YI31B_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: YI31B_YEAST
• UniProt AC: Q7LHG5
• Protein Name: Transposon Ty3-I Gag-Pol polyprotein
• Gene Name: TY3B-I
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 1498
• 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 genomic RNA-nucleocapsid complex.; Nucleocapsid protein p11 (NC) forms the nucleocore that coats the retro-elements dimeric RNA. Binds these RNAs through its zinc fingers (By similarity). Promotes primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty3 RNA and initiation of reverse transcription (By similarity).; 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: MSFMDQIPGGGNYPKLPVECLPNFPIQPSLTFRGRNDSHKLKNFISEIMLNMSMISWPNDASRIVYCRRHLLNPAAQWANDFVQEQGILEITFDTFIQGLYQHFYKPPDINKIFNAITQLSEAKLGIERLNQRFRKIWDRMPPDFMTEKAAIMTYTRLLTKETYNIVRMHKPETLKDAMEEAYQTTALTERFFPGFELDADGDTIIGATTHLQEEYDSDYDSEDNLTQNRYVHTVRTRRSYNKPMSNHRNRRNNNASREECIKNRLCFYCKKEGHRLNECRARKAVLTDLELESKDQQTLFIKTLPIVHYIAIPEMDNTAEKTIKIQNTKVKTLFDSGSPTSFIRRDIVELLKYEIYETPPLRFRGFVATKSAVTSEAVTIDLKINDLQITLAAYILDNMDYQLLIGNPILRRYPKILHTVLNTRESPDSLKPKTYRSETVNNVRTYSAGNRGNPRNIKLSFAPTILEATDPKSAGNRGNPRNTKLSLAPTILEATDPKSAGNRGDSRTKTLSLATTTPAAIDPLTTLDNPGSTQSTFAQFPIPEEASILEEDGKYSNVVSTIQSVEPNATDHSNKDTFCTLPVWLQQKYREIIRNDLPPRPADINNIPVKHDIEIKPGARLPRLQPYHVTEKNEQEINKIVQKLLDNKFIVPSKSPCSSPVVLVPKKDGTFRLCVDYRTLNKATISDPFPLPRIDNLLSRIGNAQIFTTLDLHSGYHQIPMEPKDRYKTAFVTPSGKYEYTVMPFGLVNAPSTFARYMADTFRDLRFVNVYLDDILIFSESPEEHWKHLDTVLERLKNENLIVKKKKCKFASEETEFLGYSIGIQKIAPLQHKCAAIRDFPTPKTVKQAQRFLGMINYYRRFIPNCSKIAQPIQLFICDKSQWTEKQDKAIEKLKAALCNSPVLVPFNNKANYRLTTDASKDGIGAVLEEVDNKNKLVGVVGYFSKSLESAQKNYPAGELELLGIIKALHHFRYMLHGKHFTLRTDHISLLSLQNKNEPARRVQRWLDDLATYDFTLEYLAGPKNVVADAISRAIYTITPETSRPIDTESWKSYYKSDPLCSAVLIHMKELTQHNVTPEDMSAFRSYQKKLELSETFRKNYSLEDEMIYYQDRLVVPIKQQNAVMRLYHDHTLFGGHFGVTVTLAKISPIYYWPKLQHSIIQYIRTCVQCQLIKSHRPRLHGLLQPLPIAEGRWLDISMDFVTGLPPTSNNLNMILVVVDRFSKRAHFIATRKTLDATQLIDLLFRYIFSYHGFPRTITSDRDVRMTADKYQELTKRLGIKSTMSSANHPQTDGQSERTIQTLNRLLRAYVSTNIQNWHVYLPQIEFVYNSTPTRTLGKSPFEIDLGYLPNTPAIKSDDEVNARSFTAVELAKHLKALTIQTKEQLEHAQIEMETNNNQRRKPLLLNIGDHVLVHRDAYFKKGAYMKVQQIYVGPFRVVKKINDNAYELDLNSHKKKHRVINVQFLKSLYTVQTRTQRINQSAPLRELREHTKLLHS

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
424	Phosphorylation	ILHTVLNTRESPDSL HHHHHHHCCCCCCCC	31.49	17330950
427	Phosphorylation	TVLNTRESPDSLKPK HHHHCCCCCCCCCCC	30.62	21082442
435	Phosphorylation	PDSLKPKTYRSETVN CCCCCCCCCCCCCCC	32.47	22890988
436	Phosphorylation	DSLKPKTYRSETVNN CCCCCCCCCCCCCCC	20.47	22890988
438	Phosphorylation	LKPKTYRSETVNNVR CCCCCCCCCCCCCEE	27.49	22890988
440	Phosphorylation	PKTYRSETVNNVRTY CCCCCCCCCCCEEEE	29.76	22890988
446	Phosphorylation	ETVNNVRTYSAGNRG CCCCCEEEECCCCCC	19.97	22890988
447	Phosphorylation	TVNNVRTYSAGNRGN CCCCEEEECCCCCCC	5.98	22890988
448	Phosphorylation	VNNVRTYSAGNRGNP CCCEEEECCCCCCCC	29.14	22890988
1038	Phosphorylation	AISRAIYTITPETSR HHHHHHHCCCCCCCC	16.56	19779198
1040	Phosphorylation	SRAIYTITPETSRPI HHHHHCCCCCCCCCC	13.79	19779198
1051	Phosphorylation	SRPIDTESWKSYYKS CCCCCCCHHHHHHHC	41.73	19779198
1103	Phosphorylation	ETFRKNYSLEDEMIY HHHHHCCCCHHCEEE	34.38	27017623
1110	Phosphorylation	SLEDEMIYYQDRLVV CCHHCEEEECCEEEE	8.18	27017623
1111	Phosphorylation	LEDEMIYYQDRLVVP CHHCEEEECCEEEEE	7.94	27017623

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

Oops, there are no upstream regulatory protein records of YI31B_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of YI31B_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 YI31B_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
YI31B_YEAST	YIL082W-A	physical	17964628

Drug and Disease Associations

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