YJ41B_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: YJ41B_YEAST
• UniProt AC: P47024
• Protein Name: Transposon Ty4-J Gag-Pol polyprotein
• Gene Name: TY4B-J
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 1803
• Subcellular Localization: Cytoplasm. Nucleus.
• Protein Description: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome.; The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.; Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).; Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity)..
• Protein Sequence: MATPVRGETRNVIDDNISARIQSKVKTNDTVRQTPSSLRKVSIKDEQVRQYQRNLNRFKTILNGLKAEEEKLSEADDIQMLAEKLLKLGETIDKVENRIVDLVEKIQLLETNENNNILHEHIDATGTYYLFDTLTSTNKRFYPKDCVFDYRTNNVENIPILLNNFKKFIKKYQFDDVFENDIIEIDPRENEILCKIIKEGLGESLDIMNTNTTDIFRIIDGLKKQNIEVCMVEMSELEPGEKVLVDTTCRNSALLMNKLQKLVLMEKWIFSKCCQDCPNLKDYLQEAIMGTLHESLRNSVKQRLYNIPHDVGIDHEEFLINTVIETVIDLSPIADDQIENSCMYCKSVFHCSINCKKKPNRELGLTRPISQKPIIYKVHRDNNHLSPVQNEQKSWNKTQKRSNKVYNSKKLVIIDTGSGVNITNDKTLLHNYEDSNRSTRFFGIGKNSSVSVKGYGYIKIKNGHNNTDNKCLLTYYVPEEESTIISCYDLAKKTKMVLSRKYTRLGNKIIKIKTKIVNGVIHVKMNELIERPSDDSKINAIKPTSSPGFKLNKRSITLEDAHKRMGHTGIQQIENSIKHNHYEESLDLIKEPNEFWCQTCKISKATKRNHYTGSMNNHSTDHEPGSSWCMDIFGPVSSSNADTKRYMLIMVDNNTRYCMTSTHFNKNAETILAQVRKNIQYVETQFDRKVREINSDRGTEFTNDQIEEYFISKGIHHILTSTQDHAANGRAERYIRTIITDATTLLRQSNLRVKFWEYAVTSATNIRNYLEHKSTGKLPLKAISRQPVTVRLMSFLPFGEKGIIWNHNHKKLKPSGLPSIILCKDPNSYGYKFFIPSKNKIVTSDNYTIPNYTMDGRVRNTQNINKSHQFSSDNDDEEDQIETVTNLCEALENYEDDNKPITRLEDLFTEEELSQIDSNAKYPSPSNNLEGDLDYVFSDVEESGDYDVESELSTTNNSISTDKNKILSNKDFNSELASTEISISGIDKKGLINTSHIDEDKYDEKVHRIPSIIQEKLVGSKNTIKINDENKISDRIRSKNIGSILNTGLSRCVDITDESITNKDESMHNAKPELIQEQLKKTNHETSFPKEGSIGTNVKFRNTNNEISLKTGDTSLPIKTLESINNHHSNDYSTNKVEKFEKENHHPPPIEDIVDMSDQTDMESNCQDGNNLKELKVTDKNVPTDNGTNVSPRLEQNIEASGSPVQTVNKSAFLNKEFSSLNMKRKRKRHDKNNSLTSYELERDKKRSKKNRVKLIPDNMETVSAPKIRAIYYNEAISKNPDLKEKHEYKQAYHKELQNLKDMKVFDVDVKYSRSEIPDNLIVPTNTIFTKKRNGIYKARIVCRGDTQSPDTYSVITTESLNHNHIKIFLMIANNRNMFMKTLDINHAFLYAKLEEEIYIPHPHDRRCVVKLNKALYGLKQSPKEWNDHLRQYLNGIGLKDNSYTPGLYQTEDKNLMIAVYVDDCVIAASNEQRLDEFINKLKSNFELKITGTLIDDVLDTDILGMDLVYNKRLGTIDLTLKSFINRMDKKYNEELKKIRKSSIPHMSTYKIDPKKDVLQMSEEEFRQGVLKLQQLLGELNYVRHKCRYDIEFAVKKVARLVNYPHERVFYMIYKIIQYLVRYKDIGIHYDRDCNKDKKVIAITDASVGSEYDAQSRIGVILWYGMNIFNVYSNKSTNRCVSSTEAELHAIYEGYADSETLKVTLKELGEGDNNDIVMITDSKPAIQGLNRSYQQPKEKFTWIKTEIIKEKIKEKSIKLLKITGKGNIADLLTKPVSASDFKRFIQVLKNKITSQDILASTDY

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
299	Phosphorylation	LHESLRNSVKQRLYN HHHHHHHHHHHHHHC	25.02	19779198
494	Phosphorylation	CYDLAKKTKMVLSRK HHHHHHHHHHHHCHH	24.54	27017623
974	Phosphorylation	LSNKDFNSELASTEI HCCCCCCHHHHCCEE	33.70	27017623
984	Phosphorylation	ASTEISISGIDKKGL HCCEEEEECCCCCCC	23.94	27017623
1108	Phosphorylation	RNTNNEISLKTGDTS ECCCCEEEEEECCCC	20.03	27017623
1211	Phosphorylation	PVQTVNKSAFLNKEF CCEECCHHHHHCHHH	21.03	19779198
1491	Phosphorylation	SNFELKITGTLIDDV HCCEEEEECEECCCC	23.64	27017623
1501	Phosphorylation	LIDDVLDTDILGMDL ECCCCCCCCCCCCEE	22.30	27017623
1510	Phosphorylation	ILGMDLVYNKRLGTI CCCCEEEECCCCCCH	23.43	27017623
1548	Phosphorylation	KSSIPHMSTYKIDPK HHCCCCCCCCCCCCC	26.08	22890988
1549	Phosphorylation	SSIPHMSTYKIDPKK HCCCCCCCCCCCCCC	22.66	22890988
1550	Phosphorylation	SIPHMSTYKIDPKKD CCCCCCCCCCCCCCC	9.91	22890988
1793	Phosphorylation	QVLKNKITSQDILAS HHHHCCCCHHHHHHC	23.19	27017623
1800	Phosphorylation	TSQDILASTDY---- CHHHHHHCCCC----	20.54	27017623
1801	Phosphorylation	SQDILASTDY----- HHHHHHCCCC-----	33.44	27017623
1803	Phosphorylation	DILASTDY------- HHHHCCCC-------	22.12	27017623

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of YJ41B_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of YJ41B_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of YJ41B_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
YJ41A_YEAST	YJL114W	physical	11087867
YJ41B_YEAST	YJL113W	physical	11087867
SPC72_YEAST	SPC72	physical	11087867
SMC3_YEAST	SMC3	physical	11087867

Drug and Disease Associations

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