HNRL2_MOUSE - dbPTM
HNRL2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRL2_MOUSE
UniProt AC Q00PI9
Protein Name Heterogeneous nuclear ribonucleoprotein U-like protein 2
Gene Name Hnrnpul2
Organism Mus musculus (Mouse).
Sequence Length 745
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MEVKRLKVTELRSELQRRGLDSRGLKMDLAQRLQEALDAEMLEDEAGVGGAGPGGACKAEPRPVAASGGGPGGDEEEEDDDEEEDEEALLEDEDEEPPPAQALGQAAQPPPEPPETSAMEAESEASDTPAEATAGSGGVNGGEEHDNGKGEEDGPEERSGDETPGSEAPGDKAVEEQGDDQDSEKSKPAGSDGERRGVKRQRDEKDEHGRAYYEFREEAYHSRSKSPPPPEEEAKDEEEDQTLVNLDTYTSDLHFQISKDRYGGQPLFSEKFPTLWSGARSTYGVTKGKVCFEAKVTQNLPMKEGCTEVSLLRVGWSVDFSCSQLGEDEFSYGFDGRGLKAENGQFEEFGQTFGENDVIGCFANFETEEVELSFSKNGEDLGVAFRISKESLADRALLPHVLCKNCVVELNFGQKEEPFFPPPEEFVFIHAVPVEERVRTAVPPKTIEECEVILMVGLPGSGKTQWALKYAKDNPERRYNVLGAETVLTQMRMKGLEEPEMDPKSRDLLVQQASQCLSKLVQIASRSKRNFILDQCNVYNSGQRRKLLLFKTFSRKVVVVVPNEEDWKRRLELRKEVEGDDVPESIMLEMKANFSLPEKCDYMDEVTYGELEKEEAQPIVTKYKEEARKLLPPSEKRTNRRNNRNKRNRQNRSRGQGYVGGQRRGYDNRAYGQQYWGQSGNRGGYRNFYDRYRGDYERFYSRDYEYNRYRDYYRQYNRDWQNYYYHHQQDRDRYYRNYYGYQGYR
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
26AcetylationGLDSRGLKMDLAQRL
CCCHHCCCCHHHHHH
32.9422826441
159PhosphorylationEDGPEERSGDETPGS
CCCCCCCCCCCCCCC
54.6027087446
163PhosphorylationEERSGDETPGSEAPG
CCCCCCCCCCCCCCC
37.3825521595
166PhosphorylationSGDETPGSEAPGDKA
CCCCCCCCCCCCCHH
31.6125521595
183PhosphorylationEQGDDQDSEKSKPAG
HCCCCCCCCCCCCCC
41.0925521595
185UbiquitinationGDDQDSEKSKPAGSD
CCCCCCCCCCCCCCH
68.6727667366
186PhosphorylationDDQDSEKSKPAGSDG
CCCCCCCCCCCCCHH
39.5627087446
191PhosphorylationEKSKPAGSDGERRGV
CCCCCCCCHHHCCCC
44.5427087446
212PhosphorylationKDEHGRAYYEFREEA
CCHHHCHHHHHHHHH
11.3623375375
222PhosphorylationFREEAYHSRSKSPPP
HHHHHHHCCCCCCCC
26.1023375375
224PhosphorylationEEAYHSRSKSPPPPE
HHHHHCCCCCCCCCH
40.2625521595
226PhosphorylationAYHSRSKSPPPPEEE
HHHCCCCCCCCCHHH
43.8327087446
242PhosphorylationKDEEEDQTLVNLDTY
CCHHHHCEEEEHHHH
45.0223335269
248PhosphorylationQTLVNLDTYTSDLHF
CEEEEHHHHCCCEEE
31.6825159016
249PhosphorylationTLVNLDTYTSDLHFQ
EEEEHHHHCCCEEEE
12.1525159016
250PhosphorylationLVNLDTYTSDLHFQI
EEEHHHHCCCEEEEE
20.1825159016
251PhosphorylationVNLDTYTSDLHFQIS
EEHHHHCCCEEEEEE
27.9725159016
258PhosphorylationSDLHFQISKDRYGGQ
CCEEEEEECCCCCCC
20.0925159016
261MethylationHFQISKDRYGGQPLF
EEEEECCCCCCCCCC
35.4130987679
269PhosphorylationYGGQPLFSEKFPTLW
CCCCCCCCCCCCCCC
47.7826824392
271UbiquitinationGQPLFSEKFPTLWSG
CCCCCCCCCCCCCCC
56.2822790023
271UbiquitinationGQPLFSEKFPTLWSG
CCCCCCCCCCCCCCC
56.2822790023
287UbiquitinationRSTYGVTKGKVCFEA
CCCCCCCCCEEEEEE
55.0927667366
303AcetylationVTQNLPMKEGCTEVS
ECCCCCCCCCCEEEE
49.3622826441
306S-palmitoylationNLPMKEGCTEVSLLR
CCCCCCCCEEEEEEE
2.8428526873
388PhosphorylationLGVAFRISKESLADR
CEEEEEECHHHHHHH
26.56-
440PhosphorylationPVEERVRTAVPPKTI
EHHHHHHCCCCCCCH
29.2018779572
469UbiquitinationGKTQWALKYAKDNPE
CHHHHHHHHHCCCHH
35.1022790023
469UbiquitinationGKTQWALKYAKDNPE
CHHHHHHHHHCCCHH
35.1022790023
479PhosphorylationKDNPERRYNVLGAET
CCCHHHCHHHCCHHH
18.8224759943
486PhosphorylationYNVLGAETVLTQMRM
HHHCCHHHHHHHHHH
21.9321659604
489PhosphorylationLGAETVLTQMRMKGL
CCHHHHHHHHHHCCC
18.9124759943
504UbiquitinationEEPEMDPKSRDLLVQ
CCCCCCHHHHHHHHH
54.5927667366
519UbiquitinationQASQCLSKLVQIASR
HHHHHHHHHHHHHHH
39.46-
541PhosphorylationDQCNVYNSGQRRKLL
CCCCCCCCCCCEEEE
20.72-
551UbiquitinationRRKLLLFKTFSRKVV
CEEEEEEEECCCEEE
48.9422790023
551UbiquitinationRRKLLLFKTFSRKVV
CEEEEEEEECCCEEE
48.9422790023
568UbiquitinationVPNEEDWKRRLELRK
CCCHHHHHHHHHHHH
39.7122790023
568UbiquitinationVPNEEDWKRRLELRK
CCCHHHHHHHHHHHH
39.7122790023
599UbiquitinationANFSLPEKCDYMDEV
HCCCCCCCCCCCCCC
30.3922790023
599UbiquitinationANFSLPEKCDYMDEV
HCCCCCCCCCCCCCC
30.3922790023
622UbiquitinationEAQPIVTKYKEEARK
HCCCCHHHHHHHHHH
43.3522790023
622UbiquitinationEAQPIVTKYKEEARK
HCCCCHHHHHHHHHH
43.3522790023
634PhosphorylationARKLLPPSEKRTNRR
HHHHCCCCHHHHCHH
54.53-
636UbiquitinationKLLPPSEKRTNRRNN
HHCCCCHHHHCHHCC
69.7122790023
636UbiquitinationKLLPPSEKRTNRRNN
HHCCCCHHHHCHHCC
69.7122790023
653PhosphorylationKRNRQNRSRGQGYVG
HHHHHHHHCCCCCCC
48.6025521595
654DimethylationRNRQNRSRGQGYVGG
HHHHHHHCCCCCCCC
37.91-
654MethylationRNRQNRSRGQGYVGG
HHHHHHHCCCCCCCC
37.9124129315
669MethylationQRRGYDNRAYGQQYW
CCCCCCCCCHHCCCC
26.7054556763
682DimethylationYWGQSGNRGGYRNFY
CCCCCCCCCCCCCHH
43.36-
682MethylationYWGQSGNRGGYRNFY
CCCCCCCCCCCCCHH
43.3624129315
686DimethylationSGNRGGYRNFYDRYR
CCCCCCCCCHHHHHC
30.01-
686MethylationSGNRGGYRNFYDRYR
CCCCCCCCCHHHHHC
30.0112019371
693MethylationRNFYDRYRGDYERFY
CCHHHHHCCCHHHHH
32.1916186091
701PhosphorylationGDYERFYSRDYEYNR
CCHHHHHCCCCCHHH
18.9025367039
704PhosphorylationERFYSRDYEYNRYRD
HHHHCCCCCHHHHHH
21.1425367039
718MethylationDYYRQYNRDWQNYYY
HHHHHHCCCHHHHHH
41.4354556771
736MethylationQDRDRYYRNYYGYQG
HHHHHHHHHHCCCCC
18.7524129315
741PhosphorylationYYRNYYGYQGYR---
HHHHHCCCCCCC---
5.22-
745MethylationYYGYQGYR-------
HCCCCCCC-------
47.0624129315

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 HNRL2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HNRL2_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 HNRL2_MOUSE !!

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

Oops, there are no PPI records of HNRL2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HNRL2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-186, ANDMASS SPECTROMETRY.

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