Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Splicing factor U2AF 65 kDa subunit  

UniProtKB / Swiss-Prot ID :  U2AF2_HUMAN

Gene Name (Synonyms) : 
U2AF2, U2AF65  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Necessary for the splicing of pre-mRNA. Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10. 

Protein Sequence MSDFDEFERQLNENKQERDKENRHRKRSHSRSRSRDRKRRSRSRDRRNRDQRSASRDRRRRSKPLTRGAK...
Predicted Secondary Structure CCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCHHHHHHHHCCCCCCCCCCCCCC...
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-acetylserine.---MSDFDE
---CCCHHH
47.16UniProtKB
Link-
2Phosphoserine---MSDFDE
---CCCHHH
47.16HPRD
Link-
2Phosphoserine---MSDFDE
---CCCHHH
47.16PhosphoELM
Link-
2Phosphoserine---MSDFDE
---CCCHHH
47.16Phosphositeplus
Link-
2Phosphoserine---MSDFDE
---CCCHHH
47.16SysPTM
Link-
2Phosphoserine.---MSDFDE
---CCCHHH
47.16UniProtKB
Link-
155-hydroxylysine; by JMJD6.LNENKQERD
HHHHHHHHH
47.56UniProtKB
Link-
32PhosphoserineSHSRSRSRD
HHHHHHHHH
37.31Phosphositeplus
Link-
34PhosphoserineSRSRSRDRK
HHHHHHHHC
39.52Phosphositeplus
Link-
53PhosphoserineRDQRSASRD
HHHHHHHHC
25.59HPRD
Link-
53PhosphoserineRDQRSASRD
HHHHHHHHC
25.59PhosphoELM
Link-
53PhosphoserineRDQRSASRD
HHHHHHHHC
25.59Phosphositeplus
Link-
53PhosphoserineRDQRSASRD
HHHHHHHHC
25.59SysPTM
Link-
53Phosphoserine.RDQRSASRD
HHHHHHHHC
25.59UniProtKB
Link-
55PhosphoserineQRSASRDRR
HHHHHHCCC
35.64HPRD
Link-
55PhosphoserineQRSASRDRR
HHHHHHCCC
35.64PhosphoELM
Link-
55PhosphoserineQRSASRDRR
HHHHHHCCC
35.64Phosphositeplus
Link-
55PhosphoserineQRSASRDRR
HHHHHHCCC
35.64SysPTM
Link-
55Phosphoserine.QRSASRDRR
HHHHHHCCC
35.64UniProtKB
Link-
62PhosphoserineRRRRSKPLT
CCCCCCCCC
36.49HPRD
Link-
62PhosphoserineRRRRSKPLT
CCCCCCCCC
36.49PhosphoELM
Link-
62PhosphoserineRRRRSKPLT
CCCCCCCCC
36.49Phosphositeplus
Link-
70N6-acetyllysineTRGAKEEHG
CCCCCCCCC
67.47HPRD
Link-
70N6-acetyllysineTRGAKEEHG
CCCCCCCCC
67.47Phosphositeplus
Link-
70N6-acetyllysine.TRGAKEEHG
CCCCCCCCC
67.47UniProtKB
Link-
79PhosphoserineGLIRSPRHE
CCCCCCCCC
21.20HPRD
Link-
79PhosphoserineGLIRSPRHE
CCCCCCCCC
21.20PhosphoELM
Link-
79PhosphoserineGLIRSPRHE
CCCCCCCCC
21.20Phosphositeplus
Link-
79PhosphoserineGLIRSPRHE
CCCCCCCCC
21.20SysPTM
Link-
79Phosphoserine.GLIRSPRHE
CCCCCCCCC
21.20UniProtKB
Link-
124PhosphothreonineALLPTMTPD
CCCCCCCCC
33.38HPRD
Link-
128Caspase cleavage aspartic acidTMTPDGLAV
CCCCCCCCC
56.42Phosphositeplus
Link-
2765-hydroxylysine; by JMJD6.DDQVKELLT
HHHHHHHHH
36.69UniProtKB
Link-
286Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FGPLKAFNL
CCCEEEEEE
54.81Phosphositeplus
Link-
462N6-acetyllysineVVVTKYCDP
EEEEEECCC
32.07HPRD
Link-
462N6-acetyllysineVVVTKYCDP
EEEEEECCC
32.07Phosphositeplus
Link-
462N6-acetyllysine.VVVTKYCDP
EEEEEECCC
32.07UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ATX1_HUMANphysical interactionMINT-2869830MINT16713569
ATX1_HUMANphysical interactionMINT-2869849MINT16713569
ATX1_HUMANphysical interactionMINT-2855372MINT16713569
SPF45_HUMANdirect interaction
direct interaction
DIP:58780EDIP17589525
17589525
U2AF1_HUMANdirect interactionEBI-1031973
intact11551507
U2AF1_HUMANin vitro
in vivo
HPRD:01872HPRD1388271
41_HUMANin vivoHPRD:01872HPRD9645944
SFRS1_HUMANyeast 2-hybridHPRD:01872HPRD16189514
DVL2_HUMANyeast 2-hybridHPRD:01872HPRD16189514
SRPK2_HUMANyeast 2-hybridHPRD:01872HPRD16189514
CHIC2_HUMANyeast 2-hybridHPRD:01872HPRD16189514
CJ030_HUMANyeast 2-hybridHPRD:01872HPRD16189514
DPPA2_HUMANyeast 2-hybridHPRD:01872HPRD16189514
THAP1_HUMANyeast 2-hybridHPRD:01872HPRD16189514
CA190_HUMANyeast 2-hybridHPRD:01872HPRD16189514
RPAB1_HUMANENSP00000307863STRING
SF3A1_HUMANENSP00000307863STRING
SMD3_HUMANENSP00000307863STRING
NH2L1_HUMANENSP00000307863STRING
RPAB2_HUMANENSP00000307863STRING
PHF5A_HUMANENSP00000307863STRING
PAPOA_HUMANENSP00000307863STRING
SFRS5_HUMANENSP00000307863STRING
PABP2_HUMANENSP00000307863STRING
CSTF1_HUMANENSP00000307863STRING
RPB3_HUMANENSP00000307863STRING
HNRPL_HUMANENSP00000307863STRING
RU17_HUMANENSP00000307863STRING
SF3A2_HUMANENSP00000307863STRING
RPB9_HUMANENSP00000307863STRING
SFRS9_HUMANENSP00000307863STRING
LSM2_HUMANENSP00000307863STRING
PM14_HUMANENSP00000307863STRING
CPSF3_HUMANENSP00000307863STRING
SNRPA_HUMANENSP00000307863STRING
SFRS6_HUMANENSP00000307863STRING
T2FA_HUMANENSP00000307863STRING
RU2B_HUMANENSP00000307863STRING
SF04_HUMANENSP00000307863STRING
FUS_HUMANENSP00000307863STRING
RU2A_HUMANENSP00000307863STRING
SFRS1_HUMANENSP00000307863STRING
U5S1_HUMANENSP00000307863STRING
WDR57_HUMANENSP00000307863STRING
DNJC8_HUMANENSP00000307863STRING
PRP6_HUMANENSP00000307863STRING
RUXF_HUMANENSP00000307863STRING
RUXF_HUMANENSP00000307863STRING
RUXF_HUMANENSP00000307863STRING
PRP16_HUMANENSP00000307863STRING
TXN4A_HUMANENSP00000307863STRING
SF3B4_HUMANENSP00000307863STRING
RUXG_HUMANENSP00000307863STRING
RPB4_HUMANENSP00000307863STRING
REN3B_HUMANENSP00000307863STRING
U2AF1_HUMANENSP00000307863STRING
SFRS2_HUMANENSP00000307863STRING
NXF1_HUMANENSP00000307863STRING
RPAB3_HUMANENSP00000307863STRING
PCF11_HUMANENSP00000307863STRING
CPSF2_HUMANENSP00000307863STRING
CPSF5_HUMANENSP00000307863STRING
SMD1_HUMANENSP00000307863STRING
RPB7_HUMANENSP00000307863STRING
PRP8_HUMANENSP00000307863STRING
PRP17_HUMANENSP00000307863STRING
HNRPR_HUMANENSP00000307863STRING
CLP1_HUMANENSP00000307863STRING
CD2B2_HUMANENSP00000307863STRING
PCBP1_HUMANENSP00000307863STRING
SF3B3_HUMANENSP00000307863STRING
DDX23_HUMANENSP00000307863STRING
RPB2_HUMANENSP00000307863STRING
HNRPD_HUMANENSP00000307863STRING
RPB1_HUMANENSP00000307863STRING
CSTF3_HUMANENSP00000307863STRING
ROA0_HUMANENSP00000307863STRING
U520_HUMANENSP00000307863STRING
SF3B2_HUMANENSP00000307863STRING
SMC1A_HUMANENSP00000307863STRING
RPAB5_HUMANENSP00000307863STRING
HNRPM_HUMANENSP00000307863STRING
SFRS7_HUMANENSP00000307863STRING
NCBP2_HUMANENSP00000307863STRING
WT1_HUMANENSP00000307863STRING
THOC4_HUMANENSP00000307863STRING
SF3B1_HUMANENSP00000307863STRING
HNRPC_HUMANENSP00000307863STRING
CPSF1_HUMANENSP00000307863STRING
SRPK1_HUMANENSP00000307863STRING
ROA1_HUMANENSP00000307863STRING
SMD2_HUMANENSP00000307863STRING
RPAB4_HUMANENSP00000307863STRING
RBM5_HUMANENSP00000307863STRING
CPSF7_HUMANENSP00000307863STRING
HNRPF_HUMANENSP00000307863STRING
T2FB_HUMANENSP00000307863STRING
PCBP2_HUMANENSP00000307863STRING
HNRPK_HUMANENSP00000307863STRING
SCYL2_HUMANENSP00000307863STRING
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Disease Reference
Kegg disease
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
"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-70 AND LYS-462, AND MASSSPECTROMETRY.
Hydroxylation
ReferencePubMed
"Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associatedwith RNA splicing.";
Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B.,Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M.,Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J.,Boettger A.;
Science 325:90-93(2009).
Cited for: FUNCTION, AND HYDROXYLATION AT LYS-15 AND LYS-276.
Phosphorylation
ReferencePubMed
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, 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-2; SER-53; SER-55 ANDSER-79, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, 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-79, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, 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-79, 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-79, 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-2, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures