wanglab/gogpt-training-data huggingface dataset:
Protein: Disease resistance protein RPP8 (Resistance to Peronospora parasitica protein 8) (Q8W4J9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Disease resistance protein. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. The interaction with TIP (TCV-interacting protein) may be essential for the recognition of the avirulence proteins, and the triggering of the defense response. Triggers resistance to turnip crinkle virus (TCV) via a SAG101-dependent pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20624951}.
Interaction partners:
- Disease resistance protein RPP5
- Probable disease resistance protein RPP1
- Cyclin-L1-1
- Protein EDS1
- Disease resistance protein ADR2
- Disease resistance protein RPP4
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Toll/interleukin-1 receptor-like protein
- UNC93-like protein 2
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Sequence:
MAEAFVSFGLEKLWDLLSRESERLQGIDGQLDGLKRQLRSLQSLLKDADAKKHGSDRVRNFLEDVKDLVFDAEDIIESYVLNKLSGKGKGVKKHVRRLACFLTDRHKVASDIEGITKRISEVIGEMQSFGIQQIIDGGRSLSLQERQRVQREIRQTYPDSSESDLVGVEQSVKELVGHLVENDVHQVVSIAGMGGIGKTTLARQVFHHDLVRRHFDGFAWVCVSQQFTQKHVWQRILQELQPHDGDILQMDEYALQRKLFQLLEAGRYLVVLDDVWKKEDWDVIKAVFPRKRGWKMLLTSRNEGVGIHADPTCLTFRASILNPEESWKLCERIVFPRRDETEVRLDEEMEAMGKEMVTHCGGLPLAVKALGGLLANKHTVPEWKRVFDNIGSQIVGGSWLDDNSLNSVYRILSLSYEDLPTHLKHCFLNLAHFPEDSEISTYSLFYYWAAEGIYDGSTIEDSGEYYLEELVRRNLVIADDNYLSWQSKYCQMHDMMREVCLSKAKEENFLQIIIDPTCTSTINAQSPSRSRRLSIHSGKAFHILGHKNKTKVRSLIVPRFEEDYWIRSASVFHNLTLLRVLDLSWVKFEGGKLPCSIGGLIHLRYLSLYEAKVSHLPSTMRNLKLLLYLNLRVDTEEPIHVPNVLKEMIQLRYLSLPLKMDDKTKLELGDLVNLEYLYGFSTQHSSVTDLLRMTKLRYLAVSLSERCNFETLSSSLRELRNLETLNFLFSLETYMVDYMGEFVLDHFIHLKQLGLAVRMSKIPDQHQFPPHLVHLFLIYCGMEEDPMPILEKLLHLKSVRLARKAFLGSRMVCSKGGFPQLCVIEISKESELEEWIVEEGSMPCLRTLTIDDCKKLKELPDGLKYITSLKELKIEGMKREWKEKLVPGGEDYYKVQHIPDVQFINCDQ
Protein: Promotilin [Cleaved into: Motilin; Motilin-associated peptide (MAP)] (P12872)
Organism: Homo sapiens (Human)
Function: Plays an important role in the regulation of interdigestive gastrointestinal motility and indirectly causes rhythmic contraction of duodenal and colonic smooth muscle.
Subcellular location: Secreted.
Interaction partners:
- Motilin receptor
- Gastrin
- Growth hormone secretagogue receptor type 1
- Neurotensin/neuromedin N
- Cholecystokinin
- Appetite-regulating hormone
- Pancreatic polypeptide prohormone
- Gastrin-releasing peptide
- Secretin
- G-protein coupled receptor 39
Sequence:
MVSRKAVAALLVVHVAAMLASQTEAFVPIFTYGELQRMQEKERNKGQKKSLSVWQRSGEEGPVDPAEPIREEENEMIKLTAPLEIGMRMNSRQLEKYPATLEGLLSEMLPQHAAK
Protein: p44-53 outer membrane protein (Q2GIV6)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MCFLSCKPHPSTAVIRSKLLLGSVMMSMAIVMAGNDVRAHDDVSALDTGGAGYFYVGLDYSPAFSKIRDFSIRESNGETKAVYPYLKDGKSVKLESHKFDWNTPDPRIGFKDNMLVAMEGSVGYGIGGARVELEIGYERFKTKGIRDSGSKEDEADTVYLLAKELAYDVVTGQTDKLTAALAKTSGKDIVQFAKAVGISHPTIDGKVCRTKKPSSGSNTYFGKYGEETDNGSSGEGVVAVCGAMSENTSTSKGSVTAQTLGDFVSVTLKGDGSKNWPTSTTKSSKVPAAVTNDNAKAVAGDLTKLTPEEKTIVAGLLAKTIEGGEVVEIRAVSSTSVMVNACYDLLSEGLGVVPYACVGLGGNFVGVVDGHITPKLAYRLKAGLSYQLSPEISAFAGGFYHRVVGDGVYDDLPAQLPTN
Protein: Lectin-D2 (PL-D2) (P83790)
Organism: Phytolacca americana (American pokeweed) (Phytolacca decandra)
Function: N-acetyl-D-glucosamine binding lectin. Shows no hemagglutinating activity towards rabbit erythrocytes and weak activity towards trypsin-treated erythrocytes. Has mitogenic activity towards human peripheral blood lymphocytes (HPBL).
Interaction partners:
Sequence:
APECGERASGKRCPNGKCCSQWGYCGTTDNYCGQGCQSQCDYWRCGRDFGGRLCEEDMCCSKYGWCGYSDDHCEDGCQSQCD
Protein: Bromo domain-containing protein (G5EEY5)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- SWI/SNF complex subunit SMARCC2
- SWI/SNF chromatin remodeling complex subunit swsn-7
- SWI/SNF Subunit INI1 DNA binding domain-containing protein
- HMG box domain-containing protein
- Actin-related protein 4
- PHD finger protein 10
- SWI/SNF chromatin remodeling complex core catalytic subunit swsn-4
- SWI/SNF chromatin-remodeling accessory subunit 2
- Bromo domain-containing protein
- ARID domain-containing protein
Sequence:
MSTKRKRAAEPDPEKDVASTSTASKKRKGRMTIAEKEKREFEMAKGNYVMAQIRKHRSSAGNNSVFESFLRLPPRRFEPEYYEQVKEPIDVTTIQHKLKIPEYLTYDQFNDDFMMFIKNNLTYYKDESEEHKDMMKIQELFEAATAKVKSGEYLDDAEDEEGDEDVEETVQEEEEPEESGTSSRDSTPMDLDHFMLCDLLGAVLEATDNTGRLLCPPFRVLQSREDFPLYYEKIAKPIDLKTIAQNGVNKKYSTMKELKDDLFLLFKNAQQFSGNGSDIFKDAEQLKTVVKEKIARLEEKGVHPMRRAKATRLVDALLTAVAVNENFSEDSEEDEETETNSEPMWKLYWTIRNAVHEKDRNVTLADNFLELPSKESYPDYYDEIKNPVSIFMINKRLKNGKYDLKSLVADLMQMYSNAFDYNLESSEVYISAEKLKALTISTCKQLVPSFDVSQYEPAPAQLTPVKPKATPHRARIKIEMPDTDSEDSRTPPPTHKRKSPKKPRENGSVPTPTFKGRKSTIPVDPNAAYMKQKAMMQGLWNVIHSYRVASNPGHWPAGAFIQLPSAKQYPEYYQIIQNPIDMKTIRMRIDGHQYPQVDAMINDCRVMFSNARDFNEPRSMIHMDAIQLEKAVLRAYEGMRNTSLGSSIPSTPHSSSSNLMKAMKLKTPKSEVRGRGKKNFSGSDDEESARINIQQHQRSMEDAIMQLPIEEQKMWRLFKSMKDVREEGTNRPLAVNFMRLPSKEEFPAYYDVIKKPMDMMRIKHKLENRQYVTLLDVVSDFMLMLSNACKFNETDSDIYKEAVSLQKALLEMKRELDTGDDAPRVQVELRTIFTSIFASLFSKKDEEGKCYSDHLTEFTEVLKANGVPSSEWPFTLDQIKMNIDKCRYRRLDKLQKDFFDLFERARELSKAGSSMYEAACTLQKSFIVERDTRCKDLIHSNAYCVIEKDIDEAIEKERSLKAKEEHDEEGGNKPAMVKRHESEVEMEDIEIDGTKYVAPCYAYVSRSDEKKTPLHIFRIERTFKDENGEKALQGHWVYRPEETLHLASRKFMKQEVFLTPFRDTVLAERLRGRCVVISLSTYTSKVITEYSEEDVYLCEYKYHGKPKYFAKLRTWPFTAEDEELEYTKRTKLMTPKRNLTAVDSDGNEGKDDVIVDGEEEEDEEDRARLEVSLDMERFELEASKDEESGKTYFQQIRSETGKFFWLGQCVLVFNNMKPLCDVMKINKIWREKDGSEWFSGCWFARPSETIHDEGRLFFKNEVIAVYRNDETRKLCEIQRVCDVMPAKLYIKQRQTEVSECDVFVCETMVNGSADTPDDCSLFGFQSIVDEFSDAQTMNLDYGKAMRKMKAHKLHVSIPNEEVLFYKQPIKMDKELSPLLKGEGVMPLDHLDEMMDDDTDGSESVSSSIHPKILKEGSPPATVQSQTSSVSTPPQHPSISAEMPIMTPKAVKSKSGYILFSAEVRKRIMHENPDAGFGEVSKIVGIEWKKLSEEQKKHYEMRAEVVAVEKAKQDAIKASQAMTLLPGQVRIYQCKWAACDSQYDTESALLEHVIQHHTSQIIMDSDQQFVCMWMTCLRNRKDGKPFPSLPRLHRHIKEKHMPTAAKNIYSNQLGKNFFKSIPNQGDTPGCRIVSAPYGQLPTAPSNGGIPPQQQHQQQQHHGNGMNGNMQQGAPQVINRHPVSQQMHHQHPQHMQQHHDHHPHQQHYQQGGQPHPQMQMGPPQNGMFQQGSSSSQQYHQAPPQQMIQQQHQQPGPPPQQQQPQMQPIVVTDVGRTVVRAVVPAFVAPPNQIHSRRVLHSEAYLKYIESLAQNRQKSVSRWERTLGATARNTQPAGNARAPSHWIRRIENGRPVAREEDVTKALWKLRDELLKSTCSLVMDRPTQ
Protein: Serine hydroxymethyltransferase (EC 2.1.2.1) (Q9W457)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Bifunctional purine biosynthesis protein ATIC
- Trifunctional purine biosynthetic protein adenosine-3
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial
- Aminomethyltransferase
- Glycine cleavage system P protein
- C-1-tetrahydrofolate synthase, cytoplasmic
- Sarcosine dehydrogenase
- Phosphoserine phosphatase
- Thymidylate synthase
- Dihydrofolate reductase
Sequence:
MQRARSTLTQKLRFCLSRDLNTKVGNPVNFETGKLSGALTRIAAKKQPSPTPFLPAIRRYSDSKQSTLKNMADQKLLQTPLAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGRELFNLDDEKWGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGFFTPTKKISATSIFFESMPYKVNPETGIIDYDKLAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPRAGVIFFRKGVRSTKANGDKVLYDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLISRGYQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGDKSAMNPSGIRLGTPALTTRGLAEQDIEQVVAFIDAALKVGVQAAKLAGSPKITDYHKTLAENVELKAQVDEIRKNVAQFSRKFPLPGLETL
Protein: Coiled-coil and C2 domain-containing protein 1A (Five prime repressor element under dual repression-binding protein 1) (FRE under dual repression-binding protein 1) (Freud-1) (Q66HA5)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor that binds specifically to the DRE (dual repressor element) and represses 5-HT1A gene transcription though this element. Mediates HDAC-independent repression of HTR1A promoter. CAMK2G inhibits CC2D1a-induced repression of the HTR1A. May play a role in the altered regulation of 5-HT1A receptors associated with anxiety and major depression. Performs essential function in controlling functional maturation of synapses (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12917378}. Nucleus {ECO:0000269|PubMed:12917378}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6P1N0}.
Interaction partners:
- Deformed epidermal autoregulatory factor 1 homolog
Sequence:
MHKRNGPQAPPGRGAVTARQLGLLVDFSPDGLMIPEDGVNDEELEAEFLALVGGQPQALEKLKGKGPLPMEAIEKMARLCMRDLDEDEEGTDEDVEADEDLLAELNEVLGEERKAVEPAMPVVQPKPSSPNPGIEATLQERLILYQSAVESARQAGDSAKMRRYDRGLKTLENLLVSAKKGNTINEADIPPPVASGKGPAIGHSHTHTTSHLAPVSPPAPEPSVTLEAPSTTAQTSAKPQLSPDPCSPLARLQSLQHEYKVAALRAKHQDDTATAARYLRVSKSFDPVLEALSRGELVDLSRLPPPPDQLSPEPPLPAAQPVTPASTLTRPEVPQPPKNLLEALEQRMERYHVAAAQAKAKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPPGFPPIQGLESAEPSQQSLVGVLETAMKLANHEEGSDEEEEETPKKNTPAASTAQPKASPSRAPPSGPAPAGKAASKGTSTRAQQQLAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDIAKVPPAPVNKDDFVLVQRPGPGMSQEAVRRYGELTKLLRQQHEMCLNHSTQFTHLGNIAETIKFEKLAEDCKRSMDTLKQAFARSLPTPAARFEQRTFSVIKIFPDLSNNDMLLFIVKGINLPTPPGLSPSDLDAFVRFDFPYPNVEEAQKDKTSVIKSTDSPEFKEQFKLCINRGHRGFRRAIQTKGIKFEVVHKGGLFKTDRVLGTAQLKLDTLETACEVHEILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVIDHIPAAVPTVTGPKAKVPLIPASSKEAGNRSSRPLHSLSVLAFDQERLERKILALRQARRPVPPEVAQQYQDVVQRSQWQRAQLEQGGAALRREYASHLERQLHFYTEAARRLGYDGSREAAKEALYRRNLVESELQRLRR
Protein: Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB) (P56767)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00482}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00482}.
Interaction partners:
- Photosystem I reaction center subunit XI, chloroplastic
- Photosystem I reaction center subunit II-2, chloroplastic
- Photosystem I reaction center subunit psaK, chloroplastic
- Photosystem I reaction center subunit IV A, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I reaction center subunit IX
- Photosystem I reaction center subunit VIII
- Photosystem I reaction center subunit III, chloroplastic
- Photosystem I iron-sulfur center
- Photosystem I reaction center subunit V, chloroplastic
Sequence:
MALRFPRFSQGLAQDPTTRRIWFGIATAHDFESHDDITEERLYQNIFASHFGQLAIIFLWTSGNLFHVAWQGNFETWVQDPLHVRPIAHAIWDPHFGQPAVEAFTRGGALGPVNIAYSGVYQWWYTIGLRTNEDLYTGALFLLFLSALSLIGGWLHLQPKWKPRVSWFKNAESRLNHHLSGLFGVSSLAWTGHLVHVAIPASRGEYVRWNNFLNVLPHPQGLGPLFTGQWNLYAQNPDSSSHLFGTSQGSGTAILTLLGGFHPQTQSLWLTDMAHHHLAIAILFLIAGHMYRTNFGIGHSIKDLLEAHIPPGGRLGRGHKGLYDTINNSIHFQLGLALASLGVITSLVAQHMYSLPAYAFIAQDFTTQAALYTHHQYIAGFIMTGAFAHGAIFFIRDYNPEQNEDNVLARMLDHKEAIISHLSWASLFLGFHTLGLYVHNDVMLAFGTPEKQILIEPIFAQWIQSAHGKTSYGFDVLLSSTSGPAFNAGRSIWLPGWLNAINENSNSLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDAFYLAVFWMLNTIGWVTFYWHWKHITLWQGNVSQFNESSTYLMGWLRDYLWLNSSQLINGYNPFGMNSLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLAWAHERTPLANLIRWKDKPVALSIVQARLVGLAHFSVGYIFTYAAFLIASTSGKFG
Protein: 3,5-dihydroxyphenylacetyl-CoA synthase (EC 2.3.1.246) (3,5-dihydroxyphenylacetyl-CoA synthase polyketide synthase type III) (Q939X3)
Organism: Amycolatopsis balhimycina
Function: Involved in the biosynthesis of the nonproteinogenic amino acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg) responsible of the production of balhimycin antibiotic. Catalyzes the Claisen condensation of four molecules of malonyl-CoA to yield 3,5-dihydroxyphenylacetyl-CoA (DPA-CoA) and three free coenzyme A (CoA). DpgA requires the presence of the dehydratases DpgB and DpgD to facilitate the aromatization of the DPA-S-DgpA or DPA-S-CoA intermediate.
Interaction partners:
Sequence:
MGVDVSMTTSIEPAEDLSVLSGLTEITRFAGVGTAVSASSYSQSEVLDILDVEDPKIRSVFLNSAIDRRFLTLPPESPGGGRVSEPQGDLLDKHKELAVDMGCRALEACLKSAGATLSDLRHLCCVTSTGFLTPGLSALIIRELGIDPHCSRSDIVGMGCNAGLNALNVVAGWSAAHPGELGVVLCSEACSAAYALDGTMRTAVVNSLFGDGSAALAVISGDGRVPGPRVLKFASYIITDALDAMRYDWDRDQDRFSFFLDPQIPYVVGAHAEIVADRLLSGTGLRRSDIGHWLVHSGGKKVIDSVVVNLGLSRHDVRHTTGVLRDYGNLSSGSFLFSYERLAEEGVTRPGDYGVLMTMGPGSTIEMALIQW
Protein: Cycloartenol synthase (EC 5.4.99.8) (Q8W3Z4)
Organism: Betula platyphylla (Asian white birch)
Function: Oxidosqualene cyclase converting oxidosqualene to cycloartenol.
Interaction partners:
Sequence:
MWKLKIGAETARGDGGGGGGSETWLRSLNNHLGRQIWEFHPELGTQEELQQIDDARRRFWERRFERRHSSDLLMRIQFAKENPSSANIPQVKIKDTEEVREEAVGMTLRRAINFYSTIQADDGHWPGDYGGPMFLIPGLVITLSITGTLNAFLSKEHQCEICRYLYNHQNEDGGWGLHIEGPSTMFGTALNYITLRLLGEPEDGMGAVEKARKWILDHGGATAITSWGKMWLSVLGVYEWSGNNPLPPEVWLCPYLLPCHPGRMWCHCRMVYLPMSYLYGKRFVGPITSTIQSLRKELYTVPYHEIDWNKARNDCAKEDLYYPHPLVQDILWASLYYAYEPIFMYWPAKRLREKALDTVMQHIHYEDENTRYICIGPVNKVLNMLCCWAEDPNSEAFKLHLPRILDYLWIAEDGMKMQGYNGSQLWDTTFAVQAIISTNIAEEYGQTLRKAHEYIKDSQVLEDCPGDLNFWYRHISKGAWPFSTADHGWPISDCTAEGLKAVILLSQFPSETVGKSVDVKRLYDAVHVILSLQNTDGGFATYELTRSYHWLELINPAETFGDIVIDYPYVECTSAAIQALTLFKKLHPGHRREEIENCIAKAAEFIENIQASDGSWYGSWGVCFTYAGWFGIKGLVAAGRTYKNCSSIHKACDYLLSKELASGGWGESYLSCQDKVYTNLKDNRPHIVNTGWAMLALIDAGQAERDPTPLHRAARILINSQMENGDFPQEEIMGVFNKNCMISYSAYRNIFPIWALGEYRCRVLKAL
Protein: Ras-related protein Rab-39B (Q8BHC1)
Organism: Mus musculus (Mouse)
Function: Small GTPases Rab involved in autophagy. The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). May be involved in vesicular trafficking. Plays a role in synapse formation. May regulate the homeostasis of SNCA/alpha-synuclein. Together with PICK1 proposed to ensure selectively GRIA2 exit from the endoplasmic reticulum to the Golgi and to regulate AMPAR compostion at the post-synapses and thus synaptic transmission.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96DA2}; Lipid-anchor {ECO:0000250|UniProtKB:Q96DA2}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96DA2}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q96DA2}; Lipid-anchor {ECO:0000250|UniProtKB:Q96DA2}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96DA2}. Golgi apparatus {ECO:0000269|PubMed:20159109}. Note=Partial colocalization with markers that cycle from the cell surface to the trans-Golgi network. {ECO:0000269|PubMed:20159109}.
Interaction partners:
- Guanine nucleotide exchange protein SMCR8
- WD repeat-containing protein 41
- Guanine nucleotide exchange factor C9orf72 homolog
- Sequestosome-1
- Ras-related protein Rab-8A
- Rab GDP dissociation inhibitor alpha
- Geranylgeranyl transferase type-2 subunit alpha
- Rab GDP dissociation inhibitor beta
Sequence:
MEAIWLYQFRLIVIGDSTVGKSCLIRRFTEGRFAQVSDPTVGVDFFSRLVEIEPGKRIKLQIWDTAGQERFRSITRAYYRNSVGGLLLFDITNRRSFQNVHEWLEETKVHVQPYQIVFVLVGHKCDLDTQRQVTRHEAEKLAAAYGMKYIETSARDAINVEKAFTDLTRDIYELVKRGEITIQEGWEGVKSGFVPNVVHSSEEVIKSERRCLC
Protein: Hexosyltransferase (EC 2.4.1.-) (Q584H8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}.
Interaction partners:
Sequence:
MSPLKMRPTQARRRPRTADIAVILLLVMSLLIICCNLHRIHVVSTFLDENQAGVSQPIDEDEYLMFVPSNVAAVWKAQRFLAVLGIPSVDNSERSRRRDLQRQTCWKYSGVATRSNNFSGSLLPLYLLAPHQSNSYLISHSLKEEAARTHDIITLPTNDVSPSTRKKIGENGNWGIEAEVAMSRKTYLWLRFALYMFPNVSYIVKGDDDIFIRVPKYLADLRVMPRHGLYMGRYNYYNRIWRRNQLTYVNGYCITLSRDTAQAIISYKPLERLVNMPFSMWDYFDFLDLGMFYEDVMVGMILREKVVYRNLISVEMGRCHFHNAGKFGVKKSVRNMSVVIHHIQEADYEMLMDYFPEGVIPPAPSKLMWLNSNWAAMQCEFRLGRKREILPSFPFWRKRA
Protein: Calcium permeable stress-gated cation channel 1 (AtCSC1) (Hyperosmolality-gated Ca2+ permeable channel 1.2) (AtOSCA1.2) (Q5XEZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as an osmosensitive calcium-permeable cation channel. Specifically conducts cations including Ca(2+), K(+) and Na(+) in vitro. Inactivation or closure of the channel is calcium-dependent. Mechanosensitive ion channel that converts mechanical stimuli into a flow of ions.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein MID1-COMPLEMENTING ACTIVITY 2
- Protein MID1-COMPLEMENTING ACTIVITY 1
- Mechanosensitive ion channel protein 10
Sequence:
MATLQDIGVSAGINILSAFVFFIIFAVLRLQPFNDRVYFSKWYLKGLRSSPARGGAFAQRFVNLDFRSYMKFLNWMPEALKMPEPELIDHAGLDSVVYLRIYWLGLKIFTPIAVLAWAVLVPVNWTNNTLEMAKQLRNVTSSDIDKLSVSNIPEYSMRFWTHIVMAYAFTIWTCYVLMKEYETIANMRLQFVASEARRPDQFTVLVRNVPPDADESVSELVEHFFLVNHPDHYLTHQVVCNANKLADLVKKKKKLQNWLDYYQLKYARNNSQRIMVKLGFLGLWGQKVDAIEHYIAEIDKISKEISKEREEVVNDPKAIMPAAFVSFKTRWAAAVCAQTQQTRNPTQWLTEWAPEPRDVFWSNLAIPYVSLTVRRLIMHVAFFFLTFFFIVPIAFVQSLATIEGIVKAAPFLKFIVDDKFMKSVIQGFLPGIALKLFLAFLPSILMIMSKFEGFTSISSLERRAAFRYYIFNLVNVFLASVIAGAAFEQLNSFLNQSANQIPKTIGVAIPMKATFFITYIMVDGWAGVAGEILMLKPLIMFHLKNAFLVKTDKDREEAMDPGSIGFNTGEPRIQLYFLLGLVYAPVTPMLLPFILVFFALAYIVYRHQIINVYNQEYESAAAFWPDVHGRVIAALVISQLLLMGLLGTKHAALAAPFLIALPVLTIGFHHFCKGRYEPAFIRYPLQEAMMKDTLETAREPNLNLKGYLQNAYVHPVFKGDEDDYDIDDKLGKFEDEAIIVPTKRQSRRNTPAPSIISGDDSPSLPFSGKLV
Protein: Elongation factor Tu GTP binding domain containing 2 (A0A8I6ASA3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDEDEDEDDVGEHDDDHPGMEVVLHEDKKYYPTAEEVYGPEVETIVQEEDTQPLTEPIIKPVKTKKFTLMEQTLPVTVYEMDFLADLMDNSELIRNVTLCGHLHHGKTCFVDCLIEQTHPEIRKRYDQDLCYTDILFTEQERS
Protein: Klra18 protein (Lectin-related NK cell receptor LY49R) (Q9JHV4)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MTEQKDTFSAVRFHKSSGLQNEMRLKETRKPRKAGLRVCSVPWQFIVIALGILISLRLVIVAVLMTNIFQYGQQKHELQEFLKHHNNCSIMQSDINLKDELLKNKSIECNLLESINRDQNRLYNKTKTVLDSLQHTGRGVKVYWFCYGMKCYYFIMDRKPWSRCKQSCQNSSLTLLKIDNEDELKFLQLVVPSDSCWIGLSYDNKKKDWAWIDNRPSKLALNTTKYNIRDGGCMFLSKTRLDNNYCDQSFICICGKRLDKFPH
Protein: Lipolysis-stimulated lipoprotein receptor (A0A0R4IPT5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Endomembrane system {ECO:0000256|ARBA:ARBA00046288}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00046288}.
Interaction partners:
Sequence:
MSLGVIFTLLLFTGVTTGINVICTYPRYVVIMFQPVTLRCDFTTTSTTPPLITWKYKSYCRDPIQAALNPSSADNAIAQSNPNYNPNIECADSARTVRIVASKQTAVTLGKEYQGRQISITNNADLSIVQTAWGDSGVYVCSAASAQDLSGNGECYTELIVLERKSNTTDLLPGIDLLIMEDWLLVVLVVLGFLLLLLLIGICWCQCCPHTCCCYVRCPCCPERCCCPRALYEAGKMVKSGIPSQYAATAYAQSMYGQPAYGVGAAMPGIPMMPMQMGVGGPPSNGYGRDYDGASSIGQGSQVPLLQEHDAGGNRSGYRVQADQDGNPTRVLYYMEREVANLDPSRPGIAPGKYSRLDGMSEVSSLHDGPDSRNRGRARPPQLTTVYDDVDENMSTISSVSQHMRRDEPRRGADSRGRARSMENLDDISRGYRDRDDYPPARRDGGPRGGRRGSDDEWSSSGRGYDPVDDRRRRDYSPDNRPRHGDSFRGAGFQGRRTRSRDDLMDLVRDPGRGGRDEYDDSFLREAMEKKKLGEQQRGRSRERLDSESDRSDRYRGHHSGPPPLPLVPASGNPDRRGNHSNFPPPPPPYTEDTDSLPSSKKSNLKKNGAVSRESLVV
Protein: Proton-coupled amino acid transporter-like protein acs (Protein arcus) (Q9W056)
Organism: Drosophila melanogaster (Fruit fly)
Function: Amino acid transporter which has pH-dependent electrogenic transport activity for alanine, glycine and proline. Plays a role in positive regulation of growth by directly or indirectly modulating the effects of the TOR signaling pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22574197}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:22574197}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:22574197}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000269|PubMed:37636057}; Multi-pass membrane protein {ECO:0000255}. Note=Partially colocalizes with the late endosomal and lysosomal marker Lamp1 (PubMed:22574197). Localizes to the basal labyrinth in enterocytes of the midgut (PubMed:37636057). {ECO:0000269|PubMed:22574197, ECO:0000269|PubMed:37636057}.
Interaction partners:
Sequence:
MNDDIKTVTVYPTTLELTTPTKSANGSNDDYDPHQHRELKNPTTNFQTFAHFLKASVGTGVLAMPSAFAHAGYVNGTLLTLIIGSLALYCLHILIKCMYILCKRQRVPYVSFSQAMNLGLKQGPPWLRCLAPIAVPFVDGFLAFYHFGICCVYVVFIAESIKQLVDEYLVVWDVRIHMCIIIVPLLLIYSIKNLKLLAPFSSAANLLLLVGFGIILYYIFEELPPLSERDPFVAAGKLPTFFGTVLFALEAVGVILAIEENMATPKSFVGPCGILNSGMSIVLGLYVLLGFFGYWKYGNESEGSITLNIPQSEIPAQVVKVFFAITTWISYALQGYVTAHILWDKYLAKRFKETRQTFYELIFRAIIVLLTFGCAVAIPDLSVFLSLVGSFCLSILGLIFPVLLQICVQYTEGYGPFRIKLIINLLLLCFGIFGGVVGTYVSILDIIAVYK
Protein: Fibroblast growth factor receptor 4 (FGFR-4) (EC 2.7.10.1) (CD antigen CD334) (P22455)
Organism: Homo sapiens (Human)
Function: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Mutations that lead to constitutive kinase activation or impair normal FGFR4 inactivation lead to aberrant signaling.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Endosome. Endoplasmic reticulum. Note=Internalized from the cell membrane to recycling endosomes, and from there back to the cell membrane.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
Interaction partners:
- Fibroblast growth factor 1
- Fibroblast growth factor 19
- Beta-klotho
- Fibroblast growth factor 2
- Fibroblast growth factor 4
- Fibroblast growth factor 6
- Fibroblast growth factor 9
- Fibroblast growth factor 8
- Fibroblast growth factor 5
- Fibroblast growth factor 18
Sequence:
MRLLLALLGVLLSVPGPPVLSLEASEEVELEPCLAPSLEQQEQELTVALGQPVRLCCGRAERGGHWYKEGSRLAPAGRVRGWRGRLEIASFLPEDAGRYLCLARGSMIVLQNLTLITGDSLTSSNDDEDPKSHRDPSNRHSYPQQAPYWTHPQRMEKKLHAVPAGNTVKFRCPAAGNPTPTIRWLKDGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENAVGSIRYNYLLDVLERSPHRPILQAGLPANTTAVVGSDVELLCKVYSDAQPHIQWLKHIVINGSSFGADGFPYVQVLKTADINSSEVEVLYLRNVSAEDAGEYTCLAGNSIGLSYQSAWLTVLPEEDPTWTAAAPEARYTDIILYASGSLALAVLLLLAGLYRGQALHGRHPRPPATVQKLSRFPLARQFSLESGSSGKSSSSLVRGVRLSSSGPALLAGLVSLDLPLDPLWEFPRDRLVLGKPLGEGCFGQVVRAEAFGMDPARPDQASTVAVKMLKDNASDKDLADLVSEMEVMKLIGRHKNIINLLGVCTQEGPLYVIVECAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPVLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDNVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMDRPPHCPPELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEYLDLRLTFGPYSPSGGDASSTCSSSDSVFSHDPLPLGSSSFPFGSGVQT
Protein: Endolysin (H2D0G4)
Organism: Salmonella phage SPN1S
Interaction partners:
Sequence:
MDINQFRRASGINEQLAARWFPHITTAMNEFGITKPDDQAMFIAQVGHESGGFTRLQENFNYSVNGLSGFIRAGRITPDQANALGRKTYEKSLPLERQRAIANLVYSKRMGNNGPGDGWNYRGRGLIQITGLNNYRDCGNGLKVDLVAQPELLAQDEYAARSAAWFFSSKGCMKYTGDLVRVTQIINGGQNGIDDRRTRYAAARKVLAL