SPT5H_MOUSE - dbPTM
SPT5H_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPT5H_MOUSE
UniProt AC O55201
Protein Name Transcription elongation factor SPT5
Gene Name Supt5h
Organism Mus musculus (Mouse).
Sequence Length 1082
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 (By similarity)..
Protein Sequence MSDSEDSNFSEEEDSERSSEAEEAEVEEDQRSAAGSEKEEEPEEEEEEEEEYDEEEEEEDDDRPPKKPRHGGFILDEADVDDEYEDEDQWEDGAEDILEKEEIEASNIDNVVLDEDRSGARRLQNLWRDQREEELGEYYMKKYAKSSVGETVYGGSDELSDDITQQQLLPGVKDPNLWTVKCKIGEERATAISLMRKFIAYQFTDTPLQIKSVVAPEHVKGYIYVEAYKQTHVKQAIEGVGNLRLGYWNQQMVPIKEMTDVLKVVKEVANLKPKSWVRLKRGIYKDDIAQVDYVEPSQNTISLKMIPRIDYDRIKARMSLKDWFAKRKKFKRPPQRLFDAEKIRSLGGDVASDGDFLIFEGNRYSRKGFLFKSFAMSAVITEGVKPTLSELEKFEDQPEGIDLEVVTESTGKEREHNFQPGDNVEVCEGELINLQGKVLSVDGNKITIMPKHEDLKDMLEFPAQELRKYFKMGDHVKVIAGRFEGDTGLIVRVEENFVILFSDLTMHELKVLPRDLQLCSETASGVDVGGQHEWGELVQLDPRTVGVIVRLERETFQVLNMHGKVVTVRHQAVTQKKDNRFAVALDSDQNNIHVKDIVKVIDGPHSGREGEIRHLYRSFAFLHCKKLVENGGMFVCKARHLVLAGGSKPRDVTNLTVGGFTPMSPRISSPMHPSAEGQHGGFGSPGGMSRGRGRRDNELIGQTVRISQGPYKGYIGVVKDATESTARVELHSTCQTISVDRQRLTTVDSQRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQSGAWDPNNPNTPSRAEEEYEYAFDDEPTPSPQAYGGTPNPQTPGYPDPSSPQVNPQYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSPVGYSPMTPGAPSPGGYNPHTPGSGIEQNSSDWVTTDIQVKVRDTYLDTQIVGQTGVIRSVTGGMCSVYLKDSEKVVSISSEHLEPITPTKNNKVKVILGEDREATGVLLSIDGEDGIIRMDLEDQQIKILNLRFLGKLLEA
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
2Phosphorylation------MSDSEDSNF
------CCCCCCCCC		62.24-
4Phosphorylation----MSDSEDSNFSE
----CCCCCCCCCCH		53.23-
7Phosphorylation-MSDSEDSNFSEEED
-CCCCCCCCCCHHHH		35.41-
15PhosphorylationNFSEEEDSERSSEAE
CCCHHHHHHHHHHHH		37.8825293948
18PhosphorylationEEEDSERSSEAEEAE
HHHHHHHHHHHHHHH		28.6025293948
19PhosphorylationEEDSERSSEAEEAEV
HHHHHHHHHHHHHHH		47.2325293948
32PhosphorylationEVEEDQRSAAGSEKE
HHHHHHHHHCCCCCC		19.4823684622
36PhosphorylationDQRSAAGSEKEEEPE
HHHHHCCCCCCCCCC		40.5425521595
52PhosphorylationEEEEEEEYDEEEEEE
HHHHHHHCCHHHHHC		31.7525619855
138PhosphorylationREEELGEYYMKKYAK
HHHHHHHHHHHHHHH		13.6826643407
139PhosphorylationEEELGEYYMKKYAKS
HHHHHHHHHHHHHHC		9.7326643407
156PhosphorylationGETVYGGSDELSDDI
CCCCCCCCCCCCCCC		24.4525338131
211UbiquitinationTDTPLQIKSVVAPEH
CCCCEEEEEEECCCH		25.0022790023
293PhosphorylationDDIAQVDYVEPSQNT
CCCCCCCEECCCCCE		14.09-
352PhosphorylationSLGGDVASDGDFLIF
HCCCCCCCCCCEEEE		41.8126525534
648UbiquitinationLVLAGGSKPRDVTNL
EEECCCCCCCCCCCC		47.5522790023
653PhosphorylationGSKPRDVTNLTVGGF
CCCCCCCCCCEECCC		28.8825619855
656PhosphorylationPRDVTNLTVGGFTPM
CCCCCCCEECCCCCC		21.1224925903
661PhosphorylationNLTVGGFTPMSPRIS
CCEECCCCCCCCCCC		22.7424925903
664PhosphorylationVGGFTPMSPRISSPM
ECCCCCCCCCCCCCC		16.5424925903
668PhosphorylationTPMSPRISSPMHPSA
CCCCCCCCCCCCCCC		29.6624453211
669PhosphorylationPMSPRISSPMHPSAE
CCCCCCCCCCCCCCC		24.7021082442
674PhosphorylationISSPMHPSAEGQHGG
CCCCCCCCCCCCCCC		25.0325159016
684PhosphorylationGQHGGFGSPGGMSRG
CCCCCCCCCCCCCCC		20.3625159016
689PhosphorylationFGSPGGMSRGRGRRD
CCCCCCCCCCCCCCC		34.5525159016
690MethylationGSPGGMSRGRGRRDN
CCCCCCCCCCCCCCC		29.9024129315
690Asymmetric dimethylarginineGSPGGMSRGRGRRDN
CCCCCCCCCCCCCCC		29.90-
692MethylationPGGMSRGRGRRDNEL
CCCCCCCCCCCCCCC		34.04-
692Asymmetric dimethylargininePGGMSRGRGRRDNEL
CCCCCCCCCCCCCCC		34.04-
708UbiquitinationGQTVRISQGPYKGYI
CCEEEECCCCCCCEE		55.2827667366
712UbiquitinationRISQGPYKGYIGVVK
EECCCCCCCEEEEEE		48.6622790023
712AcetylationRISQGPYKGYIGVVK
EECCCCCCCEEEEEE		48.6623806337
715UbiquitinationQGPYKGYIGVVKDAT
CCCCCCEEEEEEECC		4.6227667366
719UbiquitinationKGYIGVVKDATESTA
CCEEEEEEECCCCCE		38.9622790023
745PhosphorylationSVDRQRLTTVDSQRP
EECCCEEEEECCCCC		27.2822802335
756PhosphorylationSQRPGGMTSTYGRTP
CCCCCCCCCCCCCCC		22.6126060331
757PhosphorylationQRPGGMTSTYGRTPM
CCCCCCCCCCCCCCC		15.6726060331
758PhosphorylationRPGGMTSTYGRTPMY
CCCCCCCCCCCCCCC		22.3426060331
762PhosphorylationMTSTYGRTPMYGSQT
CCCCCCCCCCCCCCC		14.1926643407
765PhosphorylationTYGRTPMYGSQTPMY
CCCCCCCCCCCCCCC		18.1526643407
767PhosphorylationGRTPMYGSQTPMYGS
CCCCCCCCCCCCCCC		17.2526643407
769PhosphorylationTPMYGSQTPMYGSGS
CCCCCCCCCCCCCCC		16.2426643407
772PhosphorylationYGSQTPMYGSGSRTP
CCCCCCCCCCCCCCC		14.8926643407
774PhosphorylationSQTPMYGSGSRTPMY
CCCCCCCCCCCCCCC		18.9926643407
776PhosphorylationTPMYGSGSRTPMYGS
CCCCCCCCCCCCCCC		34.3826643407
778PhosphorylationMYGSGSRTPMYGSQT
CCCCCCCCCCCCCCC		17.6923527152
781PhosphorylationSGSRTPMYGSQTPLQ
CCCCCCCCCCCCCCC		18.1526643407
783PhosphorylationSRTPMYGSQTPLQDG
CCCCCCCCCCCCCCC		17.2526643407
785PhosphorylationTPMYGSQTPLQDGSR
CCCCCCCCCCCCCCC		27.8828507225
791PhosphorylationQTPLQDGSRTPHYGS
CCCCCCCCCCCCCCC		41.0726643407
793PhosphorylationPLQDGSRTPHYGSQT
CCCCCCCCCCCCCCC		19.0026643407
796PhosphorylationDGSRTPHYGSQTPLH
CCCCCCCCCCCCCCC		21.4825777480
798PhosphorylationSRTPHYGSQTPLHDG
CCCCCCCCCCCCCCC		24.5826239621
800PhosphorylationTPHYGSQTPLHDGSR
CCCCCCCCCCCCCCC		29.5226824392
806PhosphorylationQTPLHDGSRTPAQSG
CCCCCCCCCCCCCCC		38.7526643407
808PhosphorylationPLHDGSRTPAQSGAW
CCCCCCCCCCCCCCC		25.3625619855
822PhosphorylationWDPNNPNTPSRAEEE
CCCCCCCCCCHHHHH		24.7328066266
824PhosphorylationPNNPNTPSRAEEEYE
CCCCCCCCHHHHHHH		41.9228066266
1011AcetylationGMCSVYLKDSEKVVS
CEEEEEECCCCCEEE		41.3322826441
1018PhosphorylationKDSEKVVSISSEHLE
CCCCCEEEEECCCCC		21.5325619855
1020PhosphorylationSEKVVSISSEHLEPI
CCCEEEEECCCCCCC		23.3625619855
1021PhosphorylationEKVVSISSEHLEPIT
CCEEEEECCCCCCCC		27.6325619855
1028PhosphorylationSEHLEPITPTKNNKV
CCCCCCCCCCCCCEE		35.3026824392
1030PhosphorylationHLEPITPTKNNKVKV
CCCCCCCCCCCEEEE		37.4422942356
1031UbiquitinationLEPITPTKNNKVKVI
CCCCCCCCCCEEEEE		60.7822790023
1078AcetylationLNLRFLGKLLEA---
EEHHHHHHHHCC---		52.6323236377
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
664SPhosphorylationKinaseMAPK1P63085
GPS
769TPhosphorylationKinaseCDK9Q99J95
Uniprot
778TPhosphorylationKinaseCDK9Q99J95
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPT5H_MOUSE !!
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 SPT5H_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DREB_HUMANDBN1physical
16169070
S30BP_HUMANSAP30BPphysical
16169070
TLS1_HUMANC9orf78physical
16169070
TF3C1_HUMANGTF3C1physical
16169070
RED_HUMANIKphysical
16169070
PNO1_HUMANPNO1physical
16169070
PHYIP_HUMANPHYHIPphysical
16169070
PPIA_HUMANPPIAphysical
16169070
2ABD_MOUSEPpp2r2dphysical
16169070
CE126_HUMANKIAA1377physical
16169070
RL8_HUMANRPL8physical
16169070
MED31_HUMANMED31physical
16169070
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPT5H_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-793, AND MASSSPECTROMETRY.

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