wanglab/gogpt-training-data huggingface dataset:
Protein: Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (Succinyl-CoA synthetase beta chain) (SCS-beta) (Q38AM2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03219}.
Interaction partners:
- Succinate--CoA ligase subunit alpha, mitochondrial
- Citrate synthase
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Succinate dehydrogenase, putative
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Dihydrolipoamide acetyltransferase, putative
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- oxoglutarate dehydrogenase
- 2-oxoglutarate dehydrogenase subunit, putative
- Acetyl-coenzyme A synthetase
Sequence:
MTCNTDRSFCFRSLRPGSRRRTGTFSVISSPSPFIFLLSFFLSVSTNQTAEVALATKKGPERERRSYFLFISLRVSYKLQSHITVTSMFTRIGRVCLPTKAALTQCRYLNIHEYQSKALLKEGGCKTEFGVACSSIEEVEAALGKIKGDKKVVKSQILAGGRGMGTFVDGFKGGVHVCKDAAEALACARRMLNNTLVTKQTGPKGQKVSRLYVTEAISGIKRELYLALLLDRKTASPVFIGSAEGGMGIEELAQKQPDKIKKMRINVQEGINHDNCLTFAHELGFTGRAAENAAEQIKALYNVGKSKDCTMVEINPLVELENGDVMCIDAKLSFDDNAEFRQHDIFALADATQIDPKEVVAKKYDLNYIALDGNVGCLVNGAGLAMATMDLISHGGGKPANFLDVGGSATKEQIVAAFEIITGDEAVRSILVNIFGGIMRCDTIAEGIVAASRMLKSKGVREVPVVVRLSGSKEEEGKRILKESGLPLHPAQNFEEAAALACKLAA
Protein: Protein phosphatase fem-2 (EC 3.1.3.16) (Ca(2+)/calmodulin-dependent protein kinase phosphatase) (CaM-kinase phosphatase) (CaMKPase) (Feminization of XX and XO animals protein 2) (Sex-determining protein fem-2) (P49594)
Organism: Caenorhabditis elegans
Function: Dephosphorylates auto-phosphorylated Ca(2+)/calmodulin-dependent protein kinase unc-43/CAMKII in vitro. Involved in the regulation of sex determination. Together with fem-3, required for male sexual development by promoting the proteasomal-mediated degradation of tra-1, a transcription repressor of male-specific genes. Promotes apoptosis.
Interaction partners:
- Sex-determining protein fem-1
- Sex-determination protein fem-3
- Cullin-2
- Calpain-5
- Sex-determining transformer protein 2
- Protein her-1
- Sex-determining transformer protein 1
- Anti-proliferative protein domain-containing protein
- Elongin-C
Sequence:
MEKVNEERDAVFEDHIGDRRRSVRSLLEEAFADEMEKTSYDVEVADTPQPHIPIRFRHPPIAGPVHDVFGDAIHDIFQKMMKRGQAVDFCHWVSHLIATEIDEKFSEVAFRDVQYNPDIYVTDSTTEAKKLFNDKIWPAIDKILQQNAETCPILSEKWSGIHVSGDQLKGQRHKQEDRFLAYPNGQYMDRGEDPISVLAVFDGHGGHECSQYAAGHLWETWLEVRKSRDPSDSLEDQLRKSLELLDERMTVRSVKECWKGGSTAVCCAIDMDQKLMALAWLGDSPGYVMSNIEFRQLTRGHSPSDEREARRVEEAGGQLFVIGGELRVNGVLNLTRALGDVPGRPMISNEPETCQVPIESSDYLVLLACDGISDVFNERDLYQLVEAFANDYPVEDYAELSRFICTKAIEAGSADNVSVVIGFLRPPQDVWKLMKHESDDEDSDVTDEE
Protein: Rho-related GTP-binding protein Rho6 (Rho family GTPase 1) (Rnd1) (Q92730)
Organism: Homo sapiens (Human)
Function: Lacks intrinsic GTPase activity. Has a low affinity for GDP, and constitutively binds GTP. Controls rearrangements of the actin cytoskeleton. Induces the Rac-dependent neuritic process formation in part by disruption of the cortical actin filaments. Causes the formation of many neuritic processes from the cell body with disruption of the cortical actin filaments.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11940653}; Lipid-anchor {ECO:0000269|PubMed:11940653}; Cytoplasmic side {ECO:0000269|PubMed:11940653}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11940653}.
Interaction partners:
- Plexin-B1
- Plexin-A2
- Plexin-A1
- Plexin-B2
- Rho GTPase-activating protein 35
- UBX domain-containing protein 11
- Semaphorin-4D
- Plexin-A4
- Ras-related protein R-Ras
- Rho-related GTP-binding protein RhoD
Sequence:
MKERRAPQPVVARCKLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENYTACLETEEQRVELSLWDTSGSPYYDNVRPLCYSDSDAVLLCFDISRPETVDSALKKWRTEILDYCPSTRVLLIGCKTDLRTDLSTLMELSHQKQAPISYEQGCAIAKQLGAEIYLEGSAFTSEKSIHSIFRTASMLCLNKPSPLPQKSPVRSLSKRLLHLPSRSELISSTFKKEKAKSCSIM
Protein: E3 ubiquitin-protein ligase RNF113A (EC 2.3.2.27) (Cwc24 homolog) (RING finger protein 113A) (Zinc finger protein 183) (O15541)
Organism: Homo sapiens (Human)
Function: Required for pre-mRNA splicing as component of the spliceosome. E3 ubiquitin-protein ligase that catalyzes the transfer of ubiquitin onto target proteins. Catalyzes polyubiquitination of SNRNP200/BRR2 with non-canonical 'Lys-63'-linked polyubiquitin chains. Plays a role in DNA repair via its role in the synthesis of 'Lys-63'-linked polyubiquitin chains that recruit ALKBH3 and the ASCC complex to sites of DNA damage by alkylating agents. Ubiquitinates CXCR4, leading to its degradation, and thereby contributes to the termination of CXCR4 signaling.
Subcellular location: Nucleus {ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316}. Nucleus speckle {ECO:0000269|PubMed:29144457}. Note=Colocalizes with ASCC2 in nuclear foci after DNA damage by alkylating agents. In the absence of DNA damage, colocalizes with the spliceosome components SNRNP200/BRR2 and PRPF8 in nuclear speckles. {ECO:0000269|PubMed:29144457}.
Interaction partners:
- Splicing factor 3B subunit 2
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Spliceosome-associated protein CWC27 homolog
- Pre-mRNA-splicing factor CWC22 homolog
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16
- Splicing factor 3A subunit 2
- BUD13 homolog
- Splicing factor 3B subunit 1
- Smad nuclear-interacting protein 1
Sequence:
MAEQLSPGKAVDQVCTFLFKKPGRKGAAGRRKRPACDPEPGESGSSSDEGCTVVRPEKKRVTHNPMIQKTRDSGKQKAAYGDLSSEEEEENEPESLGVVYKSTRSAKPVGPEDMGATAVYELDTEKERDAQAIFERSQKIQEELRGKEDDKIYRGINNYQKYMKPKDTSMGNASSGMVRKGPIRAPEHLRATVRWDYQPDICKDYKETGFCGFGDSCKFLHDRSDYKHGWQIERELDEGRYGVYEDENYEVGSDDEEIPFKCFICRQSFQNPVVTKCRHYFCESCALQHFRTTPRCYVCDQQTNGVFNPAKELIAKLEKHRATGEGGASDLPEDPDEDAIPIT
Protein: Apoptosis regulator BAX (Q63690)
Organism: Rattus norvegicus (Rat)
Function: Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.
Subcellular location: [Isoform Alpha]: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q07812}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q07812}. Nucleus {ECO:0000250|UniProtKB:Q07812}. Note=Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress conditions, undergoes a conformation change that causes release from JNK-phosphorylated 14-3-3 proteins and translocation to the mitochondrion membrane (By similarity). {ECO:0000250|UniProtKB:Q07812}.; SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm {ECO:0000250}.
Interaction partners:
- Bcl-2-like protein 11
- BH3-interacting domain death agonist
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- BCL2-antagonist/killer 1, isoform CRA_b.
- Cytochrome c, somatic
- Cellular tumor antigen p53
- Apoptosis-inducing factor 1, mitochondrial
- NAD-dependent protein deacetylase sirtuin-1
- E3 ubiquitin-protein ligase parkin
Sequence:
MDGSGEQLGGGGPTSSEQIMKTGAFLLQGFIQDRAGRMAGETPELTLEQPPQDASTKKLSECLRRIGDELDSNMELQRMIADVDTDSPREVFFRVAADMFADGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLVWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG
Protein: Cytochrome P450 86A8 (EC 1.14.14.1) (Protein LACERATA) (O80823)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the omega-hydroxylation of various fatty acids (FA). Acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18. May be involved in the biosynthesis of cutin in the epidermis which prevents post-genital organ fusions. Hydroxylated FAs may be important for trichome differentiation, establishment of apical dominance and senescence.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Omega-hydroxypalmitate O-feruloyl transferase
- Protein HOTHEAD
- Fatty alcohol:caffeoyl-CoA acyltransferase
- F21B7.2
- Very-long-chain enoyl-CoA reductase
- Probable lysophospholipase BODYGUARD 1
- Glycerol-3-phosphate 2-O-acyltransferase 4
- Long chain acyl-CoA synthetase 2
- Probable glycerol-3-phosphate acyltransferase 8
- Acyl-CoA hydrolase 2
Sequence:
MEISTALMILSAITAYFLWLTFISRCLKGPRVWPILGSLPGLIENCERMHDWISDNLRACSGTYQTCICAIPFLAKKQGLVTVTCDPRNLEHILKNRFDNYPKGPTWQAVFHDLLGQGIFNSDGDTWLFQRKTAALEFTTRTLRQAMARWVNRAIKLRFLPILENARLGSEPIDLQDLLLRLTFDNICGLTFGKDPRTCAPGLPVNTFAVAFDRATEASLQRFILPEILWKFKRWLRLGLEVSLTRSLVQVDNYLSEIITTRKEEMMTQHNNGKHHDDLLSRFIKKKESYSDETLQRVALNFILAGRDTSSVALSWFFWLITQHPAIEDKILREICTVLVETRGDDVALWTDEPLSCEELDRLVFLKAALSETLRLYPSVPEDSKRAVKDDVLPDGTFVPAGSSITYSIYSAGRMKSTWGEDCLEFKPERWISQSDGGRFINHDPFKFVAFNAGPRICLGKDLAYLQMKSIASAVLLRHRLTVVTGHKVEQKMSLTLFMKYGLLVNVHERDLTAIAADLRECKSNVVNDGVGNGVSS
Protein: VIP peptides [Cleaved into: Intestinal peptide PHI-42; Intestinal peptide PHI-27 (Peptide histidine isoleucinamide 27); Vasoactive intestinal peptide (VIP) (Vasoactive intestinal polypeptide)] (P32648)
Organism: Mus musculus (Mouse)
Function: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.
Subcellular location: Secreted.
Interaction partners:
- Vasoactive intestinal polypeptide receptor 2
- Vasoactive intestinal polypeptide receptor 1
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Glucagon-like peptide 1 receptor
- Vasopressin V1a receptor
- Gastric inhibitory polypeptide receptor
- D
- Beta-1 adrenergic receptor
- Protachykinin-1
- Secretin
Sequence:
MEARSKPQFLAFLILFSVLFSQSLAWPLFGPPSVVRLDDRMPFEGAGDPDQVSLKADSDILQNPLAENGTPYYDVSRNARHADGVFTSDYSRLLGQISAKKYLESLIGKRISSSISEDPVPIKRHSDAVFTDNYTRLRKQMAVKKYLNSILNGKRSSEGDSADFLEELEK
Protein: Rho GTPase-activating protein gacT (GTPase activating factor for raC protein T) (Q54NL0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Rho GTPase-activating protein involved in the signal transduction pathway.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- AP-2 complex subunit mu
- AP-2 complex subunit alpha-2
- AP-2 complex subunit sigma
Sequence:
MKNIFRRSVQIFHKDKKEGDKQDYTGSSGSSGNSGTDRSPTSSLSKKDKKHSKHHQNESYSGDNSPTLSRNHHDEIGHLQYTANHHIATSHHSHSHNHNHNHNHQLTQPIQQQQQTQHVNLASNNYYIRHIYTNNQYDETTQIVMNNGIPFIYNPNARKIFGVPLTQVPCRAGSNVPIIIEKLIDHIERTSLNSEGLFRIPGVDLTINQYIKLFDNGEDVDVSPIEPYTAAGLLKRFFRDLPVFVPQSINKRVVSLFIDEEGKKKPVDMEILSNLRVLVHQLPTVHFEVMQELTNLLGKLMSRSDQNKMTISNIAICLVPTLNCVPAIVTYSIQMHDFFYNEVFPQHHLYYMRPYEEKLVESAPTQPINIMTTSGGEKRYSSRPASITISGLLPSNGQNNSPSSSTITSTTITSPHDSTAPITFTVTTTFSPEQQQQMLQQQQQQQQQQEKQSSSSLSQSQQSIQPISDTNSTKSDRRTFRVDPNLDLTQYIEDTQYNVNRNYLYNGGPSGTTGTTPNGGSLSIGGGNGGNGGSSLSVGSGGGNGGSSLSVGSNTSVGVGGGGGGNNTTDQSKIYRRSVAYTNNEDTKAAIQQIKEKIDRYSKEKKTREEKEREKLLRYSIDLERYKDRTINNKQEKRASRDINKEIEREIEKKRLSPRERLNLFGLSSSSSSVNSTLTRSTANIISTIDGSGGSNRNSKNYGNGSSSSSNRRYSNTINQQLQMQLQQLQIQQQQYQQTQQSQIPLQYQQQQQQQQQQTTTTTTTSSGSNRFSSNRYKPVDLTQSSSNFRYSREIYDDDYYSNNNLMMFGNEQPNQTPISVSSSSAFTRQRSQSCFEPENLVLLQQQYQQYQQQQQQQQQIPFQANPQYSNAVIEQKLDQIRDTINNLHRDNRVSRDYTHYLREVEDLRSSLQKETVVSNEFIKNIELEDKLRREEEKNQRLIEEIHLLETYFILKEKSKAKRLSTTKDLLTRSRSPTLPSSINMSTSSLGSSSSSAYNNNNNNNNVPK
Protein: Zinc finger protein, putative (Q38DK7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGASEAKGENWQKDSDVSGCCKCNVSFSLTTRRHHCRKCGLVVCSKCSRYRINLSSHDSDTPKRVCRHCFHTLRKNGAAGFETGVGSSASTGGWGLDGSVSPTTEKENTADDTNFETPDDEKAPAAEDCDSINCCFVGAGCGGCYGEGADAYYDTGTLYSDPITALLDVGEKTALQTEKERLLQQWTEIRQNVVFVDIQLQEVERVGENTPVGYCQEVENIMLQPELPERLRTMFPFPRGGEGNMELLMKPLEPITALTCKSQKEVSDALRQVTAQLQLSRLPNY
Protein: Cytochrome c oxidase subunit 8, mitochondrial (Cytochrome c oxidase polypeptide VIII) (P04039)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 3
Sequence:
MLCQQMIRTTAKRSSNIMTRPIIMKRSVHFKDGVYENIPFKVKGRKTPYALSHFGFFAIGFAVPFVACYVQLKKSGAF
Protein: Apelin receptor early endogenous ligand (Protein Elabela) (ELA) (Protein Toddler) (P0DMC4)
Organism: Mus musculus (Mouse)
Function: Endogenous ligand for the apelin receptor (APLNR) (By similarity). Hormone required for mesendodermal differentiation, blood vessels formation and heart morphogenesis during early development and for adult cardiovascular homeostasis. Drives internalization of the APLNR (By similarity). Acts as a motogen by promoting mesendodermal cell migration during gastrulation by binding and activating APLNR (By similarity). Acts as an early embryonic regulator of cellular movement with a role in migration and development of cardiac progenitor cells. May act as a chemoattractant for the activation of angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). Positively regulates sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel sprouting. Plays a role in placental vascular development; promotes placental trophoblast invasion and spiral artery remodeling in the uterus. Involved in the regulation of maternal cardiovascular homeostasis to prevent gestational hypertension and for potent cardioprotective functions during heart failure. Mediates myocardial contractility in an ERK1/2-dependent manner (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:28663440}. Secreted, extracellular space {ECO:0000269|PubMed:28663440}. Note=Found in blood plasma (By similarity). Found in serum of pregnant mice, peaking at midgestation; indicating a maternal and zygotic origin of circulating APELA during pregnancy (PubMed:28663440). {ECO:0000250|UniProtKB:P0DMC3, ECO:0000269|PubMed:28663440}.
Interaction partners:
- Apelin receptor
- Apelin
Sequence:
MRFQPLFWVFFIFAMSLLFISEQKPVNFPRRRKLYRHNCFRRRCIPLHSRVPFP
Protein: Coiled-coil domain containing 151 (Coiled-coil domain-containing protein 151) (F1QFD6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Armadillo repeat containing 4
- Coiled-coil domain-containing 114.
- Outer dynein arm-docking complex subunit 4
- Dynein, axonemal, heavy chain 5.
- Coiled-coil domain-containing protein 40
- Dynein, axonemal, intermediate chain 1, paralog 1.
- Dynein, axonemal, heavy chain 11.
- Dynein, axonemal, heavy chain 11.
- Calaxin
- Dynein axonemal assembly factor 19
Sequence:
MPGTSVSGGLMVPIHDKISELQRKIQLLEGDRSAYFESSQSAIKKNRESILQLRQENKNLHKKLAESDEQVIKDVFQGYGVEKAPFRNMPVKAARTVLEKQVRDKMKKLNAMKHTTQKQRQRLEDLKLQYQSMKPHNKSPLPDTQKQEDEEKKLRILENRLEKTQLKCHEAEHIMRGYLKLKEHLQEESLTFQPQLDRMETEIHRQTQVFKDLQVMNSDAHLSKDAAKAELQLQEEQVYRERKEREKILSRYKKQTVERMNQAERMKRRPQWATMHPDELSSEAQRSAIIVGEEAETTSTFEEAFQRIKEATGVTDSQEIVDRFVSQGETHGHLERMKAENERMLQELKEERNTLQTQLQDMKYSRETELSSAEQMLQECELRLQQEQQRRDAAKDHLDRLTHILNTVRAGVQQLSDKLQHIPPMKGPEPQLSPDSDEHILELMSEAEEKLMLLKEELQGNDLATIMKEMEEEEFHATIARKIPQYNTRIQLHEAHKQDPFDDEEDSGDDEGDIITRFSLKHQSQAIIDANTKRKTRIKKRKGKL
Protein: Synaptonemal complex protein 3 (SCP-3) (Q8IZU3)
Organism: Homo sapiens (Human)
Function: Component of the synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for centromere pairing during meiosis in male germ cells (By similarity). Required for normal meiosis during spermatogenesis and male fertility. Plays a lesser role in female fertility. Required for efficient phosphorylation of HORMAD1 and HORMAD2 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q60547}. Chromosome {ECO:0000250|UniProtKB:Q60547}. Chromosome, centromere {ECO:0000250|UniProtKB:Q60547}. Note=It is present in early unpaired cores, in the lateral domains of the synaptonemal complex and in the chromosome cores when they separate at diplotene. It is found axial to the metaphase I chromosomes and in association with pairs of sister centromeres. The centromere-associated protein becomes dissociated from the centromeres at anaphase II and is not found in mitotic metaphase centromeres. {ECO:0000250|UniProtKB:Q60547}.
Interaction partners:
- Synaptonemal complex protein 2
- Synaptonemal complex protein 1
- HORMA domain-containing protein 2
- HORMA domain-containing protein 1
- Synaptonemal complex central element protein 2
- Breast cancer type 2 susceptibility protein
- Testis-expressed protein 12
- Synaptonemal complex central element protein 3
- MutS protein homolog 4
- Synaptonemal complex central element protein 1
Sequence:
MVSSGKKYSRKSGKPSVEDQFTRAYDFETEDKKDLSGSEEDVIEGKTAVIEKRRKKRSSAGVVEDMGGEVQNMLEGVGVDINKALLAKRKRLEMYTKASLKTSNQKIEHVWKTQQDQRQKLNQEYSQQFLTLFQQWDLDMQKAEEQEEKILNMFRQQQKILQQSRIVQSQRLKTIKQLYEQFIKSMEELEKNHDNLLTGAQNEFKKEMAMLQKKIMMETQQQEIASVRKSLQSMLF
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial (Complex I-AGGG) (CI-AGGG) (NADH-ubiquinone oxidoreductase AGGG subunit) (Q9CPU2)
Organism: Mus musculus (Mouse)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:38575788}; Matrix side {ECO:0000269|PubMed:38575788}.
Interaction partners:
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 beta subcomplex subunit 8, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 alpha subcomplex subunit 1
Sequence:
MSALTRLVPFGRVGGRLLRGCRARAAGDSGVRHAGGGVHIQPRYREFPQLTRSQVIQGEFLSSLMWFWILWRFWHDSDAVLGHFSYPDPSQWTDEELGIPPDDED
Protein: Elongator complex protein 3 (EC 2.3.1.-) (B4DKA4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPKLKAKPIRTASGIAVVAVMCKPHRCPHISFTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSGHTSNNIYEAVKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIEQFTEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVARILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGIQCRDVRTREVGIQEIHHKVRPYQVELVRRDYVANGGWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMEEAERIAREEHGSGKIAVISGVGTRNYYRKIGYRLQGPYMVKMLK
Protein: 2-isopropylmalate synthase 2, mitochondrial (EC 2.3.3.13) (Alpha-IPM synthase 2) (Alpha-isopropylmalate synthase 2) (Alpha-isopropylmalate synthase II) (Q12166)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Redundant to LEU4, responsible for about 20% of alpha-IPMS activity. Involved in leucine synthesis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
Interaction partners:
- 2-isopropylmalate synthase
- 3-isopropylmalate dehydratase
- Dihydroxy-acid dehydratase, mitochondrial
- Branched-chain-amino-acid aminotransferase, cytosolic
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Acetolactate synthase catalytic subunit, mitochondrial
- Acetolactate synthase small subunit, mitochondrial
- Acetyl-CoA acetyltransferase
- Acetyl-coenzyme A synthetase 2
- Acetyl-coenzyme A synthetase 1
Sequence:
MVKHSFIALAEHASKLRRSIPPVKLTYKNMLRDPSVKYRAFAPPKMVKRIWPDKTIQKAPRWLSTDLRDGNQSLPDPMSVAQKKEYFHKLINIGFKEIEVSFPSASQTDFDFTRYAVENAPDDVGIQCLVQSREHLIKRTVEALTGAKRATIHTYLATSDMFREIVFNMSREEAISKAVEATKLVRKLTKDDPSQQATRWSYEFSPECFSDTPGEFAVEICEAVKKAWEPTEENPIIFNLPATVEVASPNVYADQIEYFSTHITEREKVCISTHCHNDRGCGVAATELGMLAGADRVEGCLFGNGERTGNVDLVTVAMNMYTQGVSPNLDFSDLTSISEIVHRCNKIPIPPRAPYGGELVVSAFSGSHQDAIKKGFAIQNKKQAQGETRWRIPYLPLDPKDIGRDYEAVIRVNSQSGKGGAAWVIMRSLGLDVPRPMQVDFSNTLQKNADALGRELKSEEITKLFKETYNYNNNEHIYVTLLNYEVKKLNPERRALVGQVEINDKVVNIEGYGNGPISSLVDALSNLLNVKLSVQNYSEHSLGSGSATQAASFINLSYIKDINNHATSNMWGVGVSEDTGDASIKAVFATVNNIIHSGDVLLAE
Protein: Major facilitator superfamily (MFS) profile domain-containing protein (Q8T2G9)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MSYKIINSSDDDNDNNNNNDINNNENIIREEEKNKTLPNSPIQTDEQKKKQTLSINIMVLTVFLQSIGFTLILPSMLNYLNSNDPQFKRYFGYIVALYSLGQFLGSPLFGKWSNKRAASEPVVISIVISIIGSIFYSICYKFHGFAFPAIMGTARFIVGFGAGNVSVCRAYATETATIENKTQIMGKMSGAQGAGFVLGPGIGFLLNFCNFTIGQMVINKYTAPGYLSILLAILNIILVLVSFRDARDLEKRNLKTPETASLLSINDADADADANNDADKPKKNMEQRLKPIVLSIFLFMVVITIFAVFETVLTLMTLQYYDWGSTENYIILGTSGIISVGIFIAISSPVIKKFDDRKTALFGFTCLFIALVLLINYNIPIGSRMTLPKWQFFMGSAFVSVGYPIASSLVYAIFSKVLNPNSHTQGTKMGWLTAGGSLARMVGPLWSQEIWTATNQQGMELFFVTAVITLIAIVVFIIFYKDLSPHPEFVSQQKTVNK