wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-dependent RNA helicase DDX39A (EC 3.6.4.13) (DEAD box protein 39) (Nuclear RNA helicase URH49) (O00148)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing. Required for the export of mRNA out of the nucleus.
Subcellular location: Nucleus {ECO:0000269|PubMed:21859714, ECO:0000269|PubMed:32393512, ECO:0000269|PubMed:33941617, ECO:0000269|PubMed:38225262}. Cytoplasm {ECO:0000269|PubMed:21859714, ECO:0000269|PubMed:37949067}. Note=Can translocate to the cytoplasm in the presence of MX1 (PubMed:21859714). Accumulates in the cytoplasm upon infection with chikungunya virus (PubMed:37949067). {ECO:0000269|PubMed:21859714, ECO:0000269|PubMed:37949067}.
Interaction partners:
- SAP domain-containing ribonucleoprotein
- THO complex subunit 4
- THO complex subunit 2
- Spliceosome RNA helicase DDX39B
- THO complex subunit 1
- Polymerase delta-interacting protein 3
- THO complex subunit 7
- Chromatin target of PRMT1 protein
- THO complex subunit 5
- UAP56-interacting factor
Sequence:
MAEQDVENDLLDYDEEEEPQAPQESTPAPPKKDIKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQIEPVNGQVTVLVMCHTRELAFQISKEYERFSKYMPSVKVSVFFGGLSIKKDEEVLKKNCPHVVVGTPGRILALVRNRSFSLKNVKHFVLDECDKMLEQLDMRRDVQEIFRLTPHEKQCMMFSATLSKDIRPVCRKFMQDPMEVFVDDETKLTLHGLQQYYVKLKDSEKNRKLFDLLDVLEFNQVIIFVKSVQRCMALAQLLVEQNFPAIAIHRGMAQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNVAELPEEIDISTYIEQSR
Protein: Metallo-beta-lactamase type 2 (EC 3.5.2.6) (B2 metallo-beta-lactamase) (Beta-lactamase II) (Carbapenem-hydrolyzing metallo-beta-lactamase) (Metallo-beta-lactamase type II) (P26918)
Organism: Aeromonas hydrophila
Function: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. It is able to hydrolyze penicillin and imipenem, but is much less active against cephalothin, cefotaxime, meropenem and ceftazidime.
Subcellular location: Periplasm {ECO:0000305|PubMed:1856163}.
Interaction partners:
Sequence:
MMKGWMKCGLAGAVVLMASFWGGSVRAAGMSLTQVSGPVYVVEDNYYVQENSMVYFGAKGVTVVGATWTPDTARELHKLIKRVSRKPVLEVINTNYHTDRAGGNAYWKSIGAKVVSTRQTRDLMKSDWAEIVAFTRKGLPEYPDLPLVLPNVVHDGDFTLQEGKVRAFYAGPAHTPDGIFVYFPDEQVLYGNCILKEKLGNLSFADVKAYPQTLERLKAMKLPIKTVIGGHDSPLHGPELIDHYEALIKAAPQS
Protein: Uncharacterized protein YqbD (P45920)
Organism: Bacillus subtilis (strain 168)
Interaction partners:
- Putative prophage capsid protein YqbE
- Uncharacterized protein YqbK
- Uncharacterized protein YqbG
- Uncharacterized protein YqbF
- Uncharacterized protein YqbH
- Uncharacterized protein YqbI
- Uncharacterized protein YqbM
- Uncharacterized protein YqbJ
- Uncharacterized protein YqzN
Sequence:
MPRELVNAKITHVSYVDKAANQKQFFIVKSEKQPDFQKEVRILAKEADEQKLVYGIVYEPDTVDAHGDFMTAAEIEKAAHGFLKDARQIDKQHDFQGGVGEVVESYVAPADFEMNGETIKKGSWVLVTKASEEVWEQIKKGEITGYSMAGTAETIEKQEKPVSQEKTDEKGLFNLLKNFFVGKQQQSYEEPVAKAGRKFSASNLQEIKNAHAALGNLLSQVETKEGEEEMTSEEVTKSIQEALEPIKKRLETLEKEEELNKKDKEKEEETEKEGEKLKKAISEAVQPLADRIEAIEKSRGTSKQTEESGSEQVQKSIWSGLF
Protein: Zinc finger protein 410 (Another partner for ARF 1) (Q86VK4)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds to the sequence motif 5'-CATCCCATAATA-3', and is specifically required to silence expression of fetal hemoglobin in adult erythroid cells. Prevents expression of fetal hemoglobin genes HBG1 and HBG2 through CHD4: acts as a direct transcriptional activator of CHD4, a central component of the NuRD complex that represses transcription of fetal hemoglobin genes HBG1 and HBG2 in erythroid cells. May also activate transcription of matrix-remodeling genes such as MMP1 during fibroblast senescence. May activate transcription of the gap junction gene GJC1, perhaps in response to increasing glucose. However, recent studies suggest that ZNF410 is dedicated to regulate expression of a single gene: CHD4.
Subcellular location: Nucleus {ECO:0000305|PubMed:33301730, ECO:0000305|PubMed:33859416}. Chromosome {ECO:0000269|PubMed:33301730, ECO:0000269|PubMed:33859416}. Note=Directly binds to the sequence motif 5'-CATCCCATAATA-3'. {ECO:0000269|PubMed:33301730, ECO:0000269|PubMed:33859416}.
Interaction partners:
Sequence:
MLSDELESKPELLVQFVQNTSIPLGQGLVESEAKDITCLSLLPVTEASECSRLMLPDDTTNHSNSSKEVPSSAVLRSLRVNVGPDGEETRAQTVQKSPEFLSTSESSSLLQDLQPSDSTSFILLNLTRAGLGSSAEHLVFVQDEAEDSGNDFLSSESTDSSIPWFLRVQELAHDSLIAATRAQLAKNAKTSSNGENVHLGSGDGQSKDSGPLPQVEKKLKCTVEGCDRTFVWPAHFKYHLKTHRNDRSFICPAEGCGKSFYVLQRLKVHMRTHNGEKPFMCHESGCGKQFTTAGNLKNHRRIHTGEKPFLCEAQGCGRSFAEYSSLRKHLVVHSGEKPHQCQVCGKTFSQSGSRNVHMRKHHLQLGAAGSQEQEQTAEPLMGSSLLEEASVPSKNLVSMNSQPSLGGESLNLPNTNSILGVDDEVLAEGSPRSLSSVPDVTHHLVTMQSGRQSYEVSVLTAVNPQELLNQGDLTERRT
Protein: FA complementation group L (H7C1M0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAVTEASLLRQCPLLLPQNRSKTVYEGFISAQGRDFHLRIVLPEDLQLKNARLLCSWQLRTILSGYHRIVQQRMQHSPDLMSFMMELKMLLEVALKNRQELYALPPPPQFYSSLIEEIGTLGWDKLVYADTCFSTIKLKAEDASGREHLITLKLKAKYPAESPDYFVDFPVPFCASWTPQVTDQAKMDVKIAVLPSSLISIYSQFLAAIESLKAFWDVMDEIDEKTWVLEPEKPPRSATARRIALGNNVSINIEVDPRHPTMLPECFFLGADHVVKPLGIKLSRNIHLWDPENSVLQNLKDVLEIDFPARAILEKSDFTMDCGICYAYQLDGTIPDQVCDNSQCGQPFHQICLYEWLRGLLTSRQSFNIIFGECPYCSKPITLKMSGRKH
Protein: Probable helicase (O06359)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- RNA-binding protein KhpA
- Conserved protein similar to jag protein
- ATP-dependent RNA helicase DeaD
- Probable cold shock protein A
- Probable cold shock-like protein B CspB
- Ribonuclease PH
- Ribonuclease J
Sequence:
MASFGSHLLAAAVAGTPPGERPLRHVAELPPQAGRPRGWPEWAEPDVVDAFADRGISSPWSHQAEAAELAYAGRHVVIGTGPASGKSLAYQLLVLNALATDSRARALYLSPTKALGHDQLRAAHALAAAVPRLADVAPTAYDGDSPDEVRRFARERSRWLFSNPEMTHLSVLRNHARWAVLLRNLRFVIVDECHYYRGVFGSNVAMVLRRLLRLCARYSAHPTVIFASATTASPGATAADLIGQPVVEVTEDGSPRGARTVALWEPALRSDVIGEHGAPVRRSAGAEAARVMADLIVEGAQTLTFVRSRRAAELTALGARARLVDIAPELSDTVASYRAGYLAEDRSALHQALAEGQLRGLATTNALELGVDIAGLDAVVLAGFPGTVASFWQQAGRSGRRGQGALVVLIARDDPLDTYLVHHPAALLDKPVERVVIDPVNPHLLGPQLLCAATELPLDDAEVRSWGAVEVAESLVDDGLLRRRNGRYFPAPGVKPHAAVDVRGAIGGQIVIVEAGTGRLLGSVGVGQAPAAAHPGAVYLHQGETYVVDSLDFQDGIAFVHAEDPGYATFAREVTDIAVTGTGERLVFGPVALGLVPVTVTNHVVGYLRRQLSGEVLDFVELDMPEHTLPTTAVMYTITSDALVRSGIEATRIPGSLHAAEHAAIGLLPLVASCDRGDIGGMSTATGPEGLPSVFVYDGYPGGAGFAERGFRRARTWLGATAEAIEACECPSGCPSCVQSPKCGNGNDPLDKAGAVRVLRLVLAELSEESP
Protein: L-fuculose phosphate aldolase (EC 4.1.2.17) (L-fuculose-1-phosphate aldolase) (Q58813)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Involved in the biosynthesis of the coenzyme F420 which requires phospholactate produced via the aldol cleavage of L-fuculose 1-phosphate and the NAD(+)-dependent oxidation of (S)-lactaldehyde. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and S-lactaldehyde. FucA possesses a high specificity for the dihydroxyacetone phosphate (DHAP), but accepts a great variety of different aldehydes such as DL-glyceraldehyde and glycolaldehyde.
Interaction partners:
- Triosephosphate isomerase
- Lactaldehyde dehydrogenase
- Fructose-bisphosphate aldolase/6-deoxy-5-ketofructose 1-phosphate synthase
- 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
- Probable S-methyl-5'-thioinosine phosphorylase
- Fructose-1,6-bisphosphate aldolase/phosphatase
- Putative methylthioribose-1-phosphate isomerase
- tRNA-guanine
- Ribulose bisphosphate carboxylase
- Archaeal Lon protease
Sequence:
MDKKQFIKICRKLYDRKYVVGSGGNVSVKEGDKIYLTPTGSILGFLKEDDIAEMDLDGNVIKGKPTSEKNLHLMIYRKRNDINAIIHTHSLISTFLSTINKEIELLTPEGKIFLKKIGYVDYYEAGSLKLAEETAKRDEDVIILKNHGVVCLGKDLIDAYIKVEVLEEQAKLTLLNLLVKK
Protein: Sodium/nucleoside cotransporter (Q7K4A1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Equilibrative nucleoside transporter 1, isoform A
- Concentrative nucleoside transporter 1
- Adenosine kinase
- Equilibrative nucleoside transporter 2, isoform A
Sequence:
MSAESSKGAINNGYELDHKELDIRDSEEFTEHPLDDTSEVANKKGYFEKNPKVARLVRISIYVLLHLCVVGYFSYATYHYHDITNYECYWKDNPLCGINFCTGYGMLLLLLGFIYLGLFYYYVFKPMVGHSLHRNYIKPFSKKWHNFSRTRVVSLASIALLLALLAIFVYFECRDETQKLVSLVAPCFFILCGYVFSTNRRAINWRIVITGITCQFLLGIFCIRWEVGRKIFECLGNKVATFLGYATDGAEFVFGDFLVNNNVFAFAILPVIFFFSFFISILYYMGTMQWVVIKLGWILQQILGTTVCESVTAAANIFLGMSESPLLIRPYINKLTKSEIHSIMVSGFATVSGTVLAAYLSFGASAAHLITSSVMAAPATLAISKLYMPETEESQTSSDSIELEKSQDSSLLDAASSGASNAVPIVLGIIANIVAFVAFIAFLNGLVSWFGYLVGLEQIDFEWIFSKLFIPLVWAMGVPKEDCDIIAKVVATKTIINEFVAYERLGQYIENNDITARSAGIATFAICGFANPSSLGILIGSLSAMAPHRRSTITAVAFRAFVVGSIVCFVSASFAGILIQEDDERANYNRIFEKLGRKNVTQF
Protein: Antifungal protein ginkbilobin-1 (Ginkbilobin) (GNL) (P83171)
Organism: Ginkgo biloba (Ginkgo) (Maidenhair tree)
Function: Possesses antifungal activity against B.cinerea, M.arachidicola, F.oxysporum, R.solani and C.comatus and moderate antibacterial activity against S.aureus, P.aeruginosa and E.coli. Inhibits HIV-1 reverse transcriptase and proliferation of murine splenocytes. Exerts antifungal activity through its carbohydrate-binding specificity (By similarity).
Interaction partners:
Sequence:
ANTAFVSSAHNTQKIPAGAPFNRNLRAMLADLRQNAAFAG
Protein: Auxin efflux carrier component 7 (AtPIN7) (Q940Y5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a component of the auxin efflux carrier. Mediates the initial auxin gradient which contributes to the establishment of the apical-basal axis in early embryogenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20439545}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Auxin transporter protein 1
- Auxin transporter-like protein 3
- ABC transporter B family member 19
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Auxin transporter-like protein 2
- Serine/threonine-protein kinase D6PK
- ABC transporter B family member 1
- Auxin transporter-like protein 1
- L-tryptophan--pyruvate aminotransferase 1
- Auxin-responsive protein IAA3
Sequence:
MITWHDLYTVLTAVIPLYVAMILAYGSVRWWKIFSPDQCSGINRFVAIFAVPLLSFHFISSNNPYAMNLRFIAADTLQKLIMLTLLIIWANFTRSGSLEWSITIFSLSTLPNTLVMGIPLLIAMYGEYSGSLMVQIVVLQCIIWYTLLLFLFEYRGAKILIMEQFPETGASIVSFKVESDVVSLDGHDFLETDAQIGDDGKLHVTVRKSNASRRSFYGGGGTNMTPRPSNLTGAEIYSLNTTPRGSNFNHSDFYSMMGFPGGRLSNFGPADMYSVQSSRGPTPRPSNFEESCAMASSPRFGYYPGGAPGSYPAPNPEFSTGNKTGSKAPKENHHHVGKSNSNDAKELHMFVWGSNGSPVSDRAGLQVDNGANEQVGKSDQGGAKEIRMLISDHTQNGENKAGPMNGDYGGEEESERVKEVPNGLHKLRCNSTAELNPKEAIETGETVPVKHMPPASVMTRLILIMVWRKLIRNPNTYSSLIGLIWALVAFRWDVAMPKIIQQSISILSDAGLGMAMFSLGLFMALQPKLIACGNSTATFAMAVRFFTGPAVMAVAAMAIGLRGDLLRVAIVQAALPQGIVPFVFAKEYNVHPAILSTGVIFGMLIALPITLVYYILLGL
Protein: 5'-AMP-activated protein kinase subunit gamma-2 (AMPK gamma2) (AMPK subunit gamma-2) (Q91WG5)
Organism: Mus musculus (Mouse)
Function: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (By similarity).
Interaction partners:
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase subunit beta-2
- 5'-AMP-activated protein kinase subunit beta-1
- Calcium/calmodulin-dependent protein kinase kinase 2
- Serine/threonine-protein kinase STK11
- 5'-AMP-activated protein kinase subunit gamma-1
- Glycogen [starch] synthase, muscle
- 5'-AMP-activated protein kinase subunit gamma-3
- Acetyl-CoA carboxylase 2
Sequence:
MGSAAMDTKKKKEVSSPGGSSGKKNPSLKRRSLRVHIPDLSSFAMPLLDGDVENSEKHSSRKVDSPFSSGSPSRGLFSRGPQPRPSSPVSAPVRPKTSPGSPKTVFPFSYQESPPRSPRRMSFSGIFRSSSKESSPNSNPSTSPGGIRFFSRSRKTSSVSSSPSTPTQVTKQHPFPLESYKQEPERPESRIYASSSPPDTGQRFCLAFQSPARPPLASPTYHAPLRTAVLAAAPGPAEAGMLEKLEFQEEEDSESGVYMRFMRSHKCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETWRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFLQLFMSDMPKPAFMKQNLDELGIGTYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKCSKLETLETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALILTPAGAKQKETETE
Protein: Solute carrier organic anion transporter family member 1A1 (Organic anion-transporting polypeptide 1) (OATP-1) (Sodium-independent organic anion transporter 1) (Solute carrier family 21 member 1) (P46720)
Organism: Rattus norvegicus (Rat)
Function: Mediates the Na(+)-independent transport of organic anions such as steroid sulfate conjugates (dehydroepiandrosterone sulfate (DHEAS), 17-beta-glucuronosyl estradiol, estrone-3-sulfate), conjugated (taurocholate) and unconjugated (cholate) bile acids, prostaglandin E2 (PGE2) and L-thyroxine T4. Also capable of transporting sulfobromophthalein (BSP), ouabain and gadoxetate (By similarity). Hydrogencarbonate/HCO3(-) acts as the probable counteranion that exchanges for organic anions. Shows a pH-sensitive substrate specificity which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:18308854}; Multi-pass membrane protein {ECO:0000269|PubMed:18308854}.
Interaction partners:
- Hepatic sodium/bile acid cotransporter
- Bile salt export pump
- Solute carrier family 22 member 7
- ATP-binding cassette sub-family C member 2
- Bile acid receptor
- Organic anion transporter 3
- Cytochrome P450 family 8 subfamily B member 1
- Cytochrome P450 7A1
- ATP-binding cassette sub-family C member 3
- Ileal sodium/bile acid cotransporter
Sequence:
MEETEKKIATQEGRLFSKMKVFLLSLTCACLTKSLSGVYMNSMLTQIERQFDISTSVAGLINGSFEIGNLFFIVFVSYFGTKLHRPVVIGIGCVIMGLGCLLMSLPHFFMGRYEYETTISPTGNLSSNSFLCMENRTQTLKPTQDPAECVKEMKSLMWICVMVGNIIRGIGETPIVPLGISYIEDFAKSENSPLYIGILEMGKVAGPIFGLLLGSYCAQIYVDIGSVNTDDLTITPSDTRWVGAWWIGFLVCAGVNILTSIPFFFLPKALPKKGQQENVAVTKDGKVEKYGGQAREENLGITKDFLTFMKRLFCNPIYMLFILTSVLQVNGFINKFTFLPKYLEQQYGKSTAEAIFLIGVYSLPPICLGYLIGGFIMKKFKITVKKAAYLAFCLSVFEYLLFLCHFMLTCDNAAVAGLTTSYKGVQHQLHVESKVLADCNTRCSCSTNTWDPVCGDNGVAYMSACLAGCKKFVGTGTNMVFQDCSCIQSLGNSSAVLGLCKKGPECANRLQYFLILTIIISFIYSLTAIPGYMVFLRCVKSEEKSLGVGLHTFCIRVFAGIPAPVYFGALIDRTCLHWGTLKCGQRGACRMYDINSFRHIYLGLPIALRGSSYLPAFFILILMRKFQFPGDIDSSATDHTEMMLGEKESEHTDVHGSPQVENDGELKTKL
Protein: Type 1 phosphatases regulator ypi1 (O14218)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit SDS22
- Uncharacterized protein C17A5.09c
- Serine/threonine-protein phosphatase PP1-1
- Serine/threonine-protein phosphatase PP1-2
- Serine/threonine-protein phosphatase PP-Z
- Septation initiation network scaffold protein cdc11
- Uncharacterized protein C1840.07c
- UBX domain-containing protein 3
- Cell division cycle protein 48
Sequence:
MELTRPLGDISSSATVTIESTEESASISHEESENVLHLQPEPVRRVRWTVSTVDNEHMNKKKSKVCCIFHKQRKFDESSSDSDSDSDSDSSCSSCCSRNAYERA
Protein: Proepiregulin [Cleaved into: Epiregulin (EPR)] (Q9Z0L5)
Organism: Rattus norvegicus (Rat)
Function: Ligand of the EGF receptor/EGFR and ERBB4. Stimulates EGFR and ERBB4 tyrosine phosphorylation. Contributes to inflammation, wound healing, tissue repair, and oocyte maturation by regulating angiogenesis and vascular remodeling and by stimulating cell proliferation.
Subcellular location: [Epiregulin]: Secreted, extracellular space {ECO:0000250|UniProtKB:O14944}.; SUBCELLULAR LOCATION: [Proepiregulin]: Cell membrane {ECO:0000250|UniProtKB:O14944}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O14944}.
Interaction partners:
- Receptor tyrosine-protein kinase erbB-4
- Receptor protein-tyrosine kinase
- Amphiregulin
- Receptor tyrosine-protein kinase erbB-3
- Pro-epidermal growth factor
- Proheparin-binding EGF-like growth factor
- Pro-epidermal growth factor
- Receptor tyrosine-protein kinase erbB-2
- Probetacellulin
- Protransforming growth factor alpha
Sequence:
METFPAAWVLALLCLGSHLLQAVISTTVIPSCIPEESEDNCTALVQMEDDPRVAQVLITKCSSDMDGYCLHGHCIYLVDMSEKYCRCEVGYTGLRCEHFFLTVHQPLSREYVALTVILVFLFLIVTAGSMYYFCRWYRNRKSKKSREEYERVTSGGPGLPQV
Protein: Adapter protein unc-53 (C8JQR2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLKLKLFSSKNPSSSSNSPQPTRKAAAVPQQQTLSKIAAPVKSGLKPPTSKLGSATSMSKLCTPKVSYRKTDAPIISQQDSKRCSKSSEEESGYAGFNSTSPTSSSTEGSLSMHSTSSKSSTSDEKSPSSDDLTLNASIVTAIRQPIAATPVSPNIINKPVEEKPTLAVKGVKSTAKKDPPPAVPPRDTQPTIGVVSPIMAHKKLTNDPVISEKPEPEKLQSMSIDTTDVPPLPPLKSVVPLKMTSIRQPPTYDVLLKQGKITSPVKSFGYEQSSASEDSIVAHASAQVTPPTKTSGNHSLERRMGKNKTSESSGYTSDAGVAMCAKMREKLKEYDDMTRRAQNGYPDNFEDSSSLSSGISDNNELDDISTDDLSGVDMATVASKHSDYSHFVRHPTSSSSKPRVPSRSSTSVDSRSRAEQENVYKLLSQCRTSQRGAAATSTFGQHSLRSPGYSSYSPHLSVSADKDTMSMHSQTSRRPSSQKPSYSGQFHSLDRKCHLQEFTSTEHRMAALLSPRRVPNSMSKYDSSAAALNASGMSRSMILLESLSPRPPRRHQSPADSCIITASPSAPRRSHSPRGPTARIPLSLASSPVHVNNNWGSYSARSRGGSSTGIYGETFQLHRLSDEKSPAHSAKSEMGSQLSLASTTAYGSLNEKYEHAIRDMARDLECYKNTVDSLTKKQENYGALFDLFEQKLRKLTQHIDRSNLKPEEAIRFRQDIAHLRDISNHLASNSAHANEGAGELLRQPSLESVASHRSSMSSSSKSSKQEKISLSSFGKNKKSWIRSSLSKFTKKKNKNYDEAHMPSISGSQGTLDNIDVIELKQELKERDSALYEVRLDNLDRAREVDVLRETVNKLKTENKQLKKEVDKLTNGPATRASSRASIPVIYDDEHVYDAACSSTSASQSSKRSSGCNSIKVTVNVDIAGEISSIVNPDKEIIVGYLAMPTSQSCWKDIDVSILGLFEVYLSRIDVEHQLGIDARDSILGYQIGELRRVIGDSTTMITSHPTDILTSSTTIRMFMHGAAQSRVDSLVLDMLLPKQMILQLVKSILTERRLVLAGATGIGKSKLAKTLAAYVSIRTNQSEDSIVNISIPENNKEELLQVERRLEKILRSKESCIVILDNIPKNRIAFVVSVFANVPLQNNEGPFVVCTVNRYQIPELQIHHNFKMSVMSNRLEGFILRYLRRRAVEDEYRLTVQMPSELFKIIDFFPIALQAVNNFIEKTNSVDVTVGPRACLNCPLTVDGSREWFIRLWNENFIPYLERVARDGKKTFGRCTSFEDPTDIVSEKWPWFDGENPENVLKRLQLQDLVPSPANSSRQHFNPLESLIQLHATKHQTIDNI
Protein: Protein Optix (Homeobox protein SIX3) (D-Six3) (Q95RW8)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in head or eye development; development of the clypeolabrum and several head sensory organs.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Protein phosphatase eya
- FI01127p
- Visual system homeobox 2
- Eyegone, isoform A
- Protein atonal
- Shaven, isoform A
- Protein groucho
- Dachshund, isoform B
- Homeotic protein ocelliless
- Homeotic protein distal-less
Sequence:
MAVGPTEGKQPPSESFSPTHHQIIAPSPILAVPTLAFSAAQVEIVCKTLEDSGDIERLARFLWSLPVALPNMHEILNCEAVLRARAVVAYHVGNFRELYAIIENHKFTKASYGKLQAMWLEAHYIEAEKLRGRSLGPVDKYRVRKKFPLPPTIWDGEQKTHCFKERTRSLLREWYLQDPYPNPTKKRELAKATGLNPTQVGNWFKNRRQRDRAAAAKNRIQHSQNSSGMGCRSRRADGAASPTPSDSSDSDISLGTHSPVPSSLQLQHSPGSTSNGANDREESLSVDDDKPRDLSGSLPLPLSLPLPLASPTHTPPQLPPGYGGGAGAGPGGPLTGPGCLPPFKLDAATSLFSAGCYLQSFSNLKEMSQQFPIQPIVLRPHPQLPQSLALNGASGGPPLHHPAYAAAYSVECVPGGHGPPHPPPKLRINSPEKLNSTAVAAAASVGGGGGNQHHEPTTTGYHHSGQLMLHRPFSTSPELKHSAPEIT
Protein: Bifunctional dethiobiotin synthetase/7,8-diamino-pelargonic acid aminotransferase, mitochondrial (Bifunctional BIO3-BIO1 protein) [Includes: Dethiobiotin synthetase (EC 6.3.3.3) (DTB synthetase) (DTBS) (Protein BIOTIN AUXOTROPH 3); 7,8-diamino-pelargonic acid aminotransferase (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Adenosylmethionine-8-amino-7-oxononanoate aminotransferase) (EC 2.6.1.62) (Diaminopelargonic acid synthase) (Protein BIOTIN AUXOTROPH 1)] (B0F481)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Bifunctional enzyme that catalyzes two different reactions involved in the biotin biosynthesis.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:22547782}.
Interaction partners:
- Biotin synthase, mitochondrial
- 8-amino-7-oxononanoate synthase
- Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic
- Argininosuccinate lyase, chloroplastic
- Arginine biosynthesis bifunctional protein ArgJ
- Argininosuccinate synthase, chloroplastic
- Delta-1-pyrroline-5-carboxylate synthase B
- Delta-1-pyrroline-5-carboxylate synthase A
- Ornithine transcarbamylase, chloroplastic
- Acetylglutamate kinase, chloroplastic
Sequence:
MIPVTATLIRHRLRHLRHRIRFKSTSVSPFHLPLNHPTYLIWSANTSLGKTLVSTGIAASFLLQQPSSSATKLLYLKPIQTGFPSDSDSRFVFSKLDSLSLRRQIPISISNSVLHSSLPAAKSLGLNVEVSESGMCSLNFRDEKTVTGAPELLCKTLYAWEAAISPHLAAERENATVEDSVVLQMIEKCLKEEMECGVKSEKSDLLCLVETAGGVASPGPSGTLQCDLYRPFRLPGILVGDGRLGGISGTIAAYESLKLRGYDIAAVVFEDHGLVNEVPLTSYLRNKVPVLVLPPVPKDPSDDLIEWFVESDGVFKALKETMVLANLERLERLNGMAKLAGEVFWWPFTQHKLVHQETVTVIDSRCGENFSIYKASDNSSLSQQFDACASWWTQGPDPTFQAELAREMGYTAARFGHVMFPENVYEPALKCAELLLDGVGKGWASRVYFSDNGSTAIEIALKMAFRKFCVDHNFCEATEEEKHIVVKVIALRGSYHGDTLGAMEAQAPSPYTGFLQQPWYTGRGLFLDPPTVFLSNGSWNISLPESFSEIAPEYGTFTSRDEIFDKSRDASTLARIYSAYLSKHLQEHSGVRQSAHVGALIIEPVIHGAGGMHMVDPLFQRVLVNECRNRKIPVIFDEVFTGFWRLGVETTTELLGCKPDIACFAKLLTGGMVPLAVTLATDAVFDSFSGDSKLKALLHGHSYSAHAMGCATAAKAIQWFKDPETNHNITSQGKTLRELWDEELVQQISSHSAVQRVVVIGTLFALELKADASNSGYASLYAKSLLIMLREDGIFTRPLGNVIYLMCGPCTSPEICRRLLTKLYKRLGEFNRT
Protein: Malic enzyme (A0A1W2PR68)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLSRLRVVSTTCTLACRHLHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGRNTLIQFEDFGNHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKAKIDSYQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQAECTAEEAYTLTEGRCLFASGSPFGPVKLTDGRVFTPGQGNNVYIFPGVALAVILCNTRHISDSVFLEAAKALTSQLTDEELAQGRLYPPLANIQEVSINIAIKVTEYLYANKMAFRYPEPEDKAKYVKERTWRSEYDSLLPDVYEWPESASSPPVITE