wanglab/gogpt-training-data huggingface dataset:
Protein: Mannose-binding protein C (MBP-C) (Mannan-binding protein) (Ra-reactive factor polysaccharide-binding component p28A) (RaRF p28A) (P08661)
Organism: Rattus norvegicus (Rat)
Function: Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Mannan-binding lectin serine protease 2
- Mannan-binding lectin serine protease 1
- Complement C4
- Plasma protease C1 inhibitor
- Ficolin-2
- Complement C2
- Mannose-binding protein A
- Ficolin-1
- Complement C4A
- Pentraxin-related protein PTX3
Sequence:
MSLFTSFLLLCVLTAVYAETLTEGAQSSCPVIACSSPGLNGFPGKDGHDGAKGEKGEPGQGLRGLQGPPGKVGPAGPPGNPGSKGATGPKGDRGESVEFDTTNIDLEIAALRSELRAMRKWVLLSMSENVGKKYFMSSVRRMPLNRAKALCSELQGTVATPRNAEENRAIQNVAKDVAFLGITDQRTENVFEDLTGNRVRYTNWNEGEPNNVGSGENCVVLLTNGKWNDVPCSDSFLVVCEFSD
Protein: Regulator of G-protein signaling 8 (RGS8) (Q8BXT1)
Organism: Mus musculus (Mouse)
Function: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Modulates the activity of potassium channels that are activated in response to DRD2 and CHRM2 signaling.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P49804}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49804}; Cytoplasmic side {ECO:0000250|UniProtKB:P49804}. Membrane {ECO:0000250|UniProtKB:P49804}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49804}; Cytoplasmic side {ECO:0000250|UniProtKB:P49804}. Perikaryon {ECO:0000250|UniProtKB:P49804}. Cell projection, dendrite {ECO:0000250|UniProtKB:P49804}. Nucleus {ECO:0000250|UniProtKB:P49804}. Note=Detected in Purkinje cell soma and dendrites. Associated with Purkinje cell membranes. Not detected in Purkinje cell nuclei. Detected in the nucleus after heterologous expression. Recruited to the cell membrane in the presence of GNAO1. {ECO:0000250|UniProtKB:P49804}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Regulator of G-protein signaling 7-binding protein
- Guanine nucleotide-binding protein G
Sequence:
MAALLMPRRNKGMRTRLGCLSHKSDSCSDFTAILPDKPNRALKRLSTEEATRWAESFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTRSTAKLVTKAHRIFEEFVDVQAPREVNIDFQTREATRKNMQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLDLLSQSQRRLS
Protein: UDP-glucuronate 4-epimerase 1 (EC 5.1.3.6) (UDP-glucuronic acid epimerase 1) (AtUGlcAE3) (Q9M0B6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: UDP-D-glucuronate 4-epimerase involved in the synthesis of the negatively charged monosaccharide that forms the backbone of pectic cell wall components.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- UDP-D-apiose/UDP-D-xylose synthase 1
- UDP-sugar pyrophosphorylase
- UDP-D-apiose/UDP-D-xylose synthase 2
- UTP--glucose-1-phosphate uridylyltransferase 1
- UTP--glucose-1-phosphate uridylyltransferase 2
- Sucrose synthase 3
- Sucrose synthase 2
- Sucrose synthase 5
- Sucrose synthase 1
- Sucrose synthase 6
Sequence:
MPSIEDELFPSTPGKFKIDRSNRQLHRCFASTSTMFLWALFLIALTASYLSFQSFVDSGSRYLTASWGGIQWEKQVRTSAQIHRSGGISVLVTGATGFVGSHVSLALRKRGDGVVGLDNFNNYYDPSLKRARRSLLSSRGIFVVEGDLNDAKLLAKLFDVVAFTHVMHLAAQAGVRYALENPQSYVHSNIAGLVNLLEICKAANPQPAIVWASSSSVYGLNEKVPFSESDRTDQPASLYAATKKAGEEITHTYNHIYGLAITGLRFFTVYGPWGRPDMAYFSFTRNILQGKPITIYRGKNRVDLARDFTYIDDIVKGCLGSLDSSGKSTGSGGKKRGAAPYRIFNLGNTSPVTVPILVDILEKHLKVKAKRNFVEMPGNGDVPFTHANISSARNEFGYKPTTDLETGLKKFVRWYLSYYGYNTKAKLVH
Protein: Bromodomain containing 8 (B5MCW3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATGTGKHKLLSTGPTEPWSIREKLCLASSVMRSGDQNWVSVSRAIKPFAEPGRPPDWFSQKHCASQYSELLETTETPKRKRGEKGEVVETVEDVIVRKLTAERVEELKKVIKETQERYRRLKRDAELIQAGHMDSRLDELCNDIATKKKLEEEEAEVKRKATDAAYQARQAVKTPPRRLPTVMVRSPIDSASPGGDYPLGDLTPTTMEEATSGVNESEMAVASGHLNSTGVLLEVGGVLPMIHGGEIQQTPNTVAASPAASGAPTLSRLLEAGPTQFTTPLASFTTVASEPPVKLVPPPVESVSQATIVMMPALPAPSSAPAVSTTESVAPVSQPDNCVPMEAVGDPHTVTVSMDSSEISMIINSIKEECFRSGVAEAPVGSKAPSIDGKEELDLAEKMDIAVSYTGEELDFETVGDIIAIIEDKVDDHPEVLDVAAVEAALSFCEENDDPQSLPGPWEHPIQQERDKPVPLPAPEMTVKQERLDFEETENKGIHELVDIREPSAEIKVEPAEPEPVISGAEIVAGVVPATSMEPPELRSQDLDEELGSTAAGEIVEADVAIGKGDETPLTNVKTEASPESMLSPSHGSNPIEDPLEAETQHKFEMSDSLKEESGTIFGSQIKDAPGEDEEEDGVSEAASLEEPKEEDQGEGYLSEMDNEPPVSESDDGFSIHNATLQSHTLADSIPSSPASSQFSVCSEDQEAIQAQKIWKKAIMLVWRAAANHRYANVFLQPVTDDIAPGYHSIVQRPMDLSTIKKNIENGLIRSTAEFQRDIMLMFQNAVMYNSSDHDVYHMAVEMQRDVLEQIQQFLATQLIMQTSESGISAKSLRGRDSTRKQDASEKDSVPMGSPAFLLSLFDGGTRGRRCAIEADMKMKK
Protein: GH08610p (Q95SQ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTWTTLANLRIPRSGLGAAFLKGKFYAVGGRNNNIGSSYDSDWVDRYSAVTETWRPCAPMSVPRHRVGVAVMDELMYAVGGSAGMEYHNTVEYYDPDLDRWTLVQPMHAKRLGVGVVVVNRLLYAIGGFDGNERLASVECYHPENNEWSFLPPLQTGRSGAGVAAINQYIYVVGGFDGTRQLATVERYDTENDTWDMVAPIQIARSALSLTPLDEKLYAIGGFDGNNFLSIVEVYDPRTNTWTTGTPLKSGRSGHASAVIYQPACSTTFMDYEDSDAPHPDGSNNGERNAHTPQNTYGSGSPHYPGTASNMQFHTSYGMSGCNNCDSEMDIKPYIPAEHHSFQIPAIRSEELVNPNCPWSRMQERFRRTPPASFTDDERNANDMRHKLKKAQKECLFSTAAKVFHHHIEGRLRKLTSAAT
Protein: ATP-dependent RNA helicase DBP7 (EC 3.6.4.13) (DEAD box protein 7) (P36120)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9582098}.
Interaction partners:
- Nucleolar complex protein 2
- Ribosome biogenesis protein MAK21
- rRNA biogenesis protein RRP5
- Probable ATP-dependent RNA helicase DHR1
- 27S pre-rRNA
- Ribosome biogenesis protein RPF2
- ATP-dependent RNA helicase MAK5
- Nucleolar pre-ribosomal-associated protein 1
- Nucleolar GTP-binding protein 1
- Ribosome biogenesis protein ERB1
Sequence:
MSDEDSMLLNFTTNEDTAGSSYKQAAKVTGGRWKDRRRMKMKLEGKTVSRKRKANTTGDEGIIPGRGENSIKKLHKESSYSSEEQEKYKGRNAHNTQGRTLPADSQFVSSLFTSNREITTAVNTNIHDENVAINPSNAPLKGDQFASLGVSSLLVSHLEQKMRIKKPTSIQKQAIPQIIGNAGKNDFFIHAQTGSGKTLSYLLPIISTILNMDTHVDRTSGAFALVIAPTRELASQIYHVCSTLVSCCHYLVPCLLIGGERKKSEKARLRKGCNFIIGTPGRVLDHLQNTKVIKEQLSQSLRYIVLDEGDKLMELGFDETISEIIKIVHDIPINSEKFPKLPHKLVHMLCSATLTDGVNRLRNVALKDYKLISNGTKKDSDIVTVAPDQLLQRITIVPPKLRLVTLAATLNNITKDFIASGQQSKTLRTIVFVSCSDSVEFHYDAFSGSDGHHKNLTGDSVRLLTKGNTMFPCFSDSRDPDVVIYKLHGSLSQQMRTSTLQHFARDNEATKGKHLIMFCTDVASRGLDLPHVGSVIELDPPFAVEDHLHRVGRTARAGEKGESLLFLLPGEEEKYMDYIQPYHPMGWELLKFDKEILMPAFKDVNVNRNDKFIRKDEKSSKNKDVGDKEYEWDTNATTWHLNIERRVVGDSAFKNLAVKGFISHVRAYATHISQEKKFFNVKFLHLGHLAKSFGLRERPKAMGLQSSKDGNSEKKPTKENSKNKMFRMARMAEKQIASEFNY
Protein: Brahma-associated protein 111kD (Q9BIW6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MALPSNYKQIAVGGQGSATPLQGGGGGSGGGSRSRSSGGGGGGDRNKDQTPIFTHSNYGNPAFTPQKVTKSSSSKNQNESRLPKPPKPPEKPILPYMRYSKRVWDSVKAKHPELKLWELGKKIGAMWKLLPEDEKTEFIDEYEAEKLEYEKSLKAYHQTPAYQAYMSAKSKVKTDVDMHETPSRGGGSKSQHERRIDIQPAEDEDDQDEGYTTKHLAYARYLHNHRLINEIFSEAVVPDVRSVVTTTRMQVLKRQVSSLTMHQTKLEAELQQMEEKFEAKKQRMVESSEAFQEELKRHCKPAVDEETFQKMVLRMYEDIKRDRQRLDEPNANANSAANPAAAAATAAAAPVTRSEEAVKPPTQPGQPAATPAGQEPASAVPAPAAPPKETPPAVKPATLNPTPSSTPTPAPAVHVHETASKTDPEPMDIEPPPKPSVPPPPIKPEKLEMAAALPPQSTLVEPPKTEPAKVVAQPGKVPTPVPTPTPPPEVAPAAGAVTAATTTTRRTPTPPPVPQQVPLPQQQGGPAPPPGMPQMHPHPGHPPPGHSLMPPHMGPHQPPPGMPGLPPPPPHTGYANYGGPPHGPPPGPPGGPARPYYQPQYGGHPTPQPYYAPFSPYQQSYGPPPGSHYMSPRPPPPQHNGNPGHPYAPEHGSNPPPPQQQQQQQPPPGHLHEPSGGGPGAPGGGAGAAAAAAPGAGVYPTPGAGAGPGAPPGPAGGAPLGEAAVAGGVGPPAATALGKHPEAEKHEAD
Protein: Vasoactive intestinal polypeptide receptor 2 (VIP-R-2) (Pituitary adenylate cyclase-activating polypeptide type III receptor) (PACAP type III receptor) (PACAP-R-3) (PACAP-R3) (P35000)
Organism: Rattus norvegicus (Rat)
Function: This is a receptor for VIP as well as PACAP-38 and -27, the activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Can be coupled to phospholipase C.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41587}.
Interaction partners:
- Pituitary adenylate cyclase-activating polypeptide
- VIP peptides
- Pro-glucagon
- Gastric inhibitory polypeptide
- Pro-opiomelanocortin
- Natriuretic peptides A
- Neuroendocrine secretory protein 55
- Guanine nucleotide-binding protein G
- Secretin
- Gastrin-releasing peptide
Sequence:
MRASVVLTCYCWLLVRVSSIHPECRFHLEIQEEETKCAELLSSQMENHRACSGVWDNITCWRPADIGETVTVPCPKVFSNFYSRPGNISKNCTSDGWSETFPDFIDACGYNDPEDESKITFYILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCHDQPGSWVGCKLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIPWWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQILFELCVGSFQGLVVAVLYCFLNSEVQCELKRRWRGLCLTQPGSRDYRLHSWSMSRNGSESALQIHRGSRTQSFLQSETSVI
Protein: Probable E3 ubiquitin-protein ligase LUL2 (EC 2.3.2.27) (Probable RING-type E3 ubiquitin transferase LUL2) (Protein LOG2-LIKE UBIQUITIN LIGASE 2) (RING finger protein 269) (Q9LFH6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates (in vitro).
Interaction partners:
- Zinc finger CCCH domain-containing protein 34
- Protein GLUTAMINE DUMPER 2
- Protein DA1-related 2
- E3 ubiquitin-protein ligase RHA2A
Sequence:
MGNVISGGSRPENHRDRTSPPYPNPNAQYQGNYPSPYQDCARYPYGEMASPVQYVEHQEAVTIRNDINLKKETLRLEPDEQNPGKFLLSFTFDASVPGSITVMFFAKEGKDCNLIATKEDLFPSTQVSFAKGLEQRFKQACGTGIDFSDMSEADLVEANETDVYHVAVKAEVVSEDDHPESGTPNRQITHVVLEKDHKGEYKARVVKQILWVNGNRYVLQEIYGIGNTVDDNGEDANERGKECVICLSEPRDTTVLPCRHMCMCSGCAKLLRFQTNLCPICRQPVDRLLEITVNNNDRN
Protein: Tryptophan 5-hydroxylase 2 (EC 1.14.16.4) (Tryptophan 5-monooxygenase 2) (Q9W0K2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Aromatic-L-amino-acid decarboxylase
- Pterin-4-alpha-carbinolamine dehydratase
- RE21057p
- Sepiapterin reductase
- Dihydropteridine reductase
- Tyrosine 3-monooxygenase
- MIP05841p)
- Tryptophan 2,3-dioxygenase
- Protein henna
- Dihydrofolate reductase
Sequence:
MSASGKSLLGLWLYRSGEQEWAVKQGSPLHQLKKDSTTSGSSSHPSLGRNASAPPEPPRLAIGGGGQDNGRQHSPGERISIIFTLRNQVGNLARALQVFQELGINVLHLELSPLEMATNQADVLVDVECDQRRLDQVVKMLNREVASVNYTSVNTQGLARAPSLSACSSFDFGDMVWFPRKISDLDKAQNVLMYGSELDADHPGFKDPVYRKRREQFSAIANNFKHGNPIPRVQYTPEEVKTWGTVFLELHRLYVLHAVPEYMDNWPELEKYCGYREDNVPQLQDVSVYLKRKTGFQLRPVAGYLSPRDFLSGLAFRVFHCTQYIRHSSDPFYTPEPDCCHELLGHMPLLANSSFAQFSQEIGLASLGASDADIEKLATLYFFTVEFGLCKQADSTFKVYGAGLLSSVAELQHAITAENKIKKFDPEVTCQQECIITSYQNAYYYTDSFEEAKEQMRAFAESIQRPFGVRYNPYTMSVEVLSNAKKITAVVSELRGDLSIVCSALRKISATDENLDVDSIANMLHNSLNVRGGASGGGGSPCSPDNSDNSTAEGD
Protein: SEPALLATA1 (Q5XXN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRGRVELKRIENKINRQVTFAKRRNGLLKKAYELSVLCDAEVALIIFSNRGKLYEFCSSSNMLKTLDRYQKCSYGSIEVNNKPAKELENSYREYLKLKGRYENLQRQQRNLLGEDLGPLNSKELEQLERQLDGSLKQVRSIKTQYMLDQLSDLQNKEQMLLETNRALAMKLDDMIGVRSHHMGGWEGGEQNVTYAHHQAQSQGLYQPLECNPTLQMGYDNPVCSEQITATTQAQAQPGNGYIPGWML
Protein: Small ribosomal subunit protein bS18 (C3SFP7)
Organism: Escherichia coli
Interaction partners:
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL10
- Elongation factor Tu
- 30S ribosomal protein S6
- 50S ribosomal protein L11
- GTP pyrophosphokinase
- Alternative ribosome-rescue factor A
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein bL9
Sequence:
MARYFRRRKFCRFTAEGVQEIDYKDIATLKNYITESGKIVPSRITGTRAKYQRQLARAIKRARYLSLLPYTDRHQ
Protein: Keratin-associated protein 13-2 (Q52LG2)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity).
Interaction partners:
- Keratin-associated protein 19-3
Sequence:
MSYNCCSGNFSSRSCGDYLRYPASSRGFSYPSNLVYSTDLCSPSTCQLGSSLYRGCQEICWEPTSCQTSYVESSPCQTSCYRPRTSLLCSPCKTTYSGSLGFGSSSCRSLGYGSRSCYSVGCGSSGVRSLGYGSCGFPSLGYGSGFCRPTYLASRSCQSPCYRPAYGSTFCRSTC
Protein: Telomere repeats-binding bouquet formation protein 2 (Q8NHR7)
Organism: Homo sapiens (Human)
Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA.
Subcellular location: Chromosome, telomere {ECO:0000250|UniProtKB:Q9D494}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9D494}. Note=Localizes to telomeres throughout meiotic prophase I and disappears in metaphase I. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q9D494}.
Interaction partners:
- Membrane anchored junction protein
- Telomere repeats-binding bouquet formation protein 1
- Telomeric repeat-binding factor 1
- Protein KASH5
- SUN domain-containing protein 1
- Speedy protein A
- SUN domain-containing protein 2
Sequence:
MFQGQRGWFCGSVSQDLRQFWVAEGGTISDPRAADFLFSCDASHPDTLRIYQSLDYIEDNATVFHAYYLSAVANAKIKNSVALGHFILPPACLQKEIRRKIGSFIWEQDQHFLIEKHDEVTPNEIKTLRENSELATEHKKELSKSPEKHFIRTPVVEKQMYFPLQNYPVNNMVTGYISIDAMKKFLGELHDFIPGTSGYLAYHVQNEINMSAIKNKLKRK
Protein: Tyrosine-protein kinase Blk (EC 2.7.10.2) (B lymphocyte kinase) (p55-Blk) (P51451)
Organism: Homo sapiens (Human)
Function: Non-receptor tyrosine kinase involved in B-lymphocyte development, differentiation and signaling (By similarity). B-cell receptor (BCR) signaling requires a tight regulation of several protein tyrosine kinases and phosphatases, and associated coreceptors (By similarity). Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation (By similarity). Signaling through BLK plays an important role in transmitting signals through surface immunoglobulins and supports the pro-B to pre-B transition, as well as the signaling for growth arrest and apoptosis downstream of B-cell receptor (By similarity). Specifically binds and phosphorylates CD79A at 'Tyr-188'and 'Tyr-199', as well as CD79B at 'Tyr-196' and 'Tyr-207' (By similarity). Phosphorylates also the immunoglobulin G receptors FCGR2A, FCGR2B and FCGR2C. With FYN and LYN, plays an essential role in pre-B-cell receptor (pre-BCR)-mediated NF-kappa-B activation (By similarity). Contributes also to BTK activation by indirectly stimulating BTK intramolecular autophosphorylation (By similarity). In pancreatic islets, acts as a modulator of beta-cells function through the up-regulation of PDX1 and NKX6-1 and consequent stimulation of insulin secretion in response to glucose. Phosphorylates CGAS, promoting retention of CGAS in the cytosol.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Present and active in lipid rafts. Membrane location is required for the phosphorylation of CD79A and CD79B (By similarity). {ECO:0000250}.
Interaction partners:
- Protein FAM167A
- B-cell antigen receptor complex-associated protein alpha chain
- B-cell antigen receptor complex-associated protein beta chain
- B-cell scaffold protein with ankyrin repeats
- B-lymphocyte antigen CD19
- Fc receptor-like A
- Krueppel-like factor 11
- Signal transducer and activator of transcription 3
- Epidermal growth factor receptor
- Paired box protein Pax-5
Sequence:
MGLVSSKKPDKEKPIKEKDKGQWSPLKVSAQDKDAPPLPPLVVFNHLTPPPPDEHLDEDKHFVVALYDYTAMNDRDLQMLKGEKLQVLKGTGDWWLARSLVTGREGYVPSNFVARVESLEMERWFFRSQGRKEAERQLLAPINKAGSFLIRESETNKGAFSLSVKDVTTQGELIKHYKIRCLDEGGYYISPRITFPSLQALVQHYSKKGDGLCQRLTLPCVRPAPQNPWAQDEWEIPRQSLRLVRKLGSGQFGEVWMGYYKNNMKVAIKTLKEGTMSPEAFLGEANVMKALQHERLVRLYAVVTKEPIYIVTEYMARGCLLDFLKTDEGSRLSLPRLIDMSAQIAEGMAYIERMNSIHRDLRAANILVSEALCCKIADFGLARIIDSEYTAQEGAKFPIKWTAPEAIHFGVFTIKADVWSFGVLLMEVVTYGRVPYPGMSNPEVIRNLERGYRMPRPDTCPPELYRGVIAECWRSRPEERPTFEFLQSVLEDFYTATERQYELQP
Protein: 2',5'-oligoadenylate synthetase-like 6 (2'-5' oligoadenylate synthetase 1H) (Q8VI97)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAKNLSSTRIALCSTPAWRLDKFIEGHLLGDITFLTELRTDVNSISAFLKERCFQGAAHPMRVSRVVMGGSYNRYTVLKGRSEVDLLVFFNNLTCFDDQFKLQKEVIEEIQKHLCQFQQEKRLREKFKVQSSDQPNFRSVSFKLSYPKFQQEVEFHMQTAYDALYEVRRKENHNCEIYNKVYARLIRECTMLGKEGEFNICFMELQQDFLWKRPCELKNLICLVKHWYQLCKEKLREPLPPQYALELLTVYAWEHELPDKHETQTARGFRTVLELITKYLCLRIYWTLYYDVLHEQVNAYLYSQVKRVSPLILDPADPTWNVAGLNLQGWCILAEEAKAWLDYPCFKNRDGSRVSSWDVPPDKKGFVFL
Protein: GH08937p (Q7JYN2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
KKTDSSRRTSHNIRANFQPFHYFGNARMLTNCASKTLAAVRANIRAIATSSARASDNLFVHRDTPEDNPNIPFEFTAENKKRVEAILSIYPEGHKRGAMIPLLDLAQRQYGWLPISAMHKVAEILQLPNMRVYEVATFYTMFMRKPTGKYHIQVCTTTPCWLRGSDDILETCKKQLGIGVGDTTKDRKFTISEVECLGACVNAPMVAINDDYYEDLTSKDMQDILNDLKADKISPPGPRNGRFASEPKGEPTSLSEEPKGPGFGLQAGL
Protein: Neuronal acetylcholine receptor subunit alpha-10 (Nicotinic acetylcholine receptor subunit alpha-10) (NACHR alpha-10) (Q9GZZ6)
Organism: Homo sapiens (Human)
Function: Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding may induce an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes the cell membrane. In the ear, this may lead to a reduction in basilar membrane motion, altering the activity of auditory nerve fibers and reducing the range of dynamic hearing. This may protect against acoustic trauma.
Subcellular location: Synaptic cell membrane {ECO:0000250|UniProtKB:Q9JLB5}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9JLB5}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit alpha-9
- Choline O-acetyltransferase
- Neuronal acetylcholine receptor subunit alpha-5
- Acetylcholine receptor subunit alpha
Sequence:
MGLRSHHLSLGLLLLFLLPAECLGAEGRLALKLFRDLFANYTSALRPVADTDQTLNVTLEVTLSQIIDMDERNQVLTLYLWIRQEWTDAYLRWDPNAYGGLDAIRIPSSLVWRPDIVLYNKADAQPPGSASTNVVLRHDGAVRWDAPAITRSSCRVDVAAFPFDAQHCGLTFGSWTHGGHQLDVRPRGAAASLADFVENVEWRVLGMPARRRVLTYGCCSEPYPDVTFTLLLRRRAAAYVCNLLLPCVLISLLAPLAFHLPADSGEKVSLGVTVLLALTVFQLLLAESMPPAESVPLIGKYYMATMTMVTFSTALTILIMNLHYCGPSVRPVPAWARALLLGHLARGLCVRERGEPCGQSRPPELSPSPQSPEGGAGPPAGPCHEPRCLCRQEALLHHVATIANTFRSHRAAQRCHEDWKRLARVMDRFFLAIFFSMALVMSLLVLVQAL
Protein: Lectin 8 (MtLec8) (Agglutinin LEC8) (Q2PP75)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi.
Interaction partners:
Sequence:
MANSNPKLLVTQNPFSVFLLTFLLLITNVKSDSFSFNFPKFDTDTKSIIIDGDANTTNGVLQLTKKDQLGNPSPHSFGLSFFLGAIHLSDKQSGKVADFTTEFSFVVNPKGSQLHGDGFTFFIASLDYEFPEKSSDGGFLGLFDKESAFNTSQNSIVAVEFDSFRNEWDPQIAGNSPHIGIDINTIRSSATALWPIDRVPEGSIGKAHISYNPASKKLTALVTYLNGPVIEETAVSYTVDFAAILPEYVLVGFSGATGELAETHDILSWSFTSNL
Protein: Cell fusion related protein (Q54T88)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MQKINFYFFVLAIISIIFKYNDLFVNSQINDVKSSLDLGCFSYIVEPPSGTIILNPNSFELMVEFNQNPIYIFDGVSYSKTTSVSDIELLSFFKYQDVTGLPIFNFWDKITNKTYLPNSSKTKGVGNRIWLTFINLPISNSLYFQSNIGLSSENRYLIGARSINVYSSNSVAPPKLEVNPFLSSCPISKRVEPIWNFKNPSSTQIYPSTLKVELCSTISDSIKSSSKICSGSNQKFYYSLVLPVSVGKGIVSTVLNSVTYQGFQYKFKDYQIKIQTNQDISVSIPLDYIKSYSPPYEVQLTSDPQNAPYQDLNVIDFKTLDNYISLYNSGYYNQVLYGDENVLKIFNMNSSIDSKFLIENYKSNFIFKSTTNNLIKEIYILIGENANEFYKDYFQCPQNSLRNSFTVNHGKPTIHSLGFLNPYKGFNFKLENLKINRDLQINFGHNINDDDESIKIKMNNNNSKSDYYLTKDLLVGVFVDFTVSSNQYQSLANSILFVPDSKDLNGNGLIIPKSSVGNGMNQIGLNVADWYKQQAVGFCNQEHGSNVKNQIQHYIQDGGYTLDLMIPNWINVGGQSIEGNGGGGDRTIINSTSSELLMKFNSNQALFKVYFSEFEFFEPMIHSDNLTWVGIAGTTIGKECFGQFQFDIINFGKESSIVNFDIDCIQDVYLEIVNFAQIIPGDSNQKRSFFVNVGIEKFYKSKMIQCNVSMWIDIKNRPIWSSINKSIKKMVEIPIFNGCNIPDPCLNINSEPIISKDLQPIIKYSGWNNLGNFLNSITIEIEIKNIGNNTGDFISTLDCQSNIQPPANVNIFMINDENFIITKGLEKSKTSIVQFLLYGESSPIDGIQLTCKIKTKLYKPNTICWLNYDQENLVSFNLLYPYDKCVQIYNTGKEPLIEYSLFEYSNGNAIPNYSFGVSQWFPSMDSNPLPKKHPLKVLENSLNKNSIRFGPVDTLYNQFPSIVIKNGGGKSGDFTIDIGNCSDSVFVWADSYTITIPSGEIRKFIFQVFSYPTNIKSYSVECQLSIKTDHQECQSDLGKSFLQNPFLVYPHYLPCAGNWLEPSLFKPLSFWDSNLLLNNTLEFSDLNFKIGKWNYYKGENTIIEPNYYYQDLSLQVKNVEYGYGNVISTLTCNDVGFTTTVLYDSKKSSCFISENSSCFIGWRISSLPTTPDQKLLDIIDCNLLIEIKDSEEPIQSCWTNSGKSIKSSFKLFKFIDPCITNTFDEVFLTTTTNNQIEYIYSSDWGLKTIINEYFDYFLYGMNNSTSNNLIYYSFKNIMIKNNGNGNGLVKSLVQINNPSVILILNESIIECEIQSNSYWTFTFLFGFLPNKFSSSFSSSSLLNFNDLEIKIQFLVLPKLCWSTINKTIEILIVSKLPTLPCGWDPLLSTNLSTPIYTTPPQVSLIYPNQYIIGNLNYYQNSNNVLNLKFSNWYKLTTDTLENYNFSFNENSLNQHQFYSINLTGYIYNMGDAGGVVIFRLACDNGNGTIKQFISIENDEIVSYIPAGRYYNFKFKIIVSDKSPYPSNLKSIKDNEMIMCKVSSIVNLEKCWNPYGKSVIQYIQLPFDSKYLNNQTTIYSNEKNDKILLISTLVPISFILFLILLYLILKYYKYLLFKFNEFLITSHQNKLIKPPSIKKEEEKVTNNQQQENIKDQVTVVTDDEKCGCGENLKYHCNKCPSSISNYCESLQCKNLIHSATLGNITHKHEPNIIVYRDPRDTWINNFKFKPNDEIVEDLILNKLNKFN
Protein: HTH-type transcriptional regulator AldR (Feast/famine regulatory protein Rv2779c) (O33321)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable oxidoreductase
- HTH-type transcriptional regulator Rv0880
- Alanine dehydrogenase
- Probable short-chain type dehydrogenase/reductase
- Conserved protein
- Ribonuclease VapC30
Sequence:
MIILFRGHMRDNSTEHKTRRAASSKDVRPAELDEVDRRILSLLHGDARMPNNALADTVGIAPSTCHGRVRRLVDLGVIRGFYTDIDPVAVGLPLQAMISVNLQSSARGKIRSFIQQIRRKRQVMDVYFLAGADDFILHVAARDTEDLRSFVVENLNADADVAGTQTSLIFEHLRGAAPI
Protein: NAD(P) transhydrogenase subunit beta (EC 7.1.1.1) (Nicotinamide nucleotide transhydrogenase subunit beta) (P96834)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}.
Interaction partners:
- proton-translocating NAD
- NAD
- Probable soluble pyridine nucleotide transhydrogenase
- Glutamine-dependent NAD
- NAD kinase
- Alanine dehydrogenase
- Probable nicotinate-nucleotide adenylyltransferase
- NAD-dependent protein deacylase
- NAD-capped RNA hydrolase NudC
- Possible transcriptional regulatory protein NadR
Sequence:
MNLHYLVEILYIISFSLFIYGLMGLTGPKTAVRGNLIAAAGMTIAVAATLVMIRHTSQWPLIIAGLVVGVVLGVPPARLTKMTAMPQLVAFFNGVGGGTVALIALSEFIDTTGFSAFQHGESPTVHIVVASLFAAIIGSISFWGSIVAFGKLQEIISGRPIGLGKAQQPINLLLLAVAVAAAVVIGLHAHPGSGGVALWWMIGLLVAAGVLGLMVVLPIGGADMPVVISMLNAMTGLSAAAAGLALNNTAMIVAGMIVGASGSILTNLMAKAMNRSIPAIVAGGFGGGGVAPSGGGDDKHVKATSAADAAIQMAYANQVIVVPGYGLAVAQAQHAVKDLATLLEDRGVPVKYAIHPVAGRMPGHMNVLLAEAEVDYDAMKDMDDINDEFARTDVTIVIGANDVTNPAARNETSSPIYGMPILNVDKSRSVIVLKRSMNSGFAGIDNPLFYADGTTMLFGDAKKSVTEVSEELKAL