wanglab/gogpt-training-data huggingface dataset:
Protein: Immunoglobulin heavy variable 3-7 (Ig heavy chain V-III region GAL) (Ig heavy chain V-III region GAR) (Ig heavy chain V-III region JON) (P01780)
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:
MELGLSWVFLVAILEGVQCEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVANIKQDGSEKYYVDSVKGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCAR
Protein: Thioredoxin X, chloroplastic (AtTrxx) (Q8LD49)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable thiol-disulfide oxidoreductase that may participate in various redox reactions.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19259774}.
Interaction partners:
- 2-Cys peroxiredoxin BAS1, chloroplastic
- 2-Cys peroxiredoxin BAS1-like, chloroplastic
- NADPH-dependent thioredoxin reductase 3
- Glutamyl-tRNA
- Protein CHLORORESPIRATORY REDUCTION 42
- Protein trichome birefringence-like 20
Sequence:
MDSIVSSSTILMRSYLTPPVRSCSPATSVSVKPLSSVQVTSVAANRHLLSLSSGARRTRKSSSSVIRCGGIKEIGESEFSSTVLESAQPVLVEFVATWCGPCKLIYPAMEALSQEYGDKLTIVKIDHDANPKLIAEFKVYGLPHFILFKDGKEVPGSRREGAITKAKLKEYIDGLLNSISVA
Protein: Aldehyde dehydrogenase 2 family (Mitochondrial)a (Aldehyde dehydrogenase 2 family member, tandem duplicate 1 (EC 1.2.1.3)) (Q7SXU3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLRTVFSRTFPQVFRISSCQHSTIPAPNVQPDVHYNKIFINNEWHDAVSKKTFPTINPATAEVICHVAEGDKADVDKAVKAARDAFKLGSPWRRMDASQRGLLLNRLADCIERDAAYLAELETLDNGKPYTLSFCVDLPMVVKCLRYYAGWADKWEGKTIPIDGNYFCYTRHEPIGVCGQIIPWNFPLLMQALKLGPALATGNTVVMKVAEQTPLTALYIASLIKEVGFPAGVVNIVPGFGPTAGAAIASHMDVDKVAFTGSTDVGHLIQQASSASNLKNVSLELGGKSPNIILSDANMEEAVEQAHSALFFNQGQCCCAGTRTFVQESIYDEFVERSVERAKNRIVGDPFDLNTEQGPQVDEDQFKKVLGYISSGKREGAKLMCGGAPAAERGYFIQPTVFGDVKDDMTIAREEIFGPVMQILKFKSLEEVIERANDSKYGLAAAVFTQNIDKANYISHGLRAGTVWINCYNVFGVQAPFGGYKASGIGRELGEYGLDIYTEVKTVTIKVPQKNS
Protein: Flagellar motor switch protein FliG (P0ABZ1)
Organism: Escherichia coli (strain K12)
Function: FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
Subcellular location: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Bacterial flagellum basal body.
Interaction partners:
- Flagellar basal-body rod protein FlgG
- Flagellar hook-basal body complex protein FliE
- Flagellum-specific ATP synthase
- Flagellar biosynthetic protein FliQ
- Flagellar hook-length control protein
- Flagellar assembly protein FliH
- Flagellar hook protein FlgE
- Flagellar M-ring protein
- Flagellar basal-body rod protein FlgC
- Flagellar protein FliO
Sequence:
MSNLTGTDKSVILLMTIGEDRAAEVFKHLSQREVQTLSAAMANVTQISNKQLTDVLAEFEQEAEQFAALNINANDYLRSVLVKALGEERAASLLEDILETRDTASGIETLNFMEPQSAADLIRDEHPQIIATILVHLKRAQAADILALFDERLRHDVMLRIATFGGVQPAALAELTEVLNGLLDGQNLKRSKMGGVRTAAEIINLMKTQQEEAVITAVREFDGELAQKIIDEMFLFENLVDVDDRSIQRLLQEVDSESLLIALKGAEQPLREKFLRNMSQRAADILRDDLANRGPVRLSQVENEQKAILLIVRRLAETGEMVIGSGEDTYV
Protein: Large ribosomal subunit protein uL16 (60S ribosomal protein L10) (Q54J69)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein eS30
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL1
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein uL4
Sequence:
MGRRPARCYRYCKNKPYIKSRYCRGVPDAKIRIFDLGRKKASTDEFPLCVHLISLEKEQLSSEAIEAGRISCNKYISKTGGKDSFHMRVRVHPWHVLRINKMLSCAGADRLQTGMRGAFGKPMGTVARVNIGQIIFSIRTRDNMLANVVEALRRSSYKFPGRQKIVVSKKWGFTAYNREAYQKLKADGRLMNDGANVKVITNHGTLAQYAKDIAAAN
Protein: Large ribosomal subunit protein eL15A (60S ribosomal protein L15-A) (SP-L12) (O74895)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P05748}. Nucleus {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL19A
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL22
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL8
Sequence:
MGAYKYLEELAKKKQSDVNLFLSRVRAWEYRQMNVIHRASRPSRPDKARRLGYKAKQGYVIYRIRVRRGGRKRPVPKGQTYGKPVHQGVNHLKYQRSARCTAEERVGRYCSNLRVLNSYWVNQDATYKFFEVILVDPSHKAIRRDPRINWIVNPVHKHRESRGLTSIGKKSRGIGKGHRFNNSPQHATWLRHNTLSLRRYR
Protein: AFG2 interacting ribosome maturation factor (V9GY35)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTQDRPLLAVQEALKKCFPVVEEQQGLWQSALRDCQPLLSSLSNLAEQLQAAQNLRFEDVPALRAFPDLKERLRRKQLVAGDIVLDKLGERLAILLKVRDMVSSHVERVFQIYEQHADTVGIDAVLQPSAVSPSVADMLEWL
Protein: D-methionine transport system permease protein MetI (P31547)
Organism: Escherichia coli (strain K12)
Function: Part of the binding-protein-dependent transport system for D-methionine and the toxic methionine analog alpha-methyl-methionine. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000305|PubMed:15919996}.
Interaction partners:
- D-methionine-binding lipoprotein MetQ
- Methionine import ATP-binding protein MetN
- Lipoprotein 28
- ATP-dependent lipid A-core flippase
- Spermidine/putrescine transport system permease protein PotC
- sn-glycerol-3-phosphate transport system permease protein UgpE
- Putrescine transport system permease protein PotI
- Lipopolysaccharide export system permease protein LptG
- sn-glycerol-3-phosphate transport system permease protein UgpA
- Spermidine/putrescine transport system permease protein PotB
Sequence:
MSEPMMWLLVRGVWETLAMTFVSGFFGFVIGLPVGVLLYVTRPGQIIANAKLYRTVSAIVNIFRSIPFIILLVWMIPFTRVIVGTSIGLQAAIVPLTVGAAPFIARMVENALLEIPTGLIEASRAMGATPMQIVRKVLLPEALPGLVNAATITLITLVGYSAMGGAVGAGGLGQIGYQYGYIGYNATVMNTVLVLLVILVYLIQFAGDRIVRAVTRK
Protein: Vacuolar ATPase assembly integral membrane protein vph2 (O74920)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for vacuolar ATPase assembly.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- V-type proton ATPase subunit d
- V-type proton ATPase subunit a
- Regulator of V-ATPase in vacuolar membrane protein 1
- V-type proton ATPase subunit F
- Probable diacylglycerol pyrophosphate phosphatase 1
- Probable V-type proton ATPase 20 kDa proteolipid subunit
- ER lumen protein-retaining receptor
- Splicing factor cactin
- Meiotically up-regulated gene 166 protein
- Uncharacterized mitochondrial carrier C17H9.08
Sequence:
MLYRLSEKQQTDLRCNKLTVDGFELVKMLKELRLHNRNINFLEFLRGVQIVPSDSVFLGEIDENSHTQDNTTTSILKEKELYDGIPLLPSMAGVSMDPEREKKSELRLMKNQISAIINILFTVVGTVTAVWYCTSSLSIEKKIALCAFSAILVLVADTFLYVRYLSAQPVRTSKNHTRQIIYTWTTNDPVLQSNEQLAIELGAIPSLKEKKNQ
Protein: Methyltransferase type 11 domain-containing protein (Q9HTB1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Glycosyltransferase
- Glycosyltransferase
- Acyltransferase 3 domain-containing protein
- DUF1127 domain-containing protein
- D-rhamnosyltransferase WbpZ
- GDP-6-deoxy-D-mannose reductase
- Glycosyltransferase WbpX
- Class I SAM-dependent methyltransferase
- ABC subunit of A-band LPS efflux transporter
- GDP-mannose 4,6-dehydratase
Sequence:
MLNFLKKIVSPPSPATEPVAAPPAPAPVDPYMLGLRDAVLSGWFNQETDELFSGFPISAEDTVLDVGCGDGGNVHFCAMRGARIIIADIDAEKIARTRERLADTPARELECLVSDCDPLPLADATATRVVSTEVIEHVDDPRQFLAELVRVGQPGALYLLSVPHPTSEDLQKDFAADEYFRKPNHIRVLGEEQFAALVREAGLEILSHSRYGFYWSLWMLLFWEAKVDFGNPDHPLLEHWARTWQALLDSPRGPAIKQALDAVVAKSQVIIARKPAQA
Protein: Ranatuerin-2SN1 (E7EKI9)
Organism: Sylvirana spinulosa (Fine-spined frog) (Hylarana spinulosa)
Function: Antimicrobial peptide. Weakly active against P. faecalis X29. Not active against fungi. Shows very weak hemolytic activity against human erythrocytes.
Subcellular location: Secreted {ECO:0000305|PubMed:24055160}.
Interaction partners:
Sequence:
MFTLKKSLLLIFFLGTISLSLCEKERDADDDEVEVIKQEEKRGFLNTAMNTVTNLAGTLMDKAKCKIRGC
Protein: 6,7,8-trihydroxycoumarin synthase (EC 1.14.14.-) (Cytochrome P450 CYP71AZ3) (A0A2Z5D850)
Organism: Pastinaca sativa (Wild parsnip) (Anethum pastinaca)
Function: Involved in the biosynthesis of coumarins and furanocoumarins (FCs), natural products required for defense responses against attacks by predators with potential medical and agroindustrial usages such as anticoagulant, rodenticide and artificial vanilla substitutes. Able to catalyze the hydroxylation of esculetin to produce 6,7,8-trihydroxycoumarin.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:Q6QNI4}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEPVFLFLILAFPIASVYLLFYHKKRVVGLSAPPGPPGLPFIGNFHQLYKASSTHEYLWSLSKQYGSLVTLRMGSVPILVVSSPKMAKEVLQTQDLIYCSRPAMTGMQKLSYNGLDVAFSPYTDQWRHTRKFCTLELFTQKRAQLNFRPVREQEVSRMIARLSETAAASKDVNAYEWFSNLATCIISRVAFGKRYDEDGIGKERFQRMLSEIDAMFIGFFVSDFFPMFGWIDKLSGMRDRLDRTFKDLDMFYQELIDEHLKPNRLESPTEDLIDVMLKNEGSSLTKDSMKAILLNVFNGGTGTTATVLAWAMTALLRNQGVMKKAQEEIRSVIGKKGKVDEDDFPSLPYLRAVVKETMRLYPPAPVLVPRETMESSIIGEDKDHMYMVKPKTVVYISMWAIGRDPKTWKNPMEFVPERFLERPDINYKGQQFEYVPFGAGRRICAGINLGVTTVELALANLLYTFDWEPPAGMRFEDIDDETTNGLALQKKNALYIRPKKYMFP
Protein: Induced myeloid leukemia cell differentiation protein Mcl-1 homolog (Bcl-2-related protein EAT/mcl1) (P97287)
Organism: Mus musculus (Mouse)
Function: Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 2 has antiapoptotic activity.
Subcellular location: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Mitochondrion. Nucleus, nucleoplasm {ECO:0000250}. Note=Cytoplasmic, associated with mitochondria.
Interaction partners:
- Phorbol-12-myristate-13-acetate-induced protein 1
- Bcl-2-like protein 11
- Bcl-2-binding component 3
- Beclin-1
- Bcl-2-like protein 2
- Bcl-2 homologous antagonist/killer
- Ubiquitin-like protein ATG12
- Activator of apoptosis harakiri
- Bcl-2-interacting killer
- E3 ubiquitin-protein ligase HUWE1
Sequence:
MFGLRRNAVIGLNLYCGGASLGAGGGSPAGARLVAEEAKARREGGGEAALLPGARVVARPPPVGAEDPDVTASAERRLHKSPGLLAVPPEEMAASAAAAIVSPEEELDGCEPEAIGKRPAVLPLLERVSEAAKSSGADGSLPSTPPPPEEEEDDLYRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQRNHETAFQGMLRKLDIKNEGDVKSFSRVMVHVFKDGVTNWGRIVTLISFGAFVAKHLKSVNQESFIEPLAETITDVLVRTKRDWLVKQRGWDGFVEFFHVQDLEGGIRNVLLAFAGVAGVGAGLAYLIR
Protein: Uncharacterized protein (Q38BU8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLPLRVLPFIAAGGYASQLRFYSEGKPTEGHRKINLDDDERWIEAEFDEKLRSPEERYALERQRETMKGLIKKIRNEHKQHMHESVRERDAQIDNLKEQIQTMEKKLQQLTNEKQ
Protein: Pre-mRNA-processing factor 40 homolog A (Formin-binding protein 11) (FBP-11) (Formin-binding protein 3) (Q9R1C7)
Organism: Mus musculus (Mouse)
Function: Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.
Subcellular location: Nucleus speckle. Nucleus matrix. Note=Colocalizes with AKAP8L in the nuclear matrix.
Interaction partners:
- RNA-binding protein 25
- THO complex subunit 2
- Pre-mRNA-processing factor 40 homolog B
- RNA-binding protein 39
- Serine/threonine-protein kinase PRP4 homolog
- Splicing factor 1
- Luc7-like protein 3
- Serine/arginine repetitive matrix protein 1
- Transcription elongation regulator 1
- WD40 repeat-containing protein SMU1
Sequence:
MRPGTGAERGGLMVSEMESQPPSRGPGDGERRLSGSNLCSSSWVSADGFLRRRPSMGHPGMHYAPMGMHPMGQRANMPPVPHGMMPQMMPPMGGPPMGQMPGMMSSVMSGMMMSHMSQASMQPALPPGVNSMDVAAGAASGAKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEGYQNTIVAGGLITKSNLHAMIKAEESSKQEECTTASTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAANANTSTTPTNTVGSVPVAPEPEVTSIVATAVDNENTVTVSTEEQAQLANTTAIQDLSGDISSNTGEEPAKQETVSDFTPKKEEEESQPAKKTYTWNTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAISERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKDILKDKGFVVEVNTTFEDFVAIISSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQATPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMHVLEHECQHHHSKNKKHSKKSKKHHRKRSRSRSGSESDDDDSHSKKKRQRSESHSASERSSSAESERSYKKSKKHKKKSKKRRHKSDSPESDTEREKDKKEKDRDSEKDRSRQRSESKHKSPKKKTGKDSGNWDTSGSELSEGELEKRRRTLLEQLDDDQ
Protein: Ribose-phosphate pyrophosphokinase (AFU_orthologue AFUA_3G13380) (Q5B8G1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Amidophosphoribosyltransferase
- Phosphoglucomutase, putative
- Ribose-5-phosphate isomerase
- Ribose 5-phosphate isomerase
- Ribokinase
- Transketolase
- Phosphoglucomutase
- ATP phosphoribosyltransferase
- MutT/nudix family protein
- ribose-phosphate diphosphokinase
Sequence:
MVRNIVVIGGTSHPQLTQTICDILGIPPADVLLSKFSVGETRVEIKESVRGKDVYILQSGGGKVNDHLLELLITISACKTASARRVTAVLPLFPYSRQSDIPYNKSGAPLVKSSLEGKGASNGYTFESTPTTPHPGKLEVGNPINGVSIDNLQKSLAKAQLEESSGSPVKKRLPNGLSRSDTMESLKSDSSKSTLPNGLLDDSQDKINKFEPRPGYKQWVAQAGTLVADLLTCAGADHVITMDLHDPQYQGFFDIPVDNLYGRPLLKNYIMRNIANYKEAVVVSPDAGGAKRATAIADSMGMEFALIHKERRPTRITDRQNATMMLVGDVKDRTAILIDDLADTSNTITRAAKLLKKEGASQVYALVTHGILSGDAIDRINASALDKVVVTNSVSQTEHLRRCPKLEVLEVGHVFAEAIRRVHHGESISALFQYE
Protein: Probable transcription factor GLK1 (Golden2-like protein 1) (OsGLK1) (Q5Z5I4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcriptional activator that promotes chloroplast development. Acts as an activator of nuclear photosynthetic genes involved in chlorophyll biosynthesis, light harvesting, and electron transport.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MLAVSPAMCPDIEDRAAVAGDAGMEVVGMSSDDMDQFDFSVDDIDFGDFFLRLEDGDVLPDLEVDPAEIFTDFEAIATSGGEGVQDQEVPTVELLAPADDVGVLDPCGDVVVGEENAAFAGAGEEKGGCNQDDDAGEANVDDGAAAVEAKSSSPSSTTSSSQEAESRHKSSSKSSHGKKKAKVDWTPELHRRFVQAVEQLGIDKAVPSRILEIMGIDSLTRHNIASHLQKYRSHRKHMIAREAEAASWTQRRQIYAAGGGAVAKRPESNAWTVPTIGFPPPPPPPPSPAPIQHFARPLHVWGHPTMDPSRVPVWPPRHLVPRGPAPPWVPPPPPSDPAFWHHPYMRGPAHVPTQGTPCMAMPMPAARFPAPPVPGVVPCPMYRPLTPPALASKNQQDAQLQLQVQPSSESIDAAIGDVLSKPWLPLPLGLKPPSVDSVMGELQRQGVANVPPACG
Protein: S-ribosylhomocysteine lyase (EC 4.4.1.21) (AI-2 synthesis protein) (Autoinducer-2 production protein LuxS) (A1AEN2)
Organism: Escherichia coli O1:K1 / APEC
Function: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
Interaction partners:
Sequence:
MPLLDSFTVDHTRMEAPAVRVAKTMNTPHGDAITVFDLRFCVPNKEVMPERGIHTLEHLFAGFMRNHLNGNGVEIIDISPMGCRTGFYMSLIGTPDEQRVADAWKAAMEDVLKVQDQNQIPELNVYQCGTYQMHSLQEAQDIARSILERDVRINSNEELALPKEKLQELHI
Protein: Olfactomedin 1a (Q6DGM5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MQPANKLLSLTLLVLMGTELTQVLPANPEESWQVYSSAQDSEGRCVCTVVAPQQTMCSRDARTKQLRQLLEKVQNMTQSIQNLDQRTQKDLQYVQRMEVQLRGLETKFKQVEESHKQNIAKQYKG
Protein: AFG2 interacting ribosome maturation factor (V9GYN4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTQDRPLLAVQEALKKCFPVVEEQQGLWQSALRDCQPLLSSLSNLAEQLQAAQNLRFEDVPALRAFPDLKERLRRKQLVAGDIVLDKLGERLAILLKVRDMVSSHVERVFQIYEQHADTVGIDAVLQPSAVSPSVADMLEWLQDIERHYRK
Protein: At1g72040 (P-loop containing nucleoside triphosphate hydrolases superfamily protein) (Q501D4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase iron-sulfur protein 6
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 beta subcomplex subunit 10-B
Sequence:
MQKILCKSTTSSTPVLSTPVNSLAAGFISLGFKTPVKNLPPCSTTKPLSTCFFSTSAMPTTTASVSSGGVGFSAYLQRTVHKPAPASVRFSTAGYRTCRCSIDGTNRAWVGRTGSWRALFCSDSTGGLTPVNATAGAVVESEEESDGEDEDEEKDEKPVRMNRRNRSSSGSGEFVGNPDLLKIPGVGLRNQRKLVDNGIGDVAELKKLYKDKFWKASQKMVDYLRSSVGIIHRNHAESITTFIKESVDDELKDSGPEPNLNVKKRLTFCVEGNISVGKSTFLQRIANETVELQDLVEIVPEPVDKWQDVGPDHFNILDAFYSEPQRYAYTFQNYVFVTRLMQEKESASGVKPLRLMERSVFSDRMVFVRAVHEAKWMNEMEISIYDSWFDPVVSSLPGLVPDGFIYLRASPDTCHKRMMLRKRAEEGGVSLKYLQDLHEKHESWLLPFESGNHGVLSVSRPSLHMDNSLHPDIKDRVFYLEGNHMHSSIQKVPALVLDCEPNIDFSRDIEAKTQYARQVAEFFEFVKKKQETSTEKSNSQSPVLLPHQNGGLWMGPAGNHVPGLDLPPLDLKSLLTRPSA
Protein: Serine-repeat antigen protein 5 (EC 3.4.22.-) (111 kDa antigen) (Serine protease SERA5) (p126) [Cleaved into: p47 (SER36); p56; p50; p18; p25n; p25c] (P69193)
Organism: Plasmodium falciparum (isolate CDC / Honduras)
Function: Plays an essential role during the asexual blood stage development by controlling the kinetics of merozoite egress from host erythrocytes (By similarity). Specifically, prevents premature rupture of the parasitophorous vacuole and host erythrocyte membranes (By similarity).
Subcellular location: [Serine-repeat antigen protein 5]: Parasitophorous vacuole {ECO:0000269|PubMed:12244052, ECO:0000269|PubMed:12421632}. Note=Secreted in large amount into the parasitophorous vacuole. {ECO:0000250|UniProtKB:Q9TY95}.; SUBCELLULAR LOCATION: [p18]: Secreted {ECO:0000269|PubMed:12421632}. Note=Secreted during merozoite egress from erythrocytes. {ECO:0000269|PubMed:12421632}.; SUBCELLULAR LOCATION: [p25n]: Secreted. Note=Secreted during merozoite egress from erythrocytes. {ECO:0000269|PubMed:12421632}.; SUBCELLULAR LOCATION: [p25c]: Secreted {ECO:0000269|PubMed:12421632}. Note=Secreted during merozoite egress from erythrocytes. {ECO:0000269|PubMed:12421632}.; SUBCELLULAR LOCATION: [p47]: Secreted {ECO:0000269|PubMed:12421632}. Cell membrane {ECO:0000250|UniProtKB:Q9TY95}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9TY95}; Extracellular side {ECO:0000250|UniProtKB:Q9TY95}. Note=Secreted during merozoite egress from erythrocytes (PubMed:12421632). Colocalizes at the merozoite surface with human VTN (By similarity). {ECO:0000250|UniProtKB:Q9TY95, ECO:0000269|PubMed:12421632}.; SUBCELLULAR LOCATION: [p50]: Secreted {ECO:0000269|PubMed:12421632}. Note=Secreted during merozoite egress from erythrocytes. {ECO:0000269|PubMed:12421632}.; SUBCELLULAR LOCATION: [p56]: Secreted {ECO:0000250|UniProtKB:Q9TY95}. Note=Secreted during egress from host erythrocytes. {ECO:0000250|UniProtKB:Q9TY95}.
Interaction partners:
Sequence:
MKSYISLFFILCVIFNKNVIKCTGESQTGNTGGGQAGNTVGDQAGSTGGSPQGSTGASQPGSSEPSNPVSSGHSVSTVSVSQTSTSSEKQDTIQVKSALLKDYMGLKVTGPCNENFIMFLVPHIYIDVDTEDTNIELRTTLKETNNAISFESNSGSLEKKKYVKLPSNGTTGEQGSSTGTVRGDTEPISDSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSESLPANGPDSPTVKPPRNLQNICETGKNFKLVVYIKENTLIIKWKVYGETKDTTENNKVDVRKYLINEKETPFTSILIHAYKEHNGTNLIESKNYALGSDIPEKCDTLASNCFLSGNFNIEKCFQCALLVEKENKNDVCYKYLSEDIVSNFKEIKAETEDDDEDDYTEYKLTESIDNILVKMFKTNENNDKSELIKLEEVDDSLKLELMNYCSLLKDVDTTGTLDNYGMGNEMDIFNNLKRLLIYHSEENINTLKNKFRNAAVCLKNVDDWIVNKRGLVLPELNYDLEYFNEHLYNDKNSPEDKDNKGKGVVHVDTTLEKEDTLSYDNSDNMFCNKEYCNRLKDENNCISNLQVEDQGNCDTSWIFASKYHLETIRCMKGYEPTKISALYVANCYKGEHKDRCDEGSSPMEFLQIIEDYGFLPAESNYPYNYVKVGEQCPKVEDHWMNLWDNGKILHNKNEPNSLDGKGYTAYESERFHDNMDAFVKIIKTEVMNKGSVIAYIKAENVMGYEFSGKKVQNLCGDDTADHAVNIVGYGNYVNSEGEKKSYWIVRNSWGPYWGDEGYFKVDMYGPTHCHFNFIHSVVIFNVDLPMNNKTTKKESKIYDYYLKASPEFYHNLYFKNFNVGKKNLFSEKEDNENNKKLGNNYIIFGQDTAGSGQSGKESNTALESAGTSNEVSERVHVYHILKHIKDGKIRMGMRKYIDTQDVNKKHSCTRSYAFNPENYEKCVNLCNVNWKTCEEKTSPGLCLSKLDTNNECYFCYV
Protein: Zinc finger FYVE domain-containing protein 1 (Q810J8)
Organism: Mus musculus (Mouse)
Function: Plays a role in the formation of lipid droplets (LDs) which are storage organelles at the center of lipid and energy homeostasis. Regulates the morphology, size and distribution of LDs. Mediates the formation of endoplasmic reticulum-lipid droplets (ER-LD) contact sites by forming a complex with RAB18 and ZW10 (By similarity). Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through FYVE-type zinc finger (By similarity).
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:25876663}. Golgi apparatus, Golgi stack {ECO:0000250|UniProtKB:Q9HBF4}. Endoplasmic reticulum {ECO:0000269|PubMed:25876663}. Preautophagosomal structure {ECO:0000250|UniProtKB:Q9HBF4}. Lipid droplet {ECO:0000269|PubMed:31293035}. Mitochondrion {ECO:0000269|PubMed:25876663}. Note=Resides predominantly in the cisternal stacks of the Golgi. Colocalizes with TRIM13 on the perinuclear endoplasmic reticulum. During starvation conditions, localizes to omegasomes which are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures. Localizes to lipid droplets in the presence of oleic acid (By similarity). {ECO:0000250|UniProtKB:Q9HBF4}.
Interaction partners:
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- WD repeat domain phosphoinositide-interacting protein 2
- WD repeat domain phosphoinositide-interacting protein 1
- Autophagy protein 5
- Beclin-1
- Beclin 1-associated autophagy-related key regulator
- Ubiquitin-like protein ATG12
- Activating molecule in BECN1-regulated autophagy protein 1
- Phosphoinositide 3-kinase regulatory subunit 4
- Calcium-binding and coiled-coil domain-containing protein 2
Sequence:
MSAQTSLAEKGLNPGLMCQESYACSGTDEAIFECDECCSLQCLRCEEELHRQERLRNHERIRLKAGHVPYCDPCKGPNGHSPGVRQRAAVRCQTCKINLCLECQKRTHSGGNKRRHPITVYLVSKVQESLEGEEMDEETKRKKMTERVVSFLLVDENEEIQVTNEEDFIRKLDCKPDQHLKVVSIFGNTGDGKSHTLNHTFFYGREVFKTSPAQESCTVGVWAAYDPVHKVAVIDTEGLLGATVNLSQRTRLLLKVLAISDLVIYRTHADRLHNDLFKFLGDASEAYLKHFTKELKATTARCGLDVPLSTLGPAVIIFHETVHTQLLGSDHPSEAPEKLIQDRFRKLGRFPEAFSSIHYKGTRTYNPPTDFSGLRRALEQLLENNTTRSPRHPGVIFKALKALSDRFSGEIPDDQMAHSSFFPDEYFTCSSLCLSCGAGCKNSMNHGKEGVPHEAKSRCRYSHQYDNRVYTCKACYERGKEVSVVPKTSASTDSPWMGLAKYAWSGYVIECPNCGVVYRSRQYWFGNQDPVDTVVRTEIVHVWPGTDAFLKDNNNAAQRLLDGMNFMAQSVSELSLGPTKAVTSWLTDQIAPAYWRPNSQILSCNQCATSFKDNDTKHHCRACGEGFCDSCSSKTRPVPERGWGPAPVRVCDSCYDARNVQLDVTEAQADDEGGTLIARKVGEAVQNTLGAVVTAIDIPLGLVKDAARPAYWVPDHEILHCHNCRKEFSVKLSKHHCRACGQGFCDECSHDCRAVPSRGWDHPVRVCFNCNKKPGDL