wanglab/gogpt-training-data huggingface dataset:
Protein: 7-dehydrocholesterol reductase (7-DHC) (EC 1.3.1.21) (Sterol Delta(7)-reductase) (A0A024R5F7)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU369120}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU369120}.
Interaction partners:
Sequence:
MAAKSQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFAPFIVYYFIMACDQYSCALTGPVVDIVTGHARLSDIWAKTPPITRKAAQLYTLWVTFQVLLYTSLPDFCHKFLPGYVGGIQEGAVTPAGVVNKYQINGLQAWLLTHLLWFANAHLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMVKGYFFPTSARDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYIFRVANHQKDLFRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFWGVARHFNYVGDLMGSLAYCLACGGGHLLPYFYIIYMAILLTHRCLRDEHRCASKYGRDWERYTAAVPYRLLPGIF
Protein: Probable arabinogalactan endo-beta-1,4-galactanase A (EC 3.2.1.89) (Endo-1,4-beta-galactanase A) (Galactanase A) (Q2UN61)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Endogalactanase involved in the degradation of plant cell wall polysaccharides, and more particularly of hairy regions of pectin.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- CMP/dCMP-type deaminase domain-containing protein
Sequence:
MLFSYLLATLPLLANAALTYKGADISSVFIEEKAGVAYKNLAGETQALEAILTDNGVNSIRQRVWVKNGDYDLTYNVNLAKRVAATGASIYLDLHYSDDWADPKHQTTPDGWSTDDINTLADQIYQYTLSVCNTFAEEKINVEIVSIGNEITSGLLWPLGKTPNYENIARLLHSGAWGVKDSKLATKPKILIHLDNGWDWDQQKYFYDTALGTGLLTSDDFDMIGVSYYPFYNEKATLASLKTSLTNIQTTYGKEVAVVETNWPVKCSSPEFAFPADLKDIPFSVDGQVTFLQRLAETLTATKASGFFYWEPAWTKNAGLGSSCEDNLLVDYNTNQVRNSVKAFGQV
Protein: GTP-binding nuclear protein Ran-3 (Ras-related nuclear protein 3) (Q8H156)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Exportin-T
- Protein EXPORTIN 1B
- Ran-binding protein 1 homolog a
- Protein EXPORTIN 1A
- Protein HASTY 1
- Ran-binding protein 1 homolog b
- Ran-binding protein 1 homolog c
- Elongation factor 1-alpha 1
- RAN GTPase-activating protein 1
- Importin subunit beta-1
Sequence:
MALPNQQTVDYPSFKLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIGVEVHPLDFFTNCGKIRFYCWDTAGQEKFGGLRDGYYIHGQCAIIMFDVTARLTYKNVPTWHRDLCRVCENIPIVLCGNKVDVKNRQVKAKQVTFHRKKNLQYYEISAKSNYNFEKPFLYLARKLAGDANLHFVESPALAPPEVQIDLAAQQQHEAELAAAASQPLPDDDDDTFE
Protein: MDS1 and EVI1 complex locus (A0A0C3SFZ7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKSEDYPHETMAPDIHEERQYRCEDCDQLFESKAELADHQKFPCSTPHSAFSMVEEDFQQKLESENDLQEIHTIQECKECDQVFPDLQSLEKHMLSHTEEREYKCDQCPKAFNWKSNLIRHQMSHDSGKHYECENCAKQVFTDPSNLQRHIRSQHVGARAHACPECGKTFATSSGLKQHKHIHSSVKPFICEVCHKSYTQFSNLCRHKRMHADCRTQIKCKDCGQMFSTTSSLNKHRRFCEGKNHFAAGGFFGQGISLPGTPAMDKTSMVNMSHANPGLADYFGANRHPAGLTFPTAPGFSFSFPGLFPSGLYHRPPLIPASSPVKGLSSTEQTNKSQSPLMTHPQILPATQDILKALSKHPSVGDNKPVELQPERSSEERPFEKISDQSESSDLDDVSTPSGSDLETTSGSDLESDIESDKEKFKENGKMFKDKVSPLQNLASINNKKEYSNHSIFSPSLEEQTAVSGAVNDSIKAIASIAEKYFGSTGLVGLQDKKVGALPYPSMFPLPFFPAFSQSMYPFPDRDLRSLPLKMEPQSPGEVKKLQKGSSESPFDLTTKRKDEKPLTPVPSKPPVTPATSQDQPLDLSMGSRSRASGTKLTEPRKNHVFGGKKGSNVESRPASDGSLQHARPTPFFMDPIYRVEKRKLTDPLEALKEKYLRPSPGFLFHPQFQLPDQRTWMSAIENMAEKLESFSALKPEASELLQSVPSMFNFRAPPNALPENLLRKGKERYTCRYCGKIFPRSANLTRHLRTHTGEQPYRCKYCDRSFSISSNLQRHVRNIHNKEKPFKCHLCDRCFGQQTNLDRHLKKHENGNMSGTATSSPHSELESTGAILDDKEDAYFTEIRNFIGNSNHGSQSPRNVEERMNGSHFKDEKALVTSQNSDLLDDEEVEDEVLLDEEDEDNDITGKTGKEPVTSNLHEGNPEDDYEETSALEMSCKTSPVRYKEEEYKSGLSALDHIRHFTDSLKMRKMEDNQYSEAELSSFSTSHVPEELKQPLHRKSKSQAYAMMLSLSDKESLHSTSHSSSNVWHSMARAAAESSAIQSISHV
Protein: Bifunctional protein FolD [Includes: Methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)] (P24186)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. This enzyme is specific for NADP.
Interaction partners:
- Serine hydroxymethyltransferase
- Formyltetrahydrofolate deformylase
- Phosphoribosylglycinamide formyltransferase
- 5,10-methylenetetrahydrofolate reductase
- Methionyl-tRNA formyltransferase
- Bifunctional purine biosynthesis protein PurH
- 5-formyltetrahydrofolate cyclo-ligase
- Aminomethyltransferase
- Thymidylate synthase
- Phosphoribosylamine--glycine ligase
Sequence:
MAAKIIDGKTIAQQVRSEVAQKVQARIAAGLRAPGLAVVLVGSNPASQIYVASKRKACEEVGFVSRSYDLPETTSEAELLELIDTLNADNTIDGILVQLPLPAGIDNVKVLERIHPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTFGLNAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGDWIKEGAIVIDVGINRLENGKVVGDVVFEDAAKRASYITPVPGGVGPMTVATLIENTLQACVEYHDPQDE
Protein: Probable carbohydrate esterase At4g34215 (EC 3.1.-.-) (Q8L9J9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEGGSITPGEDKPEIQSPIPPNQIFILSGQSNMAGRGGVFKDHHNNRWVWDKILPPECAPNSSILRLSADLRWEEAHEPLHVDIDTGKVCGVGPGMAFANAVKNRLETDSAVIGLVPCASGGTAIKEWERGSHLYERMVKRTEESRKCGGEIKAVLWYQGESDVLDIHDAESYGNNMDRLIKNLRHDLNLPSLPIIQVAIASGGGYIDKVREAQLGLKLSNVVCVDAKGLPLKSDNLHLTTEAQVQLGLSLAQAYLSNFC
Protein: Glycogen synthase kinase-3 beta (EC 2.7.11.26) (G1T8E2)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKDSSGTGRFTSGVRVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDGLFNEQFFALNSKGQISSLI
Protein: Sll0319 protein (P74789)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Ribonuclease D
- N-acetylmuramoyl-L-alanine amidase
- Alkaline phosphatase
Sequence:
MNWKFFPHPFLAMAVGAILAPFTPVSASTFTETAIDQTEVIAVARPYGVETTKYDLLVIEQIPGKNKCWDVTPGAPAMVDPLLLNFDFTGHCRRATDSNGYSIRIDGQDYGLDYLLRLVPRGNELVLVATSRNGRGPELVVGSTKGIGAGFMQVQLNPGWQFTKRTYEGQVLGHYYISGTQAAILGGTAVSPVGPEPITPEKQELIAPEPVQTLENNPNPTPTEVTETGTEIIIKQEVPEVPANEQSGMVMEEESVSTVTEENSVAKEMETVTPKPALVVKPNPPRRRTPTPADFRP
Protein: Ribosomal protein eS27-like (40S ribosomal protein S27-like) (Small ribosomal subunit protein eS27-like) (Q71UM5)
Organism: Homo sapiens (Human)
Interaction partners:
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein eS25
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein eS26
- Small ribosomal subunit protein uS3
Sequence:
MPLARDLLHPSLEEEKKKHKKKRLVQSPNSYFMDVKCPGCYKITTVFSHAQTVVLCVGCSTVLCQPTGGKARLTEGCSFRRKQH
Protein: Photosynthetic NDH subunit of lumenal location 5, chloroplastic (Cyclophilin of 20 kDa 2) (AtCYP20-2) (Peptidyl-prolyl cis-trans isomerase CYP20-2) (PPIase CYP20-2) (EC 5.2.1.8) (Rotamase CYP20-2) (Thylakoid lumen PPIase of 20 kDa) (TLP20) (TLP21) (Q9ASS6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (Probable). PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Responsible, with FKBP13, for all PPIase activity observed in thylakoid lumen. Modulates the conformation of BZR1, which regulates flowering.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:11826309, ECO:0000269|PubMed:15084723}; Peripheral membrane protein {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:15084723}; Lumenal side {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:15084723}. Note=Peripherally associated with PSII complexes (PubMed:15084723). {ECO:0000269|PubMed:15084723}.
Interaction partners:
- Photosynthetic NDH subunit of lumenal location 4, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 5, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 1, chloroplastic
- Photosynthetic NDH subunit of lumenal location 1, chloroplastic
- NAD
- Photosynthetic NDH subunit of subcomplex B 2, chloroplastic
- NAD
- Photosynthetic NDH subunit of lumenal location 2, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 3, chloroplastic
- Photosynthetic NDH subunit of lumenal location 3, chloroplastic
Sequence:
MATLSMTLSNPKSLSAPPRRLSPINTSAFTSTSFRLRTKSSFDSISFSSSTPFSASSLLLHTSYTKRNHRCFSVQSNAEVVTEPQSKITHKVYFDISVGNPVGKLAGRIVIGLYGDDVPQTVENFRALCTGEKGFGYKGSTFHRVIRDFMIQGGDFEKGNGTGGKSVYGRTFKDENFKLSHVGPGVLSMANAGPNTNGSQFFICTIKTSWLDGRHVVFGQVIEGMEVVKLIEEQETDRGDRPRKKVVIADCGQLPMSEA
Protein: Putative baseplate protein (H9C1B1)
Organism: Pectobacterium phage ZF40 (Bacteriophage ZF40)
Interaction partners:
Sequence:
MKSTNPLFSAIQAASMNMLGDLMIGMPGHVIAYDSEKQRAQVECGIQRRMPDGAIETLSVLINVPVQFSGSADWVLFHELPAGTEGYIHFSQRSVDAWLDMGGPVPPTGPEMFSASDAFFSPGYRSLKTAIPGLPTSGMGMSNRDGSVRIHLTDDVITLTCGGVSLTVSPEGVTANGKTTLNGRTEITTGGLAVGDIEFDDHAHGGVERGSGVSDGPQ
Protein: Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32) (Q9H4X1)
Organism: Homo sapiens (Human)
Function: Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation.
Subcellular location: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Cytoplasmic in unstimulated cells. Nuclear after activation by complement. Associated with the centrosome during prometaphase and metaphase.
Interaction partners:
- G2/mitotic-specific cyclin-B1
- Cellular tumor antigen p53
Sequence:
MKPPAAQGSPAAAAAAAPALDSAAAEDLSDALCEFDAVLADFASPFHERHFHYEEHLERMKRRSSASVSDSSGFSDSESADSLYRNSFSFSDEKLNSPTDSTPALLSATVTPQKAKLGDTKELEAFIADLDKTLASM
Protein: Homeobox protein goosecoid (P56915)
Organism: Homo sapiens (Human)
Function: Regulates chordin (CHRD). May play a role in spatial programing within discrete embryonic fields or lineage compartments during organogenesis. In concert with NKX3-2, plays a role in defining the structural components of the middle ear; required for the development of the entire tympanic ring (By similarity). Probably involved in the regulatory networks that define neural crest cell fate specification and determine mesoderm cell lineages in mammals.
Subcellular location: Nucleus.
Interaction partners:
- Centrosomal protein 20
- RRP15-like protein
- Transcription elongation factor SPT6
- Zinc finger protein 330
- PSME3-interacting protein
- WD repeat-containing protein 26
- Histone H4 transcription factor
- Tektin-2
- T-box transcription factor TBX20
- Rab11 family-interacting protein 3
Sequence:
MPASMFSIDNILAARPRCKDSVLPVAHSAAAPVVFPALHGDSLYGASGGASSDYGAFYPRPVAPGGAGLPAAVSGSRLGYNNYFYGQLHVQAAPVGPACCGAVPPLGAQQCSCVPTPPGYEGPGSVLVSPVPHQMLPYMNVGTLSRTELQLLNQLHCRRKRRHRTIFTDEQLEALENLFQETKYPDVGTREQLARKVHLREEKVEVWFKNRRAKWRRQKRSSSEESENAEKWNKTSSSKASPEKREEEGKSDLDSDS
Protein: LD22609p (Tay bridge, isoform A) (Tay bridge, isoform B) (Tay bridge, isoform C) (Q9VXM5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO03726p1
- non-specific serine/threonine protein kinase
Sequence:
MDTSNASAKSKTSASGSSSINGIGSQIKHISSSQDIGSSVPAVPVQDEKSESHSHSHSHSSSSSQSSQSQSQSQPQSTVLTVVGQSISKSSTGALAVLHLPPPTATALVQASANIADLGSMPRARPSFVSNTSSTAATTTTATSASDGGKTMAVAAIPPASPVSISEPTCPSVSTVSMAPSACDFDSDTELSIVAAAAAVSASAGIDSRSPTSPPTAAGSTIMPQLNSSAGGTASIAGNQSGFGAGSGAVAAGNTNGHSTTSSSSTHLSLNAKQQRQQKRRRERAQRLQAERDSRCNANSLSGTFIAGSSVGVGSAMSAANGGQGGGVGLVTPNSSVGGGSSAVAMGNGSAAGPGNNGMIYHINSAGSMGEDSNNSNGNFTSSSNGSNNLLPPTDSIASLLLNPPHSPECNSGLMATPSDSEGESLDEDLLSTSSSSTLLLPRDKPPPRPPPPVRRKLPRSPVLEEEIIDGFAILEFKTYEDLEFAIKLGQKRKEKRLSALDELTCTYSIEEMKIPKVIDTGQSQPLRVTSLSTLTVNNNNLKENPQPSLHRDRGGNVISNNNNNNSSNNNNSMINSNGPNANSNSSSLSNVVYLLPSVNMVGNVLETEAEPRDHWRSEYGQQQDQLQSDNSANSKSNNNISDDNQINNSSHQINHTTNNQSSKQQQAADGGCNAAKMQVNNSATVSTRFLENDNDSLMLDISLPSLGVGGAVSHSHDHIDVGVIHASCTGSSSDTKKSHNSPATSNTIDQLHVTKPLPTHQLNNLISSDLNAAANANANSNHLGVCKLGSQSAQVAKKSMGLENIETVTNSATCRSLDIQELANVSAQSFGASSSSSSSSISIKKENEQSDLLNDASTNCSSNSKGNNICDNVSNDKKNSEQIFDIDNPPTPMNISNTSSCSDRSSSRKFSELPHLKKKSAACGDRDNGPYAGVPFAAAMGTVSPDSDPSKALNIKNASESASGKAVHAHAGAPIPPPPAASVGDPGNRELGVLQKTSPDKPLYPNLCAPPSVSSVQFPNVGISAGNEKIASTVASDIDQKIIFNSKATASVSNGLSSGVQRSIVPLLSAAPSPAAVTLSSPFSAHIAAAPNAAGLSILSSASSVILANSSIKNTNNGSNNGSANGQGQLSSVGLSSTSEIAKSNSVPTTSSPPNPMVNGFLSVYPPPAATIATSSVTTSALSRVSPNAANKLVPPVSATTSISINTNYVGISGGTTTTSGMGKVVFGAGGNAIVGTGSPLLFPGAPPAPISHVATGVPMIIQAPPYRAPYTNYPLYTPYSGLTHGSYLPPVLPVATPNLSNLPPTQHRSSDSRNSRESPASLKSTPSNIGLNVSMAPTLRSITPLNNSSAISSGASQPVVSVVPSANSTALSMSNPHISHSHHVPAYASGAFSSSAAAGTSTPNSGLSTLAVTSLSTSAAPQPHSHFPQSTQMLPQSGNFSSVSHLLTTHPMSSQNQPMVRCGSTLYSQSSAAATAPPSAAAAVSNFTPSVLAVQSLTTAVTSSSSSPSTLSSSVIQKVISPKGESPCNKDRDSSYSTNIRSHGASTMLPGASQGIGLGSSFCGIAPSQYGGTGTPVLSSSSSMPPGLGNLSSYSSKAALWLNSPANAVVTTCAPTTPIVSSGSARPTPPLSNCTSMGIGMVNAASTARSSCNAISPLSIPATAGIHVSATNPSFQSSSYFPTPLAPPPSSPSPATSSAAIISSSASQFNPAVSHSMSSIVTTAGATTTTASSVTQPSVAAISNPVTNTPHPFSAESLFQPSKNDQADLLRRELDSRFLDRSGLAVTPTPPSSTYLRTDLQHQQHAHLHQHPQLLPPVSAPSTPLSAVQPSSGQIFPPPLFKDISKISSVDPQFYRTGMGLPPGGYSGYTSAGLLHSGLGGPTPFMPPNHLTSFAPKKTGRWNAMHVRIAWEIYYHQNKQSPEKQPGFPTASSNAGSINAPIPPGNMISGGGGGMASGASTPVNNVAAIPAVGGGVLVSNGPPSVLGMKTTPTLGMSSTPQHILHRASEMPPSAAFPGGLPGRLAFETSPLAASFIGAPPSHIGTAVSPFGRYVTPFGFTGLTHFGGHLDSWRTNAMQRSVAYHPSSAAPSPNWPVKSDPGLDNARREAEERERELRDREQRERDRQRREREERERKEKEEKLKREQQERERERERDRKERERERREIERREMERERMLQQQRINESNKQAAVQAAAAATAPVRDRSPHRNVGELNTEIRIKEEHPRTKEEQDVMLLRASAAAVGVGDPRYHSSSLAAAQASAAAAAAHHHHANFMAASRHGLPPPPSHLTRTMMPPTLSVGGPITHFGAPAPPGWGIDPYRDPYPILRYNPIMEAALRHEAEERQKAINIYAAQSAAHLRSKEPSPIPPSVGSLGPPPPHHRLQIVSSVAQSGVQQPGPPSQQQQQQMSSGGGMVKNSGGPQAPGSIPVQHMISVDSMGQQSVSAKKESDHTMGIVSNAGVGLSSVPGGVIGISPVSSVAPSR
Protein: Transposon Ty1-GR1 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q12141)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQTAQSHSPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIDKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELDKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: 5'-nucleotidase (EC 3.1.3.5) (A0A090N7U2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361276}.
Interaction partners:
Sequence:
MPEFQKSSVRIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDECRKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLKGFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYLNDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
Protein: Phosphatidylinositol 4-phosphate 5-kinase (EC 2.7.1.68) (Q8I239)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes.
Interaction partners:
- 1-phosphatidylinositol 4-kinase
- Secretory complex protein 61 gamma subunit
- protein-serine/threonine phosphatase
Sequence:
MKCTSVNIRNVLDISLKKKIKENTNLSDDEIIIIYKRFNYISSNGKLNYDNFEKSLGILGSIQNAYLYKSIFKAFDLNNDNYLDFYEFCVAINIMLKGNKKDKLKLSYRIVNAGFNSNEDACVHKSSCMVNKFNTKEDNNMNGDNINGDNNNNHNNINGDNNNNHNNINGDNNNNNHNNINGDNNNNHNNINGDNNNNNHNNINGDNNNNHNNINGDNNNNHNNSHNNNSHNNNNKAENSLGQPLNEKNINDPINKHRNSQSIIYNINDEYNEKIKKNKKQDYSNYITYENFEKIVLSINDIKRQLLGTGDEIITSQIKYTFRSLSILCDDGIYRMNFECYKKALKCNEFLKLLGIHTKVADVFLQHELLKRKDKNKTKNGTMRNRKKYKNDSNRIANHLIIKSFSESTNTRGSIINDSTSFLFLRKQKKKKKKKKKKKKKKEKKAILYERKSTFSSSMENKSQNKSQNKSHNKNIKSVSRILSRVNKLSSTELIPNECDHKPNEEVKSTSDVLTPIFFNNGDEKMNHDTDGNMVYHKNNVDDNLVDGDVVSQGKRCSFFSSCENKKNEENKSITFNDINSGNINTNSCIMNNMIVTKESNEEIINEEAQSSYIYNKNIFCSKYNTKKDKNEPLKCDLFECSFINNDKNIVRDEDSNHKNVRKTDDYFIIDDNNIFDNGPIIISKNKTNDRERKLLKTFSSSSLKKKSLLKNYNYHIKKKNKDPNVEDTNMLYHDDIKKEYDHKVTKNNKNTCNNNYYNNVSFNSSAYYEYHSDIDLIHFSNNLKKKKKKNVTSPRPSSKEYERKVTYHKECCSNERMKNIKVNESDLGMFCVNNDKTNIEDVKEKKACDVLNRGCIKEQVQCKISEFENDKGNEIYMQEFKKCIEKYKEYVNQGEGHLKDEEEEKNDDEEEGEDGEDDEEENDDDDDDEDGDDDEDGDDDNDDNDDNDDNDDNDDNDDNDDNDDNDDNDDNDEKSNIKIENKKDVPNIHNNNDDDGINCCTNLFKDDDTLSALEKNVTNNNLIKIMSAKYLYHKFLEYKDFMKNNTTLFSHFNKIYQHEDDKINTDNKDVLNYRPKHNNDINYYNIPCEDQIKSDEKKSLLNVEFGDDIIKKKFFISSVNSHYVMINNNLTKEQMLYLIRNILMSIEDYLKKEKNRDYNKIFFLFFSIFIYNTQNGGDQKEMHEDEKWDHTNINEDKNVEKNDDYKNLSNNENSVYYNTMLRESLWNKKKYIKLNIFKNIILVISIVRYFLHTITISQKYTSSYDSLDDSNMIKSMNSLKLNEINILLNRASEILEKYSLGSVENKKVYINKSNYYNSSKKGKLSVSLRQNKQKKTFHRILAVYFGHERWDLVMNMMIGIRISSIKKFSINDISNYFHHKDVIQLPTSNAQHKVIFKNYAPIIFKNIRNFYGIKSKEYLTSVGPEQVISNMVLGNLSTLSELLSEGKSGSLFYFTSNGKYIIKTVCRNIHNLSKKLLPKYYEHIKKNPDSLLTRLYGIHSIKYQNNLGRKKKKIYFIVMNNFFSSIVEIHRRYDIKGSLVGRTVPETKREDHTIALKDVDIDELGDIINIGPENKERLLKVLKADADFLKENMLLDYSLLFGIHYRELSKDVVNWEETKTNQINHIYDYKGNCIASRPFHQCDYGGIISVDKKKIFFFGIIDIFTKWSIKKKFEHTFRTIQKFDGKNISCIHPNAYAKRFVTFIENHMK
Protein: Protein MODIFIED TRANSPORT TO THE VACUOLE 1 (Q9C5H4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates clathrin-dependent trafficking of vacuolar cargo from the trans-Golgi network (TGN). Promotes plant growth.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:23771894}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:23771894}. Note=Colocalizes with clathrin at the trans-Golgi network (TGN). {ECO:0000269|PubMed:23771894}.
Interaction partners:
- Clathrin interactor EPSIN 1
- ENTH/VHS family protein
- Clathrin interactor EPSIN 3
- ADP-ribosylation factor GTPase-activating protein AGD5
- Clathrin interactor EPSIN 2
- Vacuolar-sorting receptor 4
- Vacuolar protein sorting-associated protein 29
Sequence:
MDTSRRAVESYWRSRMIDAVTSDEDKVAPVYKLEEICDLLRSSHVSIVKEFSEFILKRLDNKSPIVKQKALRLIKYAVGKSGSEFRREMQRNSVAVRNLFHYKGHPDPLKGDALNKAVRETAHETISAIFSEENGTKPAAPESINRRIEGFGNTNFQVPSNDNKSFLSEVVGIGSASIKQGISNFAQGHLPKKNENGSSSYRGPNLHRSLTMENENFSRYDPVKLGKDGNYGTSKNTTGGSWGHASGEASESSASVRVESKTREEKLLETIVTSGGVRLQPTRDALHVFILEAAKMDAVALSIALDGKLHSPMWQVRMKALCVLEAILRKKEDENFSIVHTYFSENLDAIQRCAESPQSSLREKANKVLSLLNGGQSSGLMSSSDNTVKREAAVDLPDLIDTGDSDDTLNNLNAIDTGSTVATAGPLMDDDWFGDSSDIGLSSSEKKTDDDPFADVSFHPNEEKESADDLFSGMTVGEKSAAVGGNHVPDLFDMFGSTAKLEAEPKDAKNINDLMGSFSIDENNSNQKGSSSSTLPQDLFAMPSTTSHQAPENPVGGILGSQNPGFIQNTMLPGGVMPFNFPQGMMMNPAFASQPLNYAAMASLLAQQQQYLGNMSNFQQFGNLNAQGSGNVLSMGTSGGNQSALPDIFQPNFGNQAPTSTMNGSKKEDTRAFDFISDHLTSARDTKRVS
Protein: DUF742 domain-containing protein (O50392)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable ATP/GTP-binding protein
- histidine kinase
- Serine protease inhibitor Rv3364c
- Pentapeptide repeat protein MfpA
- Probable fatty oxidation protein FadB
Sequence:
MFNPAGDRPKAGLVRPYTLTAGRTGTDVDLPLQAPVQTLPAGPAGRWPAYDMRRRILQLCIGSPSVAEISARLDLPVGVARVLVGDLVTSGYLRVHATLTDRSTRDERHELIGRTLRGLKAL
Protein: Voltage-dependent L-type calcium channel subunit beta-1 (Calcium channel voltage-dependent subunit beta 1) (Q6DG31)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004278}.
Interaction partners:
Sequence:
MVQEGNMSRTPSTSTQEIQMDMFDHHGSHAQGKYAKRKSRFKRSDGSTSSDTTSNSFVRQGSADSYTSRPSDSDVSLEEDPEALRKEADRQALATLEKAKTKPVAFAVRTNVGYNPGPNDDVPVQGMAISFEPKDFLHIKEKYNNDWWIGRLVKEGCEVGFIPSPVKLESTRQLQEQRMRQNRLSSSKSGGSSSLDVATGARRPTPPGTGGPAKQKQKSMEHVPPYDVVPSMRPIILVGPSLKGYEVTDMMQKALFDFLKHKFEGRISITRVTADISLAKRSVLNNPSKHTIIERSSTRSSLAEVQSEIERIFELARTLQLVALDADTINHPSQLAKTSLAPIIVYIKIASPKVLQRLIKSRGKSQAKHLNVQMVAADKLAQCPPELFDIILDENQLEDACEHLAEYLEAYWKATHPPSSNPPNPLLNRTMATAALAASPEPVSNLQVQVLTSLRRNMELLDGSPAVMQGQQEDEHAL
Protein: Uncharacterized HTH-type transcriptional regulator Rv0472c (P9WMD9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- 1,4-dihydroxy-2-naphthoate prenyltransferase
- Uncharacterized HTH-type transcriptional regulator Rv1828
- 1,4-dihydroxy-2-naphthoate prenyltransferase
- Cyclopropane mycolic acid synthase 3
- Heparin-binding hemagglutinin
Sequence:
MAERIPAVTVKTDGRKRRWHQHKVERRNELVDGTIEAIRRHGRFLSMDEIAAEIGVSKTVLYRYFVDKNDLTTAVMMRFTQTTLIPNMIAALSADMDGFELTREIIRVYVETVAAQPEPYRFVMANSSASKSKVIADSERIIARMLAVMLRRRMQEAGMDTGGVEPWAYLIVGGVQLATHSWMSDPRMSSDELIDYLTMLSWSALCGIVEAGGSLEKFREQPHPSPIVPAWGQV