wanglab/gogpt-training-data huggingface dataset:
Protein: EF-hand domain-containing protein (A0A060XEV5)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- Troponin C, skeletal muscle
- Troponin C, skeletal muscle
- Troponin C, skeletal muscle
- Troponin T type 3a
- Troponin I, fast skeletal muscle
- Troponin I, fast skeletal muscle
- Troponin I, fast skeletal muscle
- EF-hand domain-containing protein
Sequence:
MFEQSQIQEYKEAFTIIDQNRDGIISKDDLRDVLATMGQLNVKNEELEAMIKEASGPINFTVFLTMFGEKLKGADPEDVIVSAFKVLDPEATGFIKKEFIEELLTTQCDRFTAEEMSNLWAAFPPDVAGNVDYKQICYVITHGEEKEDE
Protein: IMP U3 small nucleolar ribonucleoprotein 4 (B9A008)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MITTSRDPSSRLKMFAKELKLVFPGAQRMNRGRHEVGALVRACKANGVTDLLVVHEHRGTPVGLIVSHLPFGPTAYFTLCNVVMRHDIPDLGTMSEAKPHLITHGFSSRLGKRVSDILRYLFPVPKDDSHRVITFANQDDYISFRHHVYKKTDHRNVELTEVGPRFELKLYM
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8IBX1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MASQSGGGSPQDAKHVLDEFGQQVHKEVKKEAERRSKGELKGLLTSAKLSGGEIAGTTDPCSSDYTKHFEANSNRYPCGNTNVDRFPDNDGAECDNSKIKGNKGKEDNSEGACAPYRRLSLCNKNFQNNNNDHSSNAKHDLLLDVCMAANYEAQSLITYHDKHELTNVGSQICTVLARSFADIGDIVRGKDLYLGKKKKKKTETERERDQLEQKLKGIFKKIYEGLTGGVKDHYQDTDNYYELREDWWALNRDQVWKAITCKADNSNRYFRATCDSADGKGSSVARNKCRCKDEEGKNETNEVPTYFDYVPQYLRWFEEWAEDFCRKKKKYVDIVKTYCRGKYQGEERYCSRNGFDCEKTVNARGKVRMGKGCTDCFFACNPYVDWIDNQRKQFLKQRNKYADEIKIYTEGASGGSRQRRNVRSNYDNGYEKKFYKELKNRYGSVETFLVLLNNEKACTAVDDDKGGKIDFKEVNTGGAASGGTSGTNVESQGTFYRSKYCQPCPLCGVERKGGSGWEEKDKIEKCKSINLYKPRDDKVGTTIKILKSGEEEKDIETKLKAFCDNKDSGNSDPSLYDPWQCYQIGELTKDQKEGGEDDLDYEADVQTGGGLCILKKEKKTDNDPDEIQKTFNNFFYYWVAHMLKDSIYWRMKKLERCLQNGNKKCGNQKCEKPCDCFQRWVQQKETEWGKIKTHFNTQNIGALTGCNPIVTLEGVLKLQFLKDESTEDSEENSKNSLDSEELKHLKHLSEMLQGTGVDGLTCSDSGTEQKTLMDKLIDYEEGIATECKKCDEPKPEGAAGGRSDGPPGSPPRPAEKDEDHHSDESDEEEDEEHTEQGEEKTEGKTEEQPEEVKEHTETPEDEVNPCKIVETLFTSDDNNALNEACKQKYQYGKEKFPNWKCIPSGDNSTTSSEGGDRGGQSRAKRAAPRESTTSSGDTTGGSICVPPRRRKLYIKKIVDWAESQSKTLTSVNGDGNGSQEVVSVNGASESGSQGSRSDSSSSSSSDSSQGTTSATSQSPNGDLLTAFVESAAIETFFLWDRYKKIKDIEEKEIKEKNEIYGIYTSSVDEKPQNKLNGGDIPNDFLRLMFYTLGDYRDICIGVKEDVIKALEASSDKNIETIKKAIDEILSKQSRNNQQSGQKSENPRDTWWKTNGEHIWNAMVCALTYNEDTSGAKGKQPQQDQSLKDKLIDKKTGKPEGKYHYEKVTLENSDTQAISNDTINNPKLKDFVEIPPFFRWLHEWGSDFCGKRARMLKNVKHNCRNIDNPGHQYCSGDGYDCEKIKPENYKNISDLDCRDCYKQCRKYRKWIEKKVEEFHKQEKKYKGEHGKLRNDNCSGNDNKEYCEQIKQKTSAADFLAALKHCKNDQIDGEQGNQEDKKNNEIKFEEPLKTFGPLEYCKTCPFNGVNCTVRRGTNGCIENGQIWKKVFEGISGNGENSTITVDMIDRRGPFIEKYLGDSNDLFKTSKLFKGIRKQNWTCKFNKDKNMDVCHLTNFKDNIDLNEYTTFKVLLIYWLEDFLYGYYLLKKKKKIYLCTQNKEQTCSEESKNDCACVKEWIGKKRAEWKTIRDRFNDQYKSENSGDTFPVRSFLEGLIPQIPVADVQGNVIKLSKFGNSCGCSFSAHSTNGKDDAIDCMIKKLEEKVTSCLSSTSGDNLAQCENSTPLEDDDEPFEEEENPENMRPGFCPPPEEKTEIEGTDKKCEEAPTTPPEPAPPAKSGEGTEELPSAPEPPQDKALPKPAAQPKDKKRPKRQPQNPWEHPIVIPSLATSTLMWTVGIGFATFTYFFLKKKTKSSVGNLFQILQIPKGDYDIPTLKSSNRYIPYASERYKGKTYIYMEGDSSGDEKYAFMSDTTDVTSSESEYEEMDINDIYAPRAPKYKTLIEVILEPSKRDTQNDIPSGDINSDIPNTPSDTPSPITDEEWNTLKDDFISNMLQNEQEDIPQPDVSKELPLNTHPTPSHDTLDQKPFIMSIHDRNLLNGEEYSYDIINNIGNNDLYSGFDPKSGDNVSYSGTIGSISDKTSPYSGIDLINDSLNSGNHIDIYDEILKRKENELFGTNHVKHISTHSVAKLTNSDPIECQLNLFHKWLDRHRDMCEKFSNNKEELLDKLKEQWENKTHSGNKHSDIPSGKLSDTPSDNNIHSDIHPSDIPSGKQSDIPSDNNIHSDIPYVLNSDVSIQIDMDNPNQVDDNTYLDTYPDKSTMDTIMDDLEKYNEPYYDIYYDVNDHDASNVDSNNMDVPSKVKIEMSVKNTQMMEGKYPIGDVWDI
Protein: Probable NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial (EC 7.1.1.2) (Complex I-20kD) (CI-20kD) (NADH-ubiquinone oxidoreductase 20 kDa subunit) (Q94360)
Organism: Caenorhabditis elegans
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Probable NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH-ubiquinone oxidoreductase chain 5
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Probable NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- Probable NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 8
- NADH dehydrogenase iron-sulfur protein 3
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
Sequence:
MLSALRTAGAVGTRRLASTQAIASNSEAPKGIATTGTPFLNPSSKAEYALARLDDVLNLAQRGSIWPLTFGLACCAVEMMHFAAPRYDMDRYGVVFRASPRQADLIFVAGTVTNKMAPALRRIYDQMPEAKWVISMGSCANGGGYYHYAYSVLRGCDRVIPVDIYVPGCPPTAEALLYGVLQLQKKIKRKREAQLWYRR
Protein: Tudor domain-containing protein 7 (PCTAIRE2-binding protein) (Tudor repeat associator with PCTAIRE-2) (Trap) (Q8NHU6)
Organism: Homo sapiens (Human)
Function: Component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. Required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. Also required during spermatogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21436445}. Note=Localizes to cytoplasmic RNA granules. Present in chromatoid body (CB) of spermatids (mammalian counterpart of germplasm, pole plasm or polar granules in Drosophila germ cells), also named processing bodies (P-bodies) in somatic cells. Detected in the multilobular cytoplasmic CBs (also called intermitochondrial cementin) in pachytene spermatocytes and as a single perinuclear CB in haploid round spermatids (By similarity). {ECO:0000250}.
Interaction partners:
- Cyclin-dependent kinase 17
- Coiled-coil domain-containing protein 180
- CDK5 and ABL1 enzyme substrate 1
- Piwi-like protein 1
- Piwi-like protein 2
- GA-binding protein subunit beta-1
- ATP-dependent RNA helicase TDRD9
- Cyclin-dependent kinase 18
- Dead end protein homolog 1
- Transforming acidic coiled-coil-containing protein 1
Sequence:
MLEGDLVSKMLRAVLQSHKNGVALPRLQGEYRSLTGDWIPFKQLGFPTLEAYLRSVPAVVRIETSRSGEITCYAMACTETARIAQLVARQRSSKRKTGRQVNCQMRVKKTMPFFLEGKPKATLRQPGFASNFSVGKKPNPAPLRDKGNSVGVKPDAEMSPYMLHTTLGNEAFKDIPVQRHVTMSTNNRFSPKASLQPPLQMHLSRTSTKEMSDNLNQTVEKPNVKPPASYTYKMDEVQNRIKEILNKHNNGIWISKLPHFYKELYKEDLNQGILQQFEHWPHICTVEKPCSGGQDLLLYPAKRKQLLRSELDTEKVPLSPLPGPKQTPPLKGCPTVMAGDFKEKVADLLVKYTSGLWASALPKAFEEMYKVKFPEDALKNLASLSDVCSIDYISGNPQKAILYAKLPLPTDKIQKDAGQAHGDNDIKAMVEQEYLQVEESIAESANTFMEDITVPPLMIPTEASPSVLVVELSNTNEVVIRYVGKDYSAAQELMEDEMKEYYSKNPKITPVQAVNVGQLLAVNAEEDAWLRAQVISTEENKIKVCYVDYGFSENVEKSKAYKLNPKFCSLSFQATKCKLAGLEVLSDDPDLVKVVESLTCGKIFAVEILDKADIPLVVLYDTSGEDDININATCLKAICDKSLEVHLQVDAMYTNVKVTNICSDGTLYCQVPCKGLNKLSDLLRKIEDYFHCKHMTSECFVSLPFCGKICLFHCKGKWLRVEITNVHSSRALDVQFLDSGTVTSVKVSELREIPPRFLQEMIAIPPQAIKCCLADLPQSIGMWTPDAVLWLRDSVLNCSDCSIKVTKVDETRGIAHVYLFTPKNFPDPHRSINRQITNADLWKHQKDVFLSAISSGADSPNSKNGNMPMSGNTGENFRKNLTDVIKKSMVDHTSAFSTEELPPPVHLSKPGEHMDVYVPVACHPGYFVIQPWQEIHKLEVLMEEMILYYSVSEERHIAVEKDQVYAAKVENKWHRVLLKGILTNGLVSVYELDYGKHELVNIRKVQPLVDMFRKLPFQAVTAQLAGVKCNQWSEEASMVFRNHVEKKPLVALVQTVIENANPWDRKVVVYLVDTSLPDTDTWIHDFMSEYLIELSKVN
Protein: Taste receptor type 2 (Q9JKT6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004424}.
Interaction partners:
Sequence:
MEPVIHVFATLLIHVEFIFGNLSNGLIVLSNFWDWVVKRKLSTIDKILLTLAISRITLIWEMYACFKIVYGSSSFIFGMKLQILYFAWILSSHFSLWFATALSIFYLLRIANCSWKIFLYLKWRLKQVIVGMLLASLVFLPGILMQRTLEERPYQYGGNTSEDSMETDFAKFTELILFNMTIFSVIPFSLALISFLLLIFSLWKHLQKMQLSSRGHGDPSTKAHRNALRIMVSFLLLYTSYFLSLLISWIAQKHHSKLVDIIGIITELMYPSVHSFILILGNSKLKQTSLWILSHLKCRLKGENILTPSGKPIN
Protein: Flavodoxin/ferredoxin--NADP reductase (EC 1.18.1.2) (EC 1.19.1.1) (Ferredoxin (flavodoxin):NADP(+) oxidoreductase) (Ferredoxin--NADP reductase) (FNR) (Flavodoxin--NADP reductase) (FLDR) (Methyl viologen resistance protein A) (dA1) (P28861)
Organism: Escherichia coli (strain K12)
Function: Transports electrons between flavodoxin or ferredoxin and NADPH. Reduces flavodoxin 1, flavodoxin 2 and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner. Required for the activation of several enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide reductase and cobalamin-dependent methionine synthase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7961651}.
Interaction partners:
- 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin subunit
- 3-phenylpropionate/cinnamic acid dioxygenase subunit beta
- 3-phenylpropionate/cinnamic acid dioxygenase subunit alpha
- Uncharacterized ferredoxin-like protein YfaE
- Fructose-1,6-bisphosphatase 1 class 2
Sequence:
MADWVTGKVTKVQNWTDALFSLTVHAPVLPFTAGQFTKLGLEIDGERVQRAYSYVNSPDNPDLEFYLVTVPDGKLSPRLAALKPGDEVQVVSEAAGFFVLDEVPHCETLWMLATGTAIGPYLSILQLGKDLDRFKNLVLVHAARYAADLSYLPLMQELEKRYEGKLRIQTVVSRETAAGSLTGRIPALIESGELESTIGLPMNKETSHVMLCGNPQMVRDTQQLLKETRQMTKHLRRRPGHMTAEHYW
Protein: Chromo domain-containing protein cec-4 (Q19972)
Organism: Caenorhabditis elegans
Function: Chromatin anchor protein which binds to methylated lysine residues on histone H3, thereby recruiting heterochromatin to the nuclear periphery, especially in embryonic cells, with a lesser role in differentiated cells. May be required for the correct positioning of chromatin and nucleoli in embryos.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:26607792}. Membrane {ECO:0000305|PubMed:26607792}; Peripheral membrane protein {ECO:0000305|PubMed:26607792}.
Interaction partners:
- Histone-lysine N-methyltransferase set-25
- Chromo domain-containing protein.
- LEM protein 2
- Chromobox protein homolog hpl-1
- Protein lin-61
- Chromo domain-containing protein cec-3
- MADF domain-containing protein
Sequence:
MAKKTVEGEHGTPKTNFTKKETSKNHDDFKKIIGHKVVEEHYVEYEVELTSGKTITATEFDFKGDDSLLSTYKKKVTKQSDDSSGEYAVERVLAHRKVKGSPLYLVQWKGYPHPVWNSEMWEEDLDNCKDLLAAYKKHQEDLKIAQTPKKTPSKTPKKTPKSLKRRALTPSDDEEEAGPIAPEPKKTPKQSTKKLKRTTSPETNLVEKSKKKAIPDLENHTLDQEKNDVIERVEEIQEDEDDDDEQREEVVTTAPVETKSRWGFGSWKWF
Protein: Active breakpoint cluster region-related protein (A0A0G2JTR4)
Organism: Rattus norvegicus (Rat)
Function: Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form. The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form (By similarity). Functions as an important negative regulator of neuronal RAC1 activity (By similarity). Regulates macrophage functions such as CSF-1 directed motility and phagocytosis through the modulation of RAC1 activity (By similarity).
Subcellular location: Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q5SSL4}. Cell projection, axon {ECO:0000250|UniProtKB:Q5SSL4}. Synapse {ECO:0000269|PubMed:20962234}.
Interaction partners:
Sequence:
MEPLSHRGLPRLSWIDTLYSNFSYGAEDYDAEGHEEQKGPPEGSETMPYIDESPTMSPQLSARSQGGGESISPTPPEGLAPGVEAGKGLEMRKLVLSGFLASEEIYINQLEALLLPMKPLKATATTSQPVLTIQQIETIFYKIQDIYEIHKEFYDNLCPKVQQWDSQVTMGHLFQKLASQLGVYKAFVDNYKVALETAEKCSQSNNQFQKISEELKVKGPKDSKDSHTSVTMEALLYKPIDRVTRSTLVLHDLLKHTPVDHPDYPLLQDALRISQNFLSSINEDIDPRRTAVTTPKGETRQLVKDGFLVEMSESSRKLRHVFLFTDVLLCAKLKKTSAGKHQQYDCKWYIPLADLVFPSPEESEASPQVHPFPDHELEDMKVKISALKSEIQKEKANKGQSRAIERLKKKMFENEFLLLLNSPTIPFRIHNRNGKSYLFLLSSDYERSEWREAIQKLQKKDLQAFVLSSVELQVLTGSCFKLRTVHNIPVTSNKDDDESPGLYGFLHVIVHSAKGFKQSANLYCTLEVDSFGYFVSKAKTRVFRDTTEPKWDEEFEIELEGSQSLRILCYEKCYDKTKVNKDNNEIVDKIMGKGQIQLDPQTVESKNWHTDVIEMNGIKVEFSMKFTSRDMSLKRTPSKKQTGVFGVKISVVTKRERSKVPYIVRQCIEEVEKRGIEEVGIYRISGVATDIQALKAVFDANNKDILLMLSDMDINAIAGTLKLYFRELPEPLLTDRLYPAFMEGIALSDPAAKENCMMHLLRSLPDPNLITFLFLLEHLKRVAEKEPINKMSLHNLATVFGPTLLRPSEVESKAHLTSAADIWSHDVMAQVQVLLYYLQHPPISFAELKRNTLYFSTDV
Protein: Fibronectin type-III domain-containing protein (Q18100)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MGLRETMGRGGPPNTTTFIFLLGCLLFLVSDRYYTCTAENIELKDYKFGNQFSLQITNNKRRSLQQMPPTEQYVNQSSPIALQGNQHKLHCFFSGYPAPKPRWFHNGREISEDSDAAGFRFESYGKTLVFNVTQDKAGKYDCRFATQQDIDRTFNVVVEAAPYWPLGPPPNTNTSEGEKVIFDCTTYGKPTPKVTFYKNGVEIESQKDDRYLIEGTRLTIFDVKKGTYGKGDNAVYQCKSENKHGWLWTNFYLNLLAFKPQLLIDPGKEEVEAVAGKKVTLECKFFASPNAAVKWEAPMISGSKGNQIPADAYGVGKLVFSEVTAAEEGEYECIGTNKYGQATGLITLKVRKPTIVQPFPRVEEVRMAGEEMRLACDATADNQLEVKYEWLVDGKSLPEDRISSGHYKIDDDHSLVISNPTQDDTAKYKCVVSTKLDQVEKEIKIQFKDVPVAVHSAWVQTCDKNSLTAFIKFEHYESIHTIAPIKEFWVQYQIDSETEGSQWRTHPVPSAAHPNDKIDNNLRHTTGDATVSLQPFGKYVFRVIARNSVGDSAARLAKDQCETPAKQPDKNPDEVAAKGTSPENIIVQWKPMSREEWNGADFHYVVKYRPKDEDQRVGDWKEVAVEDPFADRVTVNLDDEKDVKPFQPYEVQVQAVNSEGRTNVVPETVEGRTGEGVPSSIPSGLRVLEKSGTTVTLAWNGVDPQTANGNFTGYKITYWVDEADQDSDDSSEDDEDDEKRKFRWKRSIRVKRQSGIRKTVVFGPSATQGTLTDLKPATLNHAYIQVTNGAHEGSASDTIDFQTDEGVPSPVRSLRAYPMNSKVGGEKGVVVLVWKKPRQTNGKLARYEVEYCKTQNGKLVEKSCPRKQIDADSKEIRITGLENETPYRFILRAHTSAGEGDPNSSDATTLPETTAAGVDPGVPSLVENAIGDKYFNVSFRPAKYDDESRAPVGNTYEVQYKPQDADEWETVKPADDGLTVHVDGLSPGTKYDVRVAALQVDPEGGETTKTLSGISKITTTGTSSRERNVYLLILLLLILLLLLIICCICCVVCRQRGQNYPVSQREREQGREPILGKPDYKTDDDEKRSLTGSKAESETDSMAQYGDTDPGVFTEDGSFIGQYVPQKSLMPAERPEKGSTSTFV
Protein: Actin, aortic smooth muscle (EC 3.6.4.-) (Alpha-actin-2) [Cleaved into: Actin, aortic smooth muscle, intermediate form] (P62740)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Myosin-11
- Myosin light chain 9
- Myosin-10
- EF-hand domain-containing protein
- Actin gamma 2, smooth muscle
- Transgelin
- Uncharacterized protein
- Vimentin
- Platelet-derived growth factor receptor beta
- Collagen type I alpha 1 chain
Sequence:
MCEEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
Protein: Uncharacterized protein (P71874)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MPDDQPAVPDVDRLARSMLLLHGDHHDHNDSPEQHRTCGSWSKSRDFADDPQRAAAVREASRAERDRYLTSGLQPVDCRFCHVTVTVKRLGPGHTAVQWNTEASRRCAYFTELRARGGDSARTRSCPRLTDSIEHAVAEGYLEHHDPNR
Protein: UDP-glycosyltransferase 89A2 (EC 2.4.1.-) (Q9LZD8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glucosyltransferase that glucosylates benzoates and benzoate derivatives in vitro.
Interaction partners:
- At1g23050
- Uncharacterized protein At5g65300
- Putative pectinesterase 63
- Putative pectinesterase/pectinesterase inhibitor 45
Sequence:
MTEVLLLPGTKSENSKPPHIVVFPFPAQGHLLPLLDLTHQLCLRGFNVSVIVTPGNLTYLSPLLSAHPSSVTSVVFPFPPHPSLSPGVENVKDVGNSGNLPIMASLRQLREPIINWFQSHPNPPIALISDFFLGWTHDLCNQIGIPRFAFFSISFFLVSVLQFCFENIDLIKSTDPIHLLDLPRAPIFKEEHLPSIVRRSLQTPSPDLESIKDFSMNLLSYGSVFNSSEILEDDYLQYVKQRMGHDRVYVIGPLCSIGSGLKSNSGSVDPSLLSWLDGSPNGSVLYVCFGSQKALTKDQCDALALGLEKSMTRFVWVVKKDPIPDGFEDRVSGRGLVVRGWVSQLAVLRHVAVGGFLSHCGWNSVLEGITSGAVILGWPMEADQFVNARLLVEHLGVAVRVCEGGETVPDSDELGRVIAETMGEGGREVAARAEEIRRKTEAAVTEANGSSVENVQRLVKEFEKV
Protein: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 (6PF-2-K/Fru-2,6-P2ase 2) (PFK/FBPase 2) (6PF-2-K/Fru-2,6-P2ase heart-type isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] (O60825)
Organism: Homo sapiens (Human)
Function: Synthesis and degradation of fructose 2,6-bisphosphate.
Interaction partners:
- ATP-dependent 6-phosphofructokinase, muscle type
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
- Fructose-1,6-bisphosphatase isozyme 2
- Fructose-2,6-bisphosphatase TIGAR
- Fructose-1,6-bisphosphatase 1
- ATP-dependent 6-phosphofructokinase, liver type
- ATP-dependent 6-phosphofructokinase, platelet type
- RAC-alpha serine/threonine-protein kinase
- RAC-beta serine/threonine-protein kinase
- RAC-gamma serine/threonine-protein kinase
Sequence:
MSGASSSEQNNNSYETKTPNLRMSEKKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQCALVALEDVKAYLTEENGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNRENVMEDFLKRIECYKVTYRPLDPDNYDKDLSFIKVINVGQRFLVNRVQDYIQSKIVYYLMNIHVQPRTIYLCRHGESEFNLLGKIGGDSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQGNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLTPVAYGCKVETIKLNVEAVNTHRDKPTNNFPKNQTPVRMRRNSFTPLSSSNTIRRPRNYSVGSRPLKPLSPLRAQDMQEGAD
Protein: Similarity to unknown protein (Q9FIM1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGIDTKEIIVILWKILGYSMNMSIKFMINHPVLSGVSMFLLVLYIFLPSLFFFLIYTSPVLACALVYAREKLGLRFSSSYSEPKKSCGGEKRCHLKQQRSVRRNARMKVEEWDSQTSEEEKDKVILTSLYNDLLGRTPQFEESPKALETNVVEEEEDKEKEFLGEGVSRDLGHLNVEEPMVCNCEIKYGESDGKVEMKQEMSNANEHGISEIERNKRLESLIARRRARRRFRLALDQKNKLQAEETTSPRQNNTNNLHVTVSRNSLEKRRNNSSDGTTVKGLQIPGSAPSVMLQGRNPFDIPYDPQEERPNLTGDSFDQEFSLFNQKDLFFCRHESFCRFSLFSPEHVQCMNSPVSASDISTTRKRLDLENEYIDHTEQNLPLNGKEATIEDDDKSVVSRKSEEKEVEMNDETDSNKEECDDSSCSEESESELCRLNKAELREAICQSMDNNPGYLVNQARNSIPSTLPRGIVAPRLDDNNMFYARKCGNSHSRTFSVASDMQVEVSEIGSPPTTVDWLDDWSTGGESYIYDTDIDREIVRDEESRKRMSHQYESRSGIGSKEENSEPSTKPEAKPDQDCVVDEDLITVDDMSLLDRRTQSEEIFEQTPSSSSDVSKPTSSGRFEGMLFHTSASLSSITEEPETILDSIDGVNSEIMNSLTGELTDQRPLTSLDLSMENLIDEEVADMQQIENDDLCGSPKIIDFDIIDHQQTDQTSDSIQGEHEETKSFLDASLDTPFIESFEREVQEEEESNLDKSTEETTKETESDLKSSPGQVSTELLESVVREENGQELVKSADEKAMLVEEEKTHNVLEASSSNAHTQLVDLDYGNAENSSDVILLQVQDSHKSPLDESVDQEISKEVEKTELLKDFCGESTQEYKNRGNVEACGNAENASDVLLLQVQDGNNSPLDESTDQEISKEEEKTEVLKDFNDETPQGYKNRANVEEESVVLADTQNSQDSQTWTQQCGIDSSQGISPRTLEITQQLEQDDVIASSSNTVSQDINKDITAAVANDLAASERNDEVILKLDEQVGEAMEKELELNLESLHHNIGLVGREDDEESKKVIEEMQNAEIQTTKHENRVLG
Protein: Discoidin domain-containing receptor tyrosine kinase B (EC 2.7.10.1) (Discoidin domain-containing receptor B) (Q95ZV7)
Organism: Caenorhabditis elegans
Function: Tyrosine-protein kinase receptor which, together with ddr-1, is involved in axon guidance to establish the tracts for the ventral and dorsal nerve cords during nervous system development. Acts upstream of the adapter shc-1, and the tyrosine kinase receptors svh-1 and svh-2 to regulate axon regeneration following injury in D-type motor neurons. May mediate axon regeneration in association with the collagen emb-9.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27984580}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:23147028, ECO:0000269|PubMed:27984580, ECO:0000269|PubMed:31371405}. Perikaryon {ECO:0000269|PubMed:23147028}.
Interaction partners:
- Putative cuticle collagen 99
Sequence:
MKLLLYLFGVTFHSNTVVALELRECSHQLGMSNRKIRDEQISASSSFDLQSTGPQHARAHQESGSGAWCPKNQINSLSKEWLQISFSVDTVITSVETQGRFDDGRGMEYATAFKIQYWRPSLNAWASYKDDFELETIPANNDTEHAIRRHLDRAIIARRIRIVPVSNSTRTVCMRVEVFGCPFDDSLVFYNVDQGDLQSGISYHDFSYDGNLANSPHLTGGIGKLYDGEVGKNNVFVNHHKWVGWRRKRNGNVKLAFEFSELRNISGILIHTSNEFKKSAKAFSSATVLFSINGKDFSDTIVHFNNPEDTESEVPRWIRIPVNNRIAKVAKIRLNFGTDSDWLFISEVNFESNHTNIELLNDDVVIPDSVSYFSVTEHDDGTSMFAFIIFFFMFLIVAVIILTVLYRKREYRVKASSPSPNAKREILLTIDGNTIKHHVSPSTYQMARDNLQNALIEKMPMSPIISDYAEPDISVCSDVTANTPLLYGIDGPYDTQKRSNPLSSMVKYSDYGEVYCTTLPEIARDKLICVSRIGQGEFGEVDLCQLENRKVAVKKLHGISQADEFSFHREIRVLGSLKHPNVVEVVGVCTIQKPILCIMEYMENGDLKSYILKNPTIQTSQCISICTQLAAGLAYLESCNFVHRDIAARNCLVDGEGNVKIADFGMARSLYSQEYYKVEGKFVLPIRWMAWEALLLGKFSTASDVWGFGVTMWEIFSLCSEKPYSDMTDDDVVENLQSMSSTGSLKQVLSRPRMCPSKLYNEQILPCWNYESSRRPSFENVHLHLQSLVHTSPHIHF
Protein: Beta-secretase 2 (EC 3.4.23.45) (Aspartyl protease 1) (ASP1) (Asp 1) (Beta-site amyloid precursor protein cleaving enzyme 2) (Beta-site APP cleaving enzyme 2) (Memapsin-1) (Membrane-associated aspartic protease 1) (Theta-secretase) (Q9JL18)
Organism: Mus musculus (Mouse)
Function: Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves APP, between residues 690 and 691, leading to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. It has also been shown that it can cleave APP between residues 671 and 672. Involved in the proteolytic shedding of PMEL at early stages of melanosome biogenesis. Cleaves PMEL within the M-beta fragment to release the amyloidogenic PMEL luminal fragment containing M-alpha and a small portion of M-beta N-terminus. This is a prerequisite step for subsequent processing and assembly of PMEL fibrils into amyloid sheets. Responsible also for the proteolytic processing of CLTRN in pancreatic beta cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21907142}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q9Y5Z0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y5Z0}. Endosome {ECO:0000250|UniProtKB:Q9Y5Z0}. Melanosome {ECO:0000250|UniProtKB:Q9Y5Z0}. Note=Colocalizes with PMEL in stage I and II melanosomes. {ECO:0000250|UniProtKB:Q9Y5Z0}.
Interaction partners:
- Reticulon-3
- Reticulon-4
- Beta-secretase 1
- Amyloid-beta precursor protein
- Tyrosine-protein kinase Fyn
Sequence:
MGALLRALLLLVLAQWLLSAVPALAPAPFTLPLQVAGATNHRASAVPGLGTPELPRADGLALALEPVRATANFLAMVDNLQGDSGRGYYLEMLIGTPPQKVQILVDTGSSNFAVAGAPHSYIDTYFDSESSSTYHSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNSSFLVNIATIFESENFFLPGIKWNGILGLAYAALAKPSSSLETFFDSLVAQAKIPDIFSMQMCGAGLPVAGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQNLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARTSLIPEFSDGFWTGAQLACWTNSETPWAYFPKISIYLRDENASRSFRITILPQLYIQPMMGAGFNYECYRFGISSSTNALVIGATVMEGFYVVFDRAQRRVGFAVSPCAEIEGTTVSEISGPFSTEDIASNCVPAQALNEPILWIVSYALMSVCGAILLVLILLLLLPLHCRHAPRDPEVVNDESSLVRHRWK
Protein: Terpene synthase 6 (EC 4.2.3.160) (Q54P86)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into the sesquiterpene (2S,3R,6S,9S)-(-)-protoillud-7-ene.
Interaction partners:
Sequence:
MSLSLGDIKFPDNWDLIPNEKNYIDYVYKESIELEVWRPNNKRDLMAHNNVVSLAKYFWPHVDFNRLVMGGELMVWFFSFDDVLDAGIYTDEKQMDLVKRMDNVFINGTVESDATGPEKMALHLRKKCEVMCGKRRKDTFNRFISSCVQWVDSIIPFNKLRSAQGTSPHLELYSYLRKVNIGAYPCVTLTEVMLDHEIEYYIWSDPKWIKMNEDIAIITTLINDLVSYEKEVNDQAGDLNPLYFLQNQKNIPLPDSYKQVVDLIDFWVKDYQTMEQSLLNEMEFKDSKQRSDMEFILEHLRYLASGSKKWSMQTPRYCSPTSPFIEMRTKPSTPVMNSTKKQKIDHVPSQSFISTPIDLNN
Protein: Holocarboxylase synthetase (D4AA38)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Biotinidase
- Pyruvate carboxylase, mitochondrial
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Acetyl-CoA carboxylase 1
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- acetyl-CoA carboxylase
- Propionyl-CoA carboxylase beta chain, mitochondrial
- CCA tRNA nucleotidyltransferase 1, mitochondrial
Sequence:
MEDRLQMDNGLIAQKIVSVHLKDPALKELSKASNKQVQAPLPSPEASLEAQPAQGVMEQAGQGDWKAAGEGPSPQRRGCAPVSESAADGDPGQGSTELCQLHLSSCHECLELENSTIESVRCASAENIPDLPHDCSSSVEGTAGELCPERKGKRVNISGKAPNILLYVGSGSEEALGQLQQVRSVLTDCVDTDSYTLYHLLEDSALRDPWPDNCLLLVIASRDPIPKGIHHRFMAYLSQGGKVLGLSSSFTFGDLRVARRDVLRNTAQNLVFSKADGSEVRLSVLSSGYVYEEGPSLGRLQGHLENEDKDKMIVHVPFGTHGGEAILCQVHLELPPSAPLVQTTDDFNVLKSSNTRRLEVLKEILTALGLSCDAPQAPALTPLYLLLAAEEIQGPFMQWLARHVDPEGVIKSSKLSLKFVSSYTSEAEITPSSIPVVTDPEGFSSEHFNLETYRQNLQSTRLGRVILFAEVTSTTMSLLDGLMFEMPQEMGLIAIAVRQTQGKGRGPNAWLSPVGCALSTLLVSIPLRSQLGQRIPFVQHLMSLAVVEAVRSIPEYEDINLRVKWPNDIYYSDLMKIGGVLVNSTLVGETFYILIGCGFNVTNSNPTICINDLIEEHNKQNKAGLKPLQADCLIARAVTVLEKLIDRFQDQGPDGVLPLYYKYWAHRSAPTRFFLLKFLEVSTRV