wanglab/gogpt-training-data huggingface dataset:
Protein: Cuticlin-like protein 19 (H2KZ72)
Organism: Caenorhabditis elegans
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:21613545}.
Interaction partners:
- ZP domain-containing protein
- ZP domain-containing protein
- ZP domain-containing protein
- Golgi SNAP receptor complex member 2 homolog memb-1
- Golgi SNAP receptor complex member 2
- Vacuolar protein sorting-associated protein 52 homolog
- BET1 homolog
- Vesicle transport protein USE1
Sequence:
MVEYNRIFCVLVIFSTTIKCEYSELMNQKIGVRVEVLNMIYENETTITSTGHPRCRLTLHKSGWDRDTCSSPQFKLNDTLSWSTRVCYKWVCDTTKYAMRVESCWIGSPNMSVYILRDDGCTIEKAILTSPVYTSFNRAAAIGWMAVRQKNMKYMHVGCTIRLCHLCDPKCQTITPPRTCNDNRADDYEAMWNSSSRVKNLCFPEPSTTENLNLNFGNSPFQNVGNIIILLLVFLLR
Protein: Type 2C protein phosphatase (Q5A388)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit alpha
- Pyruvate dehydrogenase E1 component subunit beta
- Dihydrolipoyl dehydrogenase
- Type 2C protein phosphatase
- Acetyltransferase component of pyruvate dehydrogenase complex
Sequence:
MSFVLAAKPRFVYLTNKQLQTIGKRLLTQSAKSSFKSSQCLLSEPNTMIKTASPKKNQQQYRKSVALVSGVIIVGSYIVFNQSNYFNLDTLPSNLPPPQQSKKLLQDNQKKYFSTSTSSLHQKDSISHQQHKEGIFLLNEEQVSTKLRQFEESYTVNRGKGVTRYDICQLPSNSPIEDDRAEEIVQVPILQDNNIKTSTDWMFFGVFDGHGGWTTSSKLRDQLIGYVINELGTIYKPVQGEENLRYVPNSATIDQAMKNGFLKLDHELVNKNIEKLLTDGNKAKAAELLMPALSGSCALLSFYDTNSQMLKVAVTGDSRAILGSFKDNHWTVRQLSIDQTGANPSEVARIISEHPNEPKVIRNGRVLGSLEPTRAFGDCRYKLPAVIQERIYKQFFGRPLPNQLKSPPYVTAEPIITTTKINPNEHDFLVMASDGLYEMLTNEEIVGLVVKWMEKADMIKPRKSWFGFGSADSKLPEVKDVTNDKASKKPLNNKLGNSFLLEDNNVSTHLIRNALSNGGSREQTSMLISIPNPVSRRYRDDLTVTVVFFGKDTKGEDENGTLEVNWNATAGGLNSAKPKL
Protein: Aquaporin-0a2 (Auaporin-0a2) (Lens fiber major intrinsic protein-like) (A0A0K0LT76)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Filensin
- Filensin
Sequence:
MWEFRSMSFWRAVFAEFYGTMFFVFFGLGAALRWTTGPHNVLHVAFCFGLAAATLIQSIGHISGGHINPAVTFAYLIGSQMSLFRAFFYIVAQCLGALAGAAVLYGVTPNNMRGNLALNTLQPGISLGMATTMEVFLTLQLVVCIFAVTDERRNGRLGSAALAIGFSVLIGHLLGMYYTGAGMNPARSFAPAVLVRNFVNHWVYWVGPMIGGAMGAIIYDFMLFPRMRGLSERMAILKGTRPPEAESQQDTRGEAIELKTQAL
Protein: ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphofructokinase A) (Phosphohexokinase) (Tagatose-6-phosphate kinase) (EC 2.7.1.144) (P9WID7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. Can also catalyze the phosphorylation of tagatose-6-phosphate. Both sugar phosphates can function equivalently as substrates. Cannot catalyze the reverse gluconeogenic reaction.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
Interaction partners:
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- ATP-dependent 6-phosphofructokinase isozyme 2
- Pyruvate kinase
- Fructose-1,6-bisphosphatase class 2
- Transaldolase
- Transketolase
- Triosephosphate isomerase
- GMP synthase
- Enolase
Sequence:
MRIGVLTGGGDCPGLNAVIRAVVRTCHARYGSSVVGFQNGFRGLLENRRVQLHNDDRNDRLLAKGGTMLGTARVHPDKLRAGLPQIMQTLDDNGIDVLIPIGGEGTLTAASWLSEENVPVVGVPKTIDNDIDCTDVTFGHDTALTVATEAIDRLHSTAESHERVMLVEVMGRHAGWIALNAGLASGAHMTLIPEQPFDIEEVCRLVKGRFQRGDSHFICVVAEGAKPAPGTIMLREGGLDEFGHERFTGVAAQLAVEVEKRINKDVRVTVLGHIQRGGTPTAYDRVLATRFGVNAADAAHAGEYGQMVTLRGQDIGRVPLADAVRKLKLVPQSRYDDAAAFFG
Protein: Succinate dehydrogenase assembly factor 1, mitochondrial (SDH assembly factor 1) (SDHAF1) (Q3E785)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit SDH2 of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. Acts together with SDHAF3 (SDH7).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase assembly factor 3, mitochondrial
- Succinate dehydrogenase assembly factor 2, mitochondrial
- Mitochondrial zinc maintenance protein 1, mitochondrial
- Protein ISD11
- NifU-like protein
- Acyl carrier protein, mitochondrial
Sequence:
MPKRLSGLQKEVLHLYRASIRTAHTKPKENQVNFVNYIHEEFGKYRNLPRKDFTTIEHLLRVGNKKIATFSHPELTNIH
Protein: Galactoside 2-alpha-L-fucosyltransferase SEC1 (EC 2.4.1.-) (Secretory blood group protein 1) (Q9TTY3)
Organism: Bos taurus (Bovine)
Function: Catalyzes the transfer of alpha 1,2-linked fucose to ganglioside GM1 and galacto-N-biose.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:O09160}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O09160}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250|UniProtKB:O09160}.
Interaction partners:
Sequence:
MWDMRAVAPQRPAAGHPRAGWPRKLKTAATRFWATCPSSSTVCFLFVIFAVSTVFHCHRRLALVPAPWAYAGHVVLFPRHLPRGGVFTINAKGRLGNQMGEYATLYALAKMNGRAAFIPPQMHSTLAPIFRITLPVLHDATARSVPWQNYHLNDWMEEQYRHIPGEYVRLTGYPCSWTFYHHLRAEILQEFTLHAHVREEAQNFLRGLRVNGSRPSTYVGVHVRRGDYVRVMPTMWKGVLADRGYLQQALDWFRARHHSPLFVITSDDMAWCRRNINSSHRDVVFAGSGQQGSPARDFALLTQCNHTVITVGTFGIWAAYLAGGSTVYLANFTLPGSRFRMIFKPQAAFLPEWVGIAANLGQARESHP
Protein: AP-2 complex subunit sigma (Adaptin small chain) (Clathrin assembly protein 2 sigma small chain) (Sigma2-adaptin) (Q9Y7L6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity).
Subcellular location: Cell membrane {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of the plasma membrane coated vesicles. {ECO:0000250}.
Interaction partners:
- AP-2 complex subunit mu
- AP-2 complex subunit alpha
- AP-1 complex subunit beta-1
- AP-2 complex subunit beta
- AP-1 complex subunit gamma-1
- AP-3 complex subunit delta
- Probable clathrin heavy chain
- Repressor of RNA polymerase III transcription maf1
- AP-1 complex subunit mu-1
- Uncharacterized calcium-binding protein C800.10c
Sequence:
MIQFILIQNRHGKNRLSKYYVPFDDDEKVRLKARIHQLISQRNQKFQANFLEWENSKLVYRRYAGLYFCFCVDSTDNDLAILEMIHFFVEILDSFFGNVCELDLIFNFYKVSAILDEIILGGEIGESNKKSVLERIEALEKLE
Protein: Probable zinc transporter MSC2 (Meiotic sister chromatid recombination protein 2) (Q03455)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probably act as a zinc ion transporter moving zinc from the nucleus/endoplasmic reticulum to the cytoplasm. Involved in zinc ion homeostasis and cellular distribution.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. Nucleus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein ZRG17
- Zinc transporter YKE4
- Zinc-regulated transporter 3
- Zinc-regulated transporter 2
- Zinc-regulated transporter 1
- Zinc-responsive transcriptional regulator ZAP1
Sequence:
MNLQELLAKVPLLLSYPTIILSSNLIVPSHNDLISRAASTSAAEYADEKLIFFSTDHAIRLIFLPTFVASSFNLFAHYFNFINYSSRRKYYVLFTAIYFLSILTAIFHPIQSTCITLLIIKLLTTADESSPKIALNFKTILKTFVPFITLTLVILRWDPSFDASSGDVNKISTSLAAYALLILTLRYASPLILSTLSSSIGVVSKDTSVAQHSISRNKRFPLILVLPIFSFVLLYLMTIVNKTYNIQLLMVFVFFGCLSIFFLSLKDLFTEDGNQKKGGQEDEYCRMFDIKYMISYLWLTRFTILLTGIMAIVVHFLSFNEITSSIKTDLLSLLFVVVAEYVSSFSNKQPDSHSHNHAHHHSHLTDSLPLENESMFKQMALNKDTRSIFSFLLLNTAFMFVQLLYSFRSKSLGLLSDSLHMALDCTSLLLGLIAGVLTKKPASDKFPFGLNYLGTLAGFTNGVLLLGIVCGIFVEAIERIFNPIHLHATNELLVVATLGLLVNLVGLFAFDHGAHDHGGTDNENMKGIFLHILADTLGSVGVVISTLLIKLTHWPIFDPIASLLIGSLILLSALPLLKSTSANILLRLDDKKHNLVKSALNQISTTPGITGYTTPRFWPTESGSSGHSHAHTHSHAENHSHEHHHDQKNGSQEHPSLVGYIHVQYVDGENSTIIKKRVEKIFENVSIKAWVQVEPQNSTCWCRATSMNTISANPNSLPLQPIAN
Protein: Peroxisome biogenesis factor 10 (EC 2.3.2.27) (Peroxin-10) (Peroxisomal biogenesis factor 10) (Peroxisome assembly protein 10) (RING finger protein 69) (O60683)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX10 also regulates PEX5 recycling by acting as a E3 ubiquitin-protein ligase. When PEX5 recycling is compromised, PEX10 catalyzes polyubiquitination of PEX5 during its passage through the retrotranslocation channel, leading to its degradation (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:9922452}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 2
- Peroxisomal membrane protein PEX13
- Peroxisomal targeting signal 1 receptor
- Peroxisomal biogenesis factor 19
- Peroxisomal ATPase PEX6
- Peroxisomal targeting signal 2 receptor
- Peroxisomal membrane protein PEX14
- Peroxisome assembly protein 26
- Peroxisomal ATPase PEX1
Sequence:
MAPAAASPPEVIRAAQKDEYYRGGLRSAAGGALHSLAGARKWLEWRKEVELLSDVAYFGLTTLAGYQTLGEEYVSIIQVDPSRIHVPSSLRRGVLVTLHAVLPYLLDKALLPLEQELQADPDSGRPLQGSLGPGGRGCSGARRWMRHHTATLTEQQRRALLRAVFVLRQGLACLQRLHVAWFYIHGVFYHLAKRLTGITYLRVRSLPGEDLRARVSYRLLGVISLLHLVLSMGLQLYGFRQRQRARKEWRLHRGLSHRRASLEERAVSRNPLCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCREKFPPQKLIYLRHYR
Protein: Proline dehydrogenase 2, mitochondrial (EC 1.5.5.2) (Osmotic stress-induced proline dehydrogenase) (Proline oxidase) (Q6NKX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts proline to delta-1-pyrroline-5-carboxylate.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:20403182}.
Interaction partners:
- Pyrroline-5-carboxylate reductase
- Delta-1-pyrroline-5-carboxylate dehydrogenase 12A1, mitochondrial
- Ornithine aminotransferase, mitochondrial
- Delta-1-pyrroline-5-carboxylate synthase A
- Delta-1-pyrroline-5-carboxylate synthase B
- Urea-proton symporter DUR3
- Proline dehydrogenase 1, mitochondrial
- Proline iminopeptidase
- Probable prolyl 4-hydroxylase 3
- Probable prolyl 4-hydroxylase 4
Sequence:
MANRFLRPNLIHRFSTVSPVGPPTTIIPEILSFDQPKPEVDLDLSDQARLFASVPISTLLRSTAILHATSIGPMVDLGSWLMSSKLMDTTVTRDLVLRIVKGTFYDHFCAGEDAAAAARRVSSVYESTGLKGMLVYGVEHAEDGGACDENIQKFIETVEAAKTLPSSHLSSVVVKITAICPMNVLKRVSDLLRWQYKNPNFKLPWKLNSFPVFSGLSPLYHTTSEPEPLTVEEERELEKAHERLKSVCLRCQESNVPLLIDAEDTILQPAIDYMAYWSAIMFNSDKDRPIVYNTIQAYLKDAGERLHLALRESEKMNVPIGFKLVRGAYMSSEAKLADSLGYKSPVHDTIQNTHDCYNDCMSFLMEKASNGSGIAVILATHNTDSGKLGARKASELGINKENGKIEFAQLYGMSDALSFGLKRAGFNVSKYMPYGPVDTAIPYLIRRAYENRGMMSTGALDRQLMRKELKRRVMAW
Protein: Mitochondrial genome maintenance protein mgm101 (O14354)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Performs an essential function in the repair of oxidatively damaged mtDNA that is required for the maintenance of the mitochondrial genome. Binds to DNA (By similarity).
Subcellular location: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Single-stranded DNA-binding protein rim1, mitochondrial
- Non-selective voltage-gated ion channel
- Mitochondrial distribution and morphology protein 10
Sequence:
MQTMLGKPALQYFGKLSRYLYKNGEPINIWVYSRNSSFSVIPKNGLLSPKITQRFYQNSSIQYQKDKNIYEPKENLEEKELSEGFLDESRLEIPEAGHNWEKSFFGLSSQPFSKEICDLLTAPLEVDDIEIKPDGILYLPEIKYRRILNKAFGPGGWGLAPRGNTNVTSKSVSREYALVCHGRLVSVARGEQTYFDPEGIATASEGCKSNALMRCCKDLGVASELWDPRYIRVFKRENCVEVFVENVLTKKRRKLWRRKEDKFSYPYKEV
Protein: Magu, isoform F (A4UZB1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLARCVLFVTWLAVFIATGKSDDQLMKLPACAAKQGECDDNEGPVCGTDGQTYPTRCHLLRAQCGGHQVSLKYSGSCNACLEAVKFARRQQERDPGYFVPRCRKDGNFAAMQCYGNNGCWCSDSQGRPIADDNKQFRRKGKLRCRANRRDRRRLASHQIGYNPDTSASKGSSEAGSTAHRTCSKSDRSQFNTNLMRMFRNEAQSFFRQPSLSDSHILEWQFSKLDTNGNKLLDRQEIRELKKVLRRNVKPRRCGRTFGKYCDVTKDANLNWLEWSVCFTKEFHNLLNSKPETASQDLENDSNCWMDQSVTLEEQGHGGKSVLFVPQCLPDGRYQRIQCYSSTSTSYCWCVNEDTGKSIPGTSVKNKRPQCDESVAVRPMKGCTEPRKTQFLKELKAYLNTSLLPSSTTGSNSSMWKTDDERIATLSFVYLDKNKNKSWDRREWKNFRDLVTSASHLRRCGKKMPRYCDVNGDKKISLAEWLNCLQATPRESATTAKPAQSNETASPKFQGVNPVERYLKD
Protein: Uncoordinated 79, isoform E (A0A0B4LID2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTGSFKVQLINMGTRAAAFQAKLRALHEYHVRLLHNVLPAPSGVDIANNIKYFSQTLLTVLKDVRTSPHELIRDPLEDPTRMSAYPNLEYGNLYNALTMLIDVAPCIQYGQIVFGKALLQCLSCILPFLDKDLIDNLPYLVSSTISVLPPALHQCIINALCYYILPFTITRRSSDEQECQACQSVSSVIMMVLQYSNNPAHHCQLLECLMTLKHNVVKDILCVVAYGTAVSRTSAAKLLFYYWPAFNANLFDRKVLLSKLTNDLVPFTCQREHCPNSGNAEAAKVCYDHSISIAYAPDCPPPLYLCIECANEIHREHGSLEFGDILHPMQQVSMVCENKNCRSNEKSAFSICFSTECASFNGNHPIRYCSQCHSNRHNSRRGGDHVVHRSLQPAWQMDPEMQMHMVESVVSLLREAKPLNFEPGKESSSSESKKNGSGITADNISLEERQRLGRYGIWLLVGRCTPTADTPVEVLGRILSMLFHWFHVTAYSYDAAGQVESTIEKLKVDHVCNWLKDICRIHYNVFISCLLPHPPEYARVGGHWETLASRTSHLKEGLQRLICLVPYEVITSEIWDYVMPHWMEAITNDVAEKELNELKIVLSKILDPEMSPLGFDAKTMYNFVAIRFEKTTAKVQQQALHWLQILTKLEILIPLVQLFAMFGDGVRIMKYGIQHELMREKDAQSQSLAKAPKTPCKESKETKADMANPPRRSSISPVVEDDSGNTSAISDDEAPTNRHTEFSTDAEHNLTCCILMLDILLKQMELQDVEQHMGIHTSVCENVSRLIKCMVTAARVGLSSHVCALKVAECAYCEASIMWHQLATKLVQFMAPLNPVRPPDVPIEDIIEEEKSSRKSPPESDKEKTRDRDVSLSMAPLPIPLGPLGGFAGPVPVAVPQPEPHSVGGVLVHMPHVCSNNENGHSVDSNELRKVHATDEIMTATVETVSEQLDLASILPTDRAIARSITLSDADVGSANVSVTKASVMGENGANGGGACGGGENGSGSEEDEEEEDSDDFWHTSVGKFKFTLDTLPQPLQYIHQLLTEIPTIKKPEILYYVLQCLNTMALHGDALAKAAREQRGFFIWCQENLLIKNLWELCNAEHSHICQVGVPLLLHCITLPLGSDVFWRVVQEAFHDTDWRVRFTAVERVTVITRFMDSTPLRSEVGLQTALATAFCHLIASMDDINVYVAQRATLYIGTIHDTAIRSLLFCLESQFDLFIVDRPVVLQSVYQLHNSLSDRKMLGWEFFLNRFDTLFVEAQINLEKCGDISYLRDLRNSDNGSEALSAKIQKAREALSQSDTSGGMAKTLSASFGTKWPYKRTMSAPASMAPRQDSKFVPEKEKIYSRQVSAPILKRKTSRFGLDGHIHSLGGLNDDNLIGLLSRITELEESDRETIHLLVFMLMQFMSRTDQAYPSEEKPMTKTQNIVLKHLFLLLGHNQIDKTFHTTPESLRVSAVFNAFLANLPQVLDQNHLIGGLILPSVMQIILYAPNPTSTSGESYQNIVFNYSLWHLEQYPRRNWLFTLLVVLYKYSYTQPPLSGYVIAGIRLIMNSLRGHFHQCRRIPTTTILDIQGVGGAARSRDVSQPSLGTDPDDKEASPPASPMFPSEGTSAASKSKGNVAFTPKLQHAFRKYNDSSLDADETESELVAIPESDLSDSTLHGSSAPGSFDDTIHFEDVMPRNRRALEYTEEKSTKSHKSMITTKVGDTYTTKIKATTTSETLVTTHTRHSLQEGVRMIVTPLVGAETTETAIVSPPVDVHRAVTVRNKSLENAAASTSKMFAAIATNHLKALGALQDMPAAVERKAASSSGSGSRSANGSGNGSGGSAPAAIQASSSAAASKPIGRHKTIVECSAGNSSSSADDSRQKKSQTKSLRRTDKNYGSPDSPLSKMSVMPNPRDEMDESMQSLPPPKSIAALEIPTPERLLPIGTQDTVATLVERVRDGLNLPDISHLKQDSLDVSESTKDDVTPSSRTNSPRRLIKQVALESPPNPNAQLPSQPSADLHTSILKNVQQDLKQNAPEGNGLTTSNSIKRPRQKLAPFNVDSNAIPDIRSRFAGSWPPPPFQPVDPEPDDDDEIGAEASNGHGIHSTPHAPRGSSRRVGDYTIVERCSDCGAHIEEYTDEEIGIFIVILGTFIHREPAMAAPFLPEILTMTSRICLSSTHAWQGENGPPLASSAQAVACQFFRCVLHQLAPNGIFLQVFQTQMKMKIRHHHFRSIAKALQDFQDLNSTSPIYMVCESLTSKKSLPIEQLPVIFRNMAEYLNLQCVPTEAGVGLAVWSQAMQAMESLLRQVIVIMPSLTNAEYMLDIMAATLRLNCVPKTLLDPYSKIMAYCVQHTNLEYQTLYELCTLNIRSFSKDRDKNLLCRQMIFEFVQALKFKSNIPDHNLLTIIGFVLLDAGGTLPPGAAPGLPDAAPMMTTNSADCLRQYINDVIDFLADFHTLSKIKNFKNGQTSSGLGEDTLGGVLKGAVAQYLALEMSRGNSRDNKAVSRYLPWLNNAPSSLQQGPKEFTECVGHMRLLSWLLLGSLTHMALMQRRQETHSIPTPLPQQNSQGTGPAASVHYQHQGVTYSQPVPQEASCHIADHIQVIFAGFAEQSKTSVLHMSSLFHAFTLCQLWTVYLEQMAHNTNSNAEGSTLGVLFEFWAKVTPCILQLVSHAKPTVNKDQPQTPLDFQTQSANSKLSEMVNLHFLSLLEALKDTNSTVLGKLLPMWSPVLSSQTQLSDTLHVRLQNVRDYAPDYEEQQTYKSEALLKWLQRLQFKMGQIELQASTATQFYSI
Protein: Probable insulin-like peptide gamma-type 1 (Ceinsulin-3) [Cleaved into: B-chain-like peptide; A-chain-like peptide] (Q18060)
Organism: Caenorhabditis elegans
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Insulin-like peptide 7
- Probable insulin-like peptide alpha-type 3
- INSulin related
- Probable insulin-like peptide beta-type 1
Sequence:
MSSYRQTLFILIILIVIILFVNEGQGAPHHDKRHTACVLKIFKALNVMCNHEGDADVLRRTASDCCRESCSLTEMLASCTLTSSEESTRDI
Protein: ATP synthase subunit alpha (Q6FJ33)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- ATP synthase subunit 4
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit d
- ATP synthase subunit beta
- ATP synthase subunit gamma
- Candida glabrata strain CBS138 chromosome A complete sequence
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit a
- ATP synthase subunit 5, mitochondrial
- Candida glabrata strain CBS138 chromosome K complete sequence
Sequence:
MLSRVVLARNALRAVSRASRASRGSVVRTSARCYAAKAQPTEVSSILEEKIRGVSDEAQLNETGRVLAVGDGIARVFGLNNIQAEELVEFASGVKGMALNLEPGQVGIVLFGSDRLVKEGEIVKRTGKIVDVPVGPGLLGRVVDALGNPIDGKGPIESVGTARAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNDGNDESKKLYCVYVAIGQKRSTVAQLVQTLEQHDALKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDKEGAGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGERLTQLLKQSQYSPLAAEEQVPLIYAGVNGYLDNIDLGRIAEFESSFLAYLKSNHENILNDIRDKGELTKDLLATLKSATESFVATF
Protein: Kinase family with leucine-rich repeat domain-containing protein (Leucine-rich repeat receptor-like protein kinase) (Putative receptor protein kinase) (T1N24.22 protein) (Q9XGZ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- PAMP-induced secreted peptide 2
- Hydroxyproline-rich glycoprotein family protein
- At2g23270
- Proline-rich family protein
- Uncharacterized protein
- Uncharacterized protein
- Receptor-like kinase
- Transmembrane protein
- At4g37295
- Zinc knuckle
Sequence:
MTRLPLPFLFFFLTSIPLSVFSQFNDQSTLLNLKRDLGDPPSLRLWNNTSSPCNWSEITCTAGNVTGINFKNQNFTGTVPTTICDLSNLNFLDLSFNYFAGEFPTVLYNCTKLQYLDLSQNLLNGSLPVDIDRLSPELDYLDLAANGFSGDIPKSLGRISKLKVLNLYQSEYDGTFPSEIGDLSELEELRLALNDKFTPAKIPIEFGKLKKLKYMWLEEMNLIGEISPVVFENMTDLEHVDLSVNNLTGRIPDVLFGLKNLTEFYLFANGLTGEIPKSISATNLVFLDLSANNLTGSIPVSIGNLTKLQVLNLFNNKLTGEIPPVIGKLPGLKEFKIFNNKLTGEIPAEIGVHSKLERFEVSENQLTGKLPENLCKGGKLQGVVVYSNNLTGEIPESLGDCGTLLTVQLQNNDFSGKFPSRIWNASSMYSLQVSNNSFTGELPENVAWNMSRIEIDNNRFSGEIPKKIGTWSSLVEFKAGNNQFSGEFPKELTSLSNLISIFLDENDLTGELPDEIISWKSLITLSLSKNKLSGEIPRALGLLPRLLNLDLSENQFSGGIPPEIGSLKLTTFNVSSNRLTGGIPEQLDNLAYERSFLNNSNLCADNPVLSLPDCRKQRRGSRGFPGKILAMILVIAVLLLTITLFVTFFVVRDYTRKQRRRGLETWKLTSFHRVDFAESDIVSNLMEHYVIGSGGSGKVYKIFVESSGQCVAVKRIWDSKKLDQKLEKEFIAEVEILGTIRHSNIVKLLCCISREDSKLLVYEYLEKRSLDQWLHGKKKGGTVEANNLTWSQRLNIAVGAAQGLCYMHHDCTPAIIHRDVKSSNILLDSEFNAKIADFGLAKLLIKQNQEPHTMSAVAGSFGYIAPEYAYTSKVDEKIDVYSFGVVLLELVTGREGNNGDEHTNLADWSWKHYQSGKPTAEAFDEDIKEASTTEAMTTVFKLGLMCTNTLPSHRPSMKEVLYVLRQQGLEATKKTATEAYEAPLLVSLSGRRTSKRVEDEDLGFV
Protein: Merozoite surface protein P41 [Cleaved into: Merozoite surface protein P41, processed form] (Q8I1Y0)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cell surface. Cell membrane. Note=Present on the surface of merozoite. {ECO:0000269|PubMed:22848665}.
Interaction partners:
- Merozoite surface protein P12
- Merozoite surface protein P38
- Merozoite surface protein P92
Sequence:
MKGVIFCLVVLLWRQAWVSSKSHKCDFTKEKYLLSGEKEVSCEIDANPSDDITFICPNKIDSLCFHTVNISKNINQNKSTMSIQDLLYGSVVYGNTLFISPYVRTNTPFYCFCNLDTVTIQKFLKINRFLKDDDELSEADVMKHLKGGNVSEAQADEYLNKALNRFKKMKDLSKFFNDQADNTTKLNLPKSLNIPNDILNYDVYNSSNNRNDIVVKDEVTNKQIISKRGIMSVFVRSNNNVIKGCDFGNNNKNYFSHPISVAGKVNNKVCKIQGKPGELVGFKCAFEENGKVEPPNCFDQVLHKNKVTDLKTLIPGYASYTNKHSSKYPYYLKIPHFVNEQYTIQCKCKSNNSQNEYTFELDIQPGESEVVLNSFKTS
Protein: ADAM28 isoform-1 (Q7TSB4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MQQWRLLVVWFLLSPVPASAIKELPKAKNYEVVYPIRLHLLHKRETKEPEPKETFETELRYKMTVNGKVVELYLKKNNKLLAPGYLETYYNSSGNKVTTSPQIMDSCYYQGHIINEKDSAASISMCQGLRGYFSQADERYFIEPLSSEILDEQAHALFKDDPKEDQGNSNCGVDDALWLQGLHQDVVLPATRLIKLNDGMVQEPKKYIEYYVVLDNGEFKKYNKNLDEIRKRVHEMANYVNMLYNKLGAHVALVGMEIWTDEDKIKITPDANTTLENFSKWRGNDLLKRKHHDVAQLISSTDFSGSTVGLAFMSSMCSPYHSVGIVQDHSNYHLRVAGTMAHEMGHNLGMIHDYLSCKCPSEVCVMEQSLRFHMPTDFSSCSRDNYRRFLEEKLSHCLFNSPLPSDIISTPVCGNQLLEMNEDCDCGTPKECTNKCCDAETCKIKAGFQCALGECCEKCQLKKPGVVCRAAKDECDLPEMCDGKSSHCPVDRFRVNGFPCQNGHGYCLKGNCPTLQQQCMDMWGPETKVANKSCYKQNEGGSKYGYCHVENGTHMPCKAKDAMCGKLFCEGGSGDLPWKGLTIAFLTCKLFDPEDINQGVDMVANGTKCGNNKVCINAECADMEKTYKSANCSSKCKGHAVCDHELQCQCKEGWAPPDCEDSATVFRRRLHHGWRALSSGSHICGDCYSDPSSKCQKKAKESSEATTHQGCQATQAEV
Protein: Synaptotagmin-like protein 1 (Exophilin-7) (Q99N80)
Organism: Mus musculus (Mouse)
Function: Binds phosphatidylinositol 3,4,5-trisphosphate (By similarity). May play a role in vesicle trafficking. Acts as a RAB27A effector protein and may play a role in cytotoxic granule exocytosis in lymphocytes.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:18266782}; Peripheral membrane protein {ECO:0000269|PubMed:18266782}. Cell membrane {ECO:0000269|PubMed:18266782}.
Interaction partners:
- Ras-related protein Rab-27A
- TBC1 domain family member 10A
- Ras-related protein Rab-27B
Sequence:
MPQRGHPSQERLWALPSLPMAHGPGSEVEGLLDLSFLTEEEQEAISDVLKRDAHLRQLEEGRVSKLRASLEDPWQLKILTGDWFQEARSQRHHHAHFGSDLVRASIRRKKSPKGDQALGSDGEAEAAGEDTIEGEPESRVSIEVAAPERSTETQGPDLSSPYVPSKASEGQEEEPQDHECELEAPGEGGVQVAEADPELDPEQKAEQESQPTPAQSKATSKILENGEEAPGLGPSLDRMLSSSSSVSSLNSSTLSGSLMSLSGEEAGTVQVRGSVLFSLHYEPGTSELRVQVIQCQGLAAARRRRSDPYVKSYLLPDKQSKRKTSVKKRNLNPIFNETLRHSVQQADLPGRVLSLSVWHRESLGRNIFLGEVEVPLDTWNWDSEATWLPLQPRVPPSPDELPSRGLLSLSLKYVPAGSEGGGQPQSGELHFWVKEAQSLVPLRPGSLDTYIQCSVLPDDSRASRQRTRVVRRSLSPVFNHTMVYDGFGPADLRQACAELSLWDHGALASRQLGGTRLSLGTGSSYGLQVPWMDSTPEEKQLWQTLLERPCEWVDGLLPLRTNLVPRA
Protein: Mitochondrial metalloendopeptidase OMA1 (EC 3.4.24.-) (P36163)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protease that is part of the quality control system in the inner membrane of mitochondria. Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OXA1 and COX1. Cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Cleaves the misfolded multi-pass membrane protein OXA1. Involved in quality control of cytochrome oxidase assembly: mediates the cleavage of COX1 in cells lacking COA2. Required for the stability of the respiratory supercomplexes. Required for TOR signaling.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:12963738}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1
- Mitochondrial inner membrane m-AAA protease component YTA10
- Dynamin-like GTPase MGM1, mitochondrial
- Cytochrome c oxidase assembly factor 2
- Mitochondrial inner membrane protease ATP23
- CAAX prenyl protease 1
- Mitochondrial inner membrane m-AAA protease component YTA12
- Rhomboid protein 1, mitochondrial
- Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR3
- Protein MGR2
Sequence:
MLRNIIRFKGFGKGTSGGFLKPVSFRVQLTRCYRYDNGPSYRRFNNGEYSQKSSFKSILLDKSSRKYLALLFGGCSLFYYTHLDKAPVSDRSRFIWVSRPLELTIGNYTYKSIWRQTQQEILPPQHPLSIKIENIFMKIVEAAYKDPSVDNSLLDGIKWEIHVVNDPTASPNAFVLPGGKVFIFSSILPICANDDGIATVLAHEFAHQLARHTAENLSKAPIYSLLGLVLYTVTGAHAINNILLDGFLRMPASRQMETEADYIGLMIMSRACFQPQESIKVWERMANFEKQMNRGGVVNMEFLSTHPASTRRIENMSKWLPKANEIYEQSDCSSMGNYYKSFFSM