation	RPGDSDDSRSVNSVL CCCCCCCCCCCHHHH	31.29	25159016
226	Ubiquitination	QRIVIFRKNGVQAMV EEEEEEECCCEEEEE	47.51	-
245	Malonylation	VQSAQRAKASLNGAD HHHHHHHHHHHCCCH	40.47	26320211
257	Glutathionylation	GADIYSGCCTLKIEY CCHHHCCCCEEEEEE	1.00	24333276
257	S-nitrosylation	GADIYSGCCTLKIEY CCHHHCCCCEEEEEE	1.00	22588120
258	S-nitrosocysteine	ADIYSGCCTLKIEYA CHHHCCCCEEEEEEC	5.95	-
258	S-nitrosylation	ADIYSGCCTLKIEYA CHHHCCCCEEEEEEC	5.95	22588120
258	Glutathionylation	ADIYSGCCTLKIEYA CHHHCCCCEEEEEEC	5.95	24333276
264	Phosphorylation	CCTLKIEYAKPTRLN CCEEEEEECCCCEEE	24.33	-
266	Malonylation	TLKIEYAKPTRLNVF EEEEEECCCCEEEEE	46.12	26320211
266	Ubiquitination	TLKIEYAKPTRLNVF EEEEEECCCCEEEEE	46.12	-
266	Acetylation	TLKIEYAKPTRLNVF EEEEEECCCCEEEEE	46.12	-
283	Phosphorylation	DQDTWDYTNPNLSGQ CCCCCCCCCCCCCCC	41.55	-
288	Phosphorylation	DYTNPNLSGQGDPGS CCCCCCCCCCCCCCC	35.39	28066266
295	Phosphorylation	SGQGDPGSNPNKRQR CCCCCCCCCCCCCCC	55.27	28066266
299	Ubiquitination	DPGSNPNKRQRQPPL CCCCCCCCCCCCCCC	51.68	-
321	Phosphorylation	YGGPHGGYHSHYHDE HCCCCCCCCCCCCCC	12.54	22807455
351	Methylation	PPVGGHRRGPSRYGP CCCCCCCCCCCCCCC	56.55	24129315
351	Asymmetric dimethylarginine	PPVGGHRRGPSRYGP CCCCCCCCCCCCCCC	56.55	-
355	Asymmetric dimethylarginine	GHRRGPSRYGPQYGH CCCCCCCCCCCCCCC	43.49	-
355	Methylation	GHRRGPSRYGPQYGH CCCCCCCCCCCCCCC	43.49	24129315
356	Phosphorylation	HRRGPSRYGPQYGHP CCCCCCCCCCCCCCC	37.18	29514104
372	Phosphorylation	PPPPPPDYGPHADSP CCCCCCCCCCCCCCC	38.03	22807455
378	Phosphorylation	DYGPHADSPVLMVYG CCCCCCCCCEEEEEE	20.07	19060867
401	S-palmitoylation	DRVFNVFCLYGNVEK HHHEEEEEEECCEEE	2.20	28526873
401	S-nitrosylation	DRVFNVFCLYGNVEK HHHEEEEEEECCEEE	2.20	20925432
401	S-nitrosocysteine	DRVFNVFCLYGNVEK HHHEEEEEEECCEEE	2.20	-
401	Glutathionylation	DRVFNVFCLYGNVEK HHHEEEEEEECCEEE	2.20	24333276
408	Acetylation	CLYGNVEKVKFMKSK EEECCEEEEEEECCC	46.58	22826441
415	Ubiquitination	KVKFMKSKPGAAMVE EEEEECCCCCCEEEE	41.79	-
449	S-nitrosylation	FGQKMNVCVSKQPAI CCCCEEEEEECCCCC	2.13	21278135
449	Glutathionylation	FGQKMNVCVSKQPAI CCCCEEEEEECCCCC	2.13	24333276
449	S-nitrosocysteine	FGQKMNVCVSKQPAI CCCCEEEEEECCCCC	2.13	-
452	Acetylation	KMNVCVSKQPAIMPG CEEEEEECCCCCCCC	39.65	22826441
469	Glutathionylation	YGLEDGSCSYKDFSE CCCCCCCCCCCCCCH	6.70	24333276
472	Acetylation	EDGSCSYKDFSESRN CCCCCCCCCCCHHHC	35.68	23806337
483	Phosphorylation	ESRNNRFSTPEQAAK HHHCCCCCCHHHHHH	39.55	30635358
484	Phosphorylation	SRNNRFSTPEQAAKN HHCCCCCCHHHHHHH	28.29	30635358
490	Ubiquitination	STPEQAAKNRIQHPS CCHHHHHHHHCCCCH	50.18	-
530	Ubiquitination	VKRPTSVKVFSGKSE CCCCCEEEEECCCCC	37.01	-
533	Phosphorylation	PTSVKVFSGKSERSS CCEEEEECCCCCCCC	48.58	-
535	Acetylation	SVKVFSGKSERSSSG EEEEECCCCCCCCCC	48.20	23806337
536	Phosphorylation	VKVFSGKSERSSSGL EEEECCCCCCCCCCC	41.59	29514104
539	Phosphorylation	FSGKSERSSSGLLEW ECCCCCCCCCCCEEE	25.46	23984901
540	Phosphorylation	SGKSERSSSGLLEWD CCCCCCCCCCCEEEC	34.35	23984901
541	Phosphorylation	GKSERSSSGLLEWDS CCCCCCCCCCEEECC	34.41	30482847
548	Phosphorylation	SGLLEWDSKSDALET CCCEEECCHHHHHHH	34.82	23984901
549	Acetylation	GLLEWDSKSDALETL CCEEECCHHHHHHHH	50.29	23954790
550	Phosphorylation	LLEWDSKSDALETLG CEEECCHHHHHHHHH	31.87	26745281
555	Phosphorylation	SKSDALETLGFLNHY CHHHHHHHHHHCHHC	32.79	23984901
565	Ubiquitination	FLNHYQMKNPNGPYP HCHHCCCCCCCCCCC	54.44	-
571	Phosphorylation	MKNPNGPYPYTLKLC CCCCCCCCCEEEEEE	15.40	-
574	Phosphorylation	PNGPYPYTLKLCFST CCCCCCEEEEEEECC	16.95	29176673
578	S-palmitoylation	YPYTLKLCFSTAQHA CCEEEEEEECCCCCC	2.12	28526873
578	S-nitrosylation	YPYTLKLCFSTAQHA CCEEEEEEECCCCCC	2.12	21278135
578	Glutathionylation	YPYTLKLCFSTAQHA CCEEEEEEECCCCCC	2.12	24333276
578	S-nitrosocysteine	YPYTLKLCFSTAQHA CCEEEEEEECCCCCC	2.12	-
580	Phosphorylation	YTLKLCFSTAQHAS- EEEEEEECCCCCCC-	23.10	29472430
581	Phosphorylation	TLKLCFSTAQHAS-- EEEEEECCCCCCC--	15.30	27600695
586	Phosphorylation	FSTAQHAS------- ECCCCCCC-------	38.33	21082442

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
541	S	Phosphorylation	Kinase	CAMK4	P08414	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
541	S	Phosphorylation	Phosphorylation at Ser-541 by CaMK4 enhances interaction with a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the stress axis-regulated exon (STREX) of the KCNMA1 potassium channel transcripts upon membrane depolarization.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of HNRPL_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of HNRPL_MOUSE !!

Drug and Disease Associations

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