HNRL1_HUMAN - dbPTM
HNRL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRL1_HUMAN
UniProt AC Q9BUJ2
Protein Name Heterogeneous nuclear ribonucleoprotein U-like protein 1
Gene Name HNRNPUL1
Organism Homo sapiens (Human).
Sequence Length 856
Subcellular Localization Nucleus .
Protein Description Acts as a basic transcriptional regulator. Represses basic transcription driven by several virus and cellular promoters. When associated with BRD7, activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation. Plays also a role in mRNA processing and transport. Binds avidly to poly(G) and poly(C) RNA homopolymers in vitro..
Protein Sequence MDVRRLKVNELREELQRRGLDTRGLKAELAERLQAALEAEEPDDERELDADDEPGRPGHINEEVETEGGSELEGTAQPPPPGLQPHAEPGGYSGPDGHYAMDNITRQNQFYDTQVIKQENESGYERRPLEMEQQQAYRPEMKTEMKQGAPTSFLPPEASQLKPDRQQFQSRKRPYEENRGRGYFEHREDRRGRSPQPPAEEDEDDFDDTLVAIDTYNCDLHFKVARDRSSGYPLTIEGFAYLWSGARASYGVRRGRVCFEMKINEEISVKHLPSTEPDPHVVRIGWSLDSCSTQLGEEPFSYGYGGTGKKSTNSRFENYGDKFAENDVIGCFADFECGNDVELSFTKNGKWMGIAFRIQKEALGGQALYPHVLVKNCAVEFNFGQRAEPYCSVLPGFTFIQHLPLSERIRGTVGPKSKAECEILMMVGLPAAGKTTWAIKHAASNPSKKYNILGTNAIMDKMRVMGLRRQRNYAGRWDVLIQQATQCLNRLIQIAARKKRNYILDQTNVYGSAQRRKMRPFEGFQRKAIVICPTDEDLKDRTIKRTDEEGKDVPDHAVLEMKANFTLPDVGDFLDEVLFIELQREEADKLVRQYNEEGRKAGPPPEKRFDNRGGGGFRGRGGGGGFQRYENRGPPGGNRGGFQNRGGGSGGGGNYRGGFNRSGGGGYSQNRWGNNNRDNNNSNNRGSYNRAPQQQPPPQQPPPPQPPPQQPPPPPSYSPARNPPGASTYNKNSNIPGSSANTSTPTVSSYSPPQPSYSQPPYNQGGYSQGYTAPPPPPPPPPAYNYGSYGGYNPAPYTPPPPPTAQTYPQPSYNQYQQYAQQWNQYYQNQGQWPPYYGNYDYGSYSGNTQGGTSTQ
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
7Malonylation-MDVRRLKVNELREE
-CCHHHHHHHHHHHH		41.0026320211
15 (in isoform 5)Phosphorylation-4.0424043423
16 (in isoform 5)Phosphorylation-35.9824043423
17 (in isoform 4)Ubiquitination-47.4621890473
22O-linked_GlycosylationLQRRGLDTRGLKAEL
HHHCCCCHHHHHHHH		31.5131373491
22PhosphorylationLQRRGLDTRGLKAEL
HHHCCCCHHHHHHHH		31.5128555341
22 (in isoform 5)Phosphorylation-31.5124043423
23MethylationQRRGLDTRGLKAELA
HHCCCCHHHHHHHHH		48.38-
24 (in isoform 5)Phosphorylation-33.3524043423
26UbiquitinationGLDTRGLKAELAERL
CCCHHHHHHHHHHHH		42.51-
26 (in isoform 5)Phosphorylation-42.5124043423
30 (in isoform 5)Phosphorylation-7.4424043423
33 (in isoform 5)Phosphorylation-2.8224043423
46 (in isoform 4)Ubiquitination-57.6921890473
62 (in isoform 4)Ubiquitination-63.9221890473
74 (in isoform 3)Ubiquitination-38.6921890473
94 (in isoform 4)Phosphorylation-18.81-
103 (in isoform 3)Ubiquitination-25.1721890473
109 (in isoform 4)Phosphorylation-29.91-
111PhosphorylationITRQNQFYDTQVIKQ
CHHCCCCCCCCCCCC		14.3325884760
113PhosphorylationRQNQFYDTQVIKQEN
HCCCCCCCCCCCCCC		17.2328796482
117SumoylationFYDTQVIKQENESGY
CCCCCCCCCCCCCCC		53.34-
117AcetylationFYDTQVIKQENESGY
CCCCCCCCCCCCCCC		53.3426051181
117SumoylationFYDTQVIKQENESGY
CCCCCCCCCCCCCCC		53.3425114211
117UbiquitinationFYDTQVIKQENESGY
CCCCCCCCCCCCCCC		53.3421890473
117 (in isoform 1)Ubiquitination-53.3421890473
117 (in isoform 2)Ubiquitination-53.3421890473
119 (in isoform 3)Ubiquitination-58.9421890473
122PhosphorylationVIKQENESGYERRPL
CCCCCCCCCCCCCCC		59.2528796482
124PhosphorylationKQENESGYERRPLEM
CCCCCCCCCCCCCHH		18.6228796482
137PhosphorylationEMEQQQAYRPEMKTE
HHHHHHHHCHHHHHH		23.51-
142SumoylationQAYRPEMKTEMKQGA
HHHCHHHHHHHHCCC		39.40-
142SumoylationQAYRPEMKTEMKQGA
HHHCHHHHHHHHCCC		39.4025114211
142UbiquitinationQAYRPEMKTEMKQGA
HHHCHHHHHHHHCCC		39.40-
143PhosphorylationAYRPEMKTEMKQGAP
HHCHHHHHHHHCCCC		39.7528555341
146SumoylationPEMKTEMKQGAPTSF
HHHHHHHHCCCCCCC		39.07-
146SumoylationPEMKTEMKQGAPTSF
HHHHHHHHCCCCCCC		39.0728112733
146UbiquitinationPEMKTEMKQGAPTSF
HHHHHHHHCCCCCCC		39.0721890473
146 (in isoform 1)Ubiquitination-39.0721890473
146 (in isoform 2)Ubiquitination-39.0721890473
151PhosphorylationEMKQGAPTSFLPPEA
HHHCCCCCCCCCCCH		31.4121601212
152PhosphorylationMKQGAPTSFLPPEAS
HHCCCCCCCCCCCHH		24.5923898821
159PhosphorylationSFLPPEASQLKPDRQ
CCCCCCHHHCCCCHH		34.0928555341
162AcetylationPPEASQLKPDRQQFQ
CCCHHHCCCCHHHHH		36.9223954790
162SumoylationPPEASQLKPDRQQFQ
CCCHHHCCCCHHHHH		36.9228112733
162UbiquitinationPPEASQLKPDRQQFQ
CCCHHHCCCCHHHHH		36.9221906983
162 (in isoform 1)Ubiquitination-36.9221890473
162 (in isoform 2)Ubiquitination-36.9221890473
170 (in isoform 4)Acetylation-40.85-
170 (in isoform 4)Ubiquitination-40.8521890473
172MethylationRQQFQSRKRPYEENR
HHHHHHCCCCCCCCC		64.07-
172UbiquitinationRQQFQSRKRPYEENR
HHHHHHCCCCCCCCC		64.07-
175PhosphorylationFQSRKRPYEENRGRG
HHHCCCCCCCCCCCC		39.65-
179MethylationKRPYEENRGRGYFEH
CCCCCCCCCCCCCCC		39.19-
181MethylationPYEENRGRGYFEHRE
CCCCCCCCCCCCCCC		33.14-
183PhosphorylationEENRGRGYFEHREDR
CCCCCCCCCCCCCCC		12.39-
194PhosphorylationREDRRGRSPQPPAEE
CCCCCCCCCCCCCCC		30.6129255136
194 (in isoform 2)Phosphorylation-30.61-
209PhosphorylationDEDDFDDTLVAIDTY
CCCCCCCCEEEEECC		25.6129255136
209 (in isoform 2)Phosphorylation-25.61-
215PhosphorylationDTLVAIDTYNCDLHF
CCEEEEECCCCCEEE		15.5528176443
216PhosphorylationTLVAIDTYNCDLHFK
CEEEEECCCCCEEEE		15.2828176443
270AcetylationINEEISVKHLPSTEP
CCCEEEEEECCCCCC		32.4119608861
270SumoylationINEEISVKHLPSTEP
CCCEEEEEECCCCCC		32.4128112733
270UbiquitinationINEEISVKHLPSTEP
CCCEEEEEECCCCCC		32.4121890473
270 (in isoform 1)Ubiquitination-32.4121890473
270 (in isoform 2)Acetylation-32.41-
270 (in isoform 2)Ubiquitination-32.4121890473
277 (in isoform 4)S-nitrosocysteine-61.60-
309AcetylationYGYGGTGKKSTNSRF
CCCCCCCCCCCCHHH		43.3125953088
309UbiquitinationYGYGGTGKKSTNSRF
CCCCCCCCCCCCHHH		43.31-
310UbiquitinationGYGGTGKKSTNSRFE
CCCCCCCCCCCHHHH		64.95-
326 (in isoform 3)Ubiquitination-45.4821890473
340 (in isoform 4)Ubiquitination-22.1321890473
344PhosphorylationCGNDVELSFTKNGKW
CCCEEEEEEEECCEE		19.8424719451
350AcetylationLSFTKNGKWMGIAFR
EEEEECCEEEEEEEE		43.3225953088
350UbiquitinationLSFTKNGKWMGIAFR
EEEEECCEEEEEEEE		43.32-
360AcetylationGIAFRIQKEALGGQA
EEEEEEEHHHHCCCC		42.4526051181
375AcetylationLYPHVLVKNCAVEFN
CCCEEEEECEEEEEC		41.9926051181
377S-nitrosocysteinePHVLVKNCAVEFNFG
CEEEEECEEEEECCC		3.58-
377GlutathionylationPHVLVKNCAVEFNFG
CEEEEECEEEEECCC		3.5822555962
377S-nitrosylationPHVLVKNCAVEFNFG
CEEEEECEEEEECCC		3.5822178444
377 (in isoform 2)S-nitrosocysteine-3.58-
391GlutathionylationGQRAEPYCSVLPGFT
CCCCCCCCEECCCCE		3.1222555962
412 (in isoform 4)Phosphorylation-16.67-
418AcetylationGTVGPKSKAECEILM
CCCCCCCHHHHEEEE		55.0926051181
418UbiquitinationGTVGPKSKAECEILM
CCCCCCCHHHHEEEE		55.09-
421GlutathionylationGPKSKAECEILMMVG
CCCCHHHHEEEEEEC		4.7522555962
435PhosphorylationGLPAAGKTTWAIKHA
CCCCCCCHHHHHHHH		27.0126437602
440SumoylationGKTTWAIKHAASNPS
CCHHHHHHHHHCCCC		21.31-
440AcetylationGKTTWAIKHAASNPS
CCHHHHHHHHHCCCC		21.3125825284
440MethylationGKTTWAIKHAASNPS
CCHHHHHHHHHCCCC		21.31-
440SumoylationGKTTWAIKHAASNPS
CCHHHHHHHHHCCCC		21.31-
440UbiquitinationGKTTWAIKHAASNPS
CCHHHHHHHHHCCCC		21.3121890473
440 (in isoform 1)Ubiquitination-21.3121890473
440 (in isoform 2)Ubiquitination-21.3121890473
444PhosphorylationWAIKHAASNPSKKYN
HHHHHHHCCCCCCEE		50.48-
448SumoylationHAASNPSKKYNILGT
HHHCCCCCCEEEECH		61.61-
449SumoylationAASNPSKKYNILGTN
HHCCCCCCEEEECHH		48.11-
449SumoylationAASNPSKKYNILGTN
HHCCCCCCEEEECHH		48.1128112733
449UbiquitinationAASNPSKKYNILGTN
HHCCCCCCEEEECHH		48.11-
450PhosphorylationASNPSKKYNILGTNA
HCCCCCCEEEECHHH		15.92-
455PhosphorylationKKYNILGTNAIMDKM
CCEEEECHHHHHHHH		20.31-
4612-HydroxyisobutyrylationGTNAIMDKMRVMGLR
CHHHHHHHHHHHCHH		15.95-
461AcetylationGTNAIMDKMRVMGLR
CHHHHHHHHHHHCHH		15.9526051181
461UbiquitinationGTNAIMDKMRVMGLR
CHHHHHHHHHHHCHH		15.95-
487S-nitrosocysteineLIQQATQCLNRLIQI
HHHHHHHHHHHHHHH		2.94-
487S-nitrosylationLIQQATQCLNRLIQI
HHHHHHHHHHHHHHH		2.9422178444
502PhosphorylationAARKKRNYILDQTNV
HHHHCCCCCCCCCCC		13.5928152594
507PhosphorylationRNYILDQTNVYGSAQ
CCCCCCCCCCCCCHH		26.7322115753
510PhosphorylationILDQTNVYGSAQRRK
CCCCCCCCCCHHHHC		13.8719605366
512PhosphorylationDQTNVYGSAQRRKMR
CCCCCCCCHHHHCCC		11.9819664994
512 (in isoform 2)Phosphorylation-11.98-
517MalonylationYGSAQRRKMRPFEGF
CCCHHHHCCCCCCCC		41.2626320211
517UbiquitinationYGSAQRRKMRPFEGF
CCCHHHHCCCCCCCC		41.26-
527SumoylationPFEGFQRKAIVICPT
CCCCCCCCEEEECCC		31.51-
527AcetylationPFEGFQRKAIVICPT
CCCCCCCCEEEECCC		31.5126051181
527SumoylationPFEGFQRKAIVICPT
CCCCCCCCEEEECCC		31.51-
527UbiquitinationPFEGFQRKAIVICPT
CCCCCCCCEEEECCC		31.51-
532GlutathionylationQRKAIVICPTDEDLK
CCCEEEECCCCHHHH		1.7422555962
532S-palmitoylationQRKAIVICPTDEDLK
CCCEEEECCCCHHHH		1.7421044946
539SumoylationCPTDEDLKDRTIKRT
CCCCHHHHHCCCCCC		58.44-
5392-HydroxyisobutyrylationCPTDEDLKDRTIKRT
CCCCHHHHHCCCCCC		58.44-
539AcetylationCPTDEDLKDRTIKRT
CCCCHHHHHCCCCCC		58.4426051181
539SumoylationCPTDEDLKDRTIKRT
CCCCHHHHHCCCCCC		58.4428112733
539UbiquitinationCPTDEDLKDRTIKRT
CCCCHHHHHCCCCCC		58.44-
549 (in isoform 4)Phosphorylation-74.48-
551AcetylationKRTDEEGKDVPDHAV
CCCCCCCCCCCCCEE		59.8523236377
551MalonylationKRTDEEGKDVPDHAV
CCCCCCCCCCCCCEE		59.8526320211
562SumoylationDHAVLEMKANFTLPD
CCEEEEEECCEECCC		30.70-
584DimethylationVLFIELQREEADKLV
HHHHEECHHHHHHHH		57.24-
584MethylationVLFIELQREEADKLV
HHHHEECHHHHHHHH		57.24-
5892-HydroxyisobutyrylationLQREEADKLVRQYNE
ECHHHHHHHHHHHHH		56.80-
592MethylationEEADKLVRQYNEEGR
HHHHHHHHHHHHHHH		43.64-
600SumoylationQYNEEGRKAGPPPEK
HHHHHHHCCCCCCHH		69.43-
600UbiquitinationQYNEEGRKAGPPPEK
HHHHHHHCCCCCCHH		69.43-
612MethylationPEKRFDNRGGGGFRG
CHHCCCCCCCCCCCC		47.15-
616 (in isoform 4)Phosphorylation-16.62-
617 (in isoform 4)Phosphorylation-9.41-
618DimethylationNRGGGGFRGRGGGGG
CCCCCCCCCCCCCCC		36.85-
618MethylationNRGGGGFRGRGGGGG
CCCCCCCCCCCCCCC		36.85-
618 (in isoform 4)Phosphorylation-36.85-
620DimethylationGGGGFRGRGGGGGFQ
CCCCCCCCCCCCCCC		36.01-
620MethylationGGGGFRGRGGGGGFQ
CCCCCCCCCCCCCCC		36.01-
628MethylationGGGGGFQRYENRGPP
CCCCCCCCCCCCCCC		38.17-
632MethylationGFQRYENRGPPGGNR
CCCCCCCCCCCCCCC		47.24-
639Asymmetric dimethylarginineRGPPGGNRGGFQNRG
CCCCCCCCCCCCCCC		50.30-
639MethylationRGPPGGNRGGFQNRG
CCCCCCCCCCCCCCC		50.3024129315
645Asymmetric dimethylarginineNRGGFQNRGGGSGGG
CCCCCCCCCCCCCCC		34.06-
645MethylationNRGGFQNRGGGSGGG
CCCCCCCCCCCCCCC		34.0624129315
649PhosphorylationFQNRGGGSGGGGNYR
CCCCCCCCCCCCCCC		37.2220068231
649 (in isoform 2)Phosphorylation-37.22-
656Asymmetric dimethylarginineSGGGGNYRGGFNRSG
CCCCCCCCCCCCCCC		42.64-
656MethylationSGGGGNYRGGFNRSG
CCCCCCCCCCCCCCC		42.6424129315
661MethylationNYRGGFNRSGGGGYS
CCCCCCCCCCCCCCC		34.12-
662PhosphorylationYRGGFNRSGGGGYSQ
CCCCCCCCCCCCCCC		42.7821406692
667PhosphorylationNRSGGGGYSQNRWGN
CCCCCCCCCCCCCCC		15.4521406692
668PhosphorylationRSGGGGYSQNRWGNN
CCCCCCCCCCCCCCC		25.0128796482
671MethylationGGGYSQNRWGNNNRD
CCCCCCCCCCCCCCC		34.7324129315
682PhosphorylationNNRDNNNSNNRGSYN
CCCCCCCCCCCCCCC		37.2921406692
685MethylationDNNNSNNRGSYNRAP
CCCCCCCCCCCCCCC		39.42-
687PhosphorylationNNSNNRGSYNRAPQQ
CCCCCCCCCCCCCCC		18.9221406692
688PhosphorylationNSNNRGSYNRAPQQQ
CCCCCCCCCCCCCCC		16.1121406692
690MethylationNNRGSYNRAPQQQPP
CCCCCCCCCCCCCCC		39.14-
716PhosphorylationQQPPPPPSYSPARNP
CCCCCCCCCCCCCCC		43.9729255136
716 (in isoform 2)Phosphorylation-43.97-
717PhosphorylationQPPPPPSYSPARNPP
CCCCCCCCCCCCCCC		25.1729255136
717 (in isoform 2)Phosphorylation-25.17-
718PhosphorylationPPPPPSYSPARNPPG
CCCCCCCCCCCCCCC		19.2029255136
718 (in isoform 2)Phosphorylation-19.20-
727O-linked_GlycosylationARNPPGASTYNKNSN
CCCCCCCCCCCCCCC		37.0231373491
727PhosphorylationARNPPGASTYNKNSN
CCCCCCCCCCCCCCC		37.0228152594
728PhosphorylationRNPPGASTYNKNSNI
CCCCCCCCCCCCCCC		30.4928152594
729NitrationNPPGASTYNKNSNIP
CCCCCCCCCCCCCCC		22.96-
729PhosphorylationNPPGASTYNKNSNIP
CCCCCCCCCCCCCCC		22.9628450419
733O-linked_GlycosylationASTYNKNSNIPGSSA
CCCCCCCCCCCCCCC		37.4331373491
738O-linked_GlycosylationKNSNIPGSSANTSTP
CCCCCCCCCCCCCCC		22.4131373491
739O-linked_GlycosylationNSNIPGSSANTSTPT
CCCCCCCCCCCCCCC		31.3031373491
742O-linked_GlycosylationIPGSSANTSTPTVSS
CCCCCCCCCCCCCCC		33.4231373491
743O-linked_GlycosylationPGSSANTSTPTVSSY
CCCCCCCCCCCCCCC		32.0031373491
744O-linked_GlycosylationGSSANTSTPTVSSYS
CCCCCCCCCCCCCCC		22.4231373491
746O-linked_GlycosylationSANTSTPTVSSYSPP
CCCCCCCCCCCCCCC		32.8631373491
746PhosphorylationSANTSTPTVSSYSPP
CCCCCCCCCCCCCCC		32.8626074081
748O-linked_GlycosylationNTSTPTVSSYSPPQP
CCCCCCCCCCCCCCC		26.4931373491
748PhosphorylationNTSTPTVSSYSPPQP
CCCCCCCCCCCCCCC		26.4926074081
749O-linked_GlycosylationTSTPTVSSYSPPQPS
CCCCCCCCCCCCCCC		25.8731373491
749PhosphorylationTSTPTVSSYSPPQPS
CCCCCCCCCCCCCCC		25.8726074081
750PhosphorylationSTPTVSSYSPPQPSY
CCCCCCCCCCCCCCC		20.0726074081
751PhosphorylationTPTVSSYSPPQPSYS
CCCCCCCCCCCCCCC		31.8626074081
756PhosphorylationSYSPPQPSYSQPPYN
CCCCCCCCCCCCCCC		31.9726074081
757PhosphorylationYSPPQPSYSQPPYNQ
CCCCCCCCCCCCCCC		20.2926074081
758PhosphorylationSPPQPSYSQPPYNQG
CCCCCCCCCCCCCCC		40.3126074081
798O-linked_GlycosylationGYNPAPYTPPPPPTA
CCCCCCCCCCCCCCC		28.4131373491
804O-linked_GlycosylationYTPPPPPTAQTYPQP
CCCCCCCCCCCCCCC		36.8531373491
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 HNRL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HNRL1_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 HNRL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRD7_HUMANBRD7physical
12489984
ERG28_HUMANC14orf1physical
16169070
MED31_HUMANMED31physical
16169070
DPYL1_HUMANCRMP1physical
16169070
PR40A_HUMANPRPF40Aphysical
16169070
ANM2_HUMANPRMT2physical
11513728
TLX3_HUMANTLX3physical
20211142
ATM_HUMANATMphysical
18480432
ATRIP_HUMANATRIPphysical
18480432
RFA1_HUMANRPA1physical
18480432
RFA2_HUMANRPA2physical
18480432
HNRPF_HUMANHNRNPFphysical
22939629
RBMX_HUMANRBMXphysical
22939629
ROA0_HUMANHNRNPA0physical
22939629
ILF2_HUMANILF2physical
22939629
RB11B_HUMANRAB11Bphysical
22939629
VATH_HUMANATP6V1Hphysical
22939629
T179B_HUMANTMEM179Bphysical
22939629
HNRL2_HUMANHNRNPUL2physical
22939629
SAM50_HUMANSAMM50physical
22939629
RU1C_HUMANSNRPCphysical
22365833
RU2B_HUMANSNRPB2physical
22365833
SF3B4_HUMANSF3B4physical
22365833
SF01_HUMANSF1physical
22365833
SRSF9_HUMANSRSF9physical
22365833
RBM22_HUMANRBM22physical
22365833
PPIL1_HUMANPPIL1physical
22365833
ZN207_HUMANZNF207physical
22365833
HNRL1_HUMANHNRNPUL1physical
22365833
RBM4_HUMANRBM4physical
22365833
SMN_HUMANSMN1physical
22365833
HNRPF_HUMANHNRNPFphysical
22365833
HNRH2_HUMANHNRNPH2physical
22365833
HNRH3_HUMANHNRNPH3physical
22365833
IL7RA_HUMANIL7Rphysical
23151878
TGM2_HUMANTGM2physical
21988832
PIAS4_HUMANPIAS4physical
21988832
APEX1_HUMANAPEX1physical
22863883
GDN_HUMANSERPINE2physical
22863883
HNRL1_HUMANHNRNPUL1physical
25416956
ROP1A_HUMANROPN1physical
25416956
VP37C_HUMANVPS37Cphysical
25416956
RBM4B_HUMANRBM4Bphysical
25416956
MISSL_HUMANMAPK1IP1Lphysical
25416956
DMRTB_HUMANDMRTB1physical
21516116
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 HNRL1_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-270, 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-194 AND SER-512, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-209 AND SER-716, ANDMASS 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-716 AND SER-718, ANDMASS SPECTROMETRY.
"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-194, AND MASSSPECTROMETRY.
"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-194, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, 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-194, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512 AND SER-718, ANDMASS SPECTROMETRY.

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