wanglab/gogpt-training-data huggingface dataset:
Protein: Spindly-like protein spdl-1 (Q17695)
Organism: Caenorhabditis elegans
Function: Transient kinetochore component required for chromosome and spindle pole alignment and chromosome segregation during mitosis. Functions downstream of the RZZ complex to mediate kinetochore-microtubule attachments and nuclear envelope breakdown during cell division. Required for kinetochore assembly and localizes the checkpoint proteins mdf-1 and mdf-2, dynein and dynactin to unattached kinetochores. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Required for embryonic development.
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000269|PubMed:18765790, ECO:0000269|PubMed:18936247}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18765790}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18936247}. Note=Localizes to microtubules during mitosis (PubMed:18936247). Recruited to the kinetochore by the RZZ complex (PubMed:18765790, PubMed:18936247). Localization to the kinetochore is also dependent on the NDC80 complex and bub-1 (PubMed:18765790). Localizes to the kinetochore during nuclear envelope breakdown and remains there until the metaphase-anaphase transition (PubMed:18765790, PubMed:18936247). {ECO:0000269|PubMed:18765790, ECO:0000269|PubMed:18936247}.
Interaction partners:
- Protein zwilch homolog
- Eukaryotic translation initiation factor 3 subunit B
- Kinetochore NuLl
- KNL
- Kinetochore-associated protein rod-1
- HoloCentric chromosome binding Protein
- Dynactin subunit 6
- Centromere/kinetochore protein zw10 homolog
Sequence:
MPDDEEKLQLLADVERLKKILRQKDEMLEEMEDDLKNQGKPCSSKLSLEERAQELSEQLRDLHVEMDGKNATILDRDALIDSLRSEIDKLEKINKEFANGSVIPEHDDSNSFGESEMLRISEDCQKYKETATALYERNAELEKEAVNLKDEIESMMDHIRDLKNHMETRDEEIARLEGELFDERNSHEGKLAARGNSMFSEVIDAERKVEEDLKVLHGENRALKGMVKRLRMEVEEVEERLRSSTKRFNVTRMTTSDIDVKEMRRLRDRVCHLETERVHLWERMFIKMRSIPKREVGALITGYFKSFELSIASVKGGFDGLMKDNEKYVTIIRGLQQEVENLKADIVQLQFDNKCAHRKAAPVVNKDFEHPLLAAPLKTLNNGRPSFFIKPKNVEPMPQLGHSLSSIAVTPQKPAAKFTTRSSIKDDTSEWAERRMKAQAEKKLATPTPRYNYIKLSEPVPKFKPAVLQMPSTSETKEN
Protein: ABC transporter (O67181)
Organism: Aquifex aeolicus (strain VF5)
Interaction partners:
- Transport permease protein
- Mannosyltransferase A
- Polysaccharide biosynthesis protein
- Polysaccharide biosynthesis protein
- Riboflavin biosynthesis protein
- Phosphoribosyltransferase domain-containing protein
- DUF4214 domain-containing protein
- Mannosyltransferase C
Sequence:
MMIRVFDVWKKYKYYKKPQDRLKEIIFRKPFHEELWVLKGINLEIEKGEVLGIVGPNGAGKSTLLKVITGVTEPDKGFVERSGKVVGLLELGTGFNYELSGLENIYVNASLLGLSRREIDEKLESIIEFSELDDFINKPLKTYSSGMIMRLAFSIAIHTEPECFIIDEALAVGDAHFQQKCFRKLKEHKQKGGSIIFVSHDMNAVKILCDRAILLHKGEIIEEGSPETVTQAYYKLMASLENKEGITFLQNGYGNFKAVIKEVRLKSEHGYTNNFPSGDTLFIELDVEAKEDLQDVVAGILIRDRFGQDIFGINTYLMEKKVELKKGKYLFTFKMPLNLAPGKYTLTVALHKGMDHAQECYHWIDNVCNFEVNGFKKEQFVGVCYLPTEFNYRKIP
Protein: Phosphotransferase (EC 2.7.1.-) (C6KT76)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Glucose-6-phosphate isomerase
- Phosphoglucomutase, putative
- Phosphomannomutase
- glutamine--fructose-6-phosphate transaminase
- Probable ATP-dependent 6-phosphofructokinase
- Bifunctional glucose-6-phosphate 1-dehydrogenase/6-phosphogluconolactonase
- Fructose-bisphosphate aldolase
- Phosphoacetylglucosamine mutase, putative
- transketolase
- Deoxyribose-phosphate aldolase, putative
Sequence:
MSEYDIAKNDVTYTKLDTIECDIPINEELSWRINKFVNQLRISYSTLEEFVDNFVYELKKGLEAHRKHPNLWIPHECSFKMLDSCIANIPTGQEKGTYYAIDFGGTNFRAVRASLDGKGKIKRDQETYSLKFTGSYSHEKGLLDKHATASQLFDHFAERIKYIMGEFNDLDNKEVKSVGFTFSFPCTSPSINCSILIDWTKGFETGRATNDPVEGRDVCKLMNDAFVRAAIPAKVCCVLNDAVGTLMSCAYQKGRGTPPCYIGIILGTGSNGCYYEPEWKKYKYAGKIINIEFGNFDKDLPTSPIDLVMDWYSANRSRQLFEKMISGAYLGEIVRRFMVNVLQSACSKKMWISDSFNSESGSVVLNDTSKNFEDSRKVAKAAWDMDFTDEQIYVLRKICEAVYNRSAALAAGTIAAIAKRIKIIEHSKFTCGVDGSLFVKNAWYCKRLQEHLKVILADKAENLIIIPADDGSGKGAAITAAVIALNADIPQLP
Protein: Cell cycle progression protein 1 (Cell cycle progression restoration protein 8) (Q9ULG6)
Organism: Homo sapiens (Human)
Function: Acts as an assembly platform for Rho protein signaling complexes. Limits guanine nucleotide exchange activity of MCF2L toward RHOA, which results in an inhibition of both its transcriptional activation ability and its transforming activity. Does not inhibit activity of MCF2L toward CDC42, or activity of MCF2 toward either RHOA or CDC42 (By similarity). May be involved in cell cycle regulation.
Subcellular location: Cytoplasmic granule membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- RB1-inducible coiled-coil protein 1
- Gamma-aminobutyric acid receptor-associated protein
- Translocation protein SEC62
- Atlastin-3
- Reticulophagy regulator 1
- Testis-expressed protein 264
- Reticulon-3
- GABA type A receptor associated protein like 1
- Gamma-aminobutyric acid receptor-associated protein-like 2
Sequence:
MSENSSDSDSSCGWTVISHEGSDIEMLNSVTPTDSCEPAPECSSLEQEELQALQIEQGESSQNGTVLMEETAYPALEETSSTIEAEEQKIPEDSIYIGTASDDSDIVTLEPPKLEEIGNQEVVIVEEAQSSEDFNMGSSSSSQYTFCQPETVFSSQPSDDESSSDETSNQPSPAFRRRRARKKTVSASESEDRLVAEQETEPSKELSKRQFSSGLNKCVILALVIAISMGFGHFYGTIQIQKRQQLVRKIHEDELNDMKDYLSQCQQEQESFIDYKSLKENLARCWTLTEAEKMSFETQKTNLATENQYLRVSLEKEEKALSSLQEELNKLREQIRILEDKGTSTELVKENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRELERERLVTTALRGELQQLSGSQLHGKSDSPNVYTEKKEIAILRERLTELERKLTFEQQRSDLWERLYVEAKDQNGKQGTDGKKKGGRGSHRAKNKSKETFLGSVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKGNKRFGATKEAAEKPRTVFSDYLHPQYKAPTENHHNRGPTMQNDGRKEKPVHFKEFRKNTNSKKCSPGHDCRENSHSFRKACSGVFDCAQQESMSLFNTVVNPIRMDEFRQIIQRYMLKELDTFCHWNELDQFINKFFLNGVFIHDQKLFTDFVNDVKDYLRNMKEYEVDNDGVFEKLDEYIYRHFFGHTFSPPYGPRSVYIKPCHYSSL
Protein: Nuclear distribution protein nudE homolog 1 (NudE) (rNudE) (Q9ES39)
Organism: Rattus norvegicus (Rat)
Function: Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post-mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Cleavage furrow {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9NXR1}. Note=Localizes to the interphase and S phase centrosome. During mitosis, partially associated with the mitotic spindle. Concentrates at the plus ends of microtubules coincident with kinetochores in metaphase and anaphase in a CENPF-dependent manner. Also localizes to the cleavage furrow during cytokinesis (By similarity). Also localizes to the cleavage furrow during cytokinesis. Colocalizes with RAB9A to membrane vesicles (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9NXR1}.
Interaction partners:
- Disrupted in schizophrenia 1 homolog
- Platelet-activating factor acetylhydrolase IB subunit alpha
- Nuclear distribution protein nudE-like 1
- Nuclear migration protein nudC
- Trafficking kinesin protein 1
- Serine/threonine-protein kinase PLK1
- 14-3-3 protein epsilon
- Cyclin-dependent kinase 1
- Aurora kinase A
- Cell division cycle protein 20 homolog
Sequence:
MEDSGKTFGSEEEETNYWRDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQAETRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAHTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQDKPRTPMPSSGETKRTDMAVQATGSAPSTPITHQGSSSGLNTPETFRCGLGSPSSGTPLTPAARISALNIVGDLLRKVGALESKLASCKNFMYDQSPSRKSGPALGRGTKNRDGIDRRPGSTAVGDKGSGKRLEFAKPSSQLSSPALPSTQGVVKLLL
Protein: D(3) dopamine receptor (Dopamine D3 receptor) (P35462)
Organism: Homo sapiens (Human)
Function: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19520868}; Multi-pass membrane protein {ECO:0000269|PubMed:19520868}. Note=Both membrane-bound and scattered in the cytoplasm during basal conditions. Receptor stimulation results in the rapid internalization and sequestration of the receptors at the perinuclear area (5 and 15 minutes), followed by the dispersal of the receptors to the membrane (30 minutes). DRD3 and GRK4 co-localize in lipid rafts of renal proximal tubule cells.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- D
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Neurotrophic factor BDNF precursor form
- Guanine nucleotide-binding protein G
- D
- Sodium-dependent serotonin transporter
Sequence:
MASLSQLSGHLNYTCGAENSTGASQARPHAYYALSYCALILAIVFGNGLVCMAVLKERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPTVCSISNPDFVIYSSVVSFYLPFGVTVLVYARIYVVLKQRRRKRILTRQNSQCNSVRPGFPQQTLSPDPAHLELKRYYSICQDTALGGPGFQERGGELKREEKTRNSLSPTIAPKLSLEVRKLSNGRLSTSLKLGPLQPRGVPLREKKATQMVAIVLGAFIVCWLPFFLTHVLNTHCQTCHVSPELYSATTWLGYVNSALNPVIYTTFNIEFRKAFLKILSC
Protein: Leishmanolysin-like peptidase (EC 3.4.24.-) (Q384S4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MLHHKLDTVSVIALLLTLRGTVADDNITGEEEGTGHRCMHNDVAVPYDELPSMDAVHDLQTAHVAEVSNNTEGEGNKSKSVERKNVRFHIKYALGETCKGIGMTVPTYIKGTTKECTEDDVLTKWKLRSVKVMMEAATKFLSSALLVDPLEAVNVPGGKCSGVQVPKMTVPNADYVVFVTINPRPEEETTTVAWAAACLKDTRSGRPVVGHINFIPAAIQRNPSSLAEHVAMHELAHAIGFSDIAETMLRAPNGLGAKGSQRVYRKGLGKAVTLITSPKVLKVAREYYGCPGLDGVEVEDAGSEGTRGSHWKKRILFNEALVGSVTSGQLFFSPLTLAYFEDLGFYTANYSTAETGMTWGKGRGCDFLYQKCDNHPREWGEFCFRKEMFVSTCTLDRSSLGACDITTHPEDLPQLYRYFDDPRVGGSSAEMDYCPTVMGFVNAYCTAELGFAFMNVFGNEMGVHSLCYDSDVITSVFPNFPFAARCFPTTCTPSGQLLLRVQGRTVACPRDGKAGLGDTSKLKGVHGKVQCPPSENFCKNSGNGISKLQLASVADEVDGSSNTERIGHSLISPTPHTWNSEDMGSCSSRLACLKDIPPPFPACSLAARKVKECLGNDCPGSAQQWRYANEVGNSCLNPEGMVAMCMDGWRGVNELCGAVDPESKLGRSYRSMLPF
Protein: Chitinase-like protein (EC 3.2.1.14) (Q6JX04)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MEAKWLLCFTMAALMAVSNGQESVKPLVKIVKGKKLCDKGWECKGWSQFCCNQTISDYFRTYQFENLFAKRNTPVAHAVGFWDYHSFITAAAQYQPHGFGTTGGKLQSMKEVAAFLGHVGSKTSCGYGVATGGPLAWGLCYNKEMSPSKLYCDDYYKYTYPCTPGVSYHGRGALPIYWNYNYGETGDALKVDLLNHPEYIENNATLAFQAALWRWMTPVKKHQPSAHDVFVGSWKPTKNDTLAKRVPGFGATMNVLYGDQVCGRGDVDTMNNIISHYLSYLDLMGVGREEAGPHEVLTCEEQKPFTVSPSSASSSSSS
Protein: 60S ribosomal protein L18a (Q382C4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosomal protein L28, putative
- 40S ribosomal protein S25
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L17, putative
- 60S ribosomal protein L27a
- 40S ribosomal protein S13, putative
- 60S ribosomal protein L13a, putative
- 60S acidic ribosomal protein P0
- 60S ribosomal protein L39, putative
- Large ribosomal subunit protein eL18
Sequence:
MVRPHLRHYCVVGRETPSEKNPQPTVYKFEVFAPNFVVAKSRFWRMMREKNKVKSTHGDVLSCKVVKDRKLAARNYSVDIAYYSQRCGYTHMVKEFRDVCKAGAVSQAYNDLASRHRARYHNIEVLGVKSIPNHEVRRLNVAQFHPHNLSFPLLQRRVKAPRKDRVIFVKKNSKRAVVA
Protein: Lysophospholipase 1 (EC 3.1.1.5) (Phospholipase B 1) (P78854)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the release of fatty acids from lysophospholipids. Required for survival under high osmolarity, for normal osmotic stress-induced gene expression, and for nutrient-mediated repression of sexual differentiation.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Glycerophosphocholine phosphodiesterase gde1
- Lysophospholipid acyltransferase
- Triacylglycerol lipase ptl3
- Putative uncharacterized oxidoreductase C513.07
Sequence:
MLFRGLSLWMLFLASCLSALALPAAEDDGSVKVFKRAKKHSTKQEGPSYAPYYVDCPSDNIVESLSSNEIPSAESEYLSTRSTITNTAMKDFLRNANLPGLNADTLSGSEGPSIGIALSGGGLRAMILGSGALSAMDARHDNHTVLTGLLQASDYLVGTDGSAWTVGGIALNNFSTINDFSKLWAFNHPLMYPKSAIVFNAHFYSSIMNEVAEKANAGFNISLSDYWGRVISRTLGDTTYGFPNVSLSSITSQEWYRNANFPYPIITFATQNYGEDISNVNTTFFEASPNVFGTFDHGINSFIPTEYLGTTLNNGASSNGSCVINYDNFGFMMGASSTYFNKIMRNFNDSSTKNGRIIQQYLKGNFSENGQQIISIPNPFQGVESANSDAANNLGSSSSLNLVDTFLTGEKIPLWPLLQKGRDVDVIVAVDNGDDSEWLWPNGNSLVQTYERVVAAQAAGNTNVKGFPYVPSQQSFVSLHFNDRPVFFGCDGRNTTAGNHTVTRDTPPLVIYLPNVPYNYFTNISTDRTYYTEDMIQQLLTNGLISSTVDNDTYFGQCFACAVVKRTLERNNITASPECQQCYYNYCWSGLYDDSAANDDIVYNPTCRLGEGI
Protein: Ras-related protein Rab-8B (GTP-binding protein SAS2) (P20791)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Protein transport. Probably involved in vesicular traffic (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Ras-related protein Rab-8A
- Rab GDP dissociation inhibitor
Sequence:
MTSPATNKPAAYDFLVKLLLIGDSGVGKSCLLLRFSDGSFTPSFIATIGIDFKIRTIELEGKRIKLQIWDTAGQERFRTITTAYYRGAMGILLVYDVTDEKSFGSIRNWIRNIEQHASDSVNKMLIGNKCDMTEKKVVDSSRGKSLADEYGIKFLETSAKNSVNVEEAFIGLAKDIKKRMIDTPNDPDHTICITPNNKKNTCC
Protein: Sideroflexin-1 (D6RFI0)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004225}.
Interaction partners:
Sequence:
MSGELPPNINIKEPRWDQSTFIGRANHFFTVTDPRNILLTNEQLESARKIVHDYRQGIVPPGLTENELWRAKYIYDSAFHPDTGEKMILIGRMSAQVPMNMTITGCMMTFYRTTPAVLFWQWINQSFNAVVNYTNRSGDAPLTVNELGTAYVSATTGAVATALGLNALTKHVSPLIGRFVPFAAVAAANCINI
Protein: Solute carrier family 2, facilitated glucose transporter member 4 (Glucose transporter type 4, insulin-responsive) (GLUT-4) (P14672)
Organism: Homo sapiens (Human)
Function: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation. Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells. Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P14142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}. Endomembrane system {ECO:0000269|PubMed:8300557}; Multi-pass membrane protein {ECO:0000269|PubMed:8300557}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P14142}. Note=Localizes primarily to the perinuclear region, undergoing continued recycling to the plasma membrane where it is rapidly reinternalized (PubMed:8300557). The dileucine internalization motif is critical for intracellular sequestration (PubMed:8300557). Insulin stimulation induces translocation to the cell membrane (By similarity). {ECO:0000250|UniProtKB:P14142, ECO:0000269|PubMed:8300557}.
Interaction partners:
- Ras-related protein Rab-10
- Insulin
- Ras-related protein Rab-14
- TBC1 domain family member 4
- Tether containing UBX domain for GLUT4
- Ras-related protein Rab-8A
- Ras-related protein Rab-2A
- Vesicle-associated membrane protein 2
- Insulin receptor substrate 1
- Peroxisome proliferator-activated receptor gamma
Sequence:
MPSGFQQIGSEDGEPPQQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNETWLGRQGPEGPSSIPPGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLVNNVLAVLGGSLMGLANAAASYEMLILGRFLIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVIGILIAQVLGLESLLGTASLWPLLLGLTVLPALLQLVLLPFCPESPRYLYIIQNLEGPARKSLKRLTGWADVSGVLAELKDEKRKLERERPLSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFETAGVGQPAYATIGAGVVNTVFTLVSVLLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPAMSYVSIVAIFGFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFSNWTSNFIIGMGFQYVAEAMGPYVFLLFAVLLLGFFIFTFLRVPETRGRTFDQISAAFHRTPSLLEQEVKPSTELEYLGPDEND
Protein: Large ribosomal subunit protein uL10 (60S acidic ribosomal protein P0) (P22685)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
Interaction partners:
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein eS10
- Small ribosomal subunit protein eS4
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL22
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein uL2
Sequence:
MSGAGSKRKNVFIEKATKLFTTYDKMIVAEADFVGSSQLQKIRKSIRGIGAVLMGKKTMIRKVIRDLADSKPELDALNTYLKQNTCIIFCKDNIAEVKRVINTQRVGAPAKAGVFAPNDVIIPAGPTGMEPTQTSFLQDLKIATKINRGQIDIVNEVHIIKTGQKVGASEATLLQKLNIKPFTYGLEPKIIYDAGACYSPSISEEDLINKFKQGIFNIAAISLEIGYPTVASIPHSVMNAFKNLLAISFETSYTFDAAEKFKSAAAAAPVAAAPSAAAPAAAAKKVVVEEKKEESDDDMGMGLFD
Protein: High molecular weight rhoptry protein 3 (Q8I395)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Host cell membrane {ECO:0000250|UniProtKB:B0M0W2}; Single-pass membrane protein {ECO:0000255}. Host cell membrane {ECO:0000269|PubMed:35393572}; Peripheral membrane protein {ECO:0000305}. Parasitophorous vacuole membrane {ECO:0000269|PubMed:35393572}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:35393572}. Cytoplasmic vesicle, secretory vesicle, rhoptry {ECO:0000269|PubMed:28252383, ECO:0000269|PubMed:28252384, ECO:0000269|PubMed:33024030, ECO:0000269|PubMed:35393572}. Note=Export to host cytosol is mediated by the Plasmodium translocon of exported proteins (PTEX) complex. {ECO:0000250|UniProtKB:B0M0W2}.
Interaction partners:
- High molecular weight rhoptry protein 2
- Cytoadherence-linked asexual protein 3.1
- Cytoadherence linked asexual protein 3.2
Sequence:
MRSKHLVTLFIITFLSFSTVKVWGKDVFAGFVTKKLKTLLDCNFALYYNFKGNGPDAGSFLDFVDEPEQFYWFVEHFLSVKFRVPKHLKDKNIHNFTPCLNRSWVSEFLKEYEEPFVNPVMKFLDKEQRLFFTYNFGDVEPQGKYTYFPVKEFHKYCILPPLIKTNIKDGESGEFLKYQLNKEEYKVFLSSVGSQMTAIKNLYSTVEDEQRKQLLKVIIENESTNDISVQCPTYNIKLHYTKECANSNNILKCIDEFLRKTCEKKTESKHPSADLCEHLQFLFESLKNPYLDNFKKFMTNSDFTLIKPQSVWNVPIFDIYKPKNYLDSVQNLDTECFKKLNSKNLIFLSFHDDIPNNPYYNVELQEIVKLSTYTYSIFDKLYNFFFVFKKSGAPISPVSVKELSHNITDFSFKEDNSEIQCQNVRKSLDLEVDVETMKGIAAEKLCKIIEKFILTKDDASKPEKSDIHRGFRILCILISTHVEAYNIVRQLLNMESMISLTRYTSLYIHKFFKSVTLLKGNFLYKNNKAIRYSRACSKASLHVPSVLYRRNIYIPETFLSLYLGLSNLVSSNPSSPFFEYAIIEFLVTYYNKGSEKFVLYFISIISVLYINEYYYEQLSCFYPKEFELIKSRMIHPNIVDRILKGIDNLMKSTRYDKMRTMYLDFESSDIFSREKVFTALYNFDSFIKTNEQLKKKNLEEISEIPVQLETSNDGIGYRKQDVLYETDKPQTMDEASYEETVDEDAHHVNEKQHSAHFLDAIAEKDILEEKTKDQDLEIELYKYMGPLKEQSKSTSAASTSDEISGSEGPSTESTSTGNQGEDKTTDNTYKEMEELEEAEGTSNLKKGLEFYKSSLKLDQLDKEKPKKKKSKRKKKRDSSSDRILLEESKTFTSENEL
Protein: Voltage-dependent T-type calcium channel subunit alpha (E0CXK2)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
Interaction partners:
Sequence:
MADSNLPPSSSAAPDPEPGITEQPGPRSPPPSPPGLEEPLDGTNPDVPHPDLAPVAFFCLRQTTSPRNWCIKMVCNPWFECVSMLVILLNCVTLGMYQPCDDMECLSDRCKILQVFDDFIFIFFAMEMVLKMVALGIFGKKCYLGDTWNRLDFFIVMAGMVEYSLDLQNINLSAIRTVRVLRPLKAINRVPSMRILVNLLLDTLPMLGNVLLLCFFVFFIFGIIGVQLWAGLLRNRCFLEENFTIQGDVALPPYYQPEEDDEMPFICSLSGDNGIMGCHEIPPLKEQGRECCLSKDDMYDFGAGRQDLNASGLCVNWNRYYNVCRTGNANPHKGAINFDNIGYAWIVIFQVITLEGWVEIMYYVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQREHRLMLEQRQRYLSSSTVASYAEPGDCYEEIFQYVCHILRKAKRRALGLYQALQNRRQATGPGTPAPAKPGPHAKEPSHCKLCPRHSPLDTTPHTLVQPISAILASDPSSCPRCQHEAGRRPSGLGSTDSGQEGSGSGGSAEAEANGDGPQSSEDGVSSGLGKEEEQEDGAARLCGDVWRETRAKLRGIVDSKYFNRGIMMAILVNTVSMGIEHHEQPEELTNILEICNVVFTSMFALEMILKLAAFGLFDYLRNPYNIFDSIIVIISIWEIVGQADGGLSVLRTFRLLRVLKLVRFMPALRRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHIFGCKFSLRTDTGDTVPDRKNFDSLLWAIVTVFQILTQEDWNVVLYNGMASTTPWASLYFVALMTFGNYVLFNLLVAILVEGFQAEGDANRSYSDEDQSSSNLEELDKLPEGLDSSRDLKLCPIPMTPNGHLDPSLPLGGHLGPAGAMGAAPRLSLQPDPVLVALESRKSSVMSLGRMSYDQRSLSSSRSSYYGPWGRSGTWASRRSSWNSLKHKPPSAEHESLLSGERGGSCVRACEGAREDAPPRAAPLHAPHTHHAHHGPHLAHRHRHHRRTLSLDTRDSVDLAELVPVVGAHSRAAWRAAGQAPGHEDCNGRMPNIAKDVFTKMDDRRDRGEDEEEIDYTLCFRVRKMIDVYKPDWCEVREDWSVYLFSPENKFRILCQTIIAHKLFDYVVLAFIFLNCITIALERPQIEAGSTERIFLTVSNYIFTAIFVGEMTLKVVSLGLYFGEQAYLRSSWNVLDGFLVFVSIIDIVVSVASAGGAKILGVLRVLRLLRTLRPLRVISRAPGLKLVVETLISSLKPIGNIVLICCAFFIIFGILGVQLFKGKFYHCLGVDTRNITNRSDCVAANYRWVHHKYNFDNLGQALMSLFVLASKDGWVNIMYNGLDAVAVDQQPVTNHNPWMLLYFISFLLIVSFFVLNMFVGVVVENFHKCRQHQEAEEARRREEKRLRRLEKKRRKAQRLPYYATYCPTRLLIHSMCTSHYLDIFITFIICLNVVTMSLEHYNQPTSLETALKYCNYMFTTVFVLEAVLKLVAFGLRRFFKDRWNQLDLAIVLLSVMGITLEEIEINAALPINPTIIRIMRVLRIARVLKLLKMATGMRALLDTVVQALPQVGNLGLLFMLLFFIYAALGVELFGKLVCNDENPCEGMSRHATFENFGMAFLTLFQVSTGDNWNGIMKDTLRDCTHDERSCLSSLQFVSPLYFVSFVLTAQFVLINVVVAVLMKHLDDSNKEAQEDAEMDAEIELEMAHGLGPGPGPCPCPCPCPCPCPCPGPRMPTSSPGAPGRGSGGAGVGGDTESHLCRHCYSPAQETLWLDSVSLIIKDSLEGELTIIDNLSGSIFHHYSSPAGCDKCHHDKQETGPRPSCWGMT
Protein: Mediator of RNA polymerase II transcription subunit 19 (Lung cancer metastasis-related protein 1) (Mediator complex subunit 19) (A0JLT2)
Organism: Homo sapiens (Human)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 15
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 29
Sequence:
MENFTALFGAQADPPPPPTALGFGPGKPPPPPPPPAGGGPGTAPPPTAATAPPGADKSGAGCGPFYLMRELPGSTELTGSTNLITHYNLEQAYNKFCGKKVKEKLSNFLPDLPGMIDLPGSHDNSSLRSLIEKPPILSSSFNPITGTMLAGFRLHTGPLPEQCRLMHIQPPKKKNKHKHKQSRTQDPVPPETPSDSDHKKKKKKKEEDPDRKRKKKEKKKKKNRHSPDHPGMGSSQASSSSSLR
Protein: WPP domain-interacting protein 2 (Q9FH18)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates and enhances the nuclear envelope docking of RANGAP proteins mediated by WIT1 and WIT2 in the undifferentiated cells of root tips. As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:22270916}. Nucleus membrane {ECO:0000269|PubMed:17600715}; Single-pass membrane protein {ECO:0000269|PubMed:17600715}; Cytoplasmic side {ECO:0000269|PubMed:17600715}. Note=Targeted to the nuclear envelope (NE) during interphase. Associated to the cell plate during cytokinesis in root tips.
Interaction partners:
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Hapless protein
- PRA1 family protein G2
- At5g66005
Sequence:
MDLESESSVLESVEDNNGLIGDLDKELNSPVETSPLISKGFGLRKWKRRLRRDLVKDDTSVSMENSKALKRVLSGLVDPNAKQMHLPGPEVRQDSVGSVGSVNSVVGFVMGGESYGNGLAFAAGVDSDNSEDRSSTMSHSWDKHRGKVSGGKSVISSGDSSQQRKSSVEKSNKLRGERIKIEKENSHSSMESADSRSSNFVFMQGASYSLSSREQGGRRMMDYDDENSDHDAHTSKRKDNVEEEEEETEDYSQGDCVEESQIKSNGSSDNLDPLIVAVNSFQTLQEALQKELQKFQELGKEEPITSLHDGGESSSCIHAGHEGASEASSSYRFGSEKMGEMELTSLDSEILNLVNNVEHLEIKLEEAKRILEVKETQIRELESTINVSETCNGGTEIGIEDIFQQKVEAEIEYIIFSRSVGNLKRRIKLIEEEKTLGLSKLDKAETKAENLKNQAQDLQNHCVEITEIQEVECLKKRAFKTTRCLLLQLGLLFILYYSLLPEPEIAVPT