wanglab/gogpt-training-data huggingface dataset:
Protein: (-)-beta-phellandrene synthase 1, chloroplastic (EC 4.2.3.52) (Terpene synthase (-)betaphell1) (PbTPS-(-)betaphell1) (R9QMW7)
Organism: Pinus banksiana (Jack pine) (Pinus divaricata)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (-)-beta-phellandrene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MALALVSVAPLVSMRRSLFSSPYELKSIDKTIPNLVMCRKRMLGRPSIRVSSTASVSNDDGVRRRVGDYRYNHWDEDLIDSLATSYEAPSYLKRADTLVEAIKDRFNSMGVDDGERMSPLTDLYQRLWMVDSVERLGIDRHFQNEIKSALDYVFSYWKEKGIGRGRQSAVTDLNSTALGLRTLRLHGYPVSSDVLENFKDHNGQFTCSGIQTEGEIRGVLNLFRASLIAFPGEKVMEEAEIFSTMYLKHALQKIAVSSLSQEIEYLLEYGWHTNPPRLEARMYMEVFPQDTIYEQKLVELAKVEFNIFHSLQKRELQSLTRWWKHYGFPQLSFTRHIHVEYYTFGSCIATDPKQSAFRLCFAKMSYFVTVLDDIYDTYGTMEELELFTAAIKRWDPSVVDCLPEYMKGVYMAVYDTVNEMAKEAEKVQGRDTLNYVRQAWELYIDAYMPEAKWISSGYLPTFQEYLDNSKISFGTRITILQPILTLGEPLPHEILQEIDFPAKFNDLISVILRLKGDTRCYKADRARGEEASSVSCYMKDNAGITEEDAIHCINDMVNNLLKELNWELLKPDSNVPISCRKAAFDICRIFHHGYKYRDGYGDATIEVKNLVKRTVLEPVPL
Protein: Nuclear factor NF-kappa-B p105 subunit (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit] (Q04861)
Organism: Gallus gallus (Chicken)
Function: P105 is the precursor of the p50 subunit of the nuclear factor NF-kappa-B, which binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. The precursor protein itself does not bind to DNA.
Subcellular location: [Nuclear factor NF-kappa-B p105 subunit]: Cytoplasm {ECO:0000250|UniProtKB:P19838}.; SUBCELLULAR LOCATION: [Nuclear factor NF-kappa-B p50 subunit]: Nucleus {ECO:0000250|UniProtKB:P19838}. Cytoplasm {ECO:0000250|UniProtKB:P19838}. Note=Association with NFKBIA inhibitor (I-kappa-B), promotes its retention in the cytoplasm in an inactive form. Translocates into the nucleus following NFKBIA degradation. {ECO:0000250|UniProtKB:P19838}.
Interaction partners:
- NF-kappa-B inhibitor alpha
- Transcription factor p65
- Proto-oncogene c-Rel
- Mitogen-activated protein kinase kinase kinase 8
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- TNFAIP3-interacting protein 2
- Importin subunit alpha
- NFKB inhibitor epsilon.
- Interleukin-1
- Nuclear factor NF-kappa-B p100 subunit
Sequence:
MAGEDPYIMGVSDPQMFAMDQLMGMSTIFNNTGYITSDLPLRTADGPYLQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGKFCEDGVCTVNAGPKDMVVGFANLGILHVTKKKVFETLETRMIDACKKGYNPGLLVHPELGYLQAEGCGDRQLTEREREIIRQAAVQQTKEMDLSVVRLMFTAFLPDSNGGFTRRLDPVISDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEDENGGMWEGFGDFSPTDVHRQFAIVFKTPKYRDVNITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDGYGGGSGAGGGGMFGGGGGGAGSGFSYPSYGYSAFGGMHFHPGTTKSNAGMKHELSNSTVKKDEESSDKQSDKWDTKHDVKVETVEKNECRTSGHNEEKEDASLCCKDEGNKPKCGCQDGLFLEKAMQLAKRHCNALFDYAVTGDVRMLLAVQRHLTAVQDDNGDNVLHLSIIHLHRELVKNLLEVMPDMNYNNIINMRNDLYQTPLHLAVITKQAEVVEDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSLLLKHQKASSMIDLSNGEGLSAIHMVVTANSLSCLKLLIAAGVDVNAQEQKSGRTALHLAVEQENVPLAGCLLLEGDADVDSTTYDGTTPLHIAAGRGFTKLAAVLKAAGADPHVENFEPLFDVEEDVKDDDDDEGIVPGTTPLDMAANWEVYDILNGKPYIAAAAVSEDLLSQGPLRELNESSKQQLYKLLETPDPSKNWSTLAEKLGLGILNNAFRLSPSPSKTLLDNYKISGGTVQELIAALTQMDHTEAIEVIQKALSSSQRQSHQEDNTIEAFPSLSPTSFAKEETGELYNHKFQDPESTCDSGVETSFRKLSFTYSDSLNSKSSITLSKMTLGYRKAQCKAVIYLTR
Protein: Vacuolar protein sorting-associated protein 33 (Protein SLP1) (Vacuolar morphogenesis protein 5) (P20795)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for vacuolar biogenesis, maturation and function. Involved in the sorting of vacuolar proteins from the Golgi apparatus and their targeting to the vacuole. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion.
Subcellular location: Vacuole.
Interaction partners:
- Vacuolar protein sorting-associated protein 41
- E3 ubiquitin-protein ligase PEP5
- Vacuolar membrane protein PEP3
- Vacuolar protein sorting-associated protein 3
- Vacuolar morphogenesis protein 6
- Vacuolar morphogenesis protein 7
- Vacuolar protein sorting-associated protein 16
- Ypt/Rab-type GTPase YPT7
- t-SNARE VTI1
- Vacuolar v-SNARE NYV1
Sequence:
MNRFWNTKKFSLTNADGLCATLNEISQNDEVLVVQPSVLPVLNSLLTFQDLTQSTPVRKITLLDDQLSDDLPSALGSVPQMDLIFLIDVRTSLRLPPQLLDAAQKHNLSSLHIIYCRWKPSFQNTLEDTEQWQKDGFDLNSKKTHFPNVIESQLKELSNEYTLYPWDLLPFPQIDENVLLTHSLYNMENVNMYYPNLRSLQSATESILVDDMVNSLQSLIFETNSIITNVVSIGNLSKRCSHLLKKRIDEHQTENDLFIKGTLYGERTNCGLEMDLIILERNTDPITPLLTQLTYAGILDDLYEFNSGIKIKEKDMNFNYKEDKIWNDLKFLNFGSIGPQLNKLAKELQTQYDTRHKAESVHEIKEFVDSLGSLQQRQAFLKNHTTLSSDVLKVVETEEYGSFNKILELELEILMGNTLNNDIEDIILELQYQYEVDQKKILRLICLLSLCKNSLREKDYEYLRTFMIDSWGIEKCFQLESLAELGFFTSKTGKTDLHITTSKSTRLQKEYRYISQWFNTVPIEDEHAADKITNENDDFSEATFAYSGVVPLTMRLVQMLYDRSILFHNYSSQQPFILSREPRVSQTEDLIEQLYGDSHAIEESIWVPGTITKKINASIKSNNRRSIDGSNGTFHAAEDIALVVFLGGVTMGEIAIMKHLQKILGKKGINKRFIIIADGLINGTRIMNSIS
Protein: cAMP-responsive element modulator (Inducible cAMP early repressor) (ICER) (Q03060)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator that binds the cAMP response element (CRE), a sequence present in many viral and cellular promoters. Isoforms are either transcriptional activators or repressors. Plays a role in spermatogenesis and is involved in spermatid maturation.
Subcellular location: Nucleus.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Cyclic AMP-responsive element-binding protein 1
- Cyclic AMP-dependent transcription factor ATF-2
- Four and a half LIM domains protein 5
- Cyclic AMP-responsive element-binding protein 3-like protein 4
- Cyclic AMP-responsive element-binding protein 3
- Apoptosis regulator Bcl-2
- Cyclic AMP-dependent transcription factor ATF-4
- Cyclic AMP-responsive element-binding protein 3-like protein 2
- Cyclic AMP-responsive element-binding protein 5
- Cyclic AMP-responsive element-binding protein 3-like protein 3
Sequence:
MTMETVESQHDGSITASLTESKSAHVQTQTGQNSIPALAQVSVAGSGTRRGSPAVTLVQLPSGQTIHVQGVIQTPQPWVIQSSEIHTVQVAAIAETDESAESEGVIDSHKRREILSRRPSYRKILNELSSDVPGVPKIEEERSEEEGTPPSIATMAVPTSIYQTSTGQYIAIAQGGTIQISNPGSDGVQGLQALTMTNSGAPPPGATIVQYAAQSADGTQQFFVPGSQVVVQDEETELAPSHMAAATGDMPTYQIRAPTAALPQGVVMAASPGSLHSPQQLAEEATRKRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDICSPKTDY
Protein: Fimbrial protein PapE (P08407)
Organism: Escherichia coli
Function: Repeated PapE subunits make up the thin (2 nm in diameter) tip fibrillum of the P pilus. Subunits are arranged in a open helical conformation. Pili with a defective papE gene have low adhesive capacity or none; however, the binding property of the whole cell is not affected. Pili are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, and enable bacteria to colonize the epithelium of specific host organs.
Subcellular location: Secreted. Fimbrium. Note=At the tip of the P pilus.
Interaction partners:
Sequence:
MKKIRGLCLPVMLGAVLMSQHVHAVDNLTFRGKLIIPACTVSNTTVDWQDVEIQTLSQNGNHEKEFTVNMRCPYNLGTMKVTITATNTYNNAILVQNTSNTSSDGLLVYLYNSNAGNIGTAITLGTPFTPGKITGNNADKTISLHAKLGYKGNMQNLIAGPFSATATLVASYS
Protein: Fatty acyl-CoA reductase (EC 1.2.1.84) (Q9W508)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Fatty acid desaturase domain-containing protein
- Elongation of very long chain fatty acids protein
- Fatty acid synthase
Sequence:
MHHPLSGEMEEFFEDSEIFVTGGSGVVGKALVEKLLRSCNVRRIYVLLRPRKQLTAEQRLVRLRQATVFHVLAVQKPEELDKIVAVPGDVSLPGLGIDPSMMQRMKGVSLVYHCAATVRFDEPLREAVRLNVGGTLEALKFAETLPQLRAFIHVSTFYSNPYLTRVEPKYYSSPMDWRLCLRMIDDVADDGMLNALTRKLIMGFPNTYTFTKNLAESLVNDYRHRLPVIVYRPSIVLFAVEDPSPGFSPSLMGAMGLFALVGAGILKTVYLGKDIRLDITPQDIGIKSMLCYTKMGYDIYRQGPPADLPVFLSSSCTHVPHTFTQIAEQMDTLDLWRDVAFEKNLMIPGCHYTDKRWAYQFLVFTKQILPALILDLLLRIFGQKPVLMSAVRKAYQTLEVMQPFMFNNWDSPGVSDMETLSKHGEGSAFNFDAFNHPDIHGLVIQSCSNMLHSIRTHLLREDPKTLERSKRILRIKVFLYRLLRLFLLYKLILWLWRSYLAHLF
Protein: Neuroligin-3 (Gliotactin homolog) (Q8BYM5)
Organism: Mus musculus (Mouse)
Function: Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. May also play a role in glia-glia or glia-neuron interactions in the developing peripheral nervous system.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17897391}; Single-pass type I membrane protein {ECO:0000269|PubMed:17897391}. Synapse {ECO:0000269|PubMed:17897391}. Note=Detected at both glutamatergic and GABAergic synapses.
Interaction partners:
- Neurexin-3
- Neurexin-1
- Neurexin-2
- Disks large homolog 4
- SH3 and multiple ankyrin repeat domains protein 3
- Neuroligin-1
- Receptor-type tyrosine-protein phosphatase delta
- Neuroligin-2
- SH3 and multiple ankyrin repeat domains protein 1
- SH3 and multiple ankyrin repeat domains protein 2
Sequence:
MWLQPSLSLSPTPTVGRSLCLTLGFLSLVLRASTQAPAPTVNTHFGKLRGARVPLPSEILGPVDQYLGVPYAAPPIGEKRFLPPEPPPSWSGIRNATHFPPVCPQNIHTAVPEVMLPVWFTANLDIVATYIQEPNEDCLYLNVYVPTEDGSGAKKQGEDLADNDGDEDEDIRDSGAKPVMVYIHGGSYMEGTGNMIDGSVLASYGNVIVITLNYRVGVLGFLSTGDQAAKGNYGLLDQIQALRWVSENIAFFGGDPRRITVFGSGIGASCVSLLTLSHHSEGLFQRAIIQSGSALSSWAVNYQPVKYTSLLADKVGCNVLDTVDMVDCLRQKSAKELVEQDIQPARYHVAFGPVIDGDVIPDDPEILMEQGEFLNYDIMLGVNQGEGLKFVEGVVDPEDGVSGTDFDYSVSNFVDNLYGYPEGKDTLRETIKFMYTDWADRDNPETRRKTLVALFTDHQWVEPSVVTADLHARYGSPTYFYAFYHHCQSLMKPAWSDAAHGDEVPYVFGVPMVGPTDLFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNKPVPQDTKFIHTKANRFEEVAWSKYNPRDQLYLHIGLKPRVRDHYRATKVAFWKHLVPHLYNLHDMFHYTSTTTKVPPPDTTHSSHITRRPNGKTWSTKRPAISPAYSNENAPGSWNGDQDAGPLLVENPRDYSTELSVTIAVGASLLFLNVLAFAALYYRKDKRRQEPLRQPSPQRGTGAPELGTAPEEELAALQLGPTHHECEAGPPHDTLRLTALPDYTLTLRRSPDDIPLMTPNTITMIPNSLVGLQTLHPYNTFAAGFNSTGLPHSHSTTRV
Protein: Dynein light chain Tctex-type 1 (Protein CW-1) (T-complex testis-specific protein 1 homolog) (P63172)
Organism: Homo sapiens (Human)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia. May also be a accessory component of axonemal dynein.
Subcellular location: Golgi apparatus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to mitotic spindles. {ECO:0000250}.
Interaction partners:
- Cytoplasmic dynein 1 intermediate chain 2
- Dynein light chain 1, cytoplasmic
- Dynein light chain roadblock-type 1
- Dynein light chain Tctex-type 4
- Cytoplasmic dynein 1 light intermediate chain 1
- Cytoplasmic dynein 1 heavy chain 1
- Dynein light chain Tctex-type protein 2B
- Cytoplasmic dynein 1 intermediate chain 1
- Cytoplasmic dynein 2 intermediate chain 1
- Cytoplasmic dynein 1 light intermediate chain 2
Sequence:
MEDYQAAEETAFVVDEVSNIVKEAIESAIGGNAYQHSKVNQWTTNVVEQTLSQLTKLGKPFKYIVTCVIMQKNGAGLHTASSCFWDSSTDGSCTVRWENKTMYCIVSAFGLSI
Protein: Sodium/myo-inositol cotransporter (Na(+)/myo-inositol cotransporter) (Sodium/myo-inositol transporter 1) (SMIT1) (Solute carrier family 5 member 3) (Q9JKZ2)
Organism: Mus musculus (Mouse)
Function: Electrogenic Na(+)-coupled sugar symporter that actively transports myo-inositol and its stereoisomer scyllo-inositol across the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1 (By similarity). Maintains myo-inositol concentration gradient that defines cell volume and fluid balance during osmotic stress, in particular in the fetoplacental unit and central nervous system. Forms coregulatory complexes with voltage-gated K(+) ion channels, allosterically altering ion selectivity, voltage dependence and gating kinetics of the channel. In turn, K(+) efflux through the channel forms a local electrical gradient that modulates electrogenic Na(+)-coupled myo-inositol influx through the transporter (By similarity). Associates with KCNQ1-KCNE2 channel in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability. Associates with KCNQ2-KCNQ3 channel altering ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation (By similarity). Provides myo-inositol precursor for biosynthesis of phosphoinositides such as PI(4,5)P2, thus indirectly affecting the activity of phosphoinositide-dependent ion channels and Ca(2+) signaling upon osmotic stress (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:24595108}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:24595108}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with KCNQ1 at the apical membrane of choroid plexus epithelium. {ECO:0000269|PubMed:24595108}.
Interaction partners:
- Proton myo-inositol cotransporter
- Sodium- and chloride-dependent betaine transporter
Sequence:
MRAVLEAADIAVVALYFILVMCIGFFAMWKSNRSTVSGYFLAGRSMTWVAIGASLFVSNIGSEHFIGLAGSGAASGFAVGAWEFNALLLLQLLGWVFIPIYIRSGVYTMPEYLSKRFGGHRIQVYFAALSLLLYIFTKLSVDLYSGALFIQESLGWNLYVSVILLIGMTALLTVTGGLVAVIYTDTLQALLMIIGALTLMVISMVKIGGFEEVKRRYMLASPDVASILLKYNLSNTNACMVHPKANALKMLRDPTDEDVPWPGFILGQTPASVWYWCADQVIVQRVLAAKNIAHAKGSTLMAGFLKLLPMFIIVVPGMISRIVFADEIACINPEHCMQVCGSRAGCSNIAYPRLVMTLVPVGLRGLMMAVMIAALMSDLDSIFNSASTIFTLDVYKLIRKSASSRELMIVGRIFVAFMVVISIAWVPIIVEMQGGQMYLYIQEVADYLTPPVAALFLLAIFWKRCNEQGAFYGGMAGFVLGAVRLILAFTYRAPECDQPDNRPGFIKDIHYMYVATALFWITGLITVIVSLLTPPPTKDQIRTTTFWSKKTLVTKESCSQKDEPYKMQEKSILQCSENSEVISHTIPNGKSEDSIKGLQPEDVNLLVTCREEGNPVASMGHSEAETPVDAYSNGQAALMGEREREKETENRSRYWKFIDWFCGFKSKSLSKRSLRDLMDEEAVCLQMLEETPQVKVILNIGLFAVCSLGIFMFVYFSL
Protein: V-type proton ATPase 16 kDa proteolipid subunit c (V-ATPase 16 kDa proteolipid subunit c) (Vacuolar proton pump 16 kDa proteolipid subunit c) (P23956)
Organism: Bos taurus (Bovine)
Function: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32764564}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P63081}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit F
- V-type proton ATPase subunit d 1
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B, brain isoform
Sequence:
MSEAKNGPEYASFFAVMGASAAMVFSALGAAYGTAKSGTGIAAMSVMRPEMIMKSIIPVVMAGIIAIYGLVVAVLIANSLNDGISLYRSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILSTK
Protein: Ubiquitin-binding serine/threonine protein kinase (A0A1D8PPK3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Beclin 1
- Phosphatidylinositol 3-kinase VPS34
- Autophagy-related protein 6
- Serine/threonine-protein kinase ATG1
- Ubiquitin-like protein ATG12
- Autophagy-related protein 3
- Autophagy protein 5
- Autophagy-related protein 9
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagy-related protein 8
Sequence:
MGQKLSLLAPSAPTVAVSSYVDALHNYQYVEVINNSRFLKTIKAIDKTTGNLVTIKLLIKPASPNYSIQLQQVIELMVKQSSLLYPFKNALPWHRLIETDRAGYVVRQMIKTNLYDRLSIRPFLEPIEKLFITYQILKIINEIHSLNIHHGDLKLENFLITSWNWLLLSDFSNLLKPTYIPEDNPNQYSFYFDTSGRRLCYIAPERFYNSQDHPKHISNFNDDGSFTMKNSVTDAMDLFSTGCVIAELYNDGEPTFTLSQLFKFMKNEYTPDLSGIYNKDIVTIIGKLIKLDPNERSSAREILDENKGTCFPEFFYSFLYDFMEMLNNQENFVLNANNDNISISDMKISYIYDNFGLISKSLKFQYSMDESNFSRDDILPMKLNLETMPFNYRIKQSKFIDDDSQEAALILLNVVTSFSQTLKQVNSKIKCCELIVALSERIRDESKLDRAIPYLCLFLDEYIEGAFHQQEGPQTASKVVCMALYSLTTLLMSCSYINPINMLIFPEYILPKIYNLLTVKSDSSSQRLVNCAVAVCLPYLAATAKRFWIMSKAFKNTNNALSTLVSPEDAMQSFSNLSLTKDQLDSKFKEITILLLTDSESPVKISLLNNILPLCQFFGQDKTNDIILPHLISYLNDTDQELRLAFLSSVLQMGPFIGVLSFEQYILPLLVQTIGDGEQFVVLKVLEIFNMFVKERLINPRTEFNALDVYKELLLNSINLLLHPNEWIRQSVINLIISVSANLTDADKYCFLYPLIKRFLSYDLSIIDWNTLYPCLTKPLTKQIYDLAITWSLNSTSKSLFWQQKNFSMLTTKQSGNNITKKMKKMISFNKDMGKSVYLPQMMSELTFANGSNQKSNSTIPLSSEDKQWLLKLKSIGLDDKSLWKILALRDYIYHVGRSPTSTLNKRLKATTNEISILPRNIFFTVVYRSEPLSISNGTREERILGSNAEETVSIRTSSRRGSNSLILPQLERVTASVQTVEANIMGEMETHNSGVNKDGWFNDSNTSHKVFSVSNSKIIVSHIKHTYTGENPYILNFLKNPKFQPNLSDFEEFGKTIIKHQYSQQQQQQQNQNQQQLKTIDMLPPMNVLVASFRSSDKDNRLEEINALAVCPTSEFFVTGSSTGSLKVWDSLKMEKLVTVKNANLSIELNSSVCSITFLPNRFVVIVTTNDGTIRLFRIDVMRNSKSKKIVRYLKMHLIRKYIHGNDHDGSGNCNGTKKYHRPIEQIKFLQDNYIIGVDATEQKIIMLDIITMTISSELQHPLIYGIINTFIVYKDYWLLVGTDKGVLTLWDLRFKIIVKSWHVKNNENNERLGSINNLELLSNSIKLFETKNDGGSSGGSSSAYFALSGNDDISIWELPSLECKAILKTSNAVMNSSTIMKYSLIEYKDDGNEDELFIEEIIDDIELDIDHEYDRKLNLNVLTMKFFQFNTNNNNNNVDYLMCSTGSNRVILFNLTSIQDSVVLKSDNTIFNTRYYNNVVIIDPVFANDQTLLNGTTKTNMYNVVKLVDHLFEPFHMIITIDRNNCVKLYKAANC
Protein: V-type proton ATPase subunit D (V-type proton ATPase subunit d) (Vacuolar proton pump subunit D) (Q8N5Z9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000256|ARBA:ARBA00029434}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029434}.
Interaction partners:
Sequence:
MSGKDRIEIFPSRMAQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQNVHKAQVKIRAKKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHVIIPRIERTLAYIITELDEREREEFYRLKKIQEKKKILKEKSEKDLEQRRAAGEVLEPANLLAEEKDEDLLFE
Protein: CaDmium Responsive (Cadmium-inducible lysosomal protein CDR-2) (G5ECX9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVCSCTIKAALIVGAVGFFIYRKMFKKPSIKPKPEAYKKDYKKDTVYLYQFKRTRKCPNLSPFCIKVEILCRAYNIPYEICDDKLRWSRNGSIPFIELNGEHIADTDLIEMRLRRHFNIPSLPAAQEAHSVALTRLADNHLFNLLIRYKIIGDEFFHILVRSIGIPKFLQPLLFPLIRASFGKKVYQRSTGSIGDFELKEMDDILHRDFQTIQDYLGDQKFLFGDKVTAADAAVFGQIASVIYPFRCSINDALENDFPKILEYCERVRQEIYPNDFTI
Protein: Rho guanine nucleotide exchange factor 5 (Ephexin-3) (Guanine nucleotide regulatory protein TIM) (Oncogene TIM) (Transforming immortalized mammary oncogene) (p60 TIM) (Q12774)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor which activates Rho GTPases. Strongly activates RHOA. Also strongly activates RHOB, weakly activates RHOC and RHOG and shows no effect on RHOD, RHOV, RHOQ or RAC1 (By similarity). Involved in regulation of cell shape and actin cytoskeletal organization. Plays a role in actin organization by generating a loss of actin stress fibers and the formation of membrane ruffles and filopodia. Required for SRC-induced podosome formation (By similarity). Involved in positive regulation of immature dendritic cell migration (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14662653, ECO:0000269|PubMed:25911094}. Nucleus {ECO:0000269|PubMed:14662653}. Cell projection, podosome {ECO:0000250|UniProtKB:E9Q7D5}.
Interaction partners:
- Transforming protein RhoA
- Growth factor receptor-bound protein 2
- Rho-related GTP-binding protein RhoG
- Cell division control protein 42 homolog
- SHC-transforming protein 1
Sequence:
MEAEEAQRGASPPISAIEEFSIIPEAPMRSSQVSALGLEAQEDEDPSYKWREEHRLSATQQSELRDVCDYAIETMPSFPKEGSADVEPNQESLVAEACDTPEHWEAVPQSLAGRQARTLAPPELWACPIQSEHLDMAPFSSDLGSEEEEVEFWPGLTSLTLGSGQAEEEEETSSDNSGQTRYYSPCEEHPAETNQNEGSESGTIRQGEELPPEELQESQGLLHPQEVQVLEEQGQQEAGFRGEGTLREDVCADGLLGEEQMIEQVNDEKGEQKQKQEQVQDVMLGRQGERMGLTGEPEGLNDGEWEQEDMERKAQGQGGPEQGEERKRELQVPEENRADSQDEKSQTFLGKSEEVTGKQEDHGIKEKGVPVSGQEAKEPESWDGGRLGAVGRARSREEENEHHGPSMPALIAPEDSPHCDLFPGASYLMTQIPGTQTESRAEELSPAALSPSLEPIRCSHQPISLLGSFLTEESPDKEIDQNSQQEESRLRKGTVSSQGTEVVFASASVTPPRTPDSAPPSPAEAYPITPASVSARPPVAFPRRETSCAARAPETASAPLSMDDPSPCGTSEMCPAALYGFPSTGTSPPRPPANSTGTVQHLRSDSFPGSHRTEQTPDLVGMLLSYSHSELPQRPPKPAIYSSVTPRRDRRSGRDYSTVSASPTALSTLKQDSQESISNLERPSSPPSIQPWVSPHNPAFATESPAYGSSPSFVSMEDVRIHEPLPPPPPQRRDTHPSVVETDGHARVVVPTLKQHSHPPPLALGSGLHAPHKGPLPQASDPAVARQHRPLPSTPDSSHHAQATPRWRYNKPLPPTPDLPQPHLPPISAPGSSRIYRPLPPLPIIDPPTEPPPLPPKSRGRSRSTRGGHMNSGGHAKTRPACQDWTVPLPASAGRTSWPPATARSTESFTSTSRSKSEVSPGMAFSNMTNFLCPSSPTTPWTPELQGPTSKDEAGVSEHPEAPAREPLRRTTPQQGASGPGRSPVGQARQPEKPSHLHLEKASSWPHRRDSGRPPGDSSGQAVAPSEGANKHKGWSRQGLRRPSILPEGSSDSRGPAVEKHPGPSDTVVFREKKPKEVMGGFSRRCSKLINSSQLLYQEYSDVVLNKEIQSQQRLESLSETPGPSSPRQPRKALVSSESYLQRLSMASSGSLWQEIPVVRNSTVLLSMTHEDQKLQEVKFELIVSEASYLRSLNIAVDHFQLSTSLRATLSNQEHQWLFSRLQDVRDVSATFLSDLEENFENNIFSFQVCDVVLNHAPDFRRVYLPYVTNQTYQERTFQSLMNSNSNFREVLEKLESDPVCQRLSLKSFLILPFQRITRLKLLLQNILKRTQPGSSEEAEATKAHHALEQLIRDCNNNVQSMRRTEELIYLSQKIEFECKIFPLISQSRWLVKSGELTALEFSASPGLRRKLNTRPVHLHLFNDCLLLSRPREGSRFLVFDHAPFSSIRGEKCEMKLHGPHKNLFRLFLRQNTQGAQAEFLFRTETQSEKLRWISALAMPREELDLLECYNSPQVQCLRAYKPRENDELALEKADVVMVTQQSSDGWLEGVRLSDGERGWFPVQQVEFISNPEVRAQNLKEAHRVKTAKLQLVEQQA
Protein: Movement protein TGB1 (EC 3.6.4.-) (58 kDa protein) (Beta-B protein) (Triple gene block 1 protein) (TGBp1) (P04867)
Organism: Barley stripe mosaic virus (BSMV)
Function: Participates in the transport of viral genome to neighboring plant cells directly through plasmodesmata, without any budding. Multifunctional movement protein with RNA-binding, ATPase and helicase activities. Engages in homologous interactions leading to the formation of a ribonucleoprotein complex containing plus-sense viral RNAs (vRNPs). ATPase activity is probably required for vRNPs movement complex assembly. Intracellular delivery of TGBp1-containing vRNPs to plasmodesmata is facilitated by TGBp2 and TGBp3 (By similarity).
Subcellular location: Host cell junction, host plasmodesma {ECO:0000269|PubMed:19570874}. Host nucleus {ECO:0000269|PubMed:28872759}. Host cytoplasm {ECO:0000269|PubMed:28872759}. Host nucleus, host nucleolus {ECO:0000269|PubMed:28872759}. Host cytoplasm, host cytoskeleton {ECO:0000250|UniProtKB:Q9IV54}. Note=TGB1 nuclear-cytoplasmic trafficking is required for cell-to-cell movement and systemic infection (PubMed:28872759). Associates with host microtubules (By similarity). {ECO:0000250|UniProtKB:Q9IV54, ECO:0000269|PubMed:28872759}.
Interaction partners:
Sequence:
MDMTKTVEEKKTNGTDSVKGVFENSTIPKVPTGQEMGGDGSSTSKLKETLKVADQTPLSVDNGAKSKLDSSDRQVPGVADQTPLSVDNGAKSKLDSSDRQVPGPELKPNVKKSKKKRIQKPAQPSGPNDLKGGTKGSSQVGENVSENYTGISKEAAKQKQKTPKSVKMQSNLADKFKANDTRRSELINKFQQFVHETCLKSDFEYTGRQYFRARSNFFEMIKLASLYDKHLKECMARACTLERERLKRKLLLVRALKPAVDFLTGIISGVPGSGKSTIVRTLLKGEFPAVCALANPALMNDYSGIEGVYGLDDLLLSAVPITSDLLIIDEYTLAESAEILLLQRRLRASMVLLVGDVAQGKATTASSIEYLTLPVIYRSETTYRLGQETASLCSKQGNRMVSKGGRDTVIITDYDGETDETEKNIAFTVDTVRDVKDCGYDCALAIDVQGKEFDSVTLFLRNEDRKALADKHLRLVALSRHKSKLIIRADAEIRQAFLTGDIDLSSKASNSHRYSAKPDEDHSWFKAK