U2AF1_HUMAN - dbPTM
U2AF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID U2AF1_HUMAN
UniProt AC Q01081
Protein Name Splicing factor U2AF 35 kDa subunit
Gene Name U2AF1
Organism Homo sapiens (Human).
Sequence Length 240
Subcellular Localization Nucleus . Nucleus speckle .
Protein Description Plays a critical role in both constitutive and enhancer-dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Recruits U2 snRNP to the branch point. Directly mediates interactions between U2AF2 and proteins bound to the enhancers and thus may function as a bridge between U2AF2 and the enhancer complex to recruit it to the adjacent intron..
Protein Sequence MAEYLASIFGTEKDKVNCSFYFKIGACRHGDRCSRLHNKPTFSQTIALLNIYRNPQNSSQSADGLRCAVSDVEMQEHYDEFFEEVFTEMEEKYGEVEEMNVCDNLGDHLVGNVYVKFRREEDAEKAVIDLNNRWFNGQPIHAELSPVTDFREACCRQYEMGECTRGGFCNFMHLKPISRELRRELYGRRRKKHRSRSRSRERRSRSRDRGRGGGGGGGGGGGGRERDRRRSRDRERSGRF
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------MAEYLASIF
------CHHHHHHHH		17.72-
4Phosphorylation----MAEYLASIFGT
----CHHHHHHHHCC		9.6825106551
7Phosphorylation-MAEYLASIFGTEKD
-CHHHHHHHHCCCCC		18.8221955146
11PhosphorylationYLASIFGTEKDKVNC
HHHHHHCCCCCCCCC		29.1621955146
13AcetylationASIFGTEKDKVNCSF
HHHHCCCCCCCCCEE		63.7954427321
13UbiquitinationASIFGTEKDKVNCSF
HHHHCCCCCCCCCEE		63.7923000965
15SumoylationIFGTEKDKVNCSFYF
HHCCCCCCCCCEEEE		46.55-
15UbiquitinationIFGTEKDKVNCSFYF
HHCCCCCCCCCEEEE		46.5523000965
15SumoylationIFGTEKDKVNCSFYF
HHCCCCCCCCCEEEE		46.55-
152-HydroxyisobutyrylationIFGTEKDKVNCSFYF
HHCCCCCCCCCEEEE		46.55-
19PhosphorylationEKDKVNCSFYFKIGA
CCCCCCCEEEEEECC		20.1325159151
21PhosphorylationDKVNCSFYFKIGACR
CCCCCEEEEEECCCC		6.4128152594
23UbiquitinationVNCSFYFKIGACRHG
CCCEEEEEECCCCCC		28.9332015554
34PhosphorylationCRHGDRCSRLHNKPT
CCCCCHHHHHCCCCC		38.48-
39MethylationRCSRLHNKPTFSQTI
HHHHHCCCCCHHHHH		34.3924129315
39 (in isoform 3)Methylation-34.3924129315
39 (in isoform 2)Methylation-34.3924129315
43UbiquitinationLHNKPTFSQTIALLN
HCCCCCHHHHHHHHH		28.9729967540
45 (in isoform 3)Phosphorylation-13.6620049867
45 (in isoform 2)Phosphorylation-13.6620049867
52UbiquitinationTIALLNIYRNPQNSS
HHHHHHHHCCCCCCC		11.8522053931
52 (in isoform 3)Phosphorylation-11.8520049867
52 (in isoform 2)Phosphorylation-11.8520049867
58PhosphorylationIYRNPQNSSQSADGL
HHCCCCCCCCCCCCC		25.2229255136
59PhosphorylationYRNPQNSSQSADGLR
HCCCCCCCCCCCCCE		35.3917525332
61PhosphorylationNPQNSSQSADGLRCA
CCCCCCCCCCCCEEC		30.2129255136
70PhosphorylationDGLRCAVSDVEMQEH
CCCEECEECHHHHHH		19.8820058876
78UbiquitinationDVEMQEHYDEFFEEV
CHHHHHHHHHHHHHH		19.2029967540
87UbiquitinationEFFEEVFTEMEEKYG
HHHHHHHHHHHHHHC		39.3322053931
87PhosphorylationEFFEEVFTEMEEKYG
HHHHHHHHHHHHHHC		39.3320058876
92UbiquitinationVFTEMEEKYGEVEEM
HHHHHHHHHCCCEEE		45.2922053931
92SumoylationVFTEMEEKYGEVEEM
HHHHHHHHHCCCEEE		45.29-
93PhosphorylationFTEMEEKYGEVEEMN
HHHHHHHHCCCEEEE		23.07-
102UbiquitinationEVEEMNVCDNLGDHL
CCEEEEECCCCCCCC		2.1423000965
102UbiquitinationEVEEMNVCDNLGDHL
CCEEEEECCCCCCCC		2.1421890473
116UbiquitinationLVGNVYVKFRREEDA
CEEEEEEEEECHHHH		18.5729967540
125UbiquitinationRREEDAEKAVIDLNN
ECHHHHHHHEEECCC		50.0722053931
1252-HydroxyisobutyrylationRREEDAEKAVIDLNN
ECHHHHHHHEEECCC		50.07-
137UbiquitinationLNNRWFNGQPIHAEL
CCCCEECCCCCEEEC		25.7623000965
142UbiquitinationFNGQPIHAELSPVTD
ECCCCCEEECCCCCC		21.8321890473
145PhosphorylationQPIHAELSPVTDFRE
CCCEEECCCCCCHHH		14.6125159151
148PhosphorylationHAELSPVTDFREACC
EEECCCCCCHHHHHH		32.5730108239
158PhosphorylationREACCRQYEMGECTR
HHHHHHHHHCCCCCC		6.6324043423
164PhosphorylationQYEMGECTRGGFCNF
HHHCCCCCCCCCCCC		28.2224043423
165MethylationYEMGECTRGGFCNFM
HHCCCCCCCCCCCCE		55.7024129315
175SumoylationFCNFMHLKPISRELR
CCCCEECCCCCHHHH		26.15-
175UbiquitinationFCNFMHLKPISRELR
CCCCEECCCCCHHHH		26.1523000965
175SumoylationFCNFMHLKPISRELR
CCCCEECCCCCHHHH		26.15-
175AcetylationFCNFMHLKPISRELR
CCCCEECCCCCHHHH		26.1544508057
175MethylationFCNFMHLKPISRELR
CCCCEECCCCCHHHH		26.1544508057
175UbiquitinationFCNFMHLKPISRELR
CCCCEECCCCCHHHH		26.1521890473
178PhosphorylationFMHLKPISRELRREL
CEECCCCCHHHHHHH		28.3827251275
179MethylationMHLKPISRELRRELY
EECCCCCHHHHHHHH		47.92-
195PhosphorylationRRRKKHRSRSRSRER
HHHHHHHHHHHHHHH		34.0417081983
197PhosphorylationRKKHRSRSRSRERRS
HHHHHHHHHHHHHHH		35.5420068231
199PhosphorylationKHRSRSRSRERRSRS
HHHHHHHHHHHHHHH		39.4820068231
204PhosphorylationSRSRERRSRSRDRGR
HHHHHHHHHHCCCCC		40.6120068231
206PhosphorylationSRERRSRSRDRGRGG
HHHHHHHHCCCCCCC		39.5220068231
209MethylationRRSRSRDRGRGGGGG
HHHHHCCCCCCCCCC		35.2880700633
211MethylationSRSRDRGRGGGGGGG
HHHCCCCCCCCCCCC		41.2980700625
231PhosphorylationRERDRRRSRDRERSG
HHHHHHHHCHHHHHC		36.4020068231
237PhosphorylationRSRDRERSGRF----
HHCHHHHHCCC----		29.5730576142
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 U2AF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of U2AF1_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 U2AF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
U2AF2_HUMANU2AF2physical
16189514
RP9_HUMANRP9physical
15474994
U2AF2_HUMANU2AF2physical
1388271
U2AF2_HUMANU2AF2physical
22939629
ZCHC8_HUMANZCCHC8physical
22939629
DCAF1_HUMANVPRBPphysical
22939629
SMD1_HUMANSNRPD1physical
22365833
PR40A_HUMANPRPF40Aphysical
22365833
SF3B2_HUMANSF3B2physical
22365833
U2AF2_HUMANU2AF2physical
22365833
CHERP_HUMANCHERPphysical
22365833
RBM10_HUMANRBM10physical
22365833
PRP4_HUMANPRPF4physical
22365833
PR38A_HUMANPRPF38Aphysical
22365833
PRP19_HUMANPRPF19physical
22365833
MFAP1_HUMANMFAP1physical
22365833
PRP16_HUMANDHX38physical
22365833
RNPS1_HUMANRNPS1physical
22365833
F10C1_HUMANFRA10AC1physical
22365833
SRSF2_HUMANSRSF2physical
22365833
NKAP_HUMANNKAPphysical
22365833
TOE1_HUMANTOE1physical
22365833
ZCH10_HUMANZCCHC10physical
22365833
PABP1_HUMANPABPC1physical
22365833
SRPK1_HUMANSRPK1physical
22365833
SRPK2_HUMANSRPK2physical
22365833
IL7RA_HUMANIL7Rphysical
23151878
CIR1_HUMANCIR1physical
15652350
JMJD6_HUMANJMJD6physical
23455924
SUV91_HUMANSUV39H1physical
23455924
VEGFA_HUMANVEGFAphysical
21988832
U2AF2_HUMANU2AF2physical
21988832
RNPS1_HUMANRNPS1physical
25416956
U2AF2_HUMANU2AF2physical
25416956
SPB1_HUMANFTSJ3physical
26344197
U2AF2_HUMANU2AF2physical
26344197
U2AF2_HUMANU2AF2physical
28514442
SCAFB_HUMANSCAF11physical
28514442
SRPK2_HUMANSRPK2physical
28514442
SRPK1_HUMANSRPK1physical
28514442
JMJD6_HUMANJMJD6physical
28514442
U2AF4_HUMANU2AF1L4physical
28514442
CARME_HUMANC9orf41physical
28514442
ACINU_HUMANACIN1physical
28514442
GSK3B_HUMANGSK3Bphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of U2AF1_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.
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-59, 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-195 AND SER-197, ANDMASS SPECTROMETRY.

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