wanglab/gogpt-training-data huggingface dataset:
Protein: Kinesin-like protein KIF1B (EC 5.6.1.3) (O88658)
Organism: Rattus norvegicus (Rat)
Function: Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:12204119, ECO:0000305|PubMed:15086790}. Note=Has a plus-end-directed microtubule motor activity and therefore associates with microtubules. {ECO:0000305|PubMed:12204119, ECO:0000305|PubMed:15086790}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:12204119}. Note=Associates with synaptic vesicles and mediates their anterograde transport along axonal microtubules. {ECO:0000305|PubMed:12204119}.; SUBCELLULAR LOCATION: [Isoform 2]: Lysosome {ECO:0000305|PubMed:15086790}. Note=Associates with lysosome and mediates their movement along microtubules. {ECO:0000305|PubMed:15086790}.
Interaction partners:
- Disks large homolog 4
- Kinesin light chain
- Disks large homolog 1
- Transmembrane protein 127
- Kinesin heavy chain isoform 5A
- Kinesin light chain 1
- Kinesin light chain 3
- Kinesin-associated protein 3
Sequence:
MSGASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEAPKSFSFDYSYWSHTSPEDPCFASQSRVYNDIGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEESQAGIIPQLCEELFEKINDNCNEDMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKKKKKTDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINEDPNAKLVRELKEEVTRLKDLLRAQGLGDIIDIDPLMDDYSGSGGKYLKDFQNNKHRYLLASENQRPGNFSTASMGSLTSSPSSCSLNSQAGLTSVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNTGEVIVTLEPCERSETYVNGKRVAHPVQLRSGNRIIMGKNHVFRFNHPEQARAEREKTPSAETPSEPVDWTFAQRELLEKQGIDMKQEMEKRLQEMEILYKREKEEADLLLEQQRLDYESKLQALQKQVETRSLAAETTEEEEEEEEVPWTQHEFELAQWAFRKWKSHQFTSLRDLLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPVPPELLPTEMGKTHEDRPFPRTVVAVEVQDLKNGATHYWSLDKLKQRLDLMREMYDRAGEVGSNAQDDSETTMTGSDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTADSDITELADEQQDAMEDFDDEAFVDDTGSDAGTEEGSELFSDGHDPFYDRSPWFILVGRAFVYLSNLLYPVPLIHRVAIVSEKGEVRGFLRVAVQAIAADEEAPDYGSGIRQSGTAKISFDNEYFNQSDFPSAAMTRSGLSLEELRIVEGQGQSSEVISPPEEVNRMNDLDLKSGTLLDGKMVMEGFSEEIGNHLKLGSAFTFRVTVLQASGILPEYADIFCQFNFLHRHDEAFSTEPLKNNGRGSPLGFYHVQNIAVEVTESFVDYIKTKPIVFEVFGHYQQHPLHLQGQELNSPPQPSRRFFPPPMPLSRPVPATKLNTMNKTSLGQSMSKYDLLVWFEISELEPTGEYIPAVVDHTAGLPCQGTFLLHQGIQRRITVTIIHEKGSELHWKDVRELVVGRIRNKPEVDEAAVDAILSLNIISAKSLKSSHSSSRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAVITKDVCMVFYSRDAKISPPRSLRNLFGSGYSKSPDSNRVTGIYELSLCKMADTGSPGMQRRRRKVLDTSVAYVRGEENLAGWRPRGDSLILEHQWELEKLELLHEVEKTRHFLLLRERLGDSIPKSMSDSLSPSLSSGTLSTSTSISSQISTTTFESAITPSESSGYDSADIESLVDREKELATKCLQLLTHTFNREFSQVHGSISDCKLSDISPIGRDPSVSSFSSSTLTPSSTCPSLVDSRSSSMDQKTPEANSRASSPCQEFEQFQIIPTVETPYLARAGKNEFLNLVPDIEEVRAGSVVSKKGYLHFKEPLSSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMLKTPNTFAVCTKHRGVLLQALNDKDMNDWLYAFNPLLAGTIRSKLSRRCPSQPKY
Protein: Centrosomal protein 112 (A0A8I6AM07)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLNFNSFTDRSMEMGSEEEKWEKLDAEFDHFVVDMKPFVLKLPHRSERQRCALWIRKLCEPSGTGAGLMGRKNRNLYAKLLLHMLRRGVLEGPFTHRPEPGTLKVLPSYMSIYFDEPNSAQSKDSSPEKLPDWVMGELEPGERRLSDSWQLSCGEENALLLSASDAHREQYTGKLRMRSHSVSPTDREDRQHITSKICEVHPKKSPISLDDSDIEVRLNSWNLGIENPRYLRQKPLPVSLMTPKVSLRNSSNLHDDHFLSRMHEKELDMKTKMMEAKFSEEKLKLQKKHDAEVQKILERKNNELEELKILYKKKQTETEETVRKLEKKVQILIRDCQVIRETKENQITELKKICEQSTESLNNDWEKKLHSAVAEMEKEKFELQKHHTETIQELLEDTNVRLSKMEGDYMVQTQSTNHMIKDLEGRVQQLMGEAENSNLQRQKLTQEKLELERCYQITCSELQELKTRQNLLHTEKEHLVNDYEQNVKLLKTKYDSDINILRQEHALSTSKTSVVIEELEQNIRQLKQQVQESELQRKQQVKDQEDKFHMEKNHLKYIYEEKVHELKSELDKEKEDAQRKIHKFEEALKEKEEQLGRVTEVQRLQAQQADAALEEFKRQVEVTSEKVYSDMKEQMEKVEADLSRSKSLREKQSKEFLWQLEDARQRYEQQIVELKLEHEQEKTHLLQQHNAEKDSLVRDHEREVENLENQLRAANMEHENQIQESKKRDAQVIADMEAQVHKLREELINVNSHRKQQLVELGLLREEEKQRAARDHETAVKKLKAESERVKMELKKTHAAETEMTLEKANSRLKQIEKEYTQKLAKSSQIIAELQTTISSLKEESSRQQLAAERRLQDVIQKFEDEKQQLIRDNDQAIKALQDELETRSNQVRSAEKKLQHKELEAQEQMMYIRQEYETKFKGLMPASLRQELEDTISSLKSQVNFLQKRASILQEELTTYQSRR
Protein: Calcium/calmodulin-dependent protein kinase II inhibitor 2 (CaM-KII inhibitory protein) (CaM-KIIN) (CaM-KIINbeta) (Q9Z2N6)
Organism: Rattus norvegicus (Rat)
Function: Potent and specific cellular inhibitor of CaM-kinase II (CAMK2). Traps Ca(2+)/calmodulin on CAMK2.
Subcellular location: Nucleus {ECO:0000269|PubMed:9724800}. Cytoplasm, cytosol {ECO:0000269|PubMed:9724800}. Synapse {ECO:0000250|UniProtKB:Q78WH7}. Note=Excluded from nucleus when coexpressed with activated CAMK2. {ECO:0000269|PubMed:9724800}.
Interaction partners:
Sequence:
MSEILPYGEDKMGRFGADPEGSDLSFSCRLQDTNSFFAGNQAKRPPKLGQIGRAKRVVIEDDRIDDVLKGMGEKPPSGV
Protein: Cytochrome b-245 light chain (Cytochrome b(558) alpha chain) (Cytochrome b558 subunit alpha) (Neutrophil cytochrome b 22 kDa polypeptide) (Superoxide-generating NADPH oxidase light chain subunit) (p22 phagocyte B-cytochrome) (p22-phox) (p22phox) (P13498)
Organism: Homo sapiens (Human)
Function: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15585859, ECO:0000269|PubMed:17140397, ECO:0000269|PubMed:22808130}; Multi-pass membrane protein {ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210}.
Interaction partners:
- NADPH oxidase organizer 1
- NADPH oxidase 2
- Ras-related C3 botulinum toxin substrate 2
- Neutrophil cytosol factor 1
- NADPH oxidase 4
- NADPH oxidase 1
- NADPH oxidase activator 1
- Neutrophil cytosol factor 2
- Neutrophil cytosol factor 4
- NADPH oxidase 3
Sequence:
MGQIEWAMWANEQALASGLILITGGIVATAGRFTQWYFGAYSIVAGVFVCLLEYPRGKRKKGSTMERWGQKYMTAVVKLFGPFTRNYYVRAVLHLLLSVPAGFLLATILGTACLAIASGIYLLAAVRGEQWTPIEPKPRERPQIGGTIKQPPSNPPPRPPAEARKKPSEEEAAVAAGGPPGGPQVNPIPVTDEVV
Protein: Matrix metallopeptidase 28 (epilysin) (Matrix metalloproteinase-28) (Mmp28 protein) (Q8CGV8)
Organism: Mus musculus (Mouse)
Interaction partners:
- Lens fiber membrane intrinsic protein
Sequence:
MVAGVSLLLRALPLLLWGCQDAQPTQHGLPELRQEAEAFLEKYGYLSEQGSKAPASAQFRNAIREFQWISQLPLSGVLDQATLRQMTRPRCGVADTDSHATWTERISTLLAGHRAKMRRKKRFAKPGNKWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLANAFDGPGGALAHAFLPRRGEAHFDGDERWSLSRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKKLGRDALLSWDDVLAVQSLYGKPLGRSVATQLPGKVFTDFEAWDPHNSQSRRPETRGPKYCHSSFDAITVDGQWRLYVFKGSYFWEVTVDGNVSEPRPLQKRWPGLPPGIEAAAVSLEDGDFYFFKGNRCWRFQGTKSVWGFAQLCRAGGLPRHPDAALFFPPLRRLVLFKGSRYYVLAQGGMQVEPYYPRSLRDWAGVPEEVSGALPRPDGSIIFFRDDHYWHLDQAKLRVTSSGRWATELSWMGCWNANSGGALF
Protein: Dr1-associated corepressor (Dr1-associated protein 1) (Negative cofactor 2-alpha) (NC2-alpha) (Q9D6N5)
Organism: Mus musculus (Mouse)
Function: The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein Dr1
- Forkhead box protein H1
- B-TFIID TATA-box binding protein associated factor 1
- TATA-box-binding protein
- TATA box-binding protein-like 2
- TATA box-binding protein-like 1
- Cilia- and flagella-associated protein HOATZ
Sequence:
MPSKKKKYNARFPPARIKKIMQTDEEIGKVAAAVPVIISRALELFLESLLKKACQVTQSRNAKTMTTSHLKQCIELEQQFDFLKDLVASVPDMQGDGEDNHVDGDKGPRRGRKPGSSGRKNGGTGSKGKDKKLSGTDSEQEDESEDTDTDGEEETPQLPPQASHPPAHFQSPPTPFIPFTSPLPLPPAPPGPSAADAEDEEDYDS
Protein: Kon-tiki (A3RLX3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSRLRGLGFGWLWLAWLAILQLQTVAAMKVSLFGDGYVSMPLQEAKMSTNIRVKFRTRQENAFLFLAAGRTDYCLLRLESGLISFSYKIERDVVQLRSPKKQKLNDLEWHDVAVQRFENNITLQVDGYIMRKQLPGDLAALNIHFGTFLGGVGDFTAEFLDDVIGFRGCISDVFYNNINIIKRAKDRTSHTTSTGVAWTCSTEFEGSIQDSISFMRNDSYSLMMKESYAMGETLSLQFRTMASAGVIFFNGGFDFILLEIEDQHLKVTFNKAGSLVQFMTNEHISDGKWHRVFLRYNAAIAELILDDATSGYRGTHANETKASINLEKSVFFGGVQEEMRRRLISKGLRINEISFKGCMRDILVNDLPLGFAEMTISRSLALNCLWKYPCVEYNPCLKSGICSQHGVDGFICYCDQSYCIKADFQGPFKIFTETSPELELLYVSPMQLLEGGTAFLSPHFIDIILDLRRYPSLNEQSIIFHVVHQPKYGQLLQYSAEKAIFVPCRTFNLVDLATDKLKYVHNGQENFNDHATLDMQIFGDVHKIPDNILGKHRFLLHANITPINDPPQLRLHSHKILRVIEGIERVLDVDLFNIDDPDSEPGNLIYTILPTQSPQETFGCFIVGGATTSAFSQAEVNVGKVSYLYNSTTAESFSYELQLQVSDGIETSETVYLPVSVHPLELRLVNNTGLIMIHKSSLPISTANLSIGTNAVDDHIDIRYDIVKAPQHGVLQRLRQIDGSWVNVDWFSDSQLLLGHIRYLHSSDFPWQDEFKFIASFGFVTTQTFDFRITFTRLRITSTRPSQISINGSREILLTSDVLSYETTPIGSFARSVIYKITKPTRYGGIYVEGSRKAAKKLDSFTQQDIEKRRIRYQTHHTSYSSFSDHLEFVVSVAECDDVAGVLEINYRPPDELINKLGYQNHEPLQVQEGERALITKNHFGIRFNIYESLQFQVSLSPEHGVICKYDEQTGLTTPVEMFTLEQLFRNDIYYCHDDTESTRDTFELLILSGDETDLQFVSNMEVHIKLVNDNEPYRTAIERVFHVVRNGIRTLNPTVLQYLDADVNTNHTDIHYIHVSSTNGAFYKSGHYIDSFTQDDIANRRIMFQHTGADSGTASFIVTDREHEVNGLLEIRASDPFVSMMATNASIVQEGKFVVLKNKDFILETNLDMKLDEIYYEVIKPPSYGILMYLSRANEGENGTTIYKATNYTSLSNFTHLDIERERLVYWNTEIASMDKVRYRVHIKNITAEGEVMFRIYPSAYWEPLQVKQNHTLYVEESTSVLISRDVLEVVHPNISPGDITFLVTSSPMHGYLEMQSMSFDDEYNCKVFDQSSVNTEKMFYIQAGVNQSTDYFVFDVTNGITWLRQLMIKIVIIPEKLYMHSNIISVVEGKTVQLNPTDIQPYSEYYRGKILEYIVTITPSSGHVLAGNSKVKRFTQKQLEQGSIQYVHNGSENATDSITLVAMARNKESVPFELEFAVVQVNDEEPMMVTNTGLQVWNGGRYVIKNTDLLAQDYDTPPENLTFVVNHIYGGYLARKSAPHQKIEHFTQAQINLEEIYFMHDSNSRRNELSFVVTDGLFNTTTQMLNIEIKPIEILAEHNENLHVFPLTKKQILRDYLHFKCSDEEREIRYNITVPPSLGRIVNEFIDNGFTKEVSEFTQNDVDNGHIFYEHTAVIMEFRTNDSFYFDVVAERSDRLLNQKFNIEISVSSGGLLRFLPVNKLNVDEGGSVPIKLDFSKILEYLKTKAGINNPELFIEAIQKPTHGNIGLGHEFKHMQRYHPSDFFTKKVYYIHDHSDTLEDTILMSVYLTQGNIFLCNLTIPVSINPINDQPFHLVTHLPQMTVVEGENRTITRNDLLTEDADTPPEEIIYDVMSGPTLGVLRKITNDGRPEDLLAFSNQFTQADINNDRIIYVHFGMPQSTTFCFTVSDGQSNPAYEIFTIKIDSIHLQPSAMQAPVKVQQGATTAPMRLDHIGVSTNVHMERLSYNVTNSPLFGIIVYKHQPTLRFTQQQLETSQISYMQTDLNRSNDSFQVSAYVPGTNYVAQVDVVMEVEPVIQINDIVMKEAESSGGKIKLITSLDNDNPLSLKLNKFNPKFVITRMPSTGQIRKIIRSTGLTTDGQSDRSTNIFSYKELRSGVVYFVPHESVEETEADHDSFDYQLLIKTVQPAQATVSIEYRSRVEETETVHLGSAGLSINYLAIGCAIFIVLICLLIVLLILKIRKLRKHKADISKDQPPALPCPPDLTSVSPQHHLHHHHGHHYASSEADSVPATGNSTPLPGFSNIPHCKIIPVESYKHEYPDYDPDEEETDDQCDPQQMMLPQRYNPYHMEHDAWSSSCDMANDFAGYASVPQSISGSVSSPPSAPPTNPLLRRNQYWV
Protein: Long chain acyl-CoA synthetase 7, peroxisomal (AtLACS7) (EC 6.2.1.3) (Q8LKS5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation (Probable). Preferentially uses palmitate, palmitoleate, oleate, linoleate and eicosenoate as substrates. Can use myristate and linolenate as substrates. Functions redundantly with LACS6 in lipid mobilization for beta-oxidation during seed germination, which is essential for postgerminative growth and seedling establishment.
Subcellular location: Peroxisome {ECO:0000269|PubMed:12366803}.
Interaction partners:
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 2, chloroplastic
- Peroxisomal acyl-coenzyme A oxidase 1
- Acyl-coenzyme A oxidase 2, peroxisomal
- ABC transporter D family member 1
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- Acyl-coenzyme A oxidase 4, peroxisomal
- Probable acyl-CoA dehydrogenase IBR3
- Acyl-coenzyme A oxidase 3, peroxisomal
Sequence:
MEFASPEQRRLETIRSHIDTSPTNDQSSSLFLNATASSASPFFKEDSYSVVLPEKLDTGKWNVYRSKRSPTKLVSRFPDHPEIGTLHDNFVHAVETYAENKYLGTRVRSDGTIGEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGADEHLPSLPRGTGVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIMGVYGGVAVGFYQGDVFKLMDDFAVLRPTIFCSVPRLYNRIYDGITSAVKSSGVVKKRLFEIAYNSKKQAIINGRTPSAFWDKLVFNKIKEKLGGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYTSDDQPYPRGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDSFNSSLVAIVSVDPEVMKDWAASEGIKYEHLGQLCNDPRVRKTVLAEMDDLGREAQLRGFEFAKAVTLVPEPFTLENGLLTPTFKIKRPQAKAYFAEAISKMYAEIAASNPIPSKL
Protein: SrfA-induced gene J protein (Q6TMJ3)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGRVEDQIKDNYNSLSHEGERLNREAKIESEKLKNNAKLDAKDMKKDIDESVHSSWETVKEGAKTVQDYISSGIESVKHTITTEPAQKDMENLKHNVNHNLEEAEKEGSSVLNNISNFFKGSAEEAKSEAERIGYEAYKDGDQFVGDVHKNFKRTANETQKDANRLTSDVKNESNKIYKDIKDESNKLYNDVKGESSKIYNGAKKEGSKLATDLKKDTQYVADETKKMAADLKNKAADTYQDLSHDASKKATQLKKKASETLDESADAIEHQFDIMKKDFRHLNQRNGMIWGSIGLIGGATATSYLFPSASPMAKFTFIAGLASLGGYYGLHQPHNKIVDNAFHKANNKKEELKKKI
Protein: Probable pyridoxal 5'-phosphate synthase subunit SNZ3 (PLP synthase subunit SNZ3) (EC 4.3.3.6) (PDX1 homolog 3) (Pdx1.3) (P43545)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Interaction partners:
- Probable pyridoxal 5'-phosphate synthase subunit SNO3
- Probable pyridoxal 5'-phosphate synthase subunit SNO2
- Pyridoxal 5'-phosphate synthase subunit SNO1
- Probable pyridoxal 5'-phosphate synthase subunit SNZ2
- Pyridoxal 5'-phosphate synthase subunit SNZ1
- Pyridoxamine 5'-phosphate oxidase
- Putative pyridoxal kinase BUD16
- Putative pyridoxal kinase BUD17
- Uncharacterized protein YGR017W
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI5
Sequence:
MSEFKVKTGLAQMLKGGVIMDVVTPEQAIIAERAGACAVMALERIPADMRKSGQVCRMSDPRMIKEIMEAVSIPVMAKVRIGHFVEAQILEELQVDYIDESEVLTPADWTHHIEKHNFKVPFVCGAKDLGEALRRINEGAAMIRTKGEAGTGDVSEAVKHITKIKAEIQQYKENLKTESDFAAKATELRVPVDLLKTTLSEGKLPVVNFAAGGVATPADAALLMQLGCEGVFVGSGIFKSSDPEKLACAIVEATTHYDNPAKLLQVSSDLGDLMGGISIQSINEAGGKNGARLSEIGW
Protein: Tetraketide alpha-pyrone reductase 1 (EC 1.1.1.-) (Protein DIHYDROFLAVONOL 4-REDUCTASE-LIKE 1) (Q500U8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of hydroxylated tetraketide compounds that serve as sporopollenin precursors (the main constituents of exine). Is essential for pollen wall development. Acts on tetraketide alpha-pyrones and reduces the carbonyl function on the tetraketide alkyl chain to a secondary alcohol function.
Subcellular location: Cytoplasm. Nucleus. Endoplasmic reticulum {ECO:0000269|PubMed:23632852}. Note=According to PubMed:21193572, TKPR1 is associated with the endoplasmic reticulum.
Interaction partners:
- Type III polyketide synthase A
- Type III polyketide synthase B
- Cytochrome P450 704B1
- 4-coumarate--CoA ligase-like 1
- Cytochrome P450 703A2
- Putative acyl-activating enzyme 19
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- ABC transporter G family member 26
- Transcription factor MYB80
- Transcription factor DYT1
Sequence:
MDQAKGKVCVTGASGFLASWLVKRLLLEGYEVIGTVRDPGNEKKLAHLWKLEGAKERLRLVKADLMEEGSFDNAIMGCQGVFHTASPVLKPTSNPEEEILRPAIEGTLNVLRSCRKNPSLKRVVLTSSSSTVRIRDDFDPKIPLDESIWTSVELCKRFQVWYALSKTLAEQAAWKFSEENGIDLVTVLPSFLVGPSLPPDLCSTASDVLGLLKGETEKFQWHGQMGYVHIDDVARTHIVVFEHEAAQGRYICSSNVISLEELVSFLSARYPSLPIPKRFEKLNRLHYDFDTSKIQSLGLKFKSLEEMFDDCIASLVEQGYLSTVLP
Protein: RE74901p (Q8MS11)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSNYYSLLLQADTYDDESIGDERSEEDTDDASETEFRSPSRYGAMNGTSNSNNMGTNSELKEQMYQHKLFNLQKQMEELGQLVHPEYLKRVKKLDSQLKERRRMNEVYKEYMRECVERDYVLEKMAAQKEYDEKMMDLKDNLISDFEDRKRQIENERFSIELTNDSMEIKTTITRKLRRRPNEPLPVIEKRRKPATGQLLVYQLDDKEIESDLKIIQRGRPNPVPQQNGSGSYGSGSQQQQSVHVLAEPTSNSGLVETRIEDNKLLYERRWFCRGQQVYVEGKEMSKFAATITAIGNEVVWVKRTNETKVKINMSHLAKGKISIKRR
Protein: Innexin (Q8I6U1)
Organism: Hirudo medicinalis (Medicinal leech)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}.
Interaction partners:
Sequence:
MDKILGVLGGVPNTKPRNDDDFADRLVYKTTVGMFILFAIVISTKQYVGDPIQCWVPAEFTGNQEEYTNNYCWIKNTYYLPYEKNIPKEHEAEKRKIIPYYQWAPLILGVQALICYLPIILWRYLNKKSGIDVNAIVEAGEKFTNAEAAENRDKTLNFMTKLMDRYLANQRDVPTGCTLSLKHVFSRTCFKWCGRKRGNYLTTLYLFSKFLLLVSVLGQLFALNFFLGQDFHMYGFDAIRNMFMGEDQAASDRFPRVTMCDFKVRRLGNVQRYTVQCVLPINLFNEKIYLFIWFWLAFTASVMTFSIVNWMFRFFYSNDRRRYVKKHLSLMDKIGKDPSEKKALAKFVEDYLKQDGIFVLRMVGHNTNAITATEFVCQLWDNYRTKPFVERVEDVESV
Protein: CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5) (Phosphatidylglycerophosphate synthase) (PGP synthase) (P25578)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for the viability of mitochondrial petite mutant. Catalyzes the committed step to the synthesis of the acidic phospholipids.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9545322, ECO:0000269|PubMed:9799363}.
Interaction partners:
- Cardiolipin synthase
- Phosphatidate cytidylyltransferase
- Phosphatidylglycerophosphatase GEP4, mitochondrial
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Phosphatidate cytidylyltransferase, mitochondrial
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Phosphatidylserine decarboxylase proenzyme 2
- Protein UPS1, mitochondrial
- Cardiolipin-specific deacylase 1, mitochondrial
Sequence:
MTTRLLQLTRPHYRLLSLPLQKPFNIKRQMSAANPSPFGNYLNTITKSLQQNLQTCFHFQAKEIDIIESPSQFYDLLKTKILNSQNRIFIASLYLGKSETELVDCISQALTKNPKLKVSFLLDGLRGTRELPSACSATLLSSLVAKYGSERVDCRLYKTPAYHGWKKVLVPKRFNEGLGLQHMKIYGFDNEVILSGANLSNDYFTNRQDRYYLFKSRNFSNYYFKLHQLISSFSYQIIKPMVDGSINIIWPDSNPTVEPTKNKRLFLREASQLLDGFLKSSKQSLPITAVGQFSTLVYPISQFTPLFPKYNDKSTEKRTILSLLSTITSNAISWTFTAGYFNILPDIKAKLLATPVAEANVITASPFANGFYQSKGVSSNLPGAYLYLSKKFLQDVCRYRQDHAITLREWQRGVVNKPNGWSYHAKGIWLSARDKNDANNWKPFITVIGSSNYTRRAYSLDLESNALIITRDEELRKKMKAELDNLLQYTKPVTLEDFQSDPERHVGTGVKIATSILGKKL
Protein: Protein lifeguard 1 (Glutamate [NMDA] receptor-associated protein 1) (NMDA receptor glutamate-binding subunit) (Q9ESF4)
Organism: Mus musculus (Mouse)
Function: Potential apoptotic regulator.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Bax inhibitor 1
Sequence:
MSHEKSFLVSGDSYPPQNIVGPQAPMPPYVQAPYPGAPYPQAPFQPSPYGQPGYPHGPSPYPQGGYPQGPYPQGGYPQGPYPQSPFPPNPYGQPPPFQDPGSPQHGNYQEEGPPSYYDNQDFPAVNWDKNIRQAFIRKVFLVLTLQLSVTLSTVAIFTFVGEVKGFVRENVWTYYVSYAIFFISLIVLSCCGDFRRKHPWNLVALSILTVSLSYMVGMIASFYNTEAVIMAVGITTAVCFTVVIFSMQTRYDFTSCMGVLLVSVVVLFIFAILCIFIRNRILEIVYASLGALLFTCFLAVDTQLLLGNKQLSLSPEEYVFAALNLYTDIINIFLYILTIIGRAKE
Protein: Gasdermin D (E9PIB2)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MELQAQRRPWRTQLGSMGSAFERVVRRVVQELDHGGEFIPVTSLQSSTGFQPYCLVVRKPSSSWFWKPRYKCVNLSIKDILEPDAAEPDVQRGRSFHFYDAMDGQIQGSVELAAPGQAKIAGGAAVSDSSSTSMNVYSLSVDPNTWQTLLHERHLRQPEHKVLQQLRSRGDNVYVVTEVLQTQKEVEVTRTHKREGSGRFSLPGATCLQGEGQGHLSQKKTVTIPSGSTLAFRVAQLVIDSDLDVLLFPDKKQRTFQPPATGHKRSTSEGAWPQLPS
Protein: Vacuolar protein sorting-associated protein 33A (Protein slp-1) (P34260)
Organism: Caenorhabditis elegans
Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport pathways. Believed to act as a component of the putative HOPS endosomal tethering complex which is proposed to be involved in the rab-5-to-rab-7 endosome conversion probably implicating sand-1, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to rab-7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes (By similarity). Within the HOPS complex, contributes to the normal development of gut granules in embryonic and adult intestinal cells. Required for endosome/lysosome fusion. Required for early embryonic development.
Subcellular location: Lysosome {ECO:0000269|PubMed:25273556}. Early endosome {ECO:0000269|PubMed:27558849}. Late endosome {ECO:0000269|PubMed:25273556, ECO:0000269|PubMed:27558849}. Apical cell membrane {ECO:0000269|PubMed:25273556}; Peripheral membrane protein {ECO:0000269|PubMed:25273556}. Note=Localizes to lysosome-related gut granules. {ECO:0000269|PubMed:25273556}.
Interaction partners:
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 39 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Vps8 domain-containing protein
- Spermatogenesis-defective protein 39
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar fusion protein CCZ1 homolog
- Ras-related protein Rab-7a
- t-SNARE coiled-coil homology domain-containing protein
Sequence:
MAANEDRDDAAAILNWEGTSEIKSANEYSRNLLFSVLDSLDGNKTIVWDRDRSVMHRVNLFAGASVLAAHGVVANHSIETKKSASTPHVVFFLAPTMVSLDLLCDYIDNVRNDSKILYQVFFIPEAWFVVRESLKTRAEGKYWERLESVKEIPLCWLPRDGECLSLSSPQIAARLLINGDWTHLHKCAVALNQLIDMCRGRSSSSNQRPMSIYAKGKWASDVAKMMGKIRNSAEADSMTKNLDPIEGLLKINRIVLIDRWMDPLTPMLSQLTFYGLLDEIYGIGMVNSVKVPEMEFKNEKDGDPFQEKEVYLIDEVYHRLKHSHINAVSIEASKVLAEIRDDEQFDRDKMSVAEYSVLVKKMPKIINRKKMIEVHMRLAEMIQSHVYCKQSDSIKLERDLLEYSDSDKAIPLIEDLIFDASPLNAVLRLISVHSLTCGGLKPSVLQHYRRIVNQSYGSSALNKVLKMQKMGLIREKGGGGKMQCEYAQMMFQQMKKNHDMLPEEFSEAKLDDMAYAYSGFSPLLCKMLEEGDRVKWVGWPKTVIGDKSDLIAERDGRGTCVFVIGGLTRSELAIIRENLPNVALITTSALITGDKLLNNITNI
Protein: Rap1 GTPase-activating protein (F1LV89)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Ras-related protein Rap-1b
- Ras-related protein Rap-1A
- Ras GTPase-activating protein 1
Sequence:
MSGRKRSFTFGAYGGVDKSFSPRQSVWRSDGQKHSFPQTLNVLLVDSVPSHPASPYPKNTDLFEMIEKMQGSRMDEQRCSFPPPLKTEEDYIPYPSVHEVLGREGPFPLILLPQFGGYWIEGTNHEISSIPETEPLQSPTTKVKLECNPTARIYRKHFLGKEHFNYYSLDTALGHLVFSLKYDVIGDQEHLRLLLRTKCRTYHDVIPISCLTEFPNVVQMAKLVCEDVNVDRFYPVLYPKASRLIVTFDEHVISNNFKFGVIYQKLGQTSEEELFSTNEESPAFVEFLEFLGQKVKLQDFKGFRGGLDVTHGQTGTESVYCNFRNKEIMFHVSTKLPYTEGDAQQLQRKRHIGNDIVAVVFQDENTPFVPDMIASNFLHAYVVVQAEGGGPDGPLYKVSVTARDDVPFFGPPLPDPAVFRKGPEFQEFLLTKLINAEYACYKAEKFAKLEERTRAALLETLYEELHIHSQSMMGLGGDDDKMENGSGGGGFFESFKRVIRSRSQSMDAMGLSNKKPNTVSTSHSGSFTPNNPDLAKAAGISLLIPGKSASRFGRRGSALGIGAVEESLIVPGKSPTRKKSGPFGSRRSSAIGIENIQEVQEKRESPPAGQKTPDSGHVSQEPKSENSSTQSSPEMPTTKNRVESAAQRTEVLQGFSRSSSSASSFTSVVEETEGVDGDDTGMESVSSSGTPHKRDSFLYSTWLDDSVSTTSGGSSPGLTRSPHPDAVKSGDPACPEIKIQLETSEQHTPQMGC
Protein: NOTUM, palmitoleoyl-protein carboxylesterase (D3ZXI3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt-5a
- Protein Wnt
- Protein Wnt-4
Sequence:
MGGEVRVLLLLGLLHWVGGSEGRKTWRRRGQQPPQPPPPPPPPQRAEVAPGAGQPVESFPLDFTAVEGNMDSFMAQVKSLAQSLYPCSAQQLNEDLRLHLLLNTSVTCNDGSPAGYYLKESKGSRRWLLFLEGGWYCFNRENCDSRYSTMRRLMSSKDWPHTRTGTGILSSQPEENPHWWNANMVFIPYCSSDVWSGASPKSEKNEYAFMGSLIIQEVVRELLVKGLSGAKVLLLAGSSAGGTGVLLNVDRVAELLEELGYPSIQVRGLADSGWFLDNKQYRRSDCIDTINCAPTEAIRRGIRYWSGMVPERCQRQFKEGEEWNCFFGYKIYPTLRCPVFVVQWLFDEAQLTVDNVHLTGQPVQEGQWLYIQNLGRELRGTLKDVQASFAPACLSHEIIIRSYWTDVQVKGTSLPRALHCWDRSFHDSHKASKTPMKGCPFHLVDSCPWPHCNPSCPTIRDQFTGQEMNVAQFLMHMGFDVQTVAQQQGMEPSKLLGILSSGN
Protein: Indole-3-glycerol phosphate synthase, chloroplastic (IGPS) (EC 4.1.1.48) (P49572)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Indole-3-glycerol phosphate synthase required for tryptophan biosynthesis.
Subcellular location: Plastid, chloroplast {ECO:0000305|PubMed:7610197}.
Interaction partners:
- Tryptophan synthase alpha chain, chloroplastic
- N-
- N-
- Tryptophan synthase beta chain 1, chloroplastic
- Tryptophan synthase
- Tryptophan synthase alpha chain
- Tryptophan synthase beta chain 2, chloroplastic
- N-
- Anthranilate phosphoribosyltransferase, chloroplastic
- Anthranilate synthase alpha subunit 1, chloroplastic
Sequence:
MEGLVPVQRLPIKVASPSLYRCNNSVSIRRSISGFAMDRKINFRAPSQFSIRAQQSDLKESLAVSSSSVEDKGNVLRIKEWEVEMYQEELAISQGIRIRRKPPSKAPLGYSGPFELRLHNNDADSPRNILEEITWYKDVEVSRMKELNPLDVLKKAVEDAPPTRDFVGALRMAHKRTGFPGLIAEVKKASPSRGILKENFDPVEIAQAYEKGGAACLSVLTDQKYFQGGFENLEAIRSAGVKCPLLCKEFVVDPWQIYYARTKGADAVLLIAAVLADLEITFLLKICKKLSLAALVEVHDEREMGRVLGIEGIELVGINNRSLETFEVDISNTKKLLEGEHGRQIRERDMIVVGESGLFTPDDIAYVQAAGVKAVLVGESIVKQNDPEKGIAGLFGRNISHT