wanglab/gogpt-training-data huggingface dataset:
Protein: Pro-secreted protein ORF2 (Protein ORF2) (pORF2) [Cleaved into: Secreted protein ORF2 (ORF2s)] (P33426)
Organism: Hepatitis E virus genotype 1 (isolate Human/Pakistan/Sar-55) (HEV-1)
Function: Plays a role in the inhibition of host antibody-mediated neutralization without blocking viral cell entry.
Subcellular location: [Isoform Secreted protein ORF2]: Secreted {ECO:0000250|UniProtKB:Q81871}. Note=Cotranslationally translocated into the ER (By similarity). Translation from the first AUG produces a full-length protein with a signal peptide that can direct the protein into the secretory pathway (By similarity). {ECO:0000250|UniProtKB:Q68985, ECO:0000250|UniProtKB:Q9YLQ9}.; SUBCELLULAR LOCATION: [Isoform Capsid protein]: Virion {ECO:0000250|UniProtKB:Q81871}. Host cytoplasm {ECO:0000250|UniProtKB:Q81871}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:Q81871}. Host Golgi apparatus {ECO:0000250|UniProtKB:Q81871}. Host cell surface {ECO:0000250|UniProtKB:Q68985}. Host nucleus {ECO:0000250|UniProtKB:Q81871}. Note=Translation from the internal AUG codon disrupts the signal sequence, producing a cytoplasmic protein that is responsible for virion assembly (By similarity). Shuttles between cytoplasm and nucleus (PubMed:36007070). This isoform is found in quasi-enveloped virions (By similarity). {ECO:0000250|UniProtKB:Q81871, ECO:0000250|UniProtKB:Q9YLQ9, ECO:0000269|PubMed:36007070}.
Interaction partners:
Sequence:
MRPRPILLLLLMFLPMLPAPPPGQPSGRRRGRRSGGSGGGFWGDRVDSQPFAIPYIHPTNPFAPDVTAAAGAGPRVRQPARPLGSAWRDQAQRPAAASRRRPTTAGAAPLTAVAPAHDTPPVPDVDSRGAILRRQYNLSTSPLTSSVATGTNLVLYAAPLSPLLPLQDGTNTHIMATEASNYAQYRVARATIRYRPLVPNAVGGYAISISFWPQTTTTPTSVDMNSITSTDVRILVQPGIASELVIPSERLHYRNQGWRSVETSGVAEEEATSGLVMLCIHGSPVNSYTNTPYTGALGLLDFALELEFRNLTPGNTNTRVSRYSSTARHRLRRGADGTAELTTTAATRFMKDLYFTSTNGVGEIGRGIALTLFNLADTLLGGLPTELISSAGGQLFYSRPVVSANGEPTVKLYTSVENAQQDKGIAIPHDIDLGESRVVIQDYDNQHEQDRPTPSPAPSRPFSVLRANDVLWLSLTAAEYDQSTYGSSTGPVYVSDSVTLVNVATGAQAVARSLDWTKVTLDGRPLSTIQQYSKTFFVLPLRGKLSFWEAGTTKAGYPYNYNTTASDQLLVENAAGHRVAISTYTTSLGAGPVSISAVAVLAPHSVLALLEDTMDYPARAHTFDDFCPECRPLGLQGCAFQSTVAELQRLKMKVGKTREL
Protein: Signal peptidase complex subunit 1 (Microsomal signal peptidase 12 kDa subunit) (SPase 12 kDa subunit) (Q9Y6A9)
Organism: Homo sapiens (Human)
Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Dispensable for SPC enzymatic activity (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P83362}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P83362}.
Interaction partners:
- Signal peptidase complex subunit 2
- Signal peptidase complex catalytic subunit SEC11C
- Signal peptidase complex subunit 3
- Signal peptidase complex catalytic subunit SEC11
- Protein transport protein Sec61 subunit gamma
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Protein transport protein Sec61 subunit beta
- Translocon-associated protein subunit delta
- Translocon-associated protein subunit beta
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
Sequence:
MARGGDTGCTGPSETSASGAAAIALPGLEGPATDAQCQTLPLTVLKSRSPSPRSLPPALSCPPPQPAMLEHLSSLPTQMDYKGQKLAEQMFQGIILFSAIVGFIYGYVAEQFGWTVYIVMAGFAFSCLLTLPPWPIYRRHPLKWLPVQESSTDDKKPGERKIKRHAKNN
Protein: Small ribosomal subunit protein uS9m (30S ribosomal protein S9, mitochondrial) (Q8L6Z4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mitochondrial ribosomal protein required for central cell maturation. May work together with PIA2 in controlling female gametophyte development, possibly by regulating the expression of some mitochondrial proteins.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:29312411}.
Interaction partners:
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein bL21m
- 50S ribosomal protein L33
- At1g64880
- Small ribosomal subunit protein uS2m
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- Small ribosomal subunit protein bS16m/bS16c
- Small ribosomal subunit protein uS14m
- Large ribosomal subunit protein bL9c
Sequence:
MLSRLFLRHSNLRFVTLVSSKSNSQIFSSFIRPLSTNSSGGGGNGDGNGRNRNDVPWSFTGVNDDKSGPFSSDDSFGSSGVAGSGLPGGEGKWPEEPKRWNIKEEEEKVVFDTGGEVGQGIETSRERRGNEWEETKRWDMKEGEEKVVFGGGGDEVDGFGIRGEVKSNEWDVSKPWNLKEEEEGVVFDTGGEVPFSFENSLEMAEEERVKKELIEKEEKELLEVIKGPDRAFGDLIAKSGITDEMLDSLIALKDFQGVEGLPPLTEIENLRREKSSKKSSRAEIELQMQEDIAKARVRQVDETGRAYGTGRRKCSIARVWIQPGEGKFQVNEKEFDVYFPMLDHRAALLRPLAETKTLGRWDIKCTVKGGGTTGQVGAIQLGISRALQNWEPDMRTSLRAAGFLTRDSRVVERKKPGKAKARKSFQWVKR
Protein: Tryptophan--tRNA ligase, mitochondrial (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (TrpRS) (O42875)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P04803, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Tryptophan--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, mitochondrial
- Serine--tRNA ligase, cytoplasmic
- Putative leucine--tRNA ligase, mitochondrial
- Putative leucine--tRNA ligase, cytoplasmic
- Probable arginine--tRNA ligase, cytoplasmic
- Small ribosomal subunit protein uS10m
- Probable cysteine--tRNA ligase
- Probable methionine--tRNA ligase, cytoplasmic
- Putative glycine--tRNA ligase
Sequence:
MAKLPKITSLLPHSRVVSGIQPTGIPHIGNYLGSLKQWVQLQEEAARTPFSKCFFFVADLHALTVPQDPLKFRQARLDMLAALLAIGINPQKSTLFFQSDVAQHSELAWLLACSTSMGQLNRMTQWKSKLHLHDHDDLSFLDASATSSTRFNLGLFSYPVLQAADILLYGATHIPVGKDQSQHVELTRSIARSFNSSYKEKILTVPDIILNSSSSIMALCQPEKKMSKSDINSKNYILLSDSTGEIRKKISRAQTDNIKGITYGDSNRPGINNLINIFAAISDSTPSDIAQANASCSNAEFKEKVSSAIIRCLQPISTSFNEWRQNRELLRDIAKKGAEEAVAEASSCMHKLKTLTGLSVY
Protein: Putative golgin subfamily A member 8D (Q0D2H9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGALQAQVEYNQRISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKELNNENKSVLQLEQQVKELQEKLGKERLEAASQQKQQLTAQLSLMALPGEGHGGEHLDSEGEEAPRPMPSVPEDLESREAMSGFMDHLEEKADLSELVEKEELGFFQYYRERCHQKVYHPITKPGGSAKDAAPGGGHHQAGPGQGGDEGEAAGAAGDGVAAGGDYKGHSKFLVTAQNPAHEPSPGAPAPQELGAAHKHGDLCEVSLTDSVEPVQGEAREGSPHDNPTAQPIVQDHQEHPGLGSNCCVPFFCWAWLPRRRR
Protein: Photosystem II CP47 reaction center protein (PSII 47 kDa protein) (Protein CP-47) (Q6ENE8)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01495}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01495}.
Interaction partners:
- Photosystem II CP43 reaction center protein
- Cytochrome c oxidase subunit 3
- Photosystem II protein D1
- Cytochrome b559 subunit alpha
- Photosystem II D2 protein
- photosystem II
- Photosystem II protein D1
- Photosystem I iron-sulfur center
- Cytochrome b559 subunit beta
- NAD
Sequence:
MGLPWYRVHTVVLNDPGRLLSVHIMHTALVSGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGITNSWGGWSISGGTVTNPGIWSYEGVAGAHIVFSGLCFLAAIWHWVYWDLEIFCDERTGKPSLDLPKIFGIHLFLAGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQAVNPAWGAEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVSDGLAENLSLSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGSMDNGDGIAVGWLGHPIFRDKEGRELFVRRMPTFFETFPVVLVDEEGIVRADVPFRRAESKYSVEQVGVTVEFYGGELNGVSYSDPATVKKYARRSQLGEIFELDRATLKSDGVFRSSPRGWFTFGHATFALLFFFGHIWHGARTLFRDVFAGIDPDLDAQVEFGTFQKVGDPTTRRQPV
Protein: Gamete-specific homeodomain protein (Q9XEK5)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MDNRQPQFADAQAMDGAAVWRSSGTGYEWIAQALQDADDSMAGFAEASAMGLGSFTEGLGPGRGGADPGGDPALAPLQSAQLMGHLSITEAERAIAEAAAMMAAGTVYPEATPSGQPPTHPHQQPQPRMHAGTYPAQHQHQHQHQHQQHHQQHQHVVPAAVGHSHHQAATAAAAHAPHYHQPQHPHHQQYQQQQHVHHQQHPLMPDPYTSFAAGPIDLAAHAHMQHRQQHQQEQQQMLYAYHQHNQYHHQQQHLQPQHQQYQQYPPQLPHQQVQHQHQHTALGSPPVQHHQHHQHHQHHHQHHQHHHQHHHQQHVPAGAHHAAARPLPPNHQSHQHHQQQMPPVVPSQPQHHQHGMHAAAAAASSSAVSAAASARGGYTAIAPAAPPATAHSALAPPVTSTYYQTSGGAMPYPGWSVAGLEVPTPGTRSQRGSSTHLLTAPGLHPTSGGSGGGEGREVVMHPGFGAAALTGATGAAAAAAAAPTPQASPLGGRGTGASAEPATSAHSHGGGGGFGNVVSGTPMETTVSLPPQVSSHAGGRGASGSTDSSAEASTDHKRARTNNPGAGGARAAQAAALPSLDAVTSQQAAAAAGMAPAAGTLGAVPPAYPAVAVAPAAEVNGAMPYVDALTEQLRAVRLLQPTPPSSASSAPVRASAAAMADVTENVAVKAKGKKKGAAAAAAAQPPPPPLLPPAPRTEMDRRAALSGAAGAFMAACDEAVRELLLAMNFSDHDAEAIITGAAPPQLEHAASGVVSLVLRLKSSVLSHYIKHLNNAAARSQAAAASTAAVDGNAEDAADKHGAKATSAAKAPPAAGGGAGDAADQQLSTGEACLVQLQLYGGVGDALLQLLRSKLRGSACQLWALAHIVHPHPSRSEKESLAAYTGKSTKQVTDWFTNWRARHWRPAIMALQKGAAGGAAGGSLGVAADGAASGGDDGEEEECAEARAKKGKGAKDCSRAKEPASGARKAAAAAPATTAAAAGAEVGSGGRSGSRRPRSRRACRETESEEDQEDDDDEEEDEEESSPSEGGSTDDE
Protein: Serine protease HTRA1 (EC 3.4.21.-) (High-temperature requirement A serine peptidase 1) (Serine protease 11) (Q9QZK5)
Organism: Rattus norvegicus (Rat)
Function: Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q92743}. Secreted {ECO:0000250|UniProtKB:Q92743}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92743}. Note=Predominantly secreted. Also found associated with the plasma membrane. {ECO:0000250|UniProtKB:Q92743}.
Interaction partners:
- Aggrecan core protein
Sequence:
MQFLRTALLSLLLLLLAAPSLALPSGISRSAPAATVCPEHCDPTRCAPPPTDCEGGRVRDACGCCEVCGALEGAVCGLQEGPCGEGLQCVVPFGVPASATVRRRAQAGLCVCASSEPVCGSDAKTYTNLCQLRAASRRSEKLRQPPVIVLQRGACGQGQEDPNSLRHKYNFIADVVEKIAPAVVHIELYRKLPFSKREVPVASGSGFIVSEDGLIVTNAHVVTNKNRVKVELKNGATYEAKIKDVDEKADIALIKIDHQGKLPVLLLGRSSELRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTAGISFAIPSDKIKKFLTESHDRQAKGKTVTKKKYIGIRMMSLTSSKAKELKDRHRDFPDVISGAYIIEVIPDTPAEAGGLKENDVIISINGQSVVTANDVSDVIKKENTLNMVVRRGNEDIVITVVPEEIDP
Protein: DNA damage-repair/toleration protein DRT102 (Q05212)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Phosphoacetylglucosamine mutase
- Pentatricopeptide repeat-containing protein At3g22690
- DNA damage-repair/toleration protein DRT100
- Triosephosphate isomerase, chloroplastic
- Triosephosphate isomerase, cytosolic
- Receptor-like protein 14
- Protein DGS1, mitochondrial
- Double-strand break repair protein MRE11
- Dihydroxyacetone kinase
- At3g17770
Sequence:
MAGAVSAVDQPLKIITGADDFGASLKDAMVTHLRSLGIDVEDTGVSSYYSAGSEVGRRVSASSSSEVRGLVCCGTGVGVAMFANKFPGVYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPFKSPCPASGSEPWSSVISSFLDNSLSEMSQIGKSTAGDSTTKKIDETTASCVICCLAKNREFTPVDIMPGGSMKIVRETPTSAIVRFKAGSVEPAHHHTFGHDLVVIKGKKSVWNLSKKERADLVDGDYLFTPAGDVHRVKYHEDTEFFITWDGHWDIFLDEDLETAKKAIEEEA
Protein: E3 ubiquitin-protein ligase HECW2 (EC 2.3.2.26) (HECT, C2 and WW domain-containing protein 2) (HECT-type E3 ubiquitin transferase HECW2) (NEDD4-like E3 ubiquitin-protein ligase 2) (Q9P2P5)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination of TP73. Acts to stabilize TP73 and enhance activation of transcription by TP73. Involved in the regulation of mitotic metaphase/anaphase transition.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:24163370}.
Interaction partners:
- Angiomotin-like protein 1
- Arrestin domain-containing protein 1
Sequence:
MASSAREHLLFVRRRNPQMRYTLSPENLQSLAAQSSMPENMTLQRANSDTDLVTSESRSSLTASMYEYTLGQAQNLIIFWDIKEEVDPSDWIGLYHIDENSPANFWDSKNRGVTGTQKGQIVWRIEPGPYFMEPEIKICFKYYHGISGALRATTPCITVKNPAVMMGAEGMEGGASGNLHSRKLVSFTLSDLRAVGLKKGMFFNPDPYLKMSIQPGKKSSFPTCAHHGQERRSTIISNTTNPIWHREKYSFFALLTDVLEIEIKDKFAKSRPIIKRFLGKLTIPVQRLLERQAIGDQMLSYNLGRRLPADHVSGYLQFKVEVTSSVHEDASPEAVGTILGVNSVNGDLGSPSDDEDMPGSHHDSQVCSNGPVSEDSAADGTPKHSFRTSSTLEIDTEELTSTSSRTSPPRGRQDSLNDYLDAIEHNGHSRPGTATCSERSMGASPKLRSSFPTDTRLNAMLHIDSDEEDHEFQQDLGYPSSLEEEGGLIMFSRASRADDGSLTSQTKLEDNPVENEEASTHEAASFEDKPENLPELAESSLPAGPAPEEGEGGPEPQPSADQGSAELCGSQEVDQPTSGADTGTSDASGGSRRAVSETESLDQGSEPSQVSSETEPSDPARTESVSEASTRPEGESDLECADSSCNESVTTQLSSVDTRCSSLESARFPETPAFSSQEEEDGACAAEPTSSGPAEGSQESVCTAGSLPVVQVPSGEDEGPGAESATVPDQEELGEVWQRRGSLEGAAAAAESPPQEEGSAGEAQGTCEGATAQEEGATGGSQANGHQPLRSLPSVRQDVSRYQRVDEALPPNWEARIDSHGRIFYVDHVNRTTTWQRPTAPPAPQVLQRSNSIQQMEQLNRRYQSIRRTMTNERPEENTNAIDGAGEEADFHQASADFRRENILPHSTSRSRITLLLQSPPVKFLISPEFFTVLHSNPSAYRMFTNNTCLKHMITKVRRDTHHFERYQHNRDLVGFLNMFANKQLELPRGWEMKHDHQGKAFFVDHNSRTTTFIDPRLPLQSSRPTSALVHRQHLTRQRSHSAGEVGEDSRHAGPPVLPRPSSTFNTVSRPQYQDMVPVAYNDKIVAFLRQPNIFEILQERQPDLTRNHSLREKIQFIRTEGTPGLVRLSSDADLVMLLSLFEEEIMSYVPPHALLHPSYCQSPRGSPVSSPQNSPGTQRANARAPAPYKRDFEAKLRNFYRKLETKGYGQGPGKLKLIIRRDHLLEDAFNQIMGYSRKDLQRNKLYVTFVGEEGLDYSGPSREFFFLVSRELFNPYYGLFEYSANDTYTVQISPMSAFVDNHHEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRILCDLSDLEYLDEEFHQSLQWMKDNDIHDILDLTFTVNEEVFGQITERELKPGGANIPVTEKNKKEYIERMVKWRIERGVVQQTESLVRGFYEVVDARLVSVFDARELELVIAGTAEIDLSDWRNNTEYRGGYHDNHIVIRWFWAAVERFNNEQRLRLLQFVTGTSSIPYEGFASLRGSNGPRRFCVEKWGKITALPRAHTCFNRLDLPPYPSFSMLYEKLLTAVEETSTFGLE
Protein: Antimicrobial peptides [Cleaved into: Antimicrobial peptide 1 (EcAMP1); Antimicrobial peptide 3 (EcAMP3); Antimicrobial peptide 2 (EcAMP2); Antimicrobial peptide 2.1 (EcAMP2.1)] (B3EWR6)
Organism: Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli)
Function: Has antifungal activity. Inhibits spore germination of F.graminearum (EC(50)=4.5 uM), F.oxysporum (EC(50)=8.5 uM), F.solani (EC(50)=4.0 uM), F.verticillioides (EC(50)=8.1 uM), P.infestans (EC(50)=16.3 uM), P.betae (EC(50)=6.0 uM), P.debaryanum (EC(50)=12.0 uM), P.ultimatum (EC(50)=14.4 uM), B.sorokiniana (EC(50)=18.2 uM), A.alternata (EC(50)=16.0 uM) and A.solani (EC(50)=14.0 uM). Does not destroy spores but rather inhibits hyphal growth during germination. Does not affect spore germination in A.niger, C.graminicola, D.maydis and T.album. Does not inhibit trypsin.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P28794}.
Interaction partners:
Sequence:
MGKGSSGGGAWWAFLLLAGVLLAVAATAAGAEEDVATEVAAAADRDPKEDLRWCRKGCQWQYGQDTRQRKECERDCRQRHREQEQDADEEDGSGRGSCRSQCMRRHEDEPWRVQECVSQCRRRRGGGDDDVAVDACEGADRCRERCERRHRGDWQGKQRCLMECRRREQEEDVDDRCPCPCRRQCERHGDPATRQRCVEACQRRREEERRHGGGDADEEGSRGGRCERKCRRHSDWQTRQRCLQQCEQRERQEEGGRDDAGDGKDTYCADRCQSMCRQRHRGDREMQRRCARKCEREEGCPRRRDATADADEAEEDDGNDRCSQQCQHHRDPDRKQQCMRECRRHQGRSDDDDTRAGEDDS
Protein: Fibulin-2 (FIBL-2) (P98095)
Organism: Homo sapiens (Human)
Function: Its binding to fibronectin and some other ligands is calcium dependent. May act as an adapter that mediates the interaction between FBN1 and ELN.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Fibronectin
- Elastin
- Fibrillin-1
- Fibulin-1
- Aggrecan core protein
- Nidogen-1
- Vitronectin
- Microfibrillar-associated protein 2
- Nidogen-2
Sequence:
MVLLWEPAGAWLALGLALALGPSVAAAAPRQDCTGVECPPLENCIEEALEPGACCATCVQQGCACEGYQYYDCLQGGFVRGRVPAGQSYFVDFGSTECSCPPGGGKISCQFMLCPELPPNCIEAVVVADSCPQCGQVGCVHAGHKYAAGHTVHLPPCRACHCPDAGGELICYQLPGCHGNFSDAEEGDPERHYEDPYSYDQEVAEVEAATALGGEVQAGAVQAGAGGPPAALGGGSQPLSTIQAPPWPAVLPRPTAAAALGPPAPVQAKARRVTEDSEEEEEEEEEREEMAVTEQLAAGGHRGLDGLPTTAPAGPSLPIQEERAEAGARAEAGARPEENLILDAQATSRSTGPEGVTHAPSLGKAALVPTQAVPGSPRDPVKPSPHNILSTSLPDAAWIPPTREVPRKPQVLPHSHVEEDTDPNSVHSIPRSSPEGSTKDLIETCCAAGQQWAIDNDECLEIPESGTEDNVCRTAQRHCCVSYLQEKSCMAGVLGAKEGETCGAEDNDSCGISLYKQCCDCCGLGLRVRAEGQSCESNPNLGYPCNHVMLSCCEGEEPLIVPEVRRPPEPAAAPRRVSEAEMAGREALSLGTEAELPNSLPGDDQDECLLLPGELCQHLCINTVGSYHCACFPGFSLQDDGRTCRPEGHPPQPEAPQEPALKSEFSQVASNTIPLPLPQPNTCKDNGPCKQVCSTVGGSAICSCFPGYAIMADGVSCEDINECVTDLHTCSRGEHCVNTLGSFHCYKALTCEPGYALKDGECEDVDECAMGTHTCQPGFLCQNTKGSFYCQARQRCMDGFLQDPEGNCVDINECTSLSEPCRPGFSCINTVGSYTCQRNPLICARGYHASDDGTKCVDVNECETGVHRCGEGQVCHNLPGSYRCDCKAGFQRDAFGRGCIDVNECWASPGRLCQHTCENTLGSYRCSCASGFLLAADGKRCEDVNECEAQRCSQECANIYGSYQCYCRQGYQLAEDGHTCTDIDECAQGAGILCTFRCLNVPGSYQCACPEQGYTMTANGRSCKDVDECALGTHNCSEAETCHNIQGSFRCLRFECPPNYVQVSKTKCERTTCHDFLECQNSPARITHYQLNFQTGLLVPAHIFRIGPAPAFTGDTIALNIIKGNEEGYFGTRRLNAYTGVVYLQRAVLEPRDFALDVEMKLWRQGSVTTFLAKMHIFFTTFAL
Protein: Maltose/maltodextrin-binding periplasmic protein (MMBP) (Maltodextrin-binding protein) (Maltose-binding protein) (MBP) (P0AEX9)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins such as maltotriose.
Subcellular location: Periplasm {ECO:0000269|PubMed:4215651}.
Interaction partners:
- Maltoporin
- Maltose/maltodextrin import ATP-binding protein MalK
- Maltose/maltodextrin transport system permease protein MalF
- Maltose/maltodextrin transport system permease protein MalG
- Protein-export protein SecB
- Maltose operon periplasmic protein
- Outer membrane protein assembly factor BamA
- Glutathione S-transferase GstA
- Inner membrane ABC transporter permease protein YcjO
- Methyl-accepting chemotaxis protein II
Sequence:
MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRITK
Protein: Mannosyl-D-glycerate transport/metabolism system repressor MngR (Fatty acyl-responsive regulator) (Protein P30) (P13669)
Organism: Escherichia coli (strain K12)
Function: Represses mngA and mngB. Regulates its own expression.
Interaction partners:
- Trifunctional NAD biosynthesis/regulator protein NadR
- PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component
- Mannosylglycerate hydrolase
Sequence:
MGHKPLYRQIADRIREQIARGELKPGDALPTESALQTEFGVSRVTVRQALRQLVEQQILESIQGSGTYVKEERVNYDIFQLTSFDEKLSDRHVDTHSEVLIFEVIPADDFLQQQLQITPQDRVWHVKRVRYRKQKPMALEETWMPLALFPDLTWQVMENSKYHFIEEVKKMVIDRSEQEIIPLMPTEEMSRLLNISQTKPILEKVSRGYLVDGRVFEYSRNAFNTDDYKFTLIAQRKSSR
Protein: Linoleate 9S-lipoxygenase 1 (EC 1.13.11.58) (Lipoxygenase 1) (AtLOX1) (Q06327)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 9S-lipoxygenase that can use linoleic acid or linolenic acid as substrates. Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Function as regulators of root development by controlling the emergence of lateral roots. 9S-lypoxygenase-derived oxylipins may play an antagonistic role to ethylene signaling in the control of responses involving oxidative stress, lipid peroxidation and plant defense. LOX1-derived oxylipins may be involved in stress signaling from roots to shoots in response to cadmium exposure. 9S-lypoxygenase-derived oxylipins are engaged during infection to control the balance between salicylic acid (SA) and jasmonate (JA) signaling to facilitate infection by the fungal pathogen Fusarium graminearum. 9S-lypoxygenase-derived oxylipins activate brassinosteroid signaling to promote cell wall-based defense and limit pathogen infection. The LOX1-derived compound (9S)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoate protects plant tissues against infection by the bacterial pathogen Pseudomonas syringae pv tomato DC3000. The LOX1-derived oxylipins are required to trigger stomatal closure in response to both infection by the bacterial pathogen Pseudomonas syringae pv tomato DC3000, and the pathogen-associated molecular pattern (PAMP) flagellin peptide flg22. Contributes to the oxidation of free fatty acids during seed aging.
Subcellular location: Cytoplasm.
Interaction partners:
- Lipoxygenase 2, chloroplastic
- Lipoxygenase 6, chloroplastic
- Lipoxygenase 3, chloroplastic
- Lipoxygenase 4, chloroplastic
- Phospholipase A2-alpha
- Linoleate 9S-lipoxygenase 5
- Triacylglycerol lipase SDP1
- Triacylglycerol lipase SDP1L
- Allene oxide synthase, chloroplastic
- Receptor-like protein 7
Sequence:
MFGELRDLLTGGGNETTTKKVKGTVVLMKKNVLDFNDFNASFLDRLHEFLGNKITLRLVSSDVTDSENGSKGKLGKAAHLEDWITTITSLTAGESAFKVTFDYETDFGYPGAFLIRNSHFSEFLLKSLTLEDVPGHGRVHYICNSWIYPAKHYTTDRVFFSNKTYLPHETPATLLKYREEELVSLRGTGEGELKEWDRVYDYAYYNDLGVPPKNPRPVLGGTQEYPYPRRGRTGRKPTKEDPQTESRLPITSSLDIYVPRDERFGHLKMSDFLAYALKAIAQFIQPALEAVFDDTPKEFDSFEDVLKIYEEGIDLPNQALIDSIVKNIPLEMLKEIFRTDGQKFLKFPVPQVIKEDKTAWRTDEEFAREMLAGLNPVVIQLLKEFPPKSKLDSESYGNQNSTITKSHIEHNLDGLTVEEALEKERLFILDHHDTLMPYLGRVNTTTTKTYASRTLLFLKDDGTLKPLVIELSLPHPNGDKFGAVSEVYTPGEGVYDSLWQLAKAFVGVNDSGNHQLISHWMQTHASIEPFVIATNRQLSVLHPVFKLLEPHFRDTMNINALARQILINGGGIFEITVFPSKYAMEMSSFIYKNHWTFPDQALPAELKKRGMAVEDPEAPHGLRLRIKDYPYAVDGLEVWYAIESWVRDYIFLFYKIEEDIQTDTELQAWWKEVREEGHGDKKSEPWWPKMQTREELVESCTIIIWVASALHAAVNFGQYPVAGYLPNRPTISRQYMPKENTPEFEELEKNPDKVFLKTITAQLQTLLGISLIEILSTHSSDEVYLGQRDSKEWAAEKEALEAFEKFGEKVKEIEKNIDERNDDETLKNRTGLVKMPYTLLFPSSEGGVTGRGIPNSVSI
Protein: m7GpppX diphosphatase (EC 3.6.1.59) (DCS-1) (Hint-related 7meGMP-directed hydrolase 1) (Protein Dcs1p) (Scavenger mRNA-decapping enzyme DcpS) (Q06151)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP) or tri-methyl guanosine nucleoside monophosphate (m3(2,2,7)GMP), respectively. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to (m(7)GMP) and m3(2,2,7)GMP, respectively. May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCS1 to m7GMP. Binds to m7GpppG and strongly to m7GDP. May also regulate the 5'->3' exoribonucleolytic mRNA decay pathway in a cap-independent manner. Negatively regulates trehalase activity.
Subcellular location: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body. Note=Predominantly cytoplasmic.
Interaction partners:
- Inactive diphosphatase DCS2
- Cytosolic neutral trehalase
- 5'-3' exoribonuclease 1
- m7GpppN-mRNA hydrolase
- Meiotic sister chromatid recombination protein 1
Sequence:
MSQLPTDFASLIKRFQFVSVLDSNPQTKVMSLLGTIDNKDAIITAEKTHFLFDETVRRPSQDGRSTPVLYNCENEYSCINGIQELKEITSNDIYYWGLSVIKQDMESNPTAKLNLIWPATPIHIKKYEQQNFHLVRETPEMYKRIVQPYIEEMCNNGRLKWVNNILYEGAESERVVYKDFSEENKDDGFLILPDMKWDGMNLDSLYLVAIVYRTDIKTIRDLRYSDRQWLINLNNKIRSIVPGCYNYAVHPDELRILVHYQPSYYHFHIHIVNIKHPGLGNSIAAGKAILLEDIIEMLNYLGPEGYMNKTITYAIGENHDLWKRGLEEELTKQLERDGIPKIPKIVNGFK