U2AF4_HUMAN - dbPTM
U2AF4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID U2AF4_HUMAN
UniProt AC Q8WU68
Protein Name Splicing factor U2AF 26 kDa subunit
Gene Name U2AF1L4
Organism Homo sapiens (Human).
Sequence Length 220
Subcellular Localization Nucleus . Nucleus speckle . Cytoplasm . Interaction with C1QBP is required for the nuclear translocation. Displays active nucleo-cytoplasmic shuttling.
Protein Description RNA-binding protein that function as a pre-mRNA splicing factor. 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. Acts by enhancing the binding of U2AF2 to weak pyrimidine tracts. Also participates in the regulation of alternative pre-mRNA splicing. Activates exon 5 skipping of PTPRC during T-cell activation; an event reversed by GFI1. Binds to RNA at the AG dinucleotide at the 3'-splice site (By similarity). Shows a preference for AGC or AGA (By similarity)..
Protein Sequence MAEYLASIFGTEKDKVNCSFYFKIGVCRHGDRCSRLHNKPTFSQTIVLLNLYRNPQNTAQTADGSHCHVSDVEVQEHYDSFFEEVFTELQEKYGEIEEMNVCDNLGDHLVGNVYVKFRREEDGERAVAELSNRWFNGQAVHGELSPVTDFRESCCRQYEMGECTRGGFCNFMHLRPISQNLQRQLYGRGPRRRSPPRFHTGHHPRERNHRCSPDHWHGRF
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
63.7954427329
13UbiquitinationASIFGTEKDKVNCSF
HHHHCCCCCCCCCEE
63.7923000965
15SumoylationIFGTEKDKVNCSFYF
HHCCCCCCCCCEEEE
46.55-
15UbiquitinationIFGTEKDKVNCSFYF
HHCCCCCCCCCEEEE
46.5523000965
19PhosphorylationEKDKVNCSFYFKIGV
CCCCCCCEEEEEEEE
20.1326055452
21PhosphorylationDKVNCSFYFKIGVCR
CCCCCEEEEEEEECC
6.4128152594
126PhosphorylationREEDGERAVAELSNR
EHHCCHHHHHHHHHC
10.6924719451
126 (in isoform 2)Phosphorylation-10.6924719451
144PhosphorylationGQAVHGELSPVTDFR
CCCCCCCCCCCCCHH
9.2024719451
144 (in isoform 2)Phosphorylation-9.2024719451
158PhosphorylationRESCCRQYEMGECTR
HHHHCCHHCCCCCCC
6.6324043423
164PhosphorylationQYEMGECTRGGFCNF
HHCCCCCCCCCCCCE
28.2224043423
165MethylationYEMGECTRGGFCNFM
HCCCCCCCCCCCCEE
55.7058860221
194PhosphorylationGRGPRRRSPPRFHTG
CCCCCCCCCCCCCCC
37.1320068231

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 U2AF4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of U2AF4_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 U2AF4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of U2AF4_HUMAN !!

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 U2AF4_HUMAN

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Related Literatures of Post-Translational Modification

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