HNRH2_HUMAN - dbPTM
HNRH2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRH2_HUMAN
UniProt AC P55795
Protein Name Heterogeneous nuclear ribonucleoprotein H2
Gene Name HNRNPH2
Organism Homo sapiens (Human).
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. Binds poly(RG)..
Protein Sequence MMLSTEGREGFVVKVRGLPWSCSADEVMRFFSDCKIQNGTSGIRFIYTREGRPSGEAFVELESEEEVKLALKKDRETMGHRYVEVFKSNSVEMDWVLKHTGPNSPDTANDGFVRLRGLPFGCSKEEIVQFFSGLEIVPNGMTLPVDFQGRSTGEAFVQFASQEIAEKALKKHKERIGHRYIEIFKSSRAEVRTHYDPPRKLMAMQRPGPYDRPGAGRGYNSIGRGAGFERMRRGAYGGGYGGYDDYGGYNDGYGFGSDRFGRDLNYCFSGMSDHRYGDGGSSFQSTTGHCVHMRGLPYRATENDIYNFFSPLNPMRVHIEIGPDGRVTGEADVEFATHEDAVAAMAKDKANMQHRYVELFLNSTAGTSGGAYDHSYVELFLNSTAGASGGAYGSQMMGGMGLSNQSSYGGPASQQLSGGYGGGYGGQSSMSGYDQVLQENSSDYQSNLA
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-------MMLSTEGR
-------CCCCCCCC		5.7122223895
2Acetylation------MMLSTEGRE
------CCCCCCCCC		3.99-
4Phosphorylation----MMLSTEGREGF
----CCCCCCCCCEE		13.4028857561
5Phosphorylation---MMLSTEGREGFV
---CCCCCCCCCEEE		38.2028857561
14SumoylationGREGFVVKVRGLPWS
CCCEEEEEEECEECC		22.40-
14AcetylationGREGFVVKVRGLPWS
CCCEEEEEEECEECC		22.4026051181
14SumoylationGREGFVVKVRGLPWS
CCCEEEEEEECEECC		22.40-
14UbiquitinationGREGFVVKVRGLPWS
CCCEEEEEEECEECC		22.40-
21PhosphorylationKVRGLPWSCSADEVM
EEECEECCCCHHHHH		9.0328857561
22GlutathionylationVRGLPWSCSADEVMR
EECEECCCCHHHHHH		3.2522555962
23PhosphorylationRGLPWSCSADEVMRF
ECEECCCCHHHHHHH		32.9929507054
35UbiquitinationMRFFSDCKIQNGTSG
HHHHHCCEEECCCCC		52.9321890473
35SumoylationMRFFSDCKIQNGTSG
HHHHHCCEEECCCCC		52.93-
35AcetylationMRFFSDCKIQNGTSG
HHHHHCCEEECCCCC		52.9326051181
35SumoylationMRFFSDCKIQNGTSG
HHHHHCCEEECCCCC		52.9328112733
35UbiquitinationMRFFSDCKIQNGTSG
HHHHHCCEEECCCCC		52.9321890473
40PhosphorylationDCKIQNGTSGIRFIY
CCEEECCCCCEEEEE		31.1822210691
47PhosphorylationTSGIRFIYTREGRPS
CCCEEEEEEECCCCC		9.3122210691
48PhosphorylationSGIRFIYTREGRPSG
CCEEEEEEECCCCCC		19.8922210691
54PhosphorylationYTREGRPSGEAFVEL
EEECCCCCCCEEEEE		48.1523186163
63PhosphorylationEAFVELESEEEVKLA
CEEEEECCHHHHHHH		64.0325849741
72SumoylationEEVKLALKKDRETMG
HHHHHHHHHCHHHHC		47.20-
72UbiquitinationEEVKLALKKDRETMG
HHHHHHHHHCHHHHC		47.20-
73UbiquitinationEVKLALKKDRETMGH
HHHHHHHHCHHHHCC		63.97-
81MethylationDRETMGHRYVEVFKS
CHHHHCCEEEEEHHC		31.31-
87UbiquitinationHRYVEVFKSNSVEMD
CEEEEEHHCCCEEEE		54.63-
88PhosphorylationRYVEVFKSNSVEMDW
EEEEEHHCCCEEEEE		23.9128450419
90PhosphorylationVEVFKSNSVEMDWVL
EEEHHCCCEEEEEEE		26.9225159151
98"N6,N6-dimethyllysine"VEMDWVLKHTGPNSP
EEEEEEEECCCCCCC		29.51-
98MethylationVEMDWVLKHTGPNSP
EEEEEEEECCCCCCC		29.51-
98SumoylationVEMDWVLKHTGPNSP
EEEEEEEECCCCCCC		29.51-
98UbiquitinationVEMDWVLKHTGPNSP
EEEEEEEECCCCCCC		29.51-
100PhosphorylationMDWVLKHTGPNSPDT
EEEEEECCCCCCCCC		53.3925159151
104PhosphorylationLKHTGPNSPDTANDG
EECCCCCCCCCCCCC		27.5623927012
107PhosphorylationTGPNSPDTANDGFVR
CCCCCCCCCCCCCEE		30.6422167270
114MethylationTANDGFVRLRGLPFG
CCCCCCEEECCCCCC		19.19-
123PhosphorylationRGLPFGCSKEEIVQF
CCCCCCCCHHHHHHH		43.4022777824
151PhosphorylationPVDFQGRSTGEAFVQ
CCCCCCCCHHHHHHH		47.8118669648
152PhosphorylationVDFQGRSTGEAFVQF
CCCCCCCHHHHHHHH		37.3730087585
161PhosphorylationEAFVQFASQEIAEKA
HHHHHHHHHHHHHHH		29.6328450419
167AcetylationASQEIAEKALKKHKE
HHHHHHHHHHHHHHH		50.4268905
167UbiquitinationASQEIAEKALKKHKE
HHHHHHHHHHHHHHH		50.4220639865
170UbiquitinationEIAEKALKKHKERIG
HHHHHHHHHHHHHHC		58.66-
171UbiquitinationIAEKALKKHKERIGH
HHHHHHHHHHHHHCH		61.84-
180PhosphorylationKERIGHRYIEIFKSS
HHHHCHHHHHHHHHC		9.3820068231
185SumoylationHRYIEIFKSSRAEVR
HHHHHHHHHCCCCHH		53.86-
185AcetylationHRYIEIFKSSRAEVR
HHHHHHHHHCCCCHH		53.8621689993
185MethylationHRYIEIFKSSRAEVR
HHHHHHHHHCCCCHH		53.8621689993
185SumoylationHRYIEIFKSSRAEVR
HHHHHHHHHCCCCHH		53.86-
185UbiquitinationHRYIEIFKSSRAEVR
HHHHHHHHHCCCCHH		53.8621890473
186PhosphorylationRYIEIFKSSRAEVRT
HHHHHHHHCCCCHHH		17.8220068231
187PhosphorylationYIEIFKSSRAEVRTH
HHHHHHHCCCCHHHC		35.7820068231
193PhosphorylationSSRAEVRTHYDPPRK
HCCCCHHHCCCCCHH		29.9328796482
195PhosphorylationRAEVRTHYDPPRKLM
CCCHHHCCCCCHHHH		29.5428796482
199MethylationRTHYDPPRKLMAMQR
HHCCCCCHHHHHCCC		50.56-
200UbiquitinationTHYDPPRKLMAMQRP
HCCCCCHHHHHCCCC		48.68-
206MethylationRKLMAMQRPGPYDRP
HHHHHCCCCCCCCCC		25.6718961493
210PhosphorylationAMQRPGPYDRPGAGR
HCCCCCCCCCCCCCC		30.4222461510
212DimethylationQRPGPYDRPGAGRGY
CCCCCCCCCCCCCCC		26.21-
212MethylationQRPGPYDRPGAGRGY
CCCCCCCCCCCCCCC		26.2118961503
217DimethylationYDRPGAGRGYNSIGR
CCCCCCCCCCCCCCC		43.84-
217MethylationYDRPGAGRGYNSIGR
CCCCCCCCCCCCCCC		43.8424396149
219PhosphorylationRPGAGRGYNSIGRGA
CCCCCCCCCCCCCCC		12.36-
221PhosphorylationGAGRGYNSIGRGAGF
CCCCCCCCCCCCCCH		20.2430576142
224DimethylationRGYNSIGRGAGFERM
CCCCCCCCCCCHHHH		30.07-
224MethylationRGYNSIGRGAGFERM
CCCCCCCCCCCHHHH		30.0724383137
230DimethylationGRGAGFERMRRGAYG
CCCCCHHHHHCCCCC		22.96-
230MethylationGRGAGFERMRRGAYG
CCCCCHHHHHCCCCC		22.9618960601
232MethylationGAGFERMRRGAYGGG
CCCHHHHHCCCCCCC		39.85115479171
233DimethylationAGFERMRRGAYGGGY
CCHHHHHCCCCCCCC		25.42-
233MethylationAGFERMRRGAYGGGY
CCHHHHHCCCCCCCC		25.4212018901
236PhosphorylationERMRRGAYGGGYGGY
HHHHCCCCCCCCCCC		21.0820090780
240PhosphorylationRGAYGGGYGGYDDYG
CCCCCCCCCCCCCCC		15.6220090780
243PhosphorylationYGGGYGGYDDYGGYN
CCCCCCCCCCCCCCC		10.9820090780
246PhosphorylationGYGGYDDYGGYNDGY
CCCCCCCCCCCCCCC		15.0020090780
249PhosphorylationGYDDYGGYNDGYGFG
CCCCCCCCCCCCCCC		13.0120090780
253PhosphorylationYGGYNDGYGFGSDRF
CCCCCCCCCCCCCCC		16.4920090780
257PhosphorylationNDGYGFGSDRFGRDL
CCCCCCCCCCCCCCC		24.29-
259MethylationGYGFGSDRFGRDLNY
CCCCCCCCCCCCCCC		37.3082954989
266PhosphorylationRFGRDLNYCFSGMSD
CCCCCCCCCCCCCCC		11.3621945579
267GlutathionylationFGRDLNYCFSGMSDH
CCCCCCCCCCCCCCC		1.8122555962
269PhosphorylationRDLNYCFSGMSDHRY
CCCCCCCCCCCCCCC		29.9921945579
272PhosphorylationNYCFSGMSDHRYGDG
CCCCCCCCCCCCCCC		33.5223401153
276PhosphorylationSGMSDHRYGDGGSSF
CCCCCCCCCCCCCCC		19.0227251275
281PhosphorylationHRYGDGGSSFQSTTG
CCCCCCCCCCCCCCC		33.2428450419
282PhosphorylationRYGDGGSSFQSTTGH
CCCCCCCCCCCCCCC		30.4923401153
285PhosphorylationDGGSSFQSTTGHCVH
CCCCCCCCCCCCCEE		26.4028450419
286PhosphorylationGGSSFQSTTGHCVHM
CCCCCCCCCCCCEEE		26.4728450419
287PhosphorylationGSSFQSTTGHCVHMR
CCCCCCCCCCCEEEC		30.1228450419
290GlutathionylationFQSTTGHCVHMRGLP
CCCCCCCCEEECCCC		2.0822555962
294MethylationTGHCVHMRGLPYRAT
CCCCEEECCCCCCCC		28.72115479179
298PhosphorylationVHMRGLPYRATENDI
EEECCCCCCCCCCCC		20.2320090780
301PhosphorylationRGLPYRATENDIYNF
CCCCCCCCCCCCHHC		26.7323403867
306PhosphorylationRATENDIYNFFSPLN
CCCCCCCHHCCCCCC		14.5828102081
310PhosphorylationNDIYNFFSPLNPMRV
CCCHHCCCCCCCCEE		25.0822617229
315SulfoxidationFFSPLNPMRVHIEIG
CCCCCCCCEEEEEEC		7.3228183972
328PhosphorylationIGPDGRVTGEADVEF
ECCCCCCCEECCEEE		28.13-
349UbiquitinationVAAMAKDKANMQHRY
HHHHHHHHHHCCHHH		40.7421890473
375PhosphorylationSGGAYDHSYVELFLN
CCCCCCCCEEEEHHC		28.1624275569
376PhosphorylationGGAYDHSYVELFLNS
CCCCCCCEEEEHHCC		8.43-
441PhosphorylationDQVLQENSSDYQSNL
HHHHHHCCCHHHHHC		24.67-
444PhosphorylationLQENSSDYQSNLA--
HHHCCCHHHHHCC--		18.7822468782
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
104SPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HNRH2_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 HNRH2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAX_HUMANMAXphysical
22939629
SERPH_HUMANSERPINH1physical
22939629
RU1C_HUMANSNRPCphysical
22365833
RBM10_HUMANRBM10physical
22365833
SF01_HUMANSF1physical
22365833
RBM39_HUMANRBM39physical
22365833
ILF3_HUMANILF3physical
22365833
ROA0_HUMANHNRNPA0physical
22365833
PRP8_HUMANPRPF8physical
22365833
PRP31_HUMANPRPF31physical
22365833
PQBP1_HUMANPQBP1physical
22365833
WDR83_HUMANWDR83physical
22365833
DDX5_HUMANDDX5physical
22365833
HNRL1_HUMANHNRNPUL1physical
22365833
RBM4_HUMANRBM4physical
22365833
HNRH2_HUMANHNRNPH2physical
22365833
RACK1_HUMANGNB2L1physical
22365833
QKI_HUMANQKIphysical
22365833
RFOX2_HUMANRBFOX2physical
22365833
ANM6_HUMANPRMT6physical
23455924
TEKT1_HUMANTEKT1physical
25416956
MSI2H_HUMANMSI2physical
25416956
HNRH1_HUMANHNRNPH1physical
26344197
PDCD6_HUMANPDCD6physical
26344197
SF01_HUMANSF1physical
26344197
LYST_HUMANLYSTphysical
26496610
DDX1_HUMANDDX1physical
26496610
ROA2_HUMANHNRNPA2B1physical
26496610
HNRPD_HUMANHNRNPDphysical
26496610
HNRPF_HUMANHNRNPFphysical
26496610
HNRH3_HUMANHNRNPH3physical
26496610
HNRPK_HUMANHNRNPKphysical
26496610
MOV10_HUMANMOV10physical
26496610
HNRPM_HUMANHNRNPMphysical
26496610
PLOD1_HUMANPLOD1physical
26496610
PLOD2_HUMANPLOD2physical
26496610
PCP_HUMANPRCPphysical
26496610
P5CR1_HUMANPYCR1physical
26496610
TNK1_HUMANTNK1physical
26496610
PLOD3_HUMANPLOD3physical
26496610
ABC3B_HUMANAPOBEC3Bphysical
26496610
HNRPQ_HUMANSYNCRIPphysical
26496610
FASTK_HUMANFASTKphysical
26496610
ROA0_HUMANHNRNPA0physical
26496610
F120A_HUMANFAM120Aphysical
26496610
TADBP_HUMANTARDBPphysical
26496610
RUSC1_HUMANRUSC1physical
26496610
EPC2_HUMANEPC2physical
26496610
RBMX_HUMANRBMXphysical
26496610
PKN3_HUMANPKN3physical
26496610
ZSWM5_HUMANZSWIM5physical
26496610
QSER1_HUMANQSER1physical
26496610
TIRR_HUMANNUDT16L1physical
26496610
MAK16_HUMANMAK16physical
26496610
ROA3_HUMANHNRNPA3physical
26496610
HNRL2_HUMANHNRNPUL2physical
26496610
RB12B_HUMANRBM12Bphysical
26496610
PLOD1_HUMANPLOD1physical
28514442
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 HNRH2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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-310, 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-310, AND MASSSPECTROMETRY.
"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-104 AND SER-310, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND THR-107, ANDMASS SPECTROMETRY.
"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-104, AND MASSSPECTROMETRY.

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