wanglab/gogpt-training-data huggingface dataset:
Protein: Endosomal/lysosomal proton channel TMEM175 (Potassium channel TMEM175) (Transmembrane protein 175) (mTMEM175) (Q9CXY1)
Organism: Mus musculus (Mouse)
Function: Proton-activated proton channel that catalyzes proton efflux from endosomes and lysosomes to maintain a steady-state pH. Activated at low pH (under pH 4.6) by luminal side protons: selectively mediates lysosomal proton release from lysosomes, eliciting a proton leak that balances V-ATPase activity to maintain pH homeostasis (By similarity). Regulation of lumenal pH stability is required for autophagosome-lysosome fusion. May also act as a potassium channel at higher pH, regulating potassium conductance in endosomes and lysosomes. The potassium channel activity is however unclear as it was tested in non-physiological conditions for a lysosomal channel (By similarity). Constitutes the pore-forming subunit of the lysoK(GF) complex, a complex activated by extracellular growth factors. The lysoK(GF) complex is composed of TMEM175 and AKT (AKT1, AKT2 or AKT3), a major target of growth factor receptors: in the complex, TMEM175 channel is opened by conformational changes by AKT, leading to its activation. The lysoK(GF) complex is required to protect neurons against stress-induced damage.
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:Q9BSA9}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9BSA9}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclin-G-associated kinase
Sequence:
MSRLQTEEQAVDSEGDSSLHRRNEEGTQSSHRMLGFSDALLSIIATVMILPVTHTEISPEQQFDKSIQKLLATRIAVYLMTFLIVTVAWTAHTRLFQVVGKIDDTLALLNLACMMTITLLPYTFSLMVTFPDVPLGIFLFCVCVIAIGSVQAMIVGYAFHFPHLLNPQIQCSTHRDLSRRHILHLVLRGPALCFVAAVFSLFFFPLSYLLMVTVIFLPHISKATTWCKDKLMGQRESPAHDMEPFSIDLHAPLSKERVEAFSDGVYAIVATLLILDICEDNVPDPKDVQEKFSGSLVAALGAYGPQFLAYFGSFATVGLLWFAHHSLFLHVRKATQTMGLLNILSLAFVGGLPLAYQQTSAFARQPHDELERVRVSCAIIFFASIFQFAIWTTALLHQTETLQPAVQFGGQEHAFMFAKLALYPCASLLAFAATCLLSRFSTAIFHLMQISVPFAFLLLRLLVRLALAGLQVLRGLWPHHPQQDQSEPEAQSQLLPDPC
Protein: Uridine 5'-monophosphate synthase (UMP synthase) [Includes: Orotate phosphoribosyltransferase (OPRTase) (EC 2.4.2.10); Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23) (OMPdecase)] (P09556)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Participates in the last two steps of the pyrimidine biosynthetic pathway leading to UMP synthesis.
Interaction partners:
- Protein transport protein got1 homolog
- Multifunctional protein pyr1-3
- Dihydroorotate dehydrogenase
- Bifunctional purine biosynthetic protein purD
- Dihydropyrimidine dehydrogenase [NADP
- UMP-CMP kinase
- Cytochrome b5 heme-binding domain-containing protein
- Cytochrome b5 reductase
- Uridine-cytidine kinase A
- Uracil phosphoribosyltransferase
Sequence:
MNIKELVLKLNEIDAIKLGEFKLKSGIISPIYIDLRVTVSSPPLLAAIAEMMYQKVYKSGNAQETPALVCGVPYTALPIATGMSIANNIPMVVRRKEAKAYGTKQLIEGRFKEGDNVLVVEDLVTSGASVLETVRDLNSVGLKVTDVVVLLDRQQGARQALEKQGYRLHSVFTMEELINTLIEAGKLTGRTLELVQSFLDANRNVVVPLPPTLAPPAPAPIVINKPFEERAKLASNPMASKLFTLMSSKKTNLAVAADLTDKQQLLDLAESIGSEICVLKTHVDIIDNYDEEFIKSLKCIAAKHNFLIFEDRKFADIGNTVKYQFENGVYKISKWADMVTVHGVAGSSIVDGFKSGLKEYGSGLLLLAQMSSKGSLCVGDYTTQMIEMANNNKEEVMGLICQERLPSMTDGLVLMTPGVQFNSTGDAMGQQYNTPEYIIKEKNTDVIIVGRGIYQSNDPKSVANKYRTAAWETYQSKF
Protein: Charged multivesicular body protein 5 (Chromatin-modifying protein 5) (SNF7 domain-containing protein 2) (Q9D7S9)
Organism: Mus musculus (Mouse)
Function: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4 (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NZZ3}. Endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Midbody {ECO:0000250|UniProtKB:Q9NZZ3}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Flemming body. {ECO:0000250|UniProtKB:Q9NZZ3}.
Interaction partners:
- Vacuolar protein sorting-associated protein VTA1 homolog
- Vacuolar protein sorting-associated protein 4B
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 3
- IST1 homolog
- Vacuolar protein sorting-associated protein 4A
- Charged multivesicular body protein 4c
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 6
- Charged multivesicular body protein 4b
Sequence:
MNRFFGKAKPKAPPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMREGPAKNMVKQKALRVLKQKRMYEQQRDNLAQQSFNMEQANYTIQSLKDTKTTVDAMKLGVKEMKKAYKEVKIDQIEDLQDQLEDMMEDANEIQEALGRSYGTPELDEDDLEAELDALGDELLADEDSSYLDEAASAPAIPEGVPTDTKNKDGVLVDEFGLPQIPAS
Protein: Fibroblast growth factor 4 (FGF-4) (Heparin secretory-transforming protein 1) (HST) (HST-1) (HSTF-1) (Heparin-binding growth factor 4) (HBGF-4) (Transforming protein KS3) (P08620)
Organism: Homo sapiens (Human)
Function: Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Required for normal limb and cardiac valve development during embryogenesis.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Fibroblast growth factor receptor 3
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Beta-klotho
- Fibroblast growth factor-binding protein 1
- Decorin
Sequence:
MSGPGTAAVALLPAVLLALLAPWAGRGGAAAPTAPNGTLEAELERRWESLVALSLARLPVAAQPKEAAVQSGAGDYLLGIKRLRRLYCNVGIGFHLQALPDGRIGGAHADTRDSLLELSPVERGVVSIFGVASRFFVAMSSKGKLYGSPFFTDECTFKEILLPNNYNAYESYKYPGMFIALSKNGKTKKGNRVSPTMKVTHFLPRL
Protein: RGS domain-containing protein (G5EFV0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSCAISCFGKIIVCVTHNSSPSGKPYVSGSVSVEKKNQENDGPPTYEIVFGWSQSFENLMKHRAGQKYFAEFLKGEYSDENILFWQACEELKREKNAEKIEEKARIIYEDFISILSPKEVSLDSRVREIVNTNMGRPSASTFDEAQNQIYTLMQRDSYPRFLASNIYKTVMGTFGIKEEAV
Protein: Cdc42 effector protein 1 (Binder of Rho GTPases 5) (Serum protein MSE55) (Q00587)
Organism: Homo sapiens (Human)
Function: Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:10430899}; Peripheral membrane protein {ECO:0000269|PubMed:10430899}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10430899}.
Interaction partners:
- Cell division control protein 42 homolog
- Rho-related GTP-binding protein RhoQ
Sequence:
MPGPQGGRGAATMSLGKLSPVGWVSSSQGKRRLTADMISHPLGDFRHTMHVGRGGDVFGDTSFLSNHGGSSGSTHRSPRSFLAKKLQLVRRVGAPPRRMASPPAPSPAPPAISPIIKNAISLPQLNQAAYDSLVVGKLSFDSSPTSSTDGHSSYGLDSGFCTISRLPRSEKPHDRDRDGSFPSEPGLRRSDSLLSFRLDLDLGPSLLSELLGVMSLPEAPAAETPAPAANPPAPTANPTGPAANPPATTANPPAPAANPSAPAATPTGPAANPPAPAASSTPHGHCPNGVTAGLGPVAEVKSSPVGGGPRGPAGPALGRHWGAGWDGGHHYPEMDARQERVEVLPQARASWESLDEEWRAPQAGSRTPVPSTVQANTFEFADAEEDDEVKV
Protein: Lectin alpha chain [Cleaved into: Lectin beta chain; Lectin gamma-1 chain; Lectin gamma-2 chain] (P58907)
Organism: Dioclea virgata
Function: D-mannose/D-glucose-binding lectin. Has anti-inflammatory activity in rats. Induces histamine release in mast cells from hamster and rat. Induces lymphocyte proliferation and IFNG production. Shows toxicity against the aquatic snail B.glabrata at concentrations higher than 20 ug/ml.
Subcellular location: Vacuole, aleurone grain.
Interaction partners:
Sequence:
ADTIVAVELDSYPNTDIGDPSYPHIGIDIKSVRSKSTARWNMQTGKVGTAHISYNSVAKRLSAVVSYTGSSSTTVSYDVDLNNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKTNSIADANSLHFSFNQFSQNPKDLILQGDATTDSDGNLQLTRVSSDGSPQGSSVGRALFYAPVHIWEKSAVVASFDATFTFLIKSPDRDPADGITFFIANTDTSIPSGSGGRLLGLFPDAN
Protein: Krueppel-like factor 17 (Germ cell-specific zinc finger protein) (Zinc finger protein 393) (Q8CFA7)
Organism: Mus musculus (Mouse)
Function: Transcription repressor that binds to the promoter of target genes and prevents their expression. Acts as a negative regulator of epithelial-mesenchymal transition and metastasis in breast cancer. Specifically binds the 5'-CACCC-3' sequence in the promoter of ID1, a key metastasis regulator in breast cancer, and repress its expression. May be a germ cell-specific transcription factor that plays important roles in spermatid differentiation and oocyte development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MEQDNKEQAMHQPPMDNKMLVPVSNVPVSSGNSGFHQPPATQYLPEMMRSYMASAEELRCNEREWESQLIRSLPEHGVRCPSQLAPIPFQNYCQRSIGRGSHVMPVGSSGTLGVTISFSENLMPQGGLPSSRGVSVMAHSSAPAMPYPMPPTVPATTGSLKHGILLVPGMASAGTHAVAPFMDQMLHSINPCNPEMLPARFQQLLPLDSQDSLVTESNTQEEPFVREPPTPAPEGAESPSTSRGATRRQSPVSRPYVCTYNSCGKSYTKRSHLVSHQRKHTGVKPFACDWNGCTWKFFRSDELGRHKRIHTRYRPHKCDECDREFMRSDHLRQHKRTHLPK
Protein: Transcriptional regulator, TetR family (O53295)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MVRIPRPHPSAKPGVKVDARSERWREHRKKVRNEIVDAAFRAIDRLGPELSVRQIAEEAGTAKPKIYRHFTDKSDLLEAIGMRLRDMLWAAIFPSLDLATDSAREVIRRSVEEYVNLVDQHPNVLRVFIQGRSAKQSEATVRTLNEGREITLAMAEMFNNELREMELNRAALELAAFAAFGSAASATEWWLGPEPDSPRRMPREQFVAHLTTIMMGVIVGTAEALGIAVDPDQPIHDAVPNNPAVR
Protein: DNA-binding protein RFXANK (Ankyrin repeat-containing adapter protein Tvl-1) (Regulatory factor X subunit B) (RFX-B) (Regulatory factor X-associated ankyrin-containing protein) (Q9Z205)
Organism: Mus musculus (Mouse)
Function: Activates transcription from class II MHC promoters. Activation requires the activity of the MHC class II transactivator/CIITA. May regulate other genes in the cell. RFX binds the X1 box of MHC-II promoters (By similarity). May also potentiate the activation of RAF1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10329666}. Nucleus {ECO:0000269|PubMed:10329666}.
Interaction partners:
- Regulatory factor X-associated protein
- DNA-binding protein Rfx5
- MHC class II transactivator
- Histone deacetylase 4
- Cyclic AMP-responsive element-binding protein 1
- Protein NLRC5
- Histone deacetylase 5
Sequence:
MEPTQVAENLVPNQQPPVPDLEDPEDTRDESPENSDTVVLSLFPCTPDAVNPEADASASSLQGSFLKHSTTLTNRQRGNEVSALPATLDSLSIHQLAAQGELSQLKDHLRKGACPACTCLSGNNLINKPDERGFTPLIWASAFGEIETVRFLLDWGADPHILAKERESALSLASMGGYTDIVRLLLDRDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKVQQVMESHILRLFQSTLGPVDPE
Protein: Peroxiredoxin-4 (EC 1.11.1.24) (Antioxidant enzyme AOE372) (Peroxiredoxin IV) (Prx-IV) (Thioredoxin peroxidase AO372) (Thioredoxin-dependent peroxide reductase A0372) (Thioredoxin-dependent peroxiredoxin 4) (Q9Z0V5)
Organism: Rattus norvegicus (Rat)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q13162}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13162}. Secreted {ECO:0000269|PubMed:10025941, ECO:0000269|PubMed:10731722}.
Interaction partners:
- Thioredoxin domain-containing protein 5
- Endoplasmic reticulum protein 44.
- Peroxiredoxin-5, mitochondrial
- Thioredoxin
- Protein disulfide-isomerase A6
- Sulfiredoxin-1
- Protein disulfide isomerase family A, member 6 like 1
- Thioredoxin domain-containing protein 3
Sequence:
METWSKLLDGTTPSRRWRKLVLLLPPLLLFLLQTEALQGLESDDRFRTRENECHFYAGGQVYPGEVSRVSVADHSLHLSKAKISKPAPYWEGTAVINGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRIEEFKSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLNHQISKDYGVYLEDSGHTLRGLFIIDDKGVLRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN
Protein: Xrn1 N-terminal domain-containing protein (Q38B12)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGVPDFLKFVSRTAPGALCRLPRDSVATPLCFDFILIDATNAAQTIGLEVLGAFLRRSQVQVRQAVIFAVDGQRQRSDTARAQRTHSTVLDTDVVIQRFGSDLQRHYEQCGGESVPQVLISGRHVAGEADYKILDIQRFIIMQVFTNGGSDKLPTFCMVSEDSDVLCGALCGPAPHTVSIVTKLRDTMIDMCVLRVSHVLAHVGVCMEAFISGAETSVEEEKDMTVDSGPVGSTDSIFHAEQMETEGDGEEQITRRKKVDGPMVSTGVRVVLGDSDDDDDHAQSEGLRDTRNGGGNMDNELHPPKAGPSTCVPTMVSQAAVAEILQNSCVDMVFLFIIVMGNGGSVPPVIRGATKVDIQSCWRAYCKMKYNTAESEREKEMGRTLFDLNGILSIKDQQSDDIASVVVDCSFLCTLLDTAQYADVQSRPMTDEDKERALLYLSHAAYAALRYIVACNVGRVAAGRVDDTFLDTRNISEVVSVPSVAAFLSVLNQTKKRTLHFPLVGSATTDVLSSAAKGVSAVEEAITAARIRSGRGESRMVLQTDVAGTLASAVTASGAQRCVQLSRFLAPFTTAEVSRKNIMDCLKHSPRNYSKISNSVAEFGGRLSTFSRLLLAWRRTIELCVPTLGALAGKETATSTLGAVAGDEGKGVAALSSSGLLTTGRSCAKMSYSFELRRMAPVLVSEQTNHKSNAATDATRRDILFKALRISHDYVEAPQIINSKSKEPELSSSGDVDKKCQLERKRHREGETLISEREGASAPGKRHRTQSVKDVIRSKGKNKKVKRKKLS
Protein: endo-polygalacturonase (EC 3.2.1.15) (G2YD64)
Organism: Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- WH2 domain-containing protein
- Similar to actin-related protein 2/3 complex subunit ARP3
- Actin-related protein 2/3 complex subunit
- Actin-related protein 2/3 complex subunit 3
- Protein BZZ1
- Arp2/3 complex 34 kDa subunit
- Actin-related protein 2/3 complex subunit 5
- pectinesterase
- Cell division control protein
- RRM domain-containing protein
Sequence:
MRSAIILGGLASLALACDNPDHDSCANAFTVSSAAAGPFCATYTQAANSASTGLPAFATACASNPKKLSSACSCLQVATTLATVAKSTSAAAVSGVAASSAAAVPVASGSAAASSYVRSSYVKSVTASASVQAHKATTGVVASTSVPAVSSAAGASTAVITSAPAAPAGCTATAYADIADIIASCTNIVLDNISAPASSTIDLQKLQDGSTVTFSGTTSFGTTADSDFDPIVVKGTDITITGAAGHVIDGNGAAYWDGQGSNGGTDKPDHFFVVKDVVNGVISNLNIQNWPTHCFDITGAQGLTVSGLTLDNSAGDAPNSASGDDPAAHNSDGFDISGSDSVTLKDIVVKNQDDCVAVTSGSNILVTGLTCSGGHGLSIGSVGGKSNNTVSGVTFSDSTITNSQNGCRIKSNSGTTGTIENVTYSNIKMSNISDYGIDVQQDYLNGGPTGEPTNGVKISGITFSSVTGTTTDDAYNYYVLCGSGSCSDITFTDVSISGGGKTSTCNYPSTGCPS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q582J2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mitotic cyclin
- Tyrosine phosphatase, putative
- Cell cycle associated protein MOB1, putative
- Cell cycle associated protein MOB1, putative
- BTB domain-containing protein
Sequence:
MSTRKEPPKVLKGAAYTECSPISDVSHHKASASKAFLENHYRGMLRDTRSGNTARPVGPRPREPCVDDFVLVKRIGKGAFGEVYLCYKKYDNDKQLYALKRMRKTDMIRKKQISHVRSEKDVMAEAASTNPWVVKLYLSFQDEQYLYMVMEYMPGGDMISWLCIKQRFDVESTRFYIAELCAAVASVHDMFFVHRDIKPDNILLDAKGHIKLTDFGLSKRFAKVGEELLDLEEGNDALCSSNSSANLSNTCGSTCQGPNSVPVVSPHNPHSPTANYNSLTPAGSHASAHPQARRIFESIVGSPGYIAPEILLRQRYGVNCDWWSVGVIMYEMLYGIPPFFSSDTSSTCHKITHWREYLTYPSDRGVPPEATDLLRRLMCDQRDRLDFQGVKEHPFFNDIDWERLRETPPAFVPELSDPLDTHYFPEVEDNTPQQHHQRPEERNAVREVDPRGVIFADYKFNLKR
Protein: Heat shock 70 kDa protein 4 (HSP70-4) (P11145)
Organism: Trypanosoma brucei brucei
Interaction partners:
Sequence:
MTYEGAIGIDLGTTYSCVGVWQNERVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFSDSVVQSDMKHWPFKVVTKGDDKPVIQVQFRGETKTFNPEEISSMVLLKMKEVAESYLGKQVAKAVVTVPAYFNDSQRQATKDAGTIAGLEVLRIINEPTAAAIAYGLDKADEGKERNVLIFDLGGGTFDVTLLTIDGGIFEVKATNGDTHLGGEDFDNRLVAHFTEEFKRKNKGKDLSSNLRALRRLRTACERAKRTLSSAAQATIEIDALFENIDFQATITRARFEELCGDLFRGTLQPVERVLQDAKMDKRAVHDVVLVGGSTRIPKVMQLVSDFFGGKELNKSINPDEAVXYGAAVQAFILTGGKSKQTEGLLLLDVAPLTLGIETAGGVMTALIKRNTTIPTKKSQIFSTYSDNQPGVHIQVFEGERTMTKDCHLLGTFDLSGIPPAPRGVPQIEVTFDLDANGILSVSAEEKGTGKRNQIVITNDKGRLSKADIERMVSDAAKYEAEDKAHVXXIDAKNGLENYAFSMKNTINDPNVAGKLDDADKNAVTTAVEEALRWLNDNQEASLEEYNHRQKELEGVCAPILSKMYQGMGGGDGPGGMPEGMPGGMPGGMPGGMGGGMGGAAASSGPKVEEVD
Protein: Uncharacterized protein YeaE (P76234)
Organism: Escherichia coli (strain K12)
Interaction partners:
Sequence:
MQQKMIQFSGDVSLPAVGQGTWYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLREKVFLVSKVYPWNAGGQKAINACEASLRRLNTDYLDLYLLHWSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGGNQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQAGRLRNGLLKNAVVNEIAHAHNISAAQVLLAWVISHQGVMAIPKAATIAHVQQNAAVLEVELSSAELAMLDKAYPAPKGKTALDMV
Protein: Embryonic ectoderm development (A0A8I6A2I3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPAAKKQKLSSDENSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR
Protein: 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXP reductoisomerase) (EC 1.1.1.267) (1-deoxyxylulose-5-phosphate reductoisomerase) (2-C-methyl-D-erythritol 4-phosphate synthase) (P45568)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Interaction partners:
- 1-deoxy-D-xylulose-5-phosphate synthase
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- Ditrans,polycis-undecaprenyl-diphosphate synthase
- Farnesyl diphosphate synthase
- Phosphatidate cytidylyltransferase
- Isopentenyl-diphosphate Delta-isomerase
Sequence:
MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS
Protein: MLO-like protein 6 (AtMlo6) (Q94KB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in modulation of pathogen defense and leaf cell death. Activity seems to be regulated by Ca(2+)-dependent calmodulin binding and seems not to require heterotrimeric G proteins (By similarity).
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Oleosin 20.3 kDa
- AT3G21215 protein
- Syringolide-induced protein
- Arabidiol synthase
Sequence:
MADQVKEKTLEETSTWAVAVVCFVLLLISIVIEKLIHKIGSWFKKKNKKALYEALEKVKAELMLMGFISLLLTIGQGYISNICIPKNIAASMHPCSASEEARKYGKKDVPKEDEEENLRRKLLQLVDSLIPRRSLATKGYDKCAEKGKVAFVSAYGMHQLHIFIFVLAVCHVIYCIVTYALGKTKMRRWKKWEEETKTIEYQYSHDPERFRFARDTSFGRRHLSFWSKSTITLWIVCFFRQFFRSVTKVDYLTLRHGFIMAHLAPGSDARFDFRKYIQRSLEEDFKTIVEINPVIWFIAVLFLLTNTNGLNSYLWLPFIPFIVILIVGTKLQVIITKLGLRIQEKGDVVKGTPLVQPGDHFFWFGRPRFILFLIHLVLFTNAFQLAFFVWSTYEFGLKNCFHESRVDVIIRISIGLLVQILCSYVTLPLYALVTQMGSKMKPTVFNERVATALKSWHHTAKKNIKHGRTSESTTPFSSRPTTPTHGSSPIHLLRNAPHKRSRSVDESFANSFSPRNSDFDSWDPESQHETAETSNSNHRSRFGEEESEKKFVSSSVELPPGPGQIRTQHEISTISLRDFSFKR
Protein: Glycogen [starch] synthase (EC 2.4.1.11) (Q5A850)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- glycogenin glucosyltransferase
- 1,4-alpha-glucan-branching enzyme
- Glycogenin glucosyltransferase
- Trehalose-phosphatase
- Alpha-1,4 glucan phosphorylase
- UTP--glucose-1-phosphate uridylyltransferase
- Trehalose 6-phosphate synthase/phosphatase complex subunit
- Alpha,alpha-trehalose-phosphate synthase
- 1,3-beta-glucan synthase
- 1,3-beta-glucan synthase
Sequence:
MARDIDNHLLFEVATEVAHKVGGIYSVLKSKAPVTVAEYRERYTLLGPLHYDSAQIEVEELPVTDPHIKQTLDSMSSKGIRWLYGRWLIEGAPRVLLFDIWSAGHYLNEWKADLWNVAGIPTPDHDSETNDAILLGYLVAWFLGELVYNDRDRAVICQCHEWLAGIALPLCRKRRIDVTTIFTTHATLLGRYLCAGSTDFYNNLDKFDVDAEAGKRGIYHRYCIERSATHSADVFTTVSDITAYEAEHLLKRKPDGVLPNGLNVVKFQAVHEFQNLHAIKKAKINEFVKGHFYGNYDFDLDNTLYFFIAGRYEFRNKGCDFFIESLARLNHKLKEAGSKTTVVAFIIMPGKTQSYTVETLKGQAVVKQLESTIGEVQKKVGERLFEYCARYPNTDHHGNDEVPTIDELIKPADRVLLKRRIFALKRDGLPPIVTHNMVDDSTDPVLNHIRRVQLFNKPEDRVKIIFHPEFLNANNPILSLDYDEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSITTNLSGFGCYMNDLVENPTDYGIYIVDRRMKSVDESINQLTDYMFDFCAKSRRQRINQRNRTERLSVLLDWRSVHSEYSKARLLALKRAYPDYVGEKVVESKMKITRPMSVPGSPRSLLLTPGDLGSLQDANQDISYFELGEEET
Protein: RH08962p (Q7JYY0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FLFRDPHTKLRERIIMQLFVRGLETIEALEVSQDATIAGVKNQLAQIHGFNAEEFSLDCEGITLANETPVTALSSFELDLNIPMLGGKVHGSLARAGKVKGQTPKVEKQEKKKKKTGRAKRRIQYNRRFVNFVQGFGRRRGPNANST
Protein: Plastid division protein CDP1, chloroplastic (ARC6-homolog protein) (Protein CHLOROPLAST DIVISION SITE POSITIONING 1) (AtCDP1) (Protein PARALOG OF ARC6) (Protein STROMULE BIOGENESIS ALTERED 2) (Q8VY16)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the plastid division machinery required for PDV1 localization to constriction sites. Involved in chloroplast division site placement. Required for the proper formation of FtsZ rings at the division site in nongreen plastids (e.g. etioplasts). Inhibits FtsZ assembly, functioning as an antagonistic regulator of FtsZ dynamics against ARC6, by recruiting ARC3 to the middle of the plastid to facilitates its interaction with FtsZ proteins. Required during stromule biogenesis in the leaf epidermis, especially in non-mesophyll cells plastids.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:19453460}; Single-pass membrane protein {ECO:0000269|PubMed:19453460}. Note=Localizes both to the mid-plastid and to a single spot at one pole. {ECO:0000269|PubMed:19453460}.
Interaction partners:
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 3
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerase II subunit 4
- Transcription initiation factor IIF subunit alpha
- Plastid division protein PDV1
- Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 homolog
- Pentatricopeptide repeat-containing protein At4g30825
- Embryo defective 2739
- Cell division protein FtsZ homolog 1, chloroplastic
- General transcription and DNA repair factor IIH subunit TFB2
Sequence:
MPVAYTFPVLPSSCLLCGISNRSTSFVVDRPELQISGLLVVRSESGEFFGSGLSLRRFQREGRRRLNAAGGGIHVVDNAPSRTSSLAASTSTIELPVTCYQLIGVSEQAEKDEVVKSVINLKKTDAEEGYTMEAAAARQDLLMDVRDKLLFESEYAGNLKEKIAPKSPLRIPWAWLPGALCLLQEVGQEKLVLDIGRAALRNLDSKPYIHDIFLSMALAECAIAKAAFEVNKVSQGFEALARAQSFLKSKVTLGKLALLTQIEESLEELAPPCTLDLLGLPRTPENAERRRGAIAALRELLRQGLSVEASCQIQDWPCFLSQAISRLLATEIVDLLPWDDLAITRKNKKSLESHNQRVVIDFNCFYMVLLGHIAVGFSGKQNETINKAKTICECLIASEGVDLKFEEAFCSFLLKQGSEAEALEKLKQLESNSDSAVRNSILGKESRSTSATPSLEAWLMESVLANFPDTRGCSPSLANFFRAEKKYPENKKMGSPSIMNHKTNQRPLSTTQFVNSSQHLYTAVEQLTPTDLQSPVVSAKNNDETSASMPSVQLKRNLGVHKNKIWDEWLSQSSLIGRVSVVALLGCTVFFSLKLSGIRSGRLQSMPISVSARPHSESDSFLWKTESGNFRKNLDSVNRNGIVGNIKVLIDMLKMHCGEHPDALYLKSSGQSATSLSHSASELHKRPMDTEEAEELVRQWENVKAEALGPTHQVYSLSEVLDESMLVQWQTLAQTAEAKSCYWRFVLLHLEVLQAHIFEDGIAGEAAEIEALLEEAAELVDESQPKNAKYYSTYKIRYILKKQEDGLWKFCQSDIQIQK
Protein: Putative activator of 90 kDa heat shock protein ATPase homolog 2 (Activator of HSP90 ATPase homolog 2 pseudogene) (Q719I0)
Organism: Homo sapiens (Human)
Function: Co-chaperone that stimulates HSP90 ATPase activity.
Interaction partners:
Sequence:
MAKWGQGNPHWIVEEREDGTNVNNWRWTERDATSLSKGKFQELLVGIVVENDAGRGEINELKQVEGEASCSSRKGKLIFFYEWNIKLGWKGIVKESGVKHKGLIEIPNLSEENEVDDTEVSLSKKKGDGVILKDLMKTAGTAKVREALGDYLKALKTEFTTGMILPTKAMATQELTVKRKLSGNTLQVQASSPVALGVRIPTVALHMMELFDTTVEQLYSIFTVKELTNKKIIMKWRCGNWPEEHYAMVALNFVPTLGQTELQLKEFLSICKEENMKFCWQKQHFEEIKGSLQLTPLNG