HNRL2_HUMAN - dbPTM
HNRL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRL2_HUMAN
UniProt AC Q1KMD3
Protein Name Heterogeneous nuclear ribonucleoprotein U-like protein 2
Gene Name HNRNPUL2
Organism Homo sapiens (Human).
Sequence Length 747
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MEVKRLKVTELRSELQRRGLDSRGLKVDLAQRLQEALDAEMLEDEAGGGGAGPGGACKAEPRPVAASGGGPGGDEEEDEEEEEEDEEALLEDEDEEPPPAQALGQAAQPPPEPPEAAAMEAAAEPDASEKPAEATAGSGGVNGGEEQGLGKREEDEPEERSGDETPGSEVPGDKAAEEQGDDQDSEKSKPAGSDGERRGVKRQRDEKDEHGRAYYEFREEAYHSRSKSPLPPEEEAKDEEEDQTLVNLDTYTSDLHFQVSKDRYGGQPLFSEKFPTLWSGARSTYGVTKGKVCFEAKVTQNLPMKEGCTEVSLLRVGWSVDFSRPQLGEDEFSYGFDGRGLKAENGQFEEFGQTFGENDVIGCFANFETEEVELSFSKNGEDLGVAFWISKDSLADRALLPHVLCKNCVVELNFGQKEEPFFPPPEEFVFIHAVPVEERVRTAVPPKTIEECEVILMVGLPGSGKTQWALKYAKENPEKRYNVLGAETVLNQMRMKGLEEPEMDPKSRDLLVQQASQCLSKLVQIASRTKRNFILDQCNVYNSGQRRKLLLFKTFSRKVVVVVPNEEDWKKRLELRKEVEGDDVPESIMLEMKANFSLPEKCDYMDEVTYGELEKEEAQPIVTKYKEEARKLLPPSEKRTNRRNNRNKRNRQNRSRGQGYVGGQRRGYDNRAYGQQYWGQPGNRGGYRNFYDRYRGDYDRFYGRDYEYNRYRDYYRQYNRDWQSYYYHHPQDRDRYYRNYYGYQGYR
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
4Acetylation----MEVKRLKVTEL
----CCCEECCHHHH		38.4119827539
72-Hydroxyisobutyrylation-MEVKRLKVTELRSE
-CCCEECCHHHHHHH		51.66-
7Acetylation-MEVKRLKVTELRSE
-CCCEECCHHHHHHH		51.6619827549
7Malonylation-MEVKRLKVTELRSE
-CCCEECCHHHHHHH		51.6626320211
23MethylationQRRGLDSRGLKVDLA
HHCCCCCCCCCCHHH		54.88115479489
26UbiquitinationGLDSRGLKVDLAQRL
CCCCCCCCCHHHHHH		36.2129967540
41SulfoxidationQEALDAEMLEDEAGG
HHHHHHHHHCCCCCC		5.4921406390
57GlutathionylationGAGPGGACKAEPRPV
CCCCCCCCCCCCCCC		4.9222555962
58AcetylationAGPGGACKAEPRPVA
CCCCCCCCCCCCCCC		56.0725953088
58UbiquitinationAGPGGACKAEPRPVA
CCCCCCCCCCCCCCC		56.0724816145
67PhosphorylationEPRPVAASGGGPGGD
CCCCCCCCCCCCCCC		28.3815302935
138PhosphorylationPAEATAGSGGVNGGE
CCCCCCCCCCCCCCC		29.8830576142
160MethylationEEDEPEERSGDETPG
CCCCCCCCCCCCCCC		44.25115479481
161PhosphorylationEDEPEERSGDETPGS
CCCCCCCCCCCCCCC		54.6019664994
165PhosphorylationEERSGDETPGSEVPG
CCCCCCCCCCCCCCC		37.3829255136
168PhosphorylationSGDETPGSEVPGDKA
CCCCCCCCCCCCHHH		36.3029255136
174AcetylationGSEVPGDKAAEEQGD
CCCCCCHHHHHHHCC		56.2526051181
174UbiquitinationGSEVPGDKAAEEQGD
CCCCCCHHHHHHHCC		56.2522817900
185PhosphorylationEQGDDQDSEKSKPAG
HHCCCCCCCCCCCCC		41.0929255136
187UbiquitinationGDDQDSEKSKPAGSD
CCCCCCCCCCCCCCH		68.6721906983
188PhosphorylationDDQDSEKSKPAGSDG
CCCCCCCCCCCCCHH		39.5629255136
189UbiquitinationDQDSEKSKPAGSDGE
CCCCCCCCCCCCHHH		50.3722817900
193PhosphorylationEKSKPAGSDGERRGV
CCCCCCCCHHHCCCC		44.5423401153
214PhosphorylationKDEHGRAYYEFREEA
CCHHHCHHHHHHHHH		11.36-
215PhosphorylationDEHGRAYYEFREEAY
CHHHCHHHHHHHHHH		13.9627259358
222PhosphorylationYEFREEAYHSRSKSP
HHHHHHHHHCCCCCC		12.0117360941
224PhosphorylationFREEAYHSRSKSPLP
HHHHHHHCCCCCCCC		26.1026074081
226PhosphorylationEEAYHSRSKSPLPPE
HHHHHCCCCCCCCCH		40.2622167270
228PhosphorylationAYHSRSKSPLPPEEE
HHHCCCCCCCCCHHH		32.6829255136
244PhosphorylationKDEEEDQTLVNLDTY
CCHHHCCEEEEHHHC		45.0230278072
250PhosphorylationQTLVNLDTYTSDLHF
CEEEEHHHCCCCEEE		31.6823927012
251PhosphorylationTLVNLDTYTSDLHFQ
EEEEHHHCCCCEEEE		12.1523927012
252PhosphorylationLVNLDTYTSDLHFQV
EEEHHHCCCCEEEEE		20.1823927012
253PhosphorylationVNLDTYTSDLHFQVS
EEHHHCCCCEEEEEE		27.9723927012
260PhosphorylationSDLHFQVSKDRYGGQ
CCEEEEEECCCCCCC		20.3223927012
261UbiquitinationDLHFQVSKDRYGGQP
CEEEEEECCCCCCCC		47.5729967540
264PhosphorylationFQVSKDRYGGQPLFS
EEEECCCCCCCCCCC		35.4221406692
271PhosphorylationYGGQPLFSEKFPTLW
CCCCCCCCCCCCCCC		47.7828978645
273AcetylationGQPLFSEKFPTLWSG
CCCCCCCCCCCCCCC		56.2825825284
273UbiquitinationGQPLFSEKFPTLWSG
CCCCCCCCCCCCCCC		56.2821890473
283PhosphorylationTLWSGARSTYGVTKG
CCCCCCCCCCCCCCC		26.0025332170
284PhosphorylationLWSGARSTYGVTKGK
CCCCCCCCCCCCCCE		20.8128985074
285PhosphorylationWSGARSTYGVTKGKV
CCCCCCCCCCCCCEE		15.7328985074
288PhosphorylationARSTYGVTKGKVCFE
CCCCCCCCCCEEEEE		29.7125332170
289UbiquitinationRSTYGVTKGKVCFEA
CCCCCCCCCEEEEEE		55.0933845483
2912-HydroxyisobutyrylationTYGVTKGKVCFEAKV
CCCCCCCEEEEEEEE		37.07-
291UbiquitinationTYGVTKGKVCFEAKV
CCCCCCCEEEEEEEE		37.0733845483
297AcetylationGKVCFEAKVTQNLPM
CEEEEEEEECCCCCC		38.3226051181
297UbiquitinationGKVCFEAKVTQNLPM
CEEEEEEEECCCCCC		38.3232015554
304SulfoxidationKVTQNLPMKEGCTEV
EECCCCCCCCCCEEE		7.5121406390
305AcetylationVTQNLPMKEGCTEVS
ECCCCCCCCCCEEEE		49.3625953088
305UbiquitinationVTQNLPMKEGCTEVS
ECCCCCCCCCCEEEE		49.3633845483
308GlutathionylationNLPMKEGCTEVSLLR
CCCCCCCCEEEEEEE		2.8422555962
319O-linked_GlycosylationSLLRVGWSVDFSRPQ
EEEEEEEEEECCCCC		13.0923301498
323O-linked_GlycosylationVGWSVDFSRPQLGED
EEEEEECCCCCCCCC		38.2923301498
342SumoylationGFDGRGLKAENGQFE
CCCCCCCCCCCCCHH		57.38-
375PhosphorylationETEEVELSFSKNGED
CCEEEEEEECCCCCE		17.6124719451
397MethylationSKDSLADRALLPHVL
ECCHHHHHHHHHHHH		22.87115479473
406UbiquitinationLLPHVLCKNCVVELN
HHHHHHCCCCEEEEC		49.5822817900
442PhosphorylationPVEERVRTAVPPKTI
EHHHHHHCCCCCCCH		29.2028348404
452GlutathionylationPPKTIEECEVILMVG
CCCCHHHCEEEEEEE		3.0822555962
471AcetylationGKTQWALKYAKENPE
CHHHHHHHHHHHCHH		35.1019608861
471UbiquitinationGKTQWALKYAKENPE
CHHHHHHHHHHHCHH		35.1022817900
474UbiquitinationQWALKYAKENPEKRY
HHHHHHHHHCHHHHH		55.7422817900
481PhosphorylationKENPEKRYNVLGAET
HHCHHHHHHHCCHHH		22.23-
494MethylationETVLNQMRMKGLEEP
HHHHHHHHHCCCCCC		17.56115479497
496UbiquitinationVLNQMRMKGLEEPEM
HHHHHHHCCCCCCCC		50.4024816145
5062-HydroxyisobutyrylationEEPEMDPKSRDLLVQ
CCCCCCHHHHHHHHH		54.59-
506UbiquitinationEEPEMDPKSRDLLVQ
CCCCCCHHHHHHHHH		54.5929967540
516PhosphorylationDLLVQQASQCLSKLV
HHHHHHHHHHHHHHH		19.6526699800
520PhosphorylationQQASQCLSKLVQIAS
HHHHHHHHHHHHHHH		31.4126699800
521AcetylationQASQCLSKLVQIASR
HHHHHHHHHHHHHHH		39.4626051181
521UbiquitinationQASQCLSKLVQIASR
HHHHHHHHHHHHHHH		39.4632015554
531MethylationQIASRTKRNFILDQC
HHHHHCCCCCHHHCC		42.55-
541PhosphorylationILDQCNVYNSGQRRK
HHHCCCCCCCCCCEE		6.9328152594
543PhosphorylationDQCNVYNSGQRRKLL
HCCCCCCCCCCEEEE		20.7221815630
548AcetylationYNSGQRRKLLLFKTF
CCCCCCEEEEEEEEC		45.7526051181
548UbiquitinationYNSGQRRKLLLFKTF
CCCCCCEEEEEEEEC		45.7523000965
553AcetylationRRKLLLFKTFSRKVV
CEEEEEEEECCCEEE		48.9425953088
553UbiquitinationRRKLLLFKTFSRKVV
CEEEEEEEECCCEEE		48.9423000965
558UbiquitinationLFKTFSRKVVVVVPN
EEEECCCEEEEECCC		37.8823000965
5702-HydroxyisobutyrylationVPNEEDWKKRLELRK
CCCHHHHHHHHHHHH		40.10-
570AcetylationVPNEEDWKKRLELRK
CCCHHHHHHHHHHHH		40.1090693
570UbiquitinationVPNEEDWKKRLELRK
CCCHHHHHHHHHHHH		40.1032015554
571AcetylationPNEEDWKKRLELRKE
CCHHHHHHHHHHHHH		58.94130803
587PhosphorylationEGDDVPESIMLEMKA
CCCCCCHHHHHHHHH		13.7628348404
593UbiquitinationESIMLEMKANFSLPE
HHHHHHHHHCCCCCC		30.7032015554
597PhosphorylationLEMKANFSLPEKCDY
HHHHHCCCCCCCCCC		42.7025159151
601UbiquitinationANFSLPEKCDYMDEV
HCCCCCCCCCCCCCC		30.3932015554
602GlutathionylationNFSLPEKCDYMDEVT
CCCCCCCCCCCCCCC		4.2822555962
604PhosphorylationSLPEKCDYMDEVTYG
CCCCCCCCCCCCCHH		18.8829449344
609PhosphorylationCDYMDEVTYGELEKE
CCCCCCCCHHHCCHH		24.6229449344
610PhosphorylationDYMDEVTYGELEKEE
CCCCCCCHHHCCHHH		17.4922817900
615AcetylationVTYGELEKEEAQPIV
CCHHHCCHHHCCCCH		73.7626051181
6242-HydroxyisobutyrylationEAQPIVTKYKEEARK
HCCCCHHHHHHHHHH		43.35-
624SumoylationEAQPIVTKYKEEARK
HCCCCHHHHHHHHHH		43.35-
624UbiquitinationEAQPIVTKYKEEARK
HCCCCHHHHHHHHHH		43.3521906983
625PhosphorylationAQPIVTKYKEEARKL
CCCCHHHHHHHHHHH		17.80-
631UbiquitinationKYKEEARKLLPPSEK
HHHHHHHHHCCCCHH		62.5232142685
636PhosphorylationARKLLPPSEKRTNRR
HHHHCCCCHHHHCHH		54.5320068231
638UbiquitinationKLLPPSEKRTNRRNN
HHCCCCHHHHCHHCC		69.7127667366
655PhosphorylationKRNRQNRSRGQGYVG
HHHHHHHHCCCCCCC		48.6023401153
656DimethylationRNRQNRSRGQGYVGG
HHHHHHHCCCCCCCC		37.91-
656MethylationRNRQNRSRGQGYVGG
HHHHHHHCCCCCCCC		37.9112017949
660PhosphorylationNRSRGQGYVGGQRRG
HHHCCCCCCCCCCCC		6.5023403867
666MethylationGYVGGQRRGYDNRAY
CCCCCCCCCCCCCCC		39.8954556751
671MethylationQRRGYDNRAYGQQYW
CCCCCCCCCCCCCCC		26.7054556759
684DimethylationYWGQPGNRGGYRNFY
CCCCCCCCCCCCCHH		45.92-
684MethylationYWGQPGNRGGYRNFY
CCCCCCCCCCCCCHH		45.9212019353
688DimethylationPGNRGGYRNFYDRYR
CCCCCCCCCHHHHHC		30.01-
688MethylationPGNRGGYRNFYDRYR
CCCCCCCCCHHHHHC		30.0112019365
693MethylationGYRNFYDRYRGDYDR
CCCCHHHHHCCCHHH		16.2154556775
695MethylationRNFYDRYRGDYDRFY
CCHHHHHCCCHHHHC		32.1916186097
698PhosphorylationYDRYRGDYDRFYGRD
HHHHCCCHHHHCCCC		16.31-
700MethylationRYRGDYDRFYGRDYE
HHCCCHHHHCCCCCC		22.0680702167
704MethylationDYDRFYGRDYEYNRY
CHHHHCCCCCCHHHH		31.7783108513
706PhosphorylationDRFYGRDYEYNRYRD
HHHCCCCCCHHHHHH		20.9627273156
708PhosphorylationFYGRDYEYNRYRDYY
HCCCCCCHHHHHHHH		9.9428796482
716MethylationNRYRDYYRQYNRDWQ
HHHHHHHHHHCCCHH		26.6981449357
720MethylationDYYRQYNRDWQSYYY
HHHHHHCCCHHHHHC		41.4354556767
725PhosphorylationYNRDWQSYYYHHPQD
HCCCHHHHHCCCCCC		7.9217360941
726PhosphorylationNRDWQSYYYHHPQDR
CCCHHHHHCCCCCCH		11.1120090780
727PhosphorylationRDWQSYYYHHPQDRD
CCHHHHHCCCCCCHH		5.8520090780
738MethylationQDRDRYYRNYYGYQG
CCHHHHHHCCCCCCC		18.7524129315
740PhosphorylationRDRYYRNYYGYQGYR
HHHHHHCCCCCCCCC		6.8320090780
741PhosphorylationDRYYRNYYGYQGYR-
HHHHHCCCCCCCCC-		16.9525348954
743PhosphorylationYYRNYYGYQGYR---
HHHCCCCCCCCC---		5.2220090780
746PhosphorylationNYYGYQGYR------
CCCCCCCCC------		9.5320090780
747MethylationYYGYQGYR-------
CCCCCCCC-------		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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HNRL2_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF2B3_HUMANIGF2BP3physical
22939629
TMOD3_HUMANTMOD3physical
22939629
RB11B_HUMANRAB11Bphysical
22939629
PM34_HUMANSLC25A17physical
22939629
IL7RA_HUMANIL7Rphysical
23151878
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HNRL2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-471, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; THR-165 ANDSER-168, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-161 ANDSER-228, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; THR-165; SER-168AND SER-226, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161 AND SER-228, ANDMASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-188 ANDSER-228, AND MASS SPECTROMETRY.

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