wanglab/gogpt-training-data huggingface dataset:
Protein: POTE ankyrin domain family member I (P0CG38)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVAEVDSMPAASSVKKPFVLRSKMGKWCRHCFPCCRGSGKSNVGTSGDQDDSTMKTLRSKMGKWCCHCFPCCRGSGKSNVGTSGDHDDSAMKTLRSKMGKWCCHCFPCCRGSGKSNVGAWGDYDDSAFVEPRYHVRREDLDKLHRAAWWGKVARKDLIVMLRDTDVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKISSENSNPEQDLKLTSEEESQRFKGSENSQPEKMSQEPEINKDGDREVEEEMKKHESNNVGLLENLSNGVTAGNGDDGLIPQRKSRTPENQQFPDNESEEYHRICELVSDYKEKQMPKYSSENSNPEQDLKLTSEEESQRLKGSENGQPEKRSQEPEINKDGDRELENFMAIEEMKKHGSTHVGFPENLTNGATAGNGDDGLIPPRKSRTPESQQFPDTENEEYHSDEQNDTQKQFCEEQNTGILHDEILIHEEKQIEVVEKMNSELSLSCKKEKDFLHENSTLREEIAMLRLELDTMKHQSQLRKKKYLEDIESVKKKNDNLLKALQLNELTMDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPIYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMAASSSSLEKSYELPDGQVITIGNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMLKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Methyltransferase, putative (EC 2.1.1.-) (Q388U8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleolar complex protein 2
- 60S ribosome subunit biogenesis protein NIP7 homolog
- RNA-binding protein, putative
- Nucleolar GTP-binding protein 1
- Methionyl-trna formyltransferase
Sequence:
MWKPKQRCKRQRNPLTPALSALIARVSPQLDPSAPLRFLLSFATQQTAAEGVDESNGDGASPVIEGEGIIRLCKELGDSVSGCDLWEIARRIPRSRSTPDCIDVTELCFAIDQAAAPLSVHDRRRGVGSKIPMDENAPLLKYYKGDRFASLFECTNGADVGKEWCEFLTCATSPLPMTLRVHRNERVMVSIANEFLKNDPTVSSVLRPVVPLMPTSVALFGCSHAAYHADSYVEHICRTLHAASAVSFQEVVSALPVIVAGIQPHHTVLDMCAAPGSKTLQALDEMLKNGWNSSAVSSGVMVANEKDRVKATQTLPARLKRYHAPNVICTRCDAVQWPRLLCPTTQGDMHLGERRFDRVICDVPCSGDGTLRKEPSLASSWSAGYVKSLLPTQRALLRRGLDLLETDGILVYSTCSLQPKEDEEVVCAGLELFGDAVELLDVSSILRECGVQLHSFGGLLSPDTTHLRNSVLPNSYDGRKVLRVLPHKDDTGGFFIAAFRKLSGPVPVSPPVQIRKLNHWMKGKLWLQVAKEDEVWCNITDFYGIDRNDGDSFHYYGEEEREQGGLQHREDRRGDSKFGLVPVYHLNPNGGPYRRIVLMTLAAARMLFGTRPYKGPGVEIVSAGVRAFEAYDGKFLWDATCRWRAVVESASYLSSIAHARKIVINADHHPQVVKDLLSNGFVWLHEQWRCVLCQDASTTDGDLDKGSSFLRSTNSLKDLLALRDGEGEGMLKVQELLNECVVVGGVLLGLEGGKLAHREGPWWLSGTLSRTKLEVAIDVSLRAFGLLSFLGISSEERACPPDVRDP
Protein: Probable histone-binding protein rba-1 (P90917)
Organism: Caenorhabditis elegans
Function: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA (By similarity). Plays a role in regulating cell cycle progression. Required to repress the induction of vulval development by Ras signaling. In association with the zinc finger protein ztf-11, negatively regulates the expression of non-neuronal genes during neurogenesis.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- WD_REPEATS_REGION domain-containing protein
- Polycomb protein mes-6
- Histone-lysine N-methyltransferase mes-2
- DIOX_N domain-containing protein
- Chromatin assembly factor 1 subunit A dimerization domain-containing protein
- Mortality factor related protein 1
- Protein lin-9
- Histone acetyltransferase type B catalytic subunit
- Chromodomain-helicase-DNA-binding protein 3 homolog
- Histone deacetylase
Sequence:
MSEAESCEETSKEHRIWKKNVPYLYDTVVTKEVEWPSLSVQWMPDVTKTENSDSSMHRMIHGTHTCGGVQNHLMISKFTITTDTPEFDDAKWDSEREEFGGYGEGSAAKWDTEIKINHPGEVHRARYMPHNPFIIASRGPSDDVYIFDYTKHPSEPKDTKFRPQLRLKGHEGEGYGMSWSNTREGHLLTAGDDGMICHWDINANQTISGQIVPQSKFKGHSSNAEDVSFHALHNFVFGSVGDDRKLNLWDLRQSKPQLTAVGHTAEVNCITFNPFSEYILATGSVDKTVALWDMRNMRKKMYTLKHHNDEIFQVSFSPHYETVLASSGSDDRVIVWDISKIQDPSSSSAASSDSVPPEVIFIHAGHTGKVADFSWNPNRPWTICSSDEFNALQVWEVSNSLVSSEKWETEMI
Protein: ETFB lysine methyltransferase (Protein N-lysine methyltransferase METTL20) (Q9FN34)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Calmodulin-lysine N-methyltransferase
- Protein arginine N-methyltransferase 1.6
- Large ribosomal subunit protein uL11c
- tRNA
- tRNA
- Class I peptide chain release factor
- Putative ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit N-methyltransferase I
- Rubisco methyltransferase family protein
- F21J9.27
- [Fructose-bisphosphate aldolase]-lysine N-methyltransferase, chloroplastic
Sequence:
MLAWNFIKHFPCKNLSRHILRDSRVRPLCFFTSSTPPSSFSIFASLSTSSSSSSSSSCFTDESFAAPYLSVRIHCPKHALDPFSEALLCFGASSVAVDEAIEEADQDETSLASKEICIESIFPVHEEVKMCISQAANSIGLKEIPKFKVEMGDELDWITKNQDLFQPVEIAERLWIVPEWTSPPVAEAVNIILNPGFAFGTGEHPTTKLCLLLLQSLIKGGEAFLDYGTGSGILAIAALKFGAASSVGVDIDPLAINSAIHNAALNNIPLEKLELHLAPIENSSSGREIPLQKEQFDVVIANILLNPVMNLADHILSFVKPGATIGISGILSEQLPNVRERYSPFLEDISVATIGDWVCMSGTKKEEFIDN
Protein: Spindle assembly checkpoint protein BUB3 (Cell cycle arrest protein BUB3) (P26449)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for cell cycle arrest in response to loss of microtubule function. Component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Component of the mitotic checkpoint complex (MCC) which inhibits the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20. The formation of a MAD1-BUB1-BUB3 complex seems to be required for the spindle checkpoint mechanism.
Subcellular location: Nucleus {ECO:0000269|PubMed:24066227}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:24066227}.
Interaction partners:
- Spindle assembly checkpoint serine/threonine-protein kinase BUB1
- Spindle assembly checkpoint component MAD3
- APC/C activator protein CDC20
- Mitotic spindle checkpoint component MAD2
- Outer kinetochore KNL1 complex subunit SPC105
- Anaphase-promoting complex subunit CDC27
- S-phase entry cyclin-5
- Protein SIC1
- Regulatory protein SWI6
- Regulatory protein SWI4
Sequence:
MQIVQIEQAPKDYISDIKIIPSKSLLLITSWDGSLTVYKFDIQAKNVDLLQSLRYKHPLLCCNFIDNTDLQIYVGTVQGEILKVDLIGSPSFQALTNNEANLGICRICKYGDDKLIAASWDGLIEVIDPRNYGDGVIAVKNLNSNNTKVKNKIFTMDTNSSRLIVGMNNSQVQWFRLPLCEDDNGTIEESGLKYQIRDVALLPKEQEGYACSSIDGRVAVEFFDDQGDDYNSSKRFAFRCHRLNLKDTNLAYPVNSIEFSPRHKFLYTAGSDGIISCWNLQTRKKIKNFAKFNEDSVVKIACSDNILCLATSDDTFKTNAAIDQTIELNASSIYIIFDYEN
Protein: 3',5'-cyclic-AMP phosphodiesterase 4A (EC 3.1.4.53) (DPDE2) (cAMP-specific phosphodiesterase 4A) (P54748)
Organism: Rattus norvegicus (Rat)
Function: Hydrolyzes the second messenger 3',5'-cyclic AMP (cAMP), which is a key regulator of many important physiological processes.
Subcellular location: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:8557632}. Membrane; Peripheral membrane protein {ECO:0000269|PubMed:8557632}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Adenosine kinase
- Adenine phosphoribosyltransferase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- GTP:AMP phosphotransferase AK3, mitochondrial
- Deoxycytidine kinase
- Adenylosuccinate lyase
- Adenylate cyclase type 3
Sequence:
MEPPAAPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYPDSAERSETERSPHRPIERADAVDTGDRPGLRTTRMSWPSSFHGTGTGGGSSRRLEAENGPTPSPGRSPLDSQASPGLVLHAGATTSQRRESFLYRSDSDYDMSPKAVSRSSSVASEAHAEDLIVTPFAQVLASLRSVRSNFSLLTNVPIPSNKRSPLGGPPSVCKATLSEETCQQLARETLEELDWCLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNEVEIPSPTPRQRAFQQPPPSVLRQSQPMSQITGLKKLVHTGSLNTNVPRFGVKTDQEDLLAQELENLSKWGLNIFCVSEYAGGRSLSCIMYTIFQERDLLKKFHIPVDTMMMYMLTLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEENCDIFQNLSKRQRQSLRKMVIDMVLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLELYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNRDWYHSAIRQSPSPPLEEEPGGLGHPSLPDKFQFELTLEEEEEEDSLEVPGLPTTEETFLAAEDARAQAVDWSKVKGPSTTVVEVAERLKQETASAYGAPQESMEAVGCSFSPGTPILPDVRTLSSSEEAPGLLGLPSTAAEVEAPRDHLAATRACSACSGTSGDNSAIISAPGRWGSGGDPA
Protein: NsP2 protein (F2YI08)
Organism: Chikungunya virus (CHIKV)
Interaction partners:
Sequence:
GIIETPRGAIKVTAQPTDHVVGEYLVLSPQTVLRSQKLSLIHALAEQVKTCTHNGRAGRYAVEAYDGRVLVPSGYAISPEDFQSLSESATMVYNEREFVNRKLHHIAMHGPALNTDEESYELVRAERTEHEYVYDVDQRRCCKKEEAAGLVLVGDLTNPPYHEFAYEGLKIRPACPYKIAVIGVFGVPGSGKSAIIKNLVTRQDLVTSGKKENCQEITTDVMRQRGLEISARTVDSLLLNGCNRPVDVLYVDEAFACHSGTLLALIALVRPRQKVVLCGDPKQCGFFNMMQMKVNYNHNICTQVYHKSISRRCTLPVTAIVSSLHYEGKMRTTNEYNKPIVVDTTGSTKPDPGDLVLTCFRGWVKQLQIDYRGYEVMTAAASQGLTRKGVYAVRQKVNENPLYASTSEHVNVLLTRTEGKLVWKTLSGDPWIKTLQNPPKGNFKATIKEWEVEHASIMAGICSHQMTFDTFQNKANVCWAKSLVPILETAGIKLNDRQWSQIIQAFKEDKAYSPEVALNEICTRMYGVDLDSGLFSKPLVSVYYADNHWDNRPGGKMFGFNPEAASILERKYPFTKGKWNINKQICVTTRRIEDFNPTTNIIPANRRLPHSLVAEHRPVKGERMEWLVNKINGHHVLLVSDYNLALPTKRVTWVAPLGVRGADYTYNLELGLPATLGRYDLVVINIHTPFRIHHYQQCVDHAMKLQMLGGDSLRLLKPGGSLLIRAYGYADRTSERVICVLGRKFRSSRALKPPCVTSNTEMFFLFSNFDNGRRNFTTHVMNNQLNAAFVGQATRAGC
Protein: Pectate lyase PEL9 (EC 4.2.2.2) (AnPL9) (Q5BA93)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Presents an endo-cleaving activity on the homogalacturonan (HG) region in pectin. Active on homogalacturonan with a degree of polymerization above 4, and does not appear to be affected by the degree of methylation of the substrate. Does not degrade linear rhamnogalacturonan.
Subcellular location: Secreted {ECO:0000305|PubMed:35802235}.
Interaction partners:
Sequence:
MMGKSVWVFAALFPAVLAADIYVSPDGSDDAAGTIDAPLQSIQLAVDQATAGSTIYLRGGTYTPTSNIQITKSGTASAPYVLRAYEGESVIIDGEELPGTPADLDASLDNADRGILHIQDAEYWEFYDLELINGPYGVYARDASNNHYERITTRNNYETGFQLQGESSNNVVLYLDSYGNRDPRKNGESADGFACKEGSGEGNILRGARLWNNVDDGLDLWYAVNPVHPRISANTSREFKSAVTIEDTIAWGNGFNRWDFTPFEGDGNGFKLGGGDDTDIGPADHIITNCIAFSNAKDGFTDNSQPGNFVLTRNTAWDNTAVGFKFGTAVATLTGNIAASNGEAPTSLSDEQISDGNSWDGDEDWDDGSFVSVDVSLVQGERNADGTIEPSGFLLPADGEEIGATTDWSA
Protein: Serine/threonine-protein phosphatase 1 regulatory subunit 10 (MHC class I region proline-rich protein CAT53) (Q80W00)
Organism: Mus musculus (Mouse)
Function: Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}. Note=Found in discrete nucleoplasmic bodies and within nucleoli (By similarity). Associates with chromatin during interphase, excluded from condensed chromosomes during early mitosis and is reloaded onto chromosomes at the late telophase. {ECO:0000250, ECO:0000269|PubMed:20516061}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- WD repeat-containing protein 82
- TOX high mobility group box family member 4
- Nuclear inhibitor of protein phosphatase 1
- Protein phosphatase 1 regulatory subunit 12A
Sequence:
MGSGPIDPKELLKGLDSFLTRDGEVKSVDGISKIFSLMKEARKMVSRCTYLNIILQTRAPEVLVKFIDVGGYKLLNNWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKEEGKSRTTLPERPLTEVKAETRAEEAPEKKKEKPKSLRTTAPSHAKFRSTGLELDTPSLVPVKKNSSTVVVSDKYNLKPIPLKRQSATAAPGDAAPPAEKKYKPLNTAPNTTKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPSPFEGKTSTEQSTAKPSSPEPAPPAEPMDTDRPGTPVPPVEVPELMDAASSEPGALDAKPVDSPGDPNQLTRKGRKRKTVTWPEEGKLREYFYFELDETERVNVNKIKDFGEAAKREILSDRHAFETARRLSHDNMEEKVPWVCPRPLVLPSPLVIPGSNSQERYIQAEREKGILQELFLNKESPHEPDPEPYEPIPPKLIPLDEECAMDETPYVETLEPGGSGGSPDGAGGSKLPPVLANLMGSMGAGKSPQGPGGGGINVQEILTSIMGSPNSHPSEELLKQPDYSDKLKQMLVPHGLLGPGPVANGFPPGGPGGPKGMQHFPPGPGGPMPGPHGGPGGPVGPRLLGPPPPSRGGDPFWDGPGDPMRGGPMRGGPGPAPGPYHRGRGGRGGNEPPPPPPFRGARGGRSGGGPPNGRGGPGGGGMVGGGGHRPHEGPGGSMGSGHRSHDGPGGNMGSGHRSHDGPGGNMGGSGGHRSHEGPGHGGPHGHRPHDVPSHRGHDHRGPPPHEHRGHDGHGGGGHRGHDGGHSHGGDMSNRPVCRHFMMKGNCRYENNCAFYHPGVNGPPLP
Protein: Thioredoxin-like protein CITRX, chloroplastic (EC 1.8.-.-) (Cf-9-interacting thioredoxin) (LeCiTrx) (Q9LKW0)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Probable thiol-disulfide oxidoreductase that may play a role in proper chloroplast development.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Carbohydrate kinase PfkB domain-containing protein
- Thioredoxin
- Thioredoxin
- Thioredoxin
- Thioredoxin
- Thioredoxin
- 60S ribosomal protein L18a
- 60S ribosomal protein L18a
- NRC1
- CONSTANS interacting protein 5
Sequence:
MQAASLAFHPPALRTSPSYLSSKLPHHLNYSLFKHAPSTSTLSLTQVLSRNTICKPPAVGKYVREDYLVKKLSAKEIQELIKGERNVPLIIDFYATWCGPCILMAQELEMLAVEYENNALIVKVDTDDEYEFARDMQVRGLPTLYFISPDSSKDAIRTEGLIPIQMMRDIIDNDL
Protein: Transcription factor steA (O74252)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Transcription factor involved in sexual reproduction. Required for cleistothecial development and ascosporogenesis. Not required for asexual reproduction (conidiation). May act to repress medA expression.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mitogen-activated protein kinase
- Conidiophore development regulator abaA
- Importin beta-3 subunit, putative
- Mitogen-activated protein kinase hog1
- mitogen-activated protein kinase kinase kinase
Sequence:
MYSQHGAPMAPPQKPETFMLSNEAQQSLPHDAQVALQQVDNLKYFLLSAPVDWQPDQLIRRFLLPTGDYISCVLWSNLFHISGTDIVRCLAFRFQAFGRPVKNSKKFEEGIFSDLRNLKAGTDATLEEPKSPFLDFLYKNNCIRTQKKQKVFYWYSVPHDRLFLDALERDLKREKMGQEATTVAVSEPALSFEFDSSQSLYEQLTKAQQANSSSFAAHASTTYGQSASPVVRTVDAMPPPQMAPQMAPPSIPLLTDESANSQMYTSIPMPNPIPQNLIKREADYGAIQYDRNGMPIARIHQRHSSMPTFVEYSPAPSFVSSQYEDYSNRGLSFEPVTPPQHSSHIGPEPAYIANEDTGLYTAIPEMSTGSGFNPMMHLPPSNLASAHFPTPARTFHSNVYSVLEGSPTYKQRRRRSSIPPGAANPVTTGTHSPAPALSYAAHKPSDLRRSVSSSVAPGDTDDSRHESLHRSVNSTYTATLPQKNLMHEMSRNGTPLSSVGEHREQSSIPLTQAEDLPALPANGTVESGAPNGVGHKSDRYATGPVRRARSATMMELGPYPQKSHSCPIPSCGRLFKRLEHLKRHVRTHTQERPYPCPYCNKAFSRSDNLAQHRRIHEAQQDGQPLVHEDDLENDDNESVSHDEDESPSESVHPAVPGVHGMTSMPSSVALQSTMGSMMGSHMIAPQLLQQQI
Protein: Melanoma inhibitory activity protein 2 (CTAGE family member 5 ER export factor) (Q91ZV0)
Organism: Mus musculus (Mouse)
Function: Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum. Plays a role in the secretion of lipoproteins, pre-chylomicrons and pre-VLDLs, by participating in their export from the endoplasmic reticulum (By similarity). Thereby, may play a role in cholesterol and triglyceride homeostasis. Required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers and recruiting PREB/SEC12 at the endoplasmic reticulum exit sites (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21807889}; Single-pass membrane protein {ECO:0000305|PubMed:21807889}. Note=Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). {ECO:0000269|PubMed:21807889}.
Interaction partners:
- Transport and Golgi organization protein 1 homolog
- Guanine nucleotide-exchange factor SEC12
- Protein transport protein Sec23A
- SEC24 homolog B, COPII coat complex component)
- SEC24 homolog C, COPII coat complex component
- Protein SEC13 homolog
- Protein transport protein Sec16A
Sequence:
MAEVSVQRILLLVVSLAKCLEGTKLLAHLKKCGDLECETLISRVLALRDYTGPDCRYLNFTTGEEISVYVKLGGDREDLWAGSKGKDFGFFPRDAVEIEEVFISEEVEMPTKSDFLCLLGEGYIFGSEQSELNSEDDEEHMYPYEKDEDQNYNIYEGDFQPEPDLYAAAEGTLLEDQIPASEAPDDFRFSSEWKAWEGAGSQGGGEQDYTADSDQDLPSLSKPERQGWFGLGTEEAEEKVFESDTEPTQELALEEESDLEKLHSGEPQVELEQEPKSETLEFSSVPDEEYELESETESILKPQASGWFGEGLTSYLGFGNEEAGLELLSKESNPPLQDIPSSVPPDEEVPAPCREISTDKEDAVINDSSVLSPSWFYYGFGMLGFTNADEDNIVSDKGENEDGEVDNLKHPIGSDFDPEKEQERKIVTVETEDQAGTESVLEKTDESGSMQYLKKFFDNPWGFQSLPEDTELPFSKKMLDQDDIVENDKIEELSTENSPTGSMKDPVMLASRYVLSDIDSEVELPMEEHEGVHFKPSSSKRNEDDSNSWADPEELSVAQTDGSAEGALLDTQLVSPKEHAADFQLLKYLLQIDVYGFMSSALSPIEILLESVVAALPEDMRADFNPSGFSLELAVCVLSVGLLAVVLFLWRGFRSIRSRFYVGREKKLALELSALIEEKCKLLDKVSIVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEATYENLEQSKSKLEDEILLLEEKLEEERAKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQKVALEESRAQAEQALSEKESQIETLVTSLLKMKDWAAVLGEADDGNLDLDMKSGLENTAALDNQPKGALKKLIYAAKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKENAHNRQKLTETEFKFELLEKDPYALDVPNTAFGREHSPYGPSPLGRPPSETRAFLSPPTLLEGPLRLSPLLPGGGGRGSRGPENLLDHQMNTERGESSYDRLSDAPRAPSDRSLSPPWEQDRRMTAHPPPGQPYSDPALQRQDRFYPNSGRLSGPAELRSYNMPSLDKVDGPVPSEMESSGNGTKDNLGNSNVPDSPIPAECEAAGRGFFPPPFPPVRDPLFPVDPRSQFMRRGPSFPPPPPGSIYAAPRDYFPPRDFPGPPLPPFPGRTVYAPRGFPPYLPPRAGFFPPPPHPESRSELPPDLIPPSKEPAADPPETQEA
Protein: Lipopolysaccharide export system permease protein LptF (P0AF98)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Lipopolysaccharide export system ATP-binding protein LptB
- Lipopolysaccharide export system permease protein LptG
- LPS-assembly protein LptD
- Lipopolysaccharide export system protein LptC
- Lipopolysaccharide export system protein LptA
- LPS-assembly lipoprotein LptE
- ATP-dependent lipid A-core flippase
- sn-glycerol-3-phosphate import ATP-binding protein UgpC
- Potassium-transporting ATPase KdpC subunit
- Methionine import ATP-binding protein MetN
Sequence:
MIIIRYLVRETLKSQLAILFILLLIFFCQKLVRILGAAVDGDIPANLVLSLLGLGVPEMAQLILPLSLFLGLLMTLGKLYTESEITVMHACGLSKAVLVKAAMILAVFTAIVAAVNVMWAGPWSSRHQDEVLAEAKANPGMAALAQGQFQQATNGSSVLFIESVDGSDFKDVFLAQIRPKGNARPSVVVADSGHLTQLRDGSQVVTLNQGTRFEGTALLRDFRITDFQDYQAIIGHQAVALDPNDTDQMDMRTLWNTDTDRARAELNWRITLVFTVFMMALMVVPLSVVNPRQGRVLSMLPAMLLYLLFFLIQTSLKSNGGKGKLDPTLWMWTVNLIYLALAIVLNLWDTVPVRRLRASFSRKGAV
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FTH4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome G complete sequence
- Polyubiquitin
- Candida glabrata strain CBS138 chromosome D complete sequence
- Elongation factor 3
- Candida glabrata strain CBS138 chromosome H complete sequence
- S16a
- L21
- 40S ribosomal protein S24
- Candida glabrata strain CBS138 chromosome F complete sequence
- 40S ribosomal protein S8
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLKALASKYNCEKSVCRKCYARLPPRATNCRKRKCGHTNQLRPKKKLK
Protein: Peroxisomal membrane protein PEX34 (Peroxin-34) (P25584)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: In concert with the three peroxisome divisional factors, PEX11, PEX25 and PEX27, controls peroxisome morphology and abundance under conditions of peroxisome proliferation. Maintains mature peroxisomes in actively dividing cells.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21441307}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21441307}.
Interaction partners:
- Peroxisomal membrane protein PEX25
- Peroxisomal membrane protein PEX27
- Peroxisomal membrane protein PMP27
- Mitofusin FZO1
- Peroxisomal membrane protein import receptor PEX19
- Peroxisomal biogenesis factor 3
- Peroxisomal membrane protein PEX30
- Mitochondrial fission 1 protein
- Uncharacterized protein YDL157C
- Uncharacterized protein YGR168C
Sequence:
MVSKKNTAEISAKDIWENIWSGVSSLLDFFAVLENLGVVNDKLYVSGLLRKVWLCYSCISVIKCVWKLIKLCKVKFKIDQRLDGEGNGLVKDKLINFKKKYNEHIRHITAALLQDLSYLMVLIYPGTRLFKRLSNIITLCRIIV
Protein: Sublancin immunity protein SunI (SPbeta prophage-derived protein YolF) (O31989)
Organism: Bacillus subtilis (strain 168)
Function: Is essential and sufficient to confer resistance to the bacteriocin sublancin 168.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19047653}; Single-pass membrane protein {ECO:0000305|PubMed:19047653}. Note=A small amount is also associated with the cell wall, but this is probably contamination. {ECO:0000269|PubMed:19047653}.
Interaction partners:
Sequence:
MEYVVMIIILLALFFIFTVFLNTRYSFDEKCLVLKFGLSKTEIPINQIVSIKESDKYGVADNIDYKIGMPYAQPDRIVIETTNKRFLVFLNGAQQFIQKYKRVSV
Protein: Protein SLM6 (Synthetic lethal with MSS4 protein 6) (P38343)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein YBR259W
- RNases MRP/P 32.9 kDa subunit
- Maintenance of telomere capping protein 4
- COMPASS component SHG1
- Trafficking protein particle complex subunit 20
Sequence:
MCSRFSSTSLKCLLCSQNRHCSSGISTLLRSFSCITLSAISSSVNCSGSSFLGSSFSLFSSFSCKESLLRSGVFPSWLFCMFSSILALAISNSFFFFSSNACFSLLFNSFLVTGFSFSADLLVLAAAADTLESNVSNDIGGNCATRLFKL
Protein: Coiled-coil-helix-coiled-coil-helix domain containing 3 (RE38619p) (Q9VA18)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- MICOS complex subunit Mic60
- SAM50-like protein CG7639
- MICOS complex subunit MIC13 homolog QIL1
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- MICOS complex subunit
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- ATP synthase subunit d, mitochondrial
- NADH dehydrogenase 23 kDa subunit
- ATP synthase subunit gamma, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
Sequence:
MGARQSQSREPRTVSMENPTPAGVIDISDDVVKRLKAGISQQAREHAAAAEESKPVPKPTTKAAAKPAASSPAASPAPKVSSYPAAVPIYVQGGGHTISAADVQRQMNQELIKNDELWKERMAKLEENLKKTNTILEKEYANAVENVHKRFVSTASSHKVPPCQDLKSQLLACYRAHPGETLKCIEEVAQFRQCIDLHRVQKLDAEPESSKVTSKATVPAKAA
Protein: 2-Cys peroxiredoxin BAS1-like, chloroplastic (2-Cys Prx B) (2-Cys peroxiredoxin B) (EC 1.11.1.24) (Thiol-specific antioxidant protein B) (Thioredoxin-dependent peroxiredoxin BAS1-like) (Q9C5R8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. May be an antioxidant enzyme particularly in the developing shoot and photosynthesizing leaf.
Subcellular location: Plastid, chloroplast {ECO:0000250|UniProtKB:Q96291}.
Interaction partners:
- NADPH-dependent thioredoxin reductase 3
- Sulfiredoxin, chloroplastic/mitochondrial
- Peroxiredoxin-2E, chloroplastic
- Thioredoxin M4, chloroplastic
- Uncharacterized protein MHF15.4
- Thioredoxin M1, chloroplastic
- Peroxiredoxin-2F, mitochondrial
- Thioredoxin-like protein CDSP32, chloroplastic
- Peroxiredoxin-2C
- Thioredoxin-like 2-1, chloroplastic
Sequence:
MSMASIASSSSTTLLSSSRVLLPSKSSLLSPTVSFPRIIPSSSASSSSLCSGFSSLGSLTTNRSASRRNFAVKAQADDLPLVGNKAPDFEAEAVFDQEFIKVKLSEYIGKKYVILFFYPLDFTFVCPTEITAFSDRYEEFEKLNTEVLGVSVDSVFSHLAWVQTDRKSGGLGDLNYPLVSDITKSISKSFGVLIPDQGIALRGLFIIDKEGVIQHSTINNLGIGRSVDETMRTLQALQYVQENPDEVCPAGWKPGEKSMKPDPKLSKEYFSAI
Protein: Kinetoplastid-specific dual specificity phosphatase (Q38BQ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRMIDSEDVAFFFAVMTWNPELLEIMLEKAPNPLYVERAAATEAARFAAAYPLPEETSKPVVSRCRPSARRQRRARKTKRGCGVRLSIPCAFFCEYEAPDFDEEDDFYCEDDEHAMQEKKGEGDPDSSVAEVEHDHEPDPNSYSPVEGWGRNAGNCIGRVVSDSVDSGDKPLGYSMRDFLQIFFQSFLIVSLSQVQSQRVQNEFPLSLSPLERKACEIVHRYKDPFKEILRKYVISGDCEVERHGAQPLFVDGFCIKAVQHEEGEKWAPPHEQLFIAGKDPVYQPLLMEMLGITRVVQCYAEKGANYPATLHACATAVGQAASGNRDRTVHTMQSWHRLLTQHPKLSKSSDGGTDIATANEDFDLPCPSEEEWEKLQGDISRCVTPLQWKTYTVFGPYLVFSATLPFSNGCVTKLVVPAEDKDTYDLSVHFQEGVFRYIHGTPLFPVDVGPALVPKERTRMEDQRSPLLAKSCLLHCSAGMHRSSALVIGYLLWLVALSGGKLPMEGKPTLAFVPGRYASYTHRQGSVFAESYLTVVLRSQQRGSFPTEEVSASPMHAGAAVVSVAPTQEPEREIQEEDVRAKAQLSDEKSILHYCADHVRQQRSMAVPIATALQQLHRYARHLHLA