wanglab/gogpt-training-data huggingface dataset:
Protein: Elongator complex protein 1 (ELP1) (IkappaB kinase complex-associated protein) (IKK complex-associated protein) (Q8VHU4)
Organism: Rattus norvegicus (Rat)
Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (By similarity). ELP1 binds to tRNA, mediating interaction of the elongator complex with tRNA (By similarity). May act as a scaffold protein that assembles active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK) (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O95163}. Nucleus {ECO:0000250|UniProtKB:O95163}.
Interaction partners:
- Elongator complex protein 3
- Elongator complex protein 5
- Elongator complex protein 2
- Elongator complex protein 4
- Elongator complex protein 4
- Elongator complex protein 6
- ESF1 homolog
- Neuromedin B
- Diphthamide biosynthesis 3.
- NF-kappa-B essential modulator
Sequence:
MRNLKLHQTLEFRDIQAPGKPQCFCLRAEQGTVLIGSERGLTEVDPVKKEVKTEISLVAEGFLPEDGSGCIVGIQDLLDQESVCVATASGDVIVCNVSTQQLECVGNVASGISVMSWSPDQELLLLATAQQTLIMMTRDYEVITEQQIHQDDFGEGKFITVGWGSKDTQFHGSEGRPITFPVQMHESALSWDDHRPQITWRGDGQFFAVSVVCSQTGARKIRVWNREFALQSTSESVPGLGPSLAWKPSGSLIASTQDKPNQQDVVFFEKNGLLHGYFTLPFLKDEVKVNDLLWNADSSVLAVWLEDLPKEGSSTLKSYVQLWTVGNYHWYLKQSLPFSTTGKNQIVSLLWDPVTPGRLHVLCQGWRYLCCDWHWTTDRSSGNSADDLANVAVIDGNKVLVTVFQRTVTPPPMCTYRLLIPHPVNQVMSSAHLGNDLAVLDASNQISVYKCDDKPDMDSTVKLGAVGGTGFKVPLRTPHLEKRYRIQFGNKEEEEDVSPLQFRFLTWIEGDAFLAISHSHSSPQSIIHHLTMAGSEGDEEQGQLNVSSSVTVDGVVIGLCCCSKTKSSAVQLADGQVLKYLWESPSSAVEPWKNSEGRPVRFARPCTQMEAAAIGGEECVLGLTDRCRFFINDTEVASNITSFAVCDDFLLVTTHSHTCQCFSLSGASLKMLQAGLCGSQVPSGEILRKVERGSRIVTVVPQDTKLILQMPRGNLEVVHHRALVLAQIRKWLDKLMFKEAFECMRKLRINLNLIHDHNPKVFLENVETFIKQIDSVNHLNLFFTELKEEDVTKTMYPPPVTKSVQVSTNPDGKKVDLICDAMRVAMETINPRKFCLSILTSHVKKTTPELDIVLQKVHELQGKIPFVPESVSAEEALKYLLLLVDVNELFNHSLGTYDFDLVLMVAEKSQKDPKEYLPFLNTLKKMETNYQRFTIDKYLKRYEKALGHLSKCGPEYFTECLNLIKDKNLYKEALKLYRPDSPQYQAVSVAYGEHLVQELLYEPAGLVFARCGAHEKALEAFLACGSWQQALCMAAQLQMAKDKVAGLARTLAGKLVEQRKHSEAATVLEQYALDYEEAVLLLLEGSAWEEALRLVYKYDRVDIIETSVKPSILEAQKNYMDFLDSQTATFIRHKNRLKVVRELKSQRPRVHVDHEVAHGRETDLFSETSSIRSGSEMSGRYSHSNSRISARSSKNRRKAERKKHSLKEGSPLEGLALLEALSEVVQSIEKLKDEVHAILKVLFLFEFEEQARELQRAFESTLQLMGTALPDIWTLTGQQSSSTPVLGPSSTVNSIMASYQQQKTCVPVLDAWACLPPKIDQRSQWKLSLLE
Protein: 5'-3' exoribonuclease 1 (EC 3.1.13.-) (Exonuclease 2) (Exonuclease II) (Exo II) (p140) (P40383)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins (By similarity). Involved in the degradation of several hypomodified mature tRNA species and participates in the 5'-processing or the degradation of the snoRNA precursors and rRNA processing (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}.
Interaction partners:
- Deadenylation-dependent mRNA-decapping factor pdc2
- LSM1-LSM7 complex subunit lsm1
- mRNA decapping complex subunit 2
- 5'-3' exoribonuclease 2
- LSM complex subunit lsm3
- mRNA-decapping enzyme subunit 1
- Enhancer of mRNA-decapping protein 3
- H/ACA ribonucleoprotein complex subunit cbf5
- Putative ATP-dependent RNA helicase C550.03c
- Putative ATP-dependent RNA helicase ste13
Sequence:
MGIPKFFRWMSERYPLCSQLIENDRIPEFDNLYLDMNGILHNCTHKNDDHSSPPLPEEEMYIAIFNYIEHLFEKIKPKKLLYMAVDGCAPRAKMNQQRSRRFRTAKDAHDARLKAERNGEDFPEEQFDSNCITPGTTFMERVSRQLYYFIHKKVTNDSQWQNIEVIFSGHDCPGEGEHKIMEYIRTQKAQPSYNPNTRHCLYGLDADLIMLGLLSHDPHFCLLREEVTFGPASRNRSKELAHQKFYLLHLSLLREYLEFEFQECRSTFTFKYDLEKILDDFILLAFFVGNDFLPHLPGLHINEGALALMFSIYKKVMPSAGGYINEKGVINMARLELILLELENFEKEIFKAEVSETKNNGNSDKPSFDFLKYITESTNDIKAMTGEQKNYFLQIKKFLSSREPFIDFSANISSVDQRFLRRLCNDLHLSFSKIIKVDGTHLLRITFRDLEFNDEDEDEIEQDEIERVLQKYDNIPLLNEEQALKEKNVEKDFIQWKDDYYRSKVGFSYYDEEALKAMAERYVEGLQWVLFYYYRGCQSWGWYYNYHFAPKISDVLKGLDVKIDFKMGTPFRPFEQLMAVLPARSQALVPPCFRDLMVNSESPIIDFYPENFALDQNGKTASWEAVVIIPFIDETRLIDALASKDKFLTEEERKRNSFNAPTVFSLAEDYTSFYPSSLPSLFPDLVTRCIQKPYSLPSMEGKEYLVGLCPGVFLGAFGMVGFPSFHTLKHKAELVYHGINVFGNESRNPSVIVNVEDVKSALTSEQIAMQYVGKRIFVDWPYLREAYVESAMDESYMYLASNSTIEKRDLAEIEKSQWGRKCSHKIREYSKRFGVLFGDISLLLQVRPIKGLEYTREGALVKIFNESVLEDYPAQLVVEKIAIDDPRFTEREAPPVEVEYPPGTKAFHLGEYNYGRPAQITGCKDNKLIIWLSTAPGLDAQWGRVLVNDSKSKEKYYPSYIVAKLLNIHPLLLSKITSSFLISNGTKRENIGLNLKFDARNQKVLGFSRKSTKGWEFSNKTVALVKEYINTFPQLFNILTTHATKDNLTVKDCFPKDDTQQLAAVKHWIKEKGINSLTRVSLDEDALDSDIIKLIEEKASTIDSTYQVPKKVFGVPRYALLKPSQTRGILHSQEFALGDRVVYVQDSGKVPIAAYGTVVGIMLHHLDVVFDLPFMSGTTLDGRCSPYHGMQVEVSMVLNVTNPQFVVNTRAGKNRKTNVSANNVSQGTDSRLVTKPTSTFPSPPSPPSSSVWNKREHHPKPFSLHQVPPPESLIHKSKSKFSKGNHHSTNGTQSIRGRGGKRGKPLRSKELNRKHDHIVQPMGKLQIN
Protein: Exocyst complex component Sec8 (A0A1D8PPF9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Exocyst complex protein EXO70
- Exocyst complex component SEC5
- Exocyst complex component SEC15
- Exocyst subunit
- Exocyst complex component EXO84
- SNARE-binding exocyst subunit
- GTP-Rho binding exocyst subunit
- Rcy1p
- Ras-related protein SEC4
- Protein transport protein SEC9
Sequence:
MSIRRYSGNSPRINDYDSRTVDESLYSLKEVYNTIKYDWPQMLREDANPIEMAVALLDDTSVGLAHRLQEFNMLKESSEQALRSVVNEHYDLFNKSMGSYNTLLSTMKNSQEDSLEIKNFLEYSNKEVHDRSAVLGELSSASAKYSEMIEVLDAMAEMNEIPGKIDQLVIDKKIHEVYDVISEGYKTAEKYNLWSLPAMNGIKTYLEEQSNKLFDMIIDELQNEIYLKYNRNPQEGAIAWQNIIHSSNPQLTSFVTLLDSKNLEQFIFNSANLDISEVVDFLTSPVKNFIVNQLPDLHAHNSKNDGVIDYKILLDSTSNPNTESFYYIYMLLLTASKLNRLNQAVEVLLDTNQSELHGLINRTTEAVKSRNGHALSKLSKMQHLDHGSLFDVIVHGSFSDSAVVLLQDLFGSIFIRCLATFQRHKVITQIVTLLQEGKAPSTPKAVAESTPTFDSPQMGRPDTFHARNLFTIWKTIQKELKALMLNYIYDDHNYKLHSLADTTGATNRNKISNALGKKELFKFEDVTYNPSNKTTKEILDVLADVFPGYSISDDNNNGAIIETATPYVKHESFNATVEVLVPKNLFNMRIILEFFLIFIDGSQRIFFDFEDEKTRGVHARTSFHFFEDFMKISFLSYLRNTIEFNFGEQVGGAYSMKIEQAMPVNSGLKLDLISLSQDSNFKILGNAVSNVESNLIIYENAYNFKKMFLELCLILNTSLSYRENFSGAVLKTLENFSNEYNKLYQELLSTGEGTNIVRPPSRVSKWMKIPVLTEISGKILQRGVQGETANELQELIESESKVVLHDETVTHQEDLLDHEAYAQIVYLLLTTTWILSWLPLVKKESNYSIYDDEQNKTIKVSTVDKLRYNWSFLENGRQAINFTPDGTDIVQYNIYLALNSEKIGEFNNIIHNFESIRDKTLLALRYELRCKAVYFVTMSFKHVDWCPVTEPGDADHFIVNLNQEIFAMDNKLSKTVSDIERESIFLGFSQFLNDLIITRSKAVRKINSNGIKRILLNISTVQQMLRNLSSNPETIDFTKASEYFEMFTMNEFNLLKFIKSKRDNYTKDAYHTLARLIYSEKLADGNGSSFNKGKYNDLIKKIDGIFD
Protein: Spaetzle-processing enzyme (EC 3.4.21.-) (Spatzle-processing enzyme) [Cleaved into: Spaetzle-processing enzyme light chain; Spaetzle-processing enzyme heavy chain] (Q9VCJ8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Endopeptidase which plays a key role in innate immunity by cleaving Tl ligand spz and thereby activating the Toll pathway in response to fungal and Gram-positive bacterial infections. Acts downstream of pathogen recognition receptors PGRP-SA and GNBP1 and protease grass in response to Gram-positive bacterial infection. Acts downstream of protease psh in response to fungal infection.
Subcellular location: Secreted {ECO:0000305}. Note=Probably secreted in the hemolymph. {ECO:0000305}.
Interaction partners:
- Protein spaetzle
- Sphinx1
- Serine protease persephone
- trypsin
- GH03360p
- Sphinx2, isoform B
- GH10112p
- Gram-negative bacteria-binding protein 3
- Modular serine protease
- Gram-negative bacteria-binding protein 1
Sequence:
MASTERNFLLLSLVVSALSGLVHRSDAAEISFGSCTPQQSDERGQCVHITSCPYLANLLMVEPKTPAQRILLSKSQCGLDNRVEGLVNRILVCCPQSMRGNIMDSEPTPSTRDALQQGDVLPGNDVCGFLFADRIFGGTNTTLWEFPWMVLLQYKKLFSETYTFNCGGALLNSRYVLTAGHCLASRELDKSGAVLHSVRLGEWDTRTDPDCTTQMNGQRICAPKHIDIEVEKGIIHEMYAPNSVDQRNDIALVRLKRIVSYTDYVRPICLPTDGLVQNNFVDYGMDVAGWGLTENMQPSAIKLKITVNVWNLTSCQEKYSSFKVKLDDSQMCAGGQLGVDTCGGDSGGPLMVPISTGGRDVFYIAGVTSYGTKPCGLKGWPGVYTRTGAFIDWIKQKLEP
Protein: Large ribosomal subunit protein eL18B (60S ribosomal protein L18-B) (RP28) (P0CX50)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
Sequence:
MGIDHTSKQHKRSGHRTAPKSDNVYLKLLVKLYTFLARRTDAPFNKVVLKALFLSKINRPPVSVSRIARALKQEGAANKTVVVVGTVTDDARIFEFPKTTVAALRFTAGARAKIVKAGGECITLDQLAVRAPKGQNTLILRGPRNSREAVRHFGMGPHKGKAPRILSTGRKFERARGRRRSKGFKV
Protein: Uncharacterized protein Rv0508 (P9WKS9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable transport accessory protein MmpS2
- Probable transport protein MmpL2
- Ribonucleoside-diphosphate reductase subunit alpha
- Vitamin B12-dependent ribonucleoside-diphosphate reductase
- Glutamyl-tRNA reductase
- Porphobilinogen deaminase
- Phosphoserine phosphatase SerB1
- Probable uroporphyrin-III C-methyltransferase HemD
- Delta-aminolevulinic acid dehydratase
Sequence:
MSRPQVELLTRAGCAICVRVAEQLAELSSELGFDMMTIDVDVAASTGNPGLRAEFGDRLPVVLLDGREHSYWEVDEHRLRADIARSTFGSPPDKRLP
Protein: Uncharacterized protein, isoform F (A0A0B4KFE1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDNKTTQLDFKLLVDQSLNLLDSLNTALRCDAIQFLLQTLKCKYPESCDQVVRNLFSHIAAANDNGESGGRAQQHELARTKQLQLLLTAKKEKKELGIGCEAEIKRENDEEEAGSTDLNQNFEKIPCKEEFLCLEEEEEDFLDDADTQNSSSLQFHTGNNVDALALGPGDPLELIQSGVSLLVKRKYAATFDDELIGDGDGDEANSNSSDGKMVKRKRTNNMHLTVSSVRRKEEHGQLGDGYVFHEDSQYTMRYHHSTGEFSERAFKAQFRALLRLALSQHHKPFLRQFYENFVVNGRLLGTTPSMRVLKELREQRLEEWRRQRERRQLVILMEQSETQRDEEFQQQQELVENQEEVQQEQEQQQQQLEDIQQQHLEEIQRQQQLPAISFGDSELESETESQLSSAAQEIMKFEEFIDEGVGAGRLIDGLEMEPEIDDMLAGAGSMNSASGHSSNSSSSGSGSAGNGNGISGVILENNSHHTHHLSSSSSANLVINGLTSSNSISNNNNNSNNVSLHRPQLTPQAQNQLAASMKPSDHIPISMPMENMDLKAGQAAHGTANAIMQGGSSSLASQLHQQQKPYNSSNNPLSMMGGMMQQQQQQHVAMPHHQRQMMMMPEDFPQHGASMMNSRQMPALAALSNLGDTPAMSGQLNSSLELDDNDLSADEDDDDLDHDLDELDAAKQQLIDGGSSSSTSLQAPPSQHGSGSGGSGGQTPGSKKDKPSYNCLLCPKSYRKRKSLLDHYKMHPGYCHDCGQRNGNTLEEIIHHNRTMHVKEFPFVCETCGESYSRKQQFHAHVESHNKKEIKTFPCGECGLKFPQKKLQQHFEETGHKADGAICEVCGEEFQSKNALYQHIIRVHKRDNFFECHICHNRFTLKANLERHVQLHTEIKRPYVCDLCGSSYFTYPALKEHYSNAHVDVSECKCTLCGKRFGSAKSLQRHLPSHSEERPHCCNYCDQTFKWKTHLVRHKQTMHGNEPPPPKKGKQRFPKTSEEADMGSLPDMPGPPPVKASKKAATSKAKAQAAAAAAAAASSQQQQQKGSAATPTPPPPVSTTPGCLQQDPFNAAMVSSNSSQSSTASTSQHSVSTSESQQNSIYNQSFNAEKQQPGQQQPQNTLHQQHPTPPPPQQQQQQQQQQQALPQSRVGPGELHLQRMNSFGQDGQFHFESNPAAGAYQQHQLISQYQQQQQQQQQQQQQQPQQQQQHHLAQQQQQHMRSHTPQSPHPPHPSQLQQQQPQQHFSSPHHMPPMHHQHQLMMQQQHRHNQRSPLHHHPAAQQLQQQHQQPSHSPQHQHARLQSPQPAPVQQQQQQQQQQQQQQQQFLQQQAADTWGNMNFGNPPNNQQVELKDNKFYIVESAEFLGLPMNVPPSPQQQQQQAVSKPQQQQQQQHPQPQQPDPTLAGDLMSFQHMWPAPGFSQTSQQQQPQQQQQQQAAQQQQQAQSQANSSDPHNYNNIGSILTNLIDTNPAPMEYNFDLMQQQQTPSAQQQQQQQQQQQAAQQQHHSAGAYGSGLMRSGGGVYGGAYEQHLSDQLVSEQQKQNSFQPYHPHGLQAQQQQPLHPHPHLLPPPAPHNNVYDRTGVGVGVGVGVGVGVGVGYPMLGDDTKSVLPPMMGGMMQQMPPHGQQPDLIYYPVKND
Protein: Aurora kinase B-A (EC 2.7.11.1) (Aurora/IPL1-related kinase 2-A) (AIRK2-A) (XAIRK2-A) (Serine/threonine-protein kinase 12-A) (Serine/threonine-protein kinase aurora-B-A) (xAurora-B) (Q6DE08)
Organism: Xenopus laevis (African clawed frog)
Function: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Phosphorylates 'Ser-10' of histone H3 during mitosis.
Subcellular location: Nucleus. Chromosome. Note=Chromosomal until metaphase but transfers to the midzone microtubule array and the equatorial cortex during anaphase.
Interaction partners:
Sequence:
MSYKENLNPSSYTSKFTTPSSATAAQRVLRKEPYVSTFTTPSDNLLAQRTQLSRITPSASSSVPGRVAVSTEMPSQNTALAEMPKRKFTIDDFDIGRPLGKGKFGNVYLAREKQNKFIMALKVLFKSQLEKEGVEHQLRREIEIQSHLRHPNILRMYNYFHDRKRIYLMLEFAPRGELYKELQKHGRFDEQRSATFMEELADALHYCHERKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRRTMCGTLDYLPPEMIEGKTHDEKVDLWCAGVLCYEFLVGMPPFDSPSHTETHRRIVNVDLKFPPFLSDGSKDLISKLLRYHPPQRLPLKGVMEHPWVKANSRRVLPPVYQSTQSK
Protein: Probable LRR receptor-like serine/threonine-protein kinase IRK (EC 2.7.11.1) (Inflorescence and root apices receptor-like kinase) (Q9LY03)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000269|Ref.1}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- IRK-interacting protein
- Protein IQ-DOMAIN 3
- IQ-domain 21
- IQ-domain 24
- Probable protein phosphatase 2C 64
- Probable inactive receptor kinase RLK902
Sequence:
MYKALIFTVLLVSAVAPVRSLDPPLNDDVLGLIVFKADLRDPEQKLASWNEDDYTPCSWNGVKCHPRTNRVTELNLDGFSLSGRIGRGLLQLQFLHKLSLSNNNLTGIINPNMLLSLVNLKVVDLSSNGLSGSLPDEFFRQCGSLRVLSLAKNKLTGKIPVSISSCSSLAALNLSSNGFSGSMPLGIWSLNTLRSLDLSRNELEGEFPEKIDRLNNLRALDLSRNRLSGPIPSEIGSCMLLKTIDLSENSLSGSLPNTFQQLSLCYSLNLGKNALEGEVPKWIGEMRSLETLDLSMNKFSGQVPDSIGNLLALKVLNFSGNGLIGSLPVSTANCINLLALDLSGNSLTGKLPMWLFQDGSRDVSALKNDNSTGGIKKIQVLDLSHNAFSGEIGAGLGDLRDLEGLHLSRNSLTGPIPSTIGELKHLSVLDVSHNQLNGMIPRETGGAVSLEELRLENNLLEGNIPSSIKNCSSLRSLILSHNKLLGSIPPELAKLTRLEEVDLSFNELAGTLPKQLANLGYLHTFNISHNHLFGELPAGGIFNGLSPSSVSGNPGICGAVVNKSCPAISPKPIVLNPNATFDPYNGEIVPPGAGHKRILLSISSLIAISAAAAIVVGVIAITVLNLRVRASTVSRSAVPLTFSGGDDFSRSPTTDSNSGKLVMFSGEPDFSTGTHALLNKDCELGRGGFGAVYRTVIRDGYPVAIKKLTVSSLVKSQDEFEREVKKLGKLRHSNLVKLEGYYWTTSLQLLIYEFLSGGSLYKQLHEAPGGNSSLSWNDRFNIILGTAKCLAYLHQSNIIHYNIKSSNVLLDSSGEPKVGDYGLARLLPMLDRYVLSSKIQSALGYMAPEFACRTVKITEKCDVYGFGVLVLEVVTGKKPVEYMEDDVVVLCDMVREALEDGRADECIDPRLQGKFPVEEAVAVIKLGLICTSQVPSSRPHMGEAVNILRMIRCPSGSSDELGSS
Protein: ATP synthase subunit epsilon, mitochondrial, putative (EC 3.6.3.14) (Q8IBU5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- ATP synthase subunit O, mitochondrial, putative
- ATP synthase subunit alpha
- ATP synthase subunit delta, mitochondrial, putative
- ATP synthase subunit gamma
- ATP synthase subunit beta
- ATP synthase subunit C, putative
- JmjC domain-containing protein, putative
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase 21 kDa proteolipid subunit, putative
- Cytochrome b-c1 complex subunit 6
Sequence:
MWKAANVSYTRYASEMADILRKCLKDPYSDIALERSKMHIRETIYKDGKPVSQELYEEFEKAYKNLSRQKE
Protein: ABC transporter, periplasmic substrate-binding protein, putative (Q5LT62)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Interaction partners:
- Branched-chain amino acid ABC transporter, periplasmic branched-chain amino acid binding protein
- Branched-chain amino acid ABC transporter, periplasmic substrate-binding protein
- Branched-chain amino acid ABC transporter, periplasmic branched-chain amino acid-binding protein
- Branched-chain amino acid ABC transporter, periplasmic substrate-binding protein
- Branched-chain amino acid ABC transporter, periplasmic substrate-binding protein
- Branched-chain amino acid ABC transporter, periplasmic branched-chain amino acid-binding protein, putative
- Branched-chain amino acid ABC transporter, periplasmic branched-chain amino acid binding protein, putative
- Branched-chain amino acid ABC transporter, periplasmic substrate-binding protein
- Trimethylamine monooxygenase
- Transcriptional regulator, GntR family
Sequence:
MTLPGGVVEIGMLSSSFAHRMAVTSLFPQDRVGMSDPIKIGFLAPLTGPVSSWGLPGLHGCRLWEDWLNRAGGILVGGRRYPVSIVPFDCGYDPERAMEGARHLVHTEQVKLLMMLGGDTFTPLRGFLTANKVLTSTLLPSDLSPDTRYLIAPSEVHPIYNVTGVDWLARNRPELRRVAMCSQKDALGLPSIATYRAAFEAAGVPVVKEVEYDPEMTDVATIVQPMLDAQPDVLCWCTSYTPMVHAMTEYAHAKGFSGQILSCTLDNYQRLVARTSAEFMEGALFQFPDFDDPKLARKAFFFNRPSTFFKEYNARYPGNWSAVSWEYVAILDIWHAAVEKVASVHPVSVLATMKQMDPVTHAFGPARWWGESIFGIDHALVGDWPVVRIQEGKARIVEFGSIPAWLDKHEDMLRRHMQAAGQMWQQRLETGEAQTGLTTRDLVD
Protein: Terpene synthase 10 (RcSeTPS10) (EC 4.2.3.-) (B9T536)
Organism: Ricinus communis (Castor bean)
Function: Catalyzes the cyclization of farnesyl diphosphate to sesquiterpene olefins.
Interaction partners:
Sequence:
MTDPIMSNETIIRRSANYRPPIWDFDFVQSLKSEFVGELNIKRIDKLKEDVKMMLNKTMAPSDQFELIDTLQRLGLAYHFGDEIKRIVKSIYNSHRNDNTWMKEDLHTIALQFRLLRQHGYNISQEIFDIFRDELGNFKECLHEDIEGMLSLYEASYLLEEGENILEVAREFAASCLKKYIQVNKDQLLSMIVSHSLEVPLHWRMPRLETRWFIDIYEKKQGMNPLLLELAKLDFNNVQATYHEDLKYVTSWWRNTGLGEKLSFARDRLMENFLWTVGVNFPPQFGYFRRISTKVNSLITVIDDIYDVYGTLDELQLFTNAVERWDVNAMDQLPEYMKLCFLALHNSINEMAYDALREQGFHIIPYLKKAWADLCKSYLVEAKWYYIGYTPTLQEYMDNAWISISAPVILVHAYFLEGSPITNEALKSLKEYPDIIQWSSMILRFADDLGTSSDELKRGDNPKSIQCYIYETGVSELKAREHIQYLIGETWKKINKEREYIDSPFSKIFIEVATNLARMAQCMYQHGDGHGIEDGETKDHVLSLLVKPIPM
Protein: Interferon lambda-3 (IFN-lambda-3) (Cytokine Zcyto22) (Interleukin-28B) (IL-28B) (Interleukin-28C) (IL-28C) (Q8IZI9)
Organism: Homo sapiens (Human)
Function: Cytokine with antiviral, antitumour and immunomodulatory activities. Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN-stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type-selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression.
Subcellular location: Secreted {ECO:0000269|PubMed:12483210}.
Interaction partners:
- Interferon lambda receptor 1
- Interleukin-10 receptor subunit beta
- Interferon lambda-2
- Interferon lambda-1
- Interferon alpha/beta receptor 1
- Interleukin-10 receptor subunit alpha
- Interleukin-22 receptor subunit alpha-2
- Interleukin-20 receptor subunit alpha
- Interleukin-22 receptor subunit alpha-1
- Interleukin-20 receptor subunit beta
Sequence:
MTGDCMPVLVLMAAVLTVTGAVPVARLRGALPDARGCHIAQFKSLSPQELQAFKRAKDALEESLLLKDCKCRSRLFPRTWDLRQLQVRERPVALEAELALTLKVLEATADTDPALGDVLDQPLHTLHHILSQLRACIQPQPTAGPRTRGRLHHWLHRLQEAPKKESPGCLEASVTFNLFRLLTRDLNCVASGDLCV
Protein: Mastermind-like domain-containing protein 1 (P0C6A2)
Organism: Mus musculus (Mouse)
Function: Transactivates the HES3 promoter independently of NOTCH proteins. HES3 is a non-canonical NOTCH target gene which lacks binding sites for RBPJ (By similarity). Required for testosterone production.
Subcellular location: Nucleus {ECO:0000250}. Note=Punctate nuclear localization. {ECO:0000250}.
Interaction partners:
- Protein FAM118B
- Mastermind like transcriptional coactivator 2
- Mastermind-like protein 1
Sequence:
MDDWKSRLVIENMLPHFNMVGNRQETRKLQESGTSKRRQEGENFHFTGMADGSYPNKIKRPCLEDVTLSMGPGAHPTSLSTEMQMPTLNMNPTSADLGVAGQSLLLENNPLDSNVVNSSAMGSPFGVPSTADTGLKGHAVPYYEKNNSMPAVDQELQDLLEELTKIQEPSSNDLDLEKILGSKPEEPLVLHNPQAPLGPPAKLPVQMPHMESLGSSKEFASSCSQVAGTSLPIMPSSTGMSYSIPSSSKQIVSSSSSTAQAQVKNQVQNMLPVTMPPLSVPQWHHAHQLKALAASKQGSATKQGSNRNWSSLPPPGLSPPYLPVPSPHPPPPQPPPPPFSPQNFTASCMSSSSLSGSAVQSSPNALLSSMAPSSNASLGPTLPYVPAKLPGLPLNQQPQFSPQSSILANLVSSSVKSPQGHLISALPTSTPGPSPPYRPENLSSPGLPQQSFTPQYSLIRSLTPTSNLLSQQQQQQQQQQQQQQQQQQQQQQQQHQANSIFKPMTSSQQPKTLSMIMQQGLSSSSPEAPEPFTFSNTKPLSHFVSEPSPQKMASMSTHSRQSSLLHYLPQATPAHAPSATASSTATATLQLQHHHQQHHHQQHHHQQQHHQQQHHQQHHHQQQQHQQQQHQQQQQQQPDQSSFLLQQIMQQPQRFQRMMASDSMPALPGQGCCHRCAWTSTALWLEHQHQQWNSLTSTHGHVPPSNLTHVDKACKLGEARPPHVSLGRQPPSRQALGSESFLPGSSFAHELARVTSTSSYNTSEAAPWGGWDPKAWRQVPAPLLPSCDAAAREAEIRSYGNDP
Protein: Meiotic recombination protein rec8 (Cohesin rec8) (P36626)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved primarily in the early steps of meiotic recombination. Required to ensure reductional chromosome segregation.
Subcellular location: Nucleus {ECO:0000269|PubMed:10207075, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:31665745}. Chromosome {ECO:0000269|PubMed:31665745}. Note=Localizes to meiotic chromosomal axis sites. {ECO:0000269|PubMed:31665745}.
Interaction partners:
- Meiotic recombination protein rec11
- Structural maintenance of chromosomes protein 3
- Separin
- Structural maintenance of chromosomes protein 1
- Cohesin subunit psc3
- Shugoshin-1
- Sister chromatid cohesion protein pds5
- Serine/threonine-protein kinase plo1
- Cohesin subunit rad21
- Meiotic recombination protein rec12
Sequence:
MFYNQDVLTKEKGGMGVIWLAATLGSKHSLRKLHKKDIMSVDIDEACDFVAFSPEPLALRLSSNLMIGVTRVWAHQYSFFHSQVSTLHLRVRKELDHFTSKPFKNIDIQNEQTNPKQLLLAEDPAFIPEVSLYDAFNLPSVDLHVDMSSFTQPKENPNISVLETLPDSTSYLINTSQNYSLRNNVSSFVYEDSRAFSTEEPLDFEFDENGDIQELTKGTINSDPSLQAASQHSNLGSVQREYNSEEQESRIHMFEIDEDVLPLPVPLQSVMDSEHNENEPRALKRRKVQKLLEPDENIELSTRTLSQWRKNYVERMIALEATKYVRRRGASSAKKKELNKFFDWESFHPLLKPWIEKLKPSNNTPSEIDDVLRNIDTSEVEVGRDVQGELGLNIPWNTSSRSNSAINSKSHSQTGSEHSTPLLDTKYRKRLPHSPSMPSRVEFLPALESSQFHETLNSELSLQLSDDFVLYKNTQEENAHLMLSMEKECANFYEYAKTAIYENNGRITFSSLLPNDLKRPVVAQAFSHLLSLATKSAFLVKQDKPYSEISVSLNLKSTDAI
Protein: Succinate dehydrogenase assembly factor 2, mitochondrial (SDH assembly factor 2) (SDHAF2) (Q584Q5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion matrix {ECO:0000256|HAMAP-Rule:MF_03057}.
Interaction partners:
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- fumarate reductase
- fumarate reductase
- fumarate reductase
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MLRRLFTRMAPRAKNHEELMKMLREGSQVGKMAASEESGVTFRDIRTVPIGESNEAKRRRLLYQSTYRGMVEMDIILGAFARQNIETLSAPQLEEYDAVLRHFDNDLYKWLVMDVEAPAEVAQIPVFQSLHSFVRDEREKLLKCAS
Protein: GM05855p (Q5BHZ5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSQMGGTCLYDEPEIMEEFISCYQYFTALWDSSSPDYLSKQKKEPGYQELLKILRRVNSNCSIQDVKRKINSLRCCYRREFKKVQESVNGYQTRLWWFHLMDFLKPVLNIQSPARVKSENVDDSLDETSIQDVDIMSDAFPHEEDMLRLDAVGDGDVEPEPEPDNDPELDNMDDHVDDYRNNSSAGCIKNNGYQQHTVSSHQQHNGESQTSDKSGRRIRNRRRRSSNDTDYVEAARKRRNVETSNRDRDWHRERDRERDRKHESDSEYECELIGKRMASHFRRMRPDQRLFAERIISEVLVYGRMNRLSFETQFSMGHK
Protein: Lysine 6-dehydrogenase (EC 1.4.1.18) (L-lysine 6-dehydrogenase) (L-lysine epsilon-dehydrogenase) (Q9AJC6)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: Catalyzes the oxidative deamination of L-lysine in the presence of NAD. Can also use (S)-(2-aminoethyl)-L-cysteine as a substrate, but more slowly. Can use both NAD and NADP but the preferred substrate is NAD.
Interaction partners:
Sequence:
MKVLVLGAGLMGKEAARDLVQSQDVEAVTLADVDLAKAEQTVRQLHSKKLAAVRVDAGDPQQLAAAMKGHDVVVNALFYQFNETVAKTAIETGVHSVDLGGHIGHITDRVLELHERAQAAGVTIIPDLGVAPGMINILSGYGASQLDEVESILLYVGGIPVRPEPPLEYNHVFSLEGLLDHYTDPALIIRNGQKQEVPSLSEVEPIYFDRFGPLEAFHTSGGTSTLSRSFPNLKRLEYKTIRYRGHAEKCKLLVDLTLTRHDVEVEINGCRVKPRDVLLSVLKPLLDLKGKDDVVLLRVIVGGRKDGKETVLEYETVTFNDRENKVTAMARTTAYTISAVAQLIGRGVITKRGVYPPEQIVPGDVYMDEMKKRGVLISEKRTVHS