wanglab/gogpt-training-data huggingface dataset:
Protein: Anthraniloyl-CoA anthraniloyltransferase (EC 2.3.1.262) (2-heptyl-4(1H)-quinolone synthase PqsD) (PqsD) (P20582)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Required for the biosynthesis of a number of signaling molecules, such as the quinolone signal 2-heptyl-3-hydroxy-4(1H)-quinolone (PQS), 2-heptyl-4-hydroxyquinoline (HHQ) and 2,4-dihydroxyquinoline (DHQ). These molecules are required for normal biofilm formation. Catalyzes the transfer of the anthraniloyl moiety from anthraniloyl-CoA to malonyl-CoA to form 2-aminobenzoylacetyl-CoA. The first step of the reaction is the formation of a covalent anthraniloyl-PqsD intermediate. Next, the short-lived intermediate 3-(2-aminophenyl)-3-oxopropanoyl-CoA is formed. An intramolecular rearrangement of this intermediate can give rise to 2,4-dihydroxyquinoline (DHQ).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Anthranilate--CoA ligase
- 2-aminobenzoylacetyl-CoA thioesterase
- 2-heptyl-4
- 2-heptyl-4
- Anthranilate synthase component 2, pyocyanine specific
- Anthranilate synthase component 1, pyocyanine specific
- 2-heptyl-3-hydroxy-4
- Multiple virulence factor regulator MvfR
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Probable FAD-dependent monooxygenase
Sequence:
MGNPILAGLGFSLPKRQVSNHDLVGRINTSDEFIVERTGVRTRYHVEPEQAVSALMVPAARQAIEAAGLLPEDIDLLLVNTLSPDHHDPSQACLIQPLLGLRHIPVLDIRAQCSGLLYGLQMARGQILAGLARHVLVVCGEVLSKRMDCSDRGRNLSILLGDGAGAVVVSAGESLEDGLLDLRLGADGNYFDLLMTAAPGSASPTFLDENVLREGGGEFLMRGRPMFEHASQTLVRIAGEMLAAHELTLDDIDHVICHQPNLRILDAVQEQLGIPQHKFAVTVDRLGNMASASTPVTLAMFWPDIQPGQRVLVLTYGSGATWGAALYRKPEEVNRPC
Protein: Hexose transporter (Q5AD47)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Carbon catabolite-derepressing protein kinase
- Phosphotransferase
Sequence:
MSLDNSTENRDLEEKEEIPKNEHNEQGEQNENNEHIPTLEDKPLKEYIGISILCFLIAFGGFVFGFDTGTISGFINMTDFLERFGGTKADGTLYFSNVRTGLLIGLFNVGCAIGALFLSKVGDMYGRRVGIMTAMIIYIVGIIVQIASQHAWYQIMIGRIITGLAVGMLSVLCPLFISEVSPKHLRGTLVYCFQLMITLGIFLGYCTSYGTKKYSDSRQWRIPLGLCFAWALCLLGGMVRMPESPRYLVGKDRIDDAKISLAKTNKVSPEDPALYRELQLIQAGVERERLAGKASWGALITGKPRILERVIVGGMLQSLQQLTGDNYFFYYSTTIFKSVGLNDSFETSIILGVINFASTFVGIYAIERLGRRLCLLTGSVAMSICFLIYSLIGTQHLYIDQPGGPTRKPDGNAMIFITALYVFFFASTWAGGVYSIVSELYPLKVRSKAMGFANACNWLWGFLISFFTSFITDAIHFYYGFVFMGCLVFSIFFVYFMIYETKGLTLEEIDELYSTKVVPWKSAGWVPPSDEEMVRAKGYTGDIHADEEQV
Protein: Protein V (P69282)
Organism: Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))
Function: Plays an essential role in the inhibition of host immune response. Prevents the establishment of cellular antiviral state by blocking interferon-alpha/beta (IFN-alpha/beta) production and signaling pathway. Interacts with host IFIH1/MDA5 and DHX58/LGP2 to inhibit the transduction pathway involved in the activation of IFN-beta promoter, thus protecting the virus against cell antiviral state. Interacts also with and inhibits host IRF3.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:22532687}.
Interaction partners:
Sequence:
MDQDAFILKEDSEVEREAPGGRESLSDVIGFLDAVLSSEPTDIGGDRSWLHNTINTPQGPGSAHRAKSEGEGEVSTPSTQDNRSGEESRVSGRTSKPEAEAHAGNLDKQNIHRAFGGRTGTNSVSQDLGDGGDSGILENPPNERGYPRSGIEDENREMAAHPDKRGEDQAEGLPEEVRGSTSLPDEGEGGASNNGRSMEPGSSHSARVTGVLVIPSPELEEAVLRRNKRRPTNSGSKPLTPATVPGTRSPPLNRYNSTGSPPGKPPSTQDEHINSGDTPAVRVKDRKPPIGTRSVSDCPANGRSIHPGLETDSTKKGHRREHIIYERDGYIVDESWCNPVCSRIRIIPRRELCVCKTCPKVCKLCRDDIQCMRPDPFCREIFRS
Protein: Defensin NsD7 (C0HK49)
Organism: Nicotiana suaveolens (Australian tobacco)
Function: Plant defense peptide (Probable). Disrupts membranes containing phosphatidic acid (PA) via a PA-dependent oligomerization process.
Subcellular location: Vacuole {ECO:0000250|UniProtKB:Q8GTM0}.
Interaction partners:
Sequence:
KDCKRESNTFPGICITKPPCRKACIREKFTDGHCSKILRRCLCTKPC
Protein: CDGSH iron-sulfur domain-containing protein 2 homolog (Q9VAM6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- RE40412p
- DNA damage-binding protein 1
- Solute carrier family 22 member 3
- DET1- and DDB1-associated protein 1
- HDC00336
Sequence:
MEPISHLVKSSLPNYLSSLPVPDSIGGWFKLSFKDWLALIPPTVVVAGLGYTAYLAYCPAARASCAAKNSGRCNNHIRKNEPKVVDMIDVEDIAEKAAFCRCWKTKNWPYCDGSHGEHNKQTGDNVGPIVIKK
Protein: Voltage-gated chloride channel TMC4 (Transmembrane channel-like protein 4) (Q7Z404)
Organism: Homo sapiens (Human)
Function: Probable ion channel.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Membrane-bound acylglycerophosphatidylinositol O-acyltransferase MBOAT7
- Transmembrane 6 superfamily member 2
Sequence:
MEENPTLESEAWGSSRGWLAPREARGAPCSSPGPSLSSVLNELPSAATLRYRDPGVLPWGALEEEEEDGGRSRKAFTEVTQTELQDPHPSRELPWPMQARRAHRQRNASRDQVVYGSGTKTDRWARLLRRSKEKTKEGLRSLQPWAWTLKRIGGQFGAGTESYFSLLRFLLLLNVLASVLMACMTLLPTWLGGAPPGPPGPDISSPCGSYNPHSQGLVTFATQLFNLLSGEGYLEWSPLFYGFYPPRPRLAVTYLCWAFAVGLICLLLILHRSVSGLKQTLLAESEALTSYSHRVFSAWDFGLCGDVHVRLRQRIILYELKVELEETVVRRQAAVRTLGQQARVWLVRVLLNLLVVALLGAAFYGVYWATGCTVELQEMPLVQELPLLKLGVNYLPSIFIAGVNFVLPPVFKLIAPLEGYTRSRQIVFILLRTVFLRLASLVVLLFSLWNQITCGGDSEAEDCKTCGYNYKQLPCWETVLGQEMYKLLLFDLLTVLAVALLIQFPRKLLCGLCPGALGRLAGTQEFQVPDEVLGLIYAQTVVWVGSFFCPLLPLLNTVKFLLLFYLKKLTLFSTCSPAARTFRASAANFFFPLVLLLGLAISSVPLLYSIFLIPPSKLCGPFRGQSSIWAQIPESISSLPETTQNFLFFLGTQAFAVPLLLISSILMAYTVALANSYGRLISELKRQRQTEAQNKVFLARRAVALTSTKPAL
Protein: Small ribosomal subunit protein uS15 (40S ribosomal protein S13) (A0A1D8PPE0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:35613268}.
Interaction partners:
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein eS30
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein eL13
- Small ribosomal subunit protein uS8A
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein uL6
Sequence:
MGRMHSSGKGISSSALPYSRNAPSWFKLSSDDVVEQIIKYARKGLTPSQIGVILRDAHGVSQAKVVTGNKILRILKSNGLAPEIPEDLYYLIKKAVSVRKHLEKNRKDKDSKFRLILIESRIHRLARYYRTVAVLPPNWKYESATASALVA
Protein: DNA-binding protein LIV4 (J9VW97)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: DNA-binding protein that activates transcription of RNA binding protein VTS1/RBP1. Required for cell integrity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P21538}.
Interaction partners:
Sequence:
MEGIELGIQDLDRSYQIDTQAASSGDEEDRQEVPERPTKRKRTKEEKERRRSEKRARKEKRRSETAQAAQIQAPQAQVGIEAEVAEAPADYDEVEQVVEDAPVSEDNKKRKEKKHKKDKNKGKKGGSEEQEEEDREAIAASAVATLAQALVSSESDQVAPPVDQIQTPARPTTATSTSATWRTNPNQYGSTKVKKVPLELSPPPAASSLTPAPPATQLIPVTPLTAASAGASSFAVRDKINSLKHPKSSTNAPKAIRSTRKGEDTKESDAQLRLRFKDPKAQEEWLASTSIGKTELLRLEKEGILSYKKGKFTEDEKVSIKKALENYQKIHRMSSFDLVELVMTKTLQATDKETVREFWKDIAASVPGRPILNVQPFVRRMLDPKAHKGRWTSEEDELLLRAYAQHPREWTKISSIVDRTEVDCRDRYLKELVNRDTRTAGRWTKEEEDKLEEVVDRVAKGLRAEQVHGEERETPEEGTELVEPSDVPWDIVSKEMGNTRSMTQCRIKYRDAIWPRKLGLGKDDHVGRTLKVLTRLKNLNYESEKHISWSQVRETLEKYSLKEIRNSYSNLKKSVTSDPHVASLTYPELIKVMYDKAVMQRGRKVRADQRDYPSKETVESGDEAY
Protein: Lymphocyte antigen 6G (Ly-6G) (Ly-6G.1) (P35461)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}.
Interaction partners:
- Integrin alpha-M
- Adhesion G protein-coupled receptor E1
- Receptor-type tyrosine-protein phosphatase C
- Integrin alpha-X
- Low affinity immunoglobulin gamma Fc region receptor III
- T-cell surface glycoprotein CD4
- Sialic acid-binding Ig-like lectin 5
- Killer cell lectin-like receptor subfamily B member 1C
- B-lymphocyte antigen CD19
- T-cell surface glycoprotein CD3 epsilon chain
Sequence:
MDTCHIAKSCVLILLVVLLCAERAQGLECYNCIGVPPETSCNTTTCPFSDGFCVALEIEVIVDSHRSKVKSNLCLPICPTTLDNTEITGNAVNVKTYCCKEDLCNAAVPTGGSSWTMAGVLLFSLVSVLLQTFL
Protein: Peptidyl-prolyl cis-trans isomerase G (PPIase G) (Peptidyl-prolyl isomerase G) (EC 5.2.1.8) (CASP10) (Clk-associating RS-cyclophilin) (CARS-Cyp) (CARS-cyclophilin) (SR-cyclophilin) (SR-cyp) (SRcyp) (Cyclophilin G) (Rotamase G) (Q13427)
Organism: Homo sapiens (Human)
Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing.
Subcellular location: Nucleus matrix {ECO:0000269|PubMed:15358154}. Nucleus speckle {ECO:0000269|PubMed:15358154}. Note=Colocalizes with RNA splicing factors at nuclear speckles. {ECO:0000269|PubMed:15358154}.
Interaction partners:
- Pre-mRNA-processing factor 17
- Cytochrome P450 3A4)
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-splicing factor SLU7
- Cytochrome P450 2B6
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- Cytochrome P450 2D6
- Peptidyl-prolyl cis-trans isomerase-like 1
- Cytochrome P450 2C19
- Cytochrome P450 2C8
Sequence:
MGIKVQRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKSTQKPLHYKSCLFHRVVKDFMVQGGDFSEGNGRGGESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILSCGELIPKSKVKKEEKKRHKSSSSSSSSSSDSDSSSDSQSSSDSSDSESATEEKSKKRKKKHRKNSRKHKKEKKKRKKSKKSASSESEAENLEAQPQSTVRPEEIPPIPENRFLMRKSPPKADEKERKNRERERERECNPPNSQPASYQRRLLVTRSGRKIKGRGPRRYRTPSRSRSRDRFRRSETPPHWRQEMQRAQRMRVSSGERWIKGDKSELNEIKENQRSPVRVKERKITDHRNVSESPNRKNEKEKKVKDHKSNSKERDIRRNSEKDDKYKNKVKKRAKSKSRSKSKEKSKSKERDSKHNRNEEKRMRSRSKGRDHENVKEKEKQSDSKGKDQERSRSKEKSKQLESKSNEHDHSKSKEKDRRAQSRSRECDITKGKHSYNSRTRERSRSRDRSRRVRSRTHDRDRSRSKEYHRYREQEYRRRGRSRSRERRTPPGRSRSKDRRRRRRDSRSSEREESQSRNKDKYRNQESKSSHRKENSESEKRMYSKSRDHNSSNNSREKKADRDQSPFSKIKQSSQDNELKSSMLKNKEDEKIRSSVEKENQKSKGQENDHVHEKNKKFDHESSPGTDEDKSG
Protein: NADH-quinone oxidoreductase subunit I (EC 7.1.1.-) (NADH dehydrogenase I subunit I) (NDH-1 subunit I) (NUO9) (P0AFD6)
Organism: Escherichia coli (strain K12)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular location: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit L
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit N
- NADH-quinone oxidoreductase subunit K
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit C/D
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit E
Sequence:
MTLKELLVGFGTQVRSIWMIGLHAFAKRETRMYPEEPVYLPPRYRGRIVLTRDPDGEERCVACNLCAVACPVGCISLQKAETKDGRWYPEFFRINFSRCIFCGLCEEACPTTAIQLTPDFEMGEYKRQDLVYEKEDLLISGPGKYPEYNFYRMAGMAIDGKDKGEAENEAKPIDVKSLLP
Protein: Endophilin-A (SH3 domain-containing GRB2-like protein) (Q8T390)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required presynaptically at the neuromuscular junction. Implicated in synaptic vesicle endocytosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11927550, ECO:0000269|PubMed:11955450}. Membrane {ECO:0000269|PubMed:11927550, ECO:0000269|PubMed:11955450}; Peripheral membrane protein {ECO:0000269|PubMed:11927550, ECO:0000269|PubMed:11955450}. Note=Associated with internal membranes. Expressed presynaptically at NMJs. {ECO:0000269|PubMed:11927550, ECO:0000269|PubMed:11955450}.
Interaction partners:
- Dynamin
- phosphoinositide 5-phosphatase
- non-specific serine/threonine protein kinase
- Epidermal growth factor receptor
- Synaptotagmin 1
- Insulin-like receptor
- Fibroblast growth factor receptor homolog 2
- Fibroblast growth factor receptor homolog 1
- E3 ubiquitin-protein ligase parkin
- E3 ubiquitin-protein ligase CBL
Sequence:
MAFAGLKKQINKANQYMTEKMGGAEGTKLDMDFMEMERKTDVTVELVEELQLKTKEFLQPNPTARAKMAAVKGISKLSGQAKSNTYPQPEGLLAECMLTYGKKLGEDNSVFAQALVEFGEALKQMADVKYSLDDNIKQNFLEPLHHMQTKDLKEVMHHRKKLQGRRLDFDCKRRRQAKDDEIRGAEDKFGESLQLAQVGMFNLLENDTEHVSQLVTFAEALYDFHSQCADVLRGLQETLQEKRSEAESRPRNEFVPKTLLDLNLDGGGGGLNEDGTPSHISSSASPLPSPMRSPAKSMAVTPQRQQQPCCQALYDFEPENPGELAFKENDIITLLNRVDDNWFEGAVNGRTGYFPQSYVQVQVPLPNGN
Protein: EMILIN-3 (EMILIN-5) (Elastin microfibril interface-located protein 3) (Elastin microfibril interfacer 3) (Elastin microfibril interface-located protein 5) (Elastin microfibril interfacer 5) (Q9NT22)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
Sequence:
MGRRRLLVWLCAVAALLSGAQARGTPLLARPAPPGASRYSLYTTGWRPRLRPGPHKALCAYVVHRNVTCILQEGAESYVKAEYRQCRWGPKCPGTVTYRTVLRPKYKVGYKTVTDLAWRCCPGFTGKRCPEHLTDHGAASPQLEPEPQIPSGQLDPGPRPPSYSRAAPSPHGRKGPGLFGERLERLEGDVQRLAQTYGTLSGLVASHEDPNRMTGGPRAPAVPVGFGVIPEGLVGPGDRARGPLTPPLDEILSKVTEVSNTLQTKVQLLDKVHGLALGHEAHLQRLREAPPSPLTSLALLEEYVDRRLHRLWGSLLDGFEQKLQGVQSECDLRVQEVRRQCEEGQAASRRLHQSLDGRELALRQELSQLGSQLQGLSVSGRGSCCGQLALINARMDGLERALQAVTETQRGPGAPAGDELTRLSAAMLEGGVDGLLEGLETLNGTEGGARGCCLRLDMGGWGVGGFGTMLEERVQSLEERLATLAGELSHDSASPGRSARPLVQTELAVLEQRLVSLETSCTPSTTSAILDSLVAEVKAWQSRSEALLRQVASHAALLQQLNGTVAEVQGQLAEGTGSSLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAANTSLDERERKVEAEVQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVAKVASGLSRCQDTAQKLQHTVGHFDQRVAQVEGACRRLGLLAAGLDSLPTEPLRPREGLWSHVDQLNRTLAQHTQDIARLRDDLLDCQAQLAEQVRPGQAN
Protein: Eukaryotic translation initiation factor 4E type 3 (eIF-4E type 3) (eIF-4E3) (eIF4E type 3) (eIF4E-3) (Q8N5X7)
Organism: Homo sapiens (Human)
Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis. May act as an inhibitor of EIF4E1 activity (By similarity).
Interaction partners:
- Eukaryotic translation initiation factor 4 gamma 1
- Eukaryotic initiation factor 4A-I
- Eukaryotic translation initiation factor 4 gamma 3
- Eukaryotic translation initiation factor 4E-binding protein 3
- Nuclear cap-binding protein subunit 1
- Eukaryotic translation initiation factor 4 gamma 2
- Eukaryotic translation initiation factor 4E type 2
- Nuclear cap-binding protein subunit 2
- mRNA cap guanine-N
- Eukaryotic translation initiation factor 4E
Sequence:
MALPPAAAPPAGAREPPGSRAAAAAAAPEPPLGLQQLSALQPEPGGVPLHSSWTFWLDRSLPGATAAECASNLKKIYTVQTVQIFWSVYNNIPPVTSLPLRCSYHLMRGERRPLWEEESNAKGGVWKMKVPKDSTSTVWKELLLATIGEQFTDCAAADDEVIGVSVSVRDREDVVQVWNVNASLVGEATVLEKIYELLPHITFKAVFYKPHEEHHAFEGGRGKH
Protein: Kinesin-like protein KIF12 (Q9D2Z8)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Kinesin-associated protein 3
- Plasminogen
Sequence:
MEERGSPDGDPARNLEQGPEGSETPIQVVLRVRPMSTVELRRGEQSALHCSGTRTLQVSPDVAFRFGAVLDGARTQEDVFRACGVKRLGELALRGFSCTVFTFGQTGSGKTYTLTGPPPQGEGVPVPPSLAGIMQRTFTWLLDRVQHLDSPVTLRASYLEIYNEQVWDLLSLGSPRPLPVRWTKARGFYVEQLRVVEFGSLEALMELLQMGLSRRRSSSHTLNQASSRSHALLTLHISRPTSQQVPPVDLGEPPVGGKLCFVDLAGSEKVAATGSQGQLMLEANSINRSLLALGHCISLLLDPQRKQNHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRITTRPQGPKSPGVKPPQQVENELLRLQEENRHLRFQLDQMHTTAPGAHGARMAWAQRNLYGMLQEFMLENERLRKEMRQLRSSRDLARAEQRVLAQQVHDLERRLLSACPLPQQGSTPVCPCRMVPAASCHALPPLCYCHHFCPLCRVPLAHWTCPRRECHMPQVLEPEAPGHISQSVWPPPWAPPPSPGSAKPPRERSQSDWTQTRVLAEMLMGEEVVPSAPPLSAGPSNMPYGLRGGSGIPNLTPRLETLTQQINSSLHLSQRQPQPSEDTQSPGQGLSSC
Protein: ATP synthase F(1) complex catalytic subunit beta, mitochondrial (EC 7.1.2.2) (ATP synthase F1 subunit beta) (Q55CS9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00829}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00829}; Matrix side {ECO:0000250|UniProtKB:P00829}.
Interaction partners:
- ATP synthase subunit 9, mitochondrial
- ATP synthase F
- ATP synthase subunit alpha
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase subunit a
- ATP synthase F
- V-type proton ATPase proteolipid subunit
- Cytochrome c1, heme protein, mitochondrial
- 1,4-alpha-glucan-branching enzyme
Sequence:
MFVARRLSKNITQISKTAVKTSVRAVPVRGFKTTSVNQAAAPAPKTSQEKEYFEKNKSLLDKESNEESTEVDYSKLNENQGVVHQVIGAVVDVYFPHGKLPYINDALIVDDFQAENVEKVIEDLNNPSLKGKIDFNNVPISNIKLVLEVAQHLGDGIVRCVALDITDGLGRGALVLNTGSPLMVPVGQATLGRIMNVIGEPIDGCGPIPATEKRPIWRAPPPFADLAPSASILETGIKVIDLLAPYSRGGKIGLFGGAGVGKTVLIQELINNIAKAHGGFSVFTGVGERTREGNDLYHEMVEAGVIKKEGPGSKVALVFGQMNEPPGARARVTLTGLTVAEYFRDAEGQDVLLFIDNIFRFTQAGSEMSALLGRIPSAVGYQPTLATDMGCMQERIATTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRAISELGIYPCVDPLDSTSLMMDPNIIGVEHYKVATDVQKILQEYKSLQDIIAILGMDDLSEDQKATVFRARKIQRFLSQPFEVAHAFTNMEGRFVKLSDSIKAFKGILEGKYDHLPEAAFYMVGGIEDVEIKAAKLLESAGKEEKKTTTTSTTGQVKEETVREKVTRLVDEAYNAKVKKLKEYGASTAHLEELRAQYEKNFESEISQLEVLLKK
Protein: Laminin subunit beta 1 (F1MNT4)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
MGRLQVFAFSFLALCGVGVSAQEPDFSYGCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICNSQDPYHETLNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKTWGVYRYFAYDCESSFPGISTGPIKKVDDIICDSRYSDIEPSTEGEVIFRALDPAFRIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVRGNCFCYGHASECAPVDGVNEEVEGMVHGHCMCRHNTKGLNCEQCMDFYHDLPWRPAEGRNSNACKKCNCNEHSSSCHFDMAVYLATGNVSGGVCDDCQHNTMGRNCEQCKPFYYQHPERDIRDPSLCEQCTCDPAGSQNGGICDSYTDFSAGLIAGQCRCKLYVEGEHCDICKEGFYGLSAEDPFGCKSCACNPLGTIPGGNPCDSETGYCYCKRLVTGQHCDQCLPEHWGLSNDLDGCRPCDCDIGGALNNSCSAESGQCLCRPHMIGRQCSEVESGYYFTTLDHYIYEAEEANFGPGVSIVERQYIQDRIPSWTGAGFVRVPEGAYLEFFIDNIPYSMEYDILIRYEPQLPDHWEKAVIMVQRPGKIPTSSRCGNTVPDDDNQVVSLSPGSRYVVLPRPVCFEKGVNYTVRLELPQYTSSDSGVDSPYTLIDSLVLMPFCKSLDIFTVGGSGDGVVTNSAWETFQRYRCLENSRSVVKTPMTDVCRNIIFSISALLHQTGLACECDPQGSLSSVCDPNGGQCQCRPNVVGRRCDRCAPGTFGFGPSGCKPCECHLQGSVSAFCDPITGQCHCFQGVYTRQCDRCLPGFWGFPSCQPCQCNGHADDCDSVTGECLSCQDYTTGHNCERCLAGYYGDPVIGSGDHCRPCPCPDGPESGRQFASSCYQDPVSLQLACVCNPGYIGSRCDECASGFFGNPSDVGGTCQPCQCHHNIDTADPEACDKETGRCLKCLYHTEGEHCQLCRFGYYGDALRQDCRKCVCNYLGTVQEHCNGSDCQCDKTTGQCLCLPNVIGQNCDRCAPNTWQLASGTGCDPCSCDAAHSFGPSCNEFTGQCHCMPGFGGRTCSECQELFWGDPSVECRACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCHQCFALWDVIIAELTNRTQKFLEKAKALKISGVIGPYRETVDSVEKKVNEIRDILAQSPAAEPLKNIGNLFEEAEKLTKDVTEKMAQVQVDLSDTAMQNNSTARQLDTLQAEAESLDNTVKELAEQLELIKNSDIRGALDSITKYFQMSLEAEERVNASTTSSNSTVEESALTRDRVEDFILERESQFREKQEEQARLLDELAGKLQSLDLSAAAEMTCGTPPGASCSETECGGPNCRTDEGEKKCGGPGCGGLVTVAHSAWQKAMDFDRDVLSALAEVEQLSKMVSEAKLRADEAKQNAQDVLLKTNATKEKVDRSNEDLRNLIKQIRNFLTQDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVESLSQVEVILQQSAADIARAEILLEEAQKASKSATDVKVTADMVREALEEAEKAQIAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLDNELDEKYKKVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISQKVAVYSTCL
Protein: ATP-dependent lipid A-core flippase (EC 7.5.2.6) (Lipid A export ATP-binding/permease protein MsbA) (Lipid flippase) (P60752)
Organism: Escherichia coli (strain K12)
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. Shows ATPase activity. May transport glycerophospholipids. In proteoliposomes, mediates the ATP-dependent flipping of a variety of phospholipid and glycolipid derivatives. May also function as a multidrug transporter.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01703, ECO:0000269|PubMed:12119303, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8809774}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01703, ECO:0000269|PubMed:8809774}.
Interaction partners:
- Tetraacyldisaccharide 4'-kinase
- Lipopolysaccharide export system permease protein LptF
- Maltose/maltodextrin import ATP-binding protein MalK
- Lipopolysaccharide export system permease protein LptG
- Spermidine/putrescine import ATP-binding protein PotA
- Lipopolysaccharide export system ATP-binding protein LptB
- Spermidine/putrescine transport system permease protein PotB
- Putrescine transport ATP-binding protein PotG
- Methionine import ATP-binding protein MetN
- Spermidine/putrescine transport system permease protein PotC
Sequence:
MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQFGQ
Protein: G-protein beta subunit (Q5BH99)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein alpha-3 subunit
- Guanine nucleotide-binding protein subunit alpha
- DUF7582 domain-containing protein
- Developmental regulator flbA
- Uncharacterized protein
- Guanine nucleotide-binding protein alpha-2 subunit
- Serine/threonine-protein kinase ste20
- non-specific serine/threonine protein kinase
- Phosducin-like protein
Sequence:
MADMSGEQMQAKITAARREAEGLKDKIRRRKDDLADTTLRDVAQNQTDALPRIGMKPRRTLKGHLAKIYAMHWSTDRRHLVSASQDGKLIIWDAYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNICSIYNLSSREGPTRVARELSGHSGYLSCCRFINDRRIITSSGDMTCMLWDIESGSKVTEFADHLGDVMSISINPTNQNIFVSGACDAFAKLWDIRTGKAVQTFAGHESDINAIQFFPDGNAFGTGSDDTTCRLFDIRADRSLNTYQSDQILCGITSVGFSVSGRLLFAGYDDFECKVWDVLRGDKVGSLSGHENRVSCLGVSNDGISLCTGSWDSLLKVWAW