wanglab/gogpt-training-data huggingface dataset:
Protein: CIN85 and CD2AP related, isoform F (A0A0B4KHJ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLPPKPQREFCRVEFPYAPQNDDELELKVDDIIAVISTELPDKGWWKGEIRGKVGVFPDNFVKMLAPSEAAPPLPRPRPRTRPGMGGTGAGSGSGIIDGVRTPRRTQRGGSFEFLGARMASFITTIFAPINEPPSATQITQNQRKVSNTASTTSHMTTTNSSNSSTTSVTTQQQKEQIGGSSSTTSKVYIKKTGSSSNSTTSSTTTASSSAGRKESFGSRDSLNDILSETGLPTGNVAAQRKSLENKNLDLTKPPGVGASVSIGQQRSSTSSATTSSATTVATGLTSSSVSKSMENMLDEKVKSPPPPVLSKKPSVPLKKTPTGGVPMTGNLLGGKKKNTEGKLTTAVSHDLADGLAASKMLSGANQLPESGAAGNVVIRRAATIAVEDTDFDRVERASILTDMRQGRVKAPKRRPPSAAINVLGESNNNSVYVNGSGMSGSGGAGSASELSEDGGAGGKTSDDNSTGEEPQLAKPKPREWEKKKAPWMEELKASQVTRKKTSPSVEPRGASVAERTSKLFAAEQAVSSNSSSITTKVQSSAVTSSMFVENSTTSSSVITSSSHTTTNDAIMSRSLSAAKVQTASSDEETRATRPNSLAIRNQRSVSPLVKSSNASSSQSQEEKPTSQLNNHQDASSSRVAQLEQRVDKLEGLVLNQQRTIEELVNALKSEAERVKILRSELDKYAQCVTQV
Protein: Tryptophan 5-hydroxylase 2 (EC 1.14.16.4) (Tryptophan 5-monooxygenase 2) (Q1LUE3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTNSTLHPPWTSFNRIDERPDKEEQKSTHDLGKLAVIFSLKNEVGFLVKALRLFQEKHVNLAHIESRRSKRLTNEIEIYAECNCTKKEFNELVQHLKDHVNIVSYNTPQHVWSAETDCLDCVCVLGGLPDGEGIPWFPQKISELDQCSHRVLMYGSELDADHPGFKDKVYRQRRKYFVEVAMNYKFGQPIPRIEYTAEEVKTWGVVYRELTKLYPTHACREYLKNLPLLTKHCGYREDNIPQLEDVSLFLRERSGFTVRPVAGYLSPRDFLAGLAYRVFNCTQYIRHSTDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQDGQLRVYGAGLLSSIGELRHALSDKATVKVFDPKTTCYQECLITTFQDVYFVSESFEEAKEKMREFAKSIKRPFSVYYNPYTQSIDLLKDTRSIENVVQDLRSDLTTVCDALGKMNKYLGI
Protein: Bifunctional IPC transferase and DIPP synthase [Includes: 1L-myo-inositol-1-phosphate cytidylyltransferase (IPCT) (EC 2.7.7.74); CDP-L-myo-inositol myo-inositolphosphotransferase (DIPP synthase) (EC 2.7.8.34) (Di-myo-inositol-1,3'-phosphate-1'-phosphate synthase)] (Q5JDA9)
Organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Function: Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Myo-inositol-1-phosphate synthase
- Fructose-1,6-bisphosphatase/inositol-1-monophosphatase
- CDP-glycerol:poly
- Pyruvoyl-dependent arginine decarboxylase
Sequence:
MVPERAVILAAGLGTRMGRKPKGLVRVAGREILYRTIRLLQENGVKKFIVVTNERYAPLYQEFIERHGFDAEIIINPEPEKGNGHSLHLAKEKVSGKFALTMSDHVYSRDFIERAVRGRGLIADREPRWVDIGEATKVQVKDEKVWKIGKRLKEWDAIDTGFFVLDDEIFKVTEILENEKNGDYSLSEVMERAKVSVTFVDGLGWTDVDTPEEIKRARRMLVRTAVKGTGDGFVSRHLNRRISTRVSELLVEKVTPNQMTVVTFLLGIISALTTLVSLPLAGILYQLSSILDGIDGELARAQLRTSKLGGYVDSILDRYVDGSFLALLAYATINEPIWYFVALLALLGSVMVSYSTERFRGAFCRDAYKEVPALRKLPGKRDERVFLTMLFLLYQIAASIKALFLTLAVLTNFRVALTLYFVVKKVSHPKTI
Protein: Aminodeoxychorismate synthase component 1 (ADC synthase) (ADCS) (EC 2.6.1.85) (4-amino-4-deoxychorismate synthase component 1) (P28820)
Organism: Bacillus subtilis (strain 168)
Function: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC.
Interaction partners:
- Aminodeoxychorismate lyase
- Aminodeoxychorismate/anthranilate synthase component 2
- Anthranilate phosphoribosyltransferase
- Tryptophan synthase alpha chain
- Tryptophan synthase beta chain
- N-
- Chorismate synthase
- Dihydropteroate synthase
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
- Protein AroA
Sequence:
MAQRRPAGKKIPFQKDSFLQQFEKLAQSRKHHVLLESARGGRYSIAGLDPIATVKGKDGITTIKHGDEMLFKEGDPLRAFHSWFKTLETETNHEFPDFQGGAIGFLSYDYARYIENFKMLSLDDLETPDIYFLVFDDIAVYDHQEESLWLITHVNGSDQETADVKLSELEQMWLTELPAVTSREMKPETAGSFAAPFTEDGFSQAVEKIKQYIASGDVFQVNLSIRQSQSLSVHPYQIYKTLREVNPSPYMAYLETPDFQIICGSPELLVSKKGKLLETRPIAGTRSRGKTNEEDEALANELIHNEKERAEHVMLVDLERNDLGRVSRYGSVRVNEFMAIEKYSHVMHIVSNVQGELQDGYDAVDIIHAVFPGGTITGAPKVRTMEIIEELEPTRRGLYTGSIGWFGYNHDLQFNIVIRTIYATGGQAFMQSGAGVVIDSVPKHEYKESFKKAFAMQRALELSEEETKIR
Protein: GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase (EC 2.4.1.346) (Alpha-D-mannose-alpha-(1-6)-phosphatidylmyo-inositol-mannosyltransferase) (Alpha-mannosyltransferase) (Alpha-ManT) (Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase) (Phosphatidylinositol alpha-mannosyltransferase) (PI alpha-mannosyltransferase) (A0R043)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 6 of a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1) to generate phosphatidyl-myo-inositol bearing alpha-1,2- and alpha-1,6-linked mannose residues (Ac1PIM2). PimB also catalyzes the addition of a mannosyl residue from GDP-Man to the position 6 of phosphatidyl-myo-inositol bearing an acylated alpha-1,2-linked mannose residue (Ac1PIM1) to generate monoacylated phosphatidyl-myo-inositol bearing alpha-1,2- and alpha-1,6-linked mannose residues (Ac1PIM2). The addition of the second mannosyl residue by PimB preferentially occurs before the acylation of the mannosyl residue transferred by PimA. Also able to transfer a mannosyl residue from GDP-Man to the position 6 of a phosphatidyl-myo-inositol (PI), but this reaction is very slow.
Interaction partners:
- Phosphatidylinositol mannoside acyltransferase
- Polyprenol-phosphate-mannose-dependent alpha-
- Peptidase
- Polyprenol monophosphomannose synthase
- 1,4-alpha-glucan branching enzyme GlgB
- NLP/P60 family protein
- Malto-oligosyltrehalose trehalohydrolase
- Galactofuranosyltransferase GlfT2
Sequence:
MLLVTNDFPPRRGGIQSYLEAFVGELVRTHELTVYAPKWKGAEEYDEKAARSGYRVVRHPTTLMLPEPTVASRMKRLIGEHDIETVWFGAAAPLALLGPLARRAGARRIVASTHGHEVGWSMLPVARTALRRIGNDADVVTFVSRYTRSRFASAFGPSAALEHLPPGVDTDRFAPDPDARARMRERYGLGDRPVVVCLSRLVPRKGQDMLIRALPELRRRVPDTALAIVGGGPYLETLQRMASDLGVAEHVVFTRGIPAEELPAHHAMADVFAMPCRTRGAGLDVEGLGIVYLEASACGVPVVAGRSGGAPETVLDGKTGTVVDGTDVDAITTAVGDLLADPRRAAAMGVAGRHWALDNWQWRTRGARLAELLSGRREARQA
Protein: Elongator complex protein 2 (AtELP2) (Elongator component 2) (Protein GREEN NPR1 SEEDLING ON SA MEDIUM 1) (F4I1S7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). Promotes organ development by modulating cell division rate. Prevents abscisic acid (ABA) signaling leading to stomatal closure and seedling growth inhibition. Involved in oxidative stress signaling. Prevents anthocyanin accumulation. Accelerator of defense gene induction required for rapid defense gene induction, and for the establishment of both basal and effector-triggered immunity (ETI), in a NPR1-independent manner, but is not required for systemic acquired resistance (SAR) establishment.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6IA86}. Nucleus {ECO:0000250|UniProtKB:Q6IA86}.
Interaction partners:
- Elongator complex protein 3
- Elongator complex protein 1
- Elongator complex protein 4
- Protein KTI12 homolog
- Elongator complex protein 5
- Radical S-adenosyl methionine domain-containing protein 1, mitochondrial
- Elongator complex protein 6
- Putative WD-repeat membrane protein
- Transducin family protein / WD-40 repeat family protein
- Vacuolar-sorting receptor 1
Sequence:
MSENTKVEAKRVFIGAGCNRVVNNVSWGASGLVSFGAQNAVAVFCPKTAQILTTLPGHKASVNCTHWLPTSKFAFKAKKLDRQYLLSGDSDGIIILWELSTLNNDWRHVLQLPLSHKKGVTCITAYMVSETDAMFASASSDGVVNVWDVSFPSQPSEECKVVCLDSICVDTKAIVTLSLAELPQNPGRFALALGGLDNKIKLYSGERTGKFTSVCELKGHTDWIRSLDFSLPLHTTEEIPNSIMLVSSSQDKVIRIWKLVLVGDVGSWRREITLASYIEGPVFVSGTFTYQISVESVLIGHEDWVYSVEWQPPVIDFIDGRLVNHQPLSILSASMDKTMMIWRPEKKTGVWVNVVCVGELSHCALGFYGGHWSPNSLSILAHGYGGAFHLWRNVSSSKESENWQMQKVPSGHFAAVTDVTWARTGEYLLSVSQDQTTRVFSAWKNDEGNEAEDEHWHELARPQVHGHDINCVAMVQGKGNHRFVSGAEEKVVRVFEAPLSFLKTLNHTCAGGEGSFPEDLQADVQVLGANMSALGLSQKPIYLHSSSEPLERNGGGEGLDTFETVPEAAPAELKEPPIEDQLAFHTLWPESHKLYGHGNELFSLCSDHKGNLVASSCKAQSASMAEIWLWEVGTWKAVGRLQSHSLTVTHLEFSYDDTLLLSVSRDRHFSVFSIQRTDNGEVSHKLMAKVEAHKRIIWACSWNPFGHQFATSSRDKTVKIWSVENDARIKQILVLPPFGSSVTAVAWTGLDRNEKSGCVAVGMESGLIELSNVKIIETEEGTTATAALALRLEPFMCHVSAVNRLAWRPTEKCESNQSLRWLTSCGDDNCVRVFNFKF
Protein: Synapsin-3 (Synapsin III) (O70441)
Organism: Rattus norvegicus (Rat)
Function: May be involved in the regulation of neurotransmitter release and synaptogenesis. Binds ATP with high affinity and ADP with a lower affinity. This is consistent with a catalytic role of the C-domain in which ADP would be dissociated by cellular ATP after bound ATP was hydrolyzed.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Peripheral membrane protein localized to the cytoplasmic surface of synaptic vesicles.
Interaction partners:
- Synaptotagmin-1
- Vesicle-associated membrane protein 2
- Disks large homolog 4
- Ras-related protein Rab-3A
- Synaptophysin
- Regulating synaptic membrane exocytosis protein 1
- Syntaxin-binding protein 1
- Syntaxin-1A
- Vesicular glutamate transporter 1
- Vesicular inhibitory amino acid transporter
Sequence:
MNFLRRRLSDSSFVANLPNGYMPDLQRPESSSSSPASPATERRHPQPLAASFSSPGSSLFSSFSSAMKQTPQAPTGLMEPPTPVTPVVQRPRILLVIDDAHTDWSKYFHGKKVNGDIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKIVRSFKPDFILVRQHAYSMALAEDYRSLVIGLQYGGLPAVNSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMLTAPNFPVVIKLGHAHAGMGKIKVENQHDYQDITSVVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVKAVHSKNGRDYIIEVMDSSMPLIGEHVEEDKQLMADLVVSKMSQLLVPGASVPSPLRPWGPQTKSAKSPGQGQLGPLLGQPQPRPPPQGGPRQAQSPQPPRSRSPSQQRLSPQGQQPVSPQSGSPQQQRSPGSPQLSRASGGSSPNQASKPTASLSSHTRPPVQGRSTSQQGEEPQKTASPHPHLNKSQSLTNSLSTSDTSHRGTPSEDEAKAETIRNLRKSFASLFSD
Protein: SD16815p (Q8MRW9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MELGLPLRWDLIATLTVRHNSMVRVAGRQQSERLQNGRERSRRPKSDGVQHADSSIMEDDLLWPLQRFKDSRGQHLLQGEALKFGIDLSGKDFDQDESERVPAEQLPPEVLHSPSDPEYHEPSKSGPEADVPHVPPHMPHARWETGAAASTTAVPSLPNDGFVYRWMLGEWSQCSQECGAAGSGLQRRTVSCQRAAKATSSGSTSDTENNVVDNSECFAHGLELPEFFQSCGNEACPQWSKGDWTPCQRSHCHGRNTAMQRREVTCRYPNGTEGSICDEYERPAMRQECYNERCEGVWRVEPWSECNAPCGRKGIKYRILQCVWYGSRRPAGNVCKHQPRPAVMKVCKSPACQAQLSSSPAQLCRDSSRYCRNARAMGLCRLHRYKLKCCGSCEQQPNQHLIL
Protein: Disease resistance-like protein DSC1 (EC 3.2.2.6) (Protein DOMINANT SUPPRESSOR OF CAMTA3 NUMBER 1) (Q9SZ66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: TIR-NB-LRR receptor-like protein involved in plant defense. Acts as a trigger of hypersensitive response (HR). Functions as guard of CAMTA3, a negative regulator of immunity, during pathogen infection.
Interaction partners:
- Calmodulin-binding transcription activator 3
- Probable disease resistance protein At5g45490
- Protein DA1-related 5
Sequence:
MESSSPSSAEFDVFLSFRGFDTRNNFTGHLQKALRLRGIDSFIDDRLRRGDNLTALFDRIEKSKIAIIVFSTNYANSAWCLRELVKILECRNSNQQLVVPIFYKVDKSDVEKQRNSFAVPFKLPELTFPGVTPEEISSWKAALASASNILGYVVKEISTSEAKLVDEIAVDTFKKLNDLAPSGNEGLVGIESRLKNLEKLLSWEDLDTVHIIGIVGMVGIGKTTLADCLYGRMRGQFDGSCFLTNIRENSGRSGLESLLQKLFSTVLNDRDLEIGAPGNAHERFERRLKSKRLLIVLDDVNDEKQIRYLMGHCKWYQGGSRIIITTRDSKLIETIKGRKYVLPKLNDREALKLFSLNAFSNSFPLKEFEGLTNMVLDYAKGHPLALKVLGSDLCERDDLYWEAKLDRLKSRSHGDIYEVLETSYEELTTEQKNVFLDIACFFRSENVDYVTSLLNSHGVDVSGVVKDLVDKCLITLSDNRIEMHDMLQTMAKEISLKVETIGIRDCRWLSRHGNQCQWHIRLWDSEDICDLLTEGLGTDKIRGIFLDTSKLRAMRLSAKAFQGMYNLKYLKIYDSHCSRGCEAEFKLHLRRGLSFLPNELTYLHWHGYPLQSIPLDFDPKNLVDLKLPHSQLEEIWDDEKDVGMLKWVDLSHSINLRQCLGLANAHNLERLNLEGCTSLKKLPSTINCLEKLIYLNLRDCTSLRSLPKGIKTQSLQTLILSGCSSLKKFPLISENVEVLLLDGTVIKSLPESIQTFRRLALLNLKNCKKLKHLSSDLYKLKCLQELILSGCSQLEVFPEIKEDMESLEILLMDDTSITEMPKMMHLSNIKTFSLCGTSSHVSVSMFFMPPTLGCSRLTDLYLSRCSLYKLPDNIGGLSSLQSLCLSGNNIENLPESFNQLNNLKWFDLKFCKMLKSLPVLPQNLQYLDAHECESLETLANPLTPLTVGERIHSMFIFSNCYKLNQDAQASLVGHARIKSQLMANASAKRYYRGFVPEPLVGICYPATEIPSWFCHQRLGRSLEIPLPPHWCDINFVGLALSVVVSFKDYEDSAKRFSVKCCGNFENKDSSFTRFDFTLAGWNEPCGSLSHESRKLTSDHVFMGYNSCFLVKNVHGESNSCCYTKASFEFYVTDDETRKKIETCEVIKCGMSLMYVPEDDDCMLLKKTNIVQLSLKSGPSCSYDLDDVMDDVRPKRGLCQFVGGEEPGCKRRKEEKITVR
Protein: Major Facilitator Superfamily with SPX (SYG1/Pho81/XPR1) domain-containing protein (F4I0G7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVAFGKYLQRKQIEEWSGYYINYKLMKKKVKQYAEQIQGGSQHPRHVLKDFSRMLDTQILKVNHCLQIETTVLFMLEQQGLLSGRLAKLRESHDAILEQPDISRIFELREAYRDVGRDLLQLLKFVELNAIGLRKILKKFDKRFGYRFADYYVKTRANHPYSQLQQVFKHVGVGAVVGAISRNLHELQENEGSFYSIYDQPVLPAQDPVVEAINNAVDKLTFSTNFLNFLAQHALIMQDDLVTPSEDTIDERSYHFNSLLLNLGNTFLYMVNTYIIVPTADDYSMSLGAAATVCGVVIGSMAVAQVFSSVYFSAWSNKSYFKPLVFSSIALFIGNLMYALAYDANSIALLLLGRVCCGLGSARAVNRRYISDCVPLRIRMQASAGFVSASALGMACGPALAGLLQIKFKFYKFTFNQSTLPGWVMAVAWLFYLVWLCISFREPLRDTEDGEKNNRNETTSATDRVESSRVEEGLRLPLLITSGIKPEDEEECDESEESPEDSHKPANSFIEAYRLLTPSVKVQLLIYFMLKYSMEILLSESSVITSYYFSWTTSSVAIFLACLGLTVLPINILVGSYISNMFEDRQILLTSEIIVFLGILFSFNLFVPYTVPQYVISGLIMFVAAEVLEGVNLSLLSRVMSSRLSKGTYNGGLLSTEAGTLARVVADATITLGGYLGRGHLLNATLLPSLVICIGSIVATCCTYNSLY
Protein: Keratin, type II cytoskeletal 2 epidermal (Cytokeratin-2e) (CK-2e) (Epithelial keratin-2e) (Keratin-2 epidermis) (Keratin-2e) (K2e) (Type-II keratin Kb2) (Q3TTY5)
Organism: Mus musculus (Mouse)
Function: Probably contributes to terminal cornification (By similarity). Associated with keratinocyte activation, proliferation and keratinization (By similarity). Required for maintenance of corneocytes and keratin filaments in suprabasal keratinocytes in the epidermis of the ear, potentially via moderation of expression and localization of keratins and their partner proteins. Plays a role in the establishment of the epidermal barrier on plantar skin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24751727}.
Interaction partners:
- Keratin, type II cytoskeletal 79
Sequence:
MSCQISCRSRRGGGGGGGGGFRGFSSGSAVVSGGSRRSNTSFSCISRHGGGRGGSGGGGFGSQSLVGLGGYKSISSSVAGNSGGYGGSSFGGSSGFGGGRGFGGGQGFGGSGGFGGGSGFGGGQGFGGGSRFGGGSGFGGGGFGGGSFGGGRFGGGPGGFGGPGGFPGGGIHEVSVNQSLLQPLDVKVDPEIQNVKSQEREQIKTLNNKFASFIDKVRFLEQQNQVLRTKWELLQQLDVGSRTTNLDPIFQAYIGMLKKQVDRLSAERTSQESELNNMQDLVEDFKKKYEDEINKRTSAENDFVTIKKDVDSCYMDKTELQARLDILAQEVNFLRTLYDAELSQLQQDVTDTNVILSMDNNRNLDLDSIIAEVQNQYEMIAHKSKAESEELYHSKYEELQVTAVKHGDSLKEIKMEISELNRTIQRLQGEISHVKKQCKGVQDSIADAEQRGEHAIKDARGKLTDLEEALQQCREDLARLLRDYQELMNTKLSLDVEIATYRKLLEGEECRMSGDFSDNVSVSITSSTISSSVASKTGFGSGGQSSGGRGSYGGRGGGGGGGSTYGSGGRSSGSRGSGSGSGGGGYSSGGGSRGGSGGGYGSGGGSRGGSGGGYGSGGGSGSGGGYSSGGGSRGGSGGGGVSSGGGSRGGSSSGGGSRGGSSSGGGGYSSGGGSRGGSSSGGAGSSSEKGGSGSGEGCGSGVTFSFR
Protein: Adhesion G protein-coupled receptor F5 (G-protein coupled hepta-helical receptor Ig-hepta) (Ig-Hepta) (G-protein coupled receptor 116) (G5E8Q8)
Organism: Mus musculus (Mouse)
Function: Receptor that plays a critical role in lung surfactant homeostasis. May play a role in controlling adipocyte function.
Subcellular location: Cell membrane {ECO:0000269|PubMed:36073784}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase beta
- Surfactant protein C
- Cadherin-5
- Receptor activity-modifying protein 2
- Pulmonary surfactant-associated protein B
- Multimerin-2
- Roundabout homolog 4
- Adenylate cyclase type 4
- Endomucin
- Claudin-5
Sequence:
MRSPRTFTFYFLLLVICSSEAALSTPTEPIVQPSILQEHELAGEELLRPKRAAAAGDRVAEEYMVDIEISFENVSFLESIRAHLNNLSFPIRGTEADILNIAMTTVCTPAGNDLLCFCEKGYQWSEERCLHSLTCQDYDSALPGGYCSCLKGLPPQGPFCQLPEAFITLKLKVRLNIGFQEDLKNTSSALYRSYKTDLERAFRAGYRTLPGFRSVTVTQFTKGSVVVNYVVRVTSAPLPGSIHKANEQVIQNLNHTYKMDYNSFQGTPSNETKFTVIPEFIFEGDNVTLECETEFVTSNTSWYYGEKRSDIQNSDKYSIHTTVINNISLITRLTIYNFTQHDAGMYGCNVTLDIFEYGTVRKLDVTPIRILAKEERKVVCDNHPISLNCCSENIANWSSIEWKQEGKISILGNPESDLESSCSTYTLKADGTQCPSGSSGTTVIYTCEFVSAYGARGSKNIAVTFTSVANLTITRDPISVSEGQSFSITCLSDVSSFDEVYWNTSAGIKIHPRFYTMRRYQDGAESVLMVKTSTREWNGTYHCIFRYKNSYSIATKDVTVHPLPLVSDIMMDPLEASGLCTSSHQFKCCVEEDAGEEYAVTFHVDSSSFPAEREVIGKQACYTYSLPANLPRCPKDIAVFCHFTNAANSSVRSPSMKLKLIPRENVTCQDPIIGIGDPGKVIQKLCQFSGVYGSPGQAIGGTVTYKCVGTQWKEESRACISAPINGLLQVAKALIKSPTQDQKLPTYLRDLSVSAGKEEQDIRSSPGSLGAIISILDLLSTVPTQVNSEMMRDILATINVILDKSALNSWEKLLQQQSNQSSQFLHSVERFSQALQLGDSTPPFLAHPNVQMKSMVIKRGHPQIYQQQFIFKDSDLWGDVAIDECQLGNLQPDSSIVTVAFPTLKAILAQDVQRKTSSNSLVMTTTVSHNIVKPFRISMTFKNNHRSGGKPQCVFWNFSLANNTGGWDSSGCSVEDDGRDNRDRVFCKCNHLTSFSILMSPDSPDPGSLLKILLDIISYIGLGFSIVSLAACLVVEAMVWKSVTKNRTSYMRHICIVNIAFCLLIADIWFIVAGAIHDGRYPLNETACVAATFFIHFFYLSVFFWMLTLGLMLFYRLIFILHDASKSTQKAIAFSLGYGCPLIISSITVGVTQPQEVYMRKNACWLNWEDTRALLAFAIPALIIVVVNVSITVVVITKILRPSIGDKPGKQEKSSLFQISKSIGVLTPLLGLTWGFGLATVIQGSNAVFHIIFTLLNAFQGLFILLFGCLWDQKVQEALLHKFSLSRWSSQHSKSTSIGSSTPVFSMSSPISRRFNNLFGKTGTYNVSTPETTSSSLENSSSAYSLLN
Protein: Probable methyltransferase PMT23 (EC 2.1.1.-) (Q9SIZ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAISVQHVVVLLLSTLLIAITFFLFTSDNARFPFPSLSTTDYYTPIPKSPIPHRIVDVSSDQTPQKMKLNTSLEVGELKWDLCKGAESVDYIPCLDNYAAIKQLKSRRHMEHRERHCPEPSPKCLLPLPDNYKPPVPWPKSRDMIWYDNVPHPKLVEYKKEQNWVKKEGEFLVFPGGGTQFKFGVTHYVEFIEKALPSIKWGKNIRVVLDVGCGVASFGGSLLDKDVITMSFAPKDEHEAQIQFALERGIPATLSVIGTQQLTFPSNAFDLIHCARCRVHWDADGGKPLLELNRVLRPGGFFIWSATPVYRDNDRDSRIWNEMVSLTKSICWKVVTKTVDSSGIGLVIYQKPTSESCYNKRSTQDPPLCDKKEANGSWYVPLAKCLSKLPSGNVQSWPELWPKRLVSVKPQSISVKAETLKKDTEKWSASVSDVYLKHLAVNWSTVRNVMDMNAGFGGFAAALINLPLWVMNVVPVDKPDTLSVVYDRGLIGVYHDWCESVNTYPRTYDLLHSSFLLGDLTQRCEIVQVVAEIDRIVRPGGYLVVQDNMETIMKLESILGSLHWSTKIYEDRFLVGRKGFWRPAKPELR
Protein: DNA-directed RNA polymerase III subunit RPC2 (RNA polymerase III subunit C2) (EC 2.7.7.6) (C128) (DNA-directed RNA polymerase III 127.6 kDa polypeptide) (DNA-directed RNA polymerase III subunit B) (Q9NW08)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:33417887}. Cytoplasm, cytosol {ECO:0000269|PubMed:33335104}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerase III subunit RPC7
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit RPC8
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase III subunit RPC4
Sequence:
MDVLAEEFGNLTPEQLAAPIPTVEEKWRLLPAFLKVKGLVKQHIDSFNYFINVEIKKIMKANEKVTSDADPMWYLKYLNIYVGLPDVEESFNVTRPVSPHECRLRDMTYSAPITVDIEYTRGSQRIIRNALPIGRMPIMLRSSNCVLTGKTPAEFAKLNECPLDPGGYFIVKGVEKVILIQEQLSKNRIIVEADRKGAVGASVTSSTHEKKSRTNMAVKQGRFYLRHNTLSEDIPIVIIFKAMGVESDQEIVQMIGTEEHVMAAFGPSLEECQKAQIFTQMQALKYIGNKVRRQRMWGGGPKKTKIEEARELLASTILTHVPVKEFNFRAKCIYTAVMVRRVILAQGDNKVDDRDYYGNKRLELAGQLLSLLFEDLFKKFNSEMKKIADQVIPKQRAAQFDVVKHMRQDQITNGMVNAISTGNWSLKRFKMDRQGVTQVLSRLSYISALGMMTRISSQFEKTRKVSGPRSLQPSQWGMLCPSDTPEGEACGLVKNLALMTHITTDMEDGPIVKLASNLGVEDVNLLCGEELSYPNVFLVFLNGNILGVIRDHKKLVNTFRLMRRAGYINEFVSISTNLTDRCVYISSDGGRLCRPYIIVKKQKPAVTNKHMEELAQGYRNFEDFLHESLVEYLDVNEENDCNIALYEHTINKDTTHLEIEPFTLLGVCAGLIPYPHHNQSPRNTYQCAMGKQAMGTIGYNQRNRIDTLMYLLAYPQKPMVKTKTIELIEFEKLPAGQNATVAVMSYSGYDIEDALVLNKASLDRGFGRCLVYKNAKCTLKRYTNQTFDKVMGPMLDAATRKPIWRHEILDADGICSPGEKVENKQVLVNKSMPTVTQIPLEGSNVPQQPQYKDVPITYKGATDSYIEKVMISSNAEDAFLIKMLLRQTRRPEIGDKFSSRHGQKGVCGLIVPQEDMPFCDSGICPDIIMNPHGFPSRMTVGKLIELLAGKAGVLDGRFHYGTAFGGSKVKDVCEDLVRHGYNYLGKDYVTSGITGEPLEAYIYFGPVYYQKLKHMVLDKMHARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCLIGYGASMLLLERLMISSDAFEVDVCGQCGLLGYSGWCHYCKSSCHVSSLRIPYACKLLFQELQSMNIIPRLKLSKYNE
Protein: Kinesin, putative (Q386R1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Kinesin, putative
- Kinesin-like protein
Sequence:
MSKPRDAEEGHVTVCVRARPLNEREKRLNSPICLQFQNGKTVSIYKSSVPNGAAADAGCDAAGGKCFSFDRAFDSNDSQTTVYEYLGIPVLQATIKGFNACVFAYGQSGSGKSYSMMGPSGGRDVVVDPGIIPRLSRGLFEMVAKEVAENEREREAARSSGVEENALPPQLNITVLVSYMEIYQERVNCLLNPKCENLKVREHKVLGVYVEGISEVQVDSEESMMQVMHGGNQSRHIAATNMNDRSSRSHAIFSITVIQKRMGKVKDGTVSCTELRAKVNLVDLAGSERAKSTGAEGGTLREGANINKSLTVLGQVISALADIGKSKPDAGGRRHVPYRDSTLTFILKESLGGNSKTFMLSTLSPAAANYDETMSTLRYADRAKSIVTRAVVNAAAGDKRIRELEEEVQQLREKMKHYEELALRGGVMPDLANPGGLPNSTGGGHGPASNMEDLESSIPSMTPRRPHDAAVLLSKLEQAEELIKQLTKAEGKQQEAPRPTHPTIKLDRNEPFILNMEGVGDWVVEHLVAGTTYLGTEEPTPGSEWRSITVSGEGTSGVAPRHCCFVRQGNGCVLLRPLEGNLTYINDEQEPISRDVPLMSGTVVCIGDEFLQFKFTDPTAPSMTARRRPMRSAEGTILSPRFKSISESSVPSLRIPAPTQSVGVGITTVAATNSPRGGIASSAANTGNGGSAVPVVPPITAGSGVSPFVPALQLKDVLQHQAQTNTYRPPTHKDPVAADVRPTSVRLPRTAKGVGRSRIGAGEGMERIRAVKTARRLKLRDDEYNVIYRHTFLVLGCGSCGKTSFRENLHKQDKWYSIFTSDQKNLRPSFGVESTTISSTGEYPSVEMNVMELGGTGCFSLLQGLLPTRRATYVLCFSLLQSVPFEGLLPFLEFILSHTTTRDTSVVLVGTYLDRSPLKSSKLAQHFSELEMQVNNYFRTLQVVGDMRPSIAGCFAVDNVNRTVFAPMFERLRKFPDLLSWFGDQAIRRCRNDADFPNAQVPKLLLSLGKRTKEINREGKWCVAFGEFKSVANALDNRYSDNLDDLHRHIQLLMSWGVLHHHYRHRAMRKYVIVDTPWVFRVVATLSCCSTVTPKLPGNDSSLRSVPLVLCREVMQSMRKSLPFDVDAVLIEDVCGALLQGVLTMRTALALFDGVLKEKGYGFAQLGGLLELLRSYDFIIMGSRLQYSFFNDENTSVQSSPTNAGKDMREVGSGLGRKKSAGPSGGPESEHFVLIPSCFMNPTPSSFCMHVPSFLHGPFYRFTLNMVPHNFFSRIVSRVAHCAKKVYLGPATARCVKLEDLVWNPNSQDDGKGGNRVGSNVNGSSNNTKGTEPSVVATNSVYVVGSSQFWENTMWVISSPGSRALLRMVQRSLFVTFHDMENSDEFYDGLRHVIRNILYESPGVTCQESILCLRRALEDGEKAEEVHGDLTYWRHVDENVNSLEKIKQREATALMTPRGTTPRLSMKGRAGGTMEIERSRQGGSRAGVKNGSGNSDEEDELNDVVIPFVRNHTEPIDVEAALRRVCSDSLLTDNALNELKTALQAMKEARSCGDHSGECCALDRLVDVLAQT
Protein: Protein PALS2 (MAGUK p55 subfamily member 6) (Membrane protein, palmitoylated 6) (Veli-associated MAGUK 1) (VAM-1) (Q9NZW5)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Protein lin-7 homolog A
- Protein lin-7 homolog C
- Cell adhesion molecule 1
- Cell adhesion molecule 4
- Cell adhesion molecule 3
- MAGUK p55 subfamily member 2
- Tyrosine-protein kinase STYK1
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- InaD-like protein
- Protein lin-7 homolog B
Sequence:
MQQVLENLTELPSSTGAEEIDLIFLKGIMENPIVKSLAKAHERLEDSKLEAVSDNNLELVNEILEDITPLINVDENVAELVGILKEPHFQSLLEAHDIVASKCYDSPPSSPEMNNSSINNQLLPVDAIRILGIHKRAGEPLGVTFRVENNDLVIARILHGGMIDRQGLLHVGDIIKEVNGHEVGNNPKELQELLKNISGSVTLKILPSYRDTITPQQVFVKCHFDYNPYNDNLIPCKEAGLKFSKGEILQIVNREDPNWWQASHVKEGGSAGLIPSQFLEEKRKAFVRRDWDNSGPFCGTISSKKKKKMMYLTTRNAEFDRHEIQIYEEVAKMPPFQRKTLVLIGAQGVGRRSLKNRFIVLNPTRFGTTVPFTSRKPREDEKDGQAYKFVSRSEMEADIKAGKYLEHGEYEGNLYGTKIDSILEVVQTGRTCILDVNPQALKVLRTSEFMPYVVFIAAPELETLRAMHKAVVDAGITTKLLTDSDLKKTVDESARIQRAYNHYFDLIIINDNLDKAFEKLQTAIEKLRMEPQWVPISWVY