wanglab/gogpt-training-data huggingface dataset:
Protein: DNA replication licensing factor MCM2 (EC 3.6.4.12) (Minichromosome maintenance protein 2) (P29469)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Necessary for cell growth.
Subcellular location: Nucleus.
Interaction partners:
- Minichromosome maintenance protein 5
- Topoisomerase 1-associated factor 1
- DNA replication licensing factor MCM3
- Origin recognition complex subunit 3
- Origin recognition complex subunit 6
- DNA replication complex GINS protein PSF1
- Minichromosome maintenance protein 10
- DNA replication complex GINS protein PSF3
- DNA polymerase epsilon catalytic subunit A
- DDK kinase regulatory subunit DBF4
Sequence:
MSDNRRRRREEDDSDSENELPPSSPQQHFRGGMNPVSSPIGSPDMINPEGDDNEVDDVPDIDEVEEQMNEVDLMDDNMYEDYAADHNRDRYDPDQVDDREQQELSLSERRRIDAQLNERDRLLRNVAYIDDEDEEQEGAAQLDEMGLPVQRRRRRRQYEDLENSDDDLLSDMDIDPLREELTLESLSNVKANSYSEWITQPNVSRTIARELKSFLLEYTDETGRSVYGARIRTLGEMNSESLEVNYRHLAESKAILALFLAKCPEEMLKIFDLVAMEATELHYPDYARIHSEIHVRISDFPTIYSLRELRESNLSSLVRVTGVVTRRTGVFPQLKYVKFNCLKCGSILGPFFQDSNEEIRISFCTNCKSKGPFRVNGEKTVYRNYQRVTLQEAPGTVPPGRLPRHREVILLADLVDVSKPGEEVEVTGIYKNNYDGNLNAKNGFPVFATIIEANSIKRREGNTANEGEEGLDVFSWTEEEEREFRKISRDRGIIDKIISSMAPSIYGHRDIKTAVACSLFGGVPKNVNGKHSIRGDINVLLLGDPGTAKSQILKYVEKTAHRAVFATGQGASAVGLTASVRKDPITKEWTLEGGALVLADKGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTTLQARCSIIAAANPNGGRYNSTLPLAQNVSLTEPILSRFDILCVVRDLVDEEADERLATFVVDSHVRSHPENDEDREGEELKNNGESAIEQGEDEINEQLNARQRRLQRQRKKEEEISPIPQELLMKYIHYARTKIYPKLHQMDMDKVSRVYADLRRESISTGSFPITVRHLESILRIAESFAKMRLSEFVSSYDLDRAIKVVVDSFVDAQKVSVRRQLRRSFAIYTLGH
Protein: Beta-ketoacyl-[acyl-carrier-protein] synthase III (Beta-ketoacyl-ACP synthase III) (KAS III) (EC 2.3.1.180) (3-oxoacyl-[acyl-carrier-protein] synthase 3) (3-oxoacyl-[acyl-carrier-protein] synthase III) (Q8Y0J4)
Organism: Ralstonia nicotianae (strain ATCC BAA-1114 / GMI1000) (Ralstonia solanacearum)
Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815}.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- 3-oxoacyl-[acyl-carrier-protein] reductase
- 3-oxoacyl-[acyl-carrier-protein] synthase II
- Phosphate acyltransferase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- Probable 3-oxoacyl-[acyl-carrier-protein] synthase
- 3-oxoacyl-[acyl-carrier-protein] synthase
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
Sequence:
MTRYARIIGTGSYLPPKRVTNHELAAQLAEQGIETSDEWIVTRSGIRARHYAEPDVTCSDLAAKAAERAIEAAGIDRAEIDLILVATSTPDFVFPSAACLVQQKLGLSNHCAAFDLQAVCSGFVYGLATADKFIRAGGYRNALVIGAEVFSRILDFNDRTTCVLFGDGAGAVVLQASDEPGILSTALHADGSHADILCVPGNVAGGAIKGSAFLYMDGQAVFKLAVNVLDKVAREALALAEVESSQIDWLIPHQANIRIMQGTAKKLGLPGERMVVTVDEHGNTSAASIPLALDAAVRDGRIQKGHHVLLEGVGGGFTWGAALLRF
Protein: ABC transporter, ATP-binding protein (Q9WYC3)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MKTLARYLKPYWIFAVLAPLFMVVEVICDLSQPTLLARIVDEGIARGDFSLVLKTGILMLIVALIGAVGGIGCTVFASYASQNFGADLRRDLFRKVLSFSISNVNRFHTSSLITRLTNDVTQLQNLVMMLLRIVVRAPLLFVGGIVMAVSINVKLSSVLIFLIPPIVLLFVWLTKKGNPLFRKIQESTDEVNRVVRENLLGVRVVRAFRREEYENENFRKANESLRRSIISAFSLIVFALPLFIFIVNMGMIAVLWFGGVLVRNNQMEIGSIMAYTNYLMQIMFSLMMIGNILNFIVRASASAKRVLEVLNEKPAIEEADNALALPNVEGSVSFENVEFRYFENTDPVLSGVNFSVKPGSLVAVLGETGSGKSTLMNLIPRLIDPERGRVEVDELDVRTVKLKDLRGHISAVPQETVLFSGTIKENLKWGREDATDDEIVEAAKIAQIHDFIISLPEGYDSRVERGGRNFSGGQKQRLSIARALVKKPKVLILDDCTSSVDPITEKRILDGLKRYTKGCTTFIITQKIPTALLADKILVLHEGKVAGFGTHKELLEHCKPYREIYESQFGNGVMNDA
Protein: Carotene epsilon-monooxygenase, chloroplastic (EC 1.14.14.158) (Cytochrome P450 97C1) (Protein LUTEIN DEFICIENT 1) (Q6TBX7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heme-containing cytochrome P450 involved in the biosynthesis of xanthophylls. Specific for epsilon- and beta-ring hydroxylation of alpha-carotene. Has only a low activity toward the beta-rings of beta-carotene. The preferred substrate in planta is not alpha-carotene but the epsilon-ring of zeinoxanthin. Possesses a major beta-carotene hydroxylase activity in planta when depleted in its preferred substrate alpha-carotene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Lycopene beta cyclase, chloroplastic
- Beta-carotene 3-hydroxylase 2, chloroplastic
- Beta-carotene 3-hydroxylase 1, chloroplastic
- Zeta-carotene desaturase, chloroplastic/chromoplastic
- Lycopene epsilon cyclase, chloroplastic
- Protein LUTEIN DEFICIENT 5, chloroplastic
- Phytoene synthase 1, chloroplastic
- NADPH--cytochrome P450 reductase 1
- Zeaxanthin epoxidase, chloroplastic
- Prolycopene isomerase, chloroplastic
Sequence:
MESSLFSPSSSSYSSLFTAKPTRLLSPKPKFTFSIRSSIEKPKPKLETNSSKSQSWVSPDWLTTLTRTLSSGKNDESGIPIANAKLDDVADLLGGALFLPLYKWMNEYGPIYRLAAGPRNFVIVSDPAIAKHVLRNYPKYAKGLVAEVSEFLFGSGFAIAEGPLWTARRRAVVPSLHRRYLSVIVERVFCKCAERLVEKLQPYAEDGSAVNMEAKFSQMTLDVIGLSLFNYNFDSLTTDSPVIEAVYTALKEAELRSTDLLPYWKIDALCKIVPRQVKAEKAVTLIRETVEDLIAKCKEIVEREGERINDEEYVNDADPSILRFLLASREEVSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNSSALRKAQEEVDRVLEGRNPAFEDIKELKYITRCINESMRLYPHPPVLIRRAQVPDILPGNYKVNTGQDIMISVYNIHRSSEVWEKAEEFLPERFDIDGAIPNETNTDFKFIPFSGGPRKCVGDQFALMEAIVALAVFLQRLNVELVPDQTISMTTGATIHTTNGLYMKVSQR
Protein: Beta-parvin (Parvin, beta) (Q6PC42)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Scaffold protein ILK
- Paxillin
- Paxillin
- Rac/Cdc42 guanine nucleotide exchange factor
- LIM domain-containing protein.
- LIM domain-containing protein.
- Actinin, alpha 1
- Actin, cytoplasmic 2
- Actin, cytoplasmic 1
- Ras suppressor protein 1
Sequence:
MATNATRSTGQPAKTKKDESLLGKLGGTLVRKKKIKEVSDLQEEGKNAINAPLLHTSPELLPEDTLLEENAERTILDPTSREDLNFKDLQKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQSEIGQKQKLQTVLEAVNGVLRPLDWNTEWSVDSIHSKNLVSIVYLLLALAIYYAAPIRLPEHVSVQVIVVKKKEGILQTAHVTKQLTSTTTEMMIGRSERDAFDTLLDHAPDKLNVVKTSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLENYFVPLYNFYLTPENFEQKVHNVAFAFELMQDGGLQKPKARPEDVVNLNLKSTLRVLYNLFTNYKNSE
Protein: Reticulophagy regulator 1 (Reticulophagy receptor 1) (Q8VE91)
Organism: Mus musculus (Mouse)
Function: Endoplasmic reticulum (ER)-anchored autophagy regulator which mediates ER delivery into lysosomes through sequestration into autophagosomes. Promotes membrane remodeling and ER scission via its membrane bending capacity and targets the fragments into autophagosomes via interaction with ATG8 family proteins. Active under basal conditions (By similarity). Required for collagen quality control in a LIR motif-dependent manner. Required for long-term survival of nociceptive and autonomic ganglion neurons.
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:19838196}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H6L5}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Gamma-aminobutyric acid receptor-associated protein
- 60S ribosomal export protein NMD3
- Microtubule-associated protein 1 light chain 3 beta
- Large subunit GTPase 1 homolog
- Translocation protein SEC62
- Proliferation-associated protein 2G4
- Eukaryotic translation initiation factor 6
- Cell cycle progression protein 1
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein uL23
Sequence:
MASPAPEEHATQGCPATEEQPPRPGVPGEEAGPEGAGPQVEEAAGRVAAALTWLLGEPVLWLGWRADELLSWKRPLRSLLTFLGANLLFWFLALTPWRVYHLISVMILGRVIMQIIKEMVLSRTRGAQLWRSLTESWEVINSKPDERARLSQCIAESWMNFSMFLQEMSLFKQQSPGKFCLLVCSVCTFFTILGSYIPGVILSYLLLLFAFLCPLFKCNDIGQKIYSKVKSILLKLDFGIGEYINQKKRERSEADKEKSHKDDSELDFSALCPKISLTVAAKELSVSDTDVSEVSWTDNGTFNLSEGYTPQTDTSDDLDRPSEEVFSRDLSDFPSLENGTGTNDEDELSLGLPTELKRKKQQLDSAHRPSKERQSAAGLSLPLKSDQALHLMSNLAGDVITAAMTAAIKDQLEGARQALTQVAPTAGEDTDTEEGDDFELLDQAELDQIESELGLTQDQGAEAQQSKKSSGFLSNLLGGH
Protein: Upstream-binding protein 1 (Transcription factor LBP-1) (Q9NZI7)
Organism: Homo sapiens (Human)
Function: Functions as a transcriptional activator in a promoter context-dependent manner. Modulates the placental expression of CYP11A1. Involved in regulation of the alpha-globin gene in erythroid cells. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with TFCP2 (By similarity). Involved in regulation of the alpha-globin gene in erythroid cells. Binds strongly to sequences around the HIV-1 initiation site and weakly over the TATA-box. Represses HIV-1 transcription by inhibiting the binding of TFIID to the TATA-box.
Subcellular location: Nucleus {ECO:0000269|PubMed:8114710}.
Interaction partners:
- Alpha-globin transcription factor CP2
- Sphingosine-1-phosphate phosphatase 1
- Ceramide synthase
- Ankyrin repeat domain-containing protein 29
Sequence:
MAWVLKMDEVIESGLVHDFDASLSGIGQELGAGAYSMSDVLALPIFKQEDSSLPLDGETEHPPFQYVMCAATSPAVKLHDETLTYLNQGQSYEIRMLDNRKMGDMPEINGKLVKSIIRVVFHDRRLQYTEHQQLEGWKWNRPGDRLLDLDIPMSVGIIDTRTNPSQLNAVEFLWDPAKRTSAFIQVHCISTEFTPRKHGGEKGVPFRIQVDTFKQNENGEYTDHLHSASCQIKVFKPKGADRKQKTDREKMEKRTAHEKEKYQPSYDTTILTEMRLEPIIEDAVEHEQKKSSKRTLPADYGDSLAKRGSCSPWPDAPTAYVNNSPSPAPTFTSPQQSTCSVPDSNSSSPNHQGDGASQTSGEQIQPSATIQETQQWLLKNRFSSYTRLFSNFSGADLLKLTKEDLVQICGAADGIRLYNSLKSRSVRPRLTIYVCREQPSSTVLQGQQQAASSASENGSGAPYVYHAIYLEEMIASEVARKLALVFNIPLHQINQVYRQGPTGIHILVSDQMVQNFQDESCFLFSTVKAESSDGIHIILK
Protein: DNA polymerase delta subunit 3 (A0A8I6G366)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRLFRSRPLAFICTLESSNKTLNVVFLFQVTYKWLSYTLGVHVNQAKQMLYEYVERKRKENSGAQLHVTYLVSGSLIQNGHSCHKVAVVREDRLEAVKSKLAVTASIHVYSIQKAMLKDSGPLFNTDYDILKSNLQNCSKFSAIQCAAAVPRAPAESSSSRKFEQSNLQAASETQASELTTNGHGPPASKQASQQPKGIMGMLISKAATKTQDTNKDTKTEAREVTSASSAGGKAPGKGNVMSNFFGKAAMSKLKVNLDSEQAVKEEKTVEQPPVSVAEPKLAAPPALKKSSRKSEPVKMQQKEKKCRGKRVDLSDEEAKETENLKKKRRRIKLPQSDSSEDEVFADSPEMFEAVSPSPPPASPPPDPVPKTEPPPVKRSSGENKRKRKRVLKSKTFVDEEGCMVTEKVYESESCTDSEEETKMKMASAQRPPAATVKREPREERKGPKKGAAALGKANRQVSITGFFQKK
Protein: Cyclin-A1-1 (G2/mitotic-specific cyclin-A1-1) (CycA1;1) (Q9C6Y3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B2-2
- Cyclin-dependent kinase B1-2
- Cyclin-dependent kinase A-1
- Wee1-like protein kinase
- Cell division control protein 6 homolog
- Cyclin-dependent kinases regulatory subunit 1
- Cyclin-dependent kinases regulatory subunit 2
- Transcription factor E2FC
Sequence:
MSNILQNRRSSFSSSTKSSLAKRQAPSSSENSVKLMPAMTKKRAPLSNITNQKIASRLQNSDSVHCSNKSAKLKIAPSVCVNASFSSNLQQSIVPHKVASSPSKSDDGSVSMDETRSSSDSYKSPQVEYIENDDVSAVVSIERKALSNLFITPNSETIDNYCSRDVLSDMKKMDKNQIVNIDSNNGDPQLCATFACDIYKHLRASEAKKRPDVDYMERVQKDVNSSMRGILVDWLIEVSEEYRLVPETLYLTVNYIDRYLSGNVISRQKLQLLGVACMMIAAKYEEICAPQVEEFCYITDNTYLKDEVLDMESDVLNYLKFEMTAPTTKCFLRRFVRAAHGVHEAPLMQLECMANYIAELSLLEYTMLSHSPSLVAASAIFLAKYILDPTRRPWNSTLQHYTQYKAMELRGCVKDLQRLCSTAHGSTLPAVREKYSQHKYKFVAKKFCPSVIPQEFFNNS
Protein: Phospholipase A2 homolog 3 (EC 3.1.1.4) (Q10E50)
Organism: Oryza sativa subsp. japonica (Rice)
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Os04g0615100 protein
- Lipase family protein
- Lipoxygenase
- Os02g0676000 protein
- Os06g0712300 protein
- Os01g0955000 protein
- Os01g0102000 protein.
- Os09g0513100 protein
- phospholipase D
- Probable lipoxygenase 8, chloroplastic
Sequence:
MARGGSFSRLRLRAGVVVAAAAAALLLFAVVAPPAAALNIGLQSAGDGASKAGLCSRTCESDHCTTPPLLRYGKYCGILYSGCPGEQPCDELDACCMHHDNCVQAKNDYLSTACNEELLECLARLREGSSTFQGNKCMIDEVIDVISLVIEAAVVAGRLLHKP
Protein: Anoctamin (A0A8I6AHD2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU280814}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU280814}.
Interaction partners:
Sequence:
MRMETLEEFNGKPDSLFFTDGQRRIDFVLVYEDESKKENNKKGTNEKQKRKRQAYESNLISHGLQLEATRSVSDDKLVFVKVHAPWEVLCTYAEIMHIKLPLKPNDLKTRSTFDTFNWFTKVLRVNESVIKPEQEFFTAPFEKSRMNDFYILDRDSFFNPATRSRIVYFILSRVKYQVMNNVNKFGINRLVSSGIYKAAFPLHDCKFNYKSEDPNCPSERYLLYREWAHPRSIYKKQPLDLIRKYYGEKIGIYFAWLGYYTQMLLLAAVVGVACFLYGYLNQDNCTWSKEVCDPDIGGQILMCPQCDRLCPFWRLNITCESSKKLCIFDSFGTLIFAVFMGVWVTLFLEFWKRRQAELEYEWDTVELQQEEQPRPEYEAQCNHVVINEITQEEERIPFTTCGKCIRITLCASAVFFWILLIIASVIGIIVYRLSVFIVFSTTLPKNPNGTDPIQKYLTPQMATSITASIISFIIIMILNTIYEKVAIMITNFELPRTQTDYENSLTMKMFLFQFVNYYSSCFYIAFFKGKFVGYPGDPVYWLGKYRNEECDPGGCLLELTTQLTIIMGGKAIWNNIQEVLLPWVMNLIGRYKRVSGSEKITPRWEQDYHLQPMGRLGLFYEYLEMIIQFGFVTLFVASFPLAPLLALVNNILEIRVDAWKLTTQFRRMVPEKAQDIGAWQPIMQGIAILAVVTNAMIIAFTSDMIPRLVYYWSFSIPPYGDHTYYTMDGYINNTLSVFNITDFKNTDKENPYIGLGNYTLCRYRDFRNPPGHPQEYKHNIYYWHVIAAKLAFIIVMEHVIYSVKFFISYAIPDVSKITKSKIKREKYLTQKLLHESHLKDLTKNMGLIAERIGGVADSSVRPKLE
Protein: J protein JJJ1 (P53863)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cytoplasmic 60S subunit biogenesis factor REI1
- Probable metalloprotease ARX1
- Diphthamide biosynthesis protein 4
- Pre-mRNA-splicing factor CWC23
- J protein JJJ2
- Auxilin-like clathrin uncoating factor SWA2
- 60S ribosomal export protein NMD3
- ER-localized J domain-containing protein 5
- J domain-containing protein 1
- Glutathione-specific gamma-glutamylcyclotransferase
Sequence:
MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNVEEATQKFAVIRAAYEVLSDPQERAWYDSHKEQILNDTPPSTDDYYDYEVDATVTGVTTDELLLFFNSALYTKIDNSAAGIYQIAGKIFAKLAKDEILSGKRLGKFSEYQDDVFEQDINSIGYLKACDNFINKTDKLLYPLFGYSPTDYEYLKHFYKTWSAFNTLKSFSWKDEYMYSKNYDRRTKREVNRRNEKARQQARNEYNKTVKRFVVFIKKLDKRMKEGAKIAEEQRKLKEQQRKNELNNRRKFGNDNNDEEKFHLQSWQTVKEENWDELEKVYDNFGEFENSKNDKEGEVLIYECFICNKTFKSEKQLKNHINTKLHKKNMEEIRKEMEEENITLGLDNLSDLEKFDSADESVKEKEDIDLQALQAELAEIERKLAESSSEDESEDDNLNIEMDIEVEDVSSDENVHVNTKNKKKRKKKKKAKVDTETEESESFDDTKDKRSNELDDLLASLGDKGLQTDDDEDWSTKAKKKKGKQPKKNSKSTKSTPSLSTLPSSMSPTSAIEVCTTCGESFDSRNKLFNHVKIAGHAAVKNVVKRKKVKTKRI
Protein: Serine/threonine-protein kinase SKM1 (EC 2.7.11.1) (Protein kinase 75490 D) (Q12469)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in cellular signaling or cytoskeletal functions. May play a role in morphogenetic control.
Interaction partners:
- Cell division control protein 42
- Bud emergence protein 1
- Serine/threonine-protein kinase STE11
- Serine/threonine-protein kinase CLA4
- Guanine nucleotide-binding protein subunit beta
- Serine/threonine-protein kinase STE20
- Guanine nucleotide-binding protein subunit gamma
- GTP-binding protein RHO5
- Morphogenesis-related protein MSB1
Sequence:
MKGVKKEGWISYKVDGLFSFLWQKRYLVLNDSYLAFYKSDKCNEEPVLSVPLTSITNVSRIQLKQNCFEILRATDQKENISPINSYFYESNSKRSIFISTRTERDLHGWLDAIFAKCPLLSGVSSPTNFTHKVHVGFDPKVGNFVGVPDSWAKLLQTSEITYDDWNRNSKAVIKALQFYEDYNGLDTMQFNDHLNTSLDLKPLKSPTRYIINKRTNSIKRSVSRTLRKGKTDSILPVYQSELKPFPRPSDDDYKFTNIEDNKVREEGRVHVSKESTADSQTKQLGKKEQKVIQSHLRRHDNNSTFRPHRLAPSAPATKNHDSKTKWHKEDLLELKNNDDSNEIIMKMKTVAIDVNPRPYFQLVEKAGQGASGAVYLSKRIKLPQENDPRFLKSHCHRVVGERVAIKQIRLSEQPKKQLIMNELLVMNDSRQENIVNFLEAYIIDDEELWVIMEYMEGGCLTDILDAVARSNTGEHSSPLNENQMAYIVKETCQGLKFLHNKKIIHRDIKSDNILLNSQGLVKITDFGFCVELTEKRSKRATMVGTPYWMAPEIVNQKGYDEKVDVWSLGIMLIEMIEGEPPYLNEDPLKALYLIANNGSPKLRHPESVSKQTKQFLDACLQVNVESRASVRKLLTFEFLSMACSPEQLKVSLKWH
Protein: DNA-directed RNA polymerase subunit Rpo3 (EC 2.7.7.6) (DNA-directed RNA polymerase subunit D) (P39471)
Organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00320}.
Interaction partners:
- Small ribosomal subunit protein uS17
- DNA-directed RNA polymerase subunit Rpo1C
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS2
- DNA-directed RNA polymerase subunit Rpo11
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL3
Sequence:
MPISLIERNGLRLRLVLENYPLEFVNSIRRASILYVPVMAVDEVYFIENNSPLYDEILAHRLALVPFVSDEALEHYRPPEECAECKENCDGCYNRVYLDVEAKDQPLMIYSRDLKSEDQMITPVSGAIPIVLLGSKQKISLEARLRLGYGKEHIKYSPVSVSIVRYYPKVTVLGNCEKAVEVCPEGVFAMENNKLVVKNELSCILCEECLKYCAGSVSIESVENKFILEIESVGSLKPERILIEASKSLLRKLSELKSKLEAGK
Protein: Protein FIP2 (FRIGIDA-interacting protein 2) (O23550)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Casein kinase 1-like protein 10
- At5g26610
- Cytochrome P450, family 702, subfamily A, polypeptide 8
- Nuclear pore complex protein NUP35
- DExH-box ATP-dependent RNA helicase DExH14
- At3g16760
- Serine/threonine-protein kinase AFC3
- Protein phosphatase inhibitor 2
- Trihelix transcription factor GT-3a
- Trihelix transcription factor ASIL2
Sequence:
MGFAPVTPAAVETYDPDVDHDDESNGLDGFRVRSKRSGKFSGGYSDSPREVGDGYGVRSRARSNMKMYGGFKSEFDSDHDSGSGFGLKRKYNGNPKVSADFDADSDDEIVLVPKATRLRTHGKPSSGDFSHGSGGGFPLKSFGDRNFASHGFKPKNFSKPEPNFSQDLDYDDEFDDDRAEREGFNPRIQSSRSSSRVNGYSRKDGSYPRNTGASNGYGSSSRFKHEQMNAAAEVESDPIDEVVSSVKMLTEMFVRVENSKMEMMREMEKSRMEMELKHCQMMLESQQQIIGAFAEALSEKKSTNARRPVS
Protein: Acyl-coenzyme A diphosphatase fit1 (EC 3.6.1.-) (Acyl-coenzyme A diphosphatase scs3) (FIT family protein scs3) (Q9HGM4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (By similarity). May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (By similarity). May play a role in the regulation of cell morphology and cytoskeletal organization (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03231, ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03231}. Note=Enriched at sites of lipid droplet (LD) biogenesis. {ECO:0000250|UniProtKB:P53012}.
Interaction partners:
- Probable diacylglycerol pyrophosphate phosphatase 1
Sequence:
MTEKTASHYWNEETSILKLRRKDILLFEIYATTLLLGSIYSIYVDKWSITSYFGNSKNLINLIFVKRGWFWTSLVYFYHAWDQKRNKIDFKFISRYIVATLWWMFVTQWFIGPGLIDRTFALSGGSCKNFDGDSSVFIPLTASTCKGLNGSWSGGHDLSGHVFLLTHSSLFMLSENFSFILNNGIKATSTKVLFGLLGLWWWMLFVTASFYHTTFEKCTGFFSGILEWSIVYVFSSRMPAVADLLGSSDY
Protein: Uncharacterized PPE family protein PPE58 (Q50702)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- PPE family protein PPE57
- PE-PGRS family protein PE_PGRS21
- PE-PGRS family protein PE_PGRS19
- PE-PGRS family protein PE_PGRS3
- Uncharacterized protein Rv1899c
- Uncharacterized PPE family protein PPE59
- Uncharacterized PE-PGRS family protein PE_PGRS10
Sequence:
MHLMIPAEYISNVIYEGPRADSLYAADQRLRQLADSVRTTAESLNTTLDELHENWKGSSSEWMADAALRYLDWLSKHSRQILRTARVIESLVMAYEETLLRVVPPATIANNREEVRRLIASNVAGGKHSSNRRPRGTIRAVPGRKYPSNGPLSKLDPICAIEAAPMAGAAADPQERVGPRGRRGLAGQQQCRGRPGPSLRCSHDTPRFQMNQAFHTMVNMLLTCFACQEKPR
Protein: Polymerase basic protein 2 (RNA-directed RNA polymerase subunit P3) (Q9Q0V1)
Organism: Influenza A virus (strain A/Goose/Guangdong/1/1996 H5N1 genotype Gs/Gd)
Function: Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04062}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04062}.
Interaction partners:
Sequence:
MERIKELRDLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRIMEMIPERNEQGQTLWSKTNDAGSDRVMVSPLAVTWWNRNGPTTSTVHYPKVYKTYFEKVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKIAPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRATVSADPLASLLEMCHSTQIGGIRMVDILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTNGSSVKKEEEVLTGNLQTLKIKVHEGYEEFTMVGRRATAILRKATRRLIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGIEPIDNVMGMIGILPDMTPSAEMSLRGVRVSKMGVDEYSSTERVVVSIDRFLRVRDQQGNVLLSPEEVSETQGTEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQDPTMLYNKMEFESFQSLVPKAARSQYSGFVRTLFQQMRDVLGTFDTVQIIKLLPFAAAPPEPSRMQFSSLTVNVRGSGMRILVRGNSPVFNYNKATKRLTVLGKDAGALTEDPDEGTAGVESAVLRGFLILGREDKRYGPALSINELSNLAKGEKANVLIMQGDVVLVMKRKRDFSILTDSQTATKRIRMAIN
Protein: Centrin 3 (E5RFM2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLALRSELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDEAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSVLKNILLLPIWSRCLSLNREFFSEVNQEEFIAIMTGDI
Protein: Farnesol dehydrogenase (EC 1.1.1.216) (NADP(+)-dependent farnesol dehydrogenase 1) (AaSDR-1) (D2WKD9)
Organism: Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
Function: Mediates oxidation of farnesol into farnesal, a precursor of juvenile hormone in the corpora allata (CA), the glands that synthesize juvenile hormone. Able to oxidize C(10) to C(15) isoprenoid and aliphatic alcohols.
Interaction partners:
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase domain-containing protein
- aldehyde dehydrogenase
- AAEL009948-PA
- Aldehyde dehydrogenase
Sequence:
MDRWAGKVAVVTGASSGIGAAITTDLAKAGMVVVGLARRVERVEALKANLPESAKPRLHAVKCDVSKEEDITQVFKWVEKKFGGVDVLVNNAGILRQTDLLGTDNGQMLREVLDTNVMGLVLCSQKAYQSMKKRSVDGHIVHINSVVGHKVFDFPQSNIYPASKHAVTAITETMRNELRNAGSRIKVTSISPGVVRTEILPESIIEGGHALLESEDISEAVLYVLGTPPRVQVHELTIKPVGEKF