wanglab/gogpt-training-data huggingface dataset:
Protein: polynucleotide adenylyltransferase (EC 2.7.7.19) (Q57ZJ6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 2
- C3H1-type domain-containing protein
- Cleavage and polyadenylation specificity factor 30 kDa subunit
- Cleavage and polyadenylation specificity factor subunit, putative
- Cleavage and polyadenylation specificity factor-like protein, putative
- Uncharacterized protein
- Poly
- Suppressor of forked domain-containing protein
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Nucleic acid binding protein, putative
Sequence:
MEWMYGPTKPLEVPRPQDHDYDESEMLYGVLAECPSISPNPVLTLVESMALRIVQRHSQNTQEQWARAYPFGSCGLSASVAESDLDVALICPSVLTTDIFFDEFPRLLYNSVGPVSVVAARVPVVKFEYRGTAVDVVFVSVGLPQPPTEEQMLDDSFLLKVARETRPSANGIRFTFEIKRRLPVPYDVFTAVLKTVKLWAMRRMVYGNVYTYPNGAVLAIMVARVCQVLPSSHPSTLLRFFFLFYTQWMSRHDRISPVYLTATLEGRGRIPGLPDSWKPSKDKICCDLFPVISPAYPYVNDASSVGRCGLEALYSEITRVQCILTEARTLPLEEMWEPYRIEEEYSTFLVVGVSCAGHSMAETEQALSVWSSYVASRLRILIYSIERHAQARPCPRKIRPKKDNHVGGSSCFLSVNFLIGVKAKEGGPTPQPSLFTEACGEFHHAVKEGCNNDSIPWSFQRNDRAMHWPRVKFLEVHQVLHLLQDLK
Protein: Cul1b protein (Cullin-1b) (Q802D4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSSTRGQNTHGLKQIGLEQIWDDLRSGIQQVYTRQSMARSRYMELYTHVYNYCTSVHQARPTGIPSSKPSKKTPTPGGAQFVGLELYKRLKDFLRSYLTNLLKDGEDLMDESVLKFYTQQWEDYRFSSKVLDGICAYLNRHWVRRECDEGRKGIYEIYSLALATWRECLFRPLNKQVTNAVLKLVEKERNGETINTRLVSGVVQSYVELGLNEDDAFVKGPTLSVYKEYFEAQFLADTERFYTRESTEFLQQNPVTEYMKKAEARLLEEQRRVQVYLHESTQDELARKCEQVLIEKHLEIFHTEFQNLLDADKNEDLGRMYNLVSRITDGLGELKKLLESHIHNQGLAAIEKCGDSALNDPKMYVQTTLDVHKKYNALVMSAFNNDAGFVAALDKACGRFINNNAVTRMAQSSSKSPELLARYCDSLLKKSSKNPEEAELEDTLNQVMVVFKYIEDKDVFQKFYAKMLAKRLVHQNSASDDAEASMISKLKQACGFEYTSKLQRMFQDIGVSKDLNEQFKKHLSNSEPLDLDFSIQVLSSGSWPFQQSCTFALPSELERSYQRFTAFYGSRHSGRKLTWLYHLSKGELVTNCFKNRYTLQASTFQMAILLQFNTENCYSVQQLADSTQIKTDILVQVLQILLKSKLLVLEDENANIDEMDFKPDTLIKLFLGYKNKKLRVNINVPMKTEQKQEQETTHKNIEEDRKLLIQAAIVRIMKMRKVLKHQQLLAEVLNQLSSRFKPRVPVIKKCIDILIEKEYLERVDGEKDTYSYLA
Protein: Small ribosomal subunit protein eS28A (40S ribosomal protein S28-A) (S33) (P0CT79)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS13B
- Small ribosomal subunit protein eS24B
- Small ribosomal subunit protein uS19B
- Small ribosomal subunit protein eS30B
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS10B
- Small ribosomal subunit protein eS30A
Sequence:
MDSSKVPVKLAKVIKVLGRTGSRGGVTQVRVEFMDDTSRSIIRNVKGPVREDDILVLLESEREARRLR
Protein: Probable WRKY transcription factor 49 (WRKY DNA-binding protein 49) (Q9FHR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- At2g24350
- Cytochrome P450 71B8
- Protein NRT1/ PTR FAMILY 5.8
- AP2/ERF and B3 domain-containing transcription factor At1g50680
- Putative cytochrome P450 71A28
- AP2/ERF and B3 domain-containing transcription factor At1g51120
Sequence:
MEEEGYQWARRCGNNAVEDPFVYEPPLFFLPQDQHHMHGLMPNEDFIANKFVTSTLYSGPRIQDIANALALVEPLTHPVREISKSTVPLLERSTLSKVDRYTLKVKNNSNGMCDDGYKWRKYGQKSIKNSPNPRSYYKCTNPICNAKKQVERSIDESNTYIITYEGFHFHYTYPFFLPDKTRQWPNKKTKIHKHNAQDMNKKSQTQEESKEAQLGELTNQNHPVNKAQENTPANLEEGLFFPVDQCRPQQGLLEDVVAPAMKNIPTRDSVLTAS
Protein: ATP binding cassette subfamily G member 1 (G3V642)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Apolipoprotein E
- Oxysterols receptor LXR-alpha
- Oxysterols receptor LXR-beta
- Scavenger receptor class B member 1
- Sterol regulatory element-binding protein 2
- Cytochrome P450 7A1
- Apolipoprotein A-II
- Lysosome membrane protein 2
- Platelet glycoprotein 4
- Sterol regulatory element-binding protein 1
Sequence:
MACLMAAFSVGTAMNASNYSAAMTEPKSVCVSVDEVVSSNVDELETDLLNGHLKKVDNNFTEAQRFSSLPRRAAVNIEFKDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGMPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQCVYRGKVSNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSRLVRAVREGMCDSDYKRELGGDGDVNPFLWHRPAEEDSASMEGCHSFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMSVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGLDREDLHCDIAETCHFQKSEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER
Protein: Ameloblastin (Amelin) (Q62840)
Organism: Rattus norvegicus (Rat)
Function: Involved in the mineralization and structural organization of enamel.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Enamelin
- Amelogenin, X isoform
- Amelotin
- Kallikrein-4
- Matrix metallopeptidase 20
- Odontogenic ameloblast-associated protein
- Tuftelin 1.
- FAM20A, golgi associated secretory pathway pseudokinase
- Family with sequence similarity 83, member H
Sequence:
MSASKIPLFKMKGLLLFLSLVKMSLAVPAFPQQPGAQGMAPPGMASLSLETMRQLGSLQGLNALSQYSRLGFGKALNSLWLHGLLPPHNSFPWIGPREHETQQYEYSLPVHPPPLPSQPSLQPHQPGLKPFLQPTAATGVQVTPQKPGPHPPMHPGQLPLQEGELIAPDEPQVAPSENPPTPEVPIMDFADPQFPTVFQIAHSLSRGPMAHNKVPTFYPGMFYMSYGANQLNAPARIGFMSSEEMPGERGSPMAYGTLFPGYGGFRQTLRGLNQNSPKGGDFTVEVDSPVSVTKGPEKGEGPEGSPLQEASPDKGENPALLSQMAPGAHAGLLAFPNDHIPNMARGPAGQRLLGVTPAAADPLITPELAEVYETYGADVTTPLGDGEATMDITMSPDTQQPPMPGNKVHQPQVHNAWRFQEP
Protein: Heat shock 70 kDa protein 1-like (Heat shock 70 kDa protein 1L) (Heat shock 70 kDa-like protein 1) (Spermatid-specific heat shock protein 70) (P16627)
Organism: Mus musculus (Mouse)
Function: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Positive regulator of PRKN translocation to damaged mitochondria.
Interaction partners:
- Heat shock protein HSP 90-beta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit theta
- Zona pellucida-binding protein 1
- Zona pellucida-binding protein 2
- Mitogen-activated protein kinase 10
Sequence:
MAANKGMAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQSDMKLWPFQVINEAGKPKVMVSYKGEKKAFYPEEISSMVLTKMKETAEAFLGHNVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDKGSHGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKSLRDAKMDKAKIHDIVLVGGSTRIPKVQKLLQDYFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSEKVQDLLLLDVAPLSLGLETAGGVMTVLIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTRDNNLLGRFDLTGIPPAPRGVPQIEVTFDIDANGILNVTAMDKSTGKANKITITNDKGRLSKEEIERMVQEAERYKAEDEGQREKIAAKNALESYAFNMKSAVGDEGLKDKISESDKKKILDKCNEVLSWLEANQLAEKDEFDHKRKELENMCNPIITKLYQSGCTGPTCTPGYTPGRAATGPTIEEVD
Protein: KAT8 regulatory NSL complex subunit 2 (NSL complex protein NSL2) (Non-specific lethal 2 homolog) (F8VXI8)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNRIRIHVLPTNRGRITPVPRSQEPLSCAFTHRPCSHPRLEGQEFCIKHILEDKNAPFKQCSYISTKNGKRCPNAAPKPEKKDGVSFCAEHVRRNALALHAQMKKTNPGPVGETLLCQLSSYAKTELGSQTPESSRSEASRILDEDSWSDGEQEPITVDQTWRGDPDSEADSIDSDQEDPLKHAGVYTAEEVALIMREKLIRLQSLYIDQFKRLQHLLKEKKRRYLHNRKVEHEALGSSLLTGPEGLLAKERENLKRLKCLRRYRQRYGVEALLHRQLKERRMLATDGAAQQAHTTRSSQRCLAFVDDVRCSNQSLPMTRHCLTHICQDTNQVLFKCCQGSEEVPCNKPVPVSLSEDPCCPLHFQLPPQMYKPEQDLDVVGDGMQCPPSPLLFDPSLTLEDHLVKEIAEDPGQMQMAGDGCRSQGSRNSEKASAPLSQSGLATANGKPEPTSIS
Protein: Transcription-repair-coupling factor (TRCF) (EC 3.6.4.-) (P9WMQ5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00969}.
Interaction partners:
- UvrABC system protein A
- DNA-directed RNA polymerase subunit beta
- Nucleoside triphosphate pyrophosphohydrolase
- DNA-directed RNA polymerase subunit beta'
- Probable transcriptional regulatory protein
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit omega
- Possible conserved membrane protein
- Peptidyl-tRNA hydrolase
- Peptide chain release factor 2
Sequence:
MTAPGPACSDTPIAGLVELALSAPTFQQLMQRAGGRPDELTLIAPASARLLVASALARQGPLLVVTATGREADDLAAELRGVFGDAVALLPSWETLPHERLSPGVDTVGTRLMALRRLAHPDDAQLGPPLGVVVTSVRSLLQPMTPQLGMMEPLTLTVGDESPFDGVVARLVELAYTRVDMVGRRGEFAVRGGILDIFAPTAEHPVRVEFWGDEITEMRMFSVADQRSIPEIDIHTLVAFACRELLLSEDVRARAAQLAARHPAAESTVTGSASDMLAKLAEGIAVDGMEAVLPVLWSDGHALLTDQLPDGTPVLVCDPEKVRTRAADLIRTGREFLEASWSVAALGTAENQAPVDVEQLGGSGFVELDQVRAAAARTGHPWWTLSQLSDESAIELDVRAAPSARGHQRDIDEIFAMLRAHIATGGYAALVAPGTGTAHRVVERLSESDTPAGMLDPGQAPKPGVVGVLQGPLRDGVIIPGANLVVITETDLTGSRVSAAEGKRLAAKRRNIVDPLALTAGDLVVHDQHGIGRFVEMVERTVGGARREYLVLEYASAKRGGGAKNTDKLYVPMDSLDQLSRYVGGQAPALSRLGGSDWANTKTKARRAVREIAGELVSLYAKRQASPGHAFSPDTPWQAELEDAFGFTETVDQLTAIEEVKADMEKPIPMDRVICGDVGYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQHLQTFGERMSGFPVTIKGLSRFTDAAESRAVIDGLADGSVDIVIGTHRLLQTGVRWKDLGLVVVDEEQRFGVEHKEHIKSLRTHVDVLTMSATPIPRTLEMSLAGIREMSTILTPPEERYPVLTYVGPHDDKQIAAALRRELLRDGQAFYVHNRVSSIDAAAARVRELVPEARVVVAHGQMPEDLLETTVQRFWNREHDILVCTTIVETGLDISNANTLIVERADTFGLSQLHQLRGRVGRSRERGYAYFLYPPQVPLTETAYDRLATIAQNNELGAGMAVALKDLEIRGAGNVLGIEQSGHVAGVGFDLYVRLVGEALETYRDAYRAAADGQTVRTAEEPKDVRIDLPVDAHLPPDYIASDRLRLEGYRRLAAASSDREVAAVVDELTDRYGALPEPARRLAAVARLRLLCRGSGITDVTAASAATVRLSPLTLPDSAQVRLKRMYPGAHYRATTATVQVPIPRAGGLGAPRIRDVELVQMVADLITALAGKPRQHIGITNPSPPGEDGRGRNTTIKERQP
Protein: F1F0 ATP synthase subunit f (A0A1D8PRM5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- F1F0 ATP synthase subunit h
- ATP synthase subunit 4
- ATP synthase subunit beta
- ATP synthase subunit alpha
- F1F0 ATP synthase subunit i
- ATP synthase subunit d
- ATP synthase subunit 5
- ATP synthase subunit a
- ATP synthase subunit gamma
- ATP synthase subunit delta, mitochondrial
Sequence:
MSFVIRRQLSTLIPPKIASAKNLGSNPNAKRMAEVVKFYNKLPQGPAPAAKKSNNPFARYRAAYFDGDNASGKPLVHLAIAVVIFGYSLEYQHLKHAQHEGH
Protein: Transient receptor potential cation channel subfamily V member 4 (Transient receptor potential cation channel, subfamily V, member 4) (Q0PEH1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MTESLSVSSPPDNSAQDSSEAADGDPNFPMSSMAALLENDDVSQPTHELPRPGQQNDQKQNMRIRFPGPFKKGVPNPMDLLESDYTEYPKQAPMDSMFDYGTCRQINNNKKGRRKKLPRGKAEIGMSCDEGSPEPPVLKVFNRWMLFEAVSRADPRALDGLLQYLQSHEKRLTDEEFKELSTGKTCLPKALLNLHNGQNDTIPILVDIAEQTGNLREFINTPFRDVYYRGQMALHIAIERRCKQYVELLVEKGADVHAQARGRFFQPRDEGGYFYFGELPLSLAACTNQPDMVHYLTENGHKKADLRRQDSRGNTVLHALVHIADNTRDNTRFVTKMFDLLLIKCAKLYPDCNLENILNNDGMSPLMMAAKLGKIGVFQHTIRREIKDEEARHLSRKFKDWAYGPVYSNLYDLSSLDTCGEEVSVLEILVYNSKIENRHEMLAVEPINELLRAKWQKFAAVTFYISVFSYLVTMIIFTLVAYYRPSVGKPPYAYDTTEDKVRLGGEIITVGSGLFFFVTNIKDLFLKKCPGVNSIFVDGSFQLLYFIYSVLVVGSAALYLSGIEAYVSVMVFALTLGGMNPLYFTRGLKLTGTYSIMIQKILIKDLFRFLLVYVLFMIGYASALVSLLTICPNKDTCKENCPTYPECRDTNTFSEFLLDLFKLTIGIGDLDNMLKGAQYPAVFLILLVTYIILTFVPLLNMLIALMGETVGQVSKESKKIWKLQWATTILDIERSFPVCLRRSFRVGEMVTVGKGLDGKPDKRWCFRVDEVKWSHWNQNLGIINEDPGQKDLSEHTQGGRGLRRDRWSTVVPRVVELNRGSRDHTVEMEPLTGRHRLKSES
Protein: GPI inositol-deacylase (EC 3.1.-.-) (Post-GPI attachment to proteins factor 1) (Q765A7)
Organism: Rattus norvegicus (Rat)
Function: Involved in inositol deacylation of GPI-anchored proteins. GPI inositol deacylation may important for efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14734546}; Multi-pass membrane protein {ECO:0000269|PubMed:14734546}.
Interaction partners:
- GPI-anchor transamidase
- Glycosylphosphatidylinositol anchor attachment 1 protein
- Phosphatidylinositol glycan anchor biosynthesis, class T
- Transmembrane emp24 domain-containing protein 10
- GPI-anchor transamidase component PIGS
- GPI-anchor transamidase component PIGU
- Post-GPI attachment to proteins factor 3
- GPI ethanolamine phosphate transferase 1
- Urokinase plasminogen activator surface receptor
- Acyltransferase PGAP2
Sequence:
MFLHSVNLWNLAFYVFMVFLATLGLWDVFFGFEENKCSMSYMFEYPEYQKIELPKKLTKRYPAYELYLYGEGSYAEEHKILPLTGIPVLFLPGNAGSYKQVRSIGSIALRKAEDIDFKYHFDFFSVNFNEELVALYGGSLQKQTKFVHECIKAILKLYKGQEFPPTSVAIIGHSMGGLVARALLTLKNFKQDLINLLVTQATPHVAPVMPLDRFITEFYMTVNNYWILNARHINLTTLSVAGGFRDYQVRSGLTFLPTLSHHTSALSVVTSAVPKTWVSTDHLSIVWCKQLQLTTIRAFFDLIDADTKQITQKSKKKLSVLNHHFIRHPAKQFEENPSIISDLTGTSMWVPVKVSRWSYVAYNESDKIYFAFPLANHRKVYTHAYCQSTMLDTNSWIFGCINSTSMCRQGVDLSWKAELLPTIKSLTLRLQDYPSLSHIVVYVPSVHGSKFVVDCEFFKKEARSIQLPVTHLFSFGLSSRKAIINTSGRYYNIELLNLGQIYQAFKVNVVSKCTGGKEEITSIYKLHIPWSYEDSLTIAQVPSSVDISLKLHVAQPENDSHVALLKMYTSSDCQYEVTIKTSFPQILGQVVRFHGGALPAYVVSSILLAYGGQLYSLLSTGFCLEYGTMLDKEAKPYKVDPFVIMIKFLLGYKWFKELWDAVLLPELDAIVLTSQSMCFPLVSLILFLFGTCTAYWSGLLSSASVQLLSSLWLALKRPAELPKDVKVMSPDLPVLTVVFLIISWTTCGALAILLSYLYYVFKVVHLQASLTTFKNNQPVNPKHSRRSEKKSNHHKDSAIQNPRLSANDAEDSLRMHSTVINLLTWVVLLSMPSLIYWSKNLRYYFKLNPDPCKPLAFLLIPAIAVLGNTHTVSIKSSKLLKTASQFPLPLAVGVIAFGSSHLYRVPCFVIIPLVFHSLCNFM
Protein: SLIT-ROBO Rho GTPase-activating protein 3 (srGAP3) (Mental disorder-associated GAP) (Rho GTPase-activating protein 14) (WAVE-associated Rac GTPase-activating protein) (WRP) (O43295)
Organism: Homo sapiens (Human)
Function: GTPase-activating protein for RAC1 and perhaps Cdc42, but not for RhoA small GTPase. May attenuate RAC1 signaling in neurons.
Interaction partners:
- Roundabout homolog 1
- Cell division control protein 42 homolog
- Roundabout homolog 2
- SLIT-ROBO Rho GTPase-activating protein 2
- Actin-binding protein WASF1
- SLIT-ROBO Rho GTPase-activating protein 1
- Hydrocephalus-inducing protein homolog
- Formin-like protein 1
- Actin nucleation-promoting factor WASL
- G protein-regulated inducer of neurite outgrowth 2
Sequence:
MSSQTKFKKDKEIIAEYEAQIKEIRTQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRSSREHQFKKDQYLLSPVNCWYLVLHQTRRESRDHATLNDIFMNNVIVRLSQISEDVIRLFKKSKEIGLQMHEELLKVTNELYTVMKTYHMYHAESISAESKLKEAEKQEEKQFNKSGDLSMNLLRHEDRPQRRSSVKKIEKMKEKRQAKYSENKLKCTKARNDYLLNLAATNAAISKYYIHDVSDLIDCCDLGFHASLARTFRTYLSAEYNLETSRHEGLDVIENAVDNLDSRSDKHTVMDMCNQVFCPPLKFEFQPHMGDEVCQVSAQQPVQTELLMRYHQLQSRLATLKIENEEVRKTLDATMQTLQDMLTVEDFDVSDAFQHSRSTESVKSAASETYMSKINIAKRRANQQETEMFYFTKFKEYVNGSNLITKLQAKHDLLKQTLGEGERAECGTTRPPCLPPKPQKMRRPRPLSVYSHKLFNGSMEAFIKDSGQAIPLVVESCIRYINLYGLQQQGIFRVPGSQVEVNDIKNSFERGEDPLVDDQNERDINSVAGVLKLYFRGLENPLFPKERFQDLISTIKLENPAERVHQIQQILVTLPRVVIVVMRYLFAFLNHLSQYSDENMMDPYNLAICFGPTLMHIPDGQDPVSCQAHINEVIKTIIIHHEAIFPSPRELEGPVYEKCMAGGEEYCDSPHSEPGAIDEVDHDNGTEPHTSDEEVEQIEAIAKFDYMGRSPRELSFKKGASLLLYHRASEDWWEGRHNGVDGLIPHQYIVVQDMDDAFSDSLSQKADSEASSGPLLDDKASSKNDLQSPTEHISDYGFGGVMGRVRLRSDGAAIPRRRSGGDTHSPPRGLGPSIDTPPRAAACPSSPHKIPLTRGRIESPEKRRMATFGSAGSINYPDKKALSEGHSMRSTCGSTRHSSLGDHKSLEAEALAEDIEKTMSTALHELRELERQNTVKQAPDVVLDTLEPLKNPPGPVSSEPASPLHTIVIRDPDAAMRRSSSSSTEMMTTFKPALSARLAGAQLRPPPMRPVRPVVQHRSSSSSSSGVGSPAVTPTEKMFPNSSADKSGTM
Protein: Actin-4 (EC 3.6.4.-) (P53494)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. This is considered as one of the reproductive actins.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Actin-related protein 4
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 3
- F-actin-capping protein subunit beta
- Actin-related protein 9
- Tubulin beta-3 chain
- Chromatin structure-remodeling complex protein SYD
- Non-specific lipid transfer protein GPI-anchored 12
- Cyclase-associated protein 1
- Actin-related protein 2/3 complex subunit 2A
Sequence:
MADGEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVNNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDHLMKILTERGYSFTTTAEREIVRDMKEKLSYIALDFEQELETSKTSSSVEKSFELPDGQVITIGAERFRCPEVLFQPSMIGMENPGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFGGIGDRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF
Protein: General transcription factor IIH subunit 3 (General transcription factor IIH polypeptide 3) (F5GWD3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368090}.
Interaction partners:
Sequence:
MVSDEDELNLLVIVVDANPIWWGKQALKESQFTLSKCIDAVMVLGNSHLFMNRSNKLAVIASHIQESRFLYPGKNGRLGDFFGDPGNPPEFNPSGSKDGKYELLTSANEVIVEEIKDLMTKSDIKGQHTETLLAGSLAKALCYIHRMNKEVKDNQEMKSRILACDITGGLYLKVPQMPSLLQYLLWVFLPDQDQRSQLILPPPVHVDYRAACFCHRNLIEIGYVCSVCLSIFCNFSPICTTCETAFKISLPPVLKAKK
Protein: Fatty-acid amide hydrolase 2 (EC 3.5.1.99) (Amidase domain-containing protein) (Anandamide amidohydrolase 2) (Oleamide hydrolase 2) (Q6GMR7)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules. Hydrolyzes monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates.
Subcellular location: Membrane {ECO:0000305|PubMed:17015445}; Single-pass membrane protein {ECO:0000305}. Lipid droplet {ECO:0000269|PubMed:19926788}.
Interaction partners:
- Glutamyl-tRNA
- Bifunctional glutamate/proline--tRNA ligase
- Aspartate--tRNA ligase, mitochondrial
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Voltage-gated monoatomic cation channel TMEM109
- GMP synthase
- N-acylethanolamine-hydrolyzing acid amidase
- Delta-1-pyrroline-5-carboxylate synthase
- Bifunctional purine biosynthesis protein ATIC
- Pyruvate carboxylase, mitochondrial
Sequence:
MAPSFTARIQLFLLRALGFLIGLVGRAALVLGGPKFASKTPRPVTEPLLLLSGMQLAKLIRQRKVKCIDVVQAYINRIKDVNPMINGIVKYRFEEAMKEAHAVDQKLAEKQEDEATLENKWPFLGVPLTVKEAFQLQGMPNSSGLMNRRDAIAKTDATVVALLKGAGAIPLGITNCSELCMWYESSNKIYGRSNNPYDLQHIVGGSSGGEGCTLAAACSVIGVGSDIGGSIRMPAFFNGIFGHKPSPGVVPNKGQFPLAVGAQELFLCTGPMCRYAEDLAPMLKVMAGPGIKRLKLDTKVHLKDLKFYWMEHDGGSFLMSKVDQDLIMTQKKVVVHLETILGASVQHVKLKKMKYSFQLWIAMMSAKGHDGKEPVKFVDLLGDHGKHVSPLWELIKWCLGLSVYTIPSIGLALLEEKLRYSNEKYQKFKAVEESLRKELVDMLGDDGVFLYPSHPTVAPKHHVPLTRPFNFAYTGVFSALGLPVTQCPLGLNAKGLPLGIQVVAGPFNDHLTLAVAQYLEKTFGGWVCPGKF
Protein: Contig An02c0270, genomic contig (A2QDX9)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MSEGEKARTSGEVSRPEPTLPTVNPAVDKAEPPKPAFHPAVYVGVWITLSSSVILFNKHILDYAQFRFPIILTTWHLAFATFMTQLLARTTTLLDGRKTVKMTGRVYLRAIVPIGLFFSLSLICGNVTYLYLSVAFIQMLKATTPVAVLFATWGMGMAPVNLKVLMNVSIIVLGVIIASFGEIRFVFIGFLFQLGGIVFEATRLVMVQRLLSSAEYKMDPLVSLYYFAPVCAVMNGVTALFLEVPNLTMGHIYNVGVWTLLANAVVAFLLNVSVVFLIGKTSSLVMTLCGVLKDILLVAASMMIWQTPVTLTQFFGYSIALVGLVYYKLGGDKIKEYTGQANRAWAEYGVNHPAQRKFIVFGAILLIFFLLMGSMAPSYAPEQVASVKGMLGGATAGNA
Protein: Probable helicase HelY (EC 3.6.4.-) (P9WMR1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Large ribosomal subunit assembly factor BipA
- Sec-independent protein translocase protein TatC
- Protein PafC
- Hydrogenobyrinate a,c-diamide synthase
- Protein PafB
- GTPase Era
Sequence:
MTELAELDRFTAELPFSLDDFQQRACSALERGHGVLVCAPTGAGKTVVGEFAVHLALAAGSKCFYTTPLKALSNQKHTDLTARYGRDQIGLLTGDLSVNGNAPVVVMTTEVLRNMLYADSPALQGLSYVVMDEVHFLADRMRGPVWEEVILQLPDDVRVVSLSATVSNAEEFGGWIQTVRGDTTVVVDEHRPVPLWQHVLVGKRMFDLFDYRIGEAEGQPQVNRELLRHIAHRREADRMADWQPRRRGSGRPGFYRPPGRPEVIAKLDAEGLLPAITFVFSRAGCDAAVTQCLRSPLRLTSEEERARIAEVIDHRCGDLADSDLAVLGYYEWREGLLRGLAAHHAGMLPAFRHTVEELFTAGLVKAVFATETLALGINMPARTVVLERLVKFNGEQHMPLTPGEYTQLTGRAGRRGIDVEGHAVVIWHPEIEPSEVAGLASTRTFPLRSSFAPSYNMTINLVHRMGPQQAHRLLEQSFAQYQADRSVVGLVRGIERGNRILGEIAAELGGSDAPILEYARLRARVSELERAQARASRLQRRQAATDALAALRRGDIITITHGRRGGLAVVLESARDRDDPRPLVLTEHRWAGRISSADYSGTTPVGSMTLPKRVEHRQPRVRRDLASALRSAAAGLVIPAARRVSEAGGFHDPELESSREQLRRHPVHTSPGLEDQIRQAERYLRIERDNAQLERKVAAATNSLARTFDRFVGLLTEREFIDGPATDPVVTDDGRLLARIYSESDLLVAECLRTGAWEGLKPAELAGVVSAVVYETRGGDGQGAPFGADVPTPRLRQALTQTSRLSTTLRADEQAHRITPSREPDDGFVRVIYRWSRTGDLAAALAAADVNGSGSPLLAGDFVRWCRQVLDLLDQVRNAAPNPELRATAKRAIGDIRRGVVAVDAG
Protein: Uncharacterized protein At3g52155, chloroplastic (EC 3.1.3.-) (Q94BY1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MLSLQCLPPFFISVPNRSTNSCSTAPLRAVSDFAASPSTSISRRLILLRHAHSSWDDLSLRDHDRPLSKTGEADAAKVAQILSSLGWLPQLILSSDATRTRETLKSMQAQVDGFMEANVHFIPSFYSIAAMDGQTAEHLQNIISKYSTPDISTIMCMGHNKGWEEAASMLSGASIKLKTCNAALLQAFGNSWEEAFALSGPGGWKLEGLVAPDSSIFV
Protein: Rho-related GTP-binding protein RhoG (Sid 10750) (P84096)
Organism: Mus musculus (Mouse)
Function: Required for the formation of membrane ruffles during macropinocytosis. Plays a role in cell migration and is required for the formation of cup-like structures during trans-endothelial migration of leukocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Engulfment and cell motility protein 1
- Engulfment and cell motility protein 2
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Dedicator of cytokinesis protein 1
- Rho guanine nucleotide exchange factor 26
- Engulfment and cell motility protein 3
- Intersectin-1
- Rho GDP-dissociation inhibitor 1
- Proto-oncogene vav
- Rho GDP-dissociation inhibitor 3
Sequence:
MQSIKCVVVGDGAVGKTCLLICYTTNAFPKEYIPTVFDNYSAQSAVDGRTVNLNLWDTAGQEEYDRLRTLSYPQTNVFVICFSIASPPSYENVRHKWHPEVCHHCPDVPILLVGTKKDLRAQPDTLRRLKEQGQAPITPQQGQALAKQIHAVRYLECSALQQDGVKEVFAEAVRAVLNPTPIKRGRSCILL