wanglab/gogpt-training-data huggingface dataset:
Protein: Bonus, isoform C (A0A0B4KGE5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Histone deacetylase HDAC1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 homolog
- Cell division cycle protein 27 homolog
- ADD domain-containing protein 1, isoform A
- Anaphase-promoting complex subunit 4
- Anaphase promoting complex subunit 7, isoform A
- Cell division cycle 16
- Anaphase-promoting complex subunit 5
- Shattered
- EG:133E12.4 protein
Sequence:
MDMDLEQLKNDFLPLIAGIKQEQLDAVPTDALPQMSTPNTASGAPTTSSLSSSSLSLSNPCDSAEKRSESNSSASAKFTLFKCVYCAQLLGSNDRPKLLECLHVACAQCVSTKFSELDRSLPPLIHCPVCDNASQQEFIVDNQFLIEQCTAGDSGDGVGLLGLTGEGQKSSAAASIQCSSCSDGAVATSWCVDCSEYICDSCVQAHQRLKITKDHTIKPKDEANNEQLAGAAGVDKLHMCQLHPQEKLSLFCETCDKLTCRDCQLSDHRDHKYKFAHEIATESRQALSTLVSEINYKRFLLSSATKVIDDRQQLIHDKKKDLIKEITAMAVKITNTVNTRGKQLIMRLNEVCDSKLKVLVEKKETLQLLSDNTDHCIDFMQNALEKGSDFAILSSKKSLVRHLQKLKCQRADIPNPEIPVRIQVQLNQVSDLQKVISQLGIIIVDGKPYPPTPSPNGTPQPQHPPRQPPSPNMAPPLRPGLPPGMPAGLSPNGPPVNFGPQNGPPLYSNAAQQQFNNLSMSRSFPGDGSGKVRFGGMPPVGMQRHGQPHVSSSTHPQNMDISLRGLLNNQAAQSPNAHMAFNGPPSYPGGPQGAPAPAHQPMGPQMRPHFMPGQQGFSQGGGPGGGPRDANFMNSNARFQSQYQRMANHAQQAAAAAAMAGAAGGGGGQIPSPGALQRPQMMSNPMQNVSAMQNSLGFHGSQAGFNTGPPQTSPQLGGGGMHSLAKWHIPQSAQQSNMCSQQGPLLPFANGRQTSENFKISLKSPNTLKNSTPPSLGGGGAGHQGHGNGSSSAQLNAAALGLGPAVSILSNVTSTNPKTPSPSTHENTKDFTEPIDKVRDDSINDLIATIAKLDSNGVQVLPEGRTKTTSPQVHSSTDLSNTQEVNNKNEQKDDPNEDWCAVCLDGGELMCCDKCPKVFHQNCHIPAISSLPDESESWQCLLCVNIKELTKTEGSEKSSSGELSALELRILQRICLELYCQYEQSLNFREPESPANTSYYEIVSSPMSLDVIRTRLDPSSPNHYKDIAGFVSDVRLIFSNTYLFYQEDTKTYSNAKYLENFFEEQLAKWLPQFEGTKPQGKRNTSNSPALLGVNATGSPSPIENGRKSCGSASLGDSDGACLPAKRARRSAHEXNELMPGGKGTDGEQQAETGQERRQEEQQQLPAFLEEMDLEMPQRPHSLGSSVIQESADYVLQLLHAYAAAFGL
Protein: Sushi repeat-containing protein SRPX2 (B5DF94)
Organism: Rattus norvegicus (Rat)
Function: Acts as a ligand for the urokinase plasminogen activator surface receptor. Plays a role in angiogenesis by inducing endothelial cell migration and the formation of vascular network (cords). Involved in cellular migration and adhesion. Increases the phosphorylation levels of FAK. Interacts with and increases the mitogenic activity of HGF (By similarity). Promotes synapse formation.
Subcellular location: Secreted {ECO:0000250|UniProtKB:O60687}. Cytoplasm {ECO:0000250|UniProtKB:O60687}. Cell surface {ECO:0000269|PubMed:24179158}. Synapse {ECO:0000269|PubMed:24179158}.
Interaction partners:
- Olfactomedin-like protein 1
Sequence:
MKTGSLTQRGALLLLLLLAPAVTPTWYAGSGYSPDESYNEVYAEEVPDTRALDYRVPRWCYTLNIQDGEATCYSPRGGNYHSSLGTRCELSCDRGFRLIGRKSVQCLPSRRWSGTAYCRQMRCHTLPFITSGTYTCTNGMLLDSRCDYSCSSGYHLEGDRSRICMEDGRWSGGEPVCVDIDPPKIRCPHSREKIAEPEKLTARVYWDPPLVKDSADGTITRVTLRGPEPGSHFPEGEHVIRYTAYDRAYNRASCKFIVKVQVRRCPILKPPQHGYLTCSSAGDNYGAICEYHCDGGYERQGTPSRVCQSSRQWSGSPPVCTPMKINVNVNSAAGLLDQFYEKQRLLIVSAPDPSNRYYKMQISMLQQSTCGLDLRHVTIIELVGQPPQEVGRIREQQLSAGIIEELRQFQRLTRSYFNMVLIDKQGIDRERYMEPVTPEEIFTFIDDYLLSNQELARRAEQRDVCE
Protein: malate dehydrogenase (EC 1.1.1.37) (Q4QDF0)
Organism: Leishmania major
Interaction partners:
- Citrate synthase
- Probable citrate synthase, mitochondrial
- phosphoenolpyruvate carboxykinase
- Fumarate hydratase 1, mitochondrial
- phosphoenolpyruvate carboxykinase
- Fumarate hydratase 2
- Putative malic enzyme
- Transaminase A
- Aspartate aminotransferase
- Adenylosuccinate lyase
Sequence:
MVNVCVVGAAGGIGQSLSLLLVRQLPYGSTLSLFDVVGAAGVAADLSHVDNAGVQVKFAEGKIGHKRDPALAELAKGVDVFVMVAGVPRKPGMTRDDLFKINAGIILDLVLTCASSSPKAVFCIVTNPVNSTVAIAAEALKSLGVYDRNRLLGVSLLDGLRATCFINEARKPLVVSQVPVVGGHSDTTIVPLFYQLPGPLPEQATLDKIVKRVQVAGTEVVKAKAGRGSATLSMAEAGARFALKVVEGLTGTGNPLVYAYVDTDGQHETTFLAIPVVLGMNGIEKRLPIGPLHSTEETLLKAALPVIKKNIVKGSEFARSHL
Protein: Myristylated membrane protein (H9XFG5)
Organism: Rana grylio virus
Interaction partners:
Sequence:
MSIIGATRLQNDKSDTYSAGPCYAGGCSAFTPRGTCGKDWDLGEQTCASGFCTSQPLCARIKKTQVCGLRYSSKGKDPLVSAEWDSRGAPYVRCTYDADLIDTQAQVDQFVSMFGESPSLAERYCMRGVKNTAGELVSRVSSDADPAGGWCRKWYSAHRGPDQDAALGSFCIKNPGAADCKCINRASDPVYQKVKTLHAYPDQCWYVPCAADVGELKMGTQRDTPTNCPTQVCQIVFNMLDDGSVTMDDVKNTINCDFSKYVPPPPPPKPTPPTPHTPLTPLTPPTPPTPPTPPTPRPVHNRKVMFFVAGAVLVAILISTVRW
Protein: Type 2 glycosyltransferase (EC 2.4.1.-) (F9WWD1)
Organism: Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch fungus) (Septoria tritici)
Function: Glycosyltransferase involved in the maintenance of the outermost surface of the fungal cell wall. Likely functions in the synthesis of a currently unknown, potentially minor but widespread, extracellular or outer cell wall polysaccharide which plays a key role in facilitating many interactions between plants and fungi by enabling hyphal growth on solid matrices.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLSILGWFWAFVSAFVLRYLRTIVNCISNWTYRPIPIPDNPTYGPQDVTIILPTIAQGGEELEGTLRTCLRTEPYEIILVTIDANVKNLTLLAKKINSKKIRVLSVREANKRRQMCRAIPEVSTRITIFVDDDVIWPVKLLPWILAPFENPQMGGVGTSQRRVRPEKMNAWVFLNMGYLERRNWDCSACLHIDGGLPCLSGRTAAYRTSILQDDAFTHGFTNETWRTMQLNADDDNFITRWLYSHNWKIGMQYHKEAEVLTTLEAGPKYLSQCLRWVRSNWRSNIKSMFVERHYWYTQLWTTYSCLQTTITAWALPWDAFLFYSLHKASTDWSDDSRKMAFTLLFLWIFGFTKNVKLWGHYFRYPVDVIYIPVHIAFGYFHGLIKFWGLVTLSETTWGSRDGADSSELNRIRMMPLPPYGSTTPDGRKSETFEYMQEMPLIDQLPAYDTHDRHPPLSNMTSTITTTTPFHD
Protein: Myosin heavy chain kinase B (MHCK-B) (EC 2.7.11.7) (P90648)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes its autophosphorylation, which is needed for enzymatic activity and phosphorylates myosin II heavy chain at a threonine in the C-terminal tail region. This phosphorylation is critical in regulating the assembly and disassembly of myosin II filament. Participates in control of myosin localization.
Interaction partners:
- Myosin-2 heavy chain
Sequence:
MIFKVWFSYEDEEVELSELTNDTTVSAIRKILHEGKIFRFPYGTSQTDLQIGKMLPSGSGGGATADSKFEKFKARNTLADIQYKVGDTLYVRVKKSKPTNDSLLPTLNIAFLDGSERAIKWEYDPYTTTAQWTCTATLVKVEPVPFAEGAFRKAYHTLDLSKSGASGRYVSKIGKKPTPRPSYFEDVKMQMIAKKWADKYNSFKPPKKIEFLQSCVLEFVDRTSSDLICGAEPYVEGQYRKYNNNSGFVSNDERNTPQSFSHFTYEHSNHQLLIIDIQGVGDHYTDPQIHTYDGVGFGIGNLGQKGFEKFLDTHKCNAICQYLNLQSINPKSEKSDCGTVPRPDLIFPDTSERDNNNNNNNNNNNNNNNNNNNSNNNNNNNSSISKSLVEISSGSKERNDRDSPSRQLFVSNDGNTLNTNKERSKSKSIDLEKPEILINNKKKESINLETIKLIETIKGYHVTSHLCICDNLLFTGCSDNSIRVYDYKSQNMECVQTLKGHEGPVESICYNDQYLFSGSSDHSIKVWDLKKLRCIFTLEGHDKPVHTVLLNDKYLFSGSSDKTIKVWDLKTLECKYTLESHARAVKTLCISGQYLFSGSNDKTIKVWDLKTFRCNYTLKGHTKWVTTICILGTNLYSGSYDKTIRVWNLKSLECSATLRGHDRWVEHMVICDKLLFTASDDNTIKIWDLETLRCNTTLEGHNATVQCLAVWEDKKCVISCSHDQSIRVWGWN
Protein: Emerin (Q63190)
Organism: Rattus norvegicus (Rat)
Function: Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells.
Subcellular location: Nucleus inner membrane {ECO:0000250|UniProtKB:P50402}; Single-pass membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250|UniProtKB:P50402}. Nucleus outer membrane {ECO:0000250}. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Barrier-to-autointegration factor
- Prelamin-A/C
- Barrier-to-autointegration factor-like protein
- Sad1 and UNC84 domain containing 1
- LIM domain 7
- Lamin-B1
- Delta
- Sad1 and UNC84 domain containing 2
- Catenin beta-1
- Lamin B2
Sequence:
MDDYAVLSDTELAAVLRQYNIPHGPILGSTRKLYEKKIFEYETQRRRLSPPSSSSSSFSYRFSDLDSASVDSDMYDLPKKEDALLYQSKDYNDDYYEESYLTTRTYGEPESVGMSKSFRRPGTSLVDADDTFHHQVRDDIFSSSEEEGKDRERPIYGRDSAYQSIAEYRPISNVSRSSLGLSYYPRSSTSSVSSSSSSPSSWLTRRAIRPEKQAPTAALGQDRQVPLWGQLLLFLAFATFLLFVYYSIQAQEGNPFWMDP
Protein: Aspartyl beta-hydroxylase, isoform L (EC 1.14.11.16) (A0A0B4KFS5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGDVQPRKRKDKRRKRDDDESSHGVHITKMGNEDLHLHVHHDHGTGGHWCAKIIFFALMAVLLGLVGLIIMENRGLEDLDTPLSESRFSKVFDGWVDEHRDEHDGHDVQEPSGEALDDHDEHDDHDDHEDEEPLTEELEEELEEEEEPTEEDEPAADEEYEEDEDEENNAGENITAEDAEEEEEEEDNDDEGTVEATVEATTEATTEATGEYEAEEDDEDEAAADDDAVESTEAPLSKAEEQEDDEDEDEEEQEIEESVEPERSQYAAQSAPAKDNNDDDDDDDQDKNDADDGDDDEFESLAQQFENDPEDTVPAKAVESEEQDQDQADEEEPKEEGSSWLASLAVKFGVGVALALVSRLVLIRKSPNTTEDEPAPETIFRRRLTIATAEDHIPDDVEELPPLDDEYSEEEIEIEEEIEVEISDIEEEEEEVRHDNDDNVASMASYVPETFEQLSAMYKYAQEPTKDAKPEQKEKEPEKPVGHSDIYVEYEDGAIEDYEHDGVSDEEITDEEDEISDVDDADLMNRLEAKYGRLPVKEFESDPDSDDPSWTQIKPKEAAPAPAEKEDPFEQELRKANEEMIRENYAQALRSFNTLTTNFAHEPSAHLGRARLLELLAKKERSNQRLWEAIDAYKRYLAFGELVASNQEFQTAGESCIENLRFLGHHRQATTIHELLINRLPEDPRLRNQLSLTYLMVNNLQQVEKVAVETLKLWPNNAVAQLHYGLALRQFHADYAKALPYLKYAVESGEEGTQEAFFYLSLGETMQRLSMKSEALEVYGKGVAKGFFASLYQRSLYNEPRLRAQPFWQPKETGYERQLEKLTLNWRAIRDEGLALLGRSGFFEDEAELLRDKGVWQQYELYAQGRRVKDNCRRAPITCSLLEEFPESAGCRRGQVKFSVMQAKTHVWPHCGPTNCRLRAHLTLAAPEPEKASLRVAEQERTWREGELFIFDDSFEHEVWHNGSQSRLVLILDMWHPQLSAAQRRSLSPI
Protein: Outer membrane protein W (P0A915)
Organism: Escherichia coli (strain K12)
Function: Acts as a receptor for colicin S4.
Subcellular location: Cell outer membrane.
Interaction partners:
- Outer membrane protein A
- Outer membrane protein X
- Long-chain fatty acid transport protein
- Outer membrane porin C
- Outer membrane protein assembly factor BamA
- Outer membrane porin F
- Oxygen-independent coproporphyrinogen III oxidase
- Outer membrane protein TolC
- Maltoporin
- Nucleoside-specific channel-forming protein Tsx
Sequence:
MKKLTVAALAVTTLLSGSAFAHEAGEFFMRAGSATVRPTEGAGGTLGSLGGFSVTNNTQLGLTFTYMATDNIGVELLAATPFRHKIGTRATGDIATVHHLPPTLMAQWYFGDASSKFRPYVGAGINYTTFFDNGFNDHGKEAGLSDLSLKDSWGAAGQVGVDYLINRDWLVNMSVWYMDIDTTANYKLGGAQQHDSVRLDPWVFMFSAGYRF
Protein: Thyroid hormone receptor beta (Nuclear receptor subfamily 1 group A member 2) (c-erbA-2) (c-erbA-beta) (P10828)
Organism: Homo sapiens (Human)
Function: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine.
Subcellular location: Nucleus.
Interaction partners:
- Retinoic acid receptor RXR-alpha
- Nuclear receptor coactivator 2
- Nuclear receptor coactivator 1
- Nuclear receptor corepressor 1
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Nuclear receptor corepressor 2
- Thioredoxin reductase 2, mitochondrial
- Thyroid hormone receptor alpha
- Nuclear receptor coactivator 3
- Mitogen-activated protein kinase 3
Sequence:
MTPNSMTENGLTAWDKPKHCPDREHDWKLVGMSEACLHRKSHSERRSTLKNEQSSPHLIQTTWTSSIFHLDHDDVNDQSVSSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYEGKCVIDKVTRNQCQECRFKKCIYVGMATDLVLDDSKRLAKRKLIEENREKRRREELQKSIGHKPEPTDEEWELIKTVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVNAPEGGKVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVRYDPESETLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGMSLSSFNLDDTEVALLQAVLLMSSDRPGLACVERIEKYQDSFLLAFEHYINYRKHHVTHFWPKLLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFED
Protein: Evasin P1078 (A0A0K8R726)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6, CXCL11 and CXCL13.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MAFNTITFLQWAVFVAILFNMNLHSASAGSKGSSAQQSSHDSIKAEFCETNCTMKTGGKWTQCHGGCFCVHVGNETVGRCIKLDGDYDYPSSKHEE
Protein: H2.0-like homeo box 1 (Drosophila) (Q6NY96)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MKKPSFCIADILHVGDAENIQGSSSLMAHIGVRAQVHSSGSPLRPSPVTPDARLHPAYHRHGIHLTSRAAINAPPPTSKDLKFGIDRILSTDFEPKSKESPSLRDLTSIVSPNRQSAVHVSASPYFASIDPTMSETSSLMGSIGNAARQSGQHQFQDTFPGPYAVLSKDTMPQTYKRKRSWSRAVFSNLQRKGLEKRFEIQKYVTKPDRKQLAAMLGLTDAQVKVWFQNRRMKWRHSKEAQAQKDKEKEQPDKSAAETEQKERDDSECETEPSESEFEDGPEDKSDVDISDLNKASVIIPGPLPVSTQDTSSTNPTTEPNTATQMLL
Protein: Heterogeneous nuclear ribonucleoprotein A1-like 3 (Heterogeneous nuclear ribonucleoprotein A1 pseudogene 48) (A0A2R8Y4L2)
Organism: Homo sapiens (Human)
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein A1
Sequence:
MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPDAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFEGRSSGPHGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF
Protein: C11.1, isoform A (C11.1, isoform B) (LD28902p) (Q9W350)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDGRGVGGGGSGAATGGGSANNKSAAGNSAATGNADASTATAAPNDKPTILEGVLHNIFDGLMDKEEQVRIAMQQAIVKILETHPERAAEILSEHRSQQPKMTDQTVAMLLDCIRRVVGAETPLPPAANQKLIDLALQELTKNPEHLPLIQNPAQRILVAIGRSSPESCEQVMEALQEKGTSTEGVAHFMLMQCLGLLATENPAGVVPHIKAILSRSQPHLVGIRQDHIKQAHAYAIGRFSEALLEESGKKEEENCSTEISVAYDVLFNQWLHSREPKVCVEILQALSSMYPLLPKDRIQDQAARLVPQILALYRRSVDRNAVTQFLCSVLKTNLALNATVLDGIIDVLVTHLFDLVCVYPDYEKPQTVKGHYEVLRCFHLLAGHQPYSTRIMDTLLIHLRNNSERERMKSLLILTHLLNSCAGNIENRIPATIECLKQLILSERGIKMKLTLLKTIVALAQKSHIRDKEFVWFVVRHSCRFSKPSQEHGSQEEHANLVLSCENTLYMLASTVGTLDELLKRELLNYLILLDYTDICGNLAKCLASLFAKSPHIEYDIAGDDAATEQATPESMGAAGEDRSVIKRGKVMVPGAETIYARCLALLGNQQCIKRCSNILSFLRYYHPQVNPALEELWERKIPDLLLQINRESAYRQLLHDFVLETNEFLGGLDENFAQRLASKLADQMYLYPMQLPHSEWHLPDLSAERGMLLQAVALTLLQVTDVACIHTKIDLIVTTARQERLDKHVKHADYEKRIEPCARALGYISRQHLGHLIKKLTELAQVGGRKHSTGFFSNLHFIKDTHKELENYKSNLLVVKAFGRIMDEADPLQSIQHLDEDDTLLGFLIQQLAVHKDQTIMSAILQTLLSICNQLIATKEQLPAPLRHRKQIMETVFNIPIEAPFHDLPLLPTILKLGTDFIRIGGPDTEECVDGGVIFEIACRNFFGCAQQLKMKFDSQEEDERNSFLAKHLNESLPQLNALVRAIVELDASPATLDLIIGILEGWTRDRNSEVRICASHVFNNTLDVYIKSMKIGCEAPSKFNQTGQMLGKIVPRCIDSNGTVRQVSVEILQKTLEIACIYETLTIASIDSTADWLKEIETIKEHIITDEPKQIYNLAGDIAKIIALRISSFQYLQFCKTLLHSLRDPEQSSTIGASVVLKFFIQQKGSELFHAIPDLVRDSLLALRVCEVPRAKSGVLKALVALTKHHPKLVCAEMLSQPLPYDPNLVEYWHLVCNDPELTGLTLDNFLQLLSGASLQEGGQDASLSERQKLASGQPFAIFCALHEMLPCKDIKGQLETRFADMFCMLLTSLSSYTNLAAPNPINNASLSPNQTQSGKTKFGFVPNKELIKLNPCQIALETFQAFLTNLEMEQIASVLTVNTQLASSADWHNYIELLTPMAIGLGQQLQLGSPQMRQLVNSLSKYVASPYDGQRVAAVGIFSRLVPLKPTGELAASILLHLGAALSDPNAVVRGLSIQGMGYVGQLGEKEAKRYSETAIGALLKGVDDPVGDCLINIPLESMRGLSGILRALPSERVEPFHVSLAIRIRPFLGNYALEMREAAIQLFGDICEGKHDDGSSSPTSSMEALREQLIANLFPLLLHLSESEVAIASACRGTLQRVCRLLTAPRVVEMAEQQLGEERGHQLNYSSFVLEFVKTIALELTDHIQDFIDSCLPQLRSQWPEVRGSAAIVIGILHNFLSERNVQTETVASKIAVLLKDEQALVRMRAATALGYFFGDI
Protein: ATP synthase subunit a, chloroplastic (ATP synthase F0 sector subunit a) (F-ATPase subunit IV) (P0C2Y5)
Organism: Oryza sativa (Rice)
Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01393}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01393}.
Interaction partners:
Sequence:
MNIIPCSIKTLKGLYDISGVEVGQHFYWQIGGFQIHAQVLITSWVVITILLGSVIIAVRNPQTIPTDGQNFFEYVLEFIRDLSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGALLPWKIIQLPHGELAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYFEKYIKPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGHH
Protein: Extracellular fatty acid-binding protein (Ex-FABP) (Lipocalin Q83) (Q9I9P7)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Function: Siderocalin-like lipocalin tightly binding a variety of bacterial ferric siderophores, also binds long-chain unsaturated fatty acids such as linoleic acid, oleic acid, arachidonic acid and, with a lower affinity, long chain saturated fatty acids such as steraic acid. May act as an antibacterial factor, through dual ligand specificity, both as a siderophore-sequestrating molecule and a lysophosphatidic acid (LPA) sensor.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MRTLALSLGLALLCLLHAKAAATVPDRSEIAGKWYVVALASNTEFFLREKDKMKMAMARISFLGEDELKVSYAVPKPNGCRKWETTFKKTSDDGEVYYSEEAKKKVEVLDTDYKSYAVIYATRVKDGRTLHMMRLYSRSPEVSPAATAIFRKLAGERNYTDEMVAMLPRQEECTVDEV
Protein: Pleckstrin homology domain-containing family A member 8 (PH domain-containing family A member 8) (Phosphatidylinositol-four-phosphate adapter protein 2) (FAPP-2) (Phosphoinositol 4-phosphate adapter protein 2) (D2KC46)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Cargo transport protein that is required for apical transport from the trans-Golgi network (TGN). Transports AQP2 from the trans-Golgi network (TGN) to sites of AQP2 phosphorylation. Mediates the non-vesicular transport of glucosylceramide (GlcCer) from the trans-Golgi network (TGN) to the plasma membrane and plays a pivotal role in the synthesis of complex glycosphingolipids. Binding of both phosphatidylinositol 4-phosphate (PIP) and ARF1 are essential for the GlcCer transfer ability. Also required for primary cilium formation, possibly by being involved in the transport of raft lipids to the apical membrane, and for membrane tubulation.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q96JA3}. Membrane {ECO:0000250|UniProtKB:Q96JA3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96JA3}. Note=Binds through its PH domain to PtdIns(4)P and ARF1, and subsequently localizes to TGN exit sites. {ECO:0000250|UniProtKB:Q96JA3}.
Interaction partners:
- MNAT1 component of CDK activating kinase.
- Uncharacterized protein
- Transmembrane O-mannosyltransferase targeting cadherins 4.
- Glucosylceramidase beta 2.
Sequence:
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTRMDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSELRLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSELLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELNSCENGSLHMEINDGEEILMKNKSSLYLKPEIDCSISSEENTDDNITVQGEIMKEEGEDNLGNHDSSLAQPASDSSSSPPESHWEEGQEIIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMDLVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLTEVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRAAPSYEDFVAALTIKEGDHQKAAFSVGMQRDLSLYLPAMEKQLAILDTLYEVHGLESDEVV
Protein: SURF1-like protein (A1L248)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}. Mitochondrion inner membrane {ECO:0000256|RuleBase:RU363076}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363076}.
Interaction partners:
Sequence:
MSSFRLMLMISNQTFKILRCSALFSPRRTLFVTRQSLFRRQDAPVLRYNLARFSQQSTSTVEGTKKGEDTFLKWFLLLIPVTTFCLGTWQVKRRKWKLELISELQSLTTSVPIPLPVDTMEIKQLEYRRVTVRGHFDHSKELYILPRSPVDPEREAREAGRISSSGESGANVITPFFCTDLGITILVNRGYVPKNKIKPETRTKGQVIEDVDLVGVVRLTEQRKPFVPENNVEANRWHYRDLEAMAKVTGAEEIFIDAVLDSTVPGGPIGGQTRVTLRNEHLQYVITWYGLCAATSYMWYAKFIMRIAL
Protein: MHC class II transactivator (CIITA) (EC 2.3.1.-) (EC 2.7.11.1) (P33076)
Organism: Homo sapiens (Human)
Function: Essential for transcriptional activity of the HLA class II promoter; activation is via the proximal promoter. No DNA binding of in vitro translated CIITA was detected. May act in a coactivator-like fashion through protein-protein interactions by contacting factors binding to the proximal MHC class II promoter, to elements of the transcription machinery, or both. Alternatively it may activate HLA class II transcription by modifying proteins that bind to the MHC class II promoter. Also mediates enhanced MHC class I transcription; the promoter element requirements for CIITA-mediated transcription are distinct from those of constitutive MHC class I transcription, and CIITA can functionally replace TAF1 at these genes. Activates CD74 transcription. Exhibits intrinsic GTP-stimulated acetyltransferase activity. Exhibits serine/threonine protein kinase activity: can phosphorylate the TFIID component TAF7, the RAP74 subunit of the general transcription factor TFIIF, histone H2B at 'Ser-37' and other histones (in vitro). Has antiviral activity against Ebola virus and coronaviruses, including SARS-CoV-2. Induces resistance by up-regulation of the p41 isoform of CD74, which blocks cathepsin-mediated cleavage of viral glycoproteins, thereby preventing viral fusion.
Subcellular location: Nucleus {ECO:0000269|PubMed:11172716, ECO:0000269|PubMed:23007646}. Nucleus, PML body {ECO:0000269|PubMed:23007646}. Note=Recruited to PML body by PML. {ECO:0000269|PubMed:23007646}.
Interaction partners:
- DNA-binding protein RFX5
- DNA-binding protein RFXANK
- Regulatory factor X-associated protein
- Cyclic AMP-responsive element-binding protein 1
- Nuclear transcription factor Y subunit gamma
- Nuclear transcription factor Y subunit alpha
- MHC class II regulatory factor RFX1
- Signal transducer and activator of transcription 1-alpha/beta
- Nuclear transcription factor Y subunit beta
- Baculoviral IAP repeat-containing protein 1
Sequence:
MRCLAPRPAGSYLSEPQGSSQCATMELGPLEGGYLELLNSDADPLCLYHFYDQMDLAGEEEIELYSEPDTDTINCDQFSRLLCDMEGDEETREAYANIAELDQYVFQDSQLEGLSKDIFKHIGPDEVIGESMEMPAEVGQKSQKRPFPEELPADLKHWKPAEPPTVVTGSLLVRPVSDCSTLPCLPLPALFNQEPASGQMRLEKTDQIPMPFSSSSLSCLNLPEGPIQFVPTISTLPHGLWQISEAGTGVSSIFIYHGEVPQASQVPPPSGFTVHGLPTSPDRPGSTSPFAPSATDLPSMPEPALTSRANMTEHKTSPTQCPAAGEVSNKLPKWPEPVEQFYRSLQDTYGAEPAGPDGILVEVDLVQARLERSSSKSLERELATPDWAERQLAQGGLAEVLLAAKEHRRPRETRVIAVLGKAGQGKSYWAGAVSRAWACGRLPQYDFVFSVPCHCLNRPGDAYGLQDLLFSLGPQPLVAADEVFSHILKRPDRVLLILDGFEELEAQDGFLHSTCGPAPAEPCSLRGLLAGLFQKKLLRGCTLLLTARPRGRLVQSLSKADALFELSGFSMEQAQAYVMRYFESSGMTEHQDRALTLLRDRPLLLSHSHSPTLCRAVCQLSEALLELGEDAKLPSTLTGLYVGLLGRAALDSPPGALAELAKLAWELGRRHQSTLQEDQFPSADVRTWAMAKGLVQHPPRAAESELAFPSFLLQCFLGALWLALSGEIKDKELPQYLALTPRKKRPYDNWLEGVPRFLAGLIFQPPARCLGALLGPSAAASVDRKQKVLARYLKRLQPGTLRARQLLELLHCAHEAEEAGIWQHVVQELPGRLSFLGTRLTPPDAHVLGKALEAAGQDFSLDLRSTGICPSGLGSLVGLSCVTRFRAALSDTVALWESLQQHGETKLLQAAEEKFTIEPFKAKSLKDVEDLGKLVQTQRTRSSSEDTAGELPAVRDLKKLEFALGPVSGPQAFPKLVRILTAFSSLQHLDLDALSENKIGDEGVSQLSATFPQLKSLETLNLSQNNITDLGAYKLAEALPSLAASLLRLSLYNNCICDVGAESLARVLPDMVSLRVMDVQYNKFTAAGAQQLAASLRRCPHVETLAMWTPTIPFSVQEHLQQQDSRISLR
Protein: Prolactin (PRL) (P14676)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted.
Interaction partners:
- Prolactin receptor
- Uncharacterized protein.
- Thyrotropin subunit beta
- Uncharacterized protein.
- Somatotropin
- Growth hormone receptor
- VIP peptides
- Follitropin subunit beta
- Pituitary-specific positive transcription factor 1
- Pro-thyrotropin-releasing hormone
Sequence:
MSNRGASLKGLFLAVLLVSNTLLTKEGVTSLPICPIGSVNCQVSLGELFDRAVKLSHYIHYLSSEIFNEFDERYAQGRGFITKAVNGCHTSSLTTPEDKEQAQQIHHEDLLNLVVGVLRSWNDPLIHLASEVQRIKEAPDTILWKAVEIEEQNKRLLEGMEKIVGRVHSGDAGNEIYSHWDGLPSLQLADEDSRLFAFYNLLHCLRRDSHKIDNYLKVLKCRLIHDSNC
Protein: 2,5-didehydrogluconate reductase A (DkgA) (2,5-diketo-D-gluconate reductase A) (2,5-diketo-D-gluconic acid reductase (EC 1.1.1.274)) (E2D2R3)
Organism: Escherichia coli
Interaction partners:
Sequence:
MANPTVIKLQDGNVMPQLGLGVWQASNEEVITAIQKALEVGYRSIDTAAAYKNEEGVGKALKNASVNREELFITTKLWNDDHKRPREALLDSLKKLQLDYIDLYLMHWPVPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVWDFRLDKDELGEIAKLDQGKRLGPDPDQFGG
Protein: Afadin/alpha-actinin-binding protein (F4KAN9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Selenoprotein O
- Pentatricopeptide repeat-containing protein At4g35850
- At5g07590
- At2g17975
- Omega-amidase, chloroplastic
- Protein PEP-RELATED DEVELOPMENT ARRESTED 1, chloroplastic
- FKBP12-interacting protein of 37 kDa
- Eukaryotic translation initiation factor 3 subunit H
Sequence:
MPANDAEYDLKVLSQSASAGDYTFANEDNLEHCTKYLNQTMVTFGFPASLDLFSNDPVSISRTCNCMYSLLQQRQRDIEFRESANELRQRQQSDIARLEAKVERLEALLQQKDREIATITRTEAKNTAALKSQIEKLQQERDEFQRMVIGNQQVKAQQIHEMKKKEKDYIKLQERLNQVLMEKKKESRSGMEIMNLLQKEGRQRGTWNGKKTDTDFYKKIVDAYEAKNQELMAENTSLRALLRSMQTDMRDFLNAPNGSATLAGSEKREADPSQSPLGGKTDVFDLPYRMARGQIEESLRTKMASIKESMVQLQDAPKRASVTSEATERELELEAQLVEARSIIQEQESIMSKHLPKSEQRRESVASLAAEGLDNASSHAHMKSAPSLRLY
Protein: methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 2) (3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta) (D6RD67)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
VKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTVKQD