HNRDL_HUMAN - dbPTM
HNRDL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRDL_HUMAN
UniProt AC O14979
Protein Name Heterogeneous nuclear ribonucleoprotein D-like
Gene Name HNRNPDL
Organism Homo sapiens (Human).
Sequence Length 420
Subcellular Localization Nucleus . Cytoplasm . Shuttles between the nucleus and the cytoplasm in a TNPO1-dependent manner.
Protein Description Acts as a transcriptional regulator. Promotes transcription repression. Promotes transcription activation in differentiated myotubes (By similarity). Binds to double- and single-stranded DNA sequences. Binds to the transcription suppressor CATR sequence of the COX5B promoter (By similarity). Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Binds both to nuclear and cytoplasmic poly(A) mRNAs. Binds to poly(G) and poly(A), but not to poly(U) or poly(C) RNA homopolymers. Binds to the 5'-ACUAGC-3' RNA consensus sequence..
Protein Sequence MEVPPRLSHVPPPLFPSAPATLASRSLSHWRPRPPRQLAPLLPSLAPSSARQGARRAQRHVTAQQPSRLAGGAAIKGGRRRRPDLFRRHFKSSSIQRSAAAAAATRTARQHPPADSSVTMEDMNEYSNIEEFAEGSKINASKNQQDDGKMFIGGLSWDTSKKDLTEYLSRFGEVVDCTIKTDPVTGRSRGFGFVLFKDAASVDKVLELKEHKLDGKLIDPKRAKALKGKEPPKKVFVGGLSPDTSEEQIKEYFGAFGEIENIELPMDTKTNERRGFCFITYTDEEPVKKLLESRYHQIGSGKCEIKVAQPKEVYRQQQQQQKGGRGAAAGGRGGTRGRGRGQGQNWNQGFNNYYDQGYGNYNSAYGGDQNYSGYGGYDYTGYNYGNYGYGQGYADYSGQQSTYGKASRGGGNHQNNYQPY
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
6Methylation--MEVPPRLSHVPPP
--CCCCCCHHCCCCC		42.63115479035
7 (in isoform 2)Phosphorylation-5.2525849741
7 (in isoform 3)Phosphorylation-5.2525849741
8PhosphorylationMEVPPRLSHVPPPLF
CCCCCCHHCCCCCCC		24.5820068231
8 (in isoform 2)Phosphorylation-24.5825849741
8 (in isoform 3)Phosphorylation-24.5825849741
17PhosphorylationVPPPLFPSAPATLAS
CCCCCCCCCCCHHHH		39.2820068231
21PhosphorylationLFPSAPATLASRSLS
CCCCCCCHHHHCCCC		23.0720068231
23 (in isoform 2)Ubiquitination-9.8821890473
23 (in isoform 3)Ubiquitination-9.8821890473
24PhosphorylationSAPATLASRSLSHWR
CCCCHHHHCCCCCCC		26.0520068231
25DimethylationAPATLASRSLSHWRP
CCCHHHHCCCCCCCC		35.69-
25MethylationAPATLASRSLSHWRP
CCCHHHHCCCCCCCC		35.6924129315
26PhosphorylationPATLASRSLSHWRPR
CCHHHHCCCCCCCCC		31.5628555341
30 (in isoform 2)Ubiquitination-14.4821890473
30 (in isoform 3)Ubiquitination-14.4821890473
42 (in isoform 2)Ubiquitination-2.3621890473
42 (in isoform 3)Ubiquitination-2.3621890473
43 (in isoform 2)Ubiquitination-34.6721890473
43 (in isoform 3)Ubiquitination-34.6721890473
48PhosphorylationLLPSLAPSSARQGAR
CHHHCCCHHHHHHHH		30.9022210691
49PhosphorylationLPSLAPSSARQGARR
HHHCCCHHHHHHHHH		26.8122210691
61 (in isoform 2)Ubiquitination-5.3021890473
61 (in isoform 3)Ubiquitination-5.3021890473
67PhosphorylationHVTAQQPSRLAGGAA
HCCCCCCCHHHCCCC		35.2728555341
68MethylationVTAQQPSRLAGGAAI
CCCCCCCHHHCCCCC		34.93115479031
76AcetylationLAGGAAIKGGRRRRP
HHCCCCCCCCCCCCH		51.0625953088
76MethylationLAGGAAIKGGRRRRP
HHCCCCCCCCCCCCH		51.06116251837
76UbiquitinationLAGGAAIKGGRRRRP
HHCCCCCCCCCCCCH		51.06-
78 (in isoform 2)Ubiquitination-18.2121890473
78 (in isoform 3)Ubiquitination-18.2121890473
81MethylationAIKGGRRRRPDLFRR
CCCCCCCCCHHHHHH		53.79115479039
82MethylationIKGGRRRRPDLFRRH
CCCCCCCCHHHHHHH		27.5454556605
85 (in isoform 2)Ubiquitination-3.8921890473
85 (in isoform 3)Ubiquitination-3.8921890473
94PhosphorylationRRHFKSSSIQRSAAA
HHHHHCHHHHHHHHH		29.8121406692
98PhosphorylationKSSSIQRSAAAAAAT
HCHHHHHHHHHHHHH		13.0921406692
105PhosphorylationSAAAAAATRTARQHP
HHHHHHHHHHHHHCC		24.6721406692
115 (in isoform 2)Ubiquitination-47.4121890473
115 (in isoform 3)Ubiquitination-47.4121890473
116PhosphorylationRQHPPADSSVTMEDM
HHCCCCCCCCCHHHH		28.9027642862
117PhosphorylationQHPPADSSVTMEDMN
HCCCCCCCCCHHHHH		23.3530576142
119PhosphorylationPPADSSVTMEDMNEY
CCCCCCCCHHHHHHC		19.4528348404
126PhosphorylationTMEDMNEYSNIEEFA
CHHHHHHCCCHHHHH		11.3028355574
127PhosphorylationMEDMNEYSNIEEFAE
HHHHHHCCCHHHHHH		25.7521955146
136PhosphorylationIEEFAEGSKINASKN
HHHHHHCCCCCCCCC		23.1326552605
137AcetylationEEFAEGSKINASKNQ
HHHHHCCCCCCCCCC		51.3325953088
137UbiquitinationEEFAEGSKINASKNQ
HHHHHCCCCCCCCCC		51.3321139048
1422-HydroxyisobutyrylationGSKINASKNQQDDGK
CCCCCCCCCCCCCCC		57.26-
142UbiquitinationGSKINASKNQQDDGK
CCCCCCCCCCCCCCC		57.2621906983
142 (in isoform 1)Ubiquitination-57.2621890473
149AcetylationKNQQDDGKMFIGGLS
CCCCCCCCEEECEEC		37.3226051181
149UbiquitinationKNQQDDGKMFIGGLS
CCCCCCCCEEECEEC		37.3221890473
149 (in isoform 1)Ubiquitination-37.3221890473
150SulfoxidationNQQDDGKMFIGGLSW
CCCCCCCEEECEECC		3.4628183972
150 (in isoform 2)Ubiquitination-3.4621890473
150 (in isoform 3)Ubiquitination-3.4621890473
156PhosphorylationKMFIGGLSWDTSKKD
CEEECEECCCCCHHH		26.6124275569
159PhosphorylationIGGLSWDTSKKDLTE
ECEECCCCCHHHHHH		35.8728857561
160PhosphorylationGGLSWDTSKKDLTEY
CEECCCCCHHHHHHH		34.9228348404
1612-HydroxyisobutyrylationGLSWDTSKKDLTEYL
EECCCCCHHHHHHHH		53.01-
161AcetylationGLSWDTSKKDLTEYL
EECCCCCHHHHHHHH		53.0121339330
161MethylationGLSWDTSKKDLTEYL
EECCCCCHHHHHHHH		53.0123644510
161UbiquitinationGLSWDTSKKDLTEYL
EECCCCCHHHHHHHH		53.0121906983
161 (in isoform 1)Ubiquitination-53.0121890473
1622-HydroxyisobutyrylationLSWDTSKKDLTEYLS
ECCCCCHHHHHHHHH		58.71-
162UbiquitinationLSWDTSKKDLTEYLS
ECCCCCHHHHHHHHH		58.7121890473
162 (in isoform 1)Ubiquitination-58.7121890473
165PhosphorylationDTSKKDLTEYLSRFG
CCCHHHHHHHHHHHC		32.4928796482
167PhosphorylationSKKDLTEYLSRFGEV
CHHHHHHHHHHHCCE		12.5428796482
169PhosphorylationKDLTEYLSRFGEVVD
HHHHHHHHHHCCEEE		25.3528796482
177S-nitrosocysteineRFGEVVDCTIKTDPV
HHCCEEEEEEECCCC		2.61-
177GlutathionylationRFGEVVDCTIKTDPV
HHCCEEEEEEECCCC		2.6122555962
177S-nitrosylationRFGEVVDCTIKTDPV
HHCCEEEEEEECCCC		2.6122178444
178PhosphorylationFGEVVDCTIKTDPVT
HCCEEEEEEECCCCC		22.5030576142
1802-HydroxyisobutyrylationEVVDCTIKTDPVTGR
CEEEEEEECCCCCCC		28.81-
180AcetylationEVVDCTIKTDPVTGR
CEEEEEEECCCCCCC		28.8125953088
180MalonylationEVVDCTIKTDPVTGR
CEEEEEEECCCCCCC		28.8126320211
180UbiquitinationEVVDCTIKTDPVTGR
CEEEEEEECCCCCCC		28.8121906983
180 (in isoform 1)Ubiquitination-28.8121890473
181PhosphorylationVVDCTIKTDPVTGRS
EEEEEEECCCCCCCC		41.5023882029
183 (in isoform 2)Ubiquitination-30.70-
185PhosphorylationTIKTDPVTGRSRGFG
EEECCCCCCCCCCEE		32.0623312004
189MethylationDPVTGRSRGFGFVLF
CCCCCCCCCEEEEEE		43.00-
192 (in isoform 2)Ubiquitination-17.99-
197AcetylationGFGFVLFKDAASVDK
CEEEEEEECCCCCHH		42.1525825284
197UbiquitinationGFGFVLFKDAASVDK
CEEEEEEECCCCCHH		42.1521890473
197 (in isoform 1)Ubiquitination-42.1521890473
2042-HydroxyisobutyrylationKDAASVDKVLELKEH
ECCCCCHHHHHHHHH		46.71-
204AcetylationKDAASVDKVLELKEH
ECCCCCHHHHHHHHH		46.7125953088
204UbiquitinationKDAASVDKVLELKEH
ECCCCCHHHHHHHHH		46.7121890473
204 (in isoform 1)Ubiquitination-46.7121890473
2092-HydroxyisobutyrylationVDKVLELKEHKLDGK
CHHHHHHHHHCCCCC		48.69-
209AcetylationVDKVLELKEHKLDGK
CHHHHHHHHHCCCCC		48.6926051181
209SumoylationVDKVLELKEHKLDGK
CHHHHHHHHHCCCCC		48.6928112733
209UbiquitinationVDKVLELKEHKLDGK
CHHHHHHHHHCCCCC		48.69-
2162-HydroxyisobutyrylationKEHKLDGKLIDPKRA
HHHCCCCCCCCHHHH		41.77-
216AcetylationKEHKLDGKLIDPKRA
HHHCCCCCCCCHHHH		41.7719608861
216UbiquitinationKEHKLDGKLIDPKRA
HHHCCCCCCCCHHHH		41.77-
234UbiquitinationKGKEPPKKVFVGGLS
CCCCCCCCEEECCCC		46.8321890473
234 (in isoform 1)Ubiquitination-46.8321890473
241PhosphorylationKVFVGGLSPDTSEEQ
CEEECCCCCCCCHHH		24.8119664994
244PhosphorylationVGGLSPDTSEEQIKE
ECCCCCCCCHHHHHH		41.2330266825
245PhosphorylationGGLSPDTSEEQIKEY
CCCCCCCCHHHHHHH		46.6630278072
269UbiquitinationIELPMDTKTNERRGF
EECCCCCCCCCCCCE		45.122190698
269 (in isoform 1)Ubiquitination-45.1221890473
277GlutathionylationTNERRGFCFITYTDE
CCCCCCEEEEEECCC		2.4122555962
280PhosphorylationRRGFCFITYTDEEPV
CCCEEEEEECCCHHH		10.5028152594
281PhosphorylationRGFCFITYTDEEPVK
CCEEEEEECCCHHHH		13.8428152594
282PhosphorylationGFCFITYTDEEPVKK
CEEEEEECCCHHHHH		28.4328152594
2882-HydroxyisobutyrylationYTDEEPVKKLLESRY
ECCCHHHHHHHHHHH		48.71-
288AcetylationYTDEEPVKKLLESRY
ECCCHHHHHHHHHHH		48.7126051181
288UbiquitinationYTDEEPVKKLLESRY
ECCCHHHHHHHHHHH		48.71-
295NitrationKKLLESRYHQIGSGK
HHHHHHHHCCCCCCC		13.83-
295PhosphorylationKKLLESRYHQIGSGK
HHHHHHHHCCCCCCC		13.8322817900
300PhosphorylationSRYHQIGSGKCEIKV
HHHCCCCCCCCEEEE		36.3928258704
3022-HydroxyisobutyrylationYHQIGSGKCEIKVAQ
HCCCCCCCCEEEECC		30.32-
302AcetylationYHQIGSGKCEIKVAQ
HCCCCCCCCEEEECC		30.3223749302
302UbiquitinationYHQIGSGKCEIKVAQ
HCCCCCCCCEEEECC		30.32-
303GlutathionylationHQIGSGKCEIKVAQP
CCCCCCCCEEEECCH		8.1422555962
306AcetylationGSGKCEIKVAQPKEV
CCCCCEEEECCHHHH		14.8225953088
306UbiquitinationGSGKCEIKVAQPKEV
CCCCCEEEECCHHHH		14.82-
3112-HydroxyisobutyrylationEIKVAQPKEVYRQQQ
EEEECCHHHHHHHHH		47.97-
311AcetylationEIKVAQPKEVYRQQQ
EEEECCHHHHHHHHH		47.9726051181
311SuccinylationEIKVAQPKEVYRQQQ
EEEECCHHHHHHHHH		47.9723954790
311UbiquitinationEIKVAQPKEVYRQQQ
EEEECCHHHHHHHHH		47.97-
314PhosphorylationVAQPKEVYRQQQQQQ
ECCHHHHHHHHHHHH		12.0919702290
335PhosphorylationAAGGRGGTRGRGRGQ
CCCCCCCCCCCCCCC		32.5422985185
387PhosphorylationTGYNYGNYGYGQGYA
CCEECCCCCCCCCCC		13.83-
389PhosphorylationYNYGNYGYGQGYADY
EECCCCCCCCCCCCC		8.91-
396PhosphorylationYGQGYADYSGQQSTY
CCCCCCCCCCCCCCC		13.41-
408DimethylationSTYGKASRGGGNHQN
CCCCCCCCCCCCCCC		53.27-
408MethylationSTYGKASRGGGNHQN
CCCCCCCCCCCCCCC		53.2715782174
417PhosphorylationGGNHQNNYQPY----
CCCCCCCCCCC----		20.58-
420PhosphorylationHQNNYQPY-------
CCCCCCCC-------		18.70-
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 HNRDL_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
408RMethylation


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 HNRDL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ROA1_HUMANHNRNPA1physical
22939629
ROA3_HUMANHNRNPA3physical
22939629
HNRH1_HUMANHNRNPH1physical
22939629
HNRPM_HUMANHNRNPMphysical
22939629
HNRL1_HUMANHNRNPUL1physical
22939629
SRSF2_HUMANSRSF2physical
22939629
RU17_HUMANSNRNP70physical
22939629
ROA2_HUMANHNRNPA2B1physical
22939629
U2AF2_HUMANU2AF2physical
22939629
SRSF3_HUMANSRSF3physical
22939629
PTBP1_HUMANPTBP1physical
22939629
HNRPR_HUMANHNRNPRphysical
22939629
HNRPF_HUMANHNRNPFphysical
22939629
SRSF9_HUMANSRSF9physical
22939629
SRSF1_HUMANSRSF1physical
22939629
HNRH3_HUMANHNRNPH3physical
22939629
HNRPL_HUMANHNRNPLphysical
22939629
VATB1_HUMANATP6V1B1physical
22939629
HNRH2_HUMANHNRNPH2physical
22939629
RL36_HUMANRPL36physical
22939629
IF4H_HUMANEIF4Hphysical
22939629
LS14A_HUMANLSM14Aphysical
22939629
HNRPD_HUMANHNRNPDphysical
22939629
WIPF2_HUMANWIPF2physical
22939629
ROA0_HUMANHNRNPA0physical
22939629
RMD3_HUMANRMDN3physical
22939629
ODPA_HUMANPDHA1physical
22939629
RT16_HUMANMRPS16physical
22939629
RS7_HUMANRPS7physical
22939629
PICAL_HUMANPICALMphysical
22939629
UBE2S_HUMANUBE2Sphysical
22939629
IL7RA_HUMANIL7Rphysical
23151878
HMGA1_HUMANHMGA1physical
18850631
PABP4_HUMANPABPC4physical
26186194
SYYM_HUMANYARS2physical
26186194
MTEF3_HUMANMTERF3physical
26186194
RM32_HUMANMRPL32physical
26186194
ERAL1_HUMANERAL1physical
26186194
LARP1_HUMANLARP1physical
26186194
RT09_HUMANMRPS9physical
26186194
NGRN_HUMANNGRNphysical
26186194
SUV3_HUMANSUPV3L1physical
26186194
RM55_HUMANMRPL55physical
26186194
MASU1_HUMANMALSU1physical
26186194
RM19_HUMANMRPL19physical
26186194
PAIP1_HUMANPAIP1physical
26186194
ICT1_HUMANICT1physical
26186194
FABD_HUMANMCATphysical
26186194
MKRN2_HUMANMKRN2physical
26186194
CARF_HUMANCDKN2AIPphysical
26186194
RM14_HUMANMRPL14physical
26186194
STIP1_HUMANSTIP1physical
26344197
CARF_HUMANCDKN2AIPphysical
28514442
SYYM_HUMANYARS2physical
28514442
PABP4_HUMANPABPC4physical
28514442
NGRN_HUMANNGRNphysical
28514442
PAIP1_HUMANPAIP1physical
28514442
MASU1_HUMANMALSU1physical
28514442
LARP1_HUMANLARP1physical
28514442
ERAL1_HUMANERAL1physical
28514442
RM19_HUMANMRPL19physical
28514442
RT35_HUMANMRPS35physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609115Limb-girdle muscular dystrophy 1G (LGMD1G)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HNRDL_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-216, AND MASS SPECTROMETRY.
Methylation
ReferencePubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC.";
Ong S.E., Mittler G., Mann M.;
Nat. Methods 1:119-126(2004).
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-408, 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-241, AND MASSSPECTROMETRY.
"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-241, 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-241, AND MASSSPECTROMETRY.

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