wanglab/gogpt-training-data huggingface dataset:
Protein: V-type proton ATPase subunit c1 (V-ATPase subunit c1) (V-type proton ATPase 16 kDa proteolipid subunit c1) (V-ATPase 16 kDa proteolipid subunit c1) (Vacuolar H(+)-ATPase subunit c isoform 1) (Vacuolar proton pump 16 kDa proteolipid subunit c1) (Vacuolar proton pump subunit c1) (P0DH92)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subcellular location: Vacuole membrane; Multi-pass membrane protein. Note=Tonoplast.
Interaction partners:
- V-type proton ATPase subunit C
- V-type proton ATPase subunit e1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- ATP synthase subunit b, chloroplastic
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B1
- V-type proton ATPase subunit B2
- V-type proton ATPase subunit d2
Sequence:
MSTFSGDETAPFFGFLGAAAALVFSCMGAAYGTAKSGVGVASMGVMRPELVMKSIVPVVMAGVLGIYGLIIAVIISTGINPKAKSYYLFDGYAHLSSGLACGLAGLSAGMAIGIVGDAGVRANAQQPKLFVGMILILIFAEALALYGLIVGIILSSRAGQSRAE
Protein: Norrin (Norrie disease protein) (X-linked exudative vitreoretinopathy 2 protein) (Q00604)
Organism: Homo sapiens (Human)
Function: Activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. Plays a central role in retinal vascularization by acting as a ligand for FZD4 that signals via stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. Acts in concert with TSPAN12 to activate FZD4 independently of the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1). May be involved in a pathway that regulates neural cell differentiation and proliferation. Possible role in neuroectodermal cell-cell interaction.
Subcellular location: Secreted {ECO:0000269|PubMed:9407136}.
Interaction partners:
- Frizzled-4
- Low-density lipoprotein receptor-related protein 5
- Tetraspanin-12
- Leucine-rich repeat-containing G-protein coupled receptor 4
- Low-density lipoprotein receptor-related protein 6
- Ubiquitin-like protein FUBI
- Adhesion G protein-coupled receptor A2
- Frizzled-1
- Catenin beta-1
- Zinc finger protein 408
Sequence:
MRKHVLAASFSMLSLLVIMGDTDSKTDSSFIMDSDPRRCMRHHYVDSISHPLYKCSSKMVLLARCEGHCSQASRSEPLVSFSTVLKQPFRSSCHCCRPQTSKLKALRLRCSGGMRLTATYRYILSCHCEECNS
Protein: Tankyrase 2 (D3ZRP5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Axin-2
- E3 ubiquitin-protein ligase RNF146
- Telomeric repeat-binding factor
- SH3 domain-binding protein 2
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Hypoxia-inducible factor 1-alpha inhibitor
- Poly
- Glycogen synthase kinase-3 beta
- Catenin beta-1
Sequence:
MSGRRCAGGGAACSSAVAEAVEPSARELFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSAKAVLTGDYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLAPTAQLKERLSYEFKGHSLLQAAREADVTRIKKHLSLEMVNFKHPQTHETALHCAAASPYPKRKQICELLLRKGANTNEKTKEFLTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCRLLLSYGCDPNIISLQGLTALQMGNENVQQLLQEGVSLGHSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGDAALLDAAKKGCLARVKKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGADDVSALLTAAMPPSALPTCYKPQVLSGVRSPGATADALSSGPSSPSSLSAASSLDNLAGSFSELSAVVSSSTTEGATGLERKEDSGIDFSITQFIRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGISAYGHRHRLIKGVERLISGQQGLNPYLTLNNSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYSILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIVRPEGMGDG
Protein: Forkhead-associated (FHA) domain-containing protein (F4HZ48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- RuvB-like protein 1
- Protein EIN6 ENHANCER
- Alpha/beta-Hydrolases superfamily protein
- Actin-related protein 9
- Actin-related protein 5
- Actin-related protein 4
- DNA-binding protein-like
- Ubiquitin carboxyl-terminal hydrolase 2
- Ubiquitin carboxyl-terminal hydrolase
- Chromatin modification-related protein EAF1 B
Sequence:
MAFQWLPEDDYLLRKSLEDGTSLETLAKGAVRFSRKFTLSELTERWHCLLYNPKVTSLSSSVGFELQYGAQFVPQSLFDSVPVRTHYYTTRKRRRLELEESLKVNNNAIDEHLNVEEGNLFGECDDDFGFKFEDIESFRNTFPDILLSPHDYQTTIFGNEIDDEDDRMVNQMLNINDDQIHDSYVTDTITTTTEHVLLQEVFQDPLFQQPNASLNEPASPSQQQVILDQAEIWIPPPPYDPHPEIVNGVINCVINRESDEIPDNDDINLQLYNPKARNSVNPSSVRNNMKPPLPPVRRSSLQVKSKDIIDSSGFGDCAVTTRASSSSAFSDSFTEKATSTVAATTSSTLQHFPENEICEQTLSAEMDINVPEENNIEIESDEELPSFSDLEAMILDMDLEPIGQDQYELDASKYRNEEMARKIMRLEQSAESYMNRDIAAHGAFALLYGSSKHYINKPEVLLGRATGEYPVDIDLGRSGSETRFSRRQALIKLKQDGSFEIKNLGKFSIWMNDEEINHGEVVILKNNCLIQIREKSFIFEKNEKAVKRYLDGIHK
Protein: Putative cytochrome c oxidase subunit VI (O61079)
Organism: Trypanosoma brucei rhodesiense
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MPFVDHNKYKIQREDLPALPHFTDFNDPRFCGTNNKQKNGILAYYQWLHCVGNWGEEHSMCKKMRWYVERMMQEVWLEKWEEKRALGHFDHVLLYGVKPWKDFEPLYQPVKTNRKGAYEFWLDRDFEPLYDADASDFCEKAPILHDIFVKGKKPVYDE
Protein: Stress protein DDR48 (DNA damage-responsive protein 48) (DDRP 48) (Flocculent-specific protein) (YP 75) (P18899)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA damage-responsive protein that may be required for maintaining the rate of spontaneous mutagenesis. Shows low ATP and GTP hydrolysis activity. Dispensable for acquisition of thermotolerance and does not play a significant role in recovery or protection of cells from acute heat shock.
Interaction partners:
- Putative uncharacterized membrane protein YMR173W-A
- Protein ISD11
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL21B
- Large ribosomal subunit protein eL21A
Sequence:
MGLFDKVKQFANSNNNNNDSGNNNQGDYVTKAENMIGEDRVNQFKSKIGEDRFDKMESKVRQQFSNTSINDNDSNNNDSYGSNNNDSYGSNNNDSYGSNNNDSYGSNNNDSYGSNNDDSYGSSNKKKSSYGSNNDDSYGSSNNNDSYGSNNNDSYGSNNNDSYGSNNDDSYGSSNKNKSSYGSNNDDSYGSNNDDSYGSSNKKKSSYGSSNNDSYGSNNDDSYGSNNNDSYGSNNDDSYGSSNKKKSSYGSNNDDSYGSSNNNDSYGSNNDDSYGSSNKNKSSYGSSSNDDSYGSSNNDDSYGSSNKKKSSYGSNNDDSYGSNNDDSYGSSNKKKSSYGSSNNDSYGSNNDDSYGSSNKKKSSYGSNNDDSYGSSNNNDSYGSNNDDSYGSSNRNKNSYGSSNYGSSNNDDSYGSSNRGGRNQYGGDDDY
Protein: NKAP family protein (Q55ED4)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- DUF1754 family protein
- Uncharacterized protein
- Pre-mRNA-splicing factor slu7
- Initiation factor eIF-4 gamma middle domain-containing protein
- CBF1-interacting co-repressor CIR N-terminal domain-containing protein
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor SYF2
- Peptidyl-prolyl cis-trans isomerase cypE
- Probable ATP-dependent RNA helicase ddx41
- Uncharacterized protein
Sequence:
MSHRERDRDRDRDSDRDRDRNRYSRSRSRGSRSRSRSRSRSRDRNRNRDYNKDRSSNRDSYYNDRDYKKDRSSNRDRDYYDRDRNRDYKNSSSGSSSGGGGGGSGENYTVKSSSYRESNSNNSKVEIQKQENISKDYFIDNKGVNNSIERKDNIKNENNNNNSFDNRKAEFNNNSYGEKKEFDNNNNRNYHGGNSRYVNNNNNNNNNNYNNNNNKSNYNGTDFFEYRKKLREEATCFSVYERSPSPPKKGELEEIDDQFLSNKKKSKKSRRKSSSNSDSSSSDSDSDSSRSREKRKKSKSRKDKKKRKEKKKHQRKSSKRSSKYSDSDSDSDSSFSDSDYSDSDRSDSEGRSRKKRSKKRSKKRHDHHKESVHDASMWEEKVEQQTQTLSNRDIGPKPISEVQVGSYGGAMMPGEAEAIAQFVKENKRIPRRGEVGLTSEQIASFEETGYVMSGSRHRRMNAVRIRKESQVYSAEEQKALAMLNREEKAKRENRLLADFRDLINTKLQAD
Protein: Candida glabrata strain CBS138 chromosome H complete sequence (Q6FSA8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MSLNELFHGNQHDDTKKKPRRNSSTEVLQYFYKGKETDLVIYVTSQAAADDYLASPSPSKLANVVEVFKVFTNLDGKGATGTFGEASKAQLENEFGKGKKVEEVIGLILKEGVPNGKTNRVKTEGNFQK
Protein: Prenylated Rab acceptor 1 (P53633)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. Peroxisome membrane {ECO:0000305|PubMed:35563734}; Multi-pass membrane protein {ECO:0000255}. Note=Peroxisomal localization is dependent on PEX5. {ECO:0000269|PubMed:35563734}.
Interaction partners:
- Protein transport protein YIF1
- Protein transport protein YIP1
- Protein YIP4
- Rab GDP-dissociation inhibitor
- Protein YIP5
- GTP-binding protein YPT1
Sequence:
MNQLGALAQVSRFTQNFSMENIKSEFQSLQSKLATLRTPQEFFNFKKISKPQNFGEVQSRVAYNLKYFSSNYGLIIGCLSIYTLLTNLLLLFVIVLVVAGIVGINKLKGEELVTPFGSFKTNQLYTGLVCVAVPIGFLASPISTLLWLIGASAVSVFGHASLMEKPIETVFDEETV
Protein: Rho-type GTPase-activating protein 1 (O43052)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: GTPase-activating protein for Rho1. Involved in the F-actin patch localization, cell morphogenesis, regulation of septation, and cell wall synthesis.
Subcellular location: Cell tip {ECO:0000269|PubMed:11737264}. Nucleus {ECO:0000269|PubMed:11737264}. Note=Cell poles and cell division site. {ECO:0000269|PubMed:11737264}.
Interaction partners:
- Rho1 guanine nucleotide exchange factor 1
- GTP-binding protein rho1
- GTP-binding protein rho2
- Rho1 guanine nucleotide exchange factor 2
- Cell division control protein 42 homolog
- Protein kinase C-like 1
- Probable Rho-type GTPase-activating protein 3
- GTP-binding protein rho5
- GTP-binding protein rho4
- Rho1 guanine nucleotide exchange factor 3
Sequence:
MSQRDAKKDGLLYTTNGVSPTPPKRIPVPSRQNKIEENSTTKNFPHSRHTSTVAGTEGGSSLSRRHTSAESRKALPNQQQLAQSGLLNKEEQQSLKRSDTSVFPKAVRKVSSSKICASCGQVISGQYVRALGNIYHLECFRCHDCNSLVASKFFPIDDPTLNKQVPLCETDYFRRLDLLCASCGMALRGYYITALNKKFHIEHFTCSLCYTVFGPNDSYYEYEGKVYCHYHYSTLFAARCCGCDGPILRQFVEVYRNGVSQNWHVPCHMIYKFWNVKLCQKTSIETSKKKDSELSQSQLRKREKHLEQKIFHIWHALSYFEEYTASCISDMLLLVSNGEFTKSVICAQKFIRYIEILFKGIDSLETILSSFHAKSMPYVREAKLLCKKLVSIFALLAKCHNSDIRDVAIVQDFLSLFTGLAHYLKLLIRISLTGGLRLEQDHACKHALPQFLQTVEEARFVDQEGYDSSSFDMPLNLANASSDLCYVCHSALEEDCVLLGEIRCHIGCLSCTKCKYNNRENYDWARWNNQTKQIECYLCYTESSNVSNDEPHPSFEYVSRLSQYIYLLRIALVRLYTILMENNDSSQRKPLSVDPKQENVSSTVETAKQAETTASSDSFRKYANTLNDLRHLKSSRNRKATSNETQSSSNSTETSKLSKNVSESGKDKSPHWHSHGGSITGKSIVEQASSPLERRMDAFDENRAFTLDDIPKVISEQRNREHRPNAFRHMPSYTDPSYRKNSGAIYDKNDGTQKGLTPKSEDAPIRYLSDLSNLELLFTKHVAVLILHPLVRDYYSLDELMEMSDLRKGGFWEKFGKAFKGKDAEKKNVKKKGTFGVPLEILVERNNAQSTVGTGVGVKHIPAFIGNTLAAMKRKDMSVVGVFRKNGNIRRLKELSDMLDVSPDSIDYEQETPIQLAALLKKFLRELPDPLLTFKLFGLFITSSKLESEEERMRVLHLTICLLPKGHRDTMEVIFGFLYWVASFSHIDDEVGSKMDIHNLATVITPNILYSKSNDPVDESFLAIEAVHLLIENFEKFCEVPREISLLLDDPTLFYNNAAWTSKELYKRCEEIISQMSLDERNTPKHTASTKRKRQPIRRVTTNLTSDVPSGSEVADTNSLSSTTKDEASPNSDAQPKPQVKPQHAVIRDS
Protein: Biliverdin reductase A (BVR A) (EC 1.3.1.24) (Biliverdin-IX alpha-reductase) (Q9CY64)
Organism: Mus musculus (Mouse)
Function: Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor. Uses the reactants NADH or NADPH depending on the pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the alkaline range (8.5-8.7). NADPH, however, is the probable reactant in biological systems.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P53004}.
Interaction partners:
- Heme oxygenase 2
- Heme oxygenase 1
- Flavin reductase
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
Sequence:
MSTEPKRKFGVVVVGVGRAGSVRIRDLKDPHSSAFLNLIGYVSRRELGSLDNVRQISLEDALRSQEVDVAYICTESSSHEDYIRQFLQAGKHVLVEYPMALSFAAAQELWELAAQKGRVLHEEHIELLMEEFEFLKREVAGKELLKGSLRFTASPLEEEKFGFPAFSGISRLTWLVSLFGELSLISATMENRKEDQYMKMTVQLETQNKSPLSWIEEKGPGLKRNRHISIHFKSGSLEEVPNVGVNKNIFLKDQDIFIQKLLGQVSAEDLAAEKKRILHCLELASDIQRLCHRKQ
Protein: NAD-specific glutamate dehydrogenase (EC 1.4.1.2) (Q4QF83)
Organism: Leishmania major
Interaction partners:
- Isocitrate dehydrogenase
- Putative nitrilase
- Aspartate aminotransferase
- Transaminase A
- Alanine aminotransferase
- Multifunctional fusion protein
- 2-oxoglutarate dehydrogenase, e3 component,lipoamidedehydrogenase-like protein
- Dihydrolipoyl dehydrogenase
- Acetoin dehydrogenase e3 component-like protein
- Putative dihydrolipoamide dehydrogenase
Sequence:
MMRHTASRAVARLCGRGLPASHAVTSTTLLGVASLATPSRFTSSGATSPLVDRDAIIKAVTTQAVFDKKIVESLANTFVSGLEKSSYPRNFSQAEMIAHVQGLLTAEARFRMGDSFEYVHENHRTAFYICHNEPQKKLRMLRKMARFVSLNQDPHLGSNTHHYVSEDRKFAIYNASIEPFVESGSEEEHVNPKSPALPTRTAARQMTEEQKNIIRGLLRRQLSSVFPVFHVEEVEKGHVSFTMATMVERTNYVASLLSIFQEIEGAEVMMSVSYSFSNGVQVYGFEIRGATAEQIEERASLVGLLPNRPFNAITRLHEAGALSCEETVFIDAAVIFTMYFTPSPTTDDYRHLKAILAKEPNGVNRLNNLRSSLTQEVMSERYTGSVIALYPEFVKLIYEDFRLGSTPERRAAIAEKITHRLREDDRPEYDHTLFMSFLKFNEVIIKHNFCKTEKAALAFRLNPVFLKELEFPRVPHGVFLFAGGQWRGFHIRFTDIARGGVRMIICKERDYRRNKRSVFQENYNLAHTQLLKNKDIPEGGSKGTILVSSRYLNKFDEVRCQHIFLQYVDALLDVIIPGEKGVVDGLKSEEIIFLGPDENTAGTFPAAGALYSKGRGYKSWKSFTTGKDPELGGIPHDVYGMTTHSVRAYVTSIYEKLGLNESEMRKFQTGGPDGDLGSNELLRSKEKMVGMVDISASLHDPKGIDREELARLAHHRLPLREFNRSKLSPEGFLVLTEDCNVKLPDGTLVEDGSRLRNEFHFLKYSDADVFVPCGGRPRSVTLENVGRFLKIPNADGESMMEGKYANLPPEQLKFKIIVEGANLFISQDARLALEKCGVTLIKDASANKGGVTSSSLEVFAGLCLSDEEHTKYMSAKSATDAPEFYKKYVKEILDRIEENAKLEFNAIWREWEKDPQQPKTLIADALSRKNVQIRASMLSSDIFQNRDLVRYVMDQYAPKTLKEVVPVDLMLKRVPENYQHAICAMWLASGYVYQTGVNSNEFDFFRYMTEVYANAAKSAK
Protein: Usher syndrome 1C (Autosomal recessive, severe), isoform CRA_a (Usher syndrome 1C isoform 1) (A0A0S2Z4V1)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
MDRKVAREFRHKVDFLIENDAEKDYLYDVLRMYHQTMDVAVLVGDLKLVINEPSRLPLFDAIRPLIPLKHQVEYDQLTPRRSRKLKEVRLDRLHPEGLGLSVRGGLEFGCGLFISHLIKGGQADSVGLQVGDEIVRINGYSISSCTHEEVINLIRTKKTVSIKVRHIGLIPVKSSPDEPLTWQYVDQFVSESGGVRGSLGSPGNRENKEKKVFISLVGSRGLGCSISSGPIQKPGIFISHVKPGSLSAEVGLEIGDQIVEVNGVDFSNLDHKEGRELFMTDRERLAEARQRELQRQELLMQKRLAMESNKILQEQQEMERQRRKEIAQKAAEENERYRKEMEQIVEEEEKFKKQWEEDWGSKEQLLLPKTITAEVHPVPLRKPKYDQGVEPELEPADDLDGGTEEQGEQDFRKYEEGFDPYSMFTPEQIMGKDVRLLRIKKEGSLDLALEGGVDSPIGKVVVSAVYERGAAERHGGIVKGDEIMAINGKIVTDYTLAEAEAALQKAWNQGGDWIDLVVAVCPPKEYDDELTFF
Protein: Sodium/potassium-transporting ATPase subunit alpha (Q6P271)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta
- Calcium channel, voltage-dependent, P/Q type, alpha 1A subunit, b.
- E3 ubiquitin-protein ligase ZNRF1
- PRA1 family protein.
Sequence:
MGYGRSDSYRVATTQDNDDKESPKKGKGGKDLDDLKKEVPLTEHKMSIEEVCRKYNTDIVQGLTNARAAEYLARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYAIQAATEDEPAGDNLYLGIVLSAVVIITGCFSYFQEAKSSKIMESFKNMVPQQALVIREGEKLQINAEEVVGGDLVEVKGGDRIPADLRIISAHGCKVDNSSLTGESEPQTRSPDCTHDNPLETRNIAFFSTNCVEGTARGIVVCTGDRTVMGRIATLTSGLETGKTPIAKEIEHFIHIITGVAVFLGVTFFILSIILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGASFDKSSGTWLALARVAALCNRAVFKAGQESLPILKRDVAGDASESALLKCIELSCGSVKAMRDKNKKVAEIPFNSTNKYQLSVHELDESEENHYLLVMKGAPERILDRCSTILQQGKEQPMDEELKEAFQNAYLELGGLGERVLGFCHLVMPGDKYPKGFAFDTDDINFQTDNLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVIHGTDLKDLSQDQMDEVLKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLFFILVNIPLPLGTITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPLRDKLVNERLISIAYGQIGMIQALGGFFSYFVILAENGFLPSVLVGIRLNWDDRSNNDLEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADVIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMDVALRMYPLKPSWWFCAFPYSFLIFVYDEIRKLILRRNPGGWVEKETYY
Protein: LD29039p (Q95TR6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MIGASDADKSEAVETEDEVIEVEPDAVPELEPLEDADQQGTPHLSTAALLALTKGNTRRLTGTTKSKKGRVSLSLHGNIFAKSRPASFVAGKRVQLRRKLRRDRIMGRFDEARHLDQMRLSHSAQAAKSPENNNYSLHNRNEEEHLPSENNVMGKTVVLVGKRRLSPVVSTTFNVEERSETSLLQQQFEHENCVTWAMHGGESVMMEETQNDWYFEQLCKETESTAPFQLQPLDYKPLDEEQVEPKFTQLVAASCSNITTTSCATNMTGASSCTVYSIGSVHMQPLPQINITYVQQPSDLQQRRPTRHRSLMAQCRRFLRHLSLGQRLVMGFALLVMVGLSLHLADKLVLVITGILSGMGLVFLTYSCPGRN
Protein: ER lumen protein-retaining receptor A (HDEL receptor) (P35402)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor recognizes H-D-E-L.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein.
Interaction partners:
- Transmembrane emp24 domain-containing protein p24delta5
- Coatomer subunit delta
- Transmembrane emp24 domain-containing protein p24beta3
- Transmembrane emp24 domain-containing protein p24beta2
- Coatomer subunit gamma
- Transmembrane emp24 domain-containing protein p24delta9
- ADP-ribosylation factor 2-B
- Protein transport protein SEC31 homolog A
- F18C1.18 protein
- Protein GRAVITROPIC IN THE LIGHT 1
Sequence:
MNIFRFAGDMSHLISVLILLLKIYATKSCAGISLKTQELYALVFLTRYLDLFTDYVSLYNSIMKIVFIASSLAIVWCMRRHPLVRRSYDKDLDTFRHQYVVLACFVLGLILNEKFTVQEVFWAFSIYLEAVAILPQLVLLQRSGNVDNLTGQYVVFLGAYRGLYIINWIYRYFTEDHFTRWIACVSGLVQTALYADFFYYYYISWKTNTKLKLPA
Protein: Peroxisomal multifunctional enzyme type 2 (MFE-2) (17-beta-hydroxysteroid dehydrogenase 4) (17-beta-HSD 4) (D-bifunctional protein) (DBP) (Multifunctional protein 2) (MFP-2) [Cleaved into: (3R)-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.n12); Enoyl-CoA hydratase 2 (EC 4.2.1.107) (EC 4.2.1.119) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase)] (P51660)
Organism: Mus musculus (Mouse)
Function: Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids. Catalyzes the formation of 3-ketoacyl-CoA intermediates from straight-chain, 2-methyl-branched-chain fatty acids bile acid intermediates. With EHHADH, catalyzes the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity (By similarity).
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:P97852}.
Interaction partners:
- Peroxisomal acyl-coenzyme A oxidase 1
- 3-ketoacyl-CoA thiolase A, peroxisomal
- Sterol carrier protein 2
- Peroxisomal acyl-coenzyme A oxidase 3
- 3-ketoacyl-CoA thiolase B, peroxisomal
- Peroxisomal acyl-coenzyme A oxidase 2
- Peroxisomal targeting signal 1 receptor
- Peroxisomal leader peptide-processing protease
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
Sequence:
MASPLRFDGRVVLVTGAGGGLGRAYALAFAERGALVIVNDLGGDFKGIGKGSSAADKVVAEIRRKGGKAVANYDSVEAGEKLVKTALDTFGRIDVVVNNAGILRDRSFSRISDEDWDIIHRVHLRGSFQVTRAAWDHMKKQNYGRILMTSSASGIYGNFGQANYSAAKLGILGLCNTLAIEGRKNNIHCNTIAPNAGSRMTETVLPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWIGKLRWERTLGAIVRKRNQPMTPEAVRDNWEKICDFSNASKPQTIQESTGGIVEVLHKVDSEGISPNRTSHAAPAATSGFVGAVGHKLPSFSSSYTELQSIMYALGVGASVKNPKDLKFVYEGSADFSCLPTFGVIVAQKSMMNGGLAEVPGLSFNFAKALHGEQYLELYKPLPRSGELKCEAVIADILDKGSGVVIVMDVYSYSGKELICYNQFSVFVVGSGGFGGKRTSEKLKAAVAVPNRPPDAVLRDATSLNQAALYRLSGDWNPLHIDPDFASVAGFEKPILHGLCTFGFSARHVLQQFADNDVSRFKAIKVRFAKPVYPGQTLQTEMWKEGNRIHFQTKVHETGDVVISNAYVDLVPASGVSTQTPSEGGELQSALVFGEIGRRLKSVGREVVKKANAVFEWHITKGGTVAAKWTIDLKSGSGEVYQGPAKGSADVTIIISDEDFMEVVFGKLDPQKAFFSGRLKARGNIMLSQKLQMILKDYAKL
Protein: Pumilio homolog 23 (APUM-23) (AtPUM23) (Q9C552)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:20214804}.
Interaction partners:
- Pumilio homolog 24
- Bystin
- Ribosome biogenesis protein BOP1 homolog
- RNA-binding NOB1-like protein
- Nucleolar protein
- Protein THALLO
- Protein SLOW WALKER 2
- Something about silencing protein
- DEAD-box ATP-dependent RNA helicase 36
- Peter Pan-like protein
Sequence:
MVSVGSKSLPSRRHRTIEEDSLMGERGKSSNNHSERNKGMRRKDHKGNRGFDVDSSKKNQSGGAPNVKPASKKHSEFEHQNQFVRKEIDPETSKYFSEIANLFDSNEVELEERSVICGNALEETRGREYEIATDYIISHVLQTLLEGCELDQLCSFIRNSASVFPAIAMDRSGSHVAESALKSLATHLENPDAYSVIEEALHSICKVIVDNPLDMMCNCYGSHVLRRLLCLCKGVSLDSPELYGAKSSKALAKRLNLKMSQLDDNNLEIPHQGFPGMLTYLLSGLLSCSREDMKYLQVDQYSSLVLQTALRLMLKQDEQLLEIIPLILRCNSTNKKVEGFHIETNVAKEILESMKDNSFSHLVEVILEVAPESLYNEMFNKVFKNSLFELSVDRCANFVIQALISHARDQEQMGIMWEELAPRFKDLLEQGKSGVVASLIAVSQRLQSHENKCCEALVGAVCSTNESRISILPRLLFLDYYFGCRDKSTWEWAPGAKMHVMGCLILQGIFKFSSDHIQPYITSLTSMKAEYITETAKDSSGARVIEAFLASDAATKQKRRLIIKLRGHFGELSLHTSGSFTVEKCFDACNLTLREAIASELLDVKVDLSKTKQGPYLLRKLDIDGYASRPDQWKSRQEAKQSTYNEFCSAFGSNKSNFPKNTFVSDASEDAAQEIEVKNTRKEIDHHPTSGFKRHREKHAKDKDEPFAGEKRSKQKKNKTSEATDKPKLAGSKRPFLSGEMTGKNRHSNKMRI
Protein: Adenylate cyclase type 2 (EC 4.6.1.1) (ATP pyrophosphate-lyase 2) (Adenylate cyclase type II) (Adenylyl cyclase 2) (Q80TL1)
Organism: Mus musculus (Mouse)
Function: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Down-stream signaling cascades mediate changes in gene expression patterns and lead to increased IL6 production. Functions in signaling cascades downstream of the muscarinic acetylcholine receptors.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P26769}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P26769}. Cell membrane {ECO:0000250|UniProtKB:P26769}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P26769}. Cytoplasm {ECO:0000250|UniProtKB:Q08462}.
Interaction partners:
- Guanine nucleotide-binding protein G
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Guanine nucleotide-binding protein G
- Rap guanine nucleotide exchange factor 4
- Rap guanine nucleotide exchange factor 3
- Protein kinase C delta type
- Cannabinoid receptor 1
- Ectonucleoside triphosphate diphosphohydrolase 2
- Bis
Sequence:
MRRRRYLRDRAEAAAAAAAGGGEGLQRSRDWLYESYYCMSQQHPLIVFLLLIVMGACLALLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRVFSLVIWICLVAMGYLFMCFGGTVSAWDQVSFFLFIIFVVYTMLPFNMRDAIIASVLTSSSHTIVLSVYLSATPGAKEHLFWQILANVIIFICGNLAGAYHKHLMELALQQTYRDTCNCIKSRIKLEFEKRQQERLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTNNFHNLYVKRHTNVSILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVKMGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLNGAYKVEEGDGEIRDPYLKQHLVKTYFVINPKGERRSPQHLFRPRHTLDGAKMRASVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTTDVPMGQHNFQNRTLRTKSQKKRFEEELNERMIQAIDGINAQKQWLKSEDIQRISLFFYNKNIEKEYRATALPAFKYYVTCACLIFLCIFIVQILVLPKTSILGFSFGAAFLSLIFILFVCFAGQLLQCSKKASASLLWLLKSSGIIANRPWPRISLTIVTTAIILTMAVFNMFFLSNSEETTLPTANASNANVSVPDNQTAILHARNLFFLPYFIYSCILGLISCSVFLRVNYELKMLIMMVALVGYNIILLHTHAHVLDAYSQVLFQRPGIWKDLKTMGSVSLSIFFITLLVLGRQSEYYCRLDFLWKNKFKKEREEIETMENLNRVLLENVLPAHVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAVPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLILQTLGYTCTCRGIINVKGKGDLKTYFVNTEMSRSLSQSNLAS
Protein: Ribosomal protein L19 (J3QR09)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRLQKRLASSVLRCGKKKVWLDPNETNEIANANSRQQIRKLIKDGLIIRKPVTVHSRARCRKNTLARRKGRHMGIGKRKGTANARMPEKVTWMRRMRILRRLLRRYRESKKIDRHMYHSLYLKVKGNVFKNKRILMEHIHKLKADKARKKLLADQAEARRSKTKEARKRREERLQAKKEEIIKTLSKEEETKK
Protein: Acetylxylan esterase / glucomannan deacetylase (EC 3.1.1.-) (EC 3.1.1.72) (CjCE2B) (B3PDE5)
Organism: Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Function: Involved in the degradation of plant cell wall polysaccharides. Catalyzes the deacetylation of acetylated birchwood xylan and glucomannan, with a large preference for the latter, and of the synthetic substrate 4-nitrophenyl acetate (4-NPAc).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Cellulase, putative, cel5C
- Cellulase, putative, cel5D
- Cellulase, putative, cel9C
- Cellulase, putative, cel5F
- Endoglucanase A
Sequence:
MKPHALIGLLAGMLLSSSLYAADSTKPLPLHIGGRVLVESPANQPVSYTYSWPAVYFETAFKGQSLTLKFDDDQNIFRLIVDDKAPVVINKPGKVDYPVESLAPGKHRVRLEKLTETQSTSGRFLGFYTDPSAKPLALPKRKRQIEFIGDSFTVGYGNTSPSRECTDEELFKTTNSQMAFGPLTAKAFDADYQINASSGFGIVRNYNGTSPDKSLLSLYPYTLNNPDQLYHNKHWKPQVIVIGLGTNDFSTALNDNERWKTREALHADYVANYVKFVKQLHSNNARAQFILMNSDQSNGEIAEQVGKVVAQLKGGGLHQVEQIVFKGLDYSGCHWHPSANDDQLLANLLITHLQQKKGIW