wanglab/gogpt-training-data huggingface dataset:
Protein: Phospholipase DDHD1 (EC 3.1.1.111) (EC 3.1.1.32) (DDHD domain-containing protein 1) (Phosphatidic acid-preferring phospholipase A1 homolog) (PA-PLA1) (EC 3.1.1.118) (Phospholipid sn-1 acylhydrolase) (Q80YA3)
Organism: Mus musculus (Mouse)
Function: Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid. Prefers phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrolyze phosphatidylinositol (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol), PI), as well as a range of other glycerophospholipid substrates such as phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE), phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) and phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol), PG) (By similarity). Involved in the regulation of the endogenous content of polyunsaturated PI and PS lipids in the nervous system. Changes in these lipids extend to downstream metabolic products like PI phosphates PIP and PIP2, which play fundamental roles in cell biology. Regulates mitochondrial morphology. These dynamic changes may be due to PA hydrolysis at the mitochondrial surface. May play a regulatory role in spermatogenesis or sperm function.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8NEL9}.
Interaction partners:
- Triacylglycerol hydrolase DDHD2
Sequence:
MDEVYLYSDATTSKIARTVTQKLGFSKASSSGTRLHRGYVEEATLEDKPSQTSHIVFVVHGIGQKMDQGRIIKNTAMMREAARKMEEKHFSNHATHVEFLPVEWRSKLTLDGDTVDSITPDKVRGLRDMLNSSAMDIMYYTSPLYRDELVKGLQQELNRLYSLFCSRNPDFEEKGGKVSIVSHSLGCVITYDIMMGWNPGGLYEQLLQKEEELPDERWMSYEERHLLDELYITKRRLREIEDRLHGLKAPSISQTPALKFKVENFFCMGSPLAVFLALRGIRPGNSGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTSNPLPYEHMKPNFLNPAKEPTSVSDSENIAAIPSPVTSPVLSRRHYGESITNIGKASILGAASIGKGLGGMLFSRFGRSSASQPSEPSKDSLEDDKKPSASPSTTTVATQTLPHSGSGFLDSAYFRLQESFFYLPQLLFPENVMQSKDDSLVELEHRIDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMYKHEHDTEAKPSLGSL
Protein: Uncharacterized protein (Q386Y4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MWRRISAVTFASAVFLKAGGRSVFVRDLRTPVSIAKGEVEYPAVLLWRWKSNRQRHLVLSVQSPDSHVGMAPEAAAKMISEDRTAPNGGKVSTDITGDYFFGRIFLRPYDVASLLAAFEGKMRHVSMEKQHSSLHLKPIPRWQGGEGGGFGAREGKSFPALPSAFALAGEVTAKVVTAGPKNTEDGSNLLDDEDEDDDAANAGGAATKYNLDDRRSFNATIEEENLVFVMKYLDAVLGDMFGIQHQYHARITNELLVKREMAIYALQQKKKVTTKKEHRYRSMEEVDETVAVEDSCGDSFSRKARGEGVSKMLMVRGERTVAAPVRASSLTRTPPKRFVGSTAGASAVGSAIAHAAVASAAASTFRMNSGRSSSDMEVETRADAFEATSGHAKDDDESSSAASSDDGSGSYSSSYSDDSETDDSDDDGSSDDEPSTRDDDPVDDESDGDSDGDSNDNSDGSEEDSSDGDDSSDEVSIYDHDPVDDDNDEDDNSDKDGEGEDSEDECDSESSTMYGRRGDDRESDDDHTTLSSDDTGDDDDDTGNYADDDTGDDDDDDDDDDDDDDDDEHN
Protein: T-complex protein 1 subunit epsilon (TCP-1-epsilon) (CCT-epsilon) (P47209)
Organism: Caenorhabditis elegans
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
Subcellular location: Cytoplasm.
Interaction partners:
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit zeta
- SET domain-containing protein
- Heat shock protein 70
- Probable prefoldin subunit 4
Sequence:
MAQSSAQLLFDESGQPFIVMREQENQKRITGVEAVKSHILAARAVANTLRTSLGPRGLDKMLVSPDGDVTITNDGATIMEKMDVQHHVAKLMVELSKSQDHEIGDGTTGVVVLAGALLEEAEKLIDRGIHPIKIADGFDLACKKALETLDSISDKFPVENRERLVETAQTSLGSKIVNRSLRQFAEIAVDAVLSVADIESKDVNFEMIKMEGKVGGRLEDTILVKGIVIDKTMSHPQMPKELKNAKVAILTCPFEPPKPKTKHKLDITSTEDFKALRDYERETFETMIRQVKESGATLAICQWGFDDEANHLLQANDLPAVRWVGGPEIELLAIATNARIVPRFSELSKEKLGTAGLVREITFGAAKDRMLSIEQCPNNKAVTIFVRGGNKMIIDEAKRALHDALCVIRNLVRDSRIVYGGGSAELAAAIQVAKEADRIDGIEQYAFRAFADALESIPMALAENSGLAPIDALSDLKAKQIETGKSSLGIDAVFAGTNDMKEQKVIETLLSKREQISLATQVVRMILKIDDVRVPDDERMGY
Protein: Cytochrome b-c1 complex subunit 10, mitochondrial (Complex III subunit 10) (Complex III subunit XI) (Ubiquinol-cytochrome c oxidoreductase subunit 10) (Q94K78)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P37299}; Single-pass membrane protein {ECO:0000250|UniProtKB:P37299}.
Interaction partners:
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome b-c1 complex subunit Rieske-1, mitochondrial
- Cytochrome b-c1 complex subunit 8-1, mitochondrial
- Cytochrome c1 2, heme protein, mitochondrial
- Cytochrome b
- At3g57910
- Cysteine-rich PDZ-binding protein
- Uncharacterized protein At2g39910
- CASP-like protein 5B1
- Small ribosomal subunit protein uS10c
Sequence:
MAGTSGLLNAVKPKIQTIDIQAAAGWGIAAAAGAIWVVQPFGWIKKTFIDPPPTEEK
Protein: E3 ubiquitin-protein ligase MBR1 (EC 2.3.2.27) (MED25-binding RING-H2 protein 1) (RING-H2 finger MBR1) (RING-type E3 ubiquitin transferase MBR1) (Q9ZQF9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that functions as regulator of MED25 stability by targeting MED25 for degradation in a RING-H2-dependent way. Proteasome-dependent degradation of MED25 seems to activate its function as positive regulator of FLOWERING LOCUS T (FT) and is important to induce the expression of FT and consequently to promote flowering.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 25
- Mediator of RNA polymerase II transcription subunit 23
Sequence:
MNPMQGPRSIGGSSTEVNQVDGESIYCTETSLNTMLNPADTGFPNNSTPSGRPTYASSSSHAAQDHTWWRFGESSSIPGPSDQVNSIGIKTSHQLPQDGTHHFVGYGSEGRQTGLNGMMVDGGVHAGSHIRNVPSFLRGSSSNPMPQHVDMSMDMDSDNCNAQTSGVVIRHNSYGSSLGSSVQAAGESSSGPASPFGGWGSSCKRKALEGSPSHYFSGETPNRIVQTENSASHASLSQYGASSSLSLATPSQSSPNVTNHFGRTEQMFGSGGGRAVAASAFHSTRNTDTLSRAGRRLNPRQPQESVAFSVSHGGTSVRPTGSLQQNLPLNSPFVDPPDVRSSSITSGSNTGENQTNIVHLPALTRNIHQYAWDASFSSRASNPSGIGMPAERLGPQWETPRSNQEQPLFAPATDMRQPVHDLWNFARGSPGSSVDSLFVPRAGPSSAIHTPQPNPTWIPPQNAPPHNPSRTSELSPWSLFPSIESPSASHGGPLPLLPAGPSVSSNEVTMPSSSNSRSHRSRHRRSGLLLERQNELLHLRHIGRSLAADGNGRNQIISEIRQVLHAMRRGENLRVEDYMVFDPLIYQGMTDMHDRHREMRLDVDNMSYEELLALGERIGDVSTGLSEEVILKAMKQHKHTSSSPSSVELHQNIEPCCICQEEYVEGDNLGTLKCGHEFHKDCIKQWVMIKNLCPICKTEALKTP
Protein: Transcription factor SOX (Q9I9C8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR038098}.
Interaction partners:
Sequence:
MVQQTDNSETDSMSREATDSDESEFMVSINPDWCKTATGHIKRPMNAFMVWSKIERRKIMEQSPDMHNAEISKRLGKRWKMLKDSEKIPFIREAERLRLKHMADYPDYKYRPKKKPKLDSSSKPSAPSPEKCSKTSKSSKKCPKLKANKTGSKSSSHGYGDEYAFKSTKVSKTVHIKSEFTDEDDDDDSEEDSRVRVKEEEEDPIRAYNVAKVPASPTLSSSTESEGASMYEEVRNNRLYYNFKNITKQSTMYPASVSPASSRSVSTSSSSSEDADDLLFDFSLNFASSAQSSELGSQNPGNLSLSLVDKELESFSEGSLGSHFEFPDYCTPELSEMIAGDWLEANFSDLVFTY
Protein: Bradykinin-like peptide AV-12 (P84823)
Organism: Ascaphus truei (Coastal tailed frog)
Function: Induces relaxation of mouse trachea that has been precontracted with methacholine. May induce relaxation of arterial smooth muscle. May target bradykinin receptors (BDKRB).
Subcellular location: Secreted {ECO:0000269|PubMed:15922344}.
Interaction partners:
Sequence:
APVPGLSPFRVV
Protein: Bacteriophage adsorption protein A (Bacteriophage N4 adsorption protein A) (P31600)
Organism: Escherichia coli (strain K12)
Function: (Microbial infection) Allows N4 phage attachment by binding to the viral non-contractile sheath protein.
Subcellular location: Cell outer membrane.
Interaction partners:
- Bacteriophage adsorption protein B
- Uncharacterized protein YbcH
- Probable autotransporter YcgV
- Uncharacterized protein YihM
- UDP-N-acetylglucosamine 2-epimerase
Sequence:
MKENNLNRVIGWSGLLLTSLLSTSALADNIGTSAEELGLSDYRHFVIYPRLDKALKAQKNNDEATAIREFEYIHQQVPDNIPLTLYLAEAYRHFGHDDRARLLLEDQLKRHPGDARLERSLAAIPVEVKSVTTVEELLAQQKACDAAPTLRCRSEVGQNALRLAQLPVARAQLNDATFAASPEGKTLRTDLLQRAIYLKQWSQADTLYNEARQQNTLSAAERRQWFDVLLAGQLDDRILALQSQGIFTDPQSYITYATALAYRGEKARLQHYLIENKPLFTTDAQEKSWLYLLSKYSANPVQALANYTVQFADNRQYVVGATLPVLLKEGQYDAAQKLLATLPANEMLEERYAVSVATRNKAEALRLARLLYQQEPANLTRLDQLTWQLMQNEQSREAADLLLQRYPFQGDARVSQTLMARLASLLESHPYLATPAKVAILSKPLPLAEQRQWQSQLPGIADNCPAIVRLLGDMSPSYDAAAWNRLAKCYRDTLPGVALYAWLQAEQRQPSAWQHRAVAYQAYQVEDYATALAAWQKISLHDMSNEDLLAAANTAQAAGNGAARDRWLQQAEKRGLGSNALYWWLHAQRYIPGQPELALNDLTRSINIAPSANAYVARATIYRQRHNVPAAVSDLRAALELEPNNSNTQAALGYALWDSGDIAQSREMLEPAHKGLPDDPALIRQLAYVNQRLDDMPATQHYARLVIDDIDNQALITPLTPEQNQQRFNFRRLHEEVGRRWTFSFDSSIGLRSGAMSTANNNVGGAAPGKSYRSYGQLEAEYRIGRNMLLEGDLLSVYSRVFADTGENGVMMPVKNPMSGTGLRWKPLRDQIFFIAVEQQLPLNGQNGASDTMLRASASFFNGGKYSDEWHPNGSGWFAQNLYLDAAQYIRQDIQAWTADYRVSWHQKVANGQTIEPYAHVQDNGYRDKGTQGAQLGGVGVRWNIWTGETHYDAWPHKVSLGVEYQHTFKAINQRNGERNNAFLTIGVHW
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (Q5AJ65)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}.
Interaction partners:
- Calcium-transporting ATPase
- Vacuolar calcium ion transporter
- Calcium-channel protein CCH1
- Transcriptional regulator CRZ1
- Calcium channel YVC1 channel YVC1)
- Calmodulin
- Uncharacterized protein
- Calcineurin subunit B
- Mlc2p
Sequence:
MAPRTPADKLGHASTLQLPTYDNDDQSSTNSTTPLHKDTPEETTDTSTTTNDVEPFHPPKLLSKTTTSPSIKLTSMLSKTSTKQNPNFPISLQSLSELHDPKSLKQLYDLGGIDNLLASLHTSFDGLNEHNETDLSQRKQYFGINRLPQKVQKSFLKLCWEALKDKVLVILCIAAIVSLALGCYESFGSGTHYDDEGLPLPKVDYVEGVAILVAVAIVVLVGAANDYQKERQFAKLNAKKEDREVIVVRNGGEQKLISIYDLMVGDVINLQTGDVVPADCILIQGEVECDESALTGESHTIHKVPVAKAMKVYQNHLPTNEDIGSTQIKFRDPYLISGAKVLSGLGNAVITAVGTNSIHGRTMMSLNHEPESTPMQVRLNDLAEGISKYGFLAAIVLFVVLFIRFCVEIAPNGNMNGAEPADKGKRFIDIIITAVTIVVVAIPEGLPLAVTLALAFATTRMAQNGNLVRVLKSCETMGGATAVCSDKTGTLTENKMRIVRGFFGLNKQGQPLEFNDTVGNQHDEPTSIDIINNEISSEQKVYLTTNIILNSTAFENSEYDEEKAKLARQKPPKQSFFSSLFKNSKKSQYQQMGLVDEPYLGNKTESALLTLAKDKFHLFDNKSLETCRQENNGDVIQVIPFESSRKWAGIVMKIPNGFRLYVKGAAEIIFKNCGFENNINDELIKLDRSKRDDVLSKIDEYANDALRAIALAHRDFVGISSWPPSELSSSSENKKTTTTAKEADPAKLINTSSSASEIHKMFILDALVGIQDPLKKGVAEAVLQCKRAGVTVRMVTGDNINTAKSISKECNILTSDDLSNEYSCMEGPQFRKLSIQKRREIVPQLKVLARSSPEDKRILVDTLRKAGEVVAVTGDGTNDAPALKLADVGFSMGIAGTEVAREASDIILMTDDFTDIVQAIKWGRTVSTSIKKFIQFQLTVNITACVLTFVSAVASSENKSVLTAVQLLWVNLIMDTLAALALATDKPDDSFLNRKPAGRTAPLISTSMWKMIIGQSMTQLIITFILHFAGKQLFFPGQSHINNHSEKQLAAMTFNTFVWLQFWKLFVTRKLDEADEITTIRGRISRENLDFFQHLFRNWYFITIALIIGGFQILIMFVGGAAFSIARQTPGMWATAILCGFLSIPVGLLIRIIPNIWIETIFPTKAFKKFLYIVGFGWLKFRKNKKTKDNEEDDEMDLEGGGNSDLKESKE
Protein: Uncharacterized protein Rv1355c (P9WM11)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv1356c
- Uncharacterized protein Rv1354c
- HTH-type transcriptional repressor Rv1353c
- Probable transcriptional regulatory protein
- Uncharacterized protein Rv1357c
- Molybdopterin synthase catalytic subunit 1
- Putative diacyglycerol O-acyltransferase Rv0895
- Thiazole synthase
- Uncharacterized protein Rv0894
- Possible protein ThiS
Sequence:
MTIPHEGGSTGILVLRDDDHDDVLVLDRLRSDPSIEFVDRFAEQLAGVRRLLPQPDPDLLEEAKRWAYYPWRRMVVAILGLRGFRAVRLDRNRHLITAEEQRALHALRVGVVGLSAGHAIAYTLAAEGACGTLRLADFDKIELSNLNRVPVGVFDIGLNKAMIAARRIAELDPYLAVDLVTSGLSPESVDEFLDGLDVVIEECDSLDIKVILRQAACARGVPVLMATSDRGLVDVERYDVEPGRPIFHGLLGDIDADKLCGLTTKDKVPHVLNILDCQELSARCAASMIEVDQTLWGWPQLAGDIWVGAATVAEAVRRIGLGEPLESGRVRVDVSAALDRLDQPPMPSRGNGWLLESVPPTAPAEPQPTSEIVAQAAIRAPSGGNVQPWHVVAKQHSLTIRLAPEHTSAMDIAFRGSAVAVGAAMFNARVAAAAHRVLGSVEFDESQPDSPLQATMHFGRGDDPSLAALYRPMLLRTTNRHHGMPGHVHPATVELLTNTAAAEGARLQLLLSRNEIDRAATILAAADRIRYLTPRLHEEMMSELRWPGDPSLDAGIDVRSLELDSGELRVLDILRRSDVVARLAQWDCGTALEDNTNERVSASSALAIVYVDGATLTDFARGGSAMQAVWIVAQQHGLAVQPMSPIFLYARGRHDLDQASPHFAAQLHRLQLDFRELVKPGKEGHEVLIFRLFHAPPPSVCSRRRVRHAIPEPHR
Protein: L-carnitine/gamma-butyrobetaine antiporter (P31553)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the exchange of L-carnitine for gamma-butyrobetaine. Can also transport D-carnitine and, with lower efficiency, acetyl-L-carnitine and glycine betaine.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:20357772, ECO:0000269|PubMed:20829798}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000269|PubMed:20357772, ECO:0000269|PubMed:20829798}.
Interaction partners:
- Crotonobetainyl-CoA reductase
- Crotonobetaine/carnitine--CoA ligase
- L-carnitine CoA-transferase
- Carnitinyl-CoA dehydratase
- Carnitine operon protein CaiE
Sequence:
MKNEKRKTGIEPKVFFPPLIIVGILCWLTVRDLDAANVVINAVFSYVTNVWGWAFEWYMVVMLFGWFWLVFGPYAKKRLGNEPPEFSTASWIFMMFASCTSAAVLFWGSIEIYYYISTPPFGLEPNSTGAKELGLAYSLFHWGPLPWATYSFLSVAFAYFFFVRKMEVIRPSSTLVPLVGEKHAKGLFGTIVDNFYLVALIFAMGTSLGLATPLVTECMQWLFGIPHTLQLDAIIITCWIILNAICVACGLQKGVRIASDVRSYLSFLMLGWVFIVSGASFIMNYFTDSVGMLLMYLPRMLFYTDPIAKGGFPQGWTVFYWAWWVIYAIQMSIFLARISRGRTVRELCFGMVLGLTASTWILWTVLGSNTLLLIDKNIINIPNLIEQYGVARAIIETWAALPLSTATMWGFFILCFIATVTLVNACSYTLAMSTCREVRDGEEPPLLVRIGWSILVGIIGIVLLALGGLKPIQTAIIAGGCPLFFVNIMVTLSFIKDAKQNWKD
Protein: 2,3-dimethylmalate dehydratase large subunit (EC 4.2.1.85) (Q0QLE2)
Organism: Eubacterium barkeri (Clostridium barkeri)
Interaction partners:
- 2,3-dimethylmalate dehydratase small subunit
- 3-isopropylmalate dehydratase small subunit
- 3-isopropylmalate dehydrogenase
- Isocitrate dehydrogenase
- 2-isopropylmalate synthase
- Citramalate synthase
- Dihydroxy-acid dehydratase
- Ketol-acid reductoisomerase
- Acetolactate synthase small subunit
- Pyruvate:ferredoxin oxidoreductase
Sequence:
MGMTMTQKILAAHASLDSVKAGDLIMADLDMVLANDITGPVAINVFGTIDKEKVFDKDKIALVPDHFAPAKDIKSAQQCKQVRCFACDQEITNYFEIGEMGIEHALLPEKGLVAAGDVVIGADSHTCTYGALGAFSTGVGSTDMAVGMATGKAWFKVPAALRFNLTGTLNKNVSGKDLILHIIGMIGVDGALYRSMEFTGPGVACLSMDDRFTISNMAIEAGGKNGIFPVDDQTISYMEEHGSGDYKVYAADADAVYEKTFDIDLSQLKSTVAFPHLPENTKTVDAIEEPVTIDQVVIGSCTNGRFEDLKRAADILRGKHVKKGVRMLVIPATHKIYLDAMEAGYLREFIEAGATISTPTCGPCLGGYMGILAEGERCVSTTNRNFVGRMGHVDSEVYLASPEVAAASAILGRIATPDEL
Protein: Immunoglobulin heavy variable 3-53 (Ig heavy chain V-III region BUT) (P01767)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MEFWLSWVFLVAISKGVQCEVQLVETGGGLIQPGGSLRLSCAASGFTVSSNYMSWVRQAPGKGLEWVSVIYSGGSTYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAR
Protein: Acyl-Coenzyme A dehydrogenase family, member 12 (F6RGT6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XQSMLLVPMDSPGITVIRPLSVFGLEDPPGGFAEVQFKDVRVPKENIILGPGRAFEIAQGRLGRARIHNSMRLIGYSERALALMKTRVSPPVPTLTQTHCCWLRNSNHWSPLRTELTGQCPCLESASLFCMYFTWLQLASRVGWAPLCLGGQKPRAGFMVAEGKVLNPRGLWQPGTICSQHI
Protein: Auxin efflux carrier component 2 (AtPIN2) (Auxin efflux carrier AGR) (Ethylene-insensitive root 1) (AtEIR1) (Polar-auxin-transport efflux component AGR1) (Protein AGRAVITROPIC 1) (AtAGR1) (Protein WAVY 6) (Q9LU77)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a component of the auxin efflux carrier. Seems to be involved in the root-specific auxin transport, and mediates the root gravitropism. Its particular localization suggest a role in the translocation of auxin towards the elongation zone.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20439545, ECO:0000269|PubMed:33705718}; Multi-pass membrane protein {ECO:0000305}. Note=Localized the plasma membrane in a polar apical localization. {ECO:0000269|PubMed:33705718}.
Interaction partners:
- ABC transporter B family member 19
- Auxin transporter protein 1
- Protein TRANSPORT INHIBITOR RESPONSE 1
- ABC transporter B family member 1
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein kinase D6PK
- Sorting nexin 1
- Auxin transporter-like protein 3
- Auxin response factor 19
- ABC transporter B family member 4
Sequence:
MITGKDMYDVLAAMVPLYVAMILAYGSVRWWGIFTPDQCSGINRFVAVFAVPLLSFHFISSNDPYAMNYHFLAADSLQKVVILAALFLWQAFSRRGSLEWMITLFSLSTLPNTLVMGIPLLRAMYGDFSGNLMVQIVVLQSIIWYTLMLFLFEFRGAKLLISEQFPETAGSITSFRVDSDVISLNGREPLQTDAEIGDDGKLHVVVRRSSAASSMISSFNKSHGGGLNSSMITPRASNLTGVEIYSVQSSREPTPRASSFNQTDFYAMFNASKAPSPRHGYTNSYGGAGAGPGGDVYSLQSSKGVTPRTSNFDEEVMKTAKKAGRGGRSMSGELYNNNSVPSYPPPNPMFTGSTSGASGVKKKESGGGGSGGGVGVGGQNKEMNMFVWSSSASPVSEANAKNAMTRGSSTDVSTDPKVSIPPHDNLATKAMQNLIENMSPGRKGHVEMDQDGNNGGKSPYMGKKGSDVEDGGPGPRKQQMPPASVMTRLILIMVWRKLIRNPNTYSSLFGLAWSLVSFKWNIKMPTIMSGSISILSDAGLGMAMFSLGLFMALQPKIIACGKSVAGFAMAVRFLTGPAVIAATSIAIGIRGDLLHIAIVQAALPQGIVPFVFAKEYNVHPDILSTAVIFGMLVALPVTVLYYVLLGL
Protein: PHD finger protein 20-like protein 1 (A8MW92)
Organism: Homo sapiens (Human)
Function: Is a negative regulator of proteosomal degradation of a set of methylated proteins, including DNMT1 and SOX2. Involved in the maintainance of embryonic stem cells pluripotency, through the regulation of SOX2 levels (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:24492612}. Note=Localized to the perinucleolar region. {ECO:0000269|PubMed:24492612}.
Interaction partners:
- KAT8 regulatory NSL complex subunit 1
- Histone acetyltransferase KAT8
- KAT8 regulatory NSL complex subunit 3
- KAT8 regulatory NSL complex subunit 2
- Microspherule protein 1
- Chromodomain-helicase-DNA-binding protein 3
- Transcriptional repressor p66-beta
- BCL11 transcription factor A
- Transcriptional repressor p66-alpha
- Methyl-CpG-binding domain protein 2
Sequence:
MSKKPPNRPGITFEIGARLEALDYLQKWYPSRIEKIDYEEGKMLVHFERWSHRYDEWIYWDSNRLRPLERPALRKEGLKDEEDFFDFKAGEEVLARWTDCRYYPAKIEAINKEGTFTVQFYDGVIRCLKRMHIKAMPEDAKGQVKSQHPLSWCCPIDPAGSCNQSMGSEDWIALVKAAAAAAAKNKTGSKPRTSANSNKDKDKDERKWFKVPSKKEETSTCIATPDVEKKEDLPTSSETFGLHVENVPKMVFPQPESTLSNKRKNNQGNSFQAKRARLNKITGLLASKAVGVDGAEKKEDYNETAPMLEQAISPKPQSQKKNEADISSSANTQKPALLSSTLSSGKARSKKCKHESGDSSGCIKPPKSPLSPELIQVEDLTLVSQLSSSVINKTSPPQPVNPPRPFKHSERRRRSQRLATLPMPDDSVEKVSSPSPATDGKVFSISSQNQQESSVPEVPDVAHLPLEKLGPCLPLDLSRGSEVTAPVASDSSYRNECPRAEKEDTQMLPNPSSKAIADGRGAPAAAGISKTEKKVKLEDKSSTAFGKRKEKDKERREKRDKDHYRPKQKKKKKKKKKSKQHDYSDYEDSSLEFLERCSSPLTRSSGSSLASRSMFTEKTTTYQYPRAILSVDLSGENLSDVDFLDDSSTESLLLSGDEYNQDFDSTNFEESQDEDDALNEIVRCICEMDEENGFMIQCEECLCWQHSVCMGLLEESIPEQYICYICRDPPGQRWSAKYRYDKEWLNNGRMCGLSFFKENYSHLNAKKIVSTHHLLADVYGVTEVLHGLQLKIGILKNKHHPDLHLWACSGKRKDQDQIIAGVEKKIAQDTVNREEKKYVQNHKEPPRLPLKMEGTYITSEHSYQKPQSFGQDCKSLADPGSSDDDDVSSLEEEQEFHMRSKNSLQYSAKEHGMPEKNPAEGNTVFVYNDKKGTEDPGDSHLQWQLNLLTHIENVQNEVTSRMDLIEKEVDVLESWLDFTGELEPPDPLARLPQLKRHIKQLLIDMGKVQQIATLCSV
Protein: Transcription factor bHLH87 (Basic helix-loop-helix protein 87) (AtbHLH87) (bHLH 87) (Transcription factor EN 121) (bHLH transcription factor bHLH087) (Q8S3D2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- MLO-like protein 3
- protein-synthesizing GTPase
- Putative transcription factor bHLH107
- Ethylene-responsive transcription factor ERF014
- Zinc finger CCCH domain-containing protein 66
Sequence:
MEGLESVYAQAMYGMTRESKIMEHQGSDLIWGGNELMARELCSSSSYHHQLINPNLSSCFMSDLGVLGEIQQQQHVGNRASSIDPSSLDCLLSATSNSNNTSTEDDEGISVLFSDCQTLWSFGGVSSAESENREITTETTTTIKPKPLKRNRGGDGGTTETTTTTTKPKSLKRNRGDETGSHFSLVHPQDDSEKGGFKLIYDENQSKSKKPRTEKERGGSSNISFQHSTCLSDNVEPDAEAIAQMKEMIYRAAAFRPVNFGLEIVEKPKRKNVKISTDPQTVAARQRRERISEKIRVLQTLVPGGTKMDTASMLDEAANYLKFLRAQVKALENLRPKLDQTNLSFSSAPTSFPLFHPSFLPLQNPNQIHHPEC
Protein: Transcription factor TCP16 (Q9M1U4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required during early processes in pollen development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor TCP24
- Transcription factor TCP4
- PLATZ transcription factor family protein
- Transcription factor TCP3
- Transcription factor TCP17
- Transcription factor TCP5
- Transcription factor TCP2
- Transcription factor TCP10
- Transcription factor TCP12
- DNA-binding protein S1FA3
Sequence:
MDSKNGINNSQKARRTPKDRHLKIGGRDRRIRIPPSVAPQLFRLTKELGFKTDGETVSWLLQNAEPAIFAATGHGVTTTSNEDIQPNRNFPSYTFNGDNISNNVFPCTVVNTGHRQMVFPVSTMTDHAPSTNYSTISDNYNSTFNGNATASDTTSAATTTATTTV
Protein: 2-oxoglutarate-Fe(II) type oxidoreductase (EC 1.14.11.-) (Endocrocin synthesis protein D) (Q4W946)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: 2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA. The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA. The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by encC. The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself.
Interaction partners:
Sequence:
MTKPQPPPILDFSVFYGHDSQAKAQLVQRVRECCLNNGFFQITGHKVSPELQRRTFDCAKRFFDLPLIEKKKIERSPDAFNRGYEAFQSHMSQPGSAPDRKEGLFLGPDLAEDHPYCVQKKLNCGPNRWPQGLDDLEEFKLVSMEYYAALFQLAKDVVAVLALTMDYEETFFDPLTEGAIATLRYLHYPPQPVGDAEAGLGTGAHRDYSCITLLLQDGTGGLQVLDEPTGQWLDVKPVPGAYIVNLANVFARMTNGHYKSALHRVVNKSGMERYSIPFFFTGNPDYVCECLSRFRKEGEPVRHPPATVHEVVAEAVRGTVERANRYNAERQGIHAAQ
Protein: Uncharacterized protein, isoform B (EC 1.1.1.300) (Uncharacterized protein, isoform D) (Q9VE80)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RE02508p
- Uncharacterized protein, isoform B
Sequence:
MGFIFGWLSTEHYVRDIFLMTSVAAIVATLMSIRFYLRITAGRCFTETKMEGKTVIITGANSGIGKETAKDLAGRGARIIMACRNLETANAVKDEIVKETKNNKILVKKLDLGSQKSVREFAADIVKTEPKIDVLIHNAGMALAFRGQTSEDGVELTMATNHYGPFLLTHLLIDVLKKSAPARIVIVASELYRLSSVNLAKLNPIGTFPAAYLYYVSKFANIYFARELAKRLEGTKVTVNFLHPGMIDSGIWRNVPFPLNLPMMAITKGFFKTTKAGAQTTIYLATSNEVANVSGKYFMDCKEATLNAAALDEEKGLKIWEESVKIVKLTPQDPKI