wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin carboxyl-terminal hydrolase 47 (EC 3.4.19.12) (Ubiquitin thioesterase 47) (Ubiquitin-specific-processing protease 47) (Q22240)
Organism: Caenorhabditis elegans
Interaction partners:
- C2 domain-containing protein
Sequence:
MVRVEDSNGADTDTNPEGESSGYVRLAGNGLPGGEQQQASSSGVAAAPSVDSSPGRSVPLAIASSSSPANVANNQYAIPVDENGHRYVGLVNQAMTCYLNSLVQSLYMTPEFRNAMYDWEYVQQPAHIKEQRKKAEQSIPCQLQKLFLLLQTSENDSLETKDLTQSFGWTSNEAYDQHDVQELCRLMFDALEHKWKGTEHEKLIQDLYRGTMEDFVACLKCGRESVKTDYFLDLPLAVKPFGAIHAYKSVEEALTAFVQPELLDGSNQYMCENCKSKQDAHKGLRITQFPYLLTIQLKRFDFDYNTMHRIKLNDKMTFPDVLDLNDYVNKEKRSTTSSAWQQIGKNKSENEEDDMELGSPNPKRCTPGVQSPNRYQGSENVCVGQPIDHAAVDDIVKTSGDNVYELFSVMVHSGNAAGGHYFAYIKNLDQDRWYVFNDTRVDFATPLEIEKSFGGHPSGWNQSNTNAYMLMYRRIDPKRNARFILSNQLPQHIKDSQEKWKRLEREAEDERLRKLSLIQVYVTINYPFPSVVTLPDKKQLDLTPQKYQIAEDFGEYKTEISREMPIKNVFNHAFEFFNERARAYNLPFTKNSARLIYVEHGSLMMDFKSKADMDKKLRSVFNVNHGEPGSMYGVHFILDVRIASSFFPVDIKNKITIKVQRVDIGKKTTANELIVVVDANEKMIKVKSWIGGQFRDDIHGVLNARVVLEVASSRCEFMMIDVSHNATEFGSLIQQYVGHTTPTLYYDGGLNTMVTKESQEATLADRKLPFDKSVMYHILDRKCFSTMVKVRLPSQEEIEKAASTKNAYQGPTWAETIAIMKEEDRLWNEPRAAVEVMSTVSRTDTTDHALVADTDDEPIPSGRGSTASMRSVSMDDIDADIGISGSLCNNTPQMSPCVSEGDDADESQLDGKSQLMSDYMQKTSPDFYYNRDPQNHLNKNLKIALGDETPSESLSAVSSGQSTLVPSTSNQALSSMTRSDEAVDGKIVTVFSHENFHKLDVDSRMRVLEFKKWVAEQLEMDKDQFVIVKHASDDGSDSGYEANFMDDETVSGAFQSCFISIKLRAPLKSDEKMMQIILFDILENLRENWKPLFELPVSQSTVIGDVLLQCLRMYKEVYGEELTPKMVRLRELGGSGVGTGRAVLNPNDTLEKRSYNWCSHLYLQIITDEAMIGKPGEPIMVRRFRPSTVEVNPTHEVLVDANAENPVVSFVEALSKISGIPVERLAITDLKEFNWQKWPYLKSRLDMLENKVNFTKDLQVTYPLPREFLDKVGSRVLYYKDSDEEAKVLSEDERKQIKIKENGQSANANRRKERPLRIQMSSVCEA
Protein: 5'-3' exonuclease XRNA, putative (EC 3.1.11.-) (Q57XA6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 5'-3' exoribonuclease 2
- 5'-3' exonuclease XRNC, putative
- U6 snRNA-associated Sm-like protein LSm4
- Exosome component CSL4
- RNasePH-like protein exosome-associated protein 1 Rrp42 homologue
- Ribosomal RNA processing protein 45
- Centromere/microtubule binding protein cbf5, putative
- Exosome complex exonuclease RRP40
- Ribosomal RNA-processing protein 43
- Ribosomal RNA processing protein 4
Sequence:
MGVPKFFRWVAERYPSVITPFRDFPPPVDNLYLDMNGIIHNCTHPNDADATHKAPTEKAMVEAMFSYLEKLFNAIQPRKCFFLAVDGVAPRAKMNQQRQRRYRSGYEMMVAREEALSRGEELPEEADVFDSNCITPGTDFMVRISEHFQYFIMMKMSTDPAWQNCSVIYSGHDHPGEGEHKIVEFIRRRKMQPDYGPNETHCMYGLDADLVMLALATHEPHFVLLREVVTFGFGQESRRAREQREQDESDGIVADKSYQKPDEFVLFHVNVLRDYLDLEVRERLGDKLPTNYDLERVVDDFVLMCFFIGNDFLPSIPTLGIHDGSLVQMLDLYAQRVLLAHTYLTDMGRIDWRAVEGWLQGLADLEFTTIKAREAQEQEYQRRMAQQCGEHRAATISTSTVESLREYKDRYYRDKHQFAMGWDPQGEDMAKLRLHYIEGIMWVIGYYYQGPPSWKWYFPHHYAPMASDLVNLPAVAACVKFDPGKPFLPHQQLLAVLPPMSYRSMPRAYWPLLRSKNSPLARYFPEKLQIDREGTRAPWEGVVLIPFIEERTLLAAYETVQDRVTPEERKNNRLGLPTLYAYDPTIEAYEVPNSLFGPLRRTTVRRDAFDFPPLTKFIPRLCTGVCTGEQQFEGFTTLRSKWRYITPQRESGVVTIFGMPARGESLLLGLKDSFNAIAAHEVATLVGQEVLVGFPHYRRARVVAVSDKRVHISANINLEGVSCGANVRELNRDASMNIAKELETHRQCMREKLGMSVSNLTVLVYVNLFTGMRMTRKGRVVRNFSKDQTCYALPLVARLQDVKLTEDSRYVERDRVEWDNRFGSRVILVGAEPKSMKGKDQQLYGSSGVVVRSSPDAEGTFTVAARVFQKPVSIPHVLLDYASSRNWVSMPDVSNEVRVGPLALKHLVGSVRTSPQYGCREIGLGLIYTRNNLVRIGYAKQTVRGGKAWGAPGGRLGAGLENSDDAFGRPVQDAAPAGHYLESLQKGESRPRSSRPMQYMTWFSRKAVVLIKTYVERFKPLVDRLESIASSPQALDPPQFMTGEWADNDVDDVLRSIEEFIESCGIQSVPLVAAQDDAFPREHVRMLEEELDRQGPRPLEDRMLSSVARRCLYFPVTRCAGGHISQLPLPQEQTVHLGSRVVNCRACGAAPFGATGTVVRLLSTGHDAEVVYDDPFVGGSYFDGRLRQPRGSISKLSTLLVLNKPSGDESESSQGQNGSVVQNLKSICKKLQQKEDDHDQQQQHGRGVGIPSTEGTPSIPKPRSAMGETSASGIAAGRNVVSPSSLTVSGGSGGIQVAELMGKLASSKATSPDAGLNICGATYAPTVASNKLPVAPRSVTTTAAPGSGTFSVPLPRTSGNANRTNSGDGEGDKGCRKPGFSFTVPSEVLNGEFQIRPGEGALLLKRMISQHLSGDRKR
Protein: DNA damage-inducible transcript 3 protein (DDIT-3) (C/EBP zeta) (C/EBP-homologous protein) (CHOP) (C/EBP-homologous protein 10) (CHOP-10) (CCAAT/enhancer-binding protein homologous protein) (Growth arrest and DNA-damage-inducible protein GADD153) (Q62857)
Organism: Rattus norvegicus (Rat)
Function: Multifunctional transcription factor in ER stress response. Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress. Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activator of other genes. Acts as a dominant-negative regulator of C/EBP-induced transcription: dimerizes with members of the C/EBP family, impairs their association with C/EBP binding sites in the promoter regions, and inhibits the expression of C/EBP regulated genes. Positively regulates the transcription of TRIB3, IL6, IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA, BCL2L11/BIM and ERO1L. Negatively regulates; expression of BCL2 and MYOD1, ATF4-dependent transcriptional activation of asparagine synthetase (ASNS), CEBPA-dependent transcriptional activation of hepcidin (HAMP) and CEBPB-mediated expression of peroxisome proliferator-activated receptor gamma (PPARG). Inhibits the canonical Wnt signaling pathway by binding to TCF7L2/TCF4, impairing its DNA-binding properties and repressing its transcriptional activity. Plays a regulatory role in the inflammatory response through the induction of caspase-11 (CASP4/CASP11) which induces the activation of caspase-1 (CASP1) and both these caspases increase the activation of pro-IL1B to mature IL1B which is involved in the inflammatory response. Acts as a major regulator of postnatal neovascularization through regulation of endothelial nitric oxide synthase (NOS3)-related signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Note=Present in the cytoplasm under non-stressed conditions and ER stress leads to its nuclear accumulation. {ECO:0000250}.
Interaction partners:
- Cyclic AMP-dependent transcription factor ATF-4
- Cyclic AMP-dependent transcription factor ATF-6 alpha
- X-box-binding protein 1
- Apoptosis regulator Bcl-2
- Cyclic AMP-dependent transcription factor ATF-3
- CCAAT/enhancer-binding protein beta
- Mitogen-activated protein kinase 14
- Bcl-2-like protein 11
- Nuclear factor erythroid 2-related factor 2
- Atf6b protein
Sequence:
MAAESLPFAFETVSSWELEAWYEDLQEVLSSDEIGGTYISSPGNEEEESKTFTTLDPASLAWLTEEPGPAEVTSTSQSPRSPDSSQSSMAQEEEEEDQGRTRKRKQSGQCAARAGKQRMKEKEQENERKVAQLAEENERLKLEIERLTREVETTRRALIDRMVSLHQA
Protein: Plexin-A3 (P70208)
Organism: Mus musculus (Mouse)
Function: Coreceptor for SEMA3A and SEMA3F. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Regulates the migration of sympathetic neurons, but not of neural crest precursors. Required for normal dendrite spine morphology in pyramidal neurons. May play a role in regulating semaphorin-mediated programmed cell death in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Neuropilin-1
- Semaphorin-3A
- Semaphorin-3F
- Neuropilin-2
- Rho-related GTP-binding protein Rho6
- Rho-related GTP-binding protein RhoD
- Semaphorin-3B
- Semaphorin-6A
- Tyrosine-protein kinase Fyn
- Tyrosine-protein kinase Fes/Fps
Sequence:
MPTVCLLPLLFFTIGGCLGSSRPFRTFVVTDTTLTHLAVHRVTGEVFVGAVNRVFKLAPNLTELRAHVTGPIEDNARCYPPPSMRVCSHRLVPVDNVNKLLLIDYAARRLVACGSIWQGICQFLRLDDLFKLGEPHHRKEHYLSGAQEPDSMAGVIVEQVQGPSKLFVGTAVDGKSEYFPTLSSRKLIDDEDSGDMFSLVYQDEFVSSQIKIPSDTLSLYPAFDIYYIYGFVSASFVYFLTLQLDTQQTLLDTAGEKFFTSKIVRMCAGDSEFYSYVEFPIGCSWRGVEYRLVQSAHLAKPGLLLAQALGVPADEDVLFTIFSQGQKNRANPPRQTILCLFTLSSINAHIRRRIQSCYRGEGTLALPWLLNKELPCINTPLQINGNFCGLVLNQPLGGLHVIEGLPLLADSTDGMASVAAYTYHQHSVVFIGTRSGNLKKVRVDGSQDAQLYETVSVVQGSPILRDLLFSPDHRHIYLLSEKQVSQLPVETCEQYLSCAACLGSGDPHCGWCVLQHRCCREGACPGASAPHGFAEELSKCIQVRVRPNNVSVTSSGVQLTVAMRNVPDLSVGVSCSFEEVTESEAILLPSGELRCPSPSLQELQTLTRGHGATHTVRLQLLSMETGVRFAGVDFVFYNCSALQSCMSCVGSPYPCHWCKYRHVCTSHPHECSFQEGRVHSPEGCPEILPQGDLLIPVGVMQPLTLRAKNLPQPQSGQKNYECVVRVQGRQHRVPAVRFNSSSVQCQNASYFYEGDEFGDTELDFSVVWDGDFPIDKPPSFRALLYKCWAQRPSCGLCLKADPRFNCGWCISEHRCQLRAHCPAPKSNWMHPSQKGARCSHPRITQIHPLTGPKEGGTRVTIVGENLGLTSREVGLRVAGVRCNSIPTEYVSAERIVCEMEESLVPSPPPGPAELCVGDCSADFRTQSQQLYSFVTPTFDRVSPSRGPASGGTRLTISGISLDAGSRVTVIIRDGECQFVRRDAEAIVCISPVSTLGPSQSPITLAIDHANISNTGVIYTYTQDPTVTHLEPTWSIINGSTSITVSGTHLLTVQEPRVRAKYRGIETTNTCQVINDTAMLCKAPGIFLGHPQPRAQGEHPDEFGFLLDHVQAARSLNRSSFTYYPDPSFEPLGPSGVLDVKPGSHVVLKGKNLIPAAAGSSRLNYTVLIGGQPCALTVSDTQLLCDSPSQTGRQPVMVLVGGLEFWLGTLHITADRALTLPAMVGLAAGGGLLLLAITVVLVAYKRKTQDADRTLKRLQLQMDNLESRVALECKEAFAELQTDINELTNHMDGVQIPFLDYRTYAVRVLFPGIEAHPVLKELDTPPNVEKALRLFGQLLHSRAFLLTFIHTLEAQSSFSMRDRGTVASLTMVALQSRLDYATGLLKQLLADLIEKNLESKNHPKLLLRRTESVAEKMLTNWFTFLLHKFLKECAGEPLFLLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIDYKTLTLHCVCPESEGSAQVPVKVLNCDSITQAKDKLLDTVYKGIPYSQRPKAEDMDLEWRQGRMARIILQDEDITTKIECDWKRVNSLAHYQVTDGSLVALVPKQVSAYNMANSFTFTRSLSRYESLLRAASSPDSLRSRAPMLTPDQEAGTKLWHLVRNHDHTDHREGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETVFSTAHRGSALPLAIKYMFDFLDEQADQRQISDPDVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKNSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPNYKSWVERYYRDIAKMASISDQDMDAYLVEQSRLHANDFNVLSALSELYFYVTKYRQEILTSLDRDASCRKHKLRQKLEQIITLVSSSS
Protein: Guanine nucleotide-binding protein subunit alpha (Q5AK05)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- G protein subunit beta
- Guanine nucleotide-binding protein subunit gamma
- GTPase-activating protein
- Alpha-factor pheromone receptor
- Ste3p
- Mitogen-activated protein kinase
- Cst5p
- mitogen-activated protein kinase kinase kinase
- Adenylate cyclase
- Extracellular signal-regulated kinase 1
Sequence:
MGCGASVPVDDDEIDLFLQDKRINDAIEQSLQLRQQNSKKGVKLLLLGAGESGKSTVLKQLKLLHKGGFTQQERRQYSHVIWCDVIQSMKVLIIQARKLKIKLDCDQPNNSLIPYKQIILRSDPLKQIDADVAGGTDFLNDFVVKYSEENKNKRRLKSTGTTDIWGKDDDSNINSDAINQALESSLNKDSEQFTRLSIAEAIHKLWKLDSGIKKCFDRSNEFQLEGSADYYFDNVFNFADTNYLSTDLDILKGRIKTTGITETDFLIKSFQFKVLDAGGQRSERKKWIHCFEDITAVLFVLAISEYDQNLFEDERVNRMHESIVLFDSLCNSKWFANTPFILFLNKIDIFENKIKKNPLKNYFPDYDGKPDDTNEAIKFFETNFLKINQTNKPIYVHRTCATDSKSMKFVLSAVTDMIVQQNLKKSGII
Protein: Myotubularin-related protein 12 (Inactive phosphatidylinositol 3-phosphatase 12) (Phosphatidylinositol 3 phosphate 3-phosphatase adapter subunit) (3-PAP) (3-phosphatase adapter protein) (Q9C0I1)
Organism: Homo sapiens (Human)
Function: Acts as an adapter for the myotubularin-related phosphatases. Regulates phosphatase MTM1 protein stability and possibly its intracellular location. By stabilizing MTM1 protein levels, required for skeletal muscle maintenance but not for myogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12847286}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q80TA6}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:Q80TA6}. Note=Localizes to punctate vesicles when associated with MTM1 (PubMed:12847286). Localizes to triads, a structure formed by a T tubule and two sarcoplasmic reticulum terminal cisterna (By similarity). In skeletal muscles, co-localizes with MTM1 in the sarcomere (By similarity). Partially localizes to the sarcoplasmic reticulum in skeletal muscles (By similarity). {ECO:0000250|UniProtKB:Q80TA6, ECO:0000269|PubMed:12847286}.
Interaction partners:
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2
- Myotubularin
Sequence:
MLGKGVVGGGGGTKAPKPSFVSYVRPEEIHTNEKEVTEKEVTLHLLPGEQLLCEASTVLKYVQEDSCQHGVYGRLVCTDFKIAFLGDDESALDNDETQFKNKVIGENDITLHCVDQIYGVFDEKKKTLFGQLKKYPEKLIIHCKDLRVFQFCLRYTKEEEVKRIVSGIIHHTQAPKLLKRLFLFSYATAAQNNTVTDPKNHTVMFDTLKDWCWELERTKGNMKYKAVSVNEGYKVCERLPAYFVVPTPLPEENVQRFQGHGIPIWCWSCHNGSALLKMSALPKEQDDGILQIQKSFLDGIYKTIHRPPYEIVKTEDLSSNFLSLQEIQTAYSKFKQLFLIDNSTEFWDTDIKWFSLLESSSWLDIIRRCLKKAIEITECMEAQNMNVLLLEENASDLCCLISSLVQLMMDPHCRTRIGFQSLIQKEWVMGGHCFLDRCNHLRQNDKEEVPVFLLFLDCVWQLVHQHPPAFEFTETYLTVLSDSLYIPIFSTFFFNSPHQKDTNMGREGQDTQSKPLNLLTVWDWSVQFEPKAQTLLKNPLYVEKPKLDKGQRKGMRFKHQRQLSLPLTQSKSSPKRGFFREETDHLIKNLLGKRISKLINSSDELQDNFREFYDSWHSKSTDYHGLLLPHIEGPEIKVWAQRYLRWIPEAQILGGGQVATLSKLLEMMEEVQSLQEKIDERHHSQQAPQAEAPCLLRNSARLSSLFPFALLQRHSSKPVLPTSGWKALGDEDDLAKREDEFVDLGDV
Protein: SPX domain-containing protein 4 (Protein SPX DOMAIN GENE 4) (OsSPX4) (Q10B79)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Inositol polyphosphate sensor that associates with transcription factors to regulate Pi starvation responses. The SPX domain provides a basic binding surface for inositol polyphosphate signaling molecules. Interacts with PHR2 to inhibits its translocation to the nucleus and repress its DNA-binding activity, and then negatively regulate Pi signaling.
Subcellular location: Membrane {ECO:0000269|PubMed:19566645}. Nucleus {ECO:0000269|PubMed:24692424}. Cytoplasm {ECO:0000269|PubMed:24692424}. Note=Unlike PubMed:19566645, PubMed:24692424 cannot find a membrane localization.
Interaction partners:
- Protein PHOSPHATE STARVATION RESPONSE 2
Sequence:
MKFGKDFRSHLEETLPAWRDKYLAYKSLKKLIKNLPPDGDPPPVAAAAEVPAGDGDGDGGIALGNWFARVLDMELQKLNDFYIEREEWYVIRLQVLKERIERVKAKKNGAFTSKSEFTEEMLEIRKAFVIIHGEMILLQTYSSLNFAGLVKILKKYDKRTGGLLSLPFTQRARHQPFFTTEPLTRLVRECEANLELLFPIEAEVLESASSSAKLQPQNDDAASHDPASSVDVETSDVYRSTLAAMKAIQGLRKASSTYNPLSLARFFHGEDGEACSGAITSESDSYSDSQIEDAEDDDKEVQSREQNTAQNAAEGQPRDE
Protein: D-3-phosphoglycerate dehydrogenase 1 (3-PGDH 1) (EC 1.1.1.95) (2-oxoglutarate reductase) (EC 1.1.1.399) (P40054)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Interaction partners:
- D-3-phosphoglycerate dehydrogenase 2
- Phosphoserine aminotransferase
- Probable ATP-dependent kinase TDA10
- Phosphoglycerate mutase 1
- Phosphoglycerate mutase 2
- Phosphoglycerate mutase 3
- Alanine--glyoxylate aminotransferase 1
- Aminomethyltransferase, mitochondrial
- Phosphoserine phosphatase
- Serine hydroxymethyltransferase, cytosolic
Sequence:
MTSIDINNLQNTFQQAMNMSGSPGAVCTSPTQSFMNTVPQRLNAVKHPKILKPFSTGDMKILLLENVNQTAITIFEEQGYQVEFYKSSLPEEELIEKIKDVHAIGIRSKTRLTSNVLQHAKNLVCIGCFCIGTNQVDLDYATSRGIAVFNSPFSNSRSVAELVIAEIISLARQLGDRSIELHTGTWNKVAARCWEVRGKTLGIIGYGHIGSQLSVLAEAMGLHVLYYDIVTIMALGTARQVSTLDELLNKSDFVTLHVPATPETEKMLSAPQFAAMKDGAYVINASRGTVVDIPSLIQAVKANKIAGAALDVYPHEPAKNGEGSFNDELNSWTSELVSLPNIILTPHIGGSTEEAQSSIGIEVATALSKYINEGNSVGSVNFPEVALKSLSYDQENTVRVLYIHQNVPGVLKTVNDILSNHNIEKQFSDSNGEIAYLMADISSVDQSDIKDIYEQLNQTSAKISIRLLY
Protein: TMEM (Human TransMEMbrane protein) homolog (Q23481)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Transmembrane protein 231
- Transmembrane protein 237 homolog
- Nephrocystin-1-like protein
- B9 domain-containing protein 1
- NePHronoPhthisis
- MecKel-Gruber Syndrome
- Meckelin
- C2 domain-containing protein
- B9 domain-containing protein 2
- Transmembrane protein 138
Sequence:
MHLINLCLSLYFKHSLLSLTYQVIAFSACLVHLGSEGVRLGLGFYGNLAENMSALFGFLITTIIIQIPLTVFLAVNGSFLNLPLEYVFYTMITVFAIEALMKTAEREVAKYINKIQQEKVADELEKTSGKSPKSGRKTLKKQLSR
Protein: Thiol S-methyltransferase TMT1B (EC 2.1.1.9) (Methyltransferase-like protein 7B) (Thiol S-methyltransferase METTL7B) (Q6UX53)
Organism: Homo sapiens (Human)
Function: Thiol S-methyltransferase that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine to hydrogen sulfide and other thiol compounds including dithiothreitol, 7alpha-thiospironolactone, L-penicillamine, and captopril.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q562C4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q562C4}. Lipid droplet {ECO:0000250|UniProtKB:Q562C4}. Microsome {ECO:0000269|PubMed:37137720}. Cytoplasm, cytosol {ECO:0000269|PubMed:37137720}. Note=Highly concentrated in the perinuclear area of the endoplasmic reticulum (ER) and surrounding lipid droplets. May be associated with the specific regions of the LR that form lipid droplets and targeted to the initial deposits of lipids where the lipid droplets form. {ECO:0000250|UniProtKB:Q562C4}.
Interaction partners:
- Probable methyltransferase-like protein 25
Sequence:
MDILVPLLQLLVLLLTLPLHLMALLGCWQPLCKSYFPYLMAVLTPKSNRKMESKKRELFSQIKGLTGASGKVALLELGCGTGANFQFYPPGCRVTCLDPNPHFEKFLTKSMAENRHLQYERFVVAPGEDMRQLADGSMDVVVCTLVLCSVQSPRKVLQEVRRVLRPGGVLFFWEHVAEPYGSWAFMWQQVFEPTWKHIGDGCCLTRETWKDLENAQFSEIQMERQPPPLKWLPVGPHIMGKAVK
Protein: Cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91) (P0C2S1)
Organism: Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum)
Subcellular location: Secreted {ECO:0000269|PubMed:10464199, ECO:0000269|PubMed:8664281}.
Interaction partners:
Sequence:
MNFRRMLCAAIVLTIVLSIMLPSTVFALEDKSSKLPDYKNDLLYERTFDEGLCFPWHTCEDSGGKCDFAVVDVPGEPGNKAFRLTVIDKGQNKWSVQMRHRGITLEQGHTYTVRFTIWSDKSCRVYAKIGQMGEPYTEYWNNNWNPFNLTPGQKLTVEQNFTMNYPTDDTCEFTFHLGGELAAGTPYYVYLDDVSLYDPRFVKPVEYVLPQPDVRVNQVGYLPFAKKYATVVSSSTSPLKWQLLNSANQVVLEGNTIPKGLDKDSQDYVHWIDFSNFKTEGKGYYFKLPTVNSDTNYSHPFDISADIYSKMKFDALAFFYHKRSGIPIEMPYAGGEQWTRPAGHIGIEPNKGDTNVPTWPQDDEYAGRPQKYYTKDVTGGWYDAGDHGKYVVNGGIAVWTLMNMYERAKIRGIANQGAYKDGGMNIPERNNGYPDILDEARWEIEFFKKMQVTEKEDPSIAGMVHHKIHDFRWTALGMLPHEDPQPRYLRPVSTAATLNFAATLAQSARLWKDYDPTFAADCLEKAEIAWQAALKHPDIYAEYTPGSGGPGGGPYNDDYVGDEFYWAACELYVTTGKDEYKNYLMNSPHYLEMPAKMGENGGANGEDNGLWGCFTWGTTQGLGTITLALVENGLPATDIQKARNNIAKAADRWLENIEEQGYRLPIKQAEDERGGYPWGSNSFILNQMIVMGYAYDFTGNSKYLDGMQDGMSYLLGRNGLDQSYVTGYGERPLQNPHDRFWTPQTSKKFPAPPPGIIAGGPNSRFEDPTITAAVKKDTPPQKCYIDHTDSWSTNEITVNWNAPFAWVTAYLDEIDLITPPGGVDPEEPEVIYGDCNGDGKVNSTDAVALKRYILRSGISINTDNADVNADGRVNSTDLAILKRYILKEIDVLPHK
Protein: Phytochrome-like protein cph2 (Bacteriophytochrome cph2) (Q55434)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Photoreceptor which exists in two forms that are reversibly interconvertible by light: the R form that absorbs maximally in the red region of the spectrum and the FR form that absorbs maximally in the far-red region.
Interaction partners:
- Circadian input-output histidine kinase CikA
- Circadian input-output histidine kinase CikA
- Circadian input-output histidine kinase CikA
- Slr1102 protein
- Circadian input-output histidine kinase CikA
- Sll0267 protein
- Regulatory components of sensory transduction system
- histidine kinase
- Slr0359 protein
- Slr1143 protein
Sequence:
MNPNRSLEDFLRNVINKFHRALTLRETLQVIVEEARIFLGVDRVKIYKFASDGSGEVLAEAVNRAALPSLLGLHFPVEDIPPQAREELGNQRKMIAVDVAHRRKKSHELSGRISPTEHSNGHYTTVDSCHIQYLLAMGVLSSLTVPVMQDQQLWGIMAVHHSKPRRFTEQEWETMALLSKEVSLAITQSQLSRQVHQQQVQEALVQRLETTVAQYGDRPETWQYALETVGQAVEADGAVLYIAPDLTGSVAQHYQWNLRFDWGNWLETSLWQELMRGQPSAAMEPMAAVQSTWEKPRPFTSVAPLPPTNCVPHGYTLGELEQRSDWIAPPESLSAENFQSFLIVPLAADQQWVGSLILLRKEKSLVKHWAGKRGIDRRNILPRLSFEAWEETQKLVPTWNRSERKLAQVASTQLYMAITQQFVTRLITQQTAYDPLTQLPNWIIFNRQLTLALLDALYEGKMVGVLVIAMDRFKRINESFGHKTGDGLLQEVADRLNQKLSPLAAYSPLLSRWHGDGFTILLTQISDNQEMIPLCERLLSTFQEPFFLQGQPIYLTASMGISTAPYDGETAESLLKFAEIALTRAKCQGKNTYQFYRPQDSAPMLDRLTLESDLRQALTNQEFVLYFQPQVALDTGKLLGVEALVRWQHPRLGQVAPDVFIPLAEELGLINHLGQWVLETACATHQHFFRETGRRLRMAVNISARQFQDEKWLNSVLECLKRTGMPPEDLELEITESLMMEDIKGTVVLLHRLREEGVQVAIDDFGTGYSSLSILKQLPIHRLKIDKSFVNDLLNEGADTAIIQYVIDLANGLNLETVAEGIESEAQLQRLQKMGCHLGQGYFLTRPLPAEAMMTYLYYPQILDFGPTPPLPKVALPETETEAGQGNVGDRPLPNSLNRENPWTEKLHDYVLLKERLQQRNVKEKLVLKIANKIRASLNINDILYSTVTEVRQFLNTDRVVLFKFNSQWSGQVVTESHNDFCRSIINDEIDDPCFKGHYLRLYREGRVRAVSDIEKADLADCHKELLRHYQVKANLVVPVVFNENLWGLLIAHECKTPRYWQEEDLQLLMELATQVAIAIHQGELYEQLETANIRLQQISSLDALTQVGNRYLFDSTLEREWQRLQRIREPLALLLCDVDFFKGFNDNYGHPAGDRCLKKIADAMAKVAKRPTDLVARYGGEEFAIILSETSLEGAINVTEALQVEVANLAIPHTVSGTGHVTLSIGIAVYTPERHINPNALVKAADLALYEAKAKGRNQWLAYEGSQLPHVDGEV
Protein: Lantibiotic lacticin 3147 A2 (O87237)
Organism: Lactococcus lactis subsp. lactis (Streptococcus lactis)
Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually lacticin 3147 A2 exhibits weak activity towards L.lactis strain AM2 and L.lactis strain HP, and no activity towards L.lactis strain IFPL359, but when combined with lacticin 3147 A1 it displays strong activity towards all three strains.
Subcellular location: Secreted {ECO:0000269|PubMed:10608807, ECO:0000269|PubMed:10971756}.
Interaction partners:
Sequence:
MKEKNMKKNDTIELQLGKYLEDDMIELAEGDESHGGTTPATPAISILSAYISTNTCPTTKCTRAC
Protein: Down syndrome cell adhesion molecule 1, isoform AC (Q0E9J5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVNQFYGADILMEYVIRGNAAVLKCSIPSFVADFVRVESWIDEEGTELRPSENYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGSVAPKVDMHDKMDFTIRSSNRSLNLFCKAQGFPMPAFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMAPPKIAPFDFGQSASSFEDSVSVNCLVTSGDLPIDIEWLFGGEPINFATGIAILRGGKRTSLLTIDSVHAGHAGNYTCKAKNQASSSEYSAALIVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPLDDGSGHGNVHTRIRLPAWMPEWLDLNFMVPLIATVVVVAVGICVVCVALSRRRADDMRGGQKDVYYDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Pre-mRNA leakage protein 1 (Q07930)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for efficient splicing and pre-mRNA nuclear retention.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing factor CWC26
- Pre-mRNA-splicing helicase BRR2
- U2 snRNP component IST3
- U2 snRNP component HSH155
- Pre-mRNA-processing protein 45
- Pre-mRNA-splicing factor CWC22
- Pre-mRNA-splicing factor RDS3
- Pre-mRNA-splicing factor CWC21
- Peptidyl-prolyl isomerase CWC27
- Pre-mRNA-splicing factor PRP9
Sequence:
MFHRRKRPYNTRNYGHDDKKFKSQYIDIMPDFSPSGLLELESNNKEGIALKHVEPQDAISPDNYMDMLGLEARDRTMYELVIYRKNDKDKGPWKRYDLNGRSCYLVGRELGHSLDTDLDDRTEIVVADIGIPEETSSKQHCVIQFRNVRGILKCYVMDLDSSNGTCLNNVVIPGARYIELRSGDVLTLSEFEEDNDYELIFMNV