dbPTM

SPT6H_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPT6H_DROME
UniProt AC	Q9W420
Protein Name	Transcription elongation factor SPT6
Gene Name	Spt6
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	1831
Subcellular Localization	Nucleus . Recruited to sites of active transcription where it colocalizes with the elongating form of RNA polymerase II.
Protein Description	Transcription elongation factor which binds histone H3 and enhances transcription elongation by RNA polymerase II (RNAPII). Required for the transcriptional induction of heat shock response genes and for maximal recruitment of two other elongation factors, Spt5 and Paf1, to the induced Hsp70. Plays a critical role in normal fly development throughout the lifecycle..
Protein Sequence	MAEFLDSEAEESEEEEELDVNERKRLKKLKAAVSDSSEEEEDDEERLREELKDLIDDNPIEEDDGSGYDSDGVGSGKKRKKHEDDDLDDRLEDDDYDLIEENLGVKVERRKRFKRLRRIHDNESDGEEQHVDEGLVREQIAEQLFDENDESIGHRSERSHREADDYDDVDTESDADDFIVDDNGRPIAEKKKKRRPIFTDASLQEGQDIFGVDFDYDDFSKYEEDDYEDDSEGDEYDEDLGVGDDTRVKKKKALKKKVVKKTIFDIYEPSELKRGHFTDMDNEIRKTDIPERMQLREVPVTPVPEGSDELDLEAEWIYKYAFCKHTVSEQEKPESREKMRKPPTTVNKIKQTLEFIRNQQLEVPFIAFYRKEYVKPELNIDDLWKVYYYDGIWCQLNERKRKLKVLFEKMRQFQLDTLCADTDQPVPDDVRLILDSDFERLADVQSMEELKDVHMYFLLNYSHELPRMQAEQRRKAIQERREAKARRQAAAAENGDDAAEAIVVPEPEDDDDPELIDYQLKQASNSSPYAVFRKAGICGFAKHFGLTPEQYAENLRDNYQRNEITQESIGPTELAKQYLSPRFMTTDEVIHAAKYVVARQLAQEPLLRKTMREVYFDRARINIRPTKNGMVLIDENSPVYSMKYVAKKPVSDLFGDQFIKLMMAEEEKLLEITFLEEFEGNACANGTPGDYVEESKALYQLDQFAKHVQEWNKLRAECVQLALQKWVIPDLIKELRSTLHEEAQQFVLRSCTGKLYKWLKVAPYKPQLPPDFGYEEWSTLRGIRVLGLAYDPDHSVAAFCAVTTVEGDISDYLRLPNILKRKNSYNLEEKAQKLADLRKLSDFIKMKKPHIVVIGAESRDAQNIQADIKEILHELETSEQFPPIEVEIIDNELAKIYANSKKGESDFKEYPPLLKQAASLARKMQDPLVEYSQLCDADDEILCLRYHPLQERVPREQLLEQLSLQFINRTSEVGLDINLMVQNSRTINLLQYICGLGPRKGQALLKLLKQSNQRLENRTQLVTVCHLGPRVFINCSGFIKIDTSSLGDSTEAYVEVLDGSRVHPETYEWARKMAIDAMEYDDEETNPAGALEEILESPERLKDLDLDAFAVELERQGFGSKSITLYDIRNELSCLYKDYRTPYTKPSAEELFDMLTKETPDSFYVGKCVTAMVTGFTYRRPQGDQLDSANPVRLDSNESWQCPFCHKDDFPELSEVWNHFDANACPGQPSGVRVRLENGLPGFIHIKNLSDRQVRNPEERVRVSQMIHVRIIKIDIDRFSVECSSRTADLKDVNNEWRPRRDNYYDYVTEEQDNRKVSDAKARALKRKIYARRVIAHPSFFNKSYAEVVAMLAEADQGEVALRPSSKSKDHLTATWKVADDIFQHIDVREEGKENDFSLGRSLWIGTEEFEDLDEIIARHIMPMALAARELIQYKYYKPNMVTGDENERDVMEKLLREEKANDPKKIHYFFTASRAMPGKFLLSYLPKTKVRHEYVTVMPEGYRFRGQIFDTVNSLLRWFKEHWLDPTATPASASASNLTPLHLMRPPPTISSSSQTSLGPQAPYSVTGSVTGGTPRSGISSAVGGGGSSAYSITQSITGYGTSGSSAPGAGVSSSHYGSSSTPSFGAINTPYTPSGQTPFMTPYTPHASQTPRYGHNVPSPSSQSSSSQRHHYGSSSGTGSTPRYHDMGGGGGGGVGGGGGSNAYSMQPHHQQRAKENLDWQLANDAWARRRPQQHQSHQSYHAQQQHHHSQQQPHMGMSMNMGITMSLGRGTGGGGGGGYGSTPVNDYSTGGGHNRGMSSKASVRSTPRTNASPHSMNLGDATPLYDEN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MAEFLDSEAEESEE -CCCCCCHHHHCCHH	40.63	19429919
12	Phosphorylation	LDSEAEESEEEEELD CCHHHHCCHHHHCCC	41.64	19429919
34	Phosphorylation	KKLKAAVSDSSEEEE HHHHHHHCCCCCCCC	27.35	19429919
36	Phosphorylation	LKAAVSDSSEEEEDD HHHHHCCCCCCCCCH	31.95	19429919
37	Phosphorylation	KAAVSDSSEEEEDDE HHHHCCCCCCCCCHH	54.76	19429919
66	Phosphorylation	PIEEDDGSGYDSDGV CCCCCCCCCCCCCCC	40.97	19429919
68	Phosphorylation	EEDDGSGYDSDGVGS CCCCCCCCCCCCCCC	17.61	19429919
70	Phosphorylation	DDGSGYDSDGVGSGK CCCCCCCCCCCCCCC	27.99	19429919
75	Phosphorylation	YDSDGVGSGKKRKKH CCCCCCCCCCCCCCC	45.06	19429919
124	Phosphorylation	RRIHDNESDGEEQHV HHHCCCCCCCCCCCC	58.11	21082442
151	Phosphorylation	LFDENDESIGHRSER HCCCCCCCCCCHHHC	36.41	19429919
156	Phosphorylation	DESIGHRSERSHREA CCCCCCHHHCCCCCC	31.52	19429919
159	Phosphorylation	IGHRSERSHREADDY CCCHHHCCCCCCCCC	23.89	22817900
166	Phosphorylation	SHREADDYDDVDTES CCCCCCCCCCCCCCC	18.00	22817900
171	Phosphorylation	DDYDDVDTESDADDF CCCCCCCCCCCCCCE	36.92	19429919
173	Phosphorylation	YDDVDTESDADDFIV CCCCCCCCCCCCEEE	39.94	19429919
231	Phosphorylation	EDDYEDDSEGDEYDE CCCCCCCCCCCCCCC	56.66	19429919
824	Phosphorylation	NILKRKNSYNLEEKA HHHHHCCCCCHHHHH	20.59	22817900
1655	Phosphorylation	HASQTPRYGHNVPSP CHHCCCCCCCCCCCC	24.76	21082442
1661	Phosphorylation	RYGHNVPSPSSQSSS CCCCCCCCCCCCCCC	32.88	25749252
1664	Phosphorylation	HNVPSPSSQSSSSQR CCCCCCCCCCCCCCC	37.15	22817900
1680	Phosphorylation	HYGSSSGTGSTPRYH CCCCCCCCCCCCCCC	29.88	21082442
1682	Phosphorylation	GSSSGTGSTPRYHDM CCCCCCCCCCCCCCC	34.77	21082442
1683	Phosphorylation	SSSGTGSTPRYHDMG CCCCCCCCCCCCCCC	17.09	21082442
1805	Phosphorylation	RGMSSKASVRSTPRT CCCCCCCCCCCCCCC	23.07	25749252
1808	Phosphorylation	SSKASVRSTPRTNAS CCCCCCCCCCCCCCC	40.38	25749252
1812	Phosphorylation	SVRSTPRTNASPHSM CCCCCCCCCCCCCCC	36.02	19429919
1815	Phosphorylation	STPRTNASPHSMNLG CCCCCCCCCCCCCCC	25.80	19429919
1818	Phosphorylation	RTNASPHSMNLGDAT CCCCCCCCCCCCCCC	16.86	22668510
1825	Phosphorylation	SMNLGDATPLYDEN- CCCCCCCCCCCCCC-	20.68	19429919

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 SPT6H_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SPT6H_DROME !!

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 SPT6H_DROME !!

Protein-Protein Interaction

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

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SPT6H_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-36; SER-37;SER-66; SER-70; SER-75; SER-151; SER-156; SER-159; THR-171; SER-173;SER-1661; SER-1664 AND SER-1815, AND MASS SPECTROMETRY.	18327897 [Abstract]
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND MASSSPECTROMETRY.	17372656 [Abstract]