wanglab/gogpt-training-data huggingface dataset:
Protein: Probable transcription factor At5g28040 (Storekeeper-like protein At5g28040) (F4K5T4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Acyl-CoA N-acyltransferases
- Cysteine synthase 1
- Bifunctional cystathionine gamma-lyase/cysteine synthase
Sequence:
MASDQRDTDFSAESPDLEEDGGGGGGGRGGGETESDEDVVIPEPNEAEDDDHDPDPDPEYEDLNSPSMISRAPATKSSSGTVTVALPAGSAVPVASIPSDSDQKWHRMTEIVHQRPPIDDSRRLFQRLWTDEDEIELLRGFLDYITNHRGNSSHPPDTAPFYEQIKSKLQLEFNKNQLVEKLRRLKKKYRNVMSKFSSGKEVFFKSPHDQATFDISRKIWNQTGKIIGFEDNNVMDLEETNHVNNANGSSGFNVSVIGNANVDVDSENGLEKKVTISRKRSRSRIGKIDEDKPVLAPCDGVIPNAVNLNENVAVGCDFGDGRNLGVLIEETVKNCVSPMIKEMMNSTTGMMMAATGGFPGGGAHALGVLSPMLMPSMNLGFGGKGVGDERWRRQQILELEVYSRRLELVQEQIRATVNELKTMPNGG
Protein: Transcription factor E2-alpha (Class B basic helix-loop-helix protein 21) (bHLHb21) (Immunoglobulin enhancer-binding factor E12/E47) (Immunoglobulin transcription factor 1) (Kappa-E2-binding factor) (Transcription factor 3) (TCF-3) (Transcription factor ITF-1) (P15923)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator involved in the initiation of neuronal differentiation and mesenchymal to epithelial transition (By similarity). Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation (By similarity). Together with TCF15, required for the mesenchymal to epithelial transition (By similarity). Dimers bind DNA on E-box motifs: 5'-CANNTG-3' (By similarity). Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer. Binds to IEB1 and IEB2, which are short DNA sequences in the insulin gene transcription control region (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:31696227}.
Interaction partners:
- T-cell acute lymphocytic leukemia protein 1
- LIM domain-binding protein 1
- Rhombotin-2
- Protein lyl-1
- Erythroid transcription factor
- Myoblast determination protein 1
- LIM domain-binding protein 2
- DNA-binding protein inhibitor ID-2
- Runt-related transcription factor 1
- DNA-binding protein inhibitor ID-1
Sequence:
MNQPQRMAPVGTDKELSDLLDFSMMFPLPVTNGKGRPASLAGAQFGGSGLEDRPSSGSWGSGDQSSSSFDPSRTFSEGTHFTESHSSLSSSTFLGPGLGGKSGERGAYASFGRDAGVGGLTQAGFLSGELALNSPGPLSPSGMKGTSQYYPSYSGSSRRRAADGSLDTQPKKVRKVPPGLPSSVYPPSSGEDYGRDATAYPSAKTPSSTYPAPFYVADGSLHPSAELWSPPGQAGFGPMLGGGSSPLPLPPGSGPVGSSGSSSTFGGLHQHERMGYQLHGAEVNGGLPSASSFSSAPGATYGGVSSHTPPVSGADSLLGSRGTTAGSSGDALGKALASIYSPDHSSNNFSSSPSTPVGSPQGLAGTSQWPRAGAPGALSPSYDGGLHGLQSKIEDHLDEAIHVLRSHAVGTAGDMHTLLPGHGALASGFTGPMSLGGRHAGLVGGSHPEDGLAGSTSLMHNHAALPSQPGTLPDLSRPPDSYSGLGRAGATAAASEIKREEKEDEENTSAADHSEEEKKELKAPRARTSPDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLNSEKPQTKLLILHQAVSVILNLEQQVRERNLNPKAACLKRREEEKVSGVVGDPQMVLSAPHPGLSEAHNPAGHM
Protein: Multifunctional methyltransferase subunit TRM112 (Q57X98)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Methyltransferase small domain-containing protein
- Uncharacterized protein
- Fe2OG dioxygenase domain-containing protein
- Methyltransferase, putative
- peptide chain release factor N
- Methyltransferase type 11 domain-containing protein
- Eukaryotic peptide chain release factor subunit 1
- Uncharacterized protein
- tRNA
- 50S ribosomal protein L7Ae, putative
Sequence:
MRLLTHNFLCCIQCQSFPLQLQATELEVLASEYNPEFIRTMLARMDYTYLVEAFNSLRSQKQDQVDAGNVLPEKLEDVDLSDDSRDLKAVHYAIQDVAIREGALRCPQCKREYPIREFIPDMIAAEH
Protein: Nuclear factor of activated T-cells 3 (A0A8I6AB55)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTTANCGAHDELDFKLVFGEDGAPTPVSQVSRPADLEPDDCASIYIFNVDPPPSTLNSSLGLPHHGLLQSHSSVLSPSFQLQGFKNYEGTDDISESKYSSLSGPKPFECPSIQITSISPNCHQETDAHEDDLHVNDPEREYLERPSRDHLYLPLEPSYRESSLSPSPASSVSSRSWFSDASSCESLSHIYDDVDSELNEAAARFTLGSPLTSPGGSPGGCPGEESWHQQYGPGHSLSPRQSPCHSPRSSITDENWLSPRPASGPSSRPTSPCGKRRHSSAEVCYAGSLSPHHSPVPSPGHSPRGSVTEDTWLTAPVHTGSGLSPAPFPFQYCVETDIPLKTRKTSDDQAAILPGKLEVCSDDQGSLSPSRETSVDDGLGSQYPLKKDSSGDQFLSVPSPFTWSKPKPGHTPIFRTSSLPPLDWPLPTHFGQCELKIEVQPKTHHRAHYETEGSRGAVKASTGGHPVVKLLGYSEKPINLQMFIGTADDRYLRPHAFYQVHRITGKTVATASQEIIIASTKVLEIPLLPENNMSASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGKVLSLQIASIPVECSQRSAQELPHIEKYSINSCSVNGGHEMIVTGSNFLPESKIIFLEKGQDGRPHWEAEGKIIREKCQGGHIVLEVPPYHNPAVTSAVQVHFYLCNGKRKKSQSQRFTYTPVLMKQEQREDTDLSSVPSLPVPHSAQTQRPSSDTGHPHDSALSAPRSLICPVQPAYASMITSTHLPQLQCRDEGAGKEQHIIPSSVMHQPFQVTPTSPMGSSYQSIQTNMYNGPTCLPMNPASSQEFDPVLFQQDAALSNLVNLGCQPLSPIPFHSSNSDATGHLLAHSPHSVQTPPHLQSMGYHCSSAGQRSLSSPVAAQVTGQPSSHLQPITYCPSHPGSATAASPAASHALSSSPISGPPSPQLQSMPYQSPSSGTASSPSPVTRMHSGQHSTQAQSTGQGGLSVPSSLVCHSLCDPASFPPGGAAVSIKPEPEDQEPNFATIGLQDITLDDGGTVGNQKGELSQRNSK
Protein: Ring finger protein 6 isoform 2 (A0A0S2Z4G9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNQSRSRSDGGSEETLPQDHNHHENERRWQQERLHREEAYYQFINELNDEDYRLMRDHNLLGTPGEITSEELQQRLDGVKEQLASQPDLRDGTNYRDSEVPRESSHEDSLLEWLNTFRRTGNATRSGQNGNQTWRAACVKNNSRRRRRIQQILNCCTTTSNNHTGPSSEKDPSWRK
Protein: Ypt/Rab-GAP domain of gyp1p superfamily protein (Q0WV47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MWGAAAEPADSYYLIRPECTDVPNTKFKIKPGKTLSVRKWQAAFTTEGFLDIGKTLSRIQRGGIHPSIRGEVWEFLLGCYDPKSTFEEREQIRQRRRLQYASWKEECKQMFPVIGSGGFITAPVITNKGEPIYDPIVLQETNLGANGSDFFKDLASRGPLDQKVIQWLLTLHQIGLDVNRTDRTLVFYEKKENLSKLWDILALYAWIDNDVGYCQGMSDLCSPMIMLLEDEADAFWCFERLMRRLRGNFRDTGRSVGVEAQLTHLASITQIIDPKLHHHLEKLGGGDYLFAIRMIMVQFRREFSFCDSLYLWEMMWALEYDPEMYSLYEEPQFEGERIEGSSKGKPKSINQCGKYERENMKNGGKSAEGPLPISVFLVASVLKDKSSKLMTEARGLDDVVKILNDITGNLDAKKACTGAMKLHKKYLKKAKK
Protein: High-affinity gluconate transporter ght3 (Hexose transporter 3) (Q92339)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: High-affinity gluconate transporter.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- SNF1-like protein kinase ssp2
Sequence:
MNRFITSILVVFISMSGWLQGADTGSISGILGMRDFQSRFADRYNPISNSYSYSAWRQALLTGTINAGCLFGAMLSSPFTERIGKKYSICFFSGVYIIAELLLVTAVPSWIQVLVGKILAGVGIGALSVLSPGYQSEVAPPQIRGAVVATYQIFSTGAALVAACINMGTHKLRKTASWRTSFGINMLWGILLMVGVLFLPESPRYLIYKGRDEEALRIMCNMAELSPESEIIQTNFNTIKSDIEIEMAGGKARWIEIFGKDIRYRTCLGFLVMLFRELIGNNYYFYYATQVFKGTGMTDIFLPAVILGAINFGTTFGALYTIDNLGRRNPLIFGAAFQSICFFIYAAVGDRKLIYKNGTSDHRAGSVMIVFSCLFLFSYCCSWGPMGWVIVGETFPIRYRSKCASVATSGNWLGNFMISFFTPFINNAIGFKLGYIYACINLFSSFMIFFLAKETKGLTLEEVNDLYMSNIKPWESYKYVREIESHRIHFSKEEEKREREKSKGIRGQEEEFIENADEDNNDSSSSSGSVVSAVKPRRSAVSNDRFSEDSHPTYI
Protein: UDP-glucuronate decarboxylase (EC 4.1.1.35) (G5EF65)
Organism: Caenorhabditis elegans
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004447}.
Interaction partners:
- UDP-glucose 6-dehydrogenase
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase sqv-8
- Xylosylprotein 4-beta-galactosyltransferase
- UDP-sugar transporter sqv-7
- Chondroitin sulfate synthase sqv-5
- Ubiquitin-like domain-containing protein
- Xylosyltransferase sqv-6
- Beta-1,3-galactosyltransferase sqv-2
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Fatty acid synthase
Sequence:
MLSPRRIRNNSISMATRGACAVLITFFLIFVLITNTSNKSLSSDVIEKSEQKISQMEEEGRGDTIVEFNKNNIPDDTVSSLLERIKLLEDELSSMRTRMDDAENREGNAANGDEIVAPLPTTKSFPSVRYRNEETRKRILITGGAGFVGSHLVDKLMLDGHEVIALDNYFTGRKKNVEHWIGHPNFEMVHHDVVNPYFVEVDQIYHLASPASPPHYMYNPVKTIKTNTLGTINMLGLAKRVKATVLLASTSEVYGDPEVHPQPETYWGHVNTIGPRACYDEGKRVAESLMVAYNKQENIKIRIARIFNTFGPRMHMNDGRVVSNFIIQALQDKPITIYGNGTQTRSFQYVTDLVDGLIKLMNSNYSLPVNIGNPEEHTIGQFATIIRDLVPGSTSEIVNLESQQDDPQQRRPDIRRAAEQISWAPQVHMKDGLLKTVDYFRAEIDRNKRGGKPVPEPVRLAGLESRR
Protein: Monocarboxylate transporter 4 (MCT 4) (Monocarboxylate transporter 3) (MCT 3) (Solute carrier family 16 member 3) (O35910)
Organism: Rattus norvegicus (Rat)
Function: Proton-dependent transporter of monocarboxylates such as L-lactate and pyruvate (By similarity). Plays a predominant role in the L-lactate efflux from highly glycolytic cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O15427}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15427}. Basolateral cell membrane {ECO:0000250|UniProtKB:O15427}; Multi-pass membrane protein {ECO:0000255}. Note=Plasma membrane localization is dependent upon the BSG/MCT4 interaction. Basolateral sorting signals (BLSS) in C-terminal cytoplasmic tail ensure its basolateral expression in polarised epithelial cells. {ECO:0000250|UniProtKB:O15427}.
Interaction partners:
- Basigin
- L-lactate dehydrogenase A chain
- Embigin
- Carbonic anhydrase
- Malignant T-cell-amplified sequence 1
- Solute carrier family 2, facilitated glucose transporter member 3
- Pyruvate kinase PKM
- L-lactate dehydrogenase B chain
Sequence:
MGGAVVDEGPTGIKAPDGGWGWAVLFGCFIITGFSYAFPKAVSVFFKELMHEFGIGYSDTAWISSILLAMLYGTGPLCSMCVNRFGCRPVMLVGGLFASLGMVAASFCRSIIQIYLTTGVITGLGLALNFQPSLIMLNRYFNKRRPMANGLAAAGSPVFLCALSPLGQLLQDHYGWRGGFLILGGLLLNCCVCAALMRPLVAPQASGGAEPHGPQRPSPRLLDLSVFRDRGFLIYAVAASIMVLGLFVPPVFVVSYAKDMGVPDTKAAFLLTILGFIDIFARPTAGFITGLKKVRPYSVYLFSFAMFFNGFTDLTGSTASDYGGLVVFCIFFGISYGMVGALQFEVLMAIVGTQKFSSAIGLVLLLEAVAVLIGPPSGGKLLDATKVYKYVFILAGAEVLTSSLVLLLGNFFCIGKRKRPEVTKPEEVASEEEKLHKPPVDVRVDSREVEHFLKAEPEKNGEVVHTPETSV
Protein: Cytochrome P450 710A2 (EC 1.14.19.41) (C-22 sterol desaturase) (O64698)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required to form the C-22 double bond in the sterol side chain. Possesses in vitro C-22 desaturase activity toward 24-epi-campesterol and beta-sitosterol and produces brassicasterol and stigmasterol, respectively. No activity with campesterol.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Delta
- Cycloeucalenol cycloisomerase
- 24-methylenesterol C-methyltransferase 2
- Delta
- Methylsterol monooxygenase 2-1
- Methylsterol monooxygenase 2-2
- Lanosterol synthase
- Cycloartenol synthase
- Cycloartenol-C-24-methyltransferase
- Delta
Sequence:
MVFSVSIFASLAPYLVSALLLFFLIEQLSYLVKKRNLPGPLFVPPIIGNAISLVRDPTSFWFKQSDTAGTSPGLAANYLIGKFIIYIRDTELSHQIFSNVRLEAFHPLGHPFGKQLFGDHSLIYLFGEDHKTVRRHLAPNFTPKALSTYSDLQQIVMLRHLRQWEESFSGGTKPVSMRDLVRELNLETSQTVFVGPYLDKEARNTFCTDYNLFNLGSMALPINLPGFAFNKARRAVMNLEKTLSVCAGKSKKRMATGEEPTCLIDFWMHAFVTEIESGNPPPLHSEDEAIGGLLFDFLFAAQDASTSSLLWAVTFLESHPKVLSKVREEVAKIWSPQSGHLITADQLAEMKYTRAVAREVVRYRPPATMVPHIATNDFPLTESYTIPKGTIVFPSVFDASFQGFTEPNRFDPDRFSETRQEDQVFKRNYLAFGWGAHQCVGQRYALNHLVLFIAMFSSLFDFKRLQSDGCDDIIYCPTISPKDGCTVFLSKRIVTYPNL
Protein: Insulin-like peptide INSL5 (Insulin-like peptide 5) [Cleaved into: Insulin-like peptide INSL5 B chain; Insulin-like peptide INSL5 A chain] (Q9Y5Q6)
Organism: Homo sapiens (Human)
Function: May have a role in gut contractility or in thymic development and regulation. Activates RXFP4 with high potency and appears to be the endogenous ligand for this receptor.
Subcellular location: Secreted.
Interaction partners:
- Relaxin-3
- Relaxin-3 receptor 2
- Prorelaxin H1
- Prorelaxin H2
- Insulin-like 3
- Relaxin-3 receptor 1
- Relaxin receptor 1
- Relaxin receptor 2
- Insulin-like peptide INSL6
Sequence:
MKGSIFTLFLFSVLFAISEVRSKESVRLCGLEYIRTVIYICASSRWRRHQEGIPQAQQAETGNSFQLPHKREFSEENPAQNLPKVDASGEDRLWGGQMPTEELWKSKKHSVMSRQDLQTLCCTDGCSMTDLSALC
Protein: Hemoglobin alpha, adult chain 2 (A0A8L2QLW7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MVLSADDKTNIKNCWGKIGGHGGEYGEEALQRMFAAFPTTKTYFSHIDVSPGSAQVKAHGKKVADALAKAADHVEDLPGALSTLSDLHAHKLRVDPVNFKAHGKKVADALAKAADHVEDLPGALSTLSDLHAHKLRVDPVNFKFLSHCLLVTLACHHPGDFTPAMHASLDKFLASVSTVLTSKYR
Protein: Bcl-2-like protein BUFFY (Q9NGX3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
RFPSGSRTISVARNMPGTSYPTNNDNFSNGFPMATTQSERLLQAQNRRKFSFPATLHSASLLEVGGGPKETTRRRLSNVSDAVTRKLSYTIGWKAAQIPAQDIISQGRCLCGHYIKRRLRRSGLFNKKLGLQRIRSILGSTSMGIVRDVFPAVQVLGDELERMHPRIYNGVARQICRNPGGEFHTPDAVSLLLGAVGRELFRVEITWSKVISLFAIAGGLSVDCVRQGHPEYLPKLMESVSEVIEDELVPWINENGGWSGINTHVLPTTNSLNPLEWTTLVIGVVFGLILVFMILRFIFNLIVPKIYQRFTNS
Protein: Dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) (DHOdehase) (DHOD) (DHODase) (Dihydroorotate oxidase) (P9WHL1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Dihydroorotase
- Orotate phosphoribosyltransferase
- Possible oxygenase
- Aspartate carbamoyltransferase catalytic subunit
- nitric oxide dioxygenase
- Carbamoyl phosphate synthase large chain
- Orotidine 5'-phosphate decarboxylase
- Carbamoyl phosphate synthase small chain
- Possible conserved secreted protein
- Bifunctional protein PyrR
Sequence:
MYPLVRRLLFLIPPEHAHKLVFAVLRGVAAVAPVRRLLRRLLGPTDPVLASTVFGVRFPAPLGLAAGFDKDGTALSSWGAMGFGYAEIGTVTAHPQPGNPAPRLFRLADDRALLNRMGFNNHGARALAIRLARHRPEIPIGVNIGKTKKTPAGDAVNDYRASARMVGPLASYLVVNVSSPNTPGLRDLQAVESLRPILSAVRAETSTPVLVKIAPDLSDSDLDDIADLAVELDLAGIVATNTTVSRDGLTTPGVDRLGPGGISGPPLAQRAVQVLRRLYDRVGDRLALISVGGIETADDAWERITAGASLLQGYTGFIYGGERWAKDIHEGIARRLHDGGFGSLHEAVGSARRRQPS
Protein: RT01008p (TBP-related factor 4) (Q9VQE6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- B-related factor 1
- Transcription initiation factor IIB
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 7
- General transcription factor IIF subunit 2
- B double prime 1, isoform A
- Transcription initiation factor IIA subunit 1
- Zinc finger CCHC domain-containing protein 8 homolog
Sequence:
MDSVIKRFKALNHGDDYEENDARFDGVKLKEGTSAKLSSLDKLFEELKISKESSAKEDLVTEPMKTESYLYKDYFNKSPIDFPWEKAYEKGSSLGPDFYIDYENIFDNVANLAEIEEKLELHFRPFTCVMDFNCRFSMYELCLLLAESRFDPSSHPSVVVKITHPSAQVKIHAGGKISSTALNADSARSGLFKVIRILQDLDYKVDIMNFSKNIVNASFSMPFKIDLDLMSRRHVVEVAQNRSRRPFITYTTENLGVRFAVFPTGFVLVLHSTSHCETREAIANFLPILAKLKNGYPTAEEKLGQLVGDISYKLFWEKQLEDDKEGMLLYS
Protein: Small ribosomal subunit protein eS12z (40S ribosomal protein S12-1) (Q9S9P1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein uS2z
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein uS12y
- Small ribosomal subunit protein eS1z
- Small ribosomal subunit protein eS28x
- Small ribosomal subunit protein eS1y
- Small ribosomal subunit protein eS21y
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein uS12z
Sequence:
MSGDEAAPVVVPPPVAEPAAIPEDMDLMTALELTLRKARAYGGVVRGLHECAKLIEKRVAQLVVLAEDCNQPDYVKLVKALCADHEVRLLTVPSAKTLGEWAGLCKIDSEGNARKVVGCSCLVVKDFGEETTALSIVNKHIASQ
Protein: Shikimate dehydrogenase (NADP(+)) (SDH) (EC 1.1.1.25) (Q56S04)
Organism: Helicobacter pylori (Campylobacter pylori)
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). It can also use NAD to oxidize shikimate.
Interaction partners:
Sequence:
MKLKSFGVFGNPIKHSKSPLIHNACFLTFQKELGFLGHYHPILLPLESHIKSEFLHLGLSGANVTLPFKERAFQICDKIKGIALECGAVNTLVVENDELVGYNTDALGFWLSLGGEGYQSALILGSGGSAKALACELQKQGLKVSVLNRSARGLDFFQRLGCDCFMDPPKSTFDLIINATSASLNNELPLNKEVLKGYFKEGKLAYDLAYGFLTPFLSLAKELETPFQDGKDMLIYQAALSFEKFSASQIPYPKAFEVMRSVF
Protein: ECF RNA polymerase sigma-E factor (RNA polymerase sigma-E factor) (D0ZSY9)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment.
Subcellular location: Cytoplasm {ECO:0000305}. Note=Associates with the inner membrane via RseA. {ECO:0000305}.
Interaction partners:
Sequence:
MSEQLTDQVLVERVQKGDQKAFNLLVVRYQHKVASLVSRYVPSGDVPDVVQESFIKAYRALDSFRGDSAFYTWLYRIAVNTAKNYLVAQGRRPPSSDVDAIEAENFESGGALKEISNPENLMLSEELRQIVFRTIESLPEDLRMAITLRELDGLSYEEIAAIMDCPVGTVRSRIFRAREAIDNKVQPLIRR
Protein: Con-ikot-ikot (CII) (P0CB20)
Organism: Conus striatus (Striated cone)
Function: Potently and selectively blocks the desensitization of ionotropic glutamate AMPA receptor (GRIA1, GRIA2, GRIA3 and GRIA4). Can also open already desensitized GRIA1 receptors. Binds to a different site than does the drug cyclothiazide. The toxin acts like a straightjacket on the ligand-binding domain (LBD) 'gating ring' of the receptor, restraining the domains via both intra- and interdimer cross-links such that agonist-induced closure of the LBD 'clamshells' is transduced into an irislike expansion of the gating ring. Application of the toxin to hippocampal slices causes a large and rapid increase in resting AMPAR-mediated current leading to neuronal death.
Subcellular location: Secreted {ECO:0000269|PubMed:19481459}.
Interaction partners:
Sequence:
MAMNMSMTLCMFVMVVVAATVIDSTQLQEPDLSRMRRSGPADCCRMKECCTDRVNECLQRYSGREDKFVSFCYQEATVTCGSFNEIVGCCYGYQMCMIRVVKPNSLSGAHEACKTVSCGNPCA
Protein: SHATTERPROOF2 (Q5XXE7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEGGASNEVAESSKKIGRGKIEIKRIENTTNRQVTFCKRRNGLLKKAYELSVLCDAEVALVIFSTRGRLYEYANNSVRGTIERYKKACSDAVNPPTITEANTQYYQQEASKLRRQIRDIQNLNRHILGESLGSLNFKELKNLESRLEKGISRVRSKKHEMLVAEIEYMQKREIELQNDNMYLRSKITERTGLQQQESSVIHQGTAYESGVTSSHQSGQYNRNYIAVNLLEPNQNSSNQDQPPLQLV
Protein: RE05272p (Stardust, isoform F (EC 2.7.4.8)) (Q6NR03)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLTMLSVNQDNGPHREMAVDCPDTFIARNKTPPRYPPPRPPQLNGNAKPVPPPRDHLRVEKDGRLVNCSPAPQLPDRRAPGNASSGSSGATTHPLQHQQIAQIVEPTLEQLDSIKKYQEQLRRRREEEERIAQQNEFLRNSLRGSRKLKALQDTATPGKAVAQQQQQATLATQVVGVENEAYLPDEDQPQAEQIDGYGELIAALTRLQNQLSKSGLSTLAGRVSAAHSVLASASVAHVLAARTAVLQRRRSRVSGPLHHSSLGLQKDIVELLTQSNTAAAIELGNLLTSHEMEGLLLAHDRIANHTDGTPSPTPTPTPAIGAATGSTLSSPVAGPKRNLGMVVPPPVVPPPLAQRGAMPLPRGESPPPVPMPPLATMPMSMPVNLPMSACFGTLNDQNDNIRIIQIEKSTEPLGATVRNEGEAVVIGRIVRGGAAEKSGLLHEGDEILEVNGQELRGKTVNEVCALLGAMQGTLTFLIVPAGSPPSVGVMGGTTGSQLAGLGGAHRDTAVLHVRAHFDYDPEDDLYIPCRELGISFQKGDVLHVISREDPNWWQAYREGEEDQTLAGLIPSQSFQHQRETMKLAIAEEAGLARSRGKDGSGSKGATLLCARKGRKKKKKASSEAGYPLYATTAPDETDPEEILTYEEVALYYPRATHKRPIVLIGPPNIGRHELRQRLMADSERFSAAVPHTSRARREGEVPGVDYHFITRQAFEADILARRFVEHGEYEKAYYGTSLEAIRTVVASGKICVLNLHPQSLKLLRASDLKPYVVLVAPPSLDKLRQKKLRNGEPFKEEELKDIIATARDMEARWGHLFDMIIINNDTERAYHQLLAEINSLEREPQWVPAQWVHNNRDES
Protein: Phospholipid-transporting ATPase ID (EC 7.6.2.1) (ATPase class I type 8B member 2) (P4-ATPase flippase complex alpha subunit ATP8B2) (P98199)
Organism: Mus musculus (Mouse)
Function: Catalytic component of P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine (PC) from the outer to the inner leaflet of the plasma membrane. May contribute to the maintenance of membrane lipid asymmetry.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P98198}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P98198}; Multi-pass membrane protein {ECO:0000255}. Note=Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A or TMEM30B. {ECO:0000250|UniProtKB:P98198}.
Interaction partners:
- Cell cycle control protein 50A
- Cell cycle control protein 50B
- Cell cycle control protein 50C
- Phospholipid-transporting ATPase IH
- Phospholipid-transporting ATPase IB
- Phospholipid-transporting ATPase 11C
- Phospholipid-transporting ATPase IF
- Phospholipid-transporting ATPase IA
- Phospholipid-transporting ATPase VA
- Phospholipid-transporting ATPase VB
Sequence:
MTVPKEIPEKWARAGAPPSWSQKKPSWGTEEERRARANDREYNEKFQYASNCIKTSKYNIVTFLPVNLFEQFQEVANTYFLFLLILQLIPQISSLSWFTTIVPLVLVLTITAVKDATDDYFRHKSDNQVNNRHSQVLINGVLQQEQWMNVCVGDIIKLENNQFVAADLLLLSSSEPHGLCYIETAELDGETNMKVRQAIPVTSELGDVSQLARFDGEVICEPPNNKLDKFSGTLYWKENKFPLSNQNMLLRGCVLRNTEWCFGLVIFAGPDTKLMQNSGRTKFKRTSIDRLMNTLVLWIFGFLVCMGVILAIGNAIWEHEVGTRFQVYLPWDEAVDSAFFSGFLSFWSYIIILNTVVPISLYVSVEVIRLGHSYFINWDKKMFCMKKRTPAEARTTTLNEELGQVEYIFSDKTGTLTQNIMVFNKCSINGHSYGDVFDVLGHKAELGERPEPVDFSFNPLADKKFLFWDSSLLEAVKMGDPHTHEFFRLLSLCHTVMSEEKNEGELYYKAQSPDEGALVTAARNFGFVFRSRTPKTITVHELGTAITYQLLAILDFNNIRKRMSVIVRNPEGKIRLYCKGADTILLDRLHPPTQELLSSTTDHLNEYAGDGLRTLVLAYKDLDEEYYEEWARRRLQASLAQDSREDRLASIYEEVESDMMLLGATAIEDKLQQGVPETIALLTLANIKIWVLTGDKQETAVNIGYSCKMLTDDMTEVFVVTGHTVLEVREELRKARKKMVDSSHAVGNGFTYQGNLSSSKLTSVLEAVAGEYALVINGHSLAHALEADMELEFLETACACKAVICCRVTPLQKAQVVELVKKYKKAVTLAIGDGANDVSMIKTAHIGVGISGQEGIQAVLASDYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGVFDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMFFIPYGVFAEATRDDGTQLADYQSFAVTVATSLVIVVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSNGLFDMFPNQFRFVGNAQNTLAQPTVWLTIALTTAVCIMPVVAFRFLRLSLKPDLSDTVRYTQLVRKKQKAQHRCMRRVGRTGSRRSGYAFSHQEGFGELIMSGKNMRLSSLALSSFSTRSSSSWIESLRRKKSDSANSPSGGAEKPLKG
Protein: Hypoxia up-regulated protein 1 (150 kDa oxygen-regulated protein) (ORP-150) (170 kDa glucose-regulated protein) (GRP-170) (Heat shock protein family H member 4) (Q9Y4L1)
Organism: Homo sapiens (Human)
Function: Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding.
Subcellular location: Endoplasmic reticulum lumen.
Interaction partners:
- Endoplasmin
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase A4
- Nucleotide exchange factor SIL1
- DnaJ homolog subfamily B member 11
- DnaJ homolog subfamily C member 10
- Calreticulin
- DnaJ homolog subfamily B member 9
- Protein disulfide-isomerase A6
- X-box-binding protein 1
Sequence:
MADKVRRQRPRRRVCWALVAVLLADLLALSDTLAVMSVDLGSESMKVAIVKPGVPMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHVALYQARFPEHELTFDPQRQTVHFQISSQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAARMAGLKVLQLINDNTATALSYGVFRRKDINTTAQNIMFYDMGSGSTVCTIVTYQMVKTKEAGMQPQLQIRGVGFDRTLGGLEMELRLRERLAGLFNEQRKGQRAKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELGKNINADEAAAMGAVYQAAALSKAFKVKPFVVRDAVVYPILVEFTREVEEEPGIHSLKHNKRVLFSRMGPYPQRKVITFNRYSHDFNFHINYGDLGFLGPEDLRVFGSQNLTTVKLKGVGDSFKKYPDYESKGIKAHFNLDESGVLSLDRVESVFETLVEDSAEEESTLTKLGNTISSLFGGGTTPDAKENGTDTVQEEEESPAEGSKDEPGEQVELKEEAEAPVEDGSQPPPPEPKGDATPEGEKATEKENGDKSEAQKPSEKAEAGPEGVAPAPEGEKKQKPARKRRMVEEIGVELVVLDLPDLPEDKLAQSVQKLQDLTLRDLEKQEREKAANSLEAFIFETQDKLYQPEYQEVSTEEQREEISGKLSAASTWLEDEGVGATTVMLKEKLAELRKLCQGLFFRVEERKKWPERLSALDNLLNHSSMFLKGARLIPEMDQIFTEVEMTTLEKVINETWAWKNATLAEQAKLPATEKPVLLSKDIEAKMMALDREVQYLLNKAKFTKPRPRPKDKNGTRAEPPLNASASDQGEKVIPPAGQTEDAEPISEPEKVETGSEPGDTEPLELGGPGAEPEQKEQSTGQKRPLKNDEL
Protein: Coiled-coil domain-containing protein 25 (Q86WR0)
Organism: Homo sapiens (Human)
Function: Transmembrane receptor that senses neutrophil extracellular traps (NETs) and triggers the ILK-PARVB pathway to enhance cell motility. NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation. Formation of NETs is also associated with cancer metastasis, NET-DNA acting as a chemotactic factor to attract cancer cells. Specifically binds NETs on its extracellular region, in particular the 8-OHdG-enriched DNA present in NETs, and recruits ILK, initiating the ILK-PARVB cascade to induce cytoskeleton rearrangement and directional migration of cells. In the context of cancer, promotes cancer metastasis by sensing NETs and promoting migration of tumor cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:32528174}; Single-pass membrane protein {ECO:0000305|PubMed:32528174}. Endomembrane system {ECO:0000269|PubMed:32528174}. Note=Localizes to cytoplasmic membrane in tumor cells. {ECO:0000269|PubMed:32528174}.
Interaction partners:
Sequence:
MVFYFTSSSVNSSAYTIYMGKDKYENEDLIKHGWPEDIWFHVDKLSSAHVYLRLHKGENIEDIPKEVLMDCAHLVKANSIQGCKMNNVNVVYTPWSNLKKTADMDVGQIGFHRQKDVKIVTVEKKVNEILNRLEKTKVERFPDLAAEKECRDREERNEKKAQIQEMKKREKEEMKKKREMDELRSYSSLMKVENMSSNQDGNDSDEFM