HNRH1_MOUSE - dbPTM
HNRH1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRH1_MOUSE
UniProt AC O35737
Protein Name Heterogeneous nuclear ribonucleoprotein H
Gene Name Hnrnph1
Organism Mus musculus (Mouse).
Sequence Length 449
Subcellular Localization Nucleus, nucleoplasm.
Protein Description This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA alternative splicing regulation. Inhibits, together with CUGBP1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Binds to the IR RNA. Binds poly(RG) (By similarity)..
Protein Sequence MMLGAEGGEGFVVKVRGLPWSCSADEVQRFFSDCKIQNGAQGIRFIYTREGRPSGEAFVELESEDEVKLALKKDRETMGHRYVEVFKSNNVEMDWVLKHTGPNSPDTANDGFVRLRGLPFGCSKEEIVQFFSGLEIVPNGITLPVDFQGRSTGEAFVQFASQEIAEKALKKHKERIGHRYIEIFKSSRAEVRTHYDPPRKLMAMQRPGPYDRPGAGRGYNSIGRGAGFERMRRGAYGGGYGGYDDYNGYNDGYGFGSDRFGRDLNYCFSGMSDHRYGDGGSTFQSTTGHCVHMRGLPYRATENDIYNFFSPLNPVRVHIEIGPDGRVTGEADVEFATHEDAVAAMSKDKANMQHRYVELFLNSTAGASGGAYEHRYVELFLNSTAGASGGAYGSQMMGGMGLSNQSSYGGPASQQLSGGYGGGYGGQSSMSGYDQVLQENSSDFQSNIA
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
1Acetylation-------MMLGAEGG
-------CCCCCCCC		4.52-
2Acetylation------MMLGAEGGE
------CCCCCCCCC		4.80-
21PhosphorylationKVRGLPWSCSADEVQ
EEECCCCCCCHHHHH		9.0325521595
22S-nitrosocysteineVRGLPWSCSADEVQR
EECCCCCCCHHHHHH		3.25-
22S-nitrosylationVRGLPWSCSADEVQR
EECCCCCCCHHHHHH		3.2520925432
22GlutathionylationVRGLPWSCSADEVQR
EECCCCCCCHHHHHH		3.2524333276
23PhosphorylationRGLPWSCSADEVQRF
ECCCCCCCHHHHHHH		32.9930635358
35UbiquitinationQRFFSDCKIQNGAQG
HHHHHCCEECCCCCE		52.93-
47PhosphorylationAQGIRFIYTREGRPS
CCEEEEEEEECCCCC		9.31-
54PhosphorylationYTREGRPSGEAFVEL
EEECCCCCCCEEEEE		48.1528833060
63PhosphorylationEAFVELESEDEVKLA
CEEEEECCHHHHEEE		64.0725521595
77PhosphorylationALKKDRETMGHRYVE
EEHHCHHHHCCEEEE		29.37-
100PhosphorylationMDWVLKHTGPNSPDT
EEEEEEECCCCCCCC		53.3924925903
104PhosphorylationLKHTGPNSPDTANDG
EEECCCCCCCCCCCC		27.5624925903
107PhosphorylationTGPNSPDTANDGFVR
CCCCCCCCCCCCCEE		30.6424925903
161PhosphorylationEAFVQFASQEIAEKA
HHHHHHHHHHHHHHH		29.6323684622
167UbiquitinationASQEIAEKALKKHKE
HHHHHHHHHHHHHHH		50.42-
167AcetylationASQEIAEKALKKHKE
HHHHHHHHHHHHHHH		50.4222826441
180PhosphorylationKERIGHRYIEIFKSS
HHHHCHHHHHHHHHC		9.38-
185AcetylationHRYIEIFKSSRAEVR
HHHHHHHHHCCCCHH		53.8623806337
186PhosphorylationRYIEIFKSSRAEVRT
HHHHHHHHCCCCHHH		17.82-
187PhosphorylationYIEIFKSSRAEVRTH
HHHHHHHCCCCHHHC		35.78-
212MethylationQRPGPYDRPGAGRGY
CCCCCCCCCCCCCCC		26.2118961561
212DimethylationQRPGPYDRPGAGRGY
CCCCCCCCCCCCCCC		26.21-
217DimethylationYDRPGAGRGYNSIGR
CCCCCCCCCCCCCCC		43.84-
217MethylationYDRPGAGRGYNSIGR
CCCCCCCCCCCCCCC		43.8425056657
224DimethylationRGYNSIGRGAGFERM
CCCCCCCCCCCHHHH		30.07-
224MethylationRGYNSIGRGAGFERM
CCCCCCCCCCCHHHH		30.0725056661
230DimethylationGRGAGFERMRRGAYG
CCCCCHHHHHCCCCC		22.96-
230MethylationGRGAGFERMRRGAYG
CCCCCHHHHHCCCCC		22.9618960651
233MethylationAGFERMRRGAYGGGY
CCHHHHHCCCCCCCC		25.4224129315
243PhosphorylationYGGGYGGYDDYNGYN
CCCCCCCCCCCCCCC		10.9818563927
246PhosphorylationGYGGYDDYNGYNDGY
CCCCCCCCCCCCCCC		13.9518563927
249PhosphorylationGYDDYNGYNDGYGFG
CCCCCCCCCCCCCCC		13.3718563927
259MethylationGYGFGSDRFGRDLNY
CCCCCCCCCCCCCCC		37.3030759961
262MethylationFGSDRFGRDLNYCFS
CCCCCCCCCCCCCCC		42.4030759955
266PhosphorylationRFGRDLNYCFSGMSD
CCCCCCCCCCCCCCC		11.3625159016
267GlutathionylationFGRDLNYCFSGMSDH
CCCCCCCCCCCCCCC		1.8124333276
269PhosphorylationRDLNYCFSGMSDHRY
CCCCCCCCCCCCCCC		29.9928066266
272PhosphorylationNYCFSGMSDHRYGDG
CCCCCCCCCCCCCCC		33.5225159016
281PhosphorylationHRYGDGGSTFQSTTG
CCCCCCCCCCCCCCC		31.4227841257
290S-nitrosylationFQSTTGHCVHMRGLP
CCCCCCCCEEECCCC		2.0820925432
290S-nitrosocysteineFQSTTGHCVHMRGLP
CCCCCCCCEEECCCC		2.08-
301PhosphorylationRGLPYRATENDIYNF
CCCCCCCCCCCCHHC		26.7326239621
306PhosphorylationRATENDIYNFFSPLN
CCCCCCCHHCCCCCC		14.5826239621
310PhosphorylationNDIYNFFSPLNPVRV
CCCHHCCCCCCCEEE		25.0824925903
349AcetylationVAAMSKDKANMQHRY
HHHHCCCCHHCCHHH		45.4523806337
364PhosphorylationVELFLNSTAGASGGA
HHHHHHCCCCCCCCC		28.21-
368PhosphorylationLNSTAGASGGAYEHR
HHCCCCCCCCCCHHE		36.5227600695
384PhosphorylationVELFLNSTAGASGGA
EEEEEECCCCCCCCH		28.21-
388PhosphorylationLNSTAGASGGAYGSQ
EECCCCCCCCHHHCC		36.52-
392PhosphorylationAGASGGAYGSQMMGG
CCCCCCHHHCCCCCC		22.15-
394PhosphorylationASGGAYGSQMMGGMG
CCCCHHHCCCCCCCC		11.39-
403PhosphorylationMMGGMGLSNQSSYGG
CCCCCCCCCCCCCCC		27.39-
406PhosphorylationGMGLSNQSSYGGPAS
CCCCCCCCCCCCCHH		29.76-
407PhosphorylationMGLSNQSSYGGPASQ
CCCCCCCCCCCCHHH		20.31-
408PhosphorylationGLSNQSSYGGPASQQ
CCCCCCCCCCCHHHC		31.20-
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
104SPhosphorylationKinaseMAPK1P63085
GPS
104SPhosphorylationKinaseMAPK14P47811
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HNRH1_MOUSE !!
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 HNRH1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLOD1_HUMANPLOD1physical
20360068
MEP50_HUMANWDR77physical
20360068
HNRH1_HUMANHNRNPH1physical
20360068
ANM5_HUMANPRMT5physical
20360068
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HNRH1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.

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