HNRPQ_MOUSE - dbPTM
HNRPQ_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRPQ_MOUSE
UniProt AC Q7TMK9
Protein Name Heterogeneous nuclear ribonucleoprotein Q
Gene Name Syncrip
Organism Mus musculus (Mouse).
Sequence Length 623
Subcellular Localization Nucleus . Nucleus, nucleoplasm . Microsome . Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). Isoforms 1 and 2 are expressed predominantly in the nucleoplasm. According to PubMed:10734137, isoform 2 is
Protein Description Heterogeneous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1 and isoform 2 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences (By similarity). Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself (By similarity). May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (By similarity). Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 2 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins..
Protein Sequence MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGLVAHSDLDERAIEALKEFNEDGALAVLQQFKDSDLSHVQNKSAFLCGVMKTYRQREKQGTKVADSSKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTVEWADPIEDPDPEVMAKVKVLFVRNLANTVTEEILEKSFSQFGKLERVKKLKDYAFIHFDERDGAVKAMEEMNGKDLEGENIEIVFAKPPDQKRKERKAQRQAAKNQMYDDYYYYGPPHMPPPTRGRGRGGRGGYGYPPDYYGYEDYYDYYGYDYHNYRGGYEDPYYGYEDFQVGARGRGGRGARGAAPSRGRGAAPPRGRAGYSQRGGPGSARGVRGARGGAQQQRGRGVRGARGGRGGNVGGKRKADGYNQPDTKRRQTNNQNWGSQPIAQQPLQGGDHSGNYGYKSENQEFYQDTFGQQWK
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
2Acetylation------MATEHVNGN
------CCCCCCCCC		22.99-
81AcetylationLAVLQQFKDSDLSHV
HHHHHHHCCCCCHHH		52.5722826441
96S-nitrosocysteineQNKSAFLCGVMKTYR
CCHHHHHHHHHHHHH		2.89-
96S-nitrosylationQNKSAFLCGVMKTYR
CCHHHHHHHHHHHHH		2.8919101475
100AcetylationAFLCGVMKTYRQREK
HHHHHHHHHHHHHHH		39.7423236377
100MalonylationAFLCGVMKTYRQREK
HHHHHHHHHHHHHHH		39.7426320211
100UbiquitinationAFLCGVMKTYRQREK
HHHHHHHHHHHHHHH		39.74-
125UbiquitinationGPDEAKIKALLERTG
CCCHHHHHHHHHHHC		32.0722790023
131PhosphorylationIKALLERTGYTLDVT
HHHHHHHHCCEEEEC		25.7624759943
138PhosphorylationTGYTLDVTTGQRKYG
HCCEEEECCCCCCCC		25.5224759943
139PhosphorylationGYTLDVTTGQRKYGG
CCEEEECCCCCCCCC		31.0324759943
144PhosphorylationVTTGQRKYGGPPPDS
ECCCCCCCCCCCCCC		29.5122871156
159PhosphorylationVYSGQQPSVGTEIFV
CCCCCCCCCCCEEEE		28.9229514104
162PhosphorylationGQQPSVGTEIFVGKI
CCCCCCCCEEEEECC		24.6122871156
168UbiquitinationGTEIFVGKIPRDLFE
CCEEEEECCCHHHHC		44.2122790023
211GlutathionylationGYAFVTFCTKEAAQE
CEEEEEEECHHHHHH		3.7724333276
221UbiquitinationEAAQEAVKLYNNHEI
HHHHHHHHHHCCCCC		52.9122790023
221AcetylationEAAQEAVKLYNNHEI
HHHHHHHHHHCCCCC		52.91-
230PhosphorylationYNNHEIRSGKHIGVC
HCCCCCCCCCEEEEE		58.8325338131
237GlutathionylationSGKHIGVCISVANNR
CCCEEEEEEEECCCE		1.2924333276
249PhosphorylationNNRLFVGSIPKSKTK
CCEEEECCCCCCCCH		30.3426824392
276PhosphorylationGLTDVILYHQPDDKK
CCCEEEEEECCCCCC		6.3129514104
289S-nitrosocysteineKKKNRGFCFLEYEDH
CCCCCCEEEEEECCH		4.19-
289S-nitrosylationKKKNRGFCFLEYEDH
CCCCCCEEEEEECCH		4.1920925432
289GlutathionylationKKKNRGFCFLEYEDH
CCCCCCEEEEEECCH		4.1924333276
297AcetylationFLEYEDHKTAAQARR
EEEECCHHHHHHHHH		52.7822826441
308PhosphorylationQARRRLMSGKVKVWG
HHHHHHHCCCEEEEE		39.8024719451
336UbiquitinationPDPEVMAKVKVLFVR
CCHHHHHHEEEHHHH		25.2122790023
338UbiquitinationPEVMAKVKVLFVRNL
HHHHHHEEEHHHHCH		32.30-
356UbiquitinationVTEEILEKSFSQFGK
CCHHHHHHHHHHCCC		54.04-
363UbiquitinationKSFSQFGKLERVKKL
HHHHHCCCHHHHHHH		48.7622790023
363AcetylationKSFSQFGKLERVKKL
HHHHHCCCHHHHHHH		48.7622826441
373PhosphorylationRVKKLKDYAFIHFDE
HHHHHCCEEEEEEEC		11.2122817900
432PhosphorylationNQMYDDYYYYGPPHM
HHCCCCCCCCCCCCC		9.3722817900
444Asymmetric dimethylargininePHMPPPTRGRGRGGR
CCCCCCCCCCCCCCC		38.29-
444MethylationPHMPPPTRGRGRGGR
CCCCCCCCCCCCCCC		38.29-
485PhosphorylationRGGYEDPYYGYEDFQ
CCCCCCCCCCCCCCC		23.1122817900
488PhosphorylationYEDPYYGYEDFQVGA
CCCCCCCCCCCCCCC		9.0122817900
496MethylationEDFQVGARGRGGRGA
CCCCCCCCCCCCCCC		29.4324383415
510MethylationARGAAPSRGRGAAPP
CCCCCCCCCCCCCCC		37.46-
510Asymmetric dimethylarginineARGAAPSRGRGAAPP
CCCCCCCCCCCCCCC		37.46-
518Asymmetric dimethylarginineGRGAAPPRGRAGYSQ
CCCCCCCCCCCCCCC		46.28-
518MethylationGRGAAPPRGRAGYSQ
CCCCCCCCCCCCCCC		46.28-
526Asymmetric dimethylarginineGRAGYSQRGGPGSAR
CCCCCCCCCCCCCCC		46.20-
526MethylationGRAGYSQRGGPGSAR
CCCCCCCCCCCCCCC		46.20-
536Asymmetric dimethylargininePGSARGVRGARGGAQ
CCCCCCCCCCCCCCH		35.56-
536MethylationPGSARGVRGARGGAQ
CCCCCCCCCCCCCCH		35.56-
539Asymmetric dimethylarginineARGVRGARGGAQQQR
CCCCCCCCCCCHHCC		47.07-
539MethylationARGVRGARGGAQQQR
CCCCCCCCCCCHHCC		47.07-
587PhosphorylationTNNQNWGSQPIAQQP
CCCCCCCCCCCCCCC		25.1324719451
614PhosphorylationKSENQEFYQDTFGQQ
CCCCCEEHHHCCCCC		12.5325159016
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

Oops, there are no upstream regulatory protein records of HNRPQ_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HNRPQ_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 HNRPQ_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HNRPQ_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HNRPQ_MOUSE

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Related Literatures of Post-Translational Modification

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