wanglab/gogpt-training-data huggingface dataset:
Protein: Pancreatic lipase-related protein 2 (PL-RP2) (Cytotoxic T lymphocyte lipase) (Galactolipase) (EC 3.1.1.26) (Secretory glycoprotein GP-3) (Triacylglycerol lipase) (EC 3.1.1.3) (P54318)
Organism: Rattus norvegicus (Rat)
Function: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides. In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (By similarity). Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity. Can completely deacylate triacylglycerols (By similarity). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase (By similarity). Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (By similarity). Hydrolyzes medium- and long-chain fatty acyls in galactolipids. May act together with LIPF to hydrolyze partially digested triglycerides (By similarity). Hydrolyzes long-chain monoglycerides with high efficiency. In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity. In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids. The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P54317}. Zymogen granule membrane {ECO:0000269|PubMed:8486693}; Peripheral membrane protein {ECO:0000305|PubMed:8486693}. Cell projection, neuron projection {ECO:0000269|PubMed:32963038}. Note=Localizes to neurite tips in neuronal cells. {ECO:0000269|PubMed:32963038}.
Interaction partners:
- Bile salt-activated lipase
- Gastric triacylglycerol lipase
- Colipase
- Inactive pancreatic lipase-related protein 1
- Pancreatic triacylglycerol lipase
- Diacylglycerol O-acyltransferase 1
- Patatin-like phospholipase domain-containing protein 2
- Acylglycerol transacylase
- Hepatic triacylglycerol lipase
- Diacylglycerol O-acyltransferase 2
Sequence:
MLLCWIVSLLLATVGGKEVCYGHLGCFSNDKPWAGMLQRPLKIFPWSPEDIDTRFLLYTNENPNNYQKISATEPDTIKFSNFQLDRKTRFIVHGFIDKGEDGWLLDMCKKMFQVEKVNCICVDWRRGSRTEYTQASYNTRVVGAEIAFLVQVLSTEMGYSPENVHLIGHSLGAHVVGEAGRRLEGHVGRITGLDPAEPCFQGLPEEVRLDPSDAMFVDVIHTDSAPIIPYLGFGMSQKVGHLDFFPNGGKEMPGCQKNILSTIVDINGIWEGTQNFVACNHLRSYKYYASSILNPDGFLGYPCSSYEKFQQNDCFPCPEEGCPKMGHYADQFEGKTATVEQTVYLNTGDSGNFTRWRYKVSVTLSGAKKLSGYILVALYGNNGNSKQYEIFKGSLKPEARHVRDIDVDINVGEIQKVKFLWNNKVINLFRPTLGASQITVQSGVDGKEYNFCSSDTVREDVLQSLYPC
Protein: Carboxypeptidase A4 (EC 3.4.17.-) (Carboxypeptidase A3) (Q9UI42)
Organism: Homo sapiens (Human)
Function: Metalloprotease that could be involved in the histone hyperacetylation pathway. Releases a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val.
Subcellular location: Secreted {ECO:0000269|PubMed:20385563}.
Interaction partners:
- Latexin
- Chymase
- Tryptase alpha/beta-1
- Mesoderm-specific transcript homolog protein
- Cathepsin G
Sequence:
MRWILFIGALIGSSICGQEKFFGDQVLRINVRNGDEISKLSQLVNSNNLKLNFWKSPSSFNRPVDVLVPSVSLQAFKSFLRSQGLEYAVTIEDLQALLDNEDDEMQHNEGQERSSNNFNYGAYHSLEAIYHEMDNIAADFPDLARRVKIGHSFENRPMYVLKFSTGKGVRRPAVWLNAGIHSREWISQATAIWTARKIVSDYQRDPAITSILEKMDIFLLPVANPDGYVYTQTQNRLWRKTRSRNPGSSCIGADPNRNWNASFAGKGASDNPCSEVYHGPHANSEVEVKSVVDFIQKHGNFKGFIDLHSYSQLLMYPYGYSVKKAPDAEELDKVARLAAKALASVSGTEYQVGPTCTTVYPASGSSIDWAYDNGIKFAFTFELRDTGTYGFLLPANQIIPTAEETWLGLKTIMEHVRDNLY
Protein: Anaerobic glycerol-3-phosphate dehydrogenase subunit C (G-3-P dehydrogenase) (P0A996)
Organism: Escherichia coli (strain K12)
Function: Electron transfer protein; may also function as the membrane anchor for the GlpAB dimer.
Subcellular location: Cell inner membrane; Peripheral membrane protein. Note=Loosely bound to the cytoplasmic membrane often occurring in vesicles associated with fumarate reductase.
Interaction partners:
- Anaerobic glycerol-3-phosphate dehydrogenase subunit B
- Anaerobic glycerol-3-phosphate dehydrogenase subunit A
- Aerobic glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate transporter
- Glycerophosphodiester phosphodiesterase, periplasmic
- Glycolate oxidase subunit GlcD
- Probable glycerol-3-phosphate acyltransferase
- Glycerol-3-phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol kinase
Sequence:
MNDTSFENCIKCTVCTTACPVSRVNPGYPGPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDVKIGDIIQRARAKYDTTRPSLRNFVLSHTDLMGSVSTPFAPIVNTATSLKPVRQLLDAALKIDHRRTLPKYSFGTFRRWYRSVAAQQAQYKDQVAFFHGCFVNYNHPQLGKDLIKVLNAMGTGVQLLSKEKCCGVPLIANGFTDKARKQAITNVESIREAVGVKGIPVIATSSTCTFALRDEYPEVLNVDNKGLRDHIELATRWLWRKLDEGKTLPLKPLPLKVVYHTPCHMEKMGWTLYTLELLRNIPGLELTVLDSQCCGIAGTYGFKKENYPTSQAIGAPLFRQIEESGADLVVTDCETCKWQIEMSTSLRCEHPITLLAQALA
Protein: Metallothionein-2 (MT-2) (Metallothionein-II) (MT-II) [Cleaved into: Metallothionein-2' (MT-2') (Metallothionein-II') (MT-II')] (P15114)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: The metallothioneins are involved in the cellular sequestration of toxic metal ions.
Interaction partners:
- Metallothionein-1
Sequence:
MPEQVNCQYDCHCSNCACENTCNCCAKPACACTNSASNECSCQTCKCQTCKC
Protein: Protein SOSEKI 2 (AtSOK2) (Protein UPSTREAM OF FLC) (Q9LX14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of a three-gene cluster containing FLC, UFC and DFC, which is coordinately regulated in response to vernalization. Also regulated by FLX. SOSEKI proteins (SOK1-5) locally interpret global polarity cues and can influence cell division orientation to coordinate cell polarization relative to body axes, probably by guiding ANGUSTIFOLIA (AN) polarized localization.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30737509}; Peripheral membrane protein {ECO:0000269|PubMed:30737509}; Cytoplasmic side {ECO:0000269|PubMed:30737509}. Note=SOSEKI proteins integrate apical-basal and radial organismal axes to localize to polar cell edges, pointing towards the epidermis, mainly to inner basal edges. {ECO:0000269|PubMed:30737509}.
Interaction partners:
- ARM-repeat/Tetratricopeptide repeat
- PHD finger-like domain-containing protein 5A
- Protein DOWNSTREAM OF FLC
- Uncharacterized protein
- Glutamyl-tRNA
- Putative F-box protein At5g51000
- Probable protein phosphatase 2C 25
Sequence:
MEAVRCRRGRENNKSPERIIRSLNHHQHDEELEEEVKTKKPIFRRVQVVYYLTRNGHLEHPHFIEVISPVNQPLRLRDVMNRLTILRGKCMTSQYAWSCKRSYRNGFVWNDLAENDVIYPSDCAEYVLKGSEITDKFQEVHVNRPLSGSIQEAPKSRLLRSKLKPQNRTASFDDAELYVGEEEEEEDGEYELYEEKTSYTSSTTPQSRCSRGVSTETMESTEQKPNLTKTEQDLQVRSDSSDLTRSNPVVKPRRHEVSTRVEDGDPVEPGSGRGSMWLQMISCGHIATKYYAPSVMNPRQKEENLRKGVLCKNIVKKTVVDDEREMIRFMSENPRFGNPQAEEKEYFSGSIVESVSQERVTAEPSLRRSNSFNEERSKIVEMAKETKKKEERSMAKVKCIPRTCLMSSSKQIKK
Protein: Pro-neuregulin-3, membrane-bound isoform (Pro-NRG3) [Cleaved into: Neuregulin-3 (NRG-3)] (O35181)
Organism: Mus musculus (Mouse)
Function: Direct ligand for the ERBB4 tyrosine kinase receptor. Binding results in ligand-stimulated tyrosine phosphorylation and activation of the receptor. Does not bind to the EGF receptor, ERBB2 or ERBB3 receptors.
Subcellular location: [Pro-neuregulin-3, membrane-bound isoform]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}.; SUBCELLULAR LOCATION: [Neuregulin-3]: Secreted {ECO:0000250}.
Interaction partners:
- Receptor tyrosine-protein kinase erbB-4
- Pro-neuregulin-4, membrane-bound isoform
- Pro-neuregulin-2, membrane-bound isoform
- Pro-neuregulin-1, membrane-bound isoform
- SKA complex subunit 1
- SKA complex subunit 3
- SKA complex subunit 2
- Epidermal growth factor receptor
Sequence:
MSEGAAGASPPGAASAAAASAEEGTAAAAAAAAAGGGPDGGGEGAAEPPRELRCSDCIVWNRQQTWLCVVPLFIGFIGLGLSLMLLKWIVVGSVKEYVPTDLVDSKGMGQDPFFLSKPSSFPKAMETTTTTTSTTSPATPSAGGAASSRTPNRISTRLTTITRAPTRFPGHRVPIRASPRSTTARNTAAPPTVLSTTAPFFSSSTPGSRPPMPGAPSTQAMPSWPTAAYATSSYLHDSTPSWTLSPFQDAAAASSSSPSSTSSTTTTPETSTSPKFHTTTYSTERSEHFKPCRDKDLAYCLNDGECFVIETLTGSHKHCRCKEGYQGVRCDQFLPKTDSILSDPTDHLGIEFMESEDVYQRQVLSISCIIFGIVIVGMFCAAFYFKSKKQAKQIQEHLKESQNGKNYSLKASSTKSESLMKSHVHLQNYSKADRHPVTALEKIMESSFSAPQSFPEVTSPDRGSQPIKHHSPGQRSGMLHRNTFRRAPPSPRSRLGGIVGPAYQQLEESRIPDQDTIPCQGIEVRKTISHLPIQLWCVERPLDLKYVSNGLRTQQNASINMQLPSRETNPYFNSLDQKDLVGYLSPRANSVPIIPSMGLEETCMQMPGISDVKSIKWCKNSYSADIVNASMPVSDCLLEEQQEVKILLETVQEQIRILTDARRSEDFELASMETEDSASENTAFLPLSPTAKSEREAQFVLRNEIQRDSVLTK
Protein: Lipid A biosynthesis palmitoleoyltransferase (EC 2.3.1.242) (Kdo(2)-lipid IV(A) palmitoleoyltransferase) (P0ACV2)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of palmitoleate from palmitoleoyl-[acyl-carrier-protein] (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(palmitoleoyl)-lipid IV(A). Required for the biosynthesis of a distinct molecular species of lipid A, which is present only in cells grown at low temperatures. It may confer a selective advantage to cells growing at lower temperatures by making the outer membrane a more effective barrier to harmful chemicals.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01943, ECO:0000305}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01943}.
Interaction partners:
- 3-deoxy-D-manno-octulosonic acid transferase
- Lipid A biosynthesis myristoyltransferase
- Lipid A biosynthesis lauroyltransferase
- UDP-3-O-
- Lipid-A-disaccharide synthase
- Acetylornithine/succinyldiaminopimelate aminotransferase
- Tetraacyldisaccharide 4'-kinase
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
- Heme exporter protein B
- UDP-3-O-acyl-N-acetylglucosamine deacetylase
Sequence:
MFPQCKFSREFLHPRYWLTWFGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFRSLGMALVETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNQLMEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVTMVRKADYSGYRLFITPEMEGYPTDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLYI
Protein: Ornithine aminotransferase, mitochondrial (EC 2.6.1.13) (Ornithine delta-aminotransferase) (Ornithine--oxo-acid aminotransferase) [Cleaved into: Ornithine aminotransferase, hepatic form; Ornithine aminotransferase, renal form] (P04181)
Organism: Homo sapiens (Human)
Function: Catalyzes the reversible interconversion of L-ornithine and 2-oxoglutarate to L-glutamate semialdehyde and L-glutamate.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:23076989}.
Interaction partners:
- Arginase-2, mitochondrial
- Arginase-1
- Delta-1-pyrroline-5-carboxylate synthase
- N-acetylglutamate synthase, mitochondrial
- Argininosuccinate lyase
- Ornithine transcarbamylase, mitochondrial
- Argininosuccinate synthase
- Ornithine decarboxylase
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Argininosuccinate lyase
Sequence:
MFSKLAHLQRFAVLSRGVHSSVASATSVATKKTVQGPPTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEGRKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYHKVLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGRTLSAISSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEAGVVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPDIVLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIAALEVLEEENLAENADKLGIILRNELMKLPSDVVTAVRGKGLLNAIVIKETKDWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKTILSF
Protein: Protein PIR (PIR of plants) (Protein KLUNKER) (AtSRA1) (Protein PIROGI) (Q5S2C3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the ARP2/3 complex. Interacts with the active form of RHO-family GTPases.
Interaction partners:
- Protein NAP1
- Protein BRICK 1
- Protein ABIL1
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 2A
- Eukaryotic translation initiation factor isoform 4E
- Eukaryotic translation initiation factor 4E-3
- Actin-related protein 3
- Eukaryotic translation initiation factor 4E-2
- Eukaryotic translation initiation factor 4E-1
Sequence:
MAVPVEEAIAALSTFSLEDEQPEVQGPAVMVSAERAATDSPIEYSDVAAYRLSLSEDTKALNQLNTLIQEGKEMASILYTYRSCVKALPQLPESMKHSQADLYLETYQVLDLEMSRLREIQRWQSSASAKLAADMQRFSRPERRINGPTVTHLWSMLKLLDVLVQLDHLKNAKASIPNDFSWYKRTFTQVSAQWQDTDTMREELDDLQIFLSTRWAILLNLHVEMFRVNNVEDILQVLIVFIVESLELDFALLFPERYILLRVLPVLVVLATPSEKDTEALYKRVKLNRLINIFKNDPVIPAFPDLHLSPAAILKELSVYFQKFSSQTRLLTLPAPHELPPREALEYQRHYLIVNHIGALRAEHDDFTIRFASSMNQLLLLKSNDGAYTEWCREVKGNMYDMVVEGFQLLSRWTARIWEQCAWKFSRPCRDAGETPEASGSYSDYEKVVRFNYTAEERKALVELVGYIKSVGSMLQRCDTLVADALWETIHAEVQDFVQNTLATMLRTTFRKKKDLSRILSDMRTLSADWMANTRPEHEMPSSQHGNDESRGNFFYPRPVAPTAAQVHCLQFLIYEVVSGGNLRRPGGFFGNNGSEIPVNDLKQLETFFYKLSFFLHILDYSASIGILTDLGFLWFREFYLESSRVIQFPIECSLPWMLIDYILEAQNSGLLESVLLPFDIYNDSAQQALVVLRQRFLYDEIEAEVDHGFDIFVSRLSESIFTYYKSWSASELLDPSFLFALDNGEKFSIQPVRFTALFKMTKVKILGRTINLRSLIAQRMNRIFRENLEFLFDRFESQDLCAVVELEKLIDILKHSHELLSQDLSIDPFSLMLNEMQENISLVSFSSRLATQIWSEMQSDFLPNFILCNTTQRFVRSSKVPPTQKPSVPSAKPSFYCGTQDLNAAHQSFARLHSGFFGIPHLFSIVKLLGSRSLPWLIRALLDHISNKITTLEPMISGLQEALPKSIGLLSFDGGVTGCMKLIREQLNWGTKSELKSEVLRGIKEIGSVIYTMGLLDIVLREVDTKRFMQTAPWLGLIPGAEGQIVNAQDGESPLVNLLKSATSAVVSSPGCLNPAAFYTMSKQAEAADLLYKANMNGGSVLEYTLAFTSASLDKYCSKWSAPPKTGFVDITTSKDFYRIYGGLQIGYLEEITAPQSAQHEVLGDSIAWGGCTIIYLLGQQLHFELFDFSYQVLNVSEVETVSASHTHRNPQIHQGWEGLLEGMKKARRLNNHVFSMLKARCPLEDKTACAIKQSGAPLPRVRFENTVSAFETLPQKGTVG
Protein: Farnesyl pyrophosphate synthase (EC 2.5.1.10) (Q57WF1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Isopentenyl-diphosphate delta-isomerase, putative
- Diphosphomevalonate decarboxylase
- Diphosphomevalonate decarboxylase
- squalene synthase
- Protein farnesyltransferase subunit beta
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Mevalonate kinase
- Cis-prenyltransferase-like protein
- Farnesyl pyrophosphate synthetase, putative
Sequence:
MVMQMFMQVYDEIQMFLLEELKLKFDMDPNRVRYLRKMMDTTCLGGKYNRGLTVIDVAESLLSLSPNNNGEKDDGARRKRVLHDACVCGWMIEFLQAHYLVEDDIMDNSVTRRGKPCWYRHPGVTVQCAINDGLLLKSWTHMMAMHFFADRPFLQDLLCRFNRVDYTTAVGQLYDVTSMFDSNKLDPDVSQPTTTDFAEFTLSNYKRIVKYKTAYYTYLLPLVMGLIVSEALPTVDMGVTEELAMLMGEYFQVQDDVMDCFTPPERLGKVGTDIQDAKCSWLAVTFLAKASSAQIAEFKANYGSGDSEKVATVRRLYEEADLQEDYVAYEAAVAEQVKELIEKLRLCSPGFAASVETLWGKTYKRQK
Protein: Pantothenate synthetase (PS) (EC 6.3.2.1) (Pantoate--beta-alanine ligase) (Pantoate-activating enzyme) (P9WIL5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Type III pantothenate kinase
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Aspartate 1-decarboxylase
- Conserved hypothetical alanine and leucine rich protein
- Pantothenate kinase
- Glutamate decarboxylase
- 2-dehydropantoate 2-reductase
- Coenzyme A biosynthesis bifunctional protein CoaBC
- Cytidylate kinase
- aldehyde dehydrogenase
Sequence:
MTIPAFHPGELNVYSAPGDVADVSRALRLTGRRVMLVPTMGALHEGHLALVRAAKRVPGSVVVVSIFVNPMQFGAGEDLDAYPRTPDDDLAQLRAEGVEIAFTPTTAAMYPDGLRTTVQPGPLAAELEGGPRPTHFAGVLTVVLKLLQIVRPDRVFFGEKDYQQLVLIRQLVADFNLDVAVVGVPTVREADGLAMSSRNRYLDPAQRAAAVALSAALTAAAHAATAGAQAALDAARAVLDAAPGVAVDYLELRDIGLGPMPLNGSGRLLVAARLGTTRLLDNIAIEIGTFAGTDRPDGYRAILESHWRN
Protein: Histone deacetylase (EC 3.5.1.98) (Q8I9J7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
Interaction partners:
Sequence:
MSSPDDRIPIHDLPSEAGSDERLLHITPATLTLDFKPHPAVDIDQQIMELKKSQELQKQRLINSFQEQSKQMELEHKLQLEHKYQFAVNSHGAFQELRNESMVTAAAAAVAQEQHRQQLHQQQQQHQQQQQQQQHQQQQQQQQARGRDGMKLKQNCSANASPEVKQILNCFILSRKSQAAASNGTTTTSPYRNRGVVKSSSGESLPAGTVTSAHPYKIPQPPPSLLKYESDFPLRKTDCNSTPDSGPNSPPSAAALTVGVVGSRGSPTSAPIQEENEEGSQYQPGQRSSINDLPLFSSPSLPNISLGRPHLPNSAQAHAQVNAQVAAQAQAQAQAQAQAHAMFAALAAAQGGCGQPGYYNPLGMAFVGRQPAPLAMIPATGIAPQQPSPVVRSASATSTSSSQASLVGDVAPPQAHAASTILPSSSSYMQQLGSVAGSGVNLHAAAVAAAAAAAAAAGSLPPTNSHGHGHGSHAHPHPHAHGHGHGHGHGIYAGHQHNVPITDAQVAQVHLHKQGHRPLGRTQSAPLPLGHPMLTGAVQLNVVQTHYENSEAERQAYEHQVVNQKVRQTVLTRSGAAAAAAAAAGVSVVREAQLKEEDDDSAAEVMDLTDKKKPPKTVLTSTIATSTSQNLPEALAAAAAAAAYRAPHNASSNSASATKSGIKLRDQEYLQQQREQLLLLQQEEELAKSLMRPLSRTLSSPLVPLGPHGLSQIPDTGQQPAPIATSSSADHIPPVNLSLPHRQHRQLMSTLYASQLRNHQPSASGSPPHKVTTGLAYDPLMLKHSCICGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQCQLSRPKLENTLSASFVRLSCGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRMPEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPTECGSGAGLGFNVNISWSGALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAPLGGYHVSPACFGFMTRELLQLANGKVVLALEGGYDLAAICDSAQECVRALLGDPAAPIAKAELERPPCQNAINTLQKTIAIQQTHWPCVRMLEHTVGLSALETLKVEHDESETINAMAGLSMQSMHRTLSRDDSEEPMDQDETK
Protein: Ribonuclease/angiogenin inhibitor 1 (H0YCR7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
ESCGVTSDNCRDLCGIVASKASLRELALGSNKLGDVGMAELCPGLLHPSSRLRTLWIWECGITAKGCGDLCRVLRAKESLKELSLAGNELGDEGARLLCETLLEPGCQLESLWVKSCSFTAACCSHFSSVLAQNRFLLELQISNNRLEDAGVRELCQGLGQPGSVLRVLWLADCDVSDSSCSSLAATLLANHSLRELDLSNNCLGDAGILQLVESVRQPGCLLEQLVYVHALGGWCGQGCPGRKAGVGEDTGPCLPSGLCAACTTFTGLRRWRTGCRPWRRTSHP
Protein: Folate receptor beta (D4A4S5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Sperm-egg fusion protein Juno
- Folate receptor alpha
- Izumo sperm-egg fusion protein 1
- Glycine N-methyltransferase
Sequence:
MAWKQTPLLLLVYMITTCSARDRTDLLNVCMDAKHHKTKPGPEDKLHDQCSPWKRNACCSVNTSQELHKDNSRLYNFNWDHCGEMTPACKRHFIQDACLYECSPNLGPWIQQAGQSWRKERFLDVPLCKEDCQEWWEACRTSFTCKRDWHKGWDWTSGINKCPDTAPCRTFQYYFPTPASLCEGLWSHSYKVSNYSRGSGQCIQMWFDSTQGNPNEEVVKFYASFMTSGTVYHAAILLVPSLAPVLSLWLPD
Protein: Cell division protein FtsX (A5FMG4)
Organism: Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae)
Function: Required for cell division and gliding motility.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P0AC30}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0AC30}.
Interaction partners:
- Cell division ATP-binding protein FtsE
- Peptidase subfamily M23B-like protein
- Cell division protein FtsZ
- Cell division protein FtsA
- DUF3098 domain-containing protein
Sequence:
MSSNFDKFQKRRLISSYFSVVLSVFLVLFLLGVLGLFIINSKKLADDFKEKIAMTVFFKNEANDSIIKAFNSELKRAPFALSYVYVTKEKAAKEHTDIIGEDFLTFLGENPLLNSYDIHLKADYVERDSILKIESALRKNTMIEDIVYDKQLVNLVNDNIKKVSMWILIISGFLTVIAVLLINSSLRLSIHSNRFIIKTMQMVGATKSFIRKPFVMRSVKLGMLGALLAIIALIGLLFYVETNFPGLGILEDKALIGLVLLAVFGLGVLITWVSTHFATQRFLNLRTDDLY
Protein: Pyruvate decarboxylase 2 (AtPDC2) (EC 4.1.1.1) (Q9FFT4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Alcohol dehydrogenase class-P
- Alcohol dehydrogenase-like 6
- Alcohol dehydrogenase-like 3
- Alcohol dehydrogenase-like 4
- L-lactate dehydrogenase
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Alcohol dehydrogenase class-3
- Pyruvate, phosphate dikinase 1, chloroplastic
- Aldehyde dehydrogenase family 2 member B4, mitochondrial
Sequence:
MDTKIGSIDACNPTNHDIGGPPNGGVSTVQNTSPLHSTTVSPCDATLGRYLARRLVEIGVTDVFSVPGDFNLTLLDHLIAEPNLKLIGCCNELNAGYAADGYARSRGVGACVVTFTVGGLSVLNAIAGAYSENLPLICIVGGPNSNDYGTNRILHHTIGLPDFTQELRCFQAVTCFQAVINNLEEAHELIDTAISTALKESKPVYISISCNLPAIPLPTFSRHPVPFMLPMKVSNQIGLDAAVEAAAEFLNKAVKPVLVGGPKMRVAKAADAFVELADASGYGLAVMPSAKGQVPEHHKHFIGTYWGAVSTAFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGNGPAFGCVLMKDFLSELAKRIKHNNTSYENYHRIYVPEGKPLRDNPNESLRVNVLFQHIQNMLSSESAVLAETGDSWFNCQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAMPNRRVIACIGDGSFQVTAQDVSTMIRCGQKTIIFLINNGGYTIEVEIHDGPYNVIKNWNYTAFVEAIHNGEGKCWTAKVRCEEELVKAINTATNEEKESFCFIEVIVHKDDTSKELLEWGSRVSAANSRPPNPQ
Protein: Probable transporter YedE (P31064)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Putative sulfur carrier protein YedF
Sequence:
MSWQQFKHAWLIKFWAPIPAVIAAGILSTYYFGITGTFWAVTGEFTRWGGQLLQLFGVHAEEWGYFKIIHLEGSPLTRIDGMMILGMFGGCFAAALWANNVKLRMPRSRIRIMQAIIGGIIAGFGARLAMGCNLAAFFTGIPQFSLHAWFFAIATAIGSWFGARFTLLPIFRIPVKMQKVSAASPLTQKPDQARRRFRLGMLVFFGMLGWALLTAMNQPKLGLAMLFGVGFGLLIERAQICFTSAFRDMWITGRTHMAKAIIIGMAVSAIGIFSYVQLGVEPKIMWAGPNAVIGGLLFGFGIVLAGGCETGWMYRAVEGQVHYWWVGLGNVIGSTILAYYWDDFAPALATDWDKINLLKTFGPMGGLLVTYLLLFAALMLIIGWEKRFFRRAAPQTAKEIA
Protein: Protein Wnt (Q6IYD9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU003500}.
Interaction partners:
Sequence:
MIYLGYFLFLFCGLTRVMASYPIWWSLAVGHQYTSLGTQPIMCSSIPGLVPKQLRFCRNYVEIMPSVAEGVKIGIQECQHQFRGRRWNCTTINDKLAIFGPVLDKEKERKIGFKQAKATRESAFVHAIASAGVAFXVTRACTEGSATICGCDSRRKGPPGEGWKWGGCSEDVEFGSMVSREFADARENRPDARSAMNRHNNEAGRSSITDHMYLKCKCHGLSGSCEVKTCWWSQPDFRVIGDYMKDKYDSASEMVVEKHRESRGWVETLRPKYPYYKPPTETDLVYYESSPNFCEPNPETGSFGTRDRTCNLTSHGIDGCDLLCCGRGHNTRTEKRKEKCHCIFHWCCYVSCQECTRVYDVHTCK
Protein: Membrane-associated progesterone receptor component 1 (G5E5M5)
Organism: Bos taurus (Bovine)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}. Microsome membrane {ECO:0000256|ARBA:ARBA00004111}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004111}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00037812}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00037812}; Extracellular side {ECO:0000256|ARBA:ARBA00037812}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MEGWEKVKAGEMELVFGSHQVAEKTLHRARQSQAAIMAAEDVAATGADTSELESGGLLQEIFTSPLNLLLLGLCIFLLYKIVRGDQPAASDSDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTPAQQETLSDWDSQFTFKYHHVGKLLKDGEEPTVYSDEEEPKDESTRKND
Protein: DNA mismatch repair protein, putative (Q389N7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mismatch repair protein MSH8, putative
- Mismatch repair protein MSH3, putative
- Mismatch repair protein MLH1
- Mismatch repair protein PMS1, putative
- Exonuclease, putative
- Proliferating cell nuclear antigen
- MutL C-terminal dimerisation domain-containing protein
- Flap endonuclease 1
- DNA repair protein, putative
- DNA repair protein, putative
Sequence:
MSDDRDPAVVQAFNGAGGDDTSCLRLFSRASAGCFILGSWASLVAREYVKSTAVLKNWSGVDAVAVNDSITREVIRDCLLRRGVSVEQYDRQTSGGRYVCMRRGSPGHIADFEAMLFAFEDAEIQLMAIGSVVIDDKANRVNGPGGQHVRVGYAALNTTLRTLTYAEYHDTPQLTNLDVLMAQCNLKQLLYSNTDFSMNNTGEKAADSDESREQSDLLRALKQLCERANITLQERGQSNLPHGKQKSRATKRNSTGPNGELLSTLEGILRVPEDRHGLNSFPLASRALESLLESAIDPFDSTNQHTFYLKHVVPSTFMKMDAAAIEALHIIHRKPEARGSMPTSIYSWLNRCTTGMGSRLMQQWLLQPLRSIEDINQRLSLVQIMVESPILRDALITQVLRRCTDMDRLNRKLQRRTVALKDLQSILVFANTVPLAVDVLRTYHGGHDSSLLLKGYVTPLEDISEHLSNLRTLINATVDLSDENTVRINPEFDDDLSFLERQRQNLVKAIEKENHRVLKQCGWTEKQMKCEYHASYGYVFRVPRKDDHQVRTSKEFITVSTAKDGVRFVSGQLSSLSEQYKGITEDYKTRQQVLKKKLVDTVATYLPVLDDAKELLAALDVFAAWALVVKDSSRPMVRPTVRAPQSEEVKGNVDNNSNGAILTIVNARHPLVELRQPAFTPNTVQLTNEANALIITGPNMGGKSTFMRSIGVCVALAQAGCFVPADSADIVVRDAIMCRVGATDHLAQGVSTFMVEMLESAAMLNSATQQTLAIVDELGRGTSTYDGFGLAWAIAQEVAVNAKSALLFSTHFHEMTQLAARHTNVRNVHFGADVDTAARTLRFSYQLQPGPCGRSYGLYVAQLAHIPDDVLDSARQKAVELEDFGGDETKNRAQALFSTATPEVVQRVTEYAKRIRELESGEGDGDSREAARRRLCSEIKEDALLSSLVEV