wanglab/gogpt-training-data huggingface dataset:
Protein: Spermidine hydroxycinnamoyltransferase 2 (EC 2.3.1.-) (Q0ING3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from p-coumaryol-CoA to spermidine, to produce coumaroyl spermidine. Can use feruloyl-CoA as acyl donor. Contributes to the natural variation of spermidine-based phenolamides in rice cultivars.
Interaction partners:
- Nitrate reductase 1
- Nitrate reductase
- Nitrate reductase
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- 4-coumarate--CoA ligase
Sequence:
MKLDSFTARRGNPELVAPARATPRETKPLSDLDDHWDLRYLQPSLEFFRVVDGDRRPARPGDGIKAALAEALVYYYPIAGRLRELPTGHMLAVECTAEGVVFVEAEADVALEDFGEPLMPTFHGAEGFLCDVGDTRVIVGRPLFYLQITYLKCGGFVLGTYMCHCIADAFGTIQFLKAIVDIARGEAKPTTLPVWERELFLATSLQPHIKEDQKKLFDELESTTCDDIMVTMPTENMVSEYFILSQIDMAALRRHVPLNLNKTVTSFELLTAVTWRSRTIALGYRPCHIVRLMIVVNARGRWKKLPLGYYGNGLLCSVIETTVNDLCTNPLGHTIELVRKAKDEMKTEENMQLRVDLLPLWREKPYIKVQRIFEACDIKWIGQDTLDIGWAKRIGGGIPTVSPPNLTSYQFLCKNEKGEKSTVISMLLPQPAMDRFKKEMAAWLIE
Protein: Oxoeicosanoid receptor 1 (5-oxo-ETE G-protein coupled receptor) (G-protein coupled receptor 170) (G-protein coupled receptor R527) (G-protein coupled receptor TG1019) (Q8TDS5)
Organism: Homo sapiens (Human)
Function: Receptor for eicosanoids and polyunsaturated fatty acids such as 5-oxo-6E,8Z,11Z,14Z-eicosatetraenoic acid (5-OXO-ETE), 5(S)-hydroperoxy-6E,8Z,11Z,14Z-eicosatetraenoic acid (5(S)-HPETE) and arachidonic acid. Seems to be coupled to the G(i)/G(o), families of heteromeric G proteins.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MELHNLSSPSPSLSSSVLPPSFSPSPSSAPSAFTTVGGSSGGPCHPTSSSLVSAFLAPILALEFVLGLVGNSLALFIFCIHTRPWTSNTVFLVSLVAADFLLISNLPLRVDYYLLHETWRFGAAACKVNLFMLSTNRTASVVFLTAIALNRYLKVVQPHHVLSRASVGAAARVAGGLWVGILLLNGHLLLSTFSGPSCLSYRVGTKPSASLRWHQALYLLEFFLPLALILFAIVSIGLTIRNRGLGGQAGPQRAMRVLAMVVAVYTICFLPSIIFGMASMVAFWLSACRSLDLCTQLFHGSLAFTYLNSVLDPVLYCFSSPNFLHQSRALLGLTRGRQGPVSDESSYQPSRQWRYREASRKAEAIGKLKVQGEVSLEKEGSSQG
Protein: Probable oxidoreductase ENV9 (EC 1.1.1.-) (Late endosome and vacuole interface protein 9) (Q08651)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable dehydrogenase required for replication of Brome mosaic virus. Involved in vacuolar processing and morphology.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:14562095}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLDPRILPYYDPAVERKIAVVTGGNTGIGWYTVLHLYLHGFVVYICGRNSHKISKAIQEILAEAKKRCHEDDDGSSPGAGPGPSIQRLGSLHYIHLDLTDLKCVERAALKILKLEDHIDVLVNNAGIMAVPLEMTKDGFEVQLQTNYISHFIFTMRLLPLLRHCRGRIISLSSIGHHLEFMYWKLSKTWDYKPNMLFTWFRYAMSKTALIQCTKMLAIKYPDVLCLSVHPGLVMNTNLFSYWTRLPIVGIFFWLLFQVVGFFFGVSNEQGSLASLKCALDPNLSVEKDNGKYFTTGGKESKSSYVSNNVDEAASTWIWTVHQLRDRGFDI
Protein: Transcription factor bHLH78 (Basic helix-loop-helix protein 78) (AtbHLH78) (bHLH 78) (Transcription factor EN 86) (bHLH transcription factor bHLH078) (Q9FJL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds DNA to G box 5'-CACGTG-3' and to E-box 5'-CANNTG-3' (By similarity). Binds to chromatin DNA of the FT gene and promotes its expression, and thus triggers flowering in response to blue light.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Cryptochrome-2
- At2g15220/F15A23.4
- Pentatricopeptide repeat-containing protein At2g01860
- Adagio protein 2
- non-specific serine/threonine protein kinase
Sequence:
MDNELFMNTEFPPPPEMATHFEHQQSSSSAMMLNWALMDPNPHQDSSFLWEKSTEQQQQQSIFDSALSSLVSSPTPSNSNFSGGGGDGFLIRELIGKLGNIGNNNNNSGEIYGTPMSRSASCYATPMSSPPPPTNSNSQMMMNRTTPLTEFSADPGFAERAARFSCFGSRSFNGRTNTNLPINNGNNMVNNSGKLTRVSSTPALKALVSPEVTPGGEFSRKRKSVPKGKSKENPISTASPSPSFSKTAEKNGGKGGSKSSEEKGGKRRREEEDDEEEEGEGEGNKSNNTKPPEPPKDYIHVRARRGQATDSHSLAERVRREKIGERMKLLQDLVPGCNKVTGKALMLDEIINYVQSLQRQVEFLSMKLSSVNDTRLDFNVDALVSKDVMIPSSNNRLHEEGLQSKSSSHHHQQQLNIYNNNSQLLPNISSNNMMLQSPMNSLETSTLARSFTHLPTLTQFTDSISQYQMFSEEDLQSIVGMGVAENPNNESQHMKIEL
Protein: Mitochondrial division protein fszA (Q54Z54)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Probably involved in mitochondrion division process. When overexpressed, induces mitochondrial tubule formation. Binds to and hydrolyzes GTP (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:14665465}.
Interaction partners:
- Dynamin-B
- Dynamin-A
Sequence:
MSQFMIRYQIINLSKVFNSPKSLNFIKRYTTSTASTTTTTTNDDSNWISTPNITVCGIGGGGCNSVNNMINKELYGIDFVVANTDAQALAISCSRKMVQLGKTLTRGLGAGAVPEVGKKATEESIEELMNQIGDTQMLFVTAGMGGGTGTGGAAVIASAAKAKGILTVGIVTKPFHFEGKHRMKLAEQGLIELEKSVDSLIVIPNEKLMEQSQELYIGNAFQMVDDVLYNSIRGISDILVKPGLINLDFADVRSIMCNSGKALMGVGEGEGKGRDAIAANIALNNPLLENINISGAKGVLLNIAGSDLKLQEVDHIVSLVSSKVDPSANIIFGSTFDQQLEGKIRVTLIVTGMDQLIQQQQQQQKQTKIESQVEQKLHSTTIVDQELKPIEPQKSIIIEEEQEEQQQPKPIIPGIFVEQELLTTTTTANITPSQQKQESLTQNNIFSPPQQQQQQPSINLQPNYQQLYQQLYQQQQQQLQQQQPISFLKRLSNLFFTNGNNNKPYNNNKNTPGSNYE
Protein: Zinc finger E-box-binding homeobox 1 (F6TDF5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADGPRCKRRKQANPRRNNVTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDTGKEGQEILGPEAQADEAGCTVKDDECESDAENEQNHDPNVEEFLQQQDTAVIFPEAPEEDQRQGTPEASGHDENGTPDAFSQLLTCPYCDRGYKRFTSLKEHIKYRHEKNEDNFSCSLCSYTFAYRTQLERHMTSHKSGRDQRHVTQSGCNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHIS
Protein: Uncharacterized protein (Q386X7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSGCGRKHRAKHLTRQFLDASAWCGLGEGEVLAVCTEAPQGQHVRVIFVEPPLSAGTDAATVEKHNGASPSADKAEEHLVFIPGKFRKVIWLAVRDIVVVADRSTVASKPSPDQLKHFFREQPEWKRLVGAVQDYVERNRREMEQQPQYAKTAHTTTSTLPKVAYPLPSCEGYQSSVEGSSDIGELEHMNPNRNNIRHKVPFFFGEEEEEEEGGEEEGSDEETGIE
Protein: Multidrug resistance-associated protein 1 (EC 3.6.3.44) (Q9U0N4)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Multidrug resistance protein 1
Sequence:
MTTYKENVGISNKGNKKKKSCQNISFLNFLSFDWIRPLINDLIKGDIQELPNICRNFDVPYYASKLEENLRDIEVEDSEFYSEKNSSNEHVLHHCNSNDASEKKVYNVYYHNILWSILKTFKFRIILIISFYILETLIVTLGGKFIDYYMRILEGQKIPVYISFLKDFKVFSGLVVVMIMFFHLFFEALLHFYFHLFTINLKVSLMYFLYKINLCSNNNHLQNPDAFYNTYRKFSSQTEIDEISRDFLSIGKNASSSSSGIKNNNKNIDNNKFVENDYIINFIKSTKKMEKDSLNENRSLPNVNIYNIMFSDVPSVTFFVTSCINLFNVFVKIFMSFYVFHIKIGSNSVGIAIWLSIALYSAMILFEFLPSLFKSKYLIYRDKRIDNMHHVLKEFKLIKMFNWESFAFKYINIFRMKEMKYCKIRLYLSNIGVFISSISSDIVEVVIFFIYLKDRLNKKEEIKFTSIIMPLYVYKILISNVANFPNLVNNVMEGIVNIKRLNNYINDHLYYNDIKNYFMYRTRYNEDYNIVVDKTFLQNENITSHDDGTSHNLKHLKNVIKNKLTNMFKYFFFYHKMNYHKNIINKQILSGLLKNVDDNTNKKICFQEHKSNSTYNYNSSHIHEKKEEYENIHNSSNSTMSNEFKEKKKNNEYIIKLENCSFGLSYDNKCDNDHILKNINFNLKRNSLAIIIGNVGSGKSAFFHSILGDFNMTHGNLYIENFFKKMPILYVPQNSWLFMGNIRSMILFGNEYNPLIYKYTILQSELLNDLSTIEHGDMKYINDDHNLSKGQKVRICLARALYEHYIHMHKLCTDYEKKLIQPNEILDKDLINNKNISSYNNKKSKLVNYNIPFNENYLQKCLMDDNNFYLYLLDDIFTSLDPSISKKIFSNLFCKEDNISFKDNCSFIISMNKSTLDNFLIEDILDNVQYEVNIFEIQDKTLKYRGNISEYMEKNNLNITKESHWGYSNLNTIDYTRIKLFDEVELNHVKHSNKMIYKEAYFVKGNTESVSFEIDSINKEYIKKMKKKNYKKEHMNKNNKDNNNNNNNSNKDDHININMNDNHRNYNDINLGPNSTDDSPTVSSLGNEYTLDTYTSNNSDKEEIVKPLYKDTHEEFNKSSSMPFVKSSSNMINNPSNFKYEDNSSSFKGSISLETYLWYFQQVGFVLLTSVVIFMLISIFTDEIKFVFLTMMSIISKNNKEHSDTILQKQVRYLEYFVILPIISLVTSGICFSMIIYGNITSAIKVHNNILYSILNAPLYIFYNNNLGNIINRFIIDISAFDYGFLKRIYKAFFIFFRCILSSLLIIYMIRDCIFIFPFVIILIYFFVFKRFSRGCKEAQRLYLSCHTPLCNIYSNALSGKNIINIYKKNTYHLDVYEHYINNFRISYFFKWLINIWASLYIKIFILLLTTYIIMHPHLYASGIIKLYKEKNYVRILSTLGYCISFSARLGVIIKFLLCDYTHIEKEMCCVQRLEEFAKISNKENASMNKENELNVITTQTYKEKNENISDKISAIVEYKNVSLSSIINSSQDDESKKKYGIKFENVYVSYKKKIPLVNGTYKYIDEEPSLKNINMYALKNQKIGIVGKSGAGKSTILLSILGLINISQGKITVEGRDIRTYNRKGEDSIIGILAQSSFVFYNWNIRTFIDPYNNFTDDEIVHALKLNGINLGKNDLYKYMHKQDMKSNYKKIIQTSKVINQSNDNTILLTNDCIRYLSLVRLYLNRHKYKIILIDEIPIFNLNNSVHDELNSFLIGKAKSFNYIIRNHFPNNTVLIISHHANTLSCCDYIYVLRKGEITYRCSYEDVKTQSELSHLLEMDD
Protein: Matrilysin (EC 3.4.24.23) (Matrin) (Matrix metalloproteinase-7) (MMP-7) (Pump-1 protease) (Uterine metalloproteinase) (P09237)
Organism: Homo sapiens (Human)
Function: Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
- CD44 antigen
- 72 kDa type IV collagenase
- Metalloproteinase inhibitor 2
- Osteopontin
- Metalloproteinase inhibitor 1
- Metalloproteinase inhibitor 3
- Matrix metalloproteinase-9
- Interstitial collagenase
- Nidogen-1
- Stromelysin-2
Sequence:
MRLTVLCAVCLLPGSLALPLPQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLKEMQKFFGLPITGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGKRSNSRKK
Protein: 4-dimethylallyltryptophan N-methyltransferase easF (EC 2.1.1.261) (4-dimethylallyltryptophan methyltransferase) (Ergot alkaloid synthesis protein F) (Q4WZ60)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: 4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A. Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus.
Interaction partners:
- Tryptophan dimethylallyltransferase
- Chanoclavine-I dehydrogenase easD
- Catalase easC
- FAD-linked oxidoreductase easE
- Festuclavine dehydrogenase easG
- Chanoclavine-I aldehyde reductase easA
Sequence:
MTISAPPIIDIRQAGLESSIPDQVVEGLTKEVKTLPALLFYSTKGIQHWNRHSHAADFYPRHEELCILKAEASKMAASIAQDSLVIDMGSASMDKVILLLEALEEQKKSITYYALDLSYSELASNFQAIPVDRFHYVRFAALHGTFDDGLHWLQNAPDIRNRPRCILLFGLTIGNFSRDNAASFLRNIAQSALSTSPTQSSIIVSLDSCKLPTKILRAYTADGVVPFALASLSYANSLFHPKGDRKIFNEEDWYFHSEWNHALGRHEASLITQSKDIQLGAPLETVIVRRDEKIRFGCSYKYDKAERDQLFHSAGLEDAAVWTAPDCDVAFYQLRLRLN
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (E3TF51)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Interaction partners:
- Histone H2A
- Histone H2A
- Histone H2A
- Histone H2A
- Histone H2A
- Histone H2A
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor SYF1
- Nuclear pore complex protein Nup214
- SNW domain-containing protein 1
Sequence:
MSNPKVFFDIAIDGKSAGRIVIELRADVVPKTAENFRALCTGEKGFGYKGSGFHRVIPGFMCQGGDFTNHNGTGGKSIYGNKFADENFTLKHTGPGIMSMANAGPNTNGSQFFICTEKTSWLDGKHVVFGSVVQGMEVVRAVEGKGSNSGKCSAKIVIADCGQL
Protein: F-box only protein 41 (Q8TF61)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
Sequence:
MASLDLPYRCPRCGEHKRFRSLSSLRAHLEYSHTYETLYILSKTNSICDGAAAAAAAAAAASGFPLAPEPAALLAVPGARREVFESTSFQGKEQAAGPSPAAPHLLHHHHHHAPLAHFPGDLVPASLPCEELAEPGLVPAAAARYALREIEIPLGELFARKSVASSACSTPPPGPGPGPCPGPASASPASPSPADVAYEEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQVISSSCGSTPSASLGRGGGGGGAGPNARGPGRMREHHVGPAVPNTYAVSRHGSSPSTGASSRVPAASQSSGCYDSDSLELPRPEEGAPEDSGPGGLGTRAQAANGGSERSQPPRSSGLRRQAIQNWQRRPRRHSTEGEEGDVSDVGSRTTESEAEGPLDAPRPGPAMAGPLSSCRLSARPEGGSGRGRRAERVSPSRSNEVISPEILKMRAALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRVLLENARVCSKFLAMLAQWCTQAHSLTLQNLKPRQRGKKESKEEYARSTRGCLEAGLESLLKAAGGNLLILRISHCPNILTDRSLWLASCYCRALQAVTYRSATDPVGHEVIWALGAGCREIVSLQVAPLHPCQQPTRFSNRCLQMIGRCWPHLRALGVGGAGCGVQGLASLARNCMRLQVLELDHVSEITQEVAAEVCREGLKGLEMLVLTATPVTPKALLHFNSICRNLKSIVVQIGIADYFKEPSSPEAQKLFEDMVTKLQALRRRPGFSKILHIKVEGGC
Protein: Cytochrome b (Complex III subunit 3) (Complex III subunit III) (Cytochrome b-c1 complex subunit 3) (Ubiquinol-cytochrome-c reductase complex cytochrome b subunit) (Q95862)
Organism: Neogobius melanostomus (round goby)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
RKTHPLLKIANHALVDLPAPSNISAWWNFGSLLGLCLIAQIVTGLFLAMHYTSDITTAFSSVTHICRDVNFGWLIRNMXANGASFFFICIYLHIGRGLYYGSYLYKETWNIGVVLLLLVMMT
Protein: BcDNA.GH02250 (GEO05420p1) (Ocnus (EC 3.9.1.3)) (Q9Y170)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH14656p
- Cytosol aminopeptidase
- Cytosol aminopeptidase
- Cytosol aminopeptidase
- AT18965p
- Protamine A, isoform A
- Male-specific sperm protein Mst84Da
- 10 kDa heat shock protein, mitochondrial
- AT22380p
- AT13777p
Sequence:
MKTLNLLAPVSQLLKPLRRQSSSRVNALLINVPRVQLSKGKNKYLLMMIHMHGLTRFGRTIVRGSASKDHEEIFEEIQKEMDKIGICAKCLGGGFISNKEDKKVMKIYGCCKTFGEAPHGRTKDILLSWTKFQHYNIILPKKNLNAYQ
Protein: SD03374p (Q95TH7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLLHVSNRSAAVPKKAATPQVDFPALPGKGNKKNLRNLEEDMLPSGSPVPMANISAKHRSLADDYVSVASPSTFQKLQMVQKEEDEAKARQEALKKSAPKLTAAEFPSLGPSASASSSRATAPKPSSGSPSLNWSKPANEKKQRELENRKAKVAPAPVLPSPTSKPAPKASNNNVQEQQANKKDKKQKDKKSNQENQPKTAKPKERNNNNEQKTNGAPSTPIRAPPGLKPGGPLKPPPGFVSNVTANSVAKLPNNLTFTNSLGESYDIVPSPYTYTDPPDTEVRNQKLVDEVMSLLKTPEALNEFRLLSSKFRDGSCSGQAYYEHCQCAMLSSFYNLFPELLAMLPDISKQQELYLVHKQHLNKVCKQILITADLKSHQQAHELTKNFPVLGSSASNTHRN
Protein: Zinc finger MYND domain-containing protein 10 (Q5FWU8)
Organism: Xenopus laevis (African clawed frog)
Function: Plays a role in axonemal structure organization and motility. Involved in axonemal pre-assembly of inner and outer dynein arms (IDA and ODA, respectively) for proper axoneme building for cilia motility (By similarity). May act by indirectly regulating transcription of dynein proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23891469}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23891469}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q6AXZ5}. Apical cell membrane {ECO:0000250|UniProtKB:Q99ML0}. Dynein axonemal particle {ECO:0000269|PubMed:30561330, ECO:0000269|PubMed:33263282}. Note=Localizes both to the basal body and the striated rootlet, an appendage that projects away from the basal body into the cytoplasm.
Interaction partners:
Sequence:
MVQSLQTFSVRDIASGGWFKQHEYIEKLNMQAILNASAGQEEMIKDLLVTHGKIPTLIHELISVEIWKLKVFHVLCQLQDFQPKSTFPLYMVIHHEATIINLLETIFFHKEVCESAEDLTLDLIDYCYRKLTLLASQSSDRRTLSQNRLLPHTANEASSLEELKQQAEALEFDIALKCLSVTRYISDHIDSLPLSVMNRLLNTHNLPCLLVELLHQSPWTQSEKGQLQKYESGRWYPVPAEDQLKMTKLDGQAWIALYNLLLRPECQQKYNINSFTKGQLLKLRSFLTEVLLDQLPNLVDLQRFLSHLSVSEPTPPKKELILEQVPEVWDSIINENSGKWKAIAKYQVKQAFSPSEEDLRSQAKRWAQTYNMDVMEALVPEKPKCGSCGSEASKRCSRCQSEWYCKRECQVKHWQKHKKACDMVSEAMKNMQEEIQKEA
Protein: Hephaestus, isoform Q (E1JJ45)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADEISATSMVSCYTVTPPQMRGRMVYVQFSNHRELKTDQGHNNSTAHSDYSVQSPASGSPLPLSAAANATSNNANSSSDSNSAMGILQNTSAVNAGGNTNAAGGPNTVLRVIVESLMYPVSLDILHQIFQRYGKVLKIVTFTKNNSFQALIQYPDANSAQHAKSLLDGQNIYNGCCTLRIDNSKLTALNVKYNNDKSRDFTNPALPPGEPGVDIMPTAGGLMNTNDLLLIAARQRPSLSGDKIVNGLGAPGVLPPFALGLGTPLTGGYNNALPNLAAFSLANSGALQTTAPAMRGYSNVLLVSNLNEEMVTPDALFTLFGVYGDVQRVKILYNKKDSALIQMAEPQQAYLAMSHLDKLRLWGKPIRVMASKHQAVQLPKEGQPDAGLTRDYSQNPLHRFKKPGSKNYQNIYPPSATLHLSNIPSSCSEDDIKEAFTSNSFEVKAFKFFPKDRKMALLQLLSVEEAVLALIKMHNHQLSESNHLRVSFSKSNI
Protein: T-complex protein 1 subunit beta (CCT-beta) (B6V9S9)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MASLSLAPVNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGREASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAETLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNVTAGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPDHHPC
Protein: Fructose-bisphosphate aldolase 1, cytoplasmic (EC 4.1.2.13) (Cytoplasmic aldolase) (cALD) (Gravity-specific protein GSC 233) (P17784)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Fructose-bisphosphate aldolase that plays a key role in glycolysis and gluconeogenesis (By similarity). Involved in gibberellin-mediated root growth. May be regulated by CDPK13. Associates with vacuolar proton ATPase (V-ATPase) and may regulate the V-ATPase-mediated control of root cell elongation.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9SJQ9}.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Sedoheptulose-1,7-bisphosphatase, chloroplastic
- Os01g0926300 protein
- transketolase
- transketolase
- NADP-dependent glyceraldehyde-3-phosphate dehydrogenase])
- Glyceraldehyde-3-phosphate dehydrogenase
- phosphoglucomutase
- Fructose-1,6-bisphosphatase, chloroplastic
- Os09g0535000 protein
Sequence:
MSAYCGKYKDELIKNAAYIGTPGKGILAADESTGTIGKRFASINVENVEENRRSLRELLFCTPGALQYLSGVILFEETLYQKTKDGKPFVDVLKEGGVLPGIKVDKGTIEVAGTEKETTTQGHDDLGKRCAKYYEAGARFAKWRAVLKIGPNEPSQLAIDLNAQGLARYAIICQENGLVPIVEPEILVDGPHDIDRCAYVSEVVLAACYKALNEHHVLLEGTLLKPNMVTPGSDAKKVSPEVIAEYTVRTLQRTVPAAVPAIVFLSGGQSEEEATLNLNAMNKLSTKKPWSLSFSFGRALQQSTLKAWSGKAENIEKARAAFLTRCKANSEATLGTYKGDAVLGEGASESLHVKDYKY
Protein: Caveolin-2 (Q66WT7)
Organism: Bos taurus (Bovine)
Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15370296}. Cytoplasm {ECO:0000269|PubMed:15370296}. Golgi apparatus membrane {ECO:0000269|PubMed:15370296}; Peripheral membrane protein {ECO:0000269|PubMed:15370296}. Cell membrane {ECO:0000269|PubMed:15370296}; Peripheral membrane protein {ECO:0000269|PubMed:15370296}. Membrane, caveola {ECO:0000269|PubMed:15370296}; Peripheral membrane protein {ECO:0000269|PubMed:15370296}. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin. Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments (By similarity). {ECO:0000250}.
Interaction partners:
- Caveolin-1
- Caveolin-3
- Tyrosine-protein kinase
- Tyrosine-protein kinase Fyn
- Receptor protein-tyrosine kinase
- Integrin beta-5
- Integrin beta-1
- CALML5 protein
- Integrin beta
- Calmodulin-like protein 4
Sequence:
MGLETEKADVQLFMDDDSYSRHSSVDYADPDKFVDPGSDRDPHRLNSHLKVGFEDVIAEPVSTHSFDKVWICSHALFEMSKYVIYKFLTVFLAIPLAFAAGILFATLSCLHIWIIMPFVKTCLMVLPSVQTIWKSVTDVVIAPLCTSIGRSFSSVSLQLSHD
Protein: Probable cyclic di-GMP phosphodiesterase PdeN (EC 3.1.4.52) (P76446)
Organism: Escherichia coli (strain K12)
Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable diguanylate cyclase DgcC
- Diguanylate cyclase DgcP
- Diguanylate cyclase DgcM
- Diguanylate cyclase DgcN
- Diguanylate cyclase DosC
- Probable diguanylate cyclase CdgI
- Probable diguanylate cyclase DgcJ
- Probable diguanylate cyclase DgcT
- Probable diguanylate cyclase DgcI
- RNase E specificity factor CsrD
Sequence:
MFIRAPNFGRKLLLTCIVAGVMIAILVSCLQFLVAWHKHEVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQANPELTARAAFSMNVRTFVLVKDKKTFCSSATGEMDIPLNELIPALDINKNVDMAILPGTPMVPNKPAIVIWYRNPLLKNSGVFAALNLNLTPSLFYSSRQEDYDGVALIIGNTALSTFSSRLMNVNELTDMPVRETKIAGIPLTVRLYADDWTWNDVWYAFLLGGMSGTVVGLLCYYLMSVRMRPGREIMTAIKREQFYVAYQPVVDTQALRVTGLEVLLRWRHPVAGEIPPDAFINFAESQKMIVPLTQHLFELIARDAAELEKVLPVGVKFGINIAPDHLHSESFKADIQKLLTSLPAHHFQIVLEITERDMLKEQEATQLFAWLHSVGVEIAIDDFGTGHSALIYLERFTLDYLKIDRGFINAIGTETITSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLSERGVNFMQGYWISRPLPLDDFVRWLKKPYTPQW
Protein: Dehydration-responsive element-binding protein 1F (Protein DREB1F) (Q9LN86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates cold or dehydration-inducible transcription. CBF/DREB1 factors play a key role in freezing tolerance and cold acclimation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Gibberellin 2-beta-dioxygenase 7
- Transcription factor bHLH121
- LOB domain-containing protein 30
- Protein SPIRAL1-like 5
- Potassium transporter 5
- Protein SPIRAL1-like 2
Sequence:
MNNDDIILAEMRPKKRAGRRVFKETRHPVYRGIRRRNGDKWVCEVREPTHQRRIWLGTYPTADMAARAHDVAVLALRGRSACLNFADSAWRLPVPESNDPDVIRRVAAEAAEMFRPVDLESGITVLPCAGDDVDLGFGSGSGSGSGSEERNSSSYGFGDYEEVSTTMMRLAEGPLMSPPRSYMEDMTPTNVYTEEEMCYEDMSLWSYRY