TXN4A_HUMAN - dbPTM
TXN4A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TXN4A_HUMAN
UniProt AC P83876
Protein Name Thioredoxin-like protein 4A
Gene Name TXNL4A
Organism Homo sapiens (Human).
Sequence Length 142
Subcellular Localization Nucleus .
Protein Description Essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes that are involved in spliceosome assembly..
Protein Sequence MSYMLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCTVMFFFRNKHIMIDLGTGNNNKINWAMEDKQEMVDIIETVYRGARKGRGLVVSPKDYSTKYRY
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
46PhosphorylationMKMDEVLYSIAEKVK
HCHHHHHHHHHHHHC
11.82-
47PhosphorylationKMDEVLYSIAEKVKN
CHHHHHHHHHHHHCC
15.91-
51UbiquitinationVLYSIAEKVKNFAVI
HHHHHHHHHCCEEEE
49.8721890473
51AcetylationVLYSIAEKVKNFAVI
HHHHHHHHHCCEEEE
49.8725953088
73PhosphorylationVPDFNKMYELYDPCT
CCCHHHHHHHCCCCE
12.3722817900
76PhosphorylationFNKMYELYDPCTVMF
HHHHHHHCCCCEEEE
13.10-
132PhosphorylationKGRGLVVSPKDYSTK
CCCCEEECCCCCCCC
20.8223401153
132O-linked_GlycosylationKGRGLVVSPKDYSTK
CCCCEEECCCCCCCC
20.8229351928
134UbiquitinationRGLVVSPKDYSTKYR
CCEEECCCCCCCCCC
62.8921890473
136PhosphorylationLVVSPKDYSTKYRY-
EEECCCCCCCCCCC-
25.1126270265
137PhosphorylationVVSPKDYSTKYRY--
EECCCCCCCCCCC--
28.6723312004
138PhosphorylationVSPKDYSTKYRY---
ECCCCCCCCCCC---
26.3526270265
139UbiquitinationSPKDYSTKYRY----
CCCCCCCCCCC----
23.0721890473
139AcetylationSPKDYSTKYRY----
CCCCCCCCCCC----
23.0725953088

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 TXN4A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TXN4A_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 TXN4A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
REBL1_HUMANRHEBL1physical
16189514
HNRPF_HUMANHNRNPFphysical
11054566
PQBP1_HUMANPQBP1physical
11054566
PRP6_HUMANPRPF6physical
16723661
WDFY1_HUMANWDFY1physical
22939629
LZTS2_HUMANLZTS2physical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608572Burn-McKeown syndrome (BMKS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TXN4A_HUMAN

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Related Literatures of Post-Translational Modification
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-132, 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-132, AND MASSSPECTROMETRY.

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