SPT4H_HUMAN - dbPTM
SPT4H_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPT4H_HUMAN
UniProt AC P63272
Protein Name Transcription elongation factor SPT4
Gene Name SUPT4H1
Organism Homo sapiens (Human).
Sequence Length 117
Subcellular Localization Nucleus .
Protein Description Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences..
Protein Sequence MALETVPKDLRHLRACLLCSLVKTIDQFEYDGCDNCDAYLQMKGNREMVYDCTSSSFDGIIAMMSPEDSWVSKWQRVSNFKPGVYAVSVTGRLPQGIVRELKSRGVAYKSRDTAIKT
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------MALETVPKD
------CCCCCCCHH
17.6922814378
5Phosphorylation---MALETVPKDLRH
---CCCCCCCHHHHH
42.8522985185
8UbiquitinationMALETVPKDLRHLRA
CCCCCCCHHHHHHHH
66.1223000965
43UbiquitinationCDAYLQMKGNREMVY
CHHEEEECCCCCCEE
39.8222817900
56PhosphorylationVYDCTSSSFDGIIAM
EEECCCCCCCEEEEE
27.42-
78PhosphorylationVSKWQRVSNFKPGVY
HHCCEEHHCCCCCEE
38.44-
81UbiquitinationWQRVSNFKPGVYAVS
CEEHHCCCCCEEEEE
45.1523000965
85PhosphorylationSNFKPGVYAVSVTGR
HCCCCCEEEEEEECC
13.7529496907
108PhosphorylationLKSRGVAYKSRDTAI
HHHCCCEEECCCCCC
13.6923532336
109AcetylationKSRGVAYKSRDTAIK
HHCCCEEECCCCCCC
29.3125953088
109UbiquitinationKSRGVAYKSRDTAIK
HHCCCEEECCCCCCC
29.3127667366
110PhosphorylationSRGVAYKSRDTAIKT
HCCCEEECCCCCCCC
23.7823532336

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 SPT4H_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPT4H_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 SPT4H_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPT5H_HUMANSUPT5Hphysical
19860741
NSG2_HUMANHMP19physical
21900206
PDLI1_HUMANPDLIM1physical
21900206
LRIF1_HUMANLRIF1physical
21900206
A4_HUMANAPPphysical
21832049
SPT5H_HUMANSUPT5Hphysical
22939629
TAT_HV1H2tatphysical
11112772

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 SPT4H_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP