wanglab/gogpt-training-data huggingface dataset:
Protein: Guanine nucleotide-binding protein G(o) subunit alpha (EC 3.6.5.-) (P18872)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Stimulated by RGS14. The G(o) protein function is not clear.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15585744}. Membrane {ECO:0000250|UniProtKB:P09471}; Lipid-anchor {ECO:0000250|UniProtKB:P09471}.
Interaction partners:
- Regulator of G-protein signaling 16
- D
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 7
Sequence:
MGCTLSAEERAALERSKAIEKNLKEDGISAAKDVKLLLLGAGESGKSTIVKQMKIIHEDGFSGEDVKQYKPVVYSNTIQSLAAIVRAMDTLGVEYGDKERKTDSKMVCDVVSRMEDTEPFSAELLSAMMRLWGDSGIQECFNRSREYQLNDSAKYYLDSLDRIGAGDYQPTEQDILRTRVKTTGIVETHFTFKNLHFRLFDVGGQRSERKKWIHCFEDVTAIIFCVALSGYDQVLHEDETTNRMHESLMLFDSICNNKFFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYPGSNTYEDAAAYIQTQFESKNRSPNKEIYCHMTCATDTNNIQVVFDAVTDIIIANNLRGCGLY
Protein: Pleckstrin homology domain containing A7 (E9PKC0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAATVGRDTLPEHWSYGVCRDGRVFFINDQLRCTTWLHPRTGEPVNSGHMIRSDLPRGWEEGFTEEGASYFIDHNQQTTAFRHPVTGQFSPENSEFILQEEPNPHMSKQDRNQRPSSMVSETSTAGTASTLEAKPGPKIIKSSSKVHSFGKRDQAIRRNPNVPVVVRGWLHKQDSSGMRLWKRRWFVLADYCLFYYKDSREEAVLGSIPLPSYVISPVAPEDRISRKYSFKAVHTGMRALIYNSSTAGSQAEQSGMRTYYFSADTQEDMNAWVRAMNQAAQVLSRSSLKRDMEKVERQAVPQANHTESCHECGRVGPGHTRDCPHRGHDDIVNFERQEQEGEQYRSQRDPLEGKRDRSKARSPYSPAEEDALFMDLPTGPRGQQAQPQRAEKNGMLPASYGPGEQNGTGGYQRAFPPRTNPEKHSQRKSNLAQVEHWARAQKGDSRSLPLDQTLPRQGPGQSLSFPENYQTLPKSTRHPSGGSSPPPRNLPSDYKYAQDRASHLKMSSEERRAHRDGTVWQLYEWQQRQQFRHGSPTAPICLGSPEFTDQGRSRSMLEVPRSISVPPSPSDIPPPGPPRVFPPRRPHTPAERVTVKPPDQRRSVDISLGDSPRRARGHAVKNSSHVDRRSMPSMGYMTHTVSAPSLHGKSADDTYLQLKKDLEYLDLKMTGRDLLKDRSLKPVKIAESDTDVKLSIFCEQDRVLQDLEDKIRALKENKDQLESVLEVLHRQMEQYRDQPQHLEKIAYQQKLLQEDLVHIRAELSRESTEMENAWNEYLKLENDVEQLKQTLQEQHRRAFFFQEKSQIQKDLWRIEDVTAGLSANKENFRILVESVKNPERKTVPLFPHPPVPSLSTSESKPPPQPSPPTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVTSPLQSPTKAKPKVEDEAPPRPPLPELYSPEDQPPAVPPLPREATIIRHTSVRGLKRQSDERKRDRELGQCVNGDSRVELRSYVSEPELATLSGDMAQPSLGLVGPESRYQTLPGRGLSGSTSRLQQSSTIAPYVTLRRGLNAESSKATFPRPKSALERLYSGDHQRGKMSAEEQLERMKRHQKALVRERKRTLGQGERTGLPSSRYLSRPLPGDLGSWKREQDFDLQLLERVVQGEKKDKEENGWLKVQAMPVTELDLEPQDYDLDISRELSKPEKVSIPERYVELDPEEPPSLEELQARYRKAEKIRNILARSSMCNLQPTSGQDQNSVADLDLQLQEQERIINISYALASEASQRSKQVAAQAVTDP
Protein: Insulin-like growth factor 2 (Insulin-like growth factor II) (IGF-II) [Cleaved into: Preptin] (P10764)
Organism: Ovis aries (Sheep)
Function: The insulin-like growth factors possess growth-promoting activity (By similarity). Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development. IGF2 is influenced by placental lactogen. Also involved in tissue differentiation. In adults, involved in glucose metabolism in adipose tissue, skeletal muscle and liver. Acts as a ligand for integrin which is required for IGF2 signaling. Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation (By similarity). Inhibits myoblast differentiation and modulates metabolism via increasing the mitochondrial respiration rate (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01344, ECO:0000250|UniProtKB:P09535}.
Interaction partners:
- Cation-independent mannose-6-phosphate receptor
- Tyrosine-protein kinase receptor
- Insulin like growth factor binding protein 3
- Insulin-like growth factor-binding protein 6
- Insulin-like growth factor-binding protein 2
- Insulin-like growth factor-binding protein 1
- Tyrosine-protein kinase receptor
- Insulin-like growth factor 1
- Glypican-3
- Insulin-like growth factor-binding protein 4
Sequence:
MGITAGKSMLALLAFLAFASCCYAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPSSRINRRSRGIVEECCFRSCDLALLETYCAAPAKSERDVSASTTVLPDDFTAYPVGKFFQSDTWKQSTQRLRRGLPAFLRARRGRTLAKELEALREAKSHRPLIALPTQDPATHGGASSEASSD
Protein: MAP3K12-binding inhibitory protein 1 (MAPK upstream kinase-binding inhibitory protein) (MUK-binding inhibitory protein) (Q99LQ1)
Organism: Mus musculus (Mouse)
Function: Inhibits the MAP3K12 activity to induce the activation of the JNK/SAPK pathway. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shows a cytoplasmic localization when co-expressed with MAP3K12. {ECO:0000250}.
Interaction partners:
- YEATS domain-containing protein 2
- Protein Dr1
- Cysteine-rich protein 2-binding protein
- Transcriptional adapter 2-alpha
- Histone acetyltransferase KAT2A
- ZZ-type zinc finger-containing protein 3
- SAGA-associated factor 29
- Transcriptional adapter 3
- Histone acetyltransferase KAT2B
- WD repeat-containing protein 5
Sequence:
MAAAAELSSSSGSERSLEQCSSPLLTREVLCEVFRSLHTLTRQLNLRDDVVKITIDWNRLQSLSASQPALLLTALEQHVLYLQPFLAKLQSLMKENSTATEIRQTEAETKSELRAIHPTEDLQDEGKPKDCDVGDVKKTQNLFDPEVVQIKAGKAEIDRRISAFIERKQAEINENNVREFCNVIDCNQENSCARTDAVFTPYPGFKSHVKVSRVVNTYGPQTRPEGIAGSGHKPTGMLRDCGNQAVEERLQNIEAHLRLQTGGPVPRDIYQRIKKLEDKILELEGISPEYFQSVNFSGKRRKVQPPQQNYSLAELDEKISALKRALLRKSREADSMAAHLP
Protein: Calcium-binding tyrosine phosphorylation-regulated protein (Calcium-binding protein 86) (Testis-specific calcium-binding protein CBP86) (Q9D424)
Organism: Mus musculus (Mouse)
Function: May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. May bind calcium in vitro (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12801634}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12801634}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:12801634, ECO:0000269|PubMed:37709195}. Note=Localizes to fibrous sheath including the surface of the longitudinal columns and ribs of the principal piece of sperm flagella.
Interaction partners:
- Fibrous sheath CABYR-binding protein
- A-kinase anchor protein 3
- Sperm surface protein Sp17
- A-kinase anchor protein 4
- Ropporin-1
Sequence:
MISSKPRLVVPYGLKTLLEGVSRAILKTNPTNITQFAAVYFKELIVFREGNSSLDIKDLIKQFHQMKVEKWAEGVTVEKKECIKEPIKPPPVPCKPTHMEKSTDTEEDNVAGPLFSNKTTQFPSVHAEVQSEETSEGARGPSDKPTTPKTDYTPPSSPPPAPVSAEYAYVPADPAQFAAQMLGNVPSTYSEVLMVDVATSTPAVPQDVLSAEFAEEVVLSAPLVCSGETVEVQVVSKTSAQVVVGPVSEAEPPKASSAPLQGEQEPPAHEAPDTQVTSASRISSIYNDVPVNEGVVYVEEIPGYIVIPFTDHDQVACVKEIEQSPPGSPKAVEPKTKISIESLKTVQVEENSQHKSSVHVEAEATVLLSNTALDGQPEVPAEPLDAEGFFKVASENSLHLETEIVIINPDDPGQEESGGNAAPHSSGDPFPPAPGGLTEPEMQPDGEAAPEQV
Protein: GLC7-interacting protein 2 (P40036)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Glycogen [starch] synthase isoform 2
- Serine/threonine-protein phosphatase PP1-2
- Serine/threonine-protein phosphatase 1 regulatory subunit PIG1
- GLC7-interacting protein 1
- Serine/threonine-protein phosphatase PP-Z1
- Serine/threonine-protein phosphatase 1 regulatory subunit GAC1
- Glucoamylase, intracellular sporulation-specific
- Protein REG2
- Protein phosphatase 1 regulatory subunit SDS22
- Glycogen [starch] synthase isoform 1
Sequence:
MYIKAEQKPQQFERKNEKLDRNKNQQLPDLETDFKGYRVNSDLYNKERDGSTEETLNSLKFLHKPQRVTQMRANRFPEEEVQRNTDLNKRIFSAGNDENVDNESGWSKIAAAKNHTSVESLNGSTRPPFKIELPPLSPKSTVPKSFQAEYPEAKSPGNDMNFEYDEEILIPFAPPVYKKSGELLKSSLKRRSKSLPTTPGIRSGNGVQARDGSPMLIRSKSVHFDQAAPVKYFAEDESPINVNKTEQHDNCLSFKHKPVNLMVDPEEETKMLSSGLETTSIDDDLTTVAPKGFAHPAKISNPNNGKGTNNTKLRKSKRFQNLLKNRTDMPPSKSNKKFVNGGGAHEISDRNSKNYHVVGLYSKNFPILSNKNPKSLKLNIFINLSQNKKVFLQELSLYIHRDNNYFSNSSSFYNIPNSHNGNDCNGVAKGYNAGCTRLIAGRILVKNIFYDKRVVVRYTWDSWRTTHEVECVYISDGDGILPGTNMDIFHFIIDDVSKVDPRGKLEFCIHYSTRNDYEREEYWDNNNGNNYKVDVVMDGFNDPFAAAA
Protein: Uncharacterized protein LOC100124596 (Zgc:171929 protein) (A7E2L3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPRPFLVKRRQAAGAGWTWKDTETTHTHTAAAHTHTSLDSVCAPAVQKHTAAPAAAALERHRGDYVMERLPPPPPAALSSSAAALHKPRDASSAGSSEFLCSVCHKLFPLQRMLTRHLKCHSLIKRHPCRYCGKGFNDTFDLKRHMRTHTGIRPYRCDLCEKAFTQRCSLESHLRKIHGVQQQYAYRQRRSKIFVCEDCGFTSSRPDQYFLHVRQQHPGSPALRRYYRKHMLEGPGPHNISPYMLYPSAGLYI
Protein: Draxin (Dorsal inhibitory axon guidance protein) (Dorsal repulsive axon guidance protein) (Neucrin) (Q6PAL1)
Organism: Mus musculus (Mouse)
Function: Chemorepulsive axon guidance protein required for the development of spinal cord and forebrain commissures. Acts as a chemorepulsive guidance protein for commissural axons during development. Able to inhibit or repel neurite outgrowth from dorsal spinal cord. Inhibits the stabilization of cytosolic beta-catenin (CTNNB1) via its interaction with LRP6, thereby acting as an antagonist of Wnt signaling pathway.
Subcellular location: Secreted {ECO:0000255|HAMAP-Rule:MF_03060}.
Interaction partners:
- Netrin receptor DCC
- Netrin-1
- Neogenin
- Cell adhesion molecule DSCAM
Sequence:
MAGCPVLRVPTLFLILLLFPELHTAGTLASGSSARNLPETHSHLPSSALWVSQASHHGRRGLGKKDRGPGRPSRAQEGAVVTATKQASQMTLGQPPAGLLQNKELLLGLTLPYPEKEARSPAWERVKKRGREHKRRRDRLRLHRGRAAIRGPSSLMKKVEPSEDRMLEGTMEESSTSLAPTMFFLTMTDGATPTTEESRILPVTSLRPQTQPRSDGEVMPTLDMALFDWTDYEDLKPEVWPSAKKKEKHWSHFTSDGNETSPAEGDPCDHHQDCLPGTCCDLREHLCTPHNRGLNNKCFDDCMCMEGLRCYAKFHRNRRVTRRKGRCVEPETANGDQGSFINI
Protein: NK2 homeobox 4b (Transcription factor Nkx2-4b) (Q58A08)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MSLSPKHSTPFSVTDILSPIEETYRKFGGMDCTGSLASPLGAYRQTSVSQPGLQQHSMGHNNGVASAYHMPHSVSQFSSAMGGYCNGSIGNMGDLPSYQDTMRNGAAATAWYSANTEPRYPTISRFMGASNGMNMAGMGTLAGMDATKSMVTLHSAPRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLSPTQVKIWFQNHRYKMKRQAKDKATLQIQQENGNVCPQQSPRRVAVPVLVKDGKPSQNGSSTPTSGHQQVQQQNVSSGAMTASGSAVVNHHQNQLVHHPLSTAEELEEMSPSPPILHSQINMAQTEAALIEYTNNMVSSNLLYGRTW
Protein: Pregnancy-specific beta-1-glycoprotein 4 (PS-beta-G-4) (PSBG-4) (Pregnancy-specific glycoprotein 4) (Pregnancy-specific beta-1-glycoprotein 9) (PS-beta-G-9) (PSBG-9) (Pregnancy-specific glycoprotein 9) (Q00888)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Pregnancy specific beta-1-glycoprotein 7
- Pregnancy-specific beta-1-glycoprotein 1
- Pregnancy-specific beta-1-glycoprotein 2
- Pregnancy-specific beta-1-glycoprotein 5
- Pregnancy-specific beta-1-glycoprotein 6
- Pregnancy-specific beta-1-glycoprotein 9
- Pregnancy-specific beta-1-glycoprotein 3
- Chorionic somatomammotropin hormone 1
- Chorionic somatomammotropin hormone 2
Sequence:
MGPLSAPPCTQRITWKGVLLTASLLNFWNPPTTAQVTIEAQPPKVSEGKDVLLLVHNLPQNLAGYIWYKGQMTYLYHYITSYVVDGQRIIYGPAYSGRERVYSNASLLIQNVTQEDAGSYTLHIIKRRDGTGGVTGHFTFTLHLETPKPSISSSNLNPREAMEAVILTCDPATPAASYQWWMNGQSLPMTHRLQLSKTNRTLFIFGVTKYIAGPYECEIRNPVSASRSDPVTLNLLPKLSKPYITINNLNPRENKDVLTFTCEPKSKNYTYIWWLNGQSLPVSPRVKRPIENRILILPNVTRNETGPYQCEIRDRYGGIRSDPVTLNVLYGPDLPSIYPSFTYYRSGENLYLSCFAESNPRAQYSWTINGKFQLSGQKLSIPQITTKHSGLYACSVRNSATGKESSKSITVKVSDWILP
Protein: Ankyrin repeat domain-containing protein 10 (Q9NXR5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSAAGAGAGVEAGFSSEELLSLRFPLHRACRDGDLATLCSLLQQTPHAHLASEDSFYGWTPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVDLRNASGLTAADIAQTQGFQECAQFLLNLQNCHLNHFYNNGILNGGHQNVFPNHISVGTNRKRCLEDSEDFGVKKARTEAQSLDSAVPLTNGDTEDDADKMHVDREFAVVTDMKNSSSVSNTLTNGCVINGHLDFPSTTPLSGMESRNGQCLTGTNGISSGLAPGQPFPSSQGSLCISGTEEPEKTLRANPELCGSLHLNGSPSSCIASRPSWVEDIGDNLYYGHYHGFGDTAESIPELNSVVEHSKSVKVQERYDSAVLGTMHLHHGS
Protein: Vacuolar protein sorting-associated protein 4 (EC 3.6.4.6) (Q54PT2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in intracellular protein transport probably out of a prevacuolar endosomal compartment. May be involved in the release of components of the bilayered coat from the endosomal membrane. The association with ESCRT-III complex mediates the ATP-dependent disassembly of the ESCRT-III complex (By similarity).
Subcellular location: Prevacuolar compartment membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein VTA1 homolog
- Charged multivesicular body protein 1
- Charged multivesicular body protein 5
- Charged multivesicular body protein 4
- IST1-like protein
- Charged multivesicular body protein 6
- Charged multivesicular body protein 3
- Charged multivesicular body protein 2a homolog 2
- Putative calpain-like cysteine protease A
- Uncharacterized protein
Sequence:
MGDVNFLQKAIQIVQQATEQDNAKNYAEAHRLYIQSLEWFTTALKYEKSERSKATIKAKTLEYLQRAEQLKEYLDKSKNKKPVAVGGNKSNSAGSANGAGKSAKEDDEDMDPEDKKRNDSLSSSIVTTKPNVKWDDVAGLYQAKEYLKEAVIFPIKFPQMFTGNRKPWKGILLYGPPGTGKSYLAKAVATEISSTFFSISPSDIVTKWLGDSEKLVKQLFEMAREKNNSVIFIDEVDSLCSSRNDQESESARRIKTEFLIQMNGVGNDSDGILVLAATNIPWGLDLAIRRRFEKRIYIGLPEPQARAKMFQIHIGSTPNTLVQADYKKLADLTEGYSGSDIGSLVKDAIMQPVRAVQCATHFKQIRAPSREDPSVMTDYVTPCSPGDPLAQEMTWMDIDPTKLKEPEITIADCLKSLRVIKPSVNKADLDRYVEFTNDFGQDGV
Protein: Neither inactivation nor afterpotential protein C (EC 2.7.11.1) (P10676)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for photoreceptor cell function. The ninaC proteins combines putative serine/threonine-protein kinase and myosin activities. Essential for the expression and stability of the rtp protein in the photoreceptors. The rtp/ninaC complex is required for stability of inad and inac and the normal termination of phototransduction in the retina.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25822849}. Cytoplasm, cytoskeleton. Nucleus {ECO:0000269|PubMed:25822849}. Membrane {ECO:0000269|PubMed:25822849}; Peripheral membrane protein {ECO:0000305}. Cell projection, rhabdomere membrane {ECO:0000269|PubMed:25822849}; Peripheral membrane protein {ECO:0000305}. Note=Localizes in the cytoplasm or punctate structures within the nuclei in the absence of rtp. Co-localizes with rtp in the rhabdomere membrane. {ECO:0000269|PubMed:25822849}.
Interaction partners:
- Inactivation-no-after-potential D protein
- Phosrestin-1
- Opsin Rh1
- Calmodulin
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Calmodulin-related protein 97A
- MIP05401p
- FI14603p
- EF-hand domain-containing protein
- GEO12020p1
Sequence:
MMYLPYAQLPDPTDKFEIYEEIAQGVNAKVFRAKELDNDRIVALKIQHYDEEHQVSIEEEYRTLRDYCDHPNLPEFYGVYKLSKPNGPDEIWFVMEYCAGGTAVDMVNKLLKLDRRMREEHIAYIIRETCRAAIELNRNHVLHRDIRGDNILLTKNGRVKLCDFGLSRQVDSTLGKRGTCIGSPCWMAPEVVSAMESREPDITVRADVWALGITTIELADGKPPFADMHPTRAMFQIIRNPPPTLMRPTNWSQQINDFISESLEKNAENRPMMVEMVEHPFLTELIENEDEMRSDIAEMLELSRDVKTLYKEPELFVDRGYVKRFDEKPEKMYPEDLAALENPVDENIIESLRHRILMGESYSFIGDILLSLNSNEIKQEFPQEFHAKYRFKSRSENQPHIFSVADIAYQDMLHHKEPQHIVLSGESYSGKSTNARLLIKHLCYLGDGNRGATGRVESSIKAILMLVNAGTPVNNDSTRCVLQYCLTFGKTGKMSGAVFNMYMLEKLRVATTDGTQHNFHIFYYFYDFINQQNQLKEYNLKADRNYRYLRVPPEVPPSKLKYRRDDPEGNVERYREFENILRDIDFNHKQLETVRKVLAAILNIGNIRFRQNGKYAEVENTDIVSRIAELLRVDEKKFMWSLTNFIMVKGGIAERRQYTTEEARDARDAVASTLYSRLVDFIINRINMNMSFPRAVFGDTNAIIIHDMFGFECFNRNGLEQLMINTLNEQMQYHYNQRIFISEMLEMEAEDIDTINLNFYDNKTALDNLLTKPDGLFYIIDDASRSCQDQDLIMDRVSEKHSQFVKKHTATEISVAHYTGRIIYDTRAFTDINRDFVPPEMIETFRSSLDESIMLMFTNQLTKAGNLTMPFEAVQHKDESERKSYALNTLSAGCISQVNNLRTLAANFRFTCLTLLKMLSQNANLGVHFVRCIRADLEYKPRSFHSDVVQQQMKALGVLDTVIARQKGFSSRLPFDEFLRRYQFLAFDFDEPVEMTKDNCRLLFLRLKMEGWALGKTKVFLRYYNDEFLARLYELQVKKVIKVQSMMRALLARKRVKGGKVFKLGKKGPEHHDVAASKIQKAFRGFRDRVRLPPLVNEKSGQLNENTADFIRPFAKKWREKSIFQVLLHYRAARFQDFVNLSQQVHIYNQRMVAGLNKCTRAVPFERINMREVNSSQLGPLPVPIKKMPFRLDQIPFYDTQYMVDPANSISRQAFPNQLLTQHMEDDEPWDSPLQRNPSMTSCALTYNAYKKEQACQTNWDRMGESDNIYNQGYFRDPQQLRRNQMQMNMNAYNNAYNSYNSNYNNQNWGVHRSGSRRNSLKGYAAPPPPPPPMPSSNYYRNNPNQQQRNYQQRSSYPPSDPVRELQNMARNEGDNSEDPPFNFKAMLRKTNYPRGSETNTYDFNNRRGSDSGDQHTFQPPKLRSTGRRYQDDEGYNSSSGNYGVSRKFGQQQRAPTLRQSPASVGRSFEDSNARSFEEAGSYVEEEIAPGITLSGYAVDI
Protein: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic (EC 1.17.7.4) (Protein CHLOROPLAST BIOGENESIS 6) (Q94B35)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is essential for chloroplast development.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18236010}.
Interaction partners:
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- Isopentenyl-diphosphate Delta-isomerase I, chloroplastic
- Farnesyl pyrophosphate synthase 2
- Farnesyl pyrophosphate synthase 1, mitochondrial
- Solanesyl diphosphate synthase 3, chloroplastic/mitochondrial)
- Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 1, chloroplastic
- Geranylgeranyl pyrophosphate synthase 10, mitochondrial
- Geranylgeranyl pyrophosphate synthase 12, chloroplastic
Sequence:
MAVALQFSRLCVRPDTFVRENHLSGSGSLRRRKALSVRCSSGDENAPSPSVVMDSDFDAKVFRKNLTRSDNYNRKGFGHKEETLKLMNREYTSDILETLKTNGYTYSWGDVTVKLAKAYGFCWGVERAVQIAYEARKQFPEERLWITNEIIHNPTVNKRLEDMDVKIIPVEDSKKQFDVVEKDDVVILPAFGAGVDEMYVLNDKKVQIVDTTCPWVTKVWNTVEKHKKGEYTSVIHGKYNHEETIATASFAGKYIIVKNMKEANYVCDYILGGQYDGSSSTKEEFMEKFKYAISKGFDPDNDLVKVGIANQTTMLKGETEEIGRLLETTMMRKYGVENVSGHFISFNTICDATQERQDAIYELVEEKIDLMLVVGGWNSSNTSHLQEISEARGIPSYWIDSEKRIGPGNKIAYKLHYGELVEKENFLPKGPITIGVTSGASTPDKVVEDALVKVFDIKREELLQLA
Protein: Luciferase-like domain-containing protein (O06328)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTNCAAGKPSSGPNLGRFGSFGRGVTPQQATEIEALGYGAVWVGGSPPAALSWVEPILQATTTLCVATGIVNIWSAPAQRVAESFHRIEAAYPGRFLLGIGVGHAEMISEYRKPYNALVEYLDRLDDYGVPANRRVVAALGPRVLGLSARRSAGAHPYLTTPEHTARARELIGPSAFLAPEHKVVLTTDSARARTVGRQALDMYFNLANYRNNWKRLGFTDDEVSRPGSDRLVDAVVAYGTPDAIAARLNEHLLAGADHVPIQVLTEDDNLVSALTELAKPLRLT
Protein: Neutrophilic granule protein (NGP) (Cystatin-like protein) (Myeloid bactenecin protein) (Myeloid secondary granule protein) (O08692)
Organism: Mus musculus (Mouse)
Function: Acts as an inhibitor of cathepsin B (CTSB) activity. Plays a role as a negative regulator of tumor vascular development, cell invasion and metastasis.
Subcellular location: Secreted {ECO:0000269|PubMed:21518852}. Cytoplasmic granule {ECO:0000269|PubMed:8749713}. Note=Localizes in cytoplasmic granules of neutrophilic precursors (PubMed:8749713). {ECO:0000269|PubMed:21518852, ECO:0000269|PubMed:8749713}.
Interaction partners:
- Cathelicidin antimicrobial peptide
- Protein S100-A9
- Protein S100-A8
- Lactotransferrin
Sequence:
MAGLWKTFVLVVALAVVSCEALRQLRYEEIVDRAIEAYNQGRQGRPLFRLLSATPPSSQNPATNIPLQFRIKETECTSTQERQPKDCDFLEDGEERNCTGKFFRRRQSTSLTLTCDRDCSREDTQETSFNDKQDVSEKEKFEDVPPHIRNIYEDAKYDIIGNILKNF
Protein: Integral membrane protein GPR137B (Transmembrane 7 superfamily member 1 protein) (O60478)
Organism: Homo sapiens (Human)
Function: Lysosomal integral membrane protein that regulates the localization and activity of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Interacts with Rag GTPases and increases the lysosomial localization and activity of Rag GTPases and thereby regulates mTORC1 translocation and activity in lysosome. Involved in the regulation of lysosomal morphology and autophagy.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:22729905, ECO:0000269|PubMed:31036939}; Multi-pass membrane protein {ECO:0000269|PubMed:22729905}. Note=Colocalized with MTOR in lysosome after amino acid stimulation. {ECO:0000269|PubMed:31036939}.
Interaction partners:
Sequence:
MRPERPRPRGSAPGPMETPPWDPARNDSLPPTLTPAVPPYVKLGLTVVYTVFYALLFVFIYVQLWLVLRYRHKRLSYQSVFLFLCLFWASLRTVLFSFYFKDFVAANSLSPFVFWLLYCFPVCLQFFTLTLMNLYFTQVIFKAKSKYSPELLKYRLPLYLASLFISLVFLLVNLTCAVLVKTGNWERKVIVSVRVAINDTLFVLCAVSLSICLYKISKMSLANIYLESKGSSVCQVTAIGVTVILLYTSRACYNLFILSFSQNKSVHSFDYDWYNVSDQADLKNQLGDAGYVLFGVVLFVWELLPTTLVVYFFRVRNPTKDLTNPGMVPSHGFSPRSYFFDNPRRYDSDDDLAWNIAPQGLQGGFAPDYYDWGQQTNSFLAQAGTLQDSTLDPDKPSLG
Protein: Protein TALPID3 (Q9BVV6)
Organism: Homo sapiens (Human)
Function: Required for ciliogenesis and sonic hedgehog/SHH signaling. Required for the centrosomal recruitment of RAB8A and for the targeting of centriole satellite proteins to centrosomes such as of PCM1. May play a role in early ciliogenesis in the disappearance of centriolar satellites that preceeds ciliary vesicle formation. Involved in regulation of cell intracellular organization. Involved in regulation of cell polarity (By similarity). Required for asymmetrical localization of CEP120 to daughter centrioles (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19144723}. Photoreceptor inner segment {ECO:0000269|PubMed:26386247}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:24421332, ECO:0000269|PubMed:26386247}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26386247}. Note=Forms a ring-like structure at the extreme distal end of both mother and daughter centrioles (PubMed:24421332). In photoreceptor cells localized to the joint between the inner and outer segments, specifically localized at the mother centriole (basal body) and the adjacent centriole as well as between the two centrioles but not in the connecting cilium (PubMed:26386247). {ECO:0000269|PubMed:24421332, ECO:0000269|PubMed:26386247}.
Interaction partners:
- Centrosomal protein of 120 kDa
- Centriolar coiled-coil protein of 110 kDa
- Centrosomal protein of 97 kDa
- Centrosomal protein of 290 kDa
- Sonic hedgehog protein
Sequence:
MPVKRLREVVSQNHGDHLVLLKDELPCVPPALSANKRLPVGTGTSLNGTSRGSSDLTSARNCYQPLLENPMVSESDFSKDVAVQVLPLDKIEENNKQKANDIFISQYTMGQKDALRTVLKQKAQSMPVFKEVKVHLLEDAGIEKDAVTQETRISPSGIDSATTVAAATAAAIATAAPLIKVQSDLEAKVNSVTELLSKLQETDKHLQRVTEQQTSIQRKQEKLHCHDHEKQMNVFMEQHIRHLEKLQQQQIDIQTHFISAALKTSSFQPVSMPSSRAVEKYSVKPEHPNLGSCNPSLYNTFASKQAPLKEVEDTSFDKQKSPLETPAPRRFAPVPVSRDDELSKRENLLEEKENMEVSCHRGNVRLLEQILNNNDSLTRKSESSNTTSLTRSKIGWTPEKTNRFPSCEELETTKVTMQKSDDVLHDLGQKEKETNSMVQPKESLSMLKLPDLPQNSVKLQTTNTTRSVLKDAEKILRGVQNNKKVLEENLEAIIRAKDGAAMYSLINALSTNREMSEKIRIRKTVDEWIKTISAEIQDELSRTDYEQKRFDQKNQRTKKGQNMTKDIRTNTQDKTVNKSVIPRKHSQKQIEEHFRNLPMRGMPASSLQKERKEGLLKATTVIQDEDYMLQVYGKPVYQGHRSTLKKGPYLRFNSPSPKSRPQRPKVIERVKGTKVKSIRTQTDFYATKPKKMDSKMKHSVPVLPHGDQQYLFSPSREMPTFSGTLEGHLIPMAILLGQTQSNSDTMPPAGVIVSKPHPVTVTTSIPPSSRKVETGVKKPNIAIVEMKSEKKDPPQLTVQVLPSVDIDSISNSSADVLSPLSSPKEASLPPVQTWIKTPEIMKVDEEEVKFPGTNFDEIIDVIQEEEKCDEIPDSEPILEFNRSVKADSTKYNGPPFPPVASTFQPTADILDKVIERKETLENSLIQWVEQEIMSRIISGLFPVQQQIAPSISVSVSETSEPLTSDIVEGTSSGALQLFVDAGVPVNSNVIKHFVNEALAETIAVMLGDREAKKQGPVATGVSGDASTNETYLPARVCTPLPTPQPTPPCSPSSPAKECVLVKTPDSSPCDSDHDMAFPVKEICAEKGDDMPAIMLVNTPTVTPTTTPPPAAAVFTPTLSDISIDKLKVSSPELPKPWGDGDLPLEEENPNSPQEELHPRAIVMSVAKDEEPESMDFPAQPPPPEPVPFMPFPAGTKAPSPSQMPGSDSSTLESTLSVTVTETETLDKPISEGEILFSCGQKLAPKILEDIGLYLTNLNDSLSSTLHDAVEMEDDPPSEGQVIRMSHKKFHADAILSFAKQNQESAVSQQAVYHSEDLENSVGELSEGQRPQLTAAAENILMGHSLYMQPPVTNTQSLDQQCDPKPLSRQFDTVSGSIYEDSCASHGPMSLGELELEPNSKLVLPTTLLTAQENDVNLPVAAEDFSQYQLKQNQDVKQVEHKPSQSYLRVRNKSDIAPSQQQVSPGDMDRTQIELNPYLTCVFSGGKAVPLSASQMPPAKMSVMLPSVNLEDCSQSLSLSTMQEDMESSGADTF