wanglab/gogpt-training-data huggingface dataset:
Protein: Kin of irre, isoform A (Kin of irre, isoform B) (Kin of irre, isoform C) (Kin of irre, isoform D) (Kin of irre, isoform E) (Kin of irre, isoform F) (Kin of irre, isoform G) (Q9W4T9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Sticks and stones, isoform B
- Hibris, isoform B
- Rolling pebbles, isoform B
- Dreadlocks, isoform B
- FI21420p1
- Verprolin 1, isoform G
- LD47926p
- Tyrosine-protein kinase Src64B
Sequence:
MKRMRSSRLLVLPLILVLILTLLLQPIAVHAKSKKNKSSQSSHHGDSSSSSSSSSSSSGSSSAAASSANDESKPKGGDNGGQHFAMEPQDQTAVVGSRVTLPCRVMEKVGALQWTKDDFGLGQHRNLSGFERYSMVGSDEEGDFSLDIYPLMLDDDAKYQCQVGPGPQGEQGIRSRFAKLTVLVPPEAPKITQGDYLVTTEDREIELECVSQGGKPAAEITWIDGLGNVLTKGIEYVKEPLADSRRITARSILKLAPKKEHHNTTFTCQAQNTADRTYRSAKLLLEVKYAPKVIVSVVGGALAGGKIPEGAEVILSCQADANPHELSYRWFINDELMTGDFTTKMIIHNVSRQYHDAIVKCEVVNAVGKSEQSKKLDISFGPVFRQRPVSVEADLGATVSMRCDVAGNPEPEIEWISENSDQVVGVAAELKLKVSSETAGRYFCKAVVNGFPEIGAEATLYVKRAPIITSHKVQFGGVGGRVKIDCLAFSIPKAEHILWSFEGKIINMSSADPDIYIFEEHHLPEGVRAALIIRDSKATHFGKYNCTVMNSYGGDSLVITLLREPGNIPVLLVVMGSMFCVAIILMIVMIIIVYRKRRSRKKPMPADVIPEASRGGDKLNELKSELRSKAYDVEYSEAGGDGLAINLTQSPMPDVQMKGATLGVPLAGPVKFDERFSGDFGGDRYNRQCHIKNLKNQQETAYKGSPQANGYAHYFEYALDYSPPGGEGAAVVVGSGGVGKLKNGGMNSATLPHSAAATVNGGGAGNGGGASLPRNQRHEIQQSQQSNGFLGQPLLQNGIDSRFSAIYGNPYLRTNSSLLPPLPPPSTANPAATPAPPPYHAARHGHAHHANGGLKHFVGGAVITTSPVGNVNINGGGGGGSTPSGGGGVGVGVAAGGSVSGSSSNLTASSNTLAATPLAGGGVGNSGQCAQSPSGQFILSNNGKGHTQKGPLATHV
Protein: Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial (CybS) (Succinate-ubiquinone reductase membrane anchor subunit) (Q9P7X0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome B subunit
- Probable succinate dehydrogenase flavoprotein subunit, mitochondrial
- Mitochondrial import inner membrane translocase subunit tim22
- Fumarate hydratase, mitochondrial
- WW domain-containing protein C2F3.14c
- Succinate--CoA ligase subunit alpha, mitochondrial
- Mitochondrial import inner membrane translocase subunit tim54
- Succinate--CoA ligase subunit beta, mitochondrial
- Mitochondrial import inner membrane translocase subunit tim9
Sequence:
MLQTRLGLGALRQGRLLFAVKSFSTTSVAKIFPPPPQTIKGTVNDAAVFPHHSKLHGSYHWDFERIIAIAMVPQVMIPLFTGTSHPLMDAALACTLITHAHLGFESCVIDYFPARRFKKLSPLMHWILRGCTVLTLIGVYEFNTNDIGLTEGIKKLWKS
Protein: Mitochondrial oxaloacetate transport protein (Mitochondrial carrier protein PMT) (P32332)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transports oxaloacetate and sulfate.
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dolichyl-phosphate-mannose--protein mannosyltransferase 4
- 3-isopropylmalate dehydratase
- Dolichyl-phosphate-mannose--protein mannosyltransferase 2
- Acyl carrier protein, mitochondrial
- Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Dolichyl-phosphate-mannose--protein mannosyltransferase 6
- Malate dehydrogenase, mitochondrial
- Dolichyl-phosphate-mannose--protein mannosyltransferase 5
Sequence:
MSSDNSKQDKQIEKTAAQKISKFGSFVAGGLAACIAVTVTNPIELIKIRMQLQGEMSASAAKVYKNPIQGMAVIFKNEGIKGLQKGLNAAYIYQIGLNGSRLGFYEPIRSSLNQLFFPDQEPHKVQSVGVNVFSGAASGIIGAVIGSPLFLVKTRLQSYSEFIKIGEQTHYTGVWNGLVTIFKTEGVKGLFRGIDAAILRTGAGSSVQLPIYNTAKNILVKNDLMKDGPALHLTASTISGLGVAVVMNPWDVILTRIYNQKGDLYKGPIDCLVKTVRIEGVTALYKGFAAQVFRIAPHTIMCLTFMEQTMKLVYSIESRVLGHN
Protein: Laccase 2B (Q49I40)
Organism: Tribolium castaneum (Red flour beetle)
Interaction partners:
Sequence:
MDGTQRYLLIATAALFLFFDLCHGVRAPGAKKKVGPIDQSAAAASWHDFDNSDFFQSEHAVIQTHPSIGGGPRFSSGGGRKAWKHLDFRNSATAELLKNPSLSSPDECARACREGEPPRICYYHFTLELYTVLGAACQVCTPNATNTVWSHCQCVLADGVERGILTANRMIPGPSIQVCEGGKVVIDVENHIEGNEVTLHWHGVWQRGSQYYDGVPFVTQCPIQQGNTFRYQWIAGNAGTHFWHAHTGLQKMDGLYGSVVIRQPPAKDPNSHLYDYDLTTHVMLLSDWMHEDATERFPGRLAVNTGQDPESLLINGKGQFRDPNTGFMTNTPLEVFTITPGRRYRFRMINSFASVCPAQLTIQGHDLTLIATDGEPVHPVRVNTIISFSGERYDFVINADQTPGAYWIQLRGLGECGIRRVQQLGILRYAKGPYQPSQAPPTYDYGIPQGVVLNPLDAICNKPRKDAVCVSQLRNAKKVDEAILEERPDVKIFLPFRFLFYKPEDIFRPNTYNRFLAATGGDHVISLIDEISFTFPPSPPLSQIHDLSPDQFCNGDNRPPDCGQNCMCTHQVDIPLNAIVEVVLVDEVQSPNLSHPFHLHGYAFNVVGIGRSPDQNVKKINLKHALDLDRRGLLHRQFNLPPSKDTIAVPNNGYVIFRFRADNPGYWLFHCHFLFHIVIGMNLIIHVGTQADLPPVPHNFPRCGNHLPPISLH
Protein: Respiratory nitrate reductase 1 alpha chain (EC 1.7.5.1) (Nitrate reductase A subunit alpha) (Quinol-nitrate oxidoreductase subunit alpha) (P09152)
Organism: Escherichia coli (strain K12)
Function: The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.
Subcellular location: Cell membrane; Peripheral membrane protein.
Interaction partners:
- Respiratory nitrate reductase 1 beta chain
- Respiratory nitrate reductase 2 beta chain
- Nitrate reductase molybdenum cofactor assembly chaperone NarJ
- Nitrate/nitrite antiporter NarK
- Respiratory nitrate reductase 1 gamma chain
- Probable nitrate reductase molybdenum cofactor assembly chaperone NarW
- Respiratory nitrate reductase 2 gamma chain
- Nitrite reductase large subunit
- Nitrate/nitrite transporter NarU
- Periplasmic nitrate reductase
Sequence:
MSKFLDRFRYFKQKGETFADGHGQLLNTNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRLMKMWREAKALHSDPVEAWASIIEDADKAKSFKQARGRGGFVRSSWQEVNELIAASNVYTIKNYGPDRVAGFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDNPSQYFTDYVRRYTDMPMLVMLEERDGYYAAGRMLRAADLVDALGQENNPEWKTVAFNTNGEMVAPNGSIGFRWGEKGKWNLEQRDGKTGEETELQLSLLGSQDEIAEVGFPYFGGDGTEHFNKVELENVLLHKLPVKRLQLADGSTALVTTVYDLTLANYGLERGLNDVNCATSYDDVKAYTPAWAEQITGVSRSQIIRIAREFADNADKTHGRSMIIVGAGLNHWYHLDMNYRGLINMLIFCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPARHMNSTSYFYNHSSQWRYETVTAEELLSPMADKSRYTGHLIDFNVRAERMGWLPSAPQLGTNPLTIAGEAEKAGMNPVDYTVKSLKEGSIRFAAEQPENGKNHPRNLFIWRSNLLGSSGKGHEFMLKYLLGTEHGIQGKDLGQQGGVKPEEVDWQDNGLEGKLDLVVTLDFRLSSTCLYSDIILPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKKFSEVCVGHLGKETDIVTLPIQHDSAAELAQPLDVKDWKKGECDLIPGKTAPHIMVVERDYPATYERFTSIGPLMEKIGNGGKGIAWNTQSEMDLLRKLNYTKAEGPAKGQPMLNTAIDAAEMILTLAPETNGQVAVKAWAALSEFTGRDHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHELIPWRTLSGRQQLYQDHQWMRDFGESLLVYRPPIDTRSVKEVIGQKSNGNQEKALNFLTPHQKWGIHSTYSDNLLMLTLGRGGPVVWLSEADAKDLGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMMYHAQERIVNLPGSEITQQRGGIHNSVTRITPKPTHMIGGYAHLAYGFNYYGTVGSNRDEFVVVRKMKNIDWLDGEGNDQVQESVK
Protein: Large ribosomal subunit protein P1 (60S acidic ribosomal protein P1) (P05386)
Organism: Homo sapiens (Human)
Function: Plays an important role in the elongation step of protein synthesis.
Interaction partners:
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein eL15
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein eL34
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS9
Sequence:
MASVSELACIYSALILHDDEVTVTEDKINALIKAAGVNVEPFWPGLFAKALANVNIGSLICNVGAGGPAPAAGAAPAGGPAPSTAAAPAEEKKVEAKKEESEESDDDMGFGLFD
Protein: Voltage-dependent L-type calcium channel subunit beta-4 (CAB4) (Calcium channel voltage-dependent subunit beta 4) (O00305)
Organism: Homo sapiens (Human)
Function: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.
Interaction partners:
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent L-type calcium channel subunit alpha-1F
- Voltage-dependent L-type calcium channel subunit beta-3
- Voltage-dependent calcium channel subunit alpha-2/delta-4
- Voltage-dependent calcium channel subunit alpha-2/delta-2
- Voltage-dependent calcium channel gamma-3 subunit
Sequence:
MSSSSYAKNGTADGPHSPTSQVARGTTTRRSRLKRSDGSTTSTSFILRQGSADSYTSRPSDSDVSLEEDREAIRQEREQQAAIQLERAKSKPVAFAVKTNVSYCGALDEDVPVPSTAISFDAKDFLHIKEKYNNDWWIGRLVKEGCEIGFIPSPLRLENIRIQQEQKRGRFHGGKSSGNSSSSLGEMVSGTFRATPTSTAKQKQKVTEHIPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKRAIIERSNTRSSLAEVQSEIERIFELARSLQLVVLDADTINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADKLAQCPPEMFDVILDENQLEDACEHLGEYLEAYWRATHTTSSTPMTPLLGRNLGSTALSPYPTAISGLQSQRMRHSNHSTENSPIERRSLMTSDENYHNERARKSRNRLSSSSQHSRDHYPLVEEDYPDSYQDTYKPHRNRGSPGGYSHDSRHRL
Protein: ATP-dependent RNA helicase (EC 3.6.4.13) (Q57Z22)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ESF1 RRM domain-containing protein
- U3 small nucleolar RNA-associated protein 14
- RRM domain-containing protein
- MI domain-containing protein
- Sas10 C-terminal domain-containing protein
- Nrap protein domain-containing protein
- U3 small nucleolar RNA-associated protein 18
- rRNA biogenesis protein, putative
- Nop14-like protein
- NUC153 domain-containing protein
Sequence:
MDERQMEDKRTARKRRWAERQERSRLNRSEGEALRKQRQELRAALDAVDEGKQELAEQISYTRFDQLPLSQRTQLGLERGGYKLLTPIQSDALHLALAGYDVLGAARTGSGKTLCFIVPLLELLYVEQWEAEMGIGALVLSPTRELALQIFKVLQLVGYKHVMSAALLTGGRDVNEERKRVSAISIIVGTPGRVLHHLEDDDSLVTDNLQMLVMDEADRLLDMGFREVLSGILKQLPTQRQTLMFSATQTTDVQMLGQMSLRNQRYVSAHAECAAPTPSTLCQNFVVVELHRKLDVLLLFLKRHPNDKFVVFVSTCNQVRYMYLAFAKILKKMHLPCMCLTSKMKQFRREEVFLTFCRCKNAVLFCTDVAARGLDFPLIHWSVQFDCPDSAQTYIHRAGRTARAGARGVSLLFLTPREVPMLSFLAHKHIPLREIAVRPQMLRESKEIFVALVVQGLKYEAQKAFIAYLRSVYFAANKLVFDVKSIDVAPFAHSLGLMKVPDMSELGNLQRGAKNLPWDVVNFMAKRDAKEVADAKSRRERHLTASDMFRTLQQKQRYATTDSTDVDLAADANINGEDEEKNDPFLVKKPHEKGNEDHLDEGMQLTFTERMAGLSKRKVRKYIESADLRVRDLGLSKRVVYDEDDDAEEDEINMRVANEGQDISINVEGGSGSDNDLGDVPEKFAERLRQRVTQDSAADNERAKKLRRLRRLQRSGKISRKTALEDISAPKGTTDAVDSDDHTDDNSPQQSSNDYDDGDISVHSSDSFTRLIKAAKGELFSDNEDEDISSSDNGNFETEKKKKKKIKKKKEEKRLKKIKNNPTPQKSK
Protein: Exportin-1 (Chromosome region maintenance 1 protein) (Protein embargoed) (Q9TVM2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor for the leucine-rich nuclear export signal (NES). Binds cooperatively to the NES on its target protein and to the small GTPase Ran in its active GTP-bound form. Involved in the export of dl, RpS2 and the pre-40S ribosome from the nucleus to the cytoplasm. Plays an important role in nuclear pore assembly by mediating nucleoporin condensation and biogenesis of annulate lamellae. Required for the function or maintenance of certain tissues such as brain and gut.
Subcellular location: Nucleus {ECO:0000269|PubMed:17032737}. Nucleus membrane {ECO:0000269|PubMed:17032737}; Peripheral membrane protein; Nucleoplasmic side. Note=Localization to the nuclear pore complex is promoted by Nup214. {ECO:0000269|PubMed:17032737}.
Interaction partners:
- Nuclear pore complex protein Nup214
- GTP-binding nuclear protein Ran
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup88
- GTP-binding nuclear protein Ran-like
- Ran GTPase-activating protein
- 60S ribosomal export protein NMD3
- Snurportin-1
- Phosphorylated adapter RNA export protein
- Nuclear pore complex protein Nup98-Nup96
Sequence:
MATMLTSDEAGKLLDFSQKLDINLLDKIVEVVYTAQGEQLRLAQSILTTLKEHPEAWTRVDSILEYSQNQRTKFYALQILEEVIKTRWKVLPRNQCEGIKKYVVSLIIKTSSDPIVMEQNKVYLNKLNMILVHILKREWPRNWETFISDIVGASKTNESLCMNNMVILKNLSEEVFDFSQGQITQTKAKHLKDTMCSEFSQIFTLCSFVLENSMNAALIHVTLETLLRFLNWIPLGYIFETQQIETLIFKFLSVPMFRNVTLKCLSEIAGLTAANYDENFATLFKDTMVQLEQIVGQNMNMNHVFKHGSDTEQELVLNLAMFLCTFLKEHGKLVEDAKYVDYLNQALMYLVMISEVEDVEVFKICLEYWNSLVEDLYNSEFFHPTLESTKRQQVYPRRRFYAPILSKVRFIMISRMAKPEEVLVVENENGEVVREFMKDTNSINLYKNMRETLVFLTHLDSVDTDRIMTLKLLNQVNGSEFSWKNLNTLCWAIGSISGAFCEEDEKRFLVTVIKDLLGLCEQKKGKDNKAIIASNIMYVVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAIKCRRYFVTIQPNEACTFIDEILTTMSSIICDLQPQQVHTFYEAVGYMISAQVDQVQQDVLIERYMQLPNQVWDDIISRASKNVDFLKNMTAVKQLGSILKTNVAACKALGHAYVIQLGRIYLDMLNVYKITSENIIQAIEVNGVNVNNQPLIKTMHVVKKETLNLISEWVSRSNDNQLVMDNFIPPLLDAILLDYQRCKVPSAREPKVLSAMAIIVHKLRQHITNEVPKIFDAVFECTLDMINKNFEDFPQHRLSFYELLQAVNAHCFKAFLNIPPAQFKLVFDSVVWAFKHTMRNVADMGLNILFKMLQNLDQHPGAAQSFYQTYFTDILMQIFSVVTDTSHTAGLPNHAIILAYMFSLVENRKITVNLGPIPDNMIFIQEYVASLLKSAFTHLSDNQVKVFVTGLFNLDENVQAFKEHLRDFLIQIREATGEDDSDLYLEEREAALAEEQSNKHQMQRNIPGMLNPHELPEDMQDE
Protein: Levy, isoform A (Levy, isoform B) (RH03295p) (Q9W1N3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
- Cytochrome c oxidase subunit
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 4
- Cyclope, isoform A
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 5B, isoform A
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b-c1 complex subunit 9
- Cytochrome b-c1 complex subunit 7
- AT02348p
Sequence:
MSAILNHAIRRQFGASAARNMSGTAAVAGEHSGGYKVWKRLSFFVAVPAVGLCMLNAYLKHQEEHDKPRQEFVKYDYLRRREKRFPWGEGQKSLFHNPHVNALPDGYEH
Protein: 65 kDa invariant surface glycoprotein (Q587F2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMKYLLVFAIIATRIPVLLATNGGDKHVKANKKLTKEGAAALCKMKHLADKVAEERSQELKDRTQNFAGYIEFELYRIDYWLEKLNGPKGRKDGYAKLSDSDIEKVKEIFNKAKDGIAKQLPEAKKAGEEAEKLHTEVKKAAKNARGVRLSEGTNSSGLYRILDWYCFKEGENAGKSDNCDGVKFSVHYETHRRRNVIDCSSTGYEENYDWSANALQVALNSWENVKPKKVESAGSDMNCNIGQSSESHPCTMTEEWQTPYKETVEKLRELEDAYQRGKKAHDAMLGYANTAYAVNTKVEQEKPLTEVIAAAKEAGKKGAKIIIPAAAPATPTNSTKNEDSASTEHVDRGIATNETQVEVGIDADFDSLLDATEAAEVTRRHQRTAMIILAVLVPAIILVVTAVAFFIMVKRRRNSSKDVDTGKAEGGVSSVKVVM
Protein: TOM1-like protein 1 (Src-activating and signaling molecule protein) (Target of Myb-like protein 1) (Q923U0)
Organism: Mus musculus (Mouse)
Function: Probable adapter protein involved in signaling pathways. Interacts with the SH2 and SH3 domains of various signaling proteins when it is phosphorylated. May promote FYN activation, possibly by disrupting intramolecular SH3-dependent interactions.
Subcellular location: Golgi apparatus, Golgi stack. Endosome membrane {ECO:0000305}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=A small proportion is membrane-associated. {ECO:0000250}.
Interaction partners:
Sequence:
MAFGKSHRDPYATSVGHLIEKATFAGVLTEDWGQFLHICDIINTTQDGPKDAVKALKKRISKNYNHKEIQLSLSLIDMCVQNCGPSFQSLIVKKEFIKDTLVKLLNPRYTLPLETQNRILNFIKTWSQGFPGGVDVSEVKEVYLDLLKKGVQFPPSDGEPETRQEAGQISPNRPTSVPTAPALSSIIAPKNPTISLVPEQIGKLHSELDMVKMNVKVMTAILMENTPGSENHEDIELLRKLYKTGREMQERIMDLLVVVENEDVTMELIQVNEDLNNAVLGYERFTRNQQRLLEQKRNRTEATRTSSEPSAPSCDLLDLSPIVPVPTPNEGALNSVNAQLSGLSVSSLSPVITNNLYPSLQPQRDLLASEDIEIPTLFPQRTSQNLASSHTYDNFHSNSVLLQPVSLHTATAAAAANQRLPPLPSSHPVLKDGDLQPPNYYEVMEFDPLAPTTEAVYEEIDGYHQKEAQSHSDC
Protein: Small ribosomal subunit protein mS26 (28S ribosomal protein S26, mitochondrial) (H6UQ76)
Organism: Gallus gallus (Chicken)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MAPGGCLLLALLLLAGTAQGQHWSHGWYPGGKRDLSAPQAIPAWSPWLVPSRGRKSRYDPPAKAKASRLKVPPPVDPAELYVVTERYRQHRLVLSALRSIFRSEVVQRKREAQRDAEDSAALSEEHRLLMAWNDAENARQRARR
Protein: Cyclotide hyen-L (C0HLP6)
Organism: Pigea enneasperma (Spade flower) (Afrohybanthus enneaspermus)
Function: Probably participates in a plant defense mechanism (By similarity). Has cytotoxic activity against HUVEC cells (LC(50)= 2.26 uM) and various cancer cells including HeLa (LC(50)= 3.48 uM), MCF-7 and K562. Displays very weak hemolytic activity. Binds to and induces leakage in phospholipd membranes, particularly ones containing 1-palmitoyl-2-oleophosphatidylethanolamine (POPE).
Interaction partners:
Sequence:
GIPCAESCVYIPCTVTALLGCSCSDKVCYN
Protein: Homoserine/homoserine lactone efflux protein (P0AG34)
Organism: Escherichia coli (strain K12)
Function: Conducts the efflux of homoserine and homoserine lactone.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Threonine efflux protein
- Threonine/homoserine exporter RhtA
Sequence:
MTLEWWFAYLLTSIILSLSPGSGAINTMTTSLNHGYRGAVASIAGLQTGLAIHIVLVGVGLGTLFSRSVIAFEVLKWAGAAYLIWLGIQQWRAAGAIDLKSLASTQSRRHLFQRAVFVNLTNPKSIVFLAALFPQFIMPQQPQLMQYIVLGVTTIVVDIIVMIGYATLAQRIALWIKGPKQMKALNKIFGSLFMLVGALLASARHA
Protein: Uncharacterized protein (Q57XZ1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
METVPESLNVIDPFGVLDTPLEARTYMTGRQYIQLTYHLGEKLGIKNVDHYFNLPVGSEGSETEGTAVEAEISPNDDISCLLDQLVQNESNSDDVSQSNVTSSFLCNPPLCVHFVREGAMKAIGNPKSLPTVACKAVGEKLQGPPHVHCLFCLQTGDTGADTDTNSQGQPYVQAADLRHCVQGHFTEHMNRRNAYLNFLEEGAATLPEARQELLECSADREGRHTCFIASAGSAACPVVVSYCAACDQMAPLATFLEEEDECTSCETVEQRPNRSGTRSVETVELILARLLLACELRVMLTKERGAEGSGNISLVQEESYIFIATPFLFGEEEEELSEEFETGADLTHSSVILPAATVVETAKGPCLCLLKEEGEELLQLLTELPPYRINHAVVGFVMQWQSASAADERITWALDQGKRKGYKFGVQRRLVYVEDTDEWVIAHVLHNPEVSPSHGRSAVDSERSFGDVRTRELCTITKMIPLSLMEQFIRGGRGEDDGAKNKCEDRSISTDVEVEDCPYGMEARTINYFAQMTALAKAMSLATSFM
Protein: Beta-galactosidase 5 (Lactase 5) (EC 3.2.1.23) (Q9MAJ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- ARM repeat superfamily protein
- Probable methyltransferase PMT4
- Thioredoxin H1
Sequence:
MGTTILVLSKILTFLLTTMLIGSSVIQCSSVTYDKKAIVINGHRRILLSGSIHYPRSTPEMWEDLIKKAKDGGLDVIDTYVFWNGHEPSPGTYNFEGRYDLVRFIKTIQEVGLYVHLRIGPYVCAEWNFGGFPVWLKYVDGISFRTDNGPFKSAMQGFTEKIVQMMKEHRFFASQGGPIILSQIENEFEPDLKGLGPAGHSYVNWAAKMAVGLNTGVPWVMCKEDDAPDPIINTCNGFYCDYFTPNKPYKPTMWTEAWSGWFTEFGGTVPKRPVEDLAFGVARFIQKGGSYINYYMYHGGTNFGRTAGGPFITTSYDYDAPIDEYGLVQEPKYSHLKQLHQAIKQCEAALVSSDPHVTKLGNYEEAHVFTAGKGSCVAFLTNYHMNAPAKVVFNNRHYTLPAWSISILPDCRNVVFNTATVAAKTSHVQMVPSGSILYSVARYDEDIATYGNRGTITARGLLEQVNVTRDTTDYLWYTTSVDIKASESFLRGGKWPTLTVDSAGHAVHVFVNGHFYGSAFGTRENRKFSFSSQVNLRGGANKIALLSVAVGLPNVGPHFETWATGIVGSVVLHGLDEGNKDLSWQKWTYQAGLRGESMNLVSPTEDSSVDWIKGSLAKQNKQPLTWYKAYFDAPRGNEPLALDLKSMGKGQAWINGQSIGRYWMAFAKGDCGSCNYAGTYRQNKCQSGCGEPTQRWYHVPRSWLKPKGNLLVLFEELGGDISKVSVVKRSVN
Protein: Ubiquitin carboxyl-terminal hydrolase 44 (EC 3.4.19.12) (Deubiquitinating enzyme 44) (Ubiquitin thioesterase 44) (Ubiquitin-specific-processing protease 44) (Q9H0E7)
Organism: Homo sapiens (Human)
Function: Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Promotes also the deubiquitination of histone H2A and H2B. Recruited to RNF8/RNF168-ubiquitinated chromatin surrounding double stranded breaks (DSBs), promotes hydrolysis of such ubiquitin conjugates, thus negatively regulating protein recruitment to damaged chromatin. Participates in nucleotide excision repair (NER) pathway by deubiquitinating DDB2 to prevent its premature degradation so it can remain on damaged chromatin (By similarity). Promotes FOXP3 stabilization through 'Lys-48'-linked deubiquitination leading to increased stability and increased regulatory T-cell lineage stability. Plays also a positive role in innate immune response to DNA viruses by deubiquitinating STING1, selectively removing its 'Lys-48'-linked polyubiquitin chains and stabilizing it.
Subcellular location: Nucleus {ECO:0000269|PubMed:20402667, ECO:0000269|PubMed:23615962, ECO:0000269|PubMed:31968013, ECO:0000269|PubMed:32644293}. Cytoplasm {ECO:0000269|PubMed:31968013}. Note=Peaks in interphase, with relatively low levels maintained throughout mitosis. {ECO:0000250}.
Interaction partners:
- Cell division cycle protein 20 homolog
- Centrin-2
- F-box-like/WD repeat-containing protein TBL1XR1
- Zinc finger protein 501
- Zinc finger protein 569
- Zinc finger protein 436
- Zinc finger protein 629
- Zinc finger protein 763
- Zinc finger protein 44
- Nuclear receptor corepressor 1
Sequence:
MLAMDTCKHVGQLQLAQDHSSLNPQKWHCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDNTTGDLKLLRRTLSAIKSQNYHCTTRSGRFLRSMGTGDDSYFLHDGAQSLLQSEDQLYTALWHRRRILMGKIFRTWFEQSPIGRKKQEEPFQEKIVVKREVKKRRQELEYQVKAELESMPPRKSLRLQGLAQSTIIEIVSVQVPAQTPASPAKDKVLSTSENEISQKVSDSSVKRRPIVTPGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAMTASEKTRSCKHPPVTDTVVYQMNECQEKDTGFVCSRQSSLSSGLSGGASKGRKMELIQPKEPTSQYISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTSLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCSGKDIASQPCLVTEMLAKFTETEALEGKIYVCDQCNSKRRRFSSKPVVLTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVGFEEILNMEPYCCRETLKSLRPECFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYTQRVTENGHSKLLPPELLLGSQHPNEDADTSSNEILS
Protein: RNA demethylase ALKBH5 (EC 1.14.11.53) (Alkylated DNA repair protein alkB homolog 5) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5) (Q08BA6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro) (By similarity). Requires molecular oxygen, alpha-ketoglutarate and iron.
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:Q6P6C2}.
Interaction partners:
- N
- FTO alpha-ketoglutarate-dependent dioxygenase.
- Pre-mRNA-splicing regulator WTAP
- YTH domain-containing family protein 2
- YTH domain-containing family protein
- YTH domain containing 2.
- YTH domain-containing 1.
- YTH N
- RNA-binding protein 15
- Probable ATP-dependent RNA helicase DDX46
Sequence:
MAGFTDLREKLKSMTPHRDKVFEYSNGEKRKYRESDDDESEYEERRDAEARRVKSGIKQASIFTLEECARIEAKIDEVVAKADKGLYREHTVDRAPLRNKYFFGEGYTYGAQLEKRGPGQERLYSKGEVDDIPDWVHELVIDRLVTHGVIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFLFKPIRVSEPVLHLPVRRGSVTVLSGYAADDITHCIRPQDIKERRAVIILRKTRADAPRLDSNSLSPSIVSPKRRHILKAKRSHRKADPDAAHRPRVLEMDKELQRRSLSSRQRRHDDGSSENSWRRADDREPAARYTHDHAPTRRVKMRRH
Protein: Aldo-keto reductase, putative (Q585V3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Hydroxyacylglutathione hydrolase, putative
- Glutamate--cysteine ligase
- hydroxyacylglutathione hydrolase
Sequence:
MPGVNVMSYKPLGGPVLGVTRMLQMRNGYTIPQCGFGTYRMTPTEAGAAVEYAVQAGFRHFDCAKAYCNQFAVGDGLRRAISSGRVKRDDLFVTSKLWPTDQHPENVEKACRETLEELKVSYLDLYLIHWPVAWRHSPEFKTEEDKYPKHDSGLPAVDERVKLTDTWRAMCALVDKGLVRSIGLSNCSEKHIAEVMGDGDLYAPVLNQIELHPALVQRDLLNVHRTKRMLTASYSPLGMPSRFTSPDYKGLLTHEALLPLSEHSGFSVARLLLNWNLDMHNVVIVRSTRRDHIQSNAKASLYTLSDPVRMILDRFQDREGTVRTINPTNFTHSGESFFS