dbPTM

CCNT_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CCNT_DROME
UniProt AC	O96433
Protein Name	Cyclin-T
Gene Name	CycT
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	1097
Subcellular Localization	Nucleus .
Protein Description	Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNAP II)..
Protein Sequence	MSLLATPMPQAATASSSSSASAAASASGIPITANNNLPFEKDKIWYFSNDQLANSPSRRCGIKGDDELQYRQMTAYLIQEMGQRLQVSQLCINTAIVYMHRFYAFHSFTHFHRNSMASASLFLAAKVEEQPRKLEHVIRAANKCLPPTTEQNYAELAQELVFNENVLLQTLGFDVAIDHPHTHVVRTCQLVKACKDLAQTSYFLASNSLHLTSMCLQYRPTVVACFCIYLACKWSRWEIPQSTEGKHWFYYVDKTVSLDLLKQLTDEFIAIYEKSPARLKSKLNSIKAIAQGASNRTANSKDKPKEDWKITEMMKGYHSNITTPPELLNGNDSRDRDRDRERERERERDPSSLLPPPAMVPQQRRQDGGHQRSSSVSGVPGSSSSSSSSSHKMPNYPGGMPPDAHTDHKSKQPGYNNRMPSSHQRSSSSGLGSSGSGSQRSSSSSSSSSQQPGRPSMPVDYHKSSRGMPPVGVGMPPHGSHKMTSGSKPQQPQQQPVPHPSASNSSASGMSSKDKSQSNKMYPNAPPPYSNSAPQNPLMSRGGYPGASNGSQPPPPAGYGGHRSKSGSTVHGMPPFEQQLPYSQSQSYGHMQQQPVPQSQQQQMPPEASQHSLQSKNSLFSPEWPDIKKEPMSQSQPQPFNGLLPPPAPPGHDYKLNSHPRDKESPKKERLTPTKKDKHRPVMPPVGSGNSSSGSGSSKPMLPPHKKQIPHGGDLLTNPGESGSLKRPNEISGSQYGLNKLDEIDNSNMPREKLRKLDTTTGLPTYPNYEEKHTPLNMSNGIETTPDLVRSLLKESLCPSNASLLKPDALTMPGLKPPAELLEPMPAPATIKKEQGITPMTSLASGPAPMDLEVPTKQAGEIKEESSSKSEKKKKKDKHKHKEKDKSKDKTEKEERKKHKKDKQKDRSGSGGSKDSSLPNEPLKMVIKNPNGSLQAGASAPIKLKISKNKVEPNNYSAAAGLPGAIGYGLPPTTATTTSASIGAAAPVLPPYGAGGGGYSSSGGSSSGGSSKKKHSDRDRDKESKKNKSQDYAKYNGAGGGIFNPLGGAGAAPNMSGGMGAPMSTAVPPSMLLAPTGAVPPSAAGLAPPPMPVYNKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
285	Phosphorylation	RLKSKLNSIKAIAQG HHHHHHHHHHHHHHC	35.58	22817900
297	Phosphorylation	AQGASNRTANSKDKP HHCCCCCCCCCCCCC	34.15	22817900
421	Phosphorylation	GYNNRMPSSHQRSSS CCCCCCCCCCCCCCC	30.98	22817900
438	Phosphorylation	LGSSGSGSQRSSSSS CCCCCCCCCCCCCCC	24.90	21082442
621	Phosphorylation	QSKNSLFSPEWPDIK HHCCCCCCCCCCCCC	27.48	19429919
665	Phosphorylation	SHPRDKESPKKERLT CCCCCCCCCCHHCCC	48.00	19429919
732	Phosphorylation	LKRPNEISGSQYGLN CCCCCCCCCCCCCCH	26.64	21082442
734	Phosphorylation	RPNEISGSQYGLNKL CCCCCCCCCCCCHHH	17.28	21082442
916	Phosphorylation	GSGGSKDSSLPNEPL CCCCCCCCCCCCCCC	37.19	18327897

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 CCNT_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CCNT_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 CCNT_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 CCNT_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-916, AND MASSSPECTROMETRY.	18327897 [Abstract]