wanglab/gogpt-training-data huggingface dataset:
Protein: P protein (Melanocyte-specific transporter protein) (Pink-eyed dilution protein) (Q62052)
Organism: Mus musculus (Mouse)
Function: Contributes to a melanosome-specific anion (chloride) current that modulates melanosomal pH for optimal tyrosinase activity required for melanogenesis and the melanosome maturation. One of the components of the mammalian pigmentary system (By similarity). May serve as a key control point at which color variation is determined. Major determinant of eye color (Probable). Seems to regulate the post-translational processing of tyrosinase, which catalyzes the limiting reaction in melanin synthesis.
Subcellular location: Melanosome membrane {ECO:0000269|PubMed:7991586}; Multi-pass membrane protein {ECO:0000269|PubMed:7991586}.
Interaction partners:
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Tyrosinase
- Aminomethyltransferase, mitochondrial
- Sodium/potassium/calcium exchanger 5
- Membrane-associated transporter protein
- Signal transducer and activator of transcription 1
- Melanocyte-stimulating hormone receptor
- Synaptosomal-associated protein 29
- G-protein coupled receptor 143
- Glycine cleavage system H protein, mitochondrial
Sequence:
MRLENKDIRLASAVLEVELHQTSALSVPTCPDPGRLLTVKPATSNYKLGQADPCIPYAGEAAGKSVCVPEHTEFGSFLVKGSSSLKDLSFKEDTPLLWNSSQKKRSQLMPVHHPEFIATEGSWENGLTAWEQKCMLGKEVADLSALASSEKRDLAGSVHLRAQVSKLGCCVRWIKITGLFVFVVLCSILFSLYPDQGKFWQLLAVSPLENYSVNLSGHADSMILQLDLAGALMAGGPSGSGKEEHVVVVVTQTDAAGNRRRRPQQLTYNWTVLLNPRSEHVVVSRTFEIVSREAVSISIQASLQQTRLVPLLLAHQFLGASVEAQVASAVAILAGVYTLIIFEIVHRTLAAMLGALAALAALAVVGDRPSLTHVVEWIDFETLALLFGMMILVAVFSETGFFDYCAVKAYQLSRGRVWAMIFMLCLMAAILSAFLDNVTTMLLFTPVTIRLCEVLNLDPRQVLIAEVIFTNIGGAATAIGDPPNVIIVSNQELRKMGLDFAGFTAHMFLGICLVLLVSFPLLRLLYWNKKLYNKEPSEIVELKHEIHVWRLTAQRISPASREETAVRGLLLEKVLALEHLLAQRLHTFHRQISQEDKNWETNIQELQRKHRISDRSLLVKCLTVLGFVISMFFLNSFVPGIHLDLGWIAILGAIWLLILADIHDFEIILHRVEWATLLFFAALFVLMEALTHLHLVEYVGEQTALLIKMVPEDQRFAAAIVLIVWVSALASSLIDNIPFTATMIPVLLNLSQDPEISLPALPLMYALALGACLGGNGTLIGASTNVVCAGIAEKHGYGFSFMEFFRLGFPVMLMSCTIGMCYLLIAHIVVGWN
Protein: RYamide neuropeptides (Neuropeptide Y-like receptor ligand) [Cleaved into: RYamide-1; RYamide-2] (G5CKU5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Neuropeptides RYamide-1 and RYamide-2 are ligands for the G-protein coupled receptor RYa-R. May suppress feeding behavior.
Subcellular location: Secreted {ECO:0000305|PubMed:21704020, ECO:0000305|PubMed:21843505}.
Interaction partners:
- RYamide receptor
Sequence:
MNECVNKLLHLKFLFYFILGIQKRPVFFVASRYGRSTTYDESLKSRRIFIVPRNEHFFLGSRYGKRSGKYLCLSREINKLIVRKRLRNNDKERTPTLSFITKHFLMRNT
Protein: SH2 domain-containing adapter protein D (Q96IW2)
Organism: Homo sapiens (Human)
Function: May function as an adapter protein.
Interaction partners:
- Dehydrogenase/reductase SDR family member 2, mitochondrial
Sequence:
MAKWLRDYLSFGGRRPPPQPPTPDYTESDILRAYRAQKNLDFEDPYEDAESRLEPDPAGPGDSKNPGDAKYGSPKHRLIKVEAADMARAKALLGGPGEELEADTEYLDPFDAQPHPAPPDDGYMEPYDAQWVMSELPGRGVQLYDTPYEEQDPETADGPPSGQKPRQSRMPQEDERPADEYDQPWEWKKDHISRAFAVQFDSPEWERTPGSAKELRRPPPRSPQPAERVDPALPLEKQPWFHGPLNRADAESLLSLCKEGSYLVRLSETNPQDCSLSLRSSQGFLHLKFARTRENQVVLGQHSGPFPSVPELVLHYSSRPLPVQGAEHLALLYPVVTQTP
Protein: Protein DOA1 (Degradation of alpha protein 1) (Ubiquitin fusion degradation protein 3) (P36037)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ubiquitin-binding protein involved in protein ubiquitination, sorting and degradation. Acts as a ubiquitinated substrate-recruiting adapter for chaperone ATPase CDC48 by binding mono- or polyubiquitin chains. Depending on the context, promotes or prevents proteasomal degradation of ubiquitinated proteins. Involved in the ubiquitin fusion degradation (UFD) pathway by promoting the degradation of ubiquitinated proteins. Involved in the mitochondria-associated degradation pathway (MAD) by promoting the degradation of several ubiquitinated membrane proteins. By competing with UFD2 to bind CDC48, prevents the multi-ubiquitination and subsequent degradation of UFD2-dependent substrates. Required for ribophagy, a process which relocalizes ribosomal particles into the vacuole for degradation in response to starvation. Involved in the ubiquitin-mediated sorting of membrane proteins into multivesicular bodies (MVBs). In addition, plays an essential role in maintaining cellular ubiquitin levels. May affect indirectly the degradation of ubiquitinylated proteins by regulating cellular ubiquitin levels.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18508771, ECO:0000269|PubMed:27044889}. Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18508771, ECO:0000269|PubMed:27044889}. Mitochondrion outer membrane {ECO:0000269|PubMed:27044889}; Peripheral membrane protein {ECO:0000269|PubMed:27044889}; Cytoplasmic side {ECO:0000269|PubMed:27044889}. Endosome membrane {ECO:0000269|PubMed:18508771}; Peripheral membrane protein {ECO:0000269|PubMed:18508771}; Cytoplasmic side {ECO:0000269|PubMed:18508771}. Note=Predominantly localizes to the cytoplasm. Probably localizes to endosomes and mitochondria in a transient manner. {ECO:0000269|PubMed:18508771, ECO:0000269|PubMed:27044889}.
Interaction partners:
- Nuclear protein localization protein 4
- Ubiquitin fusion degradation protein 1
- Cell division control protein 48
- UBX domain-containing protein 2
- UBX domain-containing protein 1
- Ubiquitin thioesterase OTU1
- Protein SPT23
- Polyubiquitin
- E4 ubiquitin-protein ligase UFD2
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MGYQLSATLKGHDQDVRDVVAVDDSKVASVSRDGTVRLWSKDDQWLGTVVYTGQGFLNSVCYDSEKELLLFGGKDTMINGVPLFATSGEDPLYTLIGHQGNVCSLSFQDGVVISGSWDKTAKVWKEGSLVYNLQAHNASVWDAKVVSFSENKFLTASADKTIKLWQNDKVIKTFSGIHNDVVRHLAVVDDGHFISCSNDGLIKLVDMHTGDVLRTYEGHESFVYCIKLLPNGDIVSCGEDRTVRIWSKENGSLKQVITLPAISIWSVDCMSNGDIIVGSSDNLVRIFSQEKSRWASEDEINELSTQVEKSTISSKTIEFDESKLSPYEILQSPGRKEGQIVVVKSPQGTIEAHQFSNSSWKKVGDVVGAGATGNDKKIEFEGKTYDYVFDVDIEDGKPPLKLPINVSDNPYTAADNFLARYELPMSYRDQVVQFILKNTNGISLDQPNDNASSSAVSPSKTSVMKVLPVKQYLIMENYNPDTIFNGIVKINSNEKTFDDEILAQIGGALHDIDESWELLLSFANTIRSNWEIKTPAYDIVRLIVKKLPYSSDIKDYIEEGLGNKNITLTMLTVRILVNCFNNENWGVKLLESNQVYKSIFETIDTEFSQASAKQSQNLAIAVSTLIFNYSALVTKGNSDLELLPIVADAINTKYGPLEEYQECEEAAYRLTVAYGNLATVEPTLRQFANSVTWLANIKRSYGNVPRFKDIFDDLS
Protein: Inner membrane protein CbrB (CreB-regulated gene B protein) (P31468)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- UPF0167 protein CbrC
- Protein CbrA
- 6-phosphogluconate phosphatase
Sequence:
MSVSRRVIHHGLYFAVLGPLIGVLFLVLYIFFAKEPLVLWVIIHPIFLLLSITTGAIPALLTGVMVACLPEKIGSQKRYRCLAGGIGGVVITEIYCAVIVHIKGMASSELFENILSGDSLVVRIIPALLAGVVMSRIITRLPGLDISCPETDSLS
Protein: Uncharacterized protein, isoform P (M9PB72)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNKVEFKNKNKDQGPCARVRKIRPINMGGNVEQRPWTPTVRIGKIAAETTNPGPATVQLPTLIGSKVPDSKKKAAPSYSFGHKLGGKYDTSGPGPAQYNVTGMRAKGRDYPRAATLQSRPKELTRFSNPGPGEYDVVPAAKAVIDATPKYTFGQRPVALKTFQIPAPGAYCPEKVKLNKTPEFSFGIKHHEQRPDYTPAPGTYKPEQVVLEHIPAYSFGLKTKHIQVSDTPAPGAYSPEKSRLHSAPAYSIAGKASQDVVDCTPAPGAYEPEKCVLSRTPAFSFGHRAELAKSSDTPAPGTYNPEKVRLDHTPAFTLSGRPETRSVSETPAPGSYAPEKYRNDRTPAFTFGGKHEQRLESSTPAPGDYCPEKVRHDHNPAFSFAGRHDLHKPSDTPAPGAYDTEKVRQDHNPAFSFAGRHDLHKPSETPAPGAYSPEKVRQDHNPAFSMAGKHSQKVTSDSPAPGDYCPEKVRLDHTPAYSFGVKSDPKVENNTPAPGDYHPEKVRQDHNPAYSFAGRHDLQKPDNTPAPGAYFPEKVRLDHNPAFSMAGKYDAKVTNDTPAPGDYSPEKVRQDTNPAYSFAGRHDLHKPSETPAPGAYSPEKVRLDHNPAFTMAGKHDQKILNGTPAPGDYSPEKCRLDHTPAYSFGGKNDPKVENNTPAPGDYHPEKVRLDHNPAYSFAGRHDLQKPSDTPAPGAYSPEKVRQDHNPAFSMAGKPVEKLTNGTPAPGDYSPEKVRLNHTPAYTFGGKNDPKVENNTPAPGDYHPEKVRQDHNPAFSFAGRHDLHKPNDTPAPGAYCPEKVRQDHNPAFSMAGKYTQKVANDTPAPGDYSPEKVRLDHTPAYTFGGKNDPKVESNTPAPGDYHPEKVRQDHNPAFSFAGRHNLQKPSDTPAPGAYSPEKVRQDHNPAFTMAGKHDPKVSNDTPAPGDYSPEKVRLDYTPSFTFAGKNNPKVENDTPAPGDYHPEKVRQDHNPAFSFAGRHDLHKPSDTPAPGAYSPEKVRQDHNPAFSMAGKYIEKITNGTPAPGDYCPEKVRLDHTPAFTFGGKNDPKVENNTPAPGDYHPEKVRQDHVPAFSFAGRHDLHKPNETPAPGAYSPEKVRQDHNPAFTMAGKHDPKVTHDTPAPGDYHPEKVRLDHNPAFSFAGRHDLHKPSETPAPGDYFPEKVRQDFNPAFTFAGKHDPRSLSESPAPGDYSPEKVRLDHAPAFSFGGKHDPKTEHLHPAPCDYAPEKVRLDHTPAYTIAGRPAADHVSQTPAPCDYHPEQCQVDSTPAFTFGMRLGRERISDTPAPGHYHPEQCKLDSSPAYSFGLKTVPTASLPEPRGAYIEDRIVQRRERRLASPVRNNAECTTTTTNHTNNNAGSSTTTTTTTTTTTKTFINGVEQPELQKKETTKQVNGTHKELKSAPQAPLSNGNIVSNGNHSKMVSTTTRIQEVAHGQKESGNLKVVASGKSDASATKAAAVSHQTVVQADGAIVTSGQSSRMQTVKYAVEASSVQEKIISS
Protein: Hydroxyproline dehydrogenase (HYPDH) (EC 1.5.5.3) (Kidney and liver proline oxidase 1) (MmPOX1) (Probable proline dehydrogenase 2) (EC 1.5.5.2) (Probable proline oxidase 2) (Proline oxidase-like protein) (PO) (Proline oxidase) (Q8VCZ9)
Organism: Mus musculus (Mouse)
Function: Dehydrogenase that converts trans-4-L-hydroxyproline to delta-1-pyrroline-3-hydroxy-5-carboxylate (Hyp) using ubiquinone-10 as the terminal electron acceptor. Can also use proline as a substrate but with a very much lower efficiency. Does not react with other diastereomers of Hyp: trans-4-D-hydroxyproline and cis-4-L-hydroxyproline. Ubiquininone analogs such as menadione, duroquinone and ubiquinone-1 react more efficiently than oxygen as the terminal electron acceptor during catalysis.
Interaction partners:
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Pyrroline-5-carboxylate reductase 3
- Pyrroline-5-carboxylate reductase 2
- Pyrroline-5-carboxylate reductase 1, mitochondrial
- Prolyl 4-hydroxylase subunit alpha-2
- Prolyl 4-hydroxylase subunit alpha-1
- Prolyl 4-hydroxylase subunit alpha-3
- 4-hydroxy-2-oxoglutarate aldolase, mitochondrial
- Delta-1-pyrroline-5-carboxylate synthase
Sequence:
MIWTRLPLYGPSKPSTGGWQPLRFDGGAFHVKGTAELARALLVLRLCAWPPLVTHGLAFQAWSQRLLGSRLSGALLRASIYGQFVAGETAEEVRNCVGQLQALGLQPLLAVPTEEEPDSTAKTSEVWYEENLSAMLRCVDLSRALVDAHGPARNSLMQLKVTALASTRLCKELSAWIQRPRGSSELSPERLAEAMDSGRNLQLSCLSTEQNQHLQASLSRLHRVAQHARAKCVRLLVDAEYTFINPALSLLVAALAVRWNSPEEGGPWVWNTYQAYLKDTHQRLEQDAEAAHKAGLAFGVKLVRGAYLDKERSMTQLQGKEDCTQPDYEATSRSYSRCLELMLRCVSNHGPPCHLMVASHNEESVRQATKRMWELGIPLDGPVCFGQLLGMCDHVSLALGQAGYMVYKSIPYGCLEEVIPYLIRRAQENRSVLQGARREQALLSQELWRRLLGRTA
Protein: Zinc finger protein 789 (Q5FWF6)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MFPPARGKELLSFEDVAMYFTREEWGHLNWGQKDLYRDVMLENYRNMVLLGFQFPKPEMICQLENWDEQWILDLPRTGNRKASGSACPGSEARHKMKKLTPKQKFSEDLESYKISVVMQESAEKLSEKLHKCKEFVDSCRLTFPTSGDEYSRGFLQNLNLIQDQNAQTRWKQGRYDEDGKPFNQRSLLLGHERILTRAKSYECSECGKVIRRKAWFDQHQRIHFLENPFECKVCGQAFRQRSALTVHKQCHLQNKPYRCHDCGKCFRQLAYLVEHKRIHTKEKPYKCSKCEKTFSQNSTLIRHQVIHSGEKRHKCLECGKAFGRHSTLLCHQQIHSKPNTHKCSECGQSFGRNVDLIQHQRIHTKEEFFQCGECGKTFSFKRNLFRHQVIHTGSQPYQCVICGKSFKWHTSFIKHQGTHKGQIST
Protein: Opsin-3 (Encephalopsin) (Panopsin) (Q9WUK7)
Organism: Mus musculus (Mouse)
Function: G-protein coupled receptor which selectively activates G proteins via ultraviolet A (UVA) light-mediated activation in the skin. Binds both 11-cis retinal and all-trans retinal (By similarity). Regulates melanogenesis in melanocytes via inhibition of alpha-MSH-induced MC1R-mediated cAMP signaling, modulation of calcium flux, regulation of CAMK2 phosphorylation, and subsequently phosphorylation of CREB, p38, ERK and MITF in response to blue light (By similarity). Plays a role in melanocyte survival through regulation of intracellular calcium levels and subsequent BCL2/RAF1 signaling (By similarity). Additionally regulates apoptosis via cytochrome c release and subsequent activation of the caspase cascade (By similarity). Required for TYR and DCT blue light-induced complex formation in melanocytes (By similarity). Involved in keratinocyte differentiation in response to blue-light (By similarity). Required for the UVA-mediated induction of calcium and mitogen-activated protein kinase signaling resulting in the expression of MMP1, MMP2, MMP3, MMP9 and TIMP1 in dermal fibroblasts (By similarity). Plays a role in light-mediated glucose uptake, mitochondrial respiration and fatty acid metabolism in brown adipocyte tissues. May be involved in photorelaxation of airway smooth muscle cells, via blue-light dependent GPCR signaling pathways.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9H1Y3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9H1Y3}.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MYSGNRSGDQGYWEDGAGAEGAAPAGTRSPAPLFSPTAYERLALLLGCLALLGVGGNLLVLLLYSKFPRLRTPTHLFLVNLSLGDLLVSLFGVTFTFASCLRNGWVWDAVGCAWDGFSGSLFGFVSITTLTVLAYERYIRVVHARVINFSWAWRAITYIWLYSLAWAGAPLLGWNRYILDIHGLGCTVDWRSKDANDSSFVLFLFLGCLVVPVGIIAHCYGHILYSVRMLRCVEDLQTIQVIKMLRYEKKVAKMCFLMAFVFLTCWMPYIVTRFLVVNGYGHLVTPTVSIVSYLFAKSSTVYNPVIYIFMNRKFRRSLLQLLCFRLLRCQRPAKNLPAAESEMHIRPIVMSQKDGDRPKKKVTFNSSSIIFIITSDESLSVEDSDRSSASKVDVIQVRPL
Protein: Caveolae-associated protein 3 (Cavin-3) (Protein kinase C delta-binding protein) (Serum deprivation response factor-related gene product that binds to C-kinase) (hSRBC) (Q969G5)
Organism: Homo sapiens (Human)
Function: Regulates the traffic and/or budding of caveolae. Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in smooth muscle but not in the lung and heart endothelial cells. Regulates the equilibrium between cell surface-associated and cell surface-dissociated caveolae by promoting the rapid release of caveolae from the cell surface. Plays a role in the regulation of the circadian clock. Modulates the period length and phase of circadian gene expression and also regulates expression and interaction of the core clock components PER1/2 and CRY1/2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q91VJ2}. Membrane, caveola {ECO:0000269|PubMed:19262564}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q91VJ2}. Note=Localizes in the caveolae in a caveolin-dependent manner. {ECO:0000269|PubMed:19262564}.
Interaction partners:
- Caveolin-1
- Caveolae-associated protein 1
- Caveolae-associated protein 2
Sequence:
MRESALERGPVPEAPAGGPVHAVTVVTLLEKLASMLETLRERQGGLARRQGGLAGSVRRIQSGLGALSRSHDTTSNTLAQLLAKAERVSSHANAAQERAVRRAAQVQRLEANHGLLVARGKLHVLLFKEEGEVPASAFQKAPEPLGPADQSELGPEQLEAEVGESSDEEPVESRAQRLRRTGLQKVQSLRRALSGRKGPAAPPPTPVKPPRLGPGRSAEAQPEAQPALEPTLEPEPPQDTEEDPGRPGAAEEALLQMESVA
Protein: Brevinin-1Ta (P82233)
Organism: Rana temporaria (European common frog)
Function: Antibacterial activity against representative Gram-negative and Gram-positive bacteria and exhibits a very high hemolytic activity.
Subcellular location: Secreted {ECO:0000269|PubMed:10333736, ECO:0000269|PubMed:34235566}.
Interaction partners:
Sequence:
FITLLLRKFICSITKKC
Protein: RNA polymerase sigma-54 factor (B5XST9)
Organism: Klebsiella pneumoniae (strain 342)
Interaction partners:
Sequence:
MKQGLQLRLSQQLAMTPQLQQAIRLLQLSTLELQQELQQALESNPLLEQTDLHDEVEAKEVEDRESLDTVDALEQKEMPDELPLDASWDEIYTAGTPSGNGVDYQDDELPVYQGETTQTLQDYLMWQVELTPFTDTDRAIATSIVDAVDDTGYLTIQIEDIVDSIGDDEIGLEEVEAVLKRIQRFDPVGVAAKDLRDCLLIQLSQFAKETPWLEEARLIISDHLDLLANHDFRTLMRVTRLKEEVLKEAVNLIQSLDPRPGQSIHTSEPEYVIPDVLVRKVSGRWTVELNADSIPRLKINQQYAAMGNSARNDADGQFIRSNLQEARWLIKSLESRNDTLLRVSRCIVEQQQAFFEQGEEYMKPMVLADIAQAVEMHESTISRVTTQKYLHSPRGIFELKYFFSSHVNTEGGGEASSTAIRALVKKLIAAENPAKPLSDSKLTSMLSEQGIMVARRTVAKYRESLSIPPSNQRKQLV
Protein: Probable iron-sulfur-binding reductase (O33268)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Electron transfer flavoprotein subunit beta
- dTDP-glucose 4,6-dehydratase
- Electron transfer flavoprotein subunit alpha
- Glyceraldehyde-3-phosphate dehydrogenase
- Uncharacterized protein Rv2047c
- Alanine aminotransferase
- Probable enoyl-CoA hydratase EchA3
- UPF0073 membrane protein Rv1085c
Sequence:
MTTQTLIRLILGMSMTAVVGVFALRRVWWLYKLVMSGQPASGRTDNLGTRIWTQISEVLGQRRLLKWSIPGLAHFFTMWGFFILLTVYIEAYGLLFEERFHIPVIGRWDALGFLQDFFATAVFLGITTFAIIRILRNPREIGRSSRFYGSHNGGAWLVLLMIFNVIWTYVLVRGSAVNNGTLPYGNGAFLSQLFGAILRPLGQPANEIIETTALLLHIGVMLAFLILVLHSKHLHIFLAPINVTFKRLPDGLGPLLPLEADGKPIDFENPSEDAVFGRGKIEDFTWKGMLDFATCTECGRCQSQCPAWNTGKPLSPKLVIMDLRDHWMAKAPYILGQKDASAGGEAGHQEHHHVPESGFGRVPGHGPEQATRPLVGTEEQGGVIDPDVLWSCVTCGACVEQCPVDIEHVDHIVDMRRYQVMMESEFPSELSVLFKNLETKGNPWGQNASDRTNWIDEVDFDVPVYGQDVDSFDGYEYLFWVGCAGAYDDKAKKTTKAVAELLAVARVKYLVLGAGETCNGDSARRSGNEFLFQQLAQQAVETLDGLFEGVETVDRKIVVTCPHCFNTIGKEYRQLGANYTVLHHTQLLNRLVRDKRLVPVTPVSQDITYHDPCYLGRHNKAYEAPRELIGAAGASLTEMPRHADRSFCCGAGGARMWMEEHIGKRINHERVDEALATDATAIATACPFCRVMVTDGVNDRQEEAGRSGVEVLDVAQVLLGSLDHDKAQLPAKGTAAKQAQERAPKAAPKAAAPVTPVEAPAEAPQAPAPAAPAAPVKGLGMAAGAKRPGAKKAAPTPAAPAAPAAPVKGLGIAAGAKRPGAKKTPPPAPGLAEPAAQPQPEAKPQPEPAAPPKPQTDGDPAAPAAPVKGLGIARGARPPGKR
Protein: Esculentin-1B (P84841)
Organism: Pelophylax saharicus (Sahara frog) (Rana saharica)
Function: Antimicrobial peptide (By similarity). Stimulates insulin secretion by BRIN-BD11 cells in vitro.
Subcellular location: Secreted {ECO:0000269|PubMed:16394170}.
Interaction partners:
Sequence:
GIFSKLAGKKLKNLLISGLKNVGKEVGMDVVRTGIDIAGCKIKGEC
Protein: Segment polarity protein dishevelled (P51140)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required to establish coherent arrays of polarized cells and segments in embryos. Plays a role in wingless (wg) signaling, possibly through the reception of the wg signal by target cells and subsequent redistribution of arm protein in response to that signal in embryos. This signal seems to be required to establish planar cell polarity and identity.
Subcellular location: Cytoplasm. Nucleus. Membrane; Peripheral membrane protein. Note=Associated with the membrane when hyperphosphorylated.
Interaction partners:
- Protein prickle
- Low-density lipoprotein receptor-related protein
- Protein espinas
- Axin
- Vang-like protein
- Frizzled
- Frizzled-3
- Diego, isoform A
- Protein naked cuticle
- Frizzled-2
Sequence:
MDADRGGGQETKVIYHIDDETTPYLVKIPIPSAQVTLRDFKLVLNKQNNNYKYFFKSMDADFGVVKEEIADDSTILPCFNGRVVSWLVSADGTNQSDNCSELPTSECELGMGLTNRKLQQQQQQHQQQQQQQQQQHQQQQQQQQQQVQPVQLAQQQQQQVLHHQKMMGNPLLQPPPLTYQSASVLSSDLDSTSLFGTESELTLDRDMTDYSSVQRLQVRKKPQRRKKRAPSMSRTSSYSSITDSTMSLNIITVSINMEAVNFLGISIVGQSNRGGDGGIYVGSIMKGGAVALDGRIEPGDMILQVNDVNFENMTNDEAVRVLREVVQKPGPIKLVVAKCWDPNPKGYFTIPRTEPVRPIDPGAWVAHTQALTSHDSIIADIAEPIKERLDQNNLEEIVKAMTKPDSGLEIRDRMWLKITIPNAFIGADAVNWVLENVEDVQDRREARRIVSAMLRSNYIKHTVNKLTFSEQCYYVVNEERNPNLLGRGHLHPHQLPHGHGGHALSHADTESITSDIGPLPNPPIYMPYSATYNPSHGYQPIQYGIAERHISSGSSSSDVLTSKDISASQSDITSVIHQANQLTIAAHGSNKSSGSSNRGGGGGGGGGGNNTNDQDVSVFNYVL
Protein: UDP-glucuronosyltransferase 2B17 (UGT2B17) (EC 2.4.1.17) (M-1) (UDP-glucuronosyltransferase 2B5) (UDPGT 2B5) (P17717)
Organism: Mus musculus (Mouse)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (epitestosterone, androsterone) and estrogens (estradiol, epiestradiol).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O75795}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 3A11
- Cytochrome P450 3A25
- Cytochrome P450 1A1
- UDP-glucuronosyltransferase
- Cytochrome P450 2E1
- Cytochrome P450, family 2, subfamily c, polypeptide 68
- UDP-glucose 6-dehydrogenase
- Retinol dehydrogenase 7
- Beta-glucuronidase
- Carboxylesterase 1C
Sequence:
MPGKWISALLLLQISCCFRSVKCGKVLVWPMEFSHWMNIKIILDELVQRGHEVTVLRPSAYYVLDPKKSPGLKFETFPTSVSKDNLENFFIKFVDVWTYEMPRDTCLSYSPLLQNMIDEFSDYFLSLCKDVVSNKELMTKLQESKFDVLLSDPVASCGELIAELLQIPFLYSIRFSPGYQIEKSSGRFLLPPSYVPVILSGLGGQMTFIERIKNMICMLYFDFWFQMFNDKKWDSFYSEYLGRPTTLVETMGQAEMWLIRSNWDLEFPHPTLPNVDYVGGLHCKPAKPLPKDMEEFVQSSGDHGVVVFSLGSMVSNMTEEKANAIAWALAQIPQKVLWKFDGKTPATLGHNTRVYKWLPQNDLLGHPKTKAFVTHGGANGVYEAIYHGIPMIGIPLFGEQHDNIAHMVAKGAAVALNIRTMSKSDVLNALEEVIENPFYKKNAIWLSTIHHDQPMKPLDRAVFWIEFVMRHKRAKHLRPLGHNLTWYQYHSLDVIGFLLSCVATTIVLSVKCLLFIYRFFVKKENKMKNE
Protein: Rosmarinate synthase (CbRAS) (EC 2.3.1.140) (Hydroxycinnamoyl transferase) (CbHCT1) (A0PDV5)
Organism: Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides)
Function: Involved in the biosynthesis of rosmarinic acid, a compound with antiviral, antimicrobial and anti-inflammatory activities. Can use 4-coumaroyl- and caffeoyl-CoA as hydroxycinnamoyl donors and 4-Hydroxyphenyllactate and 3.4-Dihydroxyphenyllactate, but not shikimate or quinate, as hydroxycinnamoyl acceptors. Can also putatively catalyze amide formation with D-amino acids as acceptors.
Interaction partners:
Sequence:
MKIEVKDSTMIKPSAETPGGSLWLSNLDLLSPANYHTLSVHFYSHDGSDNFFDAAGLKESLSRALVEFYPYAGRLKLNGNRLEIDCNNEGLLLVEAECDGALDELGDFAPRPELNLIPKVDYSRGISTYPLMVFQLTRFKCGGVALGVANEHHLSDGVAALHFINTWAHLSRGAPAPTPLPHFDRSSLSARNPPQPQFSHAEYQPPPTLENPLPHTDIAHSRFKLTRDQLNSLKSKFKTAPADGGAGKSYSTFEVLAGHIWRSVCIARGLPEGQETKLHIPFDGRGRLQLPPGFFGNAIFFATPIATCGEIESNSLNYAVRRVSDGVSRLDEDYLRSSIDFLELQEDISKLAQGAHSFRCPNLWVISWVWLPIYEPDFGWGKAVYMGPWAAPFEGKSYLLPNPEKDGSLFVSITLHKQHMERFEKLFYEI
Protein: Chitinase 12 (EC 3.2.1.14) (Basic endochitinase 2) (Pathogenesis related (PR)-3 chitinase 12) (P25765)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Hydrolyzes chitin and plays a role in defense against fungal pathogens containing chitin. Its overexpression confers enhanced resistance to sheath blight pathogen (R.solani).
Interaction partners:
Sequence:
MRALAVVAMVATAFLAAAVHAEQCGSQAGGAVCPNCLCCSQFGWCGSTSDYCGAGCQSQCSAAGCGGGGPTPPSGSGGSGVASIVSRSLFDQMLLHRNDAACPASNFYTYDAFVAAASAFPGFAAAGGDADTNKREVAAFLAQTSHETTGGWATAPDGPYAWGYCFKEENGGAAGPDYCQQSAQWPCAAGKKYYGRGPIQLSYNFNYGPAGQAIGADLLGDPDLVASDATVSFDTAFWFWMTPQSPKPSCHAVATGQWTPSADDQAAGRVPGYGVITNIINGGLECGHGEDDRVADRIGFYKRYCDILGVSYDANLDCYSQRPFGS
Protein: ATP-dependent RNA helicase (EC 3.6.4.13) (Q5XHY0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Ribosome biogenesis protein BOP1
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- GTP-binding protein 4
- BMS1 ribosome biogenesis factor
- Pescadillo homolog
- Ribosome biogenesis protein WDR12
- NOC2-like nucleolar associated transcriptional repressor
- Periodic tryptophan protein 2 homolog
- WD repeat-containing protein 74
- Ribosome biogenesis protein BRX1 homolog
Sequence:
MSQLQMKLLRKKIEKRNAKLRQRNLKLQEASDRSLSQPENGDVPEELGKGGKAKKALKHSVTAGSAEAQSRGVPEETVENAKVKKSPQKLTILTNGEAAAMPSTDPELKKKKKKKRKIGNDTEPDPKKAKTEEGTEAREEPEGAGEEPEGAGEEPEDGVKEADDSEVPSLPLGVTGAFEDTSFASLSNLVNENTLKAIEEMGFKHMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGTGVLILSPTRELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIVVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARISLKKEPLYVGVDDDKEVATVDGLEQGYVVCPSEKRFLLLFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTARGLNGRGHALLILRPEELGFLRYLKQSKVPLNQFDFSWSKVSDIQSQLEKLIEKNYFLHKSAQEAYKSYIRAYDSHSLKQIFNVNNLNLPQVALSFGFKVPPFVDLNVSSHDGKLKKRGGGGGFGYQKTKKVEKSKIFKHISKKPADRRQFSH
Protein: Cilia- and flagella-associated protein 221 homolog (Flagella-associated protein 221) (Primary ciliary dyskinesia protein 1) (A8J6X7)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: May play a role in cilium morphogenesis.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:20421426}. Cytoplasm {ECO:0000250|UniProtKB:A9Q751}.
Interaction partners:
Sequence:
MALASNPRRRLHEVRVQKYVVIAVTWRGAQPMSQRARPSRVVRAAAWGMFARCHPGAAAGWHRCTDLVTRSSARPAYTVASQSFSQGLVEDAPLQNPNTLTYNRVYSKVGNTRILQAEPAVLNFGGYELGKVYSQVLRIRNVRASGTRFHIIPPSTPFFKATCPAKKGLLAPGMTEEVAVEFCPTQYRYYYDCVRVHCEEENLLIPLHAYPVANEALFPTRVDFGRVALGQEVVRSHTLECKVPVDFEYEIVEVKPNPAFRVEPARGVVPGRGRVTVDMWFCPLALTTEEAVIETEVAGVYVPDTMLLSAAEVGLRTKDVRGAIEARKAAAAEQQAALEKGALFRLQLALAEEAARKVALGTAPHSGQQLLTAEQPELEAGGAVHQPSAPVGSSSSGGGGGSDPAFKPEHKRTRVLDKFMRAVWRVVTHQRLQRRLERIKEVLAHLGYDKQRLAEEAANPVLLVSESDRPGTAPTKYLRPEMVRVRPLPLYRDVLFQVHHATDLSHYTDFDELAPFTSKVRERLVPSGLVPPLSDYPTMPDACKNMPYITLEIGNRYGDDRVYGAPDPSYSPYGSLDVDYAVQPRQYDVYDSARHEAVASGGVRSLRGGPGLSDSWLVRQICPAVPTDEQLAKCGGTGIVNTIPN