HNRPQ_HUMAN - dbPTM
HNRPQ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRPQ_HUMAN
UniProt AC O60506
Protein Name Heterogeneous nuclear ribonucleoprotein Q
Gene Name SYNCRIP
Organism Homo sapiens (Human).
Sequence Length 623
Subcellular Localization Cytoplasm . Microsome . Endoplasmic reticulum. Nucleus . The tyrosine phosphorylated form bound to RNA is found in microsomes (By similarity). Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity).
Isoform 1: Nucleus,
Protein Description Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. 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. 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. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function..
Protein Sequence MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGLVAHSDLDERAIEALKEFNEDGALAVLQQFKDSDLSHVQNKSAFLCGVMKTYRQREKQGTKVADSSKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTVEWADPIEDPDPEVMAKVKVLFVRNLANTVTEEILEKAFSQFGKLERVKKLKDYAFIHFDERDGAVKAMEEMNGKDLEGENIEIVFAKPPDQKRKERKAQRQAAKNQMYDDYYYYGPPHMPPPTRGRGRGGRGGYGYPPDYYGYEDYYDYYGYDYHNYRGGYEDPYYGYEDFQVGARGRGGRGARGAAPSRGRGAAPPRGRAGYSQRGGPGSARGVRGARGGAQQQRGRGVRGARGGRGGNVGGKRKADGYNQPDSKRRQTNNQNWGSQPIAQQPLQGGDHSGNYGYKSENQEFYQDTFGQQWK
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
22.9919413330
13 (in isoform 5)Ubiquitination-45.8421890473
19 (in isoform 5)Ubiquitination-23.7221890473
42AcetylationLPQKVAEKLDEIYVA
CCHHHHHHCCHHHHH
52.0426051181
47PhosphorylationAEKLDEIYVAGLVAH
HHHCCHHHHHHHHHC
5.12-
55PhosphorylationVAGLVAHSDLDERAI
HHHHHHCCCCCHHHH
30.0828348404
66AcetylationERAIEALKEFNEDGA
HHHHHHHHHHCCCCH
68.2726051181
66UbiquitinationERAIEALKEFNEDGA
HHHHHHHHHHCCCCH
68.27-
70 (in isoform 5)Ubiquitination-64.2421890473
81AcetylationLAVLQQFKDSDLSHV
HHHHHHHCCCCCHHH
52.5725825284
81UbiquitinationLAVLQQFKDSDLSHV
HHHHHHHCCCCCHHH
52.5721906983
81 (in isoform 1)Ubiquitination-52.5721890473
81 (in isoform 2)Ubiquitination-52.5721906983
81 (in isoform 3)Ubiquitination-52.5721890473
81 (in isoform 4)Ubiquitination-52.5721906983
91UbiquitinationDLSHVQNKSAFLCGV
CCHHHCCHHHHHHHH
26.52-
92PhosphorylationLSHVQNKSAFLCGVM
CHHHCCHHHHHHHHH
31.6321712546
96GlutathionylationQNKSAFLCGVMKTYR
CCHHHHHHHHHHHHH
2.8922555962
100AcetylationAFLCGVMKTYRQREK
HHHHHHHHHHHHHHH
39.7419608861
100UbiquitinationAFLCGVMKTYRQREK
HHHHHHHHHHHHHHH
39.7419608861
107UbiquitinationKTYRQREKQGTKVAD
HHHHHHHHHCCCCCC
57.10-
110PhosphorylationRQREKQGTKVADSSK
HHHHHHCCCCCCCCC
21.6122817900
111UbiquitinationQREKQGTKVADSSKG
HHHHHCCCCCCCCCC
42.1021906983
111 (in isoform 1)Ubiquitination-42.1021890473
111 (in isoform 2)Ubiquitination-42.1021906983
111 (in isoform 3)Ubiquitination-42.1021890473
111 (in isoform 4)Ubiquitination-42.1021906983
115PhosphorylationQGTKVADSSKGPDEA
HCCCCCCCCCCCCHH
24.9829632367
116PhosphorylationGTKVADSSKGPDEAK
CCCCCCCCCCCCHHH
42.0229632367
117AcetylationTKVADSSKGPDEAKI
CCCCCCCCCCCHHHH
77.6826051181
117UbiquitinationTKVADSSKGPDEAKI
CCCCCCCCCCCHHHH
77.6821906983
117 (in isoform 1)Ubiquitination-77.6821890473
117 (in isoform 2)Ubiquitination-77.6821906983
117 (in isoform 3)Ubiquitination-77.6821890473
117 (in isoform 4)Ubiquitination-77.6821906983
123TrimethylationSKGPDEAKIKALLER
CCCCCHHHHHHHHHH
42.57-
123AcetylationSKGPDEAKIKALLER
CCCCCHHHHHHHHHH
42.5725953088
123MethylationSKGPDEAKIKALLER
CCCCCHHHHHHHHHH
42.57-
123UbiquitinationSKGPDEAKIKALLER
CCCCCHHHHHHHHHH
42.5717370265
123 (in isoform 5)Ubiquitination-42.5721890473
125TrimethylationGPDEAKIKALLERTG
CCCHHHHHHHHHHHC
32.07-
125MethylationGPDEAKIKALLERTG
CCCHHHHHHHHHHHC
32.07-
131PhosphorylationIKALLERTGYTLDVT
HHHHHHHHCCEEEEC
25.7621406692
133PhosphorylationALLERTGYTLDVTTG
HHHHHHCCEEEECCC
11.9721406692
134PhosphorylationLLERTGYTLDVTTGQ
HHHHHCCEEEECCCC
20.1621406692
138PhosphorylationTGYTLDVTTGQRKYG
HCCEEEECCCCCCCC
25.5226074081
139PhosphorylationGYTLDVTTGQRKYGG
CCEEEECCCCCCCCC
31.0326074081
144PhosphorylationVTTGQRKYGGPPPDS
ECCCCCCCCCCCCCC
29.5128152594
151PhosphorylationYGGPPPDSVYSGQQP
CCCCCCCCCCCCCCC
28.8228152594
153PhosphorylationGPPPDSVYSGQQPSV
CCCCCCCCCCCCCCC
15.8428152594
154PhosphorylationPPPDSVYSGQQPSVG
CCCCCCCCCCCCCCC
28.1528152594
159PhosphorylationVYSGQQPSVGTEIFV
CCCCCCCCCCCEEEE
28.9223401153
162PhosphorylationGQQPSVGTEIFVGKI
CCCCCCCCEEEEECC
24.6128464451
168AcetylationGTEIFVGKIPRDLFE
CCEEEEECCCHHHHC
44.2125953088
168SumoylationGTEIFVGKIPRDLFE
CCEEEEECCCHHHHC
44.2128112733
168UbiquitinationGTEIFVGKIPRDLFE
CCEEEEECCCHHHHC
44.2121906983
168 (in isoform 1)Ubiquitination-44.2121890473
168 (in isoform 2)Ubiquitination-44.2121906983
168 (in isoform 3)Ubiquitination-44.2121890473
168 (in isoform 4)Ubiquitination-44.2121906983
184UbiquitinationELVPLFEKAGPIWDL
CCHHHHHHHCCHHEH
51.84-
184 (in isoform 3)Ubiquitination-51.84-
192MethylationAGPIWDLRLMMDPLT
HCCHHEHHHHHCCCC
20.33-
194SulfoxidationPIWDLRLMMDPLTGL
CHHEHHHHHCCCCCC
2.0121406390
205PhosphorylationLTGLNRGYAFVTFCT
CCCCCCCEEEEEEEC
8.1428152594
211S-palmitoylationGYAFVTFCTKEAAQE
CEEEEEEECHHHHHH
3.7729575903
213AcetylationAFVTFCTKEAAQEAV
EEEEEECHHHHHHHH
46.6826051181
213MethylationAFVTFCTKEAAQEAV
EEEEEECHHHHHHHH
46.6823644510
221AcetylationEAAQEAVKLYNNHEI
HHHHHHHHHHCCCCC
52.9119608861
221MalonylationEAAQEAVKLYNNHEI
HHHHHHHHHHCCCCC
52.9126320211
221UbiquitinationEAAQEAVKLYNNHEI
HHHHHHHHHHCCCCC
52.9121890473
221 (in isoform 1)Ubiquitination-52.9121890473
221 (in isoform 2)Ubiquitination-52.9121906983
221 (in isoform 3)Ubiquitination-52.9121890473
221 (in isoform 4)Ubiquitination-52.9121906983
223PhosphorylationAQEAVKLYNNHEIRS
HHHHHHHHCCCCCCC
14.2728152594
232AcetylationNHEIRSGKHIGVCIS
CCCCCCCCEEEEEEE
33.0426051181
238 (in isoform 5)Ubiquitination-3.2721890473
240 (in isoform 5)Ubiquitination-3.1521890473
249PhosphorylationNNRLFVGSIPKSKTK
CCEEEECCCCCCCCH
30.3430266825
253PhosphorylationFVGSIPKSKTKEQIL
EECCCCCCCCHHHHH
39.9623312004
255PhosphorylationGSIPKSKTKEQILEE
CCCCCCCCHHHHHHH
47.0727134283
256AcetylationSIPKSKTKEQILEEF
CCCCCCCHHHHHHHH
51.8926822725
256UbiquitinationSIPKSKTKEQILEEF
CCCCCCCHHHHHHHH
51.89-
258 (in isoform 5)Ubiquitination-47.3121890473
265UbiquitinationQILEEFSKVTEGLTD
HHHHHHHHHHCCCCE
59.50-
265 (in isoform 5)Ubiquitination-59.5021890473
276PhosphorylationGLTDVILYHQPDDKK
CCCEEEEEECCCCCC
6.3128152594
282AcetylationLYHQPDDKKKNRGFC
EEECCCCCCCCCCEE
73.3825953088
282UbiquitinationLYHQPDDKKKNRGFC
EEECCCCCCCCCCEE
73.38-
283AcetylationYHQPDDKKKNRGFCF
EECCCCCCCCCCEEE
63.3725953088
283UbiquitinationYHQPDDKKKNRGFCF
EECCCCCCCCCCEEE
63.37-
284UbiquitinationHQPDDKKKNRGFCFL
ECCCCCCCCCCEEEE
58.58-
286MethylationPDDKKKNRGFCFLEY
CCCCCCCCCEEEEEE
48.74-
288 (in isoform 5)Ubiquitination-2.1021890473
289GlutathionylationKKKNRGFCFLEYEDH
CCCCCCEEEEEECCH
4.1922555962
289S-palmitoylationKKKNRGFCFLEYEDH
CCCCCCEEEEEECCH
4.1929575903
293PhosphorylationRGFCFLEYEDHKTAA
CCEEEEEECCHHHHH
28.8928152594
297AcetylationFLEYEDHKTAAQARR
EEEECCHHHHHHHHH
52.7825953088
297MalonylationFLEYEDHKTAAQARR
EEEECCHHHHHHHHH
52.7826320211
297SumoylationFLEYEDHKTAAQARR
EEEECCHHHHHHHHH
52.78-
297UbiquitinationFLEYEDHKTAAQARR
EEEECCHHHHHHHHH
52.78-
308PhosphorylationQARRRLMSGKVKVWG
HHHHHHHCCCEEEEE
39.8024719451
310UbiquitinationRRRLMSGKVKVWGNV
HHHHHCCCEEEEECE
31.41-
312UbiquitinationRLMSGKVKVWGNVGT
HHHCCCEEEEECEEE
35.44-
321 (in isoform 2)Ubiquitination-36.4621906983
321 (in isoform 4)Ubiquitination-36.4621906983
328AcetylationEWADPIEDPDPEVMA
EECCCCCCCCHHHHH
54.3319608861
328UbiquitinationEWADPIEDPDPEVMA
EECCCCCCCCHHHHH
54.3319608861
328 (in isoform 2)Ubiquitination-54.3321906983
328 (in isoform 4)Ubiquitination-54.3321906983
336UbiquitinationPDPEVMAKVKVLFVR
CCHHHHHHEEEHHHH
25.2121906983
336 (in isoform 1)Ubiquitination-25.2121890473
336 (in isoform 3)Ubiquitination-25.2121890473
338AcetylationPEVMAKVKVLFVRNL
HHHHHHEEEHHHHCH
32.3024707635
338UbiquitinationPEVMAKVKVLFVRNL
HHHHHHEEEHHHHCH
32.3021890473
338 (in isoform 1)Ubiquitination-32.3021890473
338 (in isoform 3)Ubiquitination-32.3021890473
348PhosphorylationFVRNLANTVTEEILE
HHHCHHHHCCHHHHH
24.1723403867
350PhosphorylationRNLANTVTEEILEKA
HCHHHHCCHHHHHHH
26.3423403867
351 (in isoform 2)Ubiquitination-38.4121906983
351 (in isoform 4)Ubiquitination-38.4121906983
356AcetylationVTEEILEKAFSQFGK
CCHHHHHHHHHHCCC
51.8126051181
356UbiquitinationVTEEILEKAFSQFGK
CCHHHHHHHHHHCCC
51.8121906983
356 (in isoform 1)Ubiquitination-51.8121890473
356 (in isoform 3)Ubiquitination-51.8121890473
363AcetylationKAFSQFGKLERVKKL
HHHHHCCCHHHHHHH
48.7619608861
363MalonylationKAFSQFGKLERVKKL
HHHHHCCCHHHHHHH
48.7626320211
363MethylationKAFSQFGKLERVKKL
HHHHHCCCHHHHHHH
48.7622633583
363UbiquitinationKAFSQFGKLERVKKL
HHHHHCCCHHHHHHH
48.7621890473
363 (in isoform 1)Ubiquitination-48.7621890473
363 (in isoform 3)Ubiquitination-48.7621890473
371AcetylationLERVKKLKDYAFIHF
HHHHHHHCCEEEEEE
58.5326051181
371UbiquitinationLERVKKLKDYAFIHF
HHHHHHHCCEEEEEE
58.5321890473
373NitrationRVKKLKDYAFIHFDE
HHHHHCCEEEEEEEC
11.21-
373PhosphorylationRVKKLKDYAFIHFDE
HHHHHCCEEEEEEEC
11.2112601080
381MethylationAFIHFDERDGAVKAM
EEEEEECCCCHHHHH
49.89115485573
386UbiquitinationDERDGAVKAMEEMNG
ECCCCHHHHHHHHCC
41.292190698
386 (in isoform 1)Ubiquitination-41.2921890473
386 (in isoform 3)Ubiquitination-41.2921890473
394UbiquitinationAMEEMNGKDLEGENI
HHHHHCCCCCCCCCE
54.88-
394 (in isoform 3)Ubiquitination-54.88-
407UbiquitinationNIEIVFAKPPDQKRK
CEEEEEECCCCHHHH
45.69-
407 (in isoform 3)Ubiquitination-45.69-
412AcetylationFAKPPDQKRKERKAQ
EECCCCHHHHHHHHH
73.2024431059
412UbiquitinationFAKPPDQKRKERKAQ
EECCCCHHHHHHHHH
73.20-
428PhosphorylationQAAKNQMYDDYYYYG
HHHHHHCCCCCCCCC
8.9026846344
431PhosphorylationKNQMYDDYYYYGPPH
HHHCCCCCCCCCCCC
7.1726846344
432PhosphorylationNQMYDDYYYYGPPHM
HHCCCCCCCCCCCCC
9.3726846344
433PhosphorylationQMYDDYYYYGPPHMP
HCCCCCCCCCCCCCC
8.8426846344
434PhosphorylationMYDDYYYYGPPHMPP
CCCCCCCCCCCCCCC
13.6726846344
443PhosphorylationPPHMPPPTRGRGRGG
CCCCCCCCCCCCCCC
52.0826846344
444Asymmetric dimethylargininePHMPPPTRGRGRGGR
CCCCCCCCCCCCCCC
38.29-
444MethylationPHMPPPTRGRGRGGR
CCCCCCCCCCCCCCC
38.2923455924
446MethylationMPPPTRGRGRGGRGG
CCCCCCCCCCCCCCC
28.4824395445
448MethylationPPTRGRGRGGRGGYG
CCCCCCCCCCCCCCC
42.9324395453
472PhosphorylationDYYDYYGYDYHNYRG
CCCCCCCCCCCCCCC
9.37-
474PhosphorylationYDYYGYDYHNYRGGY
CCCCCCCCCCCCCCC
5.40-
478MethylationGYDYHNYRGGYEDPY
CCCCCCCCCCCCCCC
37.06-
485PhosphorylationRGGYEDPYYGYEDFQ
CCCCCCCCCCCCCCC
23.1122817900
488PhosphorylationYEDPYYGYEDFQVGA
CCCCCCCCCCCCCCC
9.01-
496DimethylationEDFQVGARGRGGRGA
CCCCCCCCCCCCCCC
29.43-
496MethylationEDFQVGARGRGGRGA
CCCCCCCCCCCCCCC
29.4323455924
498DimethylationFQVGARGRGGRGARG
CCCCCCCCCCCCCCC
38.55-
498MethylationFQVGARGRGGRGARG
CCCCCCCCCCCCCCC
38.5524396479
501MethylationGARGRGGRGARGAAP
CCCCCCCCCCCCCCC
38.12115485581
504MethylationGRGGRGARGAAPSRG
CCCCCCCCCCCCCCC
37.80115485589
509PhosphorylationGARGAAPSRGRGAAP
CCCCCCCCCCCCCCC
42.5122817900
510Asymmetric dimethylarginineARGAAPSRGRGAAPP
CCCCCCCCCCCCCCC
37.46-
510MethylationARGAAPSRGRGAAPP
CCCCCCCCCCCCCCC
37.4623455924
518Asymmetric dimethylarginineGRGAAPPRGRAGYSQ
CCCCCCCCCCCCCCC
46.28-
518MethylationGRGAAPPRGRAGYSQ
CCCCCCCCCCCCCCC
46.2823455924
520MethylationGAAPPRGRAGYSQRG
CCCCCCCCCCCCCCC
26.56115485597
524PhosphorylationPRGRAGYSQRGGPGS
CCCCCCCCCCCCCCC
16.6922817900
526Asymmetric dimethylarginineGRAGYSQRGGPGSAR
CCCCCCCCCCCCCCC
46.20-
526MethylationGRAGYSQRGGPGSAR
CCCCCCCCCCCCCCC
46.2023455924
531PhosphorylationSQRGGPGSARGVRGA
CCCCCCCCCCCCCCC
20.2322817900
533MethylationRGGPGSARGVRGARG
CCCCCCCCCCCCCCC
45.9224383427
536Asymmetric dimethylargininePGSARGVRGARGGAQ
CCCCCCCCCCCCCCH
35.56-
536MethylationPGSARGVRGARGGAQ
CCCCCCCCCCCCCCH
35.5623455924
539Asymmetric dimethylarginineARGVRGARGGAQQQR
CCCCCCCCCCCHHCC
47.07-
539MethylationARGVRGARGGAQQQR
CCCCCCCCCCCHHCC
47.0723455924
565MethylationGGNVGGKRKADGYNQ
CCCCCCCCCCCCCCC
42.54-
566AcetylationGNVGGKRKADGYNQP
CCCCCCCCCCCCCCC
55.0819829793
566UbiquitinationGNVGGKRKADGYNQP
CCCCCCCCCCCCCCC
55.08-
570PhosphorylationGKRKADGYNQPDSKR
CCCCCCCCCCCCHHH
15.9228102081
575PhosphorylationDGYNQPDSKRRQTNN
CCCCCCCHHHCCCCC
34.4421815630
576AcetylationGYNQPDSKRRQTNNQ
CCCCCCHHHCCCCCC
60.017495477
576UbiquitinationGYNQPDSKRRQTNNQ
CCCCCCHHHCCCCCC
60.01-
580PhosphorylationPDSKRRQTNNQNWGS
CCHHHCCCCCCCCCC
34.0324043423
587PhosphorylationTNNQNWGSQPIAQQP
CCCCCCCCCCCCCCC
25.1317525332
601PhosphorylationPLQGGDHSGNYGYKS
CCCCCCCCCCCCCCC
33.2121712546
607SumoylationHSGNYGYKSENQEFY
CCCCCCCCCCCCCHH
47.1028112733
614PhosphorylationKSENQEFYQDTFGQQ
CCCCCCHHHHCCCCC
12.5321945579
617PhosphorylationNQEFYQDTFGQQWK-
CCCHHHHCCCCCCC-
17.7221945579
623AcetylationDTFGQQWK-------
HCCCCCCC-------
46.2391213

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
373YPhosphorylationKinaseFGFR1P11362
PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HNRPQ_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 HNRPQ_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTN11_HUMANPTPN11physical
9847309
ABEC1_HUMANAPOBEC1physical
11352648
A1CF_HUMANA1CFphysical
11352648
SYT7_HUMANSYT7physical
10734137
SYT8_HUMANSYT8physical
10734137
SYT9_HUMANSYT9physical
10734137
HNRPD_HUMANHNRNPDphysical
12674497
A4_HUMANAPPphysical
21832049
PABP1_HUMANPABPC1physical
22939629
HNRPR_HUMANHNRNPRphysical
22939629
ROA1_HUMANHNRNPA1physical
22939629
ROA3_HUMANHNRNPA3physical
22939629
SRSF1_HUMANSRSF1physical
22939629
SRSF3_HUMANSRSF3physical
22939629
TADBP_HUMANTARDBPphysical
22939629
YBOX1_HUMANYBX1physical
22939629
ILF3_HUMANILF3physical
22939629
ILF2_HUMANILF2physical
22939629
RU2A_HUMANSNRPA1physical
22939629
RALY_HUMANRALYphysical
22939629
SRRM2_HUMANSRRM2physical
22939629
U2AF1_HUMANU2AF1physical
22939629
PP1A_HUMANPPP1CAphysical
22939629
U2AF2_HUMANU2AF2physical
22939629
RU17_HUMANSNRNP70physical
22939629
IF4H_HUMANEIF4Hphysical
22939629
IF2B1_HUMANIGF2BP1physical
22939629
PHB_HUMANPHBphysical
22939629
PTCD3_HUMANPTCD3physical
22939629
RL10_HUMANRPL10physical
22939629
RBMS2_HUMANRBMS2physical
22939629
STT3B_HUMANSTT3Bphysical
22939629
RCC1L_HUMANWBSCR16physical
22939629
TIM50_HUMANTIMM50physical
22939629
ROA0_HUMANHNRNPA0physical
22939629
NDUV2_HUMANNDUFV2physical
22939629
LS14A_HUMANLSM14Aphysical
22939629
IKIP_HUMANIKBIPphysical
22939629
ICT1_HUMANICT1physical
22939629
ML12A_HUMANMYL12Aphysical
22939629
STML2_HUMANSTOML2physical
22939629
PLP2_HUMANPLP2physical
22939629
LETM1_HUMANLETM1physical
22939629
RUSD4_HUMANRPUSD4physical
22939629
RPN1_HUMANRPN1physical
22939629
SNP23_HUMANSNAP23physical
22939629
ODP2_HUMANDLATphysical
22939629
LYAG_HUMANGAAphysical
22939629
TM177_HUMANTMEM177physical
22939629
LG3BP_HUMANLGALS3BPphysical
22939629
THIO_HUMANTXNphysical
22939629
RT28_HUMANMRPS28physical
22939629
RS20_HUMANRPS20physical
22939629
HABP4_HUMANHABP4physical
19523114
HNRPU_HUMANHNRNPUphysical
22365833
HNRPK_HUMANHNRNPKphysical
22365833
P63_HUMANTP63physical
20085233
IL7RA_HUMANIL7Rphysical
23151878
ANM8_HUMANPRMT8physical
19060904
ANM1_HUMANPRMT1physical
23455924
HMGA1_HUMANHMGA1physical
18850631
HMGA2_HUMANHMGA2physical
18850631
ANM8_HUMANPRMT8physical
23455924
HNRPU_HUMANHNRNPUphysical
22863883
IQGA1_HUMANIQGAP1physical
22863883
ANM8_HUMANPRMT8physical
25416956
DDX17_HUMANDDX17physical
26344197
DDX3X_HUMANDDX3Xphysical
26344197
DDX5_HUMANDDX5physical
26344197
HNRPU_HUMANHNRNPUphysical
26344197
MO4L1_HUMANMORF4L1physical
26344197
MO4L2_HUMANMORF4L2physical
26344197
NH2L1_HUMANNHP2L1physical
26344197
ZN598_HUMANZNF598physical
26344197
APBB2_HUMANAPBB2physical
26496610
BAD_HUMANBADphysical
26496610
BLMH_HUMANBLMHphysical
26496610
MCAT_HUMANSLC25A20physical
26496610
CRY1_HUMANCRY1physical
26496610
DKC1_HUMANDKC1physical
26496610
DYHC1_HUMANDYNC1H1physical
26496610
ECHM_HUMANECHS1physical
26496610
PHC2_HUMANPHC2physical
26496610
EI2BA_HUMANEIF2B1physical
26496610
SRC8_HUMANCTTNphysical
26496610
MTOR_HUMANMTORphysical
26496610
GOGA3_HUMANGOLGA3physical
26496610
HBA_HUMANHBA1physical
26496610
HEXA_HUMANHEXAphysical
26496610
ROAA_HUMANHNRNPABphysical
26496610
TAU_HUMANMAPTphysical
26496610
M3K4_HUMANMAP3K4physical
26496610
KI67_HUMANMKI67physical
26496610
MYH1_HUMANMYH1physical
26496610
NDUB5_HUMANNDUFB5physical
26496610
NHS_HUMANNHSphysical
26496610
NOP2_HUMANNOP2physical
26496610
YBOX1_HUMANYBX1physical
26496610
PHLP_HUMANPDCLphysical
26496610
PLCB3_HUMANPLCB3physical
26496610
PSMD2_HUMANPSMD2physical
26496610
PTMA_HUMANPTMAphysical
26496610
RECQ1_HUMANRECQLphysical
26496610
RET_HUMANRETphysical
26496610
SCO1_HUMANSCO1physical
26496610
SDC2_HUMANSDC2physical
26496610
SSXT_HUMANSS18physical
26496610
TARB1_HUMANTARBP1physical
26496610
ZEB1_HUMANZEB1physical
26496610
GCFC2_HUMANGCFC2physical
26496610
TLN1_HUMANTLN1physical
26496610
TNR1A_HUMANTNFRSF1Aphysical
26496610
UBP1_HUMANUSP1physical
26496610
ZBT14_HUMANZBTB14physical
26496610
RBM10_HUMANRBM10physical
26496610
UBP13_HUMANUSP13physical
26496610
MTA1_HUMANMTA1physical
26496610
PTTG1_HUMANPTTG1physical
26496610
COX5A_HUMANCOX5Aphysical
26496610
RM33_HUMANMRPL33physical
26496610
GT2D1_HUMANGTF2IRD1physical
26496610
RHG32_HUMANARHGAP32physical
26496610
C2CD5_HUMANC2CD5physical
26496610
HMGX4_HUMANHMGXB4physical
26496610
CEBPZ_HUMANCEBPZphysical
26496610
VINEX_HUMANSORBS3physical
26496610
VPP3_HUMANTCIRG1physical
26496610
ABCA7_HUMANABCA7physical
26496610
TBB3_HUMANTUBB3physical
26496610
TXN4A_HUMANTXNL4Aphysical
26496610
EBP2_HUMANEBNA1BP2physical
26496610
TARA_HUMANTRIOBPphysical
26496610
HNRL1_HUMANHNRNPUL1physical
26496610
FND3A_HUMANFNDC3Aphysical
26496610
SET1B_HUMANSETD1Bphysical
26496610
F120A_HUMANFAM120Aphysical
26496610
MD13L_HUMANMED13Lphysical
26496610
DICER_HUMANDICER1physical
26496610
MACF1_HUMANMACF1physical
26496610
INT7_HUMANINTS7physical
26496610
TB10B_HUMANTBC1D10Bphysical
26496610
WDR91_HUMANWDR91physical
26496610
ANR11_HUMANANKRD11physical
26496610
RGAP1_HUMANRACGAP1physical
26496610
PLPL8_HUMANPNPLA8physical
26496610
RRP15_HUMANRRP15physical
26496610
TR112_HUMANTRMT112physical
26496610
PPIL1_HUMANPPIL1physical
26496610
PPIL3_HUMANPPIL3physical
26496610
APTX_HUMANAPTXphysical
26496610
URFB1_HUMANUHRF1BP1physical
26496610
UACA_HUMANUACAphysical
26496610
CEP55_HUMANCEP55physical
26496610
NAT10_HUMANNAT10physical
26496610
UFSP2_HUMANUFSP2physical
26496610
DNJA4_HUMANDNAJA4physical
26496610
NOP10_HUMANNOP10physical
26496610
PLXA3_HUMANPLXNA3physical
26496610
PR40A_HUMANPRPF40Aphysical
26496610
BIN3_HUMANBIN3physical
26496610
DDX24_HUMANDDX24physical
26496610
Z286A_HUMANZNF286Aphysical
26496610
UVSSA_HUMANUVSSAphysical
26496610
ICE2_HUMANICE2physical
26496610
IPO4_HUMANIPO4physical
26496610
ELMO3_HUMANELMO3physical
26496610
MTMRD_HUMANSBF2physical
26496610
TLN2_HUMANTLN2physical
26496610
KLF16_HUMANKLF16physical
26496610
UBP32_HUMANUSP32physical
26496610
FBH1_HUMANFBXO18physical
26496610
SCMC2_HUMANSLC25A25physical
26496610
PTGR2_HUMANPTGR2physical
26496610
CENPV_HUMANCENPVphysical
26496610
LEMD2_HUMANLEMD2physical
26496610
NSE2_HUMANNSMCE2physical
26496610
RMXL1_HUMANRBMXL1physical
28514442
ANGE2_HUMANANGEL2physical
28514442
RS27A_HUMANRPS27Aphysical
28514442
RU17_HUMANSNRNP70physical
28514442
YTHD1_HUMANYTHDF1physical
28514442
VIGLN_HUMANHDLBPphysical
28514442
RL26L_HUMANRPL26L1physical
28514442
HNRPR_HUMANHNRNPRphysical
28514442
ELAV4_HUMANELAVL4physical
28514442
F120A_HUMANFAM120Aphysical
28514442
DUS11_HUMANDUSP11physical
28514442
ZC3H8_HUMANZC3H8physical
28514442
KNOP1_HUMANKNOP1physical
28514442
DDX54_HUMANDDX54physical
28514442
CC137_HUMANCCDC137physical
28514442
DDX21_HUMANDDX21physical
28514442
ZRAB2_HUMANZRANB2physical
28514442
DDX27_HUMANDDX27physical
28514442
NKAP_HUMANNKAPphysical
28514442
YPEL5_HUMANYPEL5physical
27173435

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 HNRPQ_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 ALA-2, AND MASS SPECTROMETRY.
"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-221 AND LYS-363, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, AND MASSSPECTROMETRY.
"Signaling initiated by overexpression of the fibroblast growth factorreceptor-1 investigated by mass spectrometry.";
Hinsby A.M., Olsen J.V., Bennett K.L., Mann M.;
Mol. Cell. Proteomics 2:29-36(2003).
Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, AND PHOSPHORYLATION ATTYR-373.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-123, AND MASSSPECTROMETRY.

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