wanglab/gogpt-training-data huggingface dataset:
Protein: Calmodulin-like protein 3 (Q9SRR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Potential calcium sensor.
Interaction partners:
- At1g01310 superfamily protein)
- Glyoxysomal processing protease, glyoxysomal
- CAP superfamily protein
- CAP superfamily protein
- Sm-like protein LSM3A
- Small ribosomal subunit protein uS19y
Sequence:
MDQAELARIFQMFDRNGDGKITKQELNDSLENLGIYIPDKDLVQMIEKIDLNGDGYVDIEEFGGLYQTIMEERDEEEDMREAFNVFDQNRDGFITVEELRSVLASLGLKQGRTLEDCKRMISKVDVDGDGMVNFKEFKQMMKGGGFAALGSNL
Protein: Protoporphyrinogen oxidase (PPO) (EC 1.3.3.4) (P40012)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:7798202}. Note=Bound to the mitochondrial inner membrane with its active site facing the cytosolic side. {ECO:0000269|PubMed:7798202}.
Interaction partners:
- Ferrochelatase, mitochondrial
- Uroporphyrinogen decarboxylase
- Oxygen-dependent coproporphyrinogen-III oxidase
- Porphobilinogen deaminase
- Uroporphyrinogen-III synthase
- Delta-aminolevulinic acid dehydratase
- 5-aminolevulinate synthase, mitochondrial
- Bifunctional protein GAL10
- Mitochondrial glycine transporter
Sequence:
MLLPLTKLKPRAKVAVVGGGVSGLCFTYFLSKLRPDVEITLFESQNRTGGWIYSCNTRDMSGNPIMLEKGPRTLRGVSDGTVLIMDTLKDLGKEAVIQSIDKGCIADKKFLLDPSDKLVQVPNSISTTVKFLLNPLGKGLITGMMGEWFRKKSPHPGQDESVESICDRRFGNNYISNNMISALLRGIYGDDVSLLSAKRTFKKIYYNELKHGSNTQAMIDNMRGKSRSKKTENLHQSLTGCLNDYSNAFGKDRSKLLDLSNTLKKYPMLGLAGGLETFPKIVRNALNEFKNVKIVTGNPVTQIMKRPANETTIGLKAKSGDQYETFDHLRLTITPPKIAKLLPKDQNSLSKLLDEIQSNTIILVNYYLPNKDVIDADLQGFGYLVPKSNKNPGKLLGVIFDSVIERNFKPLFDKLSTNPNALNKYTKVTAMIGGCMLNEHGVPVVPSREVTINAVKDALNNHLGISNKDLEAGQWEFTIADRCLPRFHVGYDAWQERAERKLQESYGQTVSVGGMGFSRSPGVPDVIVDGFNDALQLSK
Protein: LD12501p (Q95RT1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNPHQKPAQLYTQLAKLPLTVLNASPGFINLCDALNGWQLVRELKKALQLPAATSFKHVSPAGAAVGVPLNPAQAKLCMVDDLYEQLTPLATAYARARGADRMSSFGDFVALSDVCDVVTARIISREVSDGIIAAGYEPEALEILKKKKNGGYCILQMDPNYEPSAVERKTIFGLTLEQKRNDAVIDASLFSNVVSKRGPLPEVAVRDLIVATIALKYTQSNSVCYARDGQVVGIGAGQQSRIHCTRLAGEKADNWWLRQHPSVAGMKFKAGVKRAEISNAIDNYVNGTVGKDMPLSQFEGMFDKAPAQLTSEQKVEWLKQLSGVALGSDAFFPFRDNIDRASLSGVSYIASPAGSTNDAGVIAACDEHGIIMAHTNLRLFHH
Protein: Protein SLY1 (Suppressor of loss of YPT1 protein 1) (P22213)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Able to suppress the functional loss of YPT1. SLY1 is essential for cell viability. May interact indirectly, or directly with YPT1.
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein.
Interaction partners:
- Golgi SNAP receptor complex member 1
- Protein transport protein SFT1
- Integral membrane protein SED5
- Alpha-soluble NSF attachment protein
- Protein transport protein BOS1
- Synaptobrevin homolog YKT6
- Protein transport protein BET1
- Syntaxin UFE1
- Protein transport protein SEC22
- Vesicular-fusion protein SEC18
Sequence:
MAVEEIASRKDISLRDMQISAILKMLFLNKDLNNNDNITTITDDIFNQQEIIWKVLILDIKSTATISSVLRVNDLLKAGITVHSLIKQDRSPLPDVPAIYFVSPTKENIDIIVNDLKSDKYSEFYINFTSSLPRNLLEDLAQQVSITGKSDKIKQVYDQYLDFIVTEPELFSLEISNAYLTLNDPKTTEEEITGLCANIADGLFNTVLTINSIPIIRAAKGGPAEIIAEKLGTKLRDFVINTNSSSTSTLQGNDSLERGVLIILDRNIDFASMFSHSWIYQCMVFDIFKLSRNTVTIPLESKENGTDNTTAKPLATKKYDIEPNDFFWMENSHLPFPEAAENVEAALNTYKEEAAEITRKTGVTNISDLDPNSNNDTVQIQEVVKKLPELTAKKNTIDTHMNIFAALLSQLESKSLDTFFEVEQDPGSTKTRSRFLDILKDGKTNNLEDKLRSFIVLYLTSTTGLPKDFVQNVENYFKENDYDINALKYVYKLREFMQLSNMSLQNKSLEDGSDSAFKPSNLTLSGIYGLTEGKLQGGVGSLISGIKKLLPEKKTIPITNVVDAIMDPLNSSQKNLETTDSYLYIDPKITRGSHTRKPKRQSYNKSLVFVVGGGNYLEYQNLQEWAHSQLHNPKKVMYGSTAITTPAEFLNEISRLGASNSSNNDA
Protein: MORC family CW-type zinc finger protein 4 (Zinc finger CW-type coiled-coil domain protein 2) (Zinc finger CW-type domain protein 4) (Q8TE76)
Organism: Homo sapiens (Human)
Function: Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3. The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0.
Subcellular location: Nucleus {ECO:0000305|PubMed:17608765}.
Interaction partners:
- E3 ubiquitin-protein ligase NEDD4
- Polycomb group RING finger protein 1
Sequence:
MLLYRGAPAGPGAPGCGLARPGGGPQAFGIRLSTMSPRYLQSNSSSHTRPFSAIAELLDNAVDPDVSARTVFIDVEEVKNKSCLTFTDDGCGMTPHKLHRMLSFGFTDKVIKKSQCPIGVFGNGFKSGSMRLGKDALVFTKNGGTLTVGLLSQTYLECVQAQAVIVPIVPFNQQNKKMIITEDSLPSLEAILNYSIFNRENDLLAQFDAIPGKKGTRVLIWNIRRNKNGKSELDFDTDQYDILVSDFDTEEKMTGGVTSELPETEYSLRAFCGILYMKPRMKIFLRQKKVTTQMIAKSLANVEYDTYKPTFTNKQVRITFGFSCKNSNQFGIMMYHNNRLIKSFEKVGCQVKPTRGEGVGVIGVIECNFLKPAYNKQDFEYTKEYRLTINALAQKLNAYWKEKTSQDNFETSTVARPIPKVPDQTWVQCDECLKWRKLPGKIDPSMLPARWFCYYNSHPKYRRCSVPEEQELTDEDLCLSKAKKQEQTVEEKKKMPMENENHQVFSNPPKILTVQEMAGLNNKTIGYEGIHSPSVLPSGGEESRSPSLQLKPLDSSVLQFSSKYKWILGEEPVEKRRRLQNEMTTPSLDYSMPAPYRRVEAPVAYPEGENSHDKSSSERSTPPYLFPEYPEASKNTGQNREVSILYPGAKDQRQGSLLPEELEDQMPRLVAEESNRGSTTINKEEVNKGPFVAVVGVAKGVRDSGAPIQLIPFNREELAERRKAVESWNPVPYSVASAAIPAAAIGEKARGYEESEGHNTPKLKNQRELEELKRTTEKLERVLAERNLFQQKVEELEQERNHWQSEFKKVQHELVIYSTQEAEGLYWSKKHMGYRQAEFQILKAELERTKEEKQELKEKLKETETHLEMLQKAQVSYRTPEGDDLERALAKLTRLRIHVSYLLTSVLPHLELREIGYDSEQVDGILYTVLEANHILD
Protein: Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI) (O51672)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
Interaction partners:
- Triosephosphate isomerase
- ATP-dependent 6-phosphofructokinase
- Pyruvate kinase
- Enolase
- Glyceraldehyde-3-phosphate dehydrogenase
- Fructose-bisphosphate aldolase
- Phosphoglycerate kinase
- Glucose-6-phosphate 1-dehydrogenase
- Glucosamine-6-phosphate deaminase
- Lipoprotein, putative
Sequence:
MLNYKNLNELENFKILEGIAPEVLKTALTGKRIKEYDITIEGDSVHYNYASKQINETHLKIFQNLSDEANLIEKYKEVLDGEKINISENRKVLHHLTRGQIGKDVIEDNKENMREFFQSELEKIYNFAKQIHSGNIKSSNGKKFKNVVQIGIGGSSLGPKALYSSIKNYAKKHNLALMNGYFISNIDPDESEEVLSSINVDETLFIIVSKSGNTLETKANMQFLINKLKLNGIKEYKKQMVIITLKDSMLAIEEKGYLEYFFMHDSIGGRFSPTSAVGLTLLTLCFTEKVAKEILKGANEADKKSLNKNVKDNASLLAALISIYERNVLNYSSNCIIAYSKAMENFYLHLQQLEMESNGKSVNRFNETINYKTVRIIWGGIGTDVQHSFFQMLHQGTDIVPMDFIGFNETQLKEDVISDNSSSNDKLKANLIAQIIAFSKGKENSNKNKNFQGERPSALIYSKELTPYAIGAILSHYENKVMFEGFLLNINSFDQEGVQLGKIIANQILKNDNFKDEVIESYSKKILKKF
Protein: Protein phosphatase, Mg2+/Mn2+ dependent 1A (E9PKB5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLESWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVHFFTQDHKPSNPLEKERIQNAGGSVMIQRV
Protein: Uncharacterized protein (EC 3.6.1.3) (Q9W2I5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Phospholipid-transporting ATPase
- IP10114p
Sequence:
MDASKQSSPKRESNPFIKANIISKWLFLWMHSVFRKGRREELDASKLYEHLPSFDSESLTRNLQPHWEKESKKKNPSLMRLIFKVYGWQFVPVCILYSLLEMAIHSFQPLLLGGLISYFAYGQTTVTKESAYLYAMGIVLCSLVTSLVFHPFMFYVFAVGTRVRLACAGLVYRKCLRASASSGEGLGGQAISVMSIDLSQFDLTFYFFHDLWKGPVEACIFGYLMTRQVGWTSLIGIAFIVILIPLQAWAAKASASFGTRSAKHRDARVKLMNEIIGAIQVIKMYAWEKSFGRLIAAVRQSEVKAIRGSMSIYAALQCTNMISKISLFLSLVAYVYVGDLVTAKKVFILSSYYGLLNDSLLHYWPMAITTWAQTLVSARRVVEFLLQVEKPTEESCCRDNPGLELDAEKPKPAQSGRLHCVQSETKCLSFRKVSASWDKPSIKQPRKPHIEGISFHINAGQFVGIVGNVGSGKSTLLHAILGEIELMQGRVEVHGRISYAAQQPWVFQGSIRENILFVEQYEEKRYRAVVHACQLDRDLELLPRGDATVVGERGISLSGGQKARIALARAVYRQADIYLFDDPLAAVDAQVGKLLMDKCFHRLLDGKMRILVTHHVQLLKSVDQLLLLEGGKLTQQGSYEELKDVITHHAALDLEAIEADKQQVKRVLSQVDRTSKQLSKGEEKDPATIQDENGNAEQQLQGAVSYDTYKAYFRALGAPFLVCLVLSMFVLARGCQAVMDIFISRWATWEEDRGYDSVDDYEATRTKMVIWYTVLLLLTLALFLLRTFGFFFMCLRISLTLHDQLYHGIIRAWMYFFNANPSGRVLNRFSSDIQNVDVNLPQAMMDSLQFLVDVVAVLVIVAIANYWLLIPAAIMVILLYFCRALYIGASRSLKRIESLTRSPIYSHTNQTFHGHSTIRSMDAMPQLEQTFHGHQNTNSSALFLYVSANRAFSFWTDLICVIYILAVTFSFLVINQSFYSGDVGLAITQSMTLVIMCQWGMRQTAEMENNMTSVERVLEYAQTPSEPPLESPKSVNLAAEWPQAGHLRFQDLRMRYSPGDEDILRGLNFESQPMEKIGIVGRTGAGKSSIIQALFRLALNEGTIEIDGLDIGKLGLHDLRSRISIIPQDPVLFSGTLRFNLDPFDEKSDESLWSALDDVKLKKHVASLEGGLSCRMQDGGSNFSMGQRQLVCLARAILRQNRVLVMDEATANVDTETDILIQETIQTKFAECTVLTIAHRLHTVMDNDSVLVMDAGQIVEFGAPHKLLQRKDGALLKLVNQNDATTVKFLKRIASESYMRRNRRDSLTISEE
Protein: CNH domain-containing protein (Q4GYA2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Vacuolar protein sorting complex subunit, putative
- RING-type domain-containing protein
- Vacuolar assembly protein vps41, putative
- Pep3/Vps18/deep orange beta-propeller domain-containing protein
- Vacuolar protein sorting 33, putative
- RING-type domain-containing protein
- Ras-related protein Rab-7b
- Vesicle transport v-SNARE N-terminal domain-containing protein
- Vesicle-associated membrane protein, putative
Sequence:
MSSYEAFRLRELKQKIPYVIESITTAGNLVFIGTNDGKLIVYELSPSKGDLRCLHIHTARRKHPILATIPIVEKQILVAVADDAILVFRLEEPITSAATDHPREDQLQELSAITGMKDITAVHVKRQKGIFSMAVLQRKKVSIYEYREQGQRQEFIPVRDGLQVPDGGKSLTWASRNIMVALRREYLLVDVASGMVECLYPTSNSKGVNPLLLPLDPVPEVLVDNGRGNGARALHDGTILAGNEANTLVWSSPPNGATYVHPFLLTVHSSSGLEVRLPFASTTRGCSETTPLGQSIGCKGIERISHRSYADFDVTLPTKSTPADAFRRDVTIATSSSGGSTNTVYLVEMVPPREQVMGLISAKQFEFGLLLYELCVNEVEEALAKSMQTHYALWCVYKRGDVKTAILRFRDARVDPRLVISLFPGFLTQRARDAWQVPADLSELLSSFRAFEGVVCSNESVDLLLDYVTSLRPEYIAAGSSASVGMDTSLYPDVDVVLEAVDTAILRAYVFLGQEKELLNFLCTENACAPRDSEQCLLKGEQWVGLVALWYRQGLHSRSLELLKELAVTGEPTCSAIGSSVNKEGEGIDTVPNTIQDDNVIRDSFNDEFLSVLRRLLPKVMIPEHETSGIFISQSDIYSHMEAPMDQEEDLQQSARLLRRCVGVVTTILYCRKLAWDIPETLQLVARHALWVLANIPPLWSVMLFPVDKMTAEQQAAVLRLVRTDMMGVGTTNMHERVVEWLSLILGNQYDTCRDAAMHDAYWKSLVEVVFVEGEQAKSVGVGAEIEVEETEIRQRRRKVLCDFLSSSSFMNLSVVRAYLEQPTVRSQAYPERAIIYQRLKLHGEAVRMCLYEMNQLEEAKYYAIRASRDEEDVFLVLLKELLRPSTGAEPRLEEAMSIASTCGSIEPLAVLELLPDNTPIAVVEDFLRRSLSVAAMRNRSAAIYASVLEARVRQAEKVLELEKSRRVVIDIESSCAVCGKKLRPGTVFARFPNGILVHHVCIDDESVCPVTHKDFRKGVEVLLREVL
Protein: FI01102p (Munster protein) (PvuII-PstI homology 13) (Q9XZU0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Opsin Rh6
- Opsin Rh5
- Opsin Rh3
- Protein PIP82
- Protein glass
Sequence:
MDKGTMKRKQRRYRTTFNTLQLQELERAFQRTHYPDVFFREELAVRIDLTEARVQVWFQNRRAKWRKQEKIGGLGGDYKEGALDLDVSYDDSAVLGQLDSALGGGGTLLPDTPPQSSNSLDNELKASYGTGAMSPSRLSPNIFLNLNIDHLGLERGGSGLSMEWSTYPPQTQAQTHPQMDSDNQLQQHPPQQHASDPIHAGSSSHHQQQQQQHQQEQHNPQLHPGLEFAASLSLDMTDGSSAYDEMKFLSVDVDQFTIDSFKADCILSMEQSQMQAYGGHSQLVGSSNELCLDGIGMSSFGMEEGEPKSPPSLLVLDKSLPSLSIGVEGIADLVEQLHHHQHEGGPVGGGVITGDVM
Protein: Probable enoyl-CoA hydratase 2 (EC 4.2.1.119) (MFE-2) (Multifunctional enzyme B) (MFE-B) (Q54XZ0)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Peroxisome {ECO:0000305}.
Interaction partners:
- Peroxisomal multifunctional enzyme A
- SCP2 domain-containing protein
- Probable enoyl-CoA hydratase, mitochondrial
- Probable enoyl-CoA hydratase, mitochondrial
- malate synthase
- isocitrate lyase
- acetyl-CoA C-acyltransferase
- Peroxisomal acyl-coenzyme A oxidase 1
- Peroxisomal targeting signal 1 receptor
Sequence:
MTVDVKKVINHKIKPIEYNLTRKDVALYAISLGCGKKHLKFVYEGSDNFSALPTLGVIFPGQMIVDVISEGIDGIEFDPMMLLHGEQELEILNEIPVEGVFVTESKITNLYDKGKGALLILQCITSEKSSGKPIFKNIFSFFIRGIGGFGGDRGPNEKPIQIPKDRAPDAISKQATSEDQAVIYRLAGGDLNPLHIDPEMSKIGGFEVPILHGLCTYGIASRGVLEHFCDNDPSRLKSIKTRFTKHVYPGETIETEMWKINPTTILFQSKTNRDGSYVLSSGVAIIEPIKKGSL
Protein: procollagen-proline 4-dioxygenase (EC 1.14.11.2) (Q8T5S7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
Sequence:
MFRLSIILPLLCLFPVNGDYYSAISELERLLDVEAFIVEKFDEYLERAQQEQENLKRFLDQIDEQQNDRGDLEEYFGNPINAFITIKRLVHDWKFNVFDPVFDSSNFETYKNNLSDSLEKINFKGPTQEDLHGATRALLRLQNMYQLNTDHLASGVLLPGEKSPLATSLSASDCFELGKNLCEIKEYSYGSEWLLEARKRLHGKPLGFISPNVSDVEILEHLSPAFNGLGNLKLAHKLNNEILDKKPDHEEALKNKILYEGQLARERSFAPRKQVELPHIAEKEQKESYKLYTEVCRGELHQSPREQRNLRCWLSHQGVPYYRLFPFKIEQLNIDPYVAYVHEVLWDSEIDTIMEHGKGNMERSKVGQSENSTTSEVRISRNTWLWYDANPWLSKIKQRLEDVTGLSTESAEPLQLVNYGIGGQYEPHFDFVEDDGQSVFSWKGNRLLTALFYLNDVALGGATAFPFLRLAVPPVKGSLLIWYNLHSSTHKDFRTKHAGCPVLQGSKWICNEWFHVGAQEFRRPCGLSSDEGKFLHLKDI
Protein: Grunge, isoform I (M9PES2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAASTQGEIRVGPGHQAKLPDYNPISSFPIDKETDERELEESRWSPGVVADGDLLMFLRAARSMAAFQGMCDGGLEDGCLAASRDDTTINALDVLHDSGYDPGKALQALVKCPVSKGIDKKWTEDETKKFIKGLRQFGKNFFRIHKDLLPHKDTPELVEFYYLWKKTPGANNNRPHRRRRQSALRRNRVTRANNSNSNTPPKKEDTPEPQTATTATAAATAASETASRSSPAVSKEENSSLTEDDASECDSDSSLTHKRDESPSRMRTRNKQQNNNSSTSSGNNTAGNGGGNATSISSGSTGGGAAGGNSSSKDQSANAVANGKRPKRGSETPDVSGGASVDSPKTPTKAVAESSANKRKGGKQDTPNKKKRTEQESNEPSAHEENAIKEKRKRPDSPVESMNSDSRPDSVLDDGESNTTDTTTAEQQSTKDSKETVSCKEEREMVTNDLEAKAEEKAIKAEALAEDSKDSAIKNMDEETNIQAPSSADTSLVDGPNPNALPSPVAAPITMKVPTIATVEALNASVDRKEAIEKMESCDSDPEMLKKLATIKQEVSPQQQQHMQQQSQQQMQQQLAPVGIPQPPSCPPSESVYIKKEPMEDSMDATCNQNSNEPQDLKVKIEIKNEDALKHSAGGLPPSGPCAPPSALHPLSGAPVESGQEPLHLQHMPHGQVTTQPPPGYLIDGQLKYGPSGQGVPPQPPQLHSDAAGGVSGAPPGAPTTPQKYPPEMEMKFAPQDLKYPPPPPLDALKYSQEMQAAAAAAAAAGKYDMKYMMEQQGKYNVELSAAHQPPSKPGYQDSLKIPDIKPGFGHLPHNVGSPLDAAHKYGPPPTSQESQQQQPQPPAHQVPPGATPPPGIAMPKPHYQHDVQTPPLGRPFEPTGLMLKYGDPLAAKYGPPQDLKYPMPPVSQAGPADVKPYGGENLIKSSPYGPPPESPIDASARSTPGQDSQGSNSNSQPPSMPPQPQQFQSPHPSPHMPSPAGGGLPPGMHPQNLIHGPPPGAAGGSGPQPPPPPTSLHQPTPTSAGPPSLQHGLHPGHQHSQLSVASSIPPSSIGIPPTLSTMAPSHMHPHLHPHAHLQGLHRPHDLPPSMHPHAPMPLSLQGHPQHGHGLPPSHTSQQQQQQQQQQQPGGPAGTVRTPSPAQQPPRSMHDPQSSREPPTSQPSTTMAGSSGPGGPPPQQSPHAHRTSPLPGLAGSGPPPPGLIGHPMAIHPHLAHLPPGHPAHAALAHPGHHLLSHSIAGLGPGGGPIALLAGPGGLGGIPESALSRRTPPSHLPHSHASSAPLTAHSVASMTSTSMSLTTSTVPSSAFSRASPSVQISSSGGGPSGPGSVGPGGMPNSSAAAAAAAAAHRAASPASSVSSLSRQSPLHPVPQSPLSHHPSSSALSAAAAAVAERDRHALMRQQSPHMTPPPVSNASLMASPLSKMYAPQPGQRGLGTSPPPHLRPGASPPVIRHPQMPLPLPLIAPGGGIPQIGVHPGQSPYPHPLLHPSVFYSPHHHPFNSPYGYAPYGPGFPAYMKPPPQPGQLDPAAVMAAHHAGLQGPPPQQMRQDEQNAAAAAAQAAAEKQHQAAAAAAAQQHKAPQQQQPGGMPPNKPPTPKTPQGPGGGMPPGMGGPGTPTGLPPGAYPGSHMPGYPQGPPHGSPFAPQDGQPHGLKPTSHMDALRAHAHSANSAGMGGGHHPTEPLPIDIEPDPEPEIPSPTHNIPRGPSPEAKPDDTECHRSQSAIFVRHIDRGDYNSCTRTDLIFKPVADSKLARKREERDRKLAEKERERRQQQQQQQQQQQQQQAAAAQQAAQQAKMKAELKPPYADTPALRQLSEYARPHVAFRELEEIKNAQAAAASQSRLDPHWMEYYRRGIHPSQFPLYANPAISQMERERLGIPPPHHVGLDPGEHMIRLTREYHAHSHTHLHLPLHPQPQPPEAGFQLPPNVGQYPRPNMLIPREPHSDVLLRMSYADQLQYLQAAEFQRQSLHDQYFRQRPR
Protein: Ras-related protein Rab-13 (EC 3.6.5.2) (Cell growth-inhibiting gene 4 protein) (P51153)
Organism: Homo sapiens (Human)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in endocytic recycling and regulates the transport to the plasma membrane of transmembrane proteins like the tight junction protein OCLN/occludin. Thereby, it regulates the assembly and the activity of tight junctions. Moreover, it may also regulate tight junction assembly by activating the PKA signaling pathway and by reorganizing the actin cytoskeleton through the activation of the downstream effectors PRKACA and MICALL2 respectively. Through its role in tight junction assembly, may play a role in the establishment of Sertoli cell barrier. Plays also a role in angiogenesis through regulation of endothelial cells chemotaxis. Also involved in neurite outgrowth. Has also been proposed to play a role in post-Golgi membrane trafficking from the TGN to the recycling endosome. Finally, it has been involved in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore may play a role in glucose homeostasis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15528189}; Lipid-anchor {ECO:0000305|PubMed:8375503}; Cytoplasmic side {ECO:0000305|PubMed:8375503}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:15528189, ECO:0000269|PubMed:8294494}; Lipid-anchor {ECO:0000305|PubMed:8375503}; Cytoplasmic side {ECO:0000305|PubMed:8375503}. Cell junction, tight junction {ECO:0000269|PubMed:12058051, ECO:0000269|PubMed:8294494}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:18779367}. Recycling endosome membrane {ECO:0000269|PubMed:18779367}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9DD03}. Note=Tight junctions or associated with vesicles scattered throughout the cytoplasm in cells lacking tight junctions (PubMed:8294494). Relocalizes to the leading edge of lamellipodia in migrating endothelial cells (By similarity). {ECO:0000250|UniProtKB:Q9DD03, ECO:0000269|PubMed:8294494}.
Interaction partners:
- MICAL-like protein 2
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit beta
- Rab GDP dissociation inhibitor alpha
- Tight junction protein 1
- MICAL-like protein 1
- Guanine nucleotide exchange factor MSS4
- Rab GDP dissociation inhibitor beta
- Radial spoke head 14 homolog
Sequence:
MAKAYDHLFKLLLIGDSGVGKTCLIIRFAEDNFNNTYISTIGIDFKIRTVDIEGKKIKLQVWDTAGQERFKTITTAYYRGAMGIILVYDITDEKSFENIQNWMKSIKENASAGVERLLLGNKCDMEAKRKVQKEQADKLAREHGIRFFETSAKSSMNVDEAFSSLARDILLKSGGRRSGNGNKPPSTDLKTCDKKNTNKCSLG
Protein: Glutamate-gated chloride channel alpha (Avermectin-sensitive glutamate-gated chloride channel GluCl alpha) (GluCl alpha) (G5EBR3)
Organism: Caenorhabditis elegans
Function: Glutamate-gated chloride channel subunit; channel properties depend on the subunit composition. Glutamate binding triggers a rapidly reversible current in heteromeric channels formed by glc-1 and glc-2, while the anti-helmintic drug ivermectin and other avermectins trigger a permanently open channel configuration. Channels containing only glc-1 are activated by ivermectin, but not by glutamate alone (in vitro). The heteromeric channel formed by glc-1 and glc-2 is also activated by ibotenate, and it is blocked by picrotoxin and flufenamic acid. Plays a role in the regulation of locomotor behavior.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q94900}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q94900}. Cell membrane {ECO:0000255, ECO:0000269|PubMed:21572436, ECO:0000269|PubMed:25143115, ECO:0000269|PubMed:7935817}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:21572436, ECO:0000269|PubMed:25143115, ECO:0000303|PubMed:7935817}.
Interaction partners:
- Glycine--tRNA ligase
- Acetylcholine receptor-like protein cup-4
- Tubulin beta chain
Sequence:
MATWIVGKLIIASLILGIQAQQARTKSQDIFEDDNDNGTTTLESLARLTSPIHIPIEQPQTSDSKILAHLFTSGYDFRVRPPTDNGGPVVVSVNMLLRTISKIDVVNMEYSAQLTLRESWIDKRLSYGVKGDGQPDFVILTVGHQIWMPDTFFPNEKQAYKHTIDKPNVLIRIHNDGTVLYSVRISLVLSCPMYLQYYPMDVQQCSIDLASYAYTTKDIEYLWKEHSPLQLKVGLSSSLPSFQLTNTSTTYCTSVTNTGIYSCLRTTIQLKREFSFYLLQLYIPSCMLVIVSWVSFWFDRTAIPARVTLGVTTLLTMTAQSAGINSQLPPVSYIKAIDVWIGACMTFIFCALLEFALVNHIANKQGVERKARTEREKAEIPLLQNLHNDVPTKVFNQEEKVRTVPLNRRQMNSFLNLLETKTEWNDISKRVDLISRALFPVLFFVFNILYWSRFGQQNVLF
Protein: Chitobiosyldiphosphodolichol beta-mannosyltransferase (EC 2.4.1.142) (Asparagine-linked glycosylation protein 1) (Beta-1,4-mannosyltransferase) (GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase) (GDP-mannose-dolichol diphosphochitobiose mannosyltransferase) (P16661)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29939232}; Single-pass membrane protein {ECO:0000269|PubMed:29939232}.
Interaction partners:
- Alpha-1,3/1,6-mannosyltransferase ALG2
- UDP-N-acetylglucosamine transferase subunit ALG13
- UDP-N-acetylglucosamine transferase subunit ALG14
- GDP-Man:Man
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Mannose-1-phosphate guanyltransferase
- Dolichol-phosphate mannosyltransferase
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dol-P-Man:Man
- Man
Sequence:
MFLEIPRWLLALIILYLSIPLVVYYVIPYLFYGNKSTKKRIIIFVLGDVGHSPRICYHAISFSKLGWQVELCGYVEDTLPKIISSDPNITVHHMSNLKRKGGGTSVIFMVKKVLFQVLSIFKLLWELRGSDYILVQNPPSIPILPIAVLYKLTGCKLIIDWHNLAYSILQLKFKGNFYHPLVLISYMVEMIFSKFADYNLTVTEAMRKYLIQSFHLNPKRCAVLYDRPASQFQPLAGDISRQKALTTKAFIKNYIRDDFDTEKGDKIIVTSTSFTPDEDIGILLGALKIYENSYVKFDSSLPKILCFITGKGPLKEKYMKQVEEYDWKRCQIEFVWLSAEDYPKLLQLCDYGVSLHTSSSGLDLPMKILDMFGSGLPVIAMNYPVLDELVQHNVNGLKFVDRRELHESLIFAMKDADLYQKLKKNVTQEAENRWQSNWERTMRDLKLIH
Protein: Tachykinin-like peptide-VII (P.nigriventer tachykinin peptides VII) (PnTkP-VII) (U29-ctenitoxin-Pn1g) (U29-CNTX-Pn1g) (P86304)
Organism: Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer)
Subcellular location: Secreted {ECO:0000269|PubMed:15573368}.
Interaction partners:
Sequence:
QKKDRFLGLF
Protein: mRNA 3'-end-processing protein YTH1 (Yeast 30 kDa homolog 1) (Q06102)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB.
Subcellular location: Nucleus {ECO:0000269|PubMed:12819204, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-tRNA-processing protein PTA1
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Polyadenylation factor subunit 2
- Poly
- Protein PTI1
- COMPASS component SWD2
- Protein MPE1
- Pre-mRNA polyadenylation factor FIP1
- Protein CFT1
- RNA end formation protein 2
Sequence:
MSLIHPDTAKYPFKFEPFLRQEYSFSLDPDRPICEFYNSREGPKSCPRGPLCPKKHVLPIFQNKIVCRHWLRGLCKKNDQCEYLHEYNLRKMPECVFFSKNGYCTQSPDCQYLHIDPASKIPKCENYEMGFCPLGSSCPRRHIKKVFCQRYMTGFCPLGKDECDMEHPQFIIPDEGSKLRIKRDDEINTRKMDEEKERRLNAIINGEV
Protein: Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132) (P31785)
Organism: Homo sapiens (Human)
Function: Common subunit for the receptors for a variety of interleukins. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15123770}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000269|PubMed:15123770}.
Interaction partners:
- Interleukin-15 receptor subunit alpha
- Interleukin-2 receptor subunit beta
- Interleukin-15
- Interleukin-4
- Interleukin-7
- Interleukin-4 receptor subunit alpha
- Interleukin-2
- Interleukin-2 receptor subunit alpha
- Interleukin-7 receptor subunit alpha
- Tyrosine-protein kinase JAK3
Sequence:
MLKPSLPFTSLLFLQLPLLGVGLNTTILTPNGNEDTTADFFLTTMPTDSLSVSTLPLPEVQCFVFNVEYMNCTWNSSSEPQPTNLTLHYWYKNSDNDKVQKCSHYLFSEEITSGCQLQKKEIHLYQTFVVQLQDPREPRRQATQMLKLQNLVIPWAPENLTLHKLSESQLELNWNNRFLNHCLEHLVQYRTDWDHSWTEQSVDYRHKFSLPSVDGQKRYTFRVRSRFNPLCGSAQHWSEWSHPIHWGSNTSKENPFLFALEAVVISVGSMGLIISLLCVYFWLERTMPRIPTLKNLEDLVTEYHGNFSAWSGVSKGLAESLQPDYSERLCLVSEIPPKGGALGEGPGASPCNQHSPYWAPPCYTLKPET