Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Heterogeneous nuclear ribonucleoprotein R  

UniProtKB / Swiss-Prot ID :  HNRPR_HUMAN

Gene Name (Synonyms) : 
HNRNPR, HNRPR  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus, nucleoplasm. Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. 

Protein Function :  Component of ribonucleosomes, which are complexes of at least 20 other different heterogenious nuclear ribonucleoproteins (hnRNP). hnRNP play an important role in processing of precursor mRNA in the nucleus. 

Protein Sequence MANQVNGNAVQLKEEEEPMDTSSVTHTEHYKTLIEAGLPQKVAERLDEIFQTGLVAYVDLDERAIDALRE...
Predicted Secondary Structure CEEEECCCCCCCCCCCCCCCCCEEEEEHHHHHHHHCCCCHHHHHHHHHHHHHHHHHHCCCCCCHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MANQVN
---CEEEEC
18.37UniProtKB
Link-
41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GLPQKVAER
CCCHHHHHH
41.28Phosphositeplus
Link-
103N6-acetyllysineCGVMKTYRQ
HHHHHCCCC
39.74Phosphositeplus
Link-
103N6-acetyllysine.CGVMKTYRQ
HHHHHCCCC
39.74UniProtKB
Link-
187Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PLFEKAGPI
HHHHHCCCE
51.84Phosphositeplus
Link-
208PhosphotyrosineQNRGYAFIT
CCCCEEEEE
8.63Phosphositeplus
Link-
229PhosphotyrosineLCDSYEIRP
HHCCEEEEE
11.34Phosphositeplus
Link-
252PhosphoserineLFVGSIPKN
EEECCCCCC
30.34Phosphositeplus
Link-
292S-nitrosocysteineNRGFCFLEY
CCCEEEEEE
4.19dbSNO
Link-
341Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MAKVKVLFV
CCCCCEEEE
32.30Phosphositeplus
Link
359Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EILEKSFSE
HHHHHHHHH
54.04Phosphositeplus
Link
366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SEFGKLERV
HHCCCEEEE
53.12Phosphositeplus
Link
366N6-acetyllysineSEFGKLERV
HHCCCEEEE
53.12HPRD
Link
366N6-acetyllysineSEFGKLERV
HHCCCEEEE
53.12Phosphositeplus
Link
366N6-acetyllysine.SEFGKLERV
HHCCCEEEE
53.12UniProtKB
Link
389Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GAAVKAMDE
HHHHHHHHH
33.01Phosphositeplus
Link
389N6-acetyllysineGAAVKAMDE
HHHHHHHHH
33.01HPRD
Link
389N6-acetyllysineGAAVKAMDE
HHHHHHHHH
33.01Phosphositeplus
Link
389N6-acetyllysine.GAAVKAMDE
HHHHHHHHH
33.01UniProtKB
Link
397N6-acetyllysineEMNGKEIEG
HHCCCEECC
50.98HPRD
Link
397N6-acetyllysineEMNGKEIEG
HHCCCEECC
50.98Phosphositeplus
Link
397N6-acetyllysine.EMNGKEIEG
HHCCCEECC
50.98UniProtKB
Link
434PhosphotyrosineAYEDYYYHP
CCCCCCCCC
8.25HPRD
Link-
434PhosphotyrosineAYEDYYYHP
CCCCCCCCC
8.25Phosphositeplus
Link-
435PhosphotyrosineYEDYYYHPP
CCCCCCCCC
13.97HPRD
Link-
435PhosphotyrosineYEDYYYHPP
CCCCCCCCC
13.97Phosphositeplus
Link-
436PhosphotyrosineEDYYYHPPP
CCCCCCCCC
11.13HPRD
Link-
436PhosphotyrosineEDYYYHPPP
CCCCCCCCC
11.13Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RL26_HUMANphysical interactionEBI-734784
intact16169070
ANM1_HUMANphysical interactionEBI-730150
intact16169070
SYFA_HUMANphysical interactionEBI-736916
intact16169070
SMN_HUMANin vitro
in vivo
HPRD:06228HPRD11773003
11574476
BMPR2_HUMANin vitroHPRD:06228HPRD15188402
ANM1_HUMANin vitroHPRD:06228HPRD12183049
RPAB1_HUMANENSP00000304405STRING
SF3A1_HUMANENSP00000304405STRING
SMD3_HUMANENSP00000304405STRING
NH2L1_HUMANENSP00000304405STRING
RPAB2_HUMANENSP00000304405STRING
PHF5A_HUMANENSP00000304405STRING
PAPOA_HUMANENSP00000304405STRING
SFRS5_HUMANENSP00000304405STRING
PABP2_HUMANENSP00000304405STRING
CSTF1_HUMANENSP00000304405STRING
RPB3_HUMANENSP00000304405STRING
HNRPL_HUMANENSP00000304405STRING
RU17_HUMANENSP00000304405STRING
SF3A2_HUMANENSP00000304405STRING
RPB9_HUMANENSP00000304405STRING
SFRS9_HUMANENSP00000304405STRING
LSM2_HUMANENSP00000304405STRING
PM14_HUMANENSP00000304405STRING
CPSF3_HUMANENSP00000304405STRING
SNRPA_HUMANENSP00000304405STRING
SFRS6_HUMANENSP00000304405STRING
T2FA_HUMANENSP00000304405STRING
RU2B_HUMANENSP00000304405STRING
SF04_HUMANENSP00000304405STRING
FUS_HUMANENSP00000304405STRING
RU2A_HUMANENSP00000304405STRING
SFRS1_HUMANENSP00000304405STRING
U5S1_HUMANENSP00000304405STRING
WDR57_HUMANENSP00000304405STRING
DNJC8_HUMANENSP00000304405STRING
PRP6_HUMANENSP00000304405STRING
RUXF_HUMANENSP00000304405STRING
RUXF_HUMANENSP00000304405STRING
RUXF_HUMANENSP00000304405STRING
PRP16_HUMANENSP00000304405STRING
TXN4A_HUMANENSP00000304405STRING
SF3B4_HUMANENSP00000304405STRING
RUXG_HUMANENSP00000304405STRING
RPB4_HUMANENSP00000304405STRING
REN3B_HUMANENSP00000304405STRING
U2AF1_HUMANENSP00000304405STRING
SFRS2_HUMANENSP00000304405STRING
RPAB3_HUMANENSP00000304405STRING
PCF11_HUMANENSP00000304405STRING
CPSF2_HUMANENSP00000304405STRING
CPSF5_HUMANENSP00000304405STRING
SMD1_HUMANENSP00000304405STRING
RPB7_HUMANENSP00000304405STRING
PRP8_HUMANENSP00000304405STRING
PRP17_HUMANENSP00000304405STRING
CLP1_HUMANENSP00000304405STRING
CD2B2_HUMANENSP00000304405STRING
PCBP1_HUMANENSP00000304405STRING
SF3B3_HUMANENSP00000304405STRING
U2AF2_HUMANENSP00000304405STRING
DDX23_HUMANENSP00000304405STRING
RPB2_HUMANENSP00000304405STRING
HNRPD_HUMANENSP00000304405STRING
RPB1_HUMANENSP00000304405STRING
CSTF3_HUMANENSP00000304405STRING
ROA0_HUMANENSP00000304405STRING
U520_HUMANENSP00000304405STRING
SF3B2_HUMANENSP00000304405STRING
SMC1A_HUMANENSP00000304405STRING
RPAB5_HUMANENSP00000304405STRING
HNRPM_HUMANENSP00000304405STRING
SFRS7_HUMANENSP00000304405STRING
NCBP2_HUMANENSP00000304405STRING
THOC4_HUMANENSP00000304405STRING
SF3B1_HUMANENSP00000304405STRING
HNRPC_HUMANENSP00000304405STRING
CPSF1_HUMANENSP00000304405STRING
ROA1_HUMANENSP00000304405STRING
SMD2_HUMANENSP00000304405STRING
RPAB4_HUMANENSP00000304405STRING
RBM5_HUMANENSP00000304405STRING
CPSF7_HUMANENSP00000304405STRING
HNRPF_HUMANENSP00000304405STRING
T2FB_HUMANENSP00000304405STRING
PCBP2_HUMANENSP00000304405STRING
HNRPK_HUMANENSP00000304405STRING
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Disease Reference
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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-103; LYS-366; LYS-389 ANDLYS-397, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures