wanglab/gogpt-training-data huggingface dataset:
Protein: Hamartin (Tuberous sclerosis 1 protein) (Q92574)
Organism: Homo sapiens (Human)
Function: In complex with TSC2, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling. Seems not to be required for TSC2 GAP activity towards RHEB. Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling (By similarity). Acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1. Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity. Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins. Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:24529379}; Peripheral membrane protein {ECO:0000269|PubMed:9809973}. Cytoplasm, cytosol {ECO:0000269|PubMed:24529379, ECO:0000269|PubMed:9809973}. Note=Recruited to lysosomal membranes in a RHEB-dependent process in absence of nutrients (PubMed:24529379). In response to nutrients, the complex dissociates from lysosomal membranes and relocalizes to the cytosol (PubMed:24529379). {ECO:0000269|PubMed:24529379}.
Interaction partners:
- GTP-binding protein Rheb
- TBC1 domain family member 7
- Tuberin
- Stress-induced-phosphoprotein 1
- RAC-alpha serine/threonine-protein kinase
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Prostaglandin E synthase 3
- Glycogen synthase kinase-3 beta
- Serine/threonine-protein kinase mTOR
- DNA damage-inducible transcript 4 protein
Sequence:
MAQQANVGELLAMLDSPMLGVRDDVTAVFKENLNSDRGPMLVNTLVDYYLETSSQPALHILTTLQEPHDKHLLDRINEYVGKAATRLSILSLLGHVIRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCLKKPGHVAEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENLETFEEVVKPMMEHVRIHPELVTGSKDHELDPRRWKRLETHDVVIECAKISLDPTEASYEDGYSVSHQISARFPHRSADVTTSPYADTQNSYGCATSTPYSTSRLMLLNMPGQLPQTLSSPSTRLITEPPQATLWSPSMVCGMTTPPTSPGNVPPDLSHPYSKVFGTTAGGKGTPLGTPATSPPPAPLCHSDDYVHISLPQATVTPPRKEERMDSARPCLHRQHHLLNDRGSEEPPGSKGSVTLSDLPGFLGDLASEEDSIEKDKEEAAISRELSEITTAEAEPVVPRGGFDSPFYRDSLPGSQRKTHSAASSSQGASVNPEPLHSSLDKLGPDTPKQAFTPIDLPCGSADESPAGDRECQTSLETSIFTPSPCKIPPPTRVGFGSGQPPPYDHLFEVALPKTAHHFVIRKTEELLKKAKGNTEEDGVPSTSPMEVLDRLIQQGADAHSKELNKLPLPSKSVDWTHFGGSPPSDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEKDGLLKKLEEEKAEAAEAAEERLDCCNDGCSDSMVGHNEEASGHNGETKTPRPSSARGSSGSRGGGGSSSSSSELSTPEKPPHQRAGPFSSRWETTMGEASASIPTTVGSLPSSKSFLGMKARELFRNKSESQCDEDGMTSSLSESLKTELGKDLGVEAKIPLNLDGPHPSPPTPDSVGQLHIMDYNETHHEHS
Protein: Curcumin synthase 1 (EC 2.3.1.217) (C0SVZ6)
Organism: Curcuma longa (Turmeric) (Curcuma domestica)
Function: Catalyzes the synthesis of curcumin by condensing feruloyl-CoA with a diketide-CoA in the curcuminoid biosynthesis.
Interaction partners:
Sequence:
MANLHALRREQRAQGPATIMAIGTATPPNLYEQSTFPDFYFRVTNSDDKQELKKKFRRMCEKTMVKKRYLHLTEEILKERPKLCSYKEASFDDRQDIVVEEIPRLAKEAAEKAIKEWGRPKSEITHLVFCSISGIDMPGADYRLATLLGLPLTVNRLMIYSQACHMGAAMLRIAKDLAENNRGARVLVVACEITVLSFRGPNEGDFEALAGQAGFGDGAGAVVVGADPLEGIEKPIYEIAAAMQETVAESQGAVGGHLRAFGWTFYFLNQLPAIIADNLGRSLERALAPLGVREWNDVFWVAHPGNWAIIDAIEAKLQLSPDKLSTARHVFTEYGNMQSATVYFVMDELRKRSAVEGRSTTGDGLQWGVLLGFGPGLSIETVVLRSMPL
Protein: Empty spiracles homeobox 2 (Emx2 protein) (Homeobox protein EMX2) (Q568U8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MFQPTPKRCFTIESLVAKDNPLPSSRSEEPIRPAALSYANSSQMNPFLNGFHSSGRGVYSNPGLVFAEAVSHPPNSAVPVHSVPPPHALAAHPLSSSHSPHPLFASQQRDPSTFYPWLIHRYRYLGHRFQGNETSPESFLLHNALARKPKRIRTAFSPSQLLRLEHAFEKNHYVVGAERKQLAHSLSLTETQVKVWFQNRRTKFKRQKLEEEGSDSQQKKKGTHHINRWRLATKQGSPEEIDVTSDD
Protein: DCAPL1 (Q966V1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPNNRNRNRNRNRNKRNRNQNQNQNPSQNQNENQQQQAEGAEDREEQQDFQTQIAVAQSSSFVDDNGNSGSVSNGPTENSEEVTNTLEKTEKKEEIFEQPATVIQKEADSDAEMGAKNSKHRKEKSDKQASNGKSEEQVRPPPTIIRRPPGSPRQAKVIVHRIVREEDTANGKAQSPEPPKAVESKEQHMEVEDSKKEKPEAQQEIETKEERENEPSPKELPESSHLSEDAQQKHVEVEENQQVYDEVDYSKDETTDNNPQQEQHDSKEPEQYVLQLEKAMEFVENAHQQHVAAVQSYQKQRDTEQNAQQQEQNEAQHLQESTKAHQQNIAVPQILVDPKKREEGLAQQLHHDVKEEPILNNAQQQNDDTAPKSPKEVTIKVQFQTEDPYSQQPPPQKPTSKVIIHQIHVETTDEEQNAKPTFEEVSSTTGSLAGTLSPPPRYLVESPKNVSSGQFSNFSRNVQIQEMELNSDFSSGEFNSLQSPLVCEVDSESEGSVVLGPERSPSDQQVPSSSRVEQHEQVRQKRAQYRNALESHFMPQLLNPRYLDSILEENEWRNSTASSGGSDQTGIRTPKLNETFPRSQLDFSRRHKRREEAPSPLKLETKLLEESTDLESCTRLQSALSPQSEDAELVYLSSSASSSVSDLMELELEQAAALAERALVDLDTDASRLIARPDDEMSSTSTTTADRSETEAETETETEREGEQSRESTPVNANPTLASSQSSLLSAATPTPTPTPTPADREQLAKDTNVSGGSTVSFGAASPLAATREEFVRNMDKVRELIEMTRREQEQGELPRSPSPPPVPPPPASVPPYSPESSSFHLASLQLKRQESNDSHCSDSTTHSQCTAINLASPPPPPTAQPPTPPLRQKPAPPPVPQPVSPPAPPTPQSEPELSVADSVANANADVDADADTDTEAIKKLRLLCTEQLASMPYGEQVLEELASVAQNISDQSQNKMPYPMPQLPHIKELQLNANESKSSSAWLGLPTQSDPKLLVCLSPGQRDLVNNQTQPDDLLDAHQKFVERRGYHELSKAQVLEQDHQQQQSEMLKTAAMMRELRKSLSPPAPPVPPPPVPVKSAETAAKATAHENAKRDDASEQKQKIAACESSSLENKPRRAADLGAQQSAEQRQSSSTTTSSHKATTETMSSDTAKFPTLDSMESELARMFPQHKGDIFEEQRKRFSNIEFPSHQPVSQTKRYSNIETSSYESKKRMENGQVVYDVSTSSHEKKEQGDPPKDQPVPPVPPPPIMSATKLNGNTFIDGDVAPKNSQPSRESGSGSGNGTYEEFRQRAKAAADAFGEQREQQNGLDQDRVFKDFDRLSQQMHAELQSTREKREKSASMYDLSGFTRPASGHPRLDELQQRRHAHMQELEREIERSAKSRQERMSSVPRQMEATPPRTHEIPIELEPRSRRAESLCNLNEPPPRPHTTVGHYNHPVVQDDWSRYANDLGYSENIARPFAREVEICYQRQNQRTPHCIRAPRLSASTNDLSSSSQYSYDTFNAYGGRRTHAPMLNQAQQQQRPHYGSCYSMIERDPNPRYISTTSRRGVSPAPPPVATPQQQQVPPPAYDRQQRRSSLPRELHEQQLKYILSKEEELKFEVERLQQERRRLMEEMQRAPVLPAPQRRESYRPAAKLPTLSEDEVFRQQMAEEWMNKVAEREERRQHKIIRISKIEDEHDHSAVDKATISDEFLDRVKERRHKLSMPADSDWESGAESQPQPAAQSQPESDVEAPPVRILEGQAEANLRQLPRHLREFAKFSTSEQLPDGAQMERHEEQERREEATDNAHSSATKKTSIVKTYKVSRLPPSVQARPSYKSNGYVSEPEPNYDSDYSTVRYRTQNPHRVQSVSSAVNVRNLNQDEKLYGTMPNPIKSAQNSYKNQPGRIENYTTGHSSVSEKEKKEWWDEVMDIFNGNLEQSKLSPLYTEGNLSRALAKESGYTSDSNLVFRKKEVPVSSPLSPVEQKQAYKSLQAGGEPPLLGFRKPAPEKPRDLDPNAPPIPPQPPVKGLSSYDFPYSTDTVDGSDVNIHFKTPIRHEQRQNLSEEELAIRQAEHMQKLYHEERRRKYLQELQDMNSRRHTDNFTPSQKSPIALNRYDDFPTDVTLKSLVGPKTVARALFNFQGQTSKELSFRKGDTIYIRRQIDANWYEGEHNAMIGLLPASYVEIVSRDGARTPSKRPSEGQARAKYNFQAQSGIELSLNKGELVTLTRRVDGNWFEGKIANRKGIFPCSYVEVLTDIGAEDIAARTTTVITSQSTTNLRPNLDVLRTNINNEFNTLTQNGAQPPNGILKETRTLHKTDALHVDTSSEPLAYRALYKYRPQNSDELELLEGDVVHVLEKCDDGWFVGTSQRTGCFGTFPGNYVERA
Protein: Os02g0315600 protein (cDNA clone:002-118-A09, full insert sequence) (cDNA clone:002-120-C10, full insert sequence) (cDNA clone:J033103O07, full insert sequence) (Q6Z861)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MQGDHGYYGGRDSPPQGYGYGGGYGYGGGYGYDAGGYYSGGGGGYPSAGAAAAAYEDPMVGRRTHDFPAPMNELEFQPSATCPKNYVIFDQTCTKSRVMFHPSLAHKFGGGSSAYDNNVYGGGGAHDAAKGAYRDSVGYDDDDSCSVRQKEDTDEIDALLSSEDGDEDDVVSTGRTPGYRDGSSPDSTCSSSYGGGQARPGRKKERMKKMVRTLKGIIPGGNQMDTPAVLDEAVRYLKSLKVEVKKLGVRGSDN
Protein: NAD(P)H-quinone oxidoreductase subunit H, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit H) (NADH-plastoquinone oxidoreductase 49 kDa subunit) (NADH-plastoquinone oxidoreductase subunit H) (P0C335)
Organism: Oryza sativa (Rice)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01358}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01358}; Stromal side {ECO:0000255|HAMAP-Rule:MF_01358}.
Interaction partners:
Sequence:
MSLPLTRKDLMIVNMGPQHPSMHGVLRLIVTLDGEDVIDCEPILGYLHRGMEKIAENRTIIQYLPYVTRWDYLATMFTEAITVNAPEFLENIQIPQRASYIRVIMLELSRIASHLLWLGPFMADLGAQTPFFYIFRERELIYDLFEAATGMRMMHNYFRIGGVAADLPYGWIDKCLDFCDYFLRGVIEYQQLITQNPIFLERVEGVGFISGEEAVNWGLSGPMLRASGIQWDLRKVDLYESYNQFDWKVQWQKEGDSLARYLVRIGEMRESIKIIQQAVEKIPGGPYENLEVRRFKKAKNSEWNDFEYRFLGKKPSPNFELSKQELYARVEAPKGELGIYLVGDDSLFPWRWKIRPPGFINLQILPQLVKKMKLADIMTILGSIDIIMGEVDR
Protein: RNase NYN domain-containing protein (Q23342)
Organism: Caenorhabditis elegans
Interaction partners:
- MUTator
- Zc3h12a-like Ribonuclease NYN domain-containing protein
- PAP-associated domain-containing protein
- Zc3h12a-like Ribonuclease NYN domain-containing protein
- RNA helicase
- MUTator
- RNA-directed RNA polymerase
- Exonuclease mut-7
- Argonaute protein wago-1
- Piwi-like protein ergo-1
Sequence:
MTCGISETDKKEYDALECKNITLEKFCSNRLTERLKCERMRNQYLQACPEGKDQFSSVIKLYSVIPNSVARTIVIDGANVMHCGSGYPDRRENSKSSHIPDVMPLLSLIRFFVVRDFEVFVVISRKYAKQDATNFKSAIDRLIENHLCVVVPSSNLDDSVALQFASQINGVVITTDQYRDHASDSLRFNTIVRENRLGIKWENVKCKNTRAPNIENDYVPSKRVVFVNERESSSRMSENDVKMRLYAVPDHIQYEITKERRVLSEPEKKKSKTMALLNDLLAYGRQNCPGVIEEILKKPVHVPNDHSTQQPQPPEQPIRRVDIADEEHIAVYVGDGDEW
Protein: Coiled-coil and C2 domain containing 1B (H0Y517)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XKINEDEIPPPVALGKRPLAPQEPANRSPETDPPAPPALESDNPSQPETSLPGISAQPVSDLDPDPRALLSSRQREYKVAALSAKRAGELDRARELMRIGKRFGAVLEALEKGQPVDLSAMPPAPEDLKPQQASQAPTAPSVIPPAVERVQPVMAPDVPATPVAPTESQTVLDALQQRLNKYREAGIQARSGGDERKARMHERIAKQYQDAIRAHRAGRKVNFAELPVPPGFPPIPGLESTMGVEEDAVAATLAAAEKLASAEDSAPADKDEDEGEPPAQAPVAKKPARPTVPSSQRLPEPRASSSKESPSPSVREQLALLEARKLQYQRAALQAKRSQDLEQAKAYLRVAKWLEAQIIQARSGRPVDLSKVPSPLTDEEGDFILIHHEDLRLSQKAEEVYAQLQKMLLEQQEKCLLFSKQFMHQGNVAETTRFEKLAQDRKKQLEILQLAQAQGLDPPTHHFELKTFQTVRIFSELNSTEMHLIIVRGMNLPAPPGVTPDDLDAFVRFEFHYPNSDQAQKSKTAVVKNTNSPEFDQLFKLNINRNHRGFKRVIQSKGIKFEIFHKGSFFRSDKLVGTAHLKLERLENECEIREIVEVLDGRKPTGGKLEVKPMASTRRGVRPRLCRR
Protein: LD46156p (Q8MR08)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
LSKRTSLIETAIMPIEVNTPDKLEYQFFPASGGVFTFKVRSPKDAHLALTPAPEENGPIFEIFLGGWENTKSVIRKDRQKPEVAEVPTPGILDAGEFRGFWVRWYDNVITVGREGDAAAFLSYDAGSLFPVNFVGICTGWGASGTWLIDEPAPSAPVMGFAAPTGSGPGCWVPAANGEVPPNALEGGFDSSEQLYIARARHEGDLIPGKLHPSHGVTYVAWGGGEHGHAEYEVLCAGGGQWLPVDAGNIPPNALPAGETAEGEPLFIGRATHDGTITVGKVQPSHGCCYIPYGGEELAYKEFEIYVTN
Protein: RNA polymerase-associated protein C651.09c (Protein RTF1 homolog) (O94667)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. Also has a role in transcription-coupled histone modification. Important for TATA site selection by TBP. Directly or indirectly regulates the DNA-binding properties of the TATA box-binding protein, and the relative activities of different TATA elements (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- RNA polymerase II-associated protein 1 homolog
- Cell division control protein 73
- Tetratricopeptide repeat protein 1
- Uncharacterized protein C13E7.08c
- Transcription elongation factor spt5
- FACT complex subunit pob3
- FACT complex subunit spt16
- Transcription elongation factor spt4
- Transcription elongation factor spt6
- DNA-directed RNA polymerase II subunit rpb1
Sequence:
MADFQDELLALAGIDDSDVASNRKRAHDDLDDVLSSSSDEDNNENVGQDYAEESGGEGNEKSEDEFEEKFKNPYRLEGKFKDEADRAKIMAMTEIERESILFEREEEISKLMERRELAIRLHQQNAQYMAQSTRRSTRDKPLTSAAAGKRDKLTELKKRRQERSARSVSERTRKRSPVSDYEEQNESEKSEEEEGYSPSYAEEKVEQVSKDNASANLYDLNAIRLGRKHVAEYMYHPIFESTVTGCFVRVKIGERDGQGVYRLCQVKGILESRKPYRVDGVLTKVSLECFHGRSKRVFDVNVLSNEPFSDHDFQRWHHQMMEDKLSMPSKNFVQRKLNDLRDMSKYVLSEKEVSDIINRKKELSRVPSNIAAEKTRLRQRRQAAYVAGNAELVKEIDDQLNTLEELSMGSNQNSNSAMDQLAKVNERNRRRNHTEIRLAEQRMNEERRRLSAAATATPMSAPTSVLTGTSPQPSPSLSTSIMSTPKLNPSESVVVASEKASSPDLSPKLLPSESQIFDEGIAVTQTPNTLEDKDFKLHEKAVHGIDDIIATVDFGIDINI
Protein: Diabetes and obesity regulated, isoform A (Diabetes and obesity regulated, isoform B) (Diabetes and obesity regulated, isoform D) (Diabetes and obesity regulated, isoform E) (GH28550p) (Q9VZC7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, autophagosome {ECO:0000256|ARBA:ARBA00004419}. Nucleus, nuclear body {ECO:0000256|ARBA:ARBA00034306}.
Interaction partners:
Sequence:
MLSSLASYLFGSATSDSISQEANPAQNRTNASNANSSSSPGPTSDPAAGDVIEVTSSTPSVAGSSRGAVRASNGKRGKNRRGKQQRTNQQQRKQQPAITKLLTPSGEIVDEDFDEDEWYIVEKEDEEDDSLPRSDSEEELSVVEVSQPRGGSNNASSPMVTVATGTAFNCRRRQGVNSCSLYSGPRPQQQRNYLQRSRVSRPLSISTLSPPRSVPALGAGDHDTLTQSLYVASPSGSDQGQDHGQGANVLMEESCMSVYHSIRSTQEGTDSFVNLDLGVSTEVPQQREEPEPEAEPQDQRQALQEQQRAPNARFDSHAAVQLKQQTLARQSQKSKNKKEHQQLCRSAIKRANKVRDFQAKANRPRRSEMQHCKLVSGANNNRSKCCY
Protein: Fibroblast growth factor 6 (FGF-6) (Heparin secretory-transforming protein 2) (HST-2) (HSTF-2) (Heparin-binding growth factor 6) (HBGF-6) (P21658)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration.
Subcellular location: Secreted, extracellular space.
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
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 3
- Decorin
- Beta-klotho
Sequence:
MALGQRLFITMSRGAGRVQGTLQALVFLGVLVGMVVPSPAGARANGTLLDSRGWGTLLSRSRAGLAGEISGVNWESGYLVGIKRQRRLYCNVGIGFHLQVPPDGRISGTHEENPYSLLEISTVERGVVSLFGVKSALFIAMNSKGRLYTTPSFHDECKFRETLLPNNYNAYESDLYRGTYIALSKYGRVKRGSKVSPIMTVTHFLPRI
Protein: protein O-GlcNAc transferase (EC 2.4.1.255) (Q9Y148)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHVEQTRINMQSQGQSHQLPSAAHILLDQNPNSTGSNLVVKQNDIQSLSSVGLLELAHREYQAVDYESAEKHCMQLWRQDSTNTGVLLLLSSIHFQCRRLDKSAQFSTLAIKQNPVLAEAYSNLGNVFKERGQLQEALDNYRRAVRLKPDFIDGYINLAAALVAARDMESAVQAYITALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETCPGFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALNLSPNNAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPNFPDAYCNLANALKEKGQVKEAEDCYNTALRLCSNHADSLNNLANIKREQGYIEEATRLYLKALEVFPDFAAAHSNLASVLQQQGKLKEALMHYKEAIRIQPTFADAYSNMGNTLKELQDVSGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIQSYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDIRMKKLVSIVTEQLEKNRLPSVHPHHSMLYPLTHDCRKAIAARHANLCLEKVHVLHKKPYNFLKKLPTKGRLRIGYLSSDFGNHPTSHLMQSVPGLHDRSKVEIFCYALSPDDGTTFRHKISRESENFVDLSQIPCNGKAADKIFNDGIHILVNMNGYTKGARNEIFALRPAPIQVMWLGYPGTSGASFMDYIITDSVTSPLELAYQYSEKLSYMPHTYFIGDHKQMFPHLKERIIVCDKQQSSVVDNVTVINATDLSPLVENTDVKEIKEVVNAQKPVEITHKVAELPNTTQIVSMIATGQVQTSLNGVVVQNGLATTQTNNKAATGEEVPQNIVITTRRQYMLPDDAVVYCNFNQLYKIDPQTLESWVEILKNVPKSVLWLLRFPAVGEQNIKKTVSDFGISPDRVIFSNVAAKEEHVRRGQLADICLDTPLCNGHTTSMDVLWTGTPVVTLPGETLASRVAASQLATLGCPELIARTREEYQNIAIRLGTKKKKKK
Protein: Flavin-containing monooxygenase FMO GS-OX-like 1 (EC 1.8.-.-) (Flavin-monooxygenase glucosinolate S-oxygenase-like 1) (Q9FWW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of methylthioalkyl glucosinolates of any chain length into methylsulfinylalkyl glucosinolates.
Interaction partners:
- Pesticidal crystal cry8Ba protein
- Transcription repressor OFP8
- Protein WAVE-DAMPENED 2
Sequence:
MTSVITSRARHVAVIGLGAAGLVAVRELRREGHTVIGFEREKHVGGLWVYTDRVDSDSVSVDPDRTIVHSSIYQSLRTNLPRECMGYSDFPFVTRSSDGDPRRYPDHREVLMYLQDFAKEFKIEDMIRFETEVLCVEPSPENNRKWRVQFKSSNGVSGEEIFDAVVVCNGHFTEPRLAHIPGIESWPGKQIHSHNYRIPDPFKDEVVIVIGSQASGNDISTDIATIAKEVHISSKMVASDSYGCYDNLRIHPTIYRAREDGSVVFRNGKVVFADAIVHCTGYKYHFPFLKTSGYVTVEDNRVGPLYKHVFPPALAPGISFIGLPFMGLQFFMFEIQSKWVASVLSGRVKLPAEDKMMEEAVAFYSKLEDLGIPKRYTHFLTDPRGNPMLGTFKPEDAVVISQSDYFNWIAKQCGCTSIERWRERLYNVAIKKVFFGGDSYRDRWDDDQLIEEVYREFAKLKPNQDCSS
Protein: Forkhead box protein J2 (Fork head homologous X) (Q9P0K8)
Organism: Homo sapiens (Human)
Function: Transcriptional activator. Able to bind to two different type of DNA binding sites. More effective than isoform FOXJ2.S in transcriptional activation. Plays an important role in spermatogenesis, especially in spermatocyte meiosis (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- POU domain, class 3, transcription factor 2
Sequence:
MASDLESSLTSIDWLPQLTLRATIEKLGSASQAGPPGSSRKCSPGSPTDPNATLSKDEAAVHQDGKPRYSYATLITYAINSSPAKKMTLSEIYRWICDNFPYYKNAGIGWKNSIRHNLSLNKCFRKVPRPRDDPGKGSYWTIDTCPDISRKRRHPPDDDLSQDSPEQEASKSPRGGVAGSGEASLPPEGNPQMSLQSPTSIASYSQGTGSVDGGAVAAGASGRESAEGPPPLYNTNHDFKFSYSEINFQDLSWSFRNLYKSMLEKSSSSSQHGFSSLLGDIPPSNNYYMYQQQQPPPPQQQQQQQQPPQPPPQQSQPQQQQAPAQGPSAVGGAPPLHTPSTDGCTPPGGKQAGAEGYGPPPVMAMHPPPLQHGGYHPHQHHPHSHPAQQPPPPQPQAQGQAPINNTGFAFPSDWCSNIDSLKESFKMVNRLNWSSIEQSQFSELMESLRQAEQKNWTLDQHHIANLCDSLNHFLTQTGHVPPQGGTHRPPAPARIADSCALTSGKQESAMSQVNSYGHPQAPHLYPGPSPMYPIPTQDSAGYNRPAHHMVPRPSVPPPGANEEIPDDFDWDLIT
Protein: Frizzled-5 (Fz-5) (hFz5) (FzE5) (Q13467)
Organism: Homo sapiens (Human)
Function: Receptor for Wnt proteins. Can activate WNT2, WNT10B, WNT5A, but not WNT2B or WNT4 (in vitro); the in vivo situation may be different since not all of these are known to be coexpressed (By similarity). In neurons, activation of WNT7A promotes formation of synapses. Functions in the canonical Wnt/beta-catenin signaling pathway. The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (By similarity). A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable). Plays a role in yolk sac angiogenesis and in placental vascularization (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26908622}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8CHL0}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9EQD0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9EQD0}. Synapse {ECO:0000250|UniProtKB:Q8CHL0}. Perikaryon {ECO:0000250|UniProtKB:Q8CHL0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8CHL0}. Cell projection, axon {ECO:0000250|UniProtKB:Q8CHL0}. Note=Localized at the plasma membrane and also found at the Golgi apparatus. {ECO:0000250|UniProtKB:Q9EQD0}.
Interaction partners:
- Protein Wnt-5a
- Protein Wnt-7a
- E3 ubiquitin-protein ligase RNF43
- Protein Wnt-11
- Proto-oncogene Wnt-1
- Low-density lipoprotein receptor-related protein 6
- Protein Wnt-3a
- BMP and activin membrane-bound inhibitor homolog
- Segment polarity protein dishevelled homolog DVL-2
- Tyrosine-protein kinase RYK
Sequence:
MARPDPSAPPSLLLLLLAQLVGRAAAASKAPVCQEITVPMCRGIGYNLTHMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLRFFLCSMYTPICLPDYHKPLPPCRSVCERAKAGCSPLMRQYGFAWPERMSCDRLPVLGRDAEVLCMDYNRSEATTAPPRPFPAKPTLPGPPGAPASGGECPAGGPFVCKCREPFVPILKESHPLYNKVRTGQVPNCAVPCYQPSFSADERTFATFWIGLWSVLCFISTSTTVATFLIDMERFRYPERPIIFLSACYLCVSLGFLVRLVVGHASVACSREHNHIHYETTGPALCTIVFLLVYFFGMASSIWWVILSLTWFLAAGMKWGNEAIAGYAQYFHLAAWLIPSVKSITALALSSVDGDPVAGICYVGNQNLNSLRGFVLGPLVLYLLVGTLFLLAGFVSLFRIRSVIKQGGTKTDKLEKLMIRIGIFTLLYTVPASIVVACYLYEQHYRESWEAALTCACPGHDTGQPRAKPEYWVLMLKYFMCLVVGITSGVWIWSGKTVESWRRFTSRCCCRPRRGHKSGGAMAAGDYPEASAALTGRTGPPGPAATYHKQVSLSHV
Protein: Urea transporter 2 (Solute carrier family 14 member 2) (Urea transporter, kidney) (Q8R4T9)
Organism: Mus musculus (Mouse)
Function: Mediates the transport of urea driven by a concentration gradient across the cell membrane of the renal inner medullary collecting duct which is critical to the urinary concentrating mechanism.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:12217874}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:12217874}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Methylmalonyl-CoA mutase, mitochondrial
- MutS protein homolog 5
- Aquaporin-2
Sequence:
MSDHHPLKEMSDSNSSPLLPEPLSSRYKLYESELSSPTWPSSSQDTHPALPLLEMPEEKDLRSSDEDSHIVKIEKPNERNKRRESEVSRRASAGRGGFSLFQAVSYLTGDMKECKNWLKDKPLVLQFLDWVLRGAAQVMFVNNPISGLIIFIGLLIQNPWWTIAGTLGTVASTLAALALSQDRSAIASGLHGYNGMLVGLLMAVFSEKLDYYWWLLFPVTFTSMACPIISSALSTIFAKWDLPVFTLPFNIALTLYLAATGHYNLFFPTTLIKPASAAPNITWTEIEMPLLLQTIPVGVGQVYGCDNPWTGGVILVALFISSPLICLHAAIGSIVGLLAALTVATPFETIYLGLWSYNCVLSCIAIGGMFYALTWQTHLLALVCALFCAYMGAALSNTMAVVGVPSGTWAFCLSTLTFLLLTSNNTGIYKLPLSKVTYPEANRIYFLTVRRSEEEKSPNGGSGEQSHGSGQWKAEESSETVLPRRRSVFHIEWSSIRRRSKVFGKGEHQERQTKEPLPCPYRKPTVELFDLDTMEESTEIKVEANTARTSWIQSSMVAGGKRVSKALSYITGEMKECGEGLKDKSPVFQFLDWVLRGMSQVMFVNNPLSGILIVLGLFVQNPWWAISGCLGTVMSTLTALILSQDKSAIAAGLHGYNGVLVGLLMAVFSDKGNYYWWLLLPVIVMSMTCPILSSALSTVFSKWDLPVFTLPFNIAVTLYLAATGHHNLFFPTTLLQPATTTPNITWSDIQVSLLLRAIPVGIGQVYGCDNPWTGGIFLVALFISSPLICLHAAIGSTIGMLAALSIATPFDSIYFGLCGFNSTLACIAIGGMFYVITWQTHLLAIACALFAAYLGAALANMLSVFGLPPCTWPFCLSALTFLLLTSNNPAIYKLPLSKVTYPEANRIYFLSQEKNRRASTITKYQAYDVS
Protein: Band 3 anion transport protein (Anion exchange protein 1) (AE 1) (Anion exchanger 1) (Solute carrier family 4 member 1) (CD antigen CD233) (P02730)
Organism: Homo sapiens (Human)
Function: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:26542571, ECO:0000269|PubMed:7506871}; Multi-pass membrane protein {ECO:0000269|PubMed:26542571}. Basolateral cell membrane {ECO:0000269|PubMed:7506871}; Multi-pass membrane protein {ECO:0000269|PubMed:7506871}. Note=Detected in the erythrocyte cell membrane and on the basolateral membrane of alpha-intercalated cells in the collecting duct in the kidney. {ECO:0000269|PubMed:7506871}.
Interaction partners:
- Protein 4.2
- Glycophorin-A
- Ankyrin-1
- Glycophorin-B
- Ammonium transporter Rh type A
- Protein 4.1
- Ankyrin-3
- Carbonic anhydrase 2
- Ankyrin-2
- Alpha-hemoglobin-stabilizing protein
Sequence:
MEELQDDYEDMMEENLEQEEYEDPDIPESQMEEPAAHDTEATATDYHTTSHPGTHKVYVELQELVMDEKNQELRWMEAARWVQLEENLGENGAWGRPHLSHLTFWSLLELRRVFTKGTVLLDLQETSLAGVANQLLDRFIFEDQIRPQDREELLRALLLKHSHAGELEALGGVKPAVLTRSGDPSQPLLPQHSSLETQLFCEQGDGGTEGHSPSGILEKIPPDSEATLVLVGRADFLEQPVLGFVRLQEAAELEAVELPVPIRFLFVLLGPEAPHIDYTQLGRAAATLMSERVFRIDAYMAQSRGELLHSLEGFLDCSLVLPPTDAPSEQALLSLVPVQRELLRRRYQSSPAKPDSSFYKGLDLNGGPDDPLQQTGQLFGGLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPAITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLLVVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILLVVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKLIKIFQDHPLQKTYNYNVLMVPKPQGPLPNTALLSLVLMAGTFFFAMMLRKFKNSSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLSVPDGFKVSNSSARGWVIHPLGLRSEFPIWMMFASALPALLVFILIFLESQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASTPGAAAQIQEVKEQRISGLLVAVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRVLLPLIFRNVELQCLDADDAKATFDEEEGRDEYDEVAMPV
Protein: HVA22-like protein d (AtHVA22d) (Q9S760)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDKFWTFLTALHSGAGPIVMLLYPLYASVIAMESTTKVDDEQWLAYWIIYSFLSLTELILQSLIEWIPIWYTVKLVFVAWLVLPQFQGAAFIYNRVVREQFKKHGVLRSTHSKPTKPNILHSIFPHREGHEAHSH