wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome b termination protein 1 (P36038)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in 5'-end processing of mitochondrial COB, 15S rRNA, and RPM1 transcript. May also have a role in 3'-end processing of the COB pre-mRNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cytochrome B pre-mRNA-processing protein 1
- Cytochrome B pre-mRNA-processing protein 2
- Cytochrome B translational activator CBS2
- Cytochrome b translational activator protein CBS1, mitochondrial
- Cytochrome b mRNA maturase bI3
- Cytochrome b mRNA maturase bI2
- Cytochrome c oxidase assembly protein COX16
Sequence:
MVSYGSHSSEVSKVLKTPKFVLRYGNVSSKQRFALKRKINYKLRESKYQEYLNEYNTFVLYDWENSGAGSLVDSSYNLPSLWKEFITEGISKGAINDKLPTVFMKRKLTNSALGHCLGLDFLTDPSESEHEYRCMFQTVQDIPSLSQLILFNSMPNVPVRLKLHTIGININFGCKRSLISNGGDQDTEMSEAVSYIQPLLEESSRMYRNLNYWKLLKIARNNKKDEPLDQSTRIKSQVKLLLSQLATNRITSPSVTDHGGHNWLIFTRRRL
Protein: Beta-actin (Q58J72)
Organism: Meleagris gallopavo (Wild turkey)
Interaction partners:
- Uncharacterized protein.
- Uncharacterized protein.
- Uncharacterized protein.
- Unconventional myosin-XVIIIa
- Uncharacterized protein.
- Uncharacterized protein
- Myosin motor domain-containing protein
- Histone H2A
- Rho-related GTP-binding protein RhoG
Sequence:
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: NAD(P) dependent steroid dehydrogenase-like (Nsdhl protein) (Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (EC 1.1.1.170)) (Q566U2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MATRIRPSSKRCTVIGGSGFLGRHLVERLVDRGYTVNVFDIRQAYELPGVTFYQGDLCDKLALVMALKEVSIVFHCASPAPGSDDGALFQRVNIDGTRTVIQACHEAGVQKLILTSSASVVFEGTDIKNGKEDLPYAKKPIDYYTETKIKQEKLVLEACSKEKGFLTVAIRPHGIFGPRDPQLVPILVDTARRGKMKFIIGDGSNLVDFTYVENVVHGHILAAEHLKADSPLCGQAYHITNDEPVRFWDFMSQILVGLGYSAPRYHLPYALVYGIALLLWFISLILRPLIQFKPTFSPMRVALAGTHHYYSCARAKQDMGYRPLVPLQEAVVRTVESYPHLRNGE
Protein: CSC1-like protein 1 (Transmembrane protein 63A) (O94886)
Organism: Homo sapiens (Human)
Function: Acts as an osmosensitive calcium-permeable cation channel. Mechanosensitive ion channel that converts mechanical stimuli into a flow of ion.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:20957757, ECO:0000269|PubMed:38127458}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:38127458}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:37543036}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MMDSPFLELWQSKAVSIREQLGLGDRPNDSYCYNSAKNSTVLQGVTFGGIPTVLLIDVSCFLFLILVFSIIRRRFWDYGRIALVSEADSESRFQRLSSTSSSGQQDFENELGCCPWLTAIFRLHDDQILEWCGEDAIHYLSFQRHIIFLLVVVSFLSLCVILPVNLSGDLLDKDPYSFGRTTIANLQTDNDLLWLHTIFAVIYLFLTVGFMRHHTQSIKYKEENLVRRTLFITGLPRDARKETVESHFRDAYPTCEVVDVQLCYNVAKLIYLCKEKKKTEKSLTYYTNLQVKTGQRTLINPKPCGQFCCCEVLGCEWEDAISYYTRMKDRLLERITEEERHVQDQPLGMAFVTFQEKSMATYILKDFNACKCQSLQCKGEPQPSSHSRELYTSKWTVTFAADPEDICWKNLSIQGLRWWLQWLGINFTLFLGLFFLTTPSIILSTMDKFNVTKPIHALNNPIISQFFPTLLLWSFSALLPSIVYYSTLLESHWTKSGENQIMMTKVYIFLIFMVLILPSLGLTSLDFFFRWLFDKTSSEASIRLECVFLPDQGAFFVNYVIASAFIGNGMELLRLPGLILYTFRMIMAKTAADRRNVKQNQAFQYEFGAMYAWMLCVFTVIVAYSITCPIIAPFGLIYILLKHMVDRHNLYFVYLPAKLEKGIHFAAVNQALAAPILCLFWLYFFSFLRLGMKAPATLFTFLVLLLTILVCLAHTCFGCFKHLSPLNYKTEEPASDKGSEAEAHMPPPFTPYVPRILNGLASERTALSPQQQQQQTYGAIHNISGTIPGQCLAQSATGSVAAAPQEA
Protein: Mannose-6-phosphate isomerase (EC 5.3.1.8) (Phosphohexomutase) (Phosphomannose isomerase) (PMI) (P29952)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Subcellular location: Cytoplasm.
Interaction partners:
- Phosphomannomutase
- Glucose-6-phosphate isomerase
- Mannitol dehydrogenase DSF1
- Glucokinase-1
- Putative glucokinase-2
- N-acetylglucosamine kinase
- Hexokinase-2
- Hexokinase-1
- Glutamine--fructose-6-phosphate aminotransferase
- Mannose-1-phosphate guanyltransferase
Sequence:
MSNKLFRLDAGYQQYDWGKIGSSSAVAQFAAHSDPSVQIEQDKPYAELWMGTHSKMPSYNHESKESLRDIISKNPSAMLGKDIIDKFHATNELPFLFKVLSIEKVLSIQAHPDKALGKILHAQDPKNYPDDNHKPEMAIAVTDFEGFCGFKPLQEIADELKRIPELRNIVGEETSRNFIENIQPSAQKGSPEDEQNKKLLQAVFSRVMNASDDKIKIQARSLVERSKNSPSDFNKPDLPELIQRLNKQFPDDVGLFCGCLLLNHCRLNAGEAIFLRAKDPHAYISGDIMECMAASDNVVRAGFTPKFKDVKNLVSMLTYTYDPVEKQKMQPLKFDRSSGNGKSVLYNPPIEEFAVLETTFDEKLGQRHFEGVDGPSILITTKGNGYIKADGQKLKAEPGFVFFIAPHLPVDLEAEDEAFTTYRAFVEPN
Protein: Alkaline protease 1 (ALP) (EC 3.4.21.63) (Aspergillopeptidase B) (Aspergillus proteinase B) (Elastase) (Elastinolytic serine proteinase) (Oryzin) (P12547)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Secreted alkaline protease that allows assimilation of proteinaceous substrates.
Subcellular location: Secreted.
Interaction partners:
- Neutral protease 2
- Dipeptidyl-peptidase 5
- Aspergillopepsin-1
- Neutral protease 2 homolog AO090001000135
- P/Homo B domain-containing protein
- Neutral protease 2
- Ribosomal protein L14b/L23e
Sequence:
MQSIKRTLLLLGAILPAVLGAPVQETRRAAEKLPGKYIVTFKPGIDEAKIQEHTTWATNIHQRSLERRGATGGDLPVGIERNYKINKFAAYAGSFDDATIEEIRKNEDVAYVEEDQIYYLDGLTTQKSAPWGLGSISHKGQQSTDYIYDTSAGEGTYAYVVDSGVNVDHEEFEGRASKAYNAAGGQHVDSIGHGTHVSGTIAGKTYGIAKKASILSVKVFQGESSSTSVILDGFNWAANDIVSKKRTSKAAINMSLGGGYSKAFNDAVENAFEQGVLSVVAAGNENSDAGQTSPASAPDAITVAAIQKSNNRASFSNFGKVVDVFAPGQDILSAWIGSSSATNTISGTSMATPHIVGLSLYLAALENLDGPAAVTKRIKELATKDVVKDVKGSPNLLAYNGNA
Protein: Zinc finger protein 454 (Q8N9F8)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAVSHLPTMVQESVTFKDVAILFTQEEWGQLSPAQRALYRDVMLENYSNLVSLGLLGPKPDTFSQLEKREVWMPEDTPGGFCLDWMTMPASKKSTVKAEIPEEELDQWTIKERFSSSSHWKCASLLEWQCGGQEISLQRVVLTHPNTPSQECDESGSTMSSSLHSDQSQGFQPSKNAFECSECGKVFSKSSTLNKHQKIHNEKNANQKIHIKEKRYECRECGKAFHQSTHLIHHQRIHTGEKPYECKECGKAFSVSSSLTYHQKIHTGEKPFECNLCGKAFIRNIHLAHHHRIHTGEKPFKCNICEKAFVCRAHLTKHQNIHSGEKPYKCNECGKAFNQSTSFLQHQRIHTGEKPFECNECGKAFRVNSSLTEHQRIHTGEKPYKCNECGKAFRDNSSFARHRKIHTGEKPYRCGLCEKAFRDQSALAQHQRIHTGEKPYTCNICEKAFSDHSALTQHKRIHTREKPYKCKICEKAFIRSTHLTQHQRIHTGEKPYKCNKCGKAFNQTANLIQHQRHHIGEK
Protein: Apoptosis-inducing factor 1, mitochondrial (EC 1.6.99.-) (Ddaif) (Q9GRX6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Probable NADH oxidoreductase that acts as a caspase-independent mitochondrial effector of apoptotic cell death.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11598188}. Cytoplasm {ECO:0000269|PubMed:11598188}. Nucleus {ECO:0000269|PubMed:11598188}. Note=Translocates from mitochondria to the cytoplasm and secondary to the nucleus after the onset of cell death.
Interaction partners:
- Cytochrome c
- poly
- Small ribosomal subunit protein uS4m
- Cytochrome b5 heme-binding domain-containing protein
- Cytochrome b5 reductase
- Apoptosis-inducing factor homolog A
- 2Fe-2S ferredoxin-type domain-containing protein
- Apoptosis-inducing factor homolog B
- Mitochondrial import inner membrane translocase subunit tim16
Sequence:
MIRNLTKLTKFTIGNRFYQSSSKGRFSGKNGNNAFKSIVGVSVGVSALFAGCVFLDQEKEPESTPSIDVKEKKSQPPKTKEDYQKKMDEEYDIEQFKYVIIGGGTAAYHAIDKILENDKEATILLISKEYEVPYQRPPLTKSLWATKDDNVVNTLNFSDWSGKKQNLLYEQESAYGNEILQFIRTKKVIDLHIDEKLVLLNDGKLIRYDKCLIATGGEPRQLKFTSTNDKKISTYRTVEDFRKLYEVVKDGGKHVTVLGGGFLGSELTCAINSNFQDKNIKIDQIFPESGVLSTLFPDYLSKYATEEIIKSGVNVHTGTLIKDVVDNSENGRLTVTLNNGKTFETDHVVVAAGIIPNTNVVKSTTLEIDPINGGYVVNPELQARTDLYVAGDVASYYDFSLGVRRRVEHHDHARATGEMAGSNMSTKDTPAPYTYQPFFWSDLTPGVGFEAVGNTSSKLKTFSVWEKPSSDETKQSYTKGNIYYLNDNNNVVGVLCYGNYGKMDTARDLILKRRTIEDLNQLQHAIDFDEHH
Protein: chitin synthase (EC 2.4.1.16) (Q4W9P7)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- UDP-N-acetylglucosamine diphosphorylase
- Chitin synthase export chaperone
- alpha-1,3-glucan synthase
- alpha-1,3-glucan synthase
Sequence:
MSSNSSRMYPPAPNYEEEPPAYGNYGETTSFLADHDSSPRHQGVTMRLLPNSTDVDDDLSVDVERGASHHYGIEYSDDESTRANVQYVPYSGNANGGYNRFYGYNAEESPSRPASSLGNVPSIPPPAVSAVEVPQYSSRPASPLRPWSPARAADWTRPPAPPSVTGSQYERADLNGSPRPGTPSSRYGGSPRRPLPPAPLFAGPGAATGQDTSIDIGDGNDPEDPFGGGGRTNNRHEHRGSIRSFMSDSTMITDEKEEMAKINLNEDDVVDVDPNMHYGPAPEKQSRRGVREAQMSKKEVQLINGELILECKIPTILHSFLPRRDDREFTHMRYTAVTCDPDDFTQRGYKLRQQIGSTMRETELFICVTMYNEDETHFTRTMHGIMRNISHFCSRSKSRTWGKDGWKKIVVCIIADGRKKVHPRTLNALAAMGVYQEGIAKNIVNQKQVTAHVYEYTTQVSLDSDLKFKGAEKGIMPCQVIFCLKEHNQKKLNSHRWFFNAFGRALQPNICILLDVGTKPEPTALYHLWKAFDQDSNVAGAAGEIKAGKGKNMMGLLNPLVASQNFEYKMSNILDKPLESVFGYITVLPGALSAYRFFALQNDADGNGPLNQYFKGETLHGKDADVFTANMYLAEDRILCWELVAKREERWVLKFVKSAVGETDVPDTIPEFISQRRRWLNGAFFAAVYSLVNVKQLWKTDHSVPRKILLQIEAFYQFLNLLFTYFGLANFYLAFFFIAGSLSDERIDPFGHNMGKYIFFVLRYACILVMCLQFIISMGNRPQGAKKLYMSGIIVYSIIMVYTAFCALYLVVLELMAKAGVGKKELAVSDSLFINIVVSLLSTVGLYFYSSFLYLDPWHMFTSSAQYFALLPSYICTLQVYAFCNTHDVTWGTKGDNTINNDLGAARIINGTTVEVEMPSEQLDIDSGYDAALRNLRDRLEVPPPPVSENQQQEDYYRAVRTYMVSIWMVANVILAMSVSEIYGVDSGGTNVYLGIILWSVAVLALIRAVGSTTYAILLVVQKIVEGKTKFDAGNIVNSNAATSSYVSSRSTAQYGGGTSFKDKVTEAGWTLKRTAGKAMFWKK
Protein: Rho-associated protein kinase (EC 2.7.11.1) (Q90Y37)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Rho-related GTP-binding protein RhoA-B
- Rho-related GTP-binding protein RhoA-A
- Rho-related GTP-binding protein RhoA-D
- Rho-related GTP-binding protein RhoA-C
- LIM domain kinase 1a.
- LIM domain kinase 2
- LIM domain kinase 1
- Mitogen-activated protein kinase
- Myosin regulatory light chain 2a
- Myosin regulatory light chain 2b
Sequence:
MSLGAERRMENRLRQLEAMIKDPRSAINLESLLDSMNALVLDLDFPALRKNKNIENFLNRYEKVMNHIRELQMRPEDFDRVKVIGRGAFGEVQLVRHKASQKVYAMKVLSKFEMIKRSDSAFFWEERDIMAFADSPWVVQLCCAFQDDRSLYMVMEYMPGGDLVNLTSTYDVPEKWAKFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDRYGHLKLADFGTCMKMDGTGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFIYEMLVGDTPFYADSLVGTYSKIMDHKNSLNFPDDVEISQEGKNIICAFLTDREVRLGRSGVEEIKRHPFFRNDQWTFSTIRETAAPVVPELSSDIDTSNFDEIEEDKGEVETFPTPKAFVGNQLPFVGFTYFKENQLLNAVNSSAMKNDHPVSNREDNLALQKKLHCLEEQLNNEMQAKDELEQKYRSNSNRLEKITKELDEEMNSRKGLESTLRQLEREKALLQHKSVESHRRAESEADRKRCLENEVNSLRDQLDEMKKKNQNSHISNEKNIHLQKQLDEANALLRAESEVATRMRKTQTESSKQLQQLEAHVRELQDKCCMLENSKLTLERENISLQAALDTEKREQTQGSETISDLQARITGMEDEVRQMRQALSKAETEKRQLQEKLTDMEKEKSNNQIDMTYKLKMLQQGLEQEEAAHKATKARLADKNMISESIEGAKSEAVKELEQKLQEERSSKQRVENRVLELEKKNSMLDCDYKQSLQKLEELRRHKERLTEEVKNLNLKIEQEVQKRTLTQNDLKVQNQQLSTLRTSEKQLKQEINHILEIKRSLEKQNMELRKERQDSDGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKNKLYKDVQQNLQELQEERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHRQELAEKDTTISSLEEANRTLTSDVANLANEKEEFNNKLKEAEDYLQNLKNEEQSITQVKLALEKQLQSERTLKTQAVNKLAEIMNRKEVRGGGSRRGNDTDVRRKEKENRKLQLELRSEREKLNSTIIKYQREINDIQAQLLDESQVRIELQMALDSKDSDIEQLRSLLNSLNVQSLDSASMSSGPDMDTDESLLEIRLEGWLSLPVRNNTKRFGWERKYVVVSSKKILFYNSEQDKEHSNPYMVLDIDKLFHVRSVTQTDVYRADAKEIPRIFQILYANEGESKKEQELEPLPGDKSSYICHKGHEFIPTLYHFPTNCEACTKPLWNMFKPPPALECRRCHIKCHKDHMDKKEEVIAPCRVDMSTAKNLLLLASSQEDQQKWVSRLMKKIPKKPPAPDAPHRSSPRVPVKVQSSQSMRRPSRQIPAGKPS
Protein: Exonuclease, putative (Q580W0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTKNEGDGGLSQRKNKPRGRPQPFSHLLVCDFEATCDADSAGLYPHEIIEFPVVCIDTAQLAVVAEFHSYVHPVRRPKLTAFCKELTGITQSVVDDAPTLPEVIQKFGQWVREVVYPLCKMWKQQYPPSQLASNCLGDLGKKFKYDEKDNKEWVGCERMVCFATDGPWDMRKFMHECSVVRDGHIFPPLFYRWVDVRKCFKQHFNKWPRKLVDMLRTLRLDFEGKQHSGIDDSRNIARILIELMRRGFFVKRVSTIEYKCPMDVGGVILTQEMRELCDEENAKAKQRHLRE
Protein: Glutamate receptor ionotropic, NMDA 3B (GluN3B) (N-methyl-D-aspartate receptor subunit NR3B) (NMDAR3B) (NR3B) (NMDA receptor 4) (Nr4) (Q91ZU9)
Organism: Mus musculus (Mouse)
Function: NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14602821}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13224}. Postsynaptic cell membrane {ECO:0000269|PubMed:14602821}. Note=Requires the presence of GRIN1 to be targeted at the plasma membrane. {ECO:0000269|PubMed:14602821}.
Interaction partners:
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor ionotropic, NMDA 2B
- Glutamate receptor ionotropic, NMDA 2D
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 2C
- Glutamate receptor ionotropic, NMDA 3A
- Disks large homolog 4
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Proenkephalin-B
Sequence:
MECVQTLWLSLALALARGSWVVRGHPQPCGVPTRAGASVRLAALLPRAPAARARVLAALATPSPRLPHNLSLELVAVASPTRDPASLARGLCQVLAPPGVVASITFPEARPELRLLQFLAAATETPVLSVLRREVRAPLGAPTPFHLQLDWASPLETILDVLVSLVRAHAWEDIALVLCRVRDPSGLVTLWTSRASQAPKFVLDLSQLDSGNDSLRATLALLGTLEGGGTPVSAAVLLGCSTAHAHEVLEAAPPGPQWLLGTPLPAEALPKTGLPPGVLVLGETGQPSLEAAVHDMVELVARALSSMALMHPERALLPAAVNCEDLKTGGSESTARTLARFLSNTSFQGRTGAVWVAGSSQVHVSRHFKVWSLRRDPLGAPAWATVGSWQDGQLDFQPGAAALRVPSPSGTQARPKLRVVTLVEHPFVFTRESDEDGQCPAGQLCLDPGTNDSARLDALFTALENGSVPRTLRRCCYGYCIDLLERLAEDLAFDFELYIVGDGKYGALRDGRWTGLVGDLLAGRAHMAVTSFSINSARSQVVDFTSPFFSTSLGIMVRTRDTASPIGAFMWPLHWSMWVGVFAALHLTALFLTLYEWRSPYGLTPRGRNRGTVFSYSSALNLCYAILFGRTVSSKTPKCPTGRFLMNLWAIFCLLVLSSYTANLAAVMVGDKTFEELSGIHDPKLHHPSQGFRFGTVWESSAEAYIKASFPEMHAHMRRHSAPTTPHGVAMLTSDPPKLNAFIMDKSLLDYEVSIDADCKLLTVGKPFAIEGYGIGLPQNSPLTSNLSEFISRYKSSGFIDLLHDKWYKMVPCGKRVFAVTETLQMGVYHLSGLFVLLCLGLGSALLTSLGEHVFYRLVLPRIRRGNKLQYWLHTSQKIHRALNTGPPEGQQERAEQECSGPKEEQPAADGAGRWRRVRRAVVERERRVRFLLEPGEAGGDHPWLCSNGPGVQAELRELELRIEAARERLRSALLRRGELRAQLGDGTRLRPLRLLHAAPAES
Protein: Guard cell S-type anion channel SLAC1 (Protein CARBON DIOXIDE INSENSITIVE 3) (Protein OZONE-SENSITIVE 1) (Protein RADICAL-INDUCED CELL DEATH 3) (Protein SLOW ANION CHANNEL-ASSOCIATED 1) (Q9LD83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Slow, weak voltage-dependent S-type anion efflux channel involved in maintenance of anion homeostasis. Cl(-) efflux through SLAC1 causes membrane depolarization, which activates outward-rectifying K1 channels, leading to KCl and water efflux to reduce turgor further and cause stomatal closure, that reduces water loss and promotes leaf turgor. Essential for stomatal closure in response to CO(2), abscisic acid (ABA), ozone O(3), light/dark transitions, humidity change, calcium ions, hydrogen peroxide H(2)O(2), reactive oxygen species (ROS), and nitric oxide. Binds to the highly selective inward-rectifying potassium channels KAT1 and AKT2, and inhibits their activities. Functions as an essential negative regulator of inward potassium channels in guard cells. Essential for the efficient stomatal closure and opening in guard cells. Involved in the local and/or systemic stomatal responses (e.g. stomatal closure) to light stress.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18305482, ECO:0000269|PubMed:18305484, ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:19955427}; Multi-pass membrane protein {ECO:0000269|PubMed:18305482, ECO:0000269|PubMed:18305484, ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:19955427}.
Interaction partners:
- Serine/threonine-protein kinase SRK2E
- Calcium-dependent protein kinase 6
- Calcium-dependent protein kinase 21
- Calcium-dependent protein kinase 23
- LRR receptor-like serine/threonine-protein kinase GHR1
- Calcium-dependent protein kinase 3
- Aluminum-activated malate transporter 12
- Protein phosphatase 2C 37
- Potassium channel GORK channel)
- Protein phosphatase 2C 56
Sequence:
MERKQSNAHSTFADINEVEDEAEQELQQQENNNNKRFSGNRGPNRGKQRPFRGFSRQVSLETGFSVLNRESRERDDKKSLPRSGRSFGGFESGGIINGGDGRKTDFSMFRTKSTLSKQKSLLPSIIRERDIENSLRTEDGETKDDSINENVSAGRYFAALRGPELDEVKDNEDILLPKEEQWPFLLRFPIGCFGICLGLSSQAVLWLALAKSPATNFLHITPLINLVVWLFSLVVLVSVSFTYILKCIFYFEAVKREYFHPVRVNFFFAPWVVCMFLAISVPPMFSPNRKYLHPAIWCVFMGPYFFLELKIYGQWLSGGKRRLCKVANPSSHLSVVGNFVGAILASKVGWDEVAKFLWAVGFAHYLVVFVTLYQRLPTSEALPKELHPVYSMFIAAPSAASIAWNTIYGQFDGCSRTCFFIALFLYISLVARINFFTGFKFSVAWWSYTFPMTTASVATIKYAEAVPGYPSRALALTLSFISTAMVCVLFVSTLLHAFVWQTLFPNDLAIAITKRKLTREKKPFKRAYDLKRWTKQALAKKISAEKDFEAEEESHH
Protein: Spore coat protein SP96 (P14328)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Spore wall. Note=Outer layer of the coat matrix and interspore matrix.
Interaction partners:
- Spore coat protein SP60
- Spore coat protein SP85
- Spore coat protein SP70
Sequence:
MRVLLVLVACLTYFSGGALAQSCSSYSGDNCPSTCFQGSYDIPCGAQVKYCTEMKDNCGEGGDVKCWKDGSNLPVQTWSSCVPSELFGPNGKFKPSEIPNSSNCPTNCENGVEWVNLCGLSCDAKTACCPDVCQCKGGQTSGGSTTGSQTSGGSTSGGSTTGSQTSGGSTTGSQTSGSQTSGGSCSNTQCPNGFYCQVQGNNAVCVPQQSSTSGGHQNDPCDTVQCPYGYSCESRDGFEAKCTRDEDEPTHRPTHRPKPPHDSDKYLCDNVHCPRGYKCNAKNGVAKCIAGYEIPRVCRNIQCPTGYRCEDHNRNPICVLEERENPDNCLTCNDVNCEASGLVCVMTRARCKVGAAKCCDVQPTCIKPSTIAGSTIASIASTIASTGSTGATSPCSVAQCPTGYVCVAQNNVAVCLPRPTTTTGSTSDSSALGSTSESSASGSSAVSSSASGSSAASSSPSSSAASSSPSSSAASSSPSSSAASSSPSSSASSSSSPSSSASSSSAPSSSASSSSAPSSSASSSSASSSSASSAATTAATTIATTAATTTATTTATTATTTATTTATTTAATIATTTAATTTATTTATTATTTATTTATS
Protein: Kinetochore NuLl (O76406)
Organism: Caenorhabditis elegans
Interaction partners:
- Outer kinetochore KNL1 complex subunit knl-1
- KNL
- KNL
- Kinesin-like protein klp-19
- Spindly-like protein spdl-1
- Aurora/IPL1-related protein kinase 2
- Mitotic checkpoint serine/threonine-protein kinase bub-1
- Mitotic checkpoint protein bub-3
- BUB1 N-terminal domain-containing protein
- Kinetochore protein Nuf2 homolog
Sequence:
MSQKSNDTTFSVRAALFASPVGSSSAVPKKKVAREVPRAGPPVFALEHDVSEVTDRNKDGTFLAADACASGPTLKVPDETQGCPETFSVSEHEDDDDVEPMEVDGTIVPSPQRATPTRGVTPCEKSTTPRRRSSRKSMPTPGKRLFFTSKDTTNEDRKADDSTQLELLMAKIPQEMSGYMKKLATDIKEMSQYDAQLARNIDDMEAVFKSRETKLKSAIEIAKDSFISSALPLRLETLDMTLRKEESPNDIVARLHGSFLDKTQDAGNVNTAQKENQQLEDERGMLEEKLESLNKIKREKDEFLAKMRKEEEEALARREEIKQGFERIDALMSKIKPIPIFEF
Protein: Trehalose synthase/amylase TreS (EC 3.2.1.1) (EC 5.4.99.16) (Maltose alpha-D-glucosyltransferase) (MTase) (A0R6E0)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Maltose is the preferred substrate. To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose. TreS plays a key role in the utilization of trehalose for the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P). Might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro.
Interaction partners:
- Maltokinase
- Malto-oligosyltrehalose trehalohydrolase
- 1,4-alpha-glucan branching enzyme GlgB
- Trehalose 6-phosphate phosphatase
- Trehalase
- Glycogen debranching enzyme GlgX
- Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- Glycogen debranching enzyme GlgX
- glycogen phosphorylase
- 4-alpha-glucanotransferase
Sequence:
MEEHTQGSHVEAGIVEHPNAEDFGHARTLPTDTNWFKHAVFYEVLVRAFYDSNADGIGDLRGLTEKLDYIKWLGVDCLWLPPFYDSPLRDGGYDIRDFYKVLPEFGTVDDFVTLLDAAHRRGIRIITDLVMNHTSDQHEWFQESRHNPDGPYGDFYVWSDTSDRYPDARIIFVDTEESNWTFDPVRRQFYWHRFFSHQPDLNYDNPAVQEAMLDVLRFWLDLGIDGFRLDAVPYLFEREGTNCENLPETHAFLKRCRKAIDDEYPGRVLLAEANQWPADVVAYFGDPDTGGDECHMAFHFPLMPRIFMAVRRESRFPISEILAQTPPIPDTAQWGIFLRNHDELTLEMVTDEERDYMYAEYAKDPRMKANVGIRRRLAPLLENDRNQIELFTALLLSLPGSPVLYYGDEIGMGDIIWLGDRDSVRTPMQWTPDRNAGFSKATPGRLYLPPNQDAVYGYHSVNVEAQLDSSSSLLNWTRNMLAVRSRHDAFAVGTFRELGGSNPSVLAYIREVTRQQGDGGAKTDAVLCVNNLSRFPQPIELNLQQWAGYIPVEMTGYVEFPSIGQLPYLLTLPGHGFYWFQLREPDPEPGAQQ
Protein: Putative uncharacterized protein YLR235C (A0A023PXP4)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized protein YLR236C
- DNA topoisomerase 3
Sequence:
MLIGAPSNMRLRGALELLWRRLLHGLMQLRLVLKMHICSQLNHAIKRRAFLKTKGGKNALHGCLDTVINLQESILAGIRLVPVLPILLDYVLYNISLGGMTFADFLEVLLHFSALEGLCKGVFEADGLEAVH
Protein: Myosin-6 (Myosin heavy chain 6) (Myosin heavy chain, cardiac muscle alpha isoform) (MyHC-alpha) (P02563)
Organism: Rattus norvegicus (Rat)
Function: Muscle contraction.
Subcellular location: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Myosin light chain 3
- Actin, alpha cardiac muscle 1
- Myosin-binding protein C, cardiac-type
- Myosin light chain 4
- Troponin I, cardiac muscle
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Troponin T, cardiac muscle
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin-7
- Tropomyosin alpha-1 chain
Sequence:
MTDAQMADFGAARYLRKSEKERLEAQTRPFDIRTECFVPDDKEEYVKAKIVSREGGKVTAETENGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRSKKDNPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSGKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQARGQLMRIEFKKMVERRDALLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLTRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSHMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALIWQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNAQAHLKDTQLQLDDAVRANDDLKENIAIVERRNTLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLVRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKQKMHDEE