wanglab/gogpt-training-data huggingface dataset:
Protein: Monocarboxylate transporter 1 (MCT 1) (Solute carrier family 16 member 1) (P53985)
Organism: Homo sapiens (Human)
Function: Bidirectional proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, acetate and the ketone bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to the maintenance of intracellular pH. The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter (By similarity). Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis (By similarity). Facilitates the protonated monocarboxylate form of succinate export, that its transient protonation upon muscle cell acidification in exercising muscle and ischemic heart. Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 309-Asp is essential for the conformational transition.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10921872, ECO:0000269|PubMed:12946269, ECO:0000269|PubMed:15505343, ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:24390345, ECO:0000269|PubMed:25957687}; Multi-pass membrane protein {ECO:0000269|PubMed:33333023}. Basolateral cell membrane {ECO:0000250|UniProtKB:P53987}; Multi-pass membrane protein {ECO:0000269|PubMed:33333023}. Apical cell membrane {ECO:0000269|PubMed:15901598}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P53987}. Note=Expression at the cell surface requires the ancillary proteins BSG and EMB. Binds preferentially to BSG. {ECO:0000269|PubMed:10921872}.
Interaction partners:
- Basigin
- Embigin
- MFS-type transporter SLC18B1
- Chromaffin granule amine transporter
- Carbonic anhydrase 2
- ATP-sensitive inward rectifier potassium channel 11
- Sodium-coupled monocarboxylate transporter 1
- Hexokinase-4
Sequence:
MPPAVGGPVGYTPPDGGWGWAVVIGAFISIGFSYAFPKSITVFFKEIEGIFHATTSEVSWISSIMLAVMYGGGPISSILVNKYGSRIVMIVGGCLSGCGLIAASFCNTVQQLYVCIGVIGGLGLAFNLNPALTMIGKYFYKRRPLANGLAMAGSPVFLCTLAPLNQVFFGIFGWRGSFLILGGLLLNCCVAGALMRPIGPKPTKAGKDKSKASLEKAGKSGVKKDLHDANTDLIGRHPKQEKRSVFQTINQFLDLTLFTHRGFLLYLSGNVIMFFGLFAPLVFLSSYGKSQHYSSEKSAFLLSILAFVDMVARPSMGLVANTKPIRPRIQYFFAASVVANGVCHMLAPLSTTYVGFCVYAGFFGFAFGWLSSVLFETLMDLVGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVVLIISGIYLFIGMGINYRLLAKEQKANEQKKESKEEETSIDVAGKPNEVTKAAESPDQKDTDGGPKEEESPV
Protein: A-kinase anchor protein 3 (AKAP-3) (A-kinase anchor protein 110 kDa) (AKAP 110) (Protein kinase A-anchoring protein 3) (PRKA3) (O77797)
Organism: Bos taurus (Bovine)
Function: May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:O88987}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:O88987}. Note=Dorsal margin of the acrosomal segment. Ribs of the fibrous sheath in the principal piece of the sperm tail. {ECO:0000250|UniProtKB:O88987}.
Interaction partners:
- Calcium-binding tyrosine phosphorylation-regulated protein
- Ropporin-1
- Outer dense fiber protein 1
- Sperm surface protein Sp17
Sequence:
MSDRVDWLQSQNGVCKVDVYSPGDSQPQDWKMSDESLSIFKEASHDPIRVLSWLRRDLEKSTAGFQDIRFKPGESSLGREMVSSGDPRKGFCVDYYNTTSRGSPGRLHFEMSHRENPHQGPTCNGSSVDEVSFYANRLTNLVIAMARKEINEKIDGSENRCVHQSVYMGDEPPPNKSLSKVASELVNETVTACSKNTPSDKAPGSGDRASGTLQSPPNLKYKSTLKIKESNKGGRGPDDRPSSKKSFFYKEVFESRNAGDAKEGGRTLPAERKMFRGYERPDDFTASISQGIMTYANSVVSDMMVSIMKTLKIQVKDTTIATIVLKKVLIKHAKEVVSDLIDSFMKNLHNVTGTLMTDTDFVSAVKRSFFSHGSQKATDIMDAMLGKLYSVIFAKKPPETVRKTKDKSESYSLVSMKGMGDPKHRNVNFASMKSEGKVRERVCTPTPKPEKSCVETLGEHIIKEGLTLWHNSQQKEGISACLQGSPFVTPKRQYKPVPDFPLGFPFDPCNFSLPMQCPEKPENFMCDSDSWAKDLLVSALLLIQYHLAQGGNMDAQSFLEAAGTSNLYPTKSPAVSHESSLRSPQVGADPEEVEKKDLMSVFFNLIRNLLSETIFKSDHSCDPKATKEDNSPQCERPVTPSPAKLNECDETGGAFAGLTKMVANKLDGHMNGQMVDHLMDSVMKLCLIIAKSCDSPLAELGDDKSGDASRPTSAFPESLYECLSTKGTGTAETLLQNAYQAIHNELRSLSAQPPEGCTAPKVIVSNHNLTDTVQNKQLQAVLQWVAASELNVPILYFAGDDEGIQEKLLQLSAAAVEKGRSVGEVLQSVLRYEKERQLDEAVGNVTRLQLLDWLMVNL
Protein: Mitochondrial dynamics protein MID51 (Mitochondrial dynamics protein of 51 kDa homolog) (Mitochondrial elongation factor 1) (Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like) (Q8BGV8)
Organism: Mus musculus (Mouse)
Function: Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity and DNM1L oligomerization. Binds ADP and can also bind GDP, although with lower affinity. Does not bind CDP, UDP, ATP, AMP or GTP. Inhibits DNM1L GTPase activity in the absence of bound ADP. Requires ADP to stimulate DNM1L GTPase activity and the assembly of DNM1L into long, oligomeric tubules with a spiral pattern, as opposed to the ring-like DNM1L oligomers observed in the absence of bound ADP. Does not require ADP for its function in recruiting DNM1L.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:24508339}; Single-pass membrane protein {ECO:0000269|PubMed:24508339}.
Interaction partners:
- Dynamin-1-like protein
- Mitochondrial fission factor
- Mitochondrial fission 1 protein
- Dynamin-like GTPase OPA1, mitochondrial
- Mitofusin-2
- Mitofusin-1
Sequence:
MAGAGERKGKKDDNGIGTAIDFVLSNARLVLGVGGAAMLGIATLAVKRMYDRAISAPTSPTRLSHSGKRSWEEPNWMGSPRLLNKDMKAGLSRSLQTLPTDSSAFDTDTFCPPRPKPLARRGQVDLKKSRLRMSLQEKLLSYYRNRAAIPAGEQARAKQAAVDICAELRSFLRAKLPDMPLRDMYLSGSLYDDLQVVTADHIQLIVPLVLEQNLWSCIPGEDTIMNVPGFFLVRRENPEYFPRGSSYWDRCVVGGYLSPKTVADTFEKVVAGSINWPAIGSLLDYVIRPAPPPEALTLEVQYEKDKHLVIDFLPSVTLGDTVLVARPHRLAQYDNLWRLSLRPAETARLRALDQADSGCRSLCLKILKAICKSTPALGHLTASQLTNVILHLAQEEADWSPDMLADRFLQALRGLISYLEAGVLPSALNPKVNLFAELTPQEIDELGYTLYCSLSEPEVLLQT
Protein: NEDD8-like protein RUB1 (Related to ubiquitin protein 1) (Ubiquitin-like protein RUB1) (Q03919)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ubiquitin-like protein modifier that can be covalently attached to lysine residues of target proteins. Activated by the dimeric UBA3-ULA1 E1 enzyme and conjugated by the E2 UBC12 to substrate proteins. RUB1-conjugated (neddylated) substrate proteins include the cullins CDC53, RTT101 and CUL3, and the modification enhances the ubiquitin-ligase activity of the corresponding cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs).
Interaction partners:
- NEDD8-conjugating enzyme UBC12
- Suppressor of kinetochore protein 1
- Ubiquitin carboxyl-terminal hydrolase YUH1
- NEDD8-activating enzyme E1 catalytic subunit
- Cell division control protein 53
- Ubiquitin-conjugating enzyme E2-34 kDa
- NEDD8-activating enzyme E1 regulatory subunit
- 26S proteasome regulatory subunit RPN10
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein uL23
Sequence:
MIVKVKTLTGKEISVELKESDLVYHIKELLEEKEGIPPSQQRLIFQGKQIDDKLTVTDAHLVEGMQLHLVLTLRGGN
Protein: Actin cytoskeleton-regulatory complex protein sla1 (O13736)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:16823372}. Note=Cytoplasmic and cortical actin patches. {ECO:0000250}.
Interaction partners:
- Putative Rho GTPase-activating protein C1565.02c
- Actin-binding protein wsp1
- Polyubiquitin
- SH3 domain-containing protein PJ696.02
- Actin cytoskeleton-regulatory complex protein end3
- Protein app1
- Fimbrin
- Endocytosis protein end4
- Phospholipid-transporting ATPase dnf1
- Cofilin
Sequence:
MANLPIIGIYKVLYSYEPQEINPGEEIPENEREISIVEDEIVCLLEKGEDDWYLVKRNVNSNDDDEEIGIVPSNYITEAEPSTKMKALYDYTQQSVDEISFQADQTLDCYGDTDSDWILVGFNNNFGLAPRNYVEGMDASSAPASQEPSASGVNAPTVSAPNSMVSPPPSFQPPSAAAPATSLPSDYNPPPPPPPPPAVEDQAADANEPDDYYSSGRAVSPEIPPTYTPKQADPLPAPPPPPPPTLPPQSTNTSQLPMPSRNVNNLGSQVNIPPPPATPSQPPRPPTNASTRSTGTSSSMAHSYDSPPSPSSPSDAYGDPNQHLKLRTDSHDDSRAYDSSSSMGNPAYEKWEVREVVGKKKKRTGILAINNKSIVLTFTKTMDAAQVWPVTDLVNYSSERKHVFIEFNSDSGITSLHLHASSNTNADNIIRALGDVAGSARAAGLREIAAASGSPMPKLPSDSALHRLNAASDAAGVNGGRTGDYEMSTVYGDRSARAEDHKPKDSSAGQKMGTVLYDFIAEAADELTVKANMRVVIVNDTASSDWWKCSVDGKEGVVPSNFIKPDTEGDAKSPPSSSKSGQGSSLSRRASKHESKHKRDSKHEARPESKHESHRESKSAEKDKKDKKDKKEDSKRSRSHSVSKPDSSKLRTWTDRTGAFKVEAEFLGYSDDKIHLHKTNGVKISVPSAKMSYKDLDYVELMTGKKVYSRTERKKDTQKQSHDHGHSHSKSHDREKEKEKKKDREHRKHRETEEEDEGPPPQPARPESTRPALAPPSSSHSNDKYDVIQERPKISYDWFDFFLRCGVDFTVCNRYTHNFNNEHLDEACIPSLNPDTLRTLGLKEGDIIRVMNHVNELNGVSTKPASAITPETKSTVNQIMSGGEALAAPVAVPAPIPAPVAEPAPPAAPAKEVVEKAPSPPATRPKSTTPQKFDDDAWANKPVTEPPVRASSVTVEPARVTESMNKMNISEEAKKPEAPSRPRTAPIPEPEEQKKAPVEKKDAEKSVQAPIPAQPTGNITIQNAYFTAPQPMAADPFQSPLYVQPTGFQPPPSALPIQPTGYMQPIPVQATGYQPLMVQPTGLQPHMTGVMPQVTGVMPQMTGVVPQMTGVMPQMTGVQVQKTGAMPQQPVNYGYQVAGMQPQATGIISQPTGIRAQATGIMTQPTGLHTQATGMMQPTGMQPQATGIMPQATGMMQPTGMQPQVTGIMPQSMPMQPQMTGVQVQKTGMVAQPMLSQYTGYQQNYTPTAMPAADGYGMQPSMNDTQAYYNMNAQTPVNYGFAGGQDTSFGYEQQQMYSPMQQQQQQYYGTEMQPDMGYQQPMMSNYYDPMQMQQQTPYGYNQTGMEGYSEYGYAQPAGNMANPMSYDPVSNASLYMPSDYNQQTQPANYYDSSFGGAQGANEAGKKASIYQATPDNPFGF
Protein: Protein phosphatase methylesterase 1 (PME-1) (EC 3.1.1.89) (Q4FZT2)
Organism: Rattus norvegicus (Rat)
Function: Demethylates proteins that have been reversibly carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme (By similarity).
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Leucine carboxyl methyltransferase 1
- Protein phosphatase 2 scaffold subunit A alpha
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
Sequence:
MSALEKSMHLGRLPSRPPLPGSGGSQSGAKMRMGPGRKRDFTPVPWSQYFESMEDVEVENETGKDTFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRVQCRIVALDLRSHGETKVKNSEDLSAETMAKDVGNVVEAMYGDLPPPVMLIGHSMGGAIAVHTAAANLVPSLLGLCMIDVVEGTAMDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNLESARVSMVGQVKQCEGITSPESSKSIVEGIIEEEEEDEEGSESVNKRKKEDDMETKKDHPYTWRIELAKTEKYWDGWFRGLSNLFLSCPIPKLLLLAGVDRLDKDLTIGQMQGKFQMQVLPQCGHAVHEDAPDKVAEAVATFLIRHRFAEPIGGFQCVFPGC
Protein: Anaphase-promoting complex subunit CDC23 (Cell division control protein 23) (P16522)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Note=Associated with the kinetochore.
Interaction partners:
- Anaphase-promoting complex subunit CDC16
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit MND2
- Anaphase-promoting complex subunit DOC1
- Anaphase-promoting complex subunit SWM1
- Anaphase-promoting complex subunit 9
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit CDC27
- Anaphase-promoting complex subunit 5
Sequence:
MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM
Protein: Enteropeptidase (EC 3.4.21.9) (Enterokinase) (Serine protease 7) (Transmembrane protease serine 15) [Cleaved into: Enteropeptidase non-catalytic heavy chain; Enteropeptidase catalytic light chain] (P98073)
Organism: Homo sapiens (Human)
Function: Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Serine protease 1
- Agrin
- Serine protease inhibitor Kazal-type 1
- Thioredoxin
Sequence:
MGSKRGISSRHHSLSSYEIMFAALFAILVVLCAGLIAVSCLTIKESQRGAALGQSHEARATFKITSGVTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQFENGSIIVVFDLFFAQWVSDENVKEELIQGLEANKSSQLVTFHIDLNSVDILDKLTTTSHLATPGNVSIECLPGSSPCTDALTCIKADLFCDGEVNCPDGSDEDNKMCATVCDGRFLLTGSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYTDILDIYEGVGSSKILRASIWETNPGTIRIFSNQVTATFLIESDESDYVGFNATYTAFNSSELNNYEKINCNFEDGFCFWVQDLNDDNEWERIQGSTFSPFTGPNFDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSFWYHMYGENVHKLSINISNDQNMEKTVFQKEGNYGDNWNYGQVTLNETVKFKVAFNAFKNKILSDIALDDISLTYGICNGSLYPEPTLVPTPPPELPTDCGGPFELWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLENINDVVEIRDGEEADSLLLAVYTGPGPVKDVFSTTNRMTVLLITNDVLARGGFKANFTTGYHLGIPEPCKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADCVRFFNGTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSGNSSKPIFPTDGGPFVKLNTAPDGHLILTPSQQCLQDSLIRLQCNHKSCGKKLAAQDITPKIVGGSNAKEGAWPWVVGLYYGGRLLCGASLVSSDWLVSAAHCVYGRNLEPSKWTAILGLHMKSNLTSPQTVPRLIDEIVINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTVVYQGTTANILQEADVPLLSNERCQQQMPEYNITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWIQSFLH
Protein: Xyloglucan endotransglucosylase/hydrolase protein 19 (At-XTH19) (XTH-19) (EC 2.4.1.207) (Q9M0D1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses xyloglucan endotransglucosylase (XET) activity in vitro. Does not possess xyloglucan endohydrolysis (XEH) activity. Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues. Involved in cell proliferation in the tissue reunion process of wounded inflorescence stems. Maybe a downstream target of NAC071 as a consequence of auxin action in wounded stems.
Subcellular location: Secreted, cell wall {ECO:0000305}. Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- NAC domain-containing protein 71
- Protein REDUCED WALL ACETYLATION 1
- Methylesterase 8
Sequence:
MKSFTFLILFLFAAQSISVYAGSFHKDVKIHWGDGRGKIHDNQGKLLSLSLDKSSGSGFQSNQEFLYGKAEVQMKLVPGNSAGTVTTFYLKSPGTTWDEIDFEFLGNISGHPYTLHTNVYTKGSGDKEQQFHLWFDPTANFHTYCITWNPQRIIFTVDGIPIREFMNAESRGVPFPTKQPMRLYASLWEAEHWATRGGLEKTDWSKAPFTAYYRNYNVEGCVWVNGKSVCPANSQWFTQKLDSNGQTRMKGVQSKYMVYNYCSDKKRFPRGVPPECS
Protein: FI05338p (Q9VIU4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- phosphatidate phosphatase
- Diacylglycerol kinase
- Ethanolamine kinase
- Diacylglycerol kinase
- Phospholipase
- Lysophospholipid acyltransferase 5
- Diacylglycerol kinase 1
- GH11618p
- FI04477p
Sequence:
MRQLFRRLMNHQYLTQDQINGFDNYKYSAIDTSPLSQYVMHPFWDWLVKFFPRWFAPNLMTFLGFLFSAMNLVLLSYYDWNFDASSGEEGTTPIPSWVWLCTAINIFLAYTLDGIDGKQARRIGLSGPLGELFDHGLDSYTAMLIPTCLYSIFGRSRVYSVRPMRMYYVCLTVYFNFFISHWEKYNTGILYLPWGYDLSMWGSTAMYLVTWWMGFERWKFELPLGSYGTLPLGNVMEAVLHVSAMANLPLVIINVYNSYAHRTGRLLSFWEAVRPMWPFITYFVILLAWPYVSPNDIMEKDPRAIFMLSGTIFSNVSCRLIVSQMSVTRCEAWHWQTPMFILSFLTSLWIPLLERPLLYLLLIVTTLSHWQYGASVVNQMCEHFNRVCFTVHKRVPQEELPKKKTLLAEEISQADKPQAEEPLKKDI
Protein: Bacillopeptidase (D2D3C3)
Organism: Bacillus amyloliquefaciens (Bacillus velezensis)
Interaction partners:
Sequence:
MKKKTRNRWTGSVLSAIVVSSLLFPGAAGANSTPGAVSFTKDLSSSKSIQHKISDSVKKRFEKNDKVTFLIKFKEKANTKKAVKEAEKNAKSQSLSAAKTEYQKRSAVVSSLKLAAHDAQQNLKTYLEKQKKKGKADHIHSYYIVNGMAVTASKEVMEKAASFPEVEKVLPNEKRQLTQRQSKAPFQMKKKQKEIKAKEGIEWNISQIDAPQAWASGYDGTGTVVASIDTGVQWEHPALKEKYRGYDPENPAKPNHEMNWYDAVSHKDAPYDDLEHGTHVTGTMTGSEPDGSNQIGVAPGAKWIAVKAFSDDGGTDADILDAGEWVLAPKDKNGTPHPEMAPDVVNNSWAGGSGMDEWYRDMVNAWRAAGIFPEFSAGNEDLFTPGGPGSIANPANYPETFATGATDIDKKLADFSLQGPSPYHETKPDISAPGVNIRSSIPGGTYEGGWDGTSMAGPHVAATAALLRQANASITVDEMEDVLTRTAEKLTDSVFPESPNNGYGHGLVNAFDAVSAVTDGIGSVAGKVSSAGEDHNPPSFHHEPVSAAYKGANLPLTVTAEDDVSVTEVILSYQFDEGEWKTTAAVQKSGDEKKGTYQAEIPDVTGSKISYKWTIKDFGGHSVESDTYRADVKPSVTAGYKEDFESQPAGWSSYGTHDQWEWGTPGSGPGTAFSGDKVYATNLSGPYADSANMNLVMPPIQVPETGRLFLQFKSWHKLEEFFDYGYVFVLPEGKSNWEQAAVYNGDSAGWNDEEADLSAYKGQNIKLMLNMQSDEVLNEDGWYIDDVRLSSSPLGKAAKKNKHKRQPPPGHLKKKAVSPKQAKPAVKSPGKRVKRETNLLPLRAQISVSETGKSVYSDPASGSYSLSHKAGSYTLKAEAYGFKSASKQVSIQSDKTAQADFTLEQMPSGTLKGTITNQSTGEPVKGAALYVAEDAAIEPAVTNDKGEYSLKAYEGSYTIKVAAKGFYNSEFSVDIKGDAEKNVKLKPYIGYEGEIAYDNGTEEAALSYFKAGSKSAVKMTLKDGKEHGMLTGGLFKFWGADWPDPGGTEFQAEVYDASGPDGAPGSKIAGPFQAEALRNGEWTKVDLSSKGIAVGKNFYLVFRQTKPDPYTPALSSDDGSPYSNRNWQYLDGRWSKTDKSDGNFMIRALVDYEASVPDITSPEDRSFTNKRSITVKGTASPKTAVRLTNNGKTAAETKADADGNFQAGVTLTEDANRLTAASVTDSGSTDESRPVTVILDEDKPDVTIDSPANGDKTNKEAVTVKGKVHDAHLEWVKVNGKKAEVNNGSYQARTLLENGSNEIKVTASDEAGNKTTKKTVIDVNYNAPVISGLVPGADKELKAGESVKIAFSSGKKLDASFVIRLPLTNARAGSQNATELPLREIFPGRYEGYWTATSSIKASGAKIDVIARDDYGNETRQTAKGKLYINE
Protein: Galectin-4 (Gal-4) (Antigen NY-CO-27) (L-36 lactose-binding protein) (L36LBP) (Lactose-binding lectin 4) (P56470)
Organism: Homo sapiens (Human)
Function: Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions.
Interaction partners:
- TATA-box-binding protein
- Transcription initiation factor IIB
- D-3-phosphoglycerate dehydrogenase
- Chromodomain-helicase-DNA-binding protein 7
- Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
- Cellular tumor antigen p53
- Cadherin-17
- Solute carrier organic anion transporter family member 6A1
- Galectin-3
- Transcription initiation factor TFIID subunit 12
Sequence:
MAYVPAPGYQPTYNPTLPYYQPIPGGLNVGMSVYIQGVASEHMKRFFVNFVVGQDPGSDVAFHFNPRFDGWDKVVFNTLQGGKWGSEERKRSMPFKKGAAFELVFIVLAEHYKVVVNGNPFYEYGHRLPLQMVTHLQVDGDLQLQSINFIGGQPLRPQGPPMMPPYPGPGHCHQQLNSLPTMEGPPTFNPPVPYFGRLQGGLTARRTIIIKGYVPPTGKSFAINFKVGSSGDIALHINPRMGNGTVVRNSLLNGSWGSEEKKITHNPFGPGQFFDLSIRCGLDRFKVYANGQHLFDFAHRLSAFQRVDTLEIQGDVTLSYVQI
Protein: BZIP domain-containing protein (A7S0E2)
Organism: Nematostella vectensis (Starlet sea anemone)
Interaction partners:
- BZIP domain-containing protein
Sequence:
MKKEGSSKILRETDISDELLATIPVKDLNNLLRGLPEDDVFKLKQRRRTLKNRGYAQNSRTKRVRQREDLEYERQQLKDELFMVSKENEDLRRERDEAKRKYDSLQKLLTSR
Protein: Glutathione S-transferase Mu 4 (EC 2.5.1.18) (GST class-mu 4) (GSTM4-4) (Glutathione transferase GSTM7-7) (Leukotriene C4 synthase GSTM4) (EC 4.4.1.20) (Q8R5I6)
Organism: Mus musculus (Mouse)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4. Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q03013}.
Interaction partners:
- Glutathione S-transferase theta-1
- Glutathione S-transferase theta-2
- Glutathione S-transferase kappa 1
- Glutathione S-transferase omega-2
- Glutathione S-transferase theta-3
- Glutathione S-transferase omega-1
- Glutathione S-transferase A3
- Glutathione S-transferase Mu 5
- Glutathione S-transferase theta-4
- Glutathione S-transferase Mu 1
Sequence:
MPMTLGYWDIRGLAHAIRLLLEYTGSSYEEKRYTMGDAPDYDRSQWLSEKFKLGLDFPNLPYLIDGSHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDFEKLKVEYLEQLPGMVKLFSQFLGQRTWFVGEKITFVDFLAYDILDLHLIFEPTCLDAFPNLKDFVARFEVLKRISAYMKTSRFLRTPLYTKVATWGNK
Protein: UL16 binding protein 1 (UL16-binding protein-like transcript 1 splice variant) (D2CKI9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MELTASNKVLSCCLSLLCLLSVCLCPRIEETASLCNIYKVNRSESGQHSHEVQGLLNRQPLFVYKDKKCHAIGAHRNSMNATKICEKEVDTLKDGIDIFKGLLLHIVQETNTTGKPLTLQAEVCGQYEVDKHFTGYAIVSLNGKNIFRVDTSTGNWTQLDHEFEKFIEMCKEDKVLAAFLKKTTEGDCRTWLDELMLHWKEHLEPAGSFSTLMIILCVIAIAFLGLIFGVSCKLRHLRTKKIGLQSSPPPLLDDSLTVPTSPQSSVCGTMIQCLCPRKLKSPVFMQVKWFESPLLSLIGFAKYSLE
Protein: Fcgbp protein (Q497G7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
NNDKIVSKVHIFFQDGLVTVIPSKGAWVNGLRVDLPATVLTSVSVRRMPDGSMLVHQKAGVTVWLGKDGLLDVMVGDDLAAMLCGACGNFDGDQTNDAYGSQGKTPIEKWRAQDFSPCSN
Protein: Eukaryotic translation initiation factor 3 subunit L (eIF3l) (Q38BD7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03011}.
Interaction partners:
- CSN8/PSMD8/EIF3K domain-containing protein
- RNA-binding protein, putative
- Eukaryotic translation initiation factor 3 subunit 7-like protein
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit 8, putative
- Eukaryotic translation initiation factor 3 subunit E
- Translation initiation factor, putative
- protein-synthesizing GTPase
- Elongation initiation factor 2 alpha subunit, putative
Sequence:
MASNPDSKLHIPDEMFNFFNSLNTAVDTGDISSFHNLYENIFPSHLSKYYAAEQGEFRPLPVLQRMEVAECFGNDTAGKLYSFLCFKHLFTDRDVTAEDAKVSWRTFCDLFVSLPGSCDIPNWFLWDIFDEFLFQMTVVYQKRFAEGAEWSVTEAVQMMEKVISESGIEEVMESDKADDITKSGENHVRWMSGFFGIITVAKINVLLGDYNSALSVLKPLDIYGRGKKILAEVAPANVSLMYYVGFSYLMLRRYADASRVFRQSLSAKVSSRKFSERVRLDCAFMHVVSCILCGTQPDNLSWLMDSRKLQVLEDDKELLATGDEERFRDVFDRCSPKFLAVPPVPPTVCKGMEGKELQARLFLRAVKQQQDTIKLRVYLGVYQTTTTELVKTVLDVNDGLVPLFAMKLTSRQLVHDGVSADLHSGTYVVRAALDCTVEGDNICVVQKSSYRTIESKYFKRMTQRRPRHRHFDNPRQGRRPAPDAHNTN