wanglab/gogpt-training-data huggingface dataset:
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8IAS3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MPPLGRQVGGSPQDDDAKNMFDRIGKDVYDQVKKGVAETYKEALTGQLSLATLLGVESASTTDPCGLDYSKLISGSGVAARGHPCGNESVSEKRFSKERVDEYDEKKIKDNKGNRGNNEGECAPYRRLSLCNKNFQKINNIDSDKARHNLLVDVCLAAHYEGDSIKAHLEQYDATYPGSGSTTCTALARSFADIGDIVRGRDLYRGNKKKIKTETERDKLEQKLKEIFKNIKKENNEKLKSLTDDQIREYWWTANRHTVWKAITCKADASSAYFHATCSDSHRSGTFSQANNYCRCNGDQPGNDKENIDPPTYFDYVPQYLRWFEEWAEDFCRKKKHKLNDAIQKCRGEDKYGKDRYCDLNGYDCEKTKRGRNMYRWDHKCTGCFLSCSHFRTWIDNQKLEFLKQKEKYTNEISGGKSRKKRAARSSSSSSYDNGYEKKFYDQLKAGGYNGVNSFLDLLSKEKTCKDITDTEGGKIDFKNVNSDKNSYDDDSNKTFSHTEYCQACPLCGVKRNGRKWERKEVMKDCPPINLYKPKKDAEGTLINFLYSGDETNEIAKKLKAFCAQANGDTTNGTGGNGTGGSVAGGTGTSGSNELYQKWKCYEIDELTKDQKEGGEDDPVYDEDVKTGGGLCILENKNKSKGSQSNSQKEPDEIQKTFNPFFYYWVVHMLKDSIHWRTKKLDKCINNSNESKACKNNNKCKDDCGCFLKWVVQKKTEWENIKKHFKKQKDIPPGFTHDDVLEGVLEKEVLLTSIKEGYGNEKDIKHIKKLLDEEEAAGVTDNENKTTIDKLLKHEKDEADKCKQIQEECNKQKQQERGGPGGRSADPSPPADLDEHSSDEGEEDDDDDEEEENANEETAEDATEDTQVDGTEVVEETVAEVTEVTEVKPCEIVQKLFTNGDLQNTFKDACEQKYGYPQRHWGWKCISDTTTGKSGDNTGSSGAICIPPRRRKLYIGKIKEWANSGNTQAAEPQEDGKAQTPQGQTPSQSGKESSQSQKLREAFIQSAAIETFFLWDRYKKVKNKEIAEKKQRDSTNPFGFTQSTSGGMQALPVGGAVQGAQAQLPDGAGGSDQTPEKQLAGGKIPEVFLRQMFYTLGDYRDICVGNTPSGIDTNDKENMQKIQNKIKSVIEKSDSTPRTPGTHSPSSGTTPQALWDKISPSIWEGMLCALTYKDGGEGKKIEKVNDANGDDLFQKLKDKYSDYKTVTLEEDNTSSAMSTSPRTSETTSASSDNTPTLNNPKLSDFVLRPPYFRYLEEWGQNFCKKRTEMLEKIKEECRSGTGGHEYCSGDGHDCTDNDRKYNKMIADFHCPGCAKECMKYKTWIGKKFEEFKKQENTYKVEHGKLTNNNCSGSDNTKFCQQIKNNSFDKFLELLRHCKDGKDDTDKDNELNFSKPLQTFSRSTYCKACPIYGVKYNRGTYSAINESEYMSKNGISGENKNDKKPTEIKVLLLGRKGEVRNNDEELKELKEVCNNAGFVEDYSLQKWNCQKKNGVDQCNLTNSVDNIDDSDKIIPFNVFFQRWLRNFVHDYNKLKQKIHPCIKNEDGKEHKCIEGCKKKCECVEKWLDKKSTEWDEIKKHYEKHSKDHNEGIPHSVKGYLVQAPFKDEVLKAIKPCDFDNFKTSCGLNGTDNSQNGNNNDLVLCMIKNLEKKIEQCKKKHDENKKTPCDPLPPLPDENDETLEENPVAQPNICPQLPEEPKETCEEAVTPSEPKKAEEEPAAEPEAVPEEEAPLPPPPPAAPPRESKEKAKPPPKPRIKTRHVLDHPAVIPALMSSTIMWSIGIGFAAFTYFFLKKKTKSSVGNLFQILQIPKSNYDIPTKRSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSSESEYEEMDINDIYAPRAPKYKTLIEVVLEPSGNNTTASGKNTPSDTQNDIPTSDTPPPITDDEWNTLKHDFISQYLPNTQNTEPNILHDNLDNNTHPTPSRHTLDQKPFIMSIHDRDLYSGEEISYNIHMSTNSMDDPKYVSNNVYSGIDLINDTLSGNKHIDIYDEVLKRKENELFGTNYKKNTSNNSVTKNINSDPIDNQLNLFHTWLDRHRDMCEQWNNKEELLDKLKEEWENETHSGNKHSDIPSGKLSDTPSDNNIHSDIHPSDIPSGKQSDIPSDNNIHSDIPYVLNTDVSIQIHMDNPKTTNEFTYVDSNPNQVDDTYVDSNPDNSSMDTILDDLEKYNEPYYDVQDDIYYDVNDHDTSTVDSNAMDIPSKVQIEMDVNTKLVKEKYPIGDVWDI
Protein: Major facilitator superfamily (MFS) profile domain-containing protein (A0A060VUB5)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- malate synthase
- Cytochrome b5 heme-binding domain-containing protein
- Cytochrome b5 heme-binding domain-containing protein
- Cytochrome b5 heme-binding domain-containing protein
- Oxidoreductase FAD/NAD
- Major facilitator superfamily
- Solute carrier family 2, facilitated glucose transporter member 5
- Solute carrier family 2, facilitated glucose transporter member 4
- Major facilitator superfamily
- Haloacid dehalogenase-like hydrolase domain-containing protein 3
Sequence:
MLTVGAAVIGSLQFGYNTGVINAPQKVIERFLNETWFDRYQEPISKTSLTTLWSVSVAIFSVGGIFGSFSVGLFVNRFGRRNSMLMANVLAFVSAALMGFSKMGGSWEMLIIGRFVVGLYSGLSTGFVPMYVGEVAPTALRGALGTLHQLGIVTGILMAQVFGMEALMGNASLWPFLLGFTFIPALAQCALLPFCPESPRFLLINRNEENKAKTVLKKLRGTTDVSADMQEMKEEARQMMREKKVTILELFRSPLYRQPIFIAIMLQLSQQLSGINAVFYYSTRIFEKAGVAQPVYATIGAGVVNTAFTVVSLFVVERAGRRSLHLLGLIGMAGAAVLMTIALALLDKLPWMSYVSIVAIFAFVAFFEIGPGPIPWFIVAELFSQGPRPSAFAVAGFSNWTANFIVGMAFQYVEELCGPYVFVIFTILLLSFFIFTYFKVPETKGRTFDEISAGFRQSSGTGGEKHSPEELNSLGADSQL
Protein: Regulator of G-protein signaling 13 (RGS13) (Q8K443)
Organism: Mus musculus (Mouse)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to both G(i)-alpha and G(q)-alpha.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MSRHICWICKLCRDESKRLPSNLTLDEVLKWAQSLESLMATKYGPIVYTAYLKLEHSDENIKFWMACETYKKIASRRGRISRAKKLYNIYIQPQSPREINIDSTTREAIIKSIREPTQTCFEEAQKIVYMHMEMDSYPRFLKSEMYQQLLKTVQSQSS
Protein: Nuclear inhibitor of protein phosphatase 1 (Nuclear inhibitor of protein phosphatase type 1) (SD02428p) (Q9V7W9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine/threonine-protein phosphatase beta isoform
- Serine/threonine-protein phosphatase alpha-2 isoform
- Serine/threonine-protein phosphatase alpha-1 isoform
- Serine/threonine-protein phosphatase alpha-3 isoform
- LD35087p
- GH07711p
- E3 ubiquitin-protein ligase PPP1R11
Sequence:
MANSYDIPSWAGKPPTGLHLDVLKDDKLVQKLMVDEKRCYLFGRNSQMNDFCIDHASCSRVHSAFVYHKHLNIAYLVDLGSTHGTFIGTLRLEAHKPTQLQINSTFHFGASTRNYILRERPSGHHSNIMEDLPLSETSDGALLGLPESQTELDNLTEYNTAHNRRISMLGIDDDTNMRKQNALKQGRRTRNVTFNDEEIVINPEDVDPNVGRFRNLVQTTVVPAKRARCDVNHMGIHSGNSSLSSANAAHVHQMFQQSLVDMKQQHREMPPPNAVLHSPTNSLYQGLPAEMHGKGDLEPISPLSIGSKLGLLLPNPAPEVLPVYDEAVETSTLAQKLAVANANVRRFGEDPHDSSGEGDSLCPQKKKYAKEAWPGRKPMLGQL
Protein: Polyamine aminopropyltransferase (1,3-diaminopropane aminopropyltransferase) (EC 2.5.1.23) (Norspermidine aminopropyltransferase) (EC 2.5.1.126) (Norspermine synthase) (Putrescine aminopropyltransferase) (PAPT) (EC 2.5.1.16) (Spermidine aminopropyltransferase) (EC 2.5.1.79) (Spermidine synthase) (SPDS) (SPDSY) (Sym-norspermidine synthase) (Thermospermine synthase) (Q9UXE4)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to various amine acceptors such as putrescine (1,4-diaminobutane), 1,3-diaminopropane, sym-norspermidine and spermidine. The biosynthesis of caldopentamine from norspermine has been also observed, but with a very low activity. The reaction involves a nucleophilic attack on the C-3 methylene of the propylamine moiety adjacent to the positively charged sulfur of decarboxy-AdoMet. S-adenosylmethioninamine is the only amino donor.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
Interaction partners:
- S-adenosylmethionine decarboxylase proenzyme
- Arginine decarboxylase proenzyme
- Putative snRNP Sm-like protein
- Agmatinase
- Agmatinase
- S-methyl-5'-thioadenosine phosphorylase
- Purine nucleoside phosphorylase
- Large ribosomal subunit protein eL37
- Small nuclear riboprotein protein
- Sm domain-containing protein
Sequence:
MFGWHWLLEWQTPYEFHGHLIEKVLAEEKTPYQHVTLVEFTRFGKGLIIDGKVQSTLYDEHIYHELLVHPLLLSLTKPPKSVLILGGGEGATLREVLKYKSVEKAVMVDIDEKVIEFAKKYLYEWHQGAFEDKRTNLVITDGLKFIKETKEKYDAIILDLTDPIKNSTSYMLYTKEFYEKLREILNERGGIVTQATSPSFSLEVYVTIYNTIKEVFKEASASYTYMASFDGLWGFVYGGVRPDLLSEDEVDSKINERIDGQLRFYDGYSHKISFSLPKNIKSEFQKITKISTEKDPIYVPA
Protein: Regulator of chromosome condensation 1 (C9JW69)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSPKRIAKRRSPPADAIPKSKKVKDTRAAASRRVPGARSCQVSHRSHSTEPGLVLTLGQGDVGQLGLGENVMERKKPALVSIPEDVVQAEAGGMHTVCLSKSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEKVVQVSAGDSHTAALTDDGRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDVPVVKVASGNDHLVMLTADGDLYTLGCGEQGQLGRVPELFANRGGRQGLERLLVPKCVMLKSRGSRGHVRFQDAFCGAYFTFAISHEGHVYGFGLSNYHQLGTPGTESCFIPQNLTSFKNSTKSWVGFSGGQHHTVCMDSEGKAYSLGRAEYGRLGLGEGAEEKSIPTLISRLPAVSSVACGAS
Protein: Candida glabrata strain CBS138 chromosome L complete sequence (Q6FKT0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome G complete sequence
Sequence:
MHRTYSLRSSRAPTAAQMQSPPPPPSSTKSRFFGKGGIASTFRKSTAGNFGPELSRKLSQLVKTEKNVLRALEVVSNERRAAARQLSLWGSENDDDVSDVTDKLGVLIFELGELQDQFIDKYDQYRVTMKSIRNIEASVQPSRDRKEKITDEIAHLKYKDPSSTKIPVLEQELVRAEAESLVAEAQLSNITREKLKAAFNYQFDSIRELAEKFALIAGYGKALLELLDDSPVTPGETRPAYDGYDASRQIIMDAEGALEAWTLDVAAVKPTLSFHQTVDDVYEEEDGEEVQEGEEGQQWEEEQQEEHHEGEN
Protein: GTPase IMAP family member 5 (GTPase of the immunity-associated protein 5) (Immunity-associated nucleotide 4-like 1 protein) (Immunity-associated protein 3) (Q8BWF2)
Organism: Mus musculus (Mouse)
Function: Plays a role in T lymphocyte development and the optimal generation of CD4/CD8 double-positive thymocytes. Inhibitor of GSK3A. May act by sequestering GSK3A in cytoplasmic vesicles and impairing its translocation to the nucleus. Consequently, impairs GSK3A-dependent transcriptional program and regulation of the DNA damage response occurring during T cells proliferation. Required for the survival of bone marrow hematopoietic stem cells, as well as of peripheral T cells, natural killer (NK) and NK T-cell development and the maintenance of normal liver function. May promote the survival of mature T lymphocytes upon cytokine withdrawal. May regulate Ca(2+) homeostasis by modulating lysosomal Ca(2+) stores, preventing its accumulation in the absence of T cell activation (By similarity). May play a role in mitochondrial DNA segregation in hematopoietic tissues. Is a regulator of liver endothelial cell homeostasis.
Subcellular location: Lysosome {ECO:0000269|PubMed:33956074}. Lysosome membrane {ECO:0000269|PubMed:21487483, ECO:0000269|PubMed:29382851}; Single-pass type IV membrane protein {ECO:0000305}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:21487483}; Single-pass type IV membrane protein {ECO:0000305}. Endosome membrane {ECO:0000250|UniProtKB:Q8K3L6}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q8K3L6}.
Interaction partners:
- GTPase IMAP family member 1
Sequence:
MEHLQKSTYGTIVQGPEAHCVQESSCLRILLVGKSGCGKSATGNSILRRPAFQSRLRGQSVTRTSQAETGTWEGRSILVVDTPPIFESKAQNQDMDKDIGDCYLLCAPGPHVLLLVTQLGRFTAEDAMAVRMVKEVFGVGVMRHMIVLFTRKEDLEEKSLEEFVTHTDNRSLRSLTQECGRRYCAFNNRASGEEQQGQLAELMALVRRLEQECEGSFHSNDLFLHAEALLREGYSVHQEAYRCYLAKVRQEVEKQRRELEEQEGSWIAKMICTVKSCWSSHTAACALLIVLGLTLLTTFINLCISRCK
Protein: Trafficking protein particle complex subunit 2-like protein (A0A0B4J294)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
Interaction partners:
Sequence:
MAVCIAVIAKENYPLYIRSTPTENELKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKVYGYVTNSKVKFVMVVDSSNTALRDNEIRSMFRKLHNSYTDVMCNPFYNPGDRIQSSGSVSLSRAFDNMVTSMMIQVC
Protein: Protein Tat (Transactivating regulatory protein) (P20893)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate OYI) (HIV-1)
Function: Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs.
Subcellular location: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. {ECO:0000255|HAMAP-Rule:MF_04079}.
Interaction partners:
Sequence:
MEPVDPRLEPWKHPGSQPKTASNNCYCKRCCLHCQVCFTKKGLGISYGRKKRRQRRRAPQDSKTHQVSLSKQPASQPRGDPTGPKESKKKVERETETDPED
Protein: AT-rich interactive domain-containing protein 3A (ARID domain-containing protein 3A) (B-cell regulator of IgH transcription) (Bright) (Dead ringer-like protein 1) (Q62431)
Organism: Mus musculus (Mouse)
Function: Transcription factor involved in B-cell differentiation. Binds a VH promoter proximal site necessary for induced mu-heavy-chain transcription. Binds the minor groove of a restricted ATC sequence that is sufficient for nuclear matrix association. This sequence motif is present in matrix-associating regions (MARS) proximal to the promoter and flanking E mu. Activates E mu-driven transcription by binding these sites. May be involved in the control of cell cycle progression by the RB1/E2F1 pathway.
Subcellular location: Nucleus. Cytoplasm. Note=Shuttles between nucleus and cytoplasm.
Interaction partners:
- Tyrosine-protein kinase BTK
Sequence:
MKLQAVMETLIQRQQRARQELEARQAPPPPPPEPTGVRARTTMTDEDREPENARMHRTQMAALAAMRAAAAGLGHPSSPGGSEDGPPISGDEDTAREGTLSSPALHGSVLEGAGHAEGDRHLMDVGSDDDDTKSKWEEQELEELGEEEEEEEEEDDFEEEEEEEEGLGPPESASLGTAGLFTRKAPPAQAFRGDGGPRMLSGPERLGPGPAHPSHMASQMPPPDHGDWTFEEQFKQLYELDADPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLFMLYVLVTEKGGLVEVINKKLWREITKGLNLPTSITSAAFTLRTQYMKYLYPYECERRGLSSPNELQAAIDSNRREGRRQSFGGSLFAYSPSGAHSMLPSPKLPVTPLGLAASTNGSSITPAPKIKKEEDSAIPITVPGRLPVSLAGHPVVAAQAAAVQAAAAQAAVAAQAAALEQLREKLESTEPPEKKMALVADEQQRLMQRAVQQSFLAMTAQLPMNIRINSQASESRQDSAVSLTSANGSNSISMSVEMNGIVYTGVLFAQPPPPTAPSAPGKGGVSSIGTNTTTGSRTGASGSTVSGGQVGLPGVSTPTMSSTSNNSLP
Protein: Two pore potassium channel b (Two K(+) channel b) (Calcium-activated outward-rectifying potassium channel 2) (OsKCO2) (Q8LIN5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Highly selective inward-rectifying potassium channel that is specifically located in the tonoplast of protein storage vacuoles. Functions independently of the voltage difference across the membrane.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:21224427}; Multi-pass membrane protein {ECO:0000269|PubMed:21224427}. Note=Tonoplast of protein storage vacuoles.
Interaction partners:
- protein-serine/threonine phosphatase
- Ribosomal protein L37
- Ribosomal protein L37
- Os02g0815000 protein
Sequence:
MAALDQQPLLHDGGDQKPPPEGAARRFRRCRTAPSSEPPPTDKDNSSAADAPPKTLFTGGGRPSFRLVGLLLVAYLLLGTIAFYLAMDHMSGTRTTRALDALYFCVVTMTTVGYGDLVPASDAAKLLACAFVFAGVAVVGTFLSKAADYLVEKQEALLFRALHSHTMVRAMEMNKVRYKLYTAGLLLVAAVASGTVVLWKVEGMRAVDAFYCVCATVTTLGYGDRSFSSEGGRAFAVAWITVSTVVVALFFLYAAELYTERRQRELARWVLRRRTTNMDLEAADLDGDHRVGAADFVLYKLKELGKISQEDISEFLDEFDNLDADHSGTLSPADLAAAQPTPDPPPSLR
Protein: Heat shock 70 kDa protein, mitochondrial, putative (Q585X3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GrpE protein homolog
- Uncharacterized protein
- Chaperonin HSP60, mitochondrial
- J domain-containing protein
- Lipophosphoglycan biosynthetic protein, putative
- Chaperonin HSP60, mitochondrial
- Chaperonin Hsp60, mitochondrial, putative
- Heat shock protein, putative
- 10 kDa heat shock protein, putative
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MLARRVCAPMCLASAPFARWQSSKVTGDVIGIDLGTTYSCVAVMEGDRPRVLENTEGFRTTPSVVAFKGQEKLVGLAAKRQAITNPQSTFFAVKRLIGRRFDDEHIQHDIKNVPYKIIRSNNGDAWVQDGNGKQYSPSQVGAFVLEKMKETAENFLGRKVSNAVVTCPAYFNDAQRQATKDAGTIAGLNVIRVVNEPTAAALAYGLDKTKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLCLSDHILEEFRKTSGIDLSKERMALQRIREAAEKAKCELSTTMETEVNLPFITANQDGAQHVQMMVSRSKFESLADKLVQRSLGPCKQCIKDAAVDLKEISEVVLVGGMTRMPKVVEAVKQFFGREPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPLSLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMASDNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGICHVTAKDKATGKTQNITITAHGGLTKEQIENMIRDSEMHAEADRVKRELVEVRNNAETQANTAERQLTEWKYVTDAEKENVRTLLAELRKVMENPNVTKDELSASTDKLQKAVMECGRTEYQQAAAANSGSSGSSSTEGQGEQQQQQASGEKKE
Protein: 3-isopropylmalate dehydrogenase (EC 1.1.1.85) (3-IPM-DH) (Beta-IPM dehydrogenase) (IMDH) (P9WKK9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01035}.
Interaction partners:
- 3-isopropylmalate dehydratase large subunit
- 3-isopropylmalate dehydratase small subunit
- Putative acetolactate synthase small subunit
- Acetolactate synthase large subunit IlvG
- D-3-phosphoglycerate dehydrogenase
- L-threonine dehydratase biosynthetic IlvA
- Acetolactate synthase large subunit IlvB1
- Ketol-acid reductoisomerase
- Dihydroxy-acid dehydratase
- Putative acetolactate synthase large subunit IlvB2
Sequence:
MKLAIIAGDGIGPEVTAEAVKVLDAVVPGVQKTSYDLGARRFHATGEVLPDSVVAELRNHDAILLGAIGDPSVPSGVLERGLLLRLRFELDHHINLRPARLYPGVASPLSGNPGIDFVVVREGTEGPYTGNGGAIRVGTPNEVATEVSVNTAFGVRRVVADAFERARRRRKHLTLVHKTNVLTFAGGLWLRTVDEVGECYPDVEVAYQHVDAATIHMITDPGRFDVIVTDNLFGDIITDLAAAVCGGIGLAASGNIDATRANPSMFEPVHGSAPDIAGQGIADPTAAIMSVALLLSHLGEHDAAARVDRAVEAHLATRGSERLATSDVGERIAAAL
Protein: Harpin hrpN (E0SDH1)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MQITIKAHIGGDLGVSGLGLGAQGLKGLNSATSSLGSSLDKLSGTIDKLTSALTSMMFGGALSQGMGSGLARGAGNQLGASLNTFGSGAQGAGNVLSKPQSGSDALSKMFDKALDDLLGHDTVTKLTNQSNQLANSLLNASQMTQGNMNAFGSGLNDALSSILGNGLGQAMGGFSPLSLGAGGLQGLNGAGAFSQLGNAIGMGVGQNAALNALSNVSTHVDGNNRNFVDKEDRGLAKEIGQFMDQYPEIFGKPQYQKDGWSSAKTDDKSWAKALSKPDDDGMTGASMDKFRQALGMIKSAVAGDTGNTNLNLRGAGGASLGIDAAVVGDKIANMSLGKLAHA
Protein: Fumarate hydratase class I, aerobic (EC 4.2.1.2) (Fumarase A) (Oxaloacetate keto--enol-isomerase) (OAAKE isomerase) (Oxaloacetate tautomerase) (EC 5.3.2.2) (P0AC33)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate.
Interaction partners:
- Fumarate hydratase class II
- Malate dehydrogenase
- Succinate dehydrogenase flavoprotein subunit
- Citrate synthase
- Succinate dehydrogenase iron-sulfur subunit
- Succinate dehydrogenase cytochrome b556 subunit
- NADP-dependent malic enzyme
- Succinate dehydrogenase hydrophobic membrane anchor subunit
- NAD-dependent malic enzyme
- Aconitate hydratase B
Sequence:
MSNKPFHYQAPFPLKKDDTEYYLLTSEHVSVSEFEGQEILKVAPEALTLLARQAFHDASFMLRPAHQQQVADILRDPEASENDKYVALQFLRNSDIAAKGVLPTCQDTGTAIIVGKKGQRVWTGGGDEAALARGVYNTYIEDNLRYSQNAPLDMYKEVNTGTNLPAQIDLYAVDGDEYKFLCIAKGGGSANKTYLYQETKALLTPGKLKNYLVEKMRTLGTAACPPYHIAFVIGGTSAETNLKTVKLASAKYYDELPTEGNEHGQAFRDVELEKELLIEAQNLGLGAQFGGKYFAHDIRVIRLPRHGASCPVGMGVSCSADRNIKAKINRQGIWIEKLEHNPGKYIPEELRKAGEGEAVRVDLNRPMKEILAQLSQYPVSTRLSLNGTIIVGRDIAHAKLKERMDNGEGLPQYIKDHPIYYAGPAKTPEGYASGSLGPTTAGRMDSYVDQLQAQGGSMIMLAKGNRSQQVTDACKKHGGFYLGSIGGPAAVLAQGSIKSLECVEYPELGMEAIWKIEVEDFPAFILVDDKGNDFFQQIQLTQCTRCVK
Protein: Uncharacterized protein (Q586D9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSDVEGSISFSNVESHILASEAVMQHQEVVDTFSDGWNSPTGVHVTGNNDRGSIVCNTAEWATGSDGLDDGDLGRRRSSIYLDAKDGDGPVSVAQGRSTIDNVALTVDTRPSDLAATLEGENYPYYDLDYVCSYAFQSEHADLNSHDYGLDAFIHGMRLGPWPLQSTVTTSPPRVLDGQSNRLAQFGGLQSSLTVASESPLRNDVGVLREANSLQDKTSPNGTSERWLRWSFRAFDGKCNLPQGTTRGCDTLGVSESSLYDVDMVLGLLCTDNGIPGVLSSGSCSEGHTQKASEICMGVMRRGDSGSNNELMLFPRHDDRGTGALTNGTSGAVYPRCSEDIIGAPTGVVNAQPLRTEEGKASGNVELTMVGDVLPKTFSCPSAASDFVGAEGPLGDVKEGTGLSLPSKALPISAILTDRARGRVGTPSCNSLVDSLIGGMEYPYFSGLKGDSNLIISSPLPSRQSICTAEEGEGAILSAEGVSVGMERECEQYLQSHISCSVGVHLRCGTELRSINPCIARCGDSRPGSTCRPASCSLDKNQGVGQGVCMGGSEQLSIQKRSREKAVQGPGRMNGSSISLVAGAESITASQSFVRPPAAVVSRKRWHPCSELSTGGVSGSHTVKVAEDGMCLVEGGSSPIIRVSRERQSVPSNRVRLIVLNHKTGTGQNDVQTAVNLRGESTLEVCPPQGLPHFFSVDEYLECTDDNDMCSVTLAELQGKFLRGMNVAMFVAGSESVPLSGWCAVFEVMNHVFRDINDECELFMSVVLIRQESARDLLSESEGGVRTLSSSVMAPWVAFENVTHMKLKSAHHFITLLSRGLEVADLKHNCVGSRVVLSVMLKQIDVNDVILSSMLVTGGATPNDLDVLLREGDQSARKLFHEALGGPYFTVVVSSLCERDRDLLQLLSAQHKFTSVVNQPCTVGSVSRLIDNAEAEVAGCSTDDQIVLERKQFLLERIALAKHIMYNPKGLSLVVDVEESVRLEKRVHCGVKFDKQPFPGPQSSSVSACGGDSHNAASALCVEEGQSSKQRQEPCPKFFSEAQWLKPSSKGDTRVTLMGGAPPSSLPQRNHYGEGKTPSCLPCVTAAGMPTPRDPRLERQVRPSSRRLSIPVEPDQASYATTCSMSDPQRGEGLPSLGPLATTCGMELAPSTQRRAHRCFPSSASSDHTTCAYSQRLFSLTPARGASHDAEVSCKIDTPGVPDAEKVRTSTTPDAFSCPGISTKVKYDPGLSLPSLKAARGPPCSMTSCFPFDPILTGPPGVVEPVEHCGISQGPALCRQREQPQLPDASVACSGGSPTLTCKQVAHASQNSVHTDIKKKQISDGGSDSSARSAEGSEDDVLHSAMSAPSKVRTLVVVDQGCGHVIGAGNDDGGPFLRTGGSHEGYEVDEVVKWGDGCGDVPSKVLGELFDVFVLGCNAAILTAESGSSTVSSTVLRGLVRNVLSEVVDASGLQNSNRRGLLSLSIVKLSGERMLDLLDDSSEPERLVIAMSPIFGPCVHNARRFPVSSCSGFDSLLASALRRAKNAGVDDGLVFVSVVLKQKLKADGDVLVSSLAVSLAGENVDLYTSVLNRVSRAPRALFHYALGGPCYTVALLSIDVATTQTENMLRVQKCIGEVVNRPIHRGSIVKFISGIRDDLVPSLREKFQGSNKCEPSDNILYRLEEMVRDAELLLENFESNDPRAYLSDKETRSPKGCVSLLETKARTGDEGRVHSLLFFEQRLLSDGTAGVQGNSVFTRAGAITRRYGVDEVVLRGPDSDSNATLCSRLLDELVRKFMSGHCTAVLAADSHNSASTPLILRKIVYLILQSTKAGVGCGPVGGDLLLSMALVKNGVTVDLLAAEESEAVHRFGVEISPLFDRHVRGVSHRVVADTEAFDRFLVGAVEHVVPTLQAEDPGLMVVSLKLTHHVEEPVHDVFVSSLMVTTVFDHVSHYSDILSNRSSELTDLFKLALGGPCFTIVALGLCDEDDDAEALLSVQTKLSQVRNLPSHRTSALRRMDELTKTIQVLGVQLQEEESEEEKAQLRVRIVRARRFLLEVESLLKNPPREMGCVRAYKSVH
Protein: NEDD8-specific protease 1 (EC 3.4.22.-) (O42980)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Protease that catalyzes two essential functions in the NEDD8 pathway: processing of full-length NEDD8 to its mature form and deconjugation of NEDD8 from targeted proteins such as the pcu1, pcu2 and pcu4 cullins and other proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15769255}.
Interaction partners:
- Ubiquitin-like protein 1
- NEDD8-activating enzyme E1 catalytic subunit
- NEDD8-conjugating enzyme ubc12
Sequence:
MSSSPTVLELFDVCFKQEDVDSLKKPNWFTDVSIDYVDELIEHLWFPSYPNQANEILLLRPSLVFLLAEAAISPEELKVALPKKLMNCKYLFMPINDLDKHAAGSGGSHWSLMVASIPDGQCYYYDSLSNGKTKDCRSALARVSDLFKKKFTIECMPVQQQRNGYDCGAHVCAFTLELVRRLLHSPMPTSSMWNLSTFQPDVTAIREQLSRCLDHIINSLGTRVSGDFDEDFPTGTVFFDLESHLPLLDVALPVLPKSSDSSETSHESSNSNLKKSSESGSTNHHNNHESDKDLHHEGHHHHHHHHHHHHSHDDDPSSPAEKKQNHVPSPSEKIQDHVPSPSEKKQDRVPSPSNNKEDHLPLLSDEKLDKSAIDKIEPTPLPSVHMNSHIAKGELPKFHNSTDNPFLTPPEELVSGDFPF
Protein: Palustrin-1c (P84276)
Organism: Lithobates palustris (Pickerel frog) (Rana palustris)
Function: Antimicrobial activity against Gram-negative bacterium E.coli. Stimulates insulin release.
Subcellular location: Secreted {ECO:0000269|PubMed:11087945, ECO:0000269|PubMed:15128283}.
Interaction partners:
Sequence:
MFTTKKSLLLLFFLGTISLSLCEEERGADEEEGDGEKLTKRALSILRGLEKLAKMGIALTNCKATKKC