wanglab/gogpt-training-data huggingface dataset:
Protein: GTPase activating protein, putative (Q38AJ6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MINNGLEADKPRTLKEFAETTGLKMEQAKKCFDGFGGYAPALASFAQSYTTLPDNFFEDKERAVKNAAVINAELKLIYKRAREIKERSGEGDKDVWGSYYKHLATLAPKQQEKQPPSAPPQPTEPPKSIFGFCSAAFPTQSPATVNFGFGEAPVNSTGSQTSGKPNFQGFGQAAKPVEKTNDKPRTEQVKYCKPKYFTGPFFDMPLFWEEEVEALCPLLNLNGGFLEENRGGLRGRLERWVTKASFYRQPVQYIEIDDEDEETVRVIIKDADRTFFHPDHRKKFVSFLNAMSHEFKAYGQAMSYLAGICLLVLNEEETAAVLRFVSKEYIPGHWAAEAVGFATSAWVVEHFMKRKFPDVAKHLEDLKFWPDTYLQKILTGLCVHVLSFKDLFVFLDLFIDGGINFLIKFCLAVVERFRSSILRVKSANDANTLYEIMRLDSKVTDSNDIKEILQRARLMELGDEELSIDVLRSKAFDEHVAPRLQRAPKTEAFEPCEVCNERKPKWWNEDIGAVCTECKEAAPGLTYTKY
Protein: Vesicle-associated membrane protein 2 (VAMP-2) (Synaptobrevin-2) (P63044)
Organism: Mus musculus (Mouse)
Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane. Major SNARE protein of synaptic vesicles which mediates fusion of synaptic vesicles to release neurotransmitters. Essential for fast vesicular exocytosis and activity-dependent neurotransmitter release as well as fast endocytosis that mediates rapid reuse of synaptic vesicles. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P63027}; Single-pass type IV membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P63045}. Note=Colocalizes with PRKCZ and WDFY2 in intracellular vesicles. {ECO:0000250|UniProtKB:P63027}.
Interaction partners:
- Synaptophysin
- Syntaxin-4
- Synaptosomal-associated protein 23
- Syntaxin-1A
- Synaptosomal-associated protein 25
- Syntaxin-1B
- Syntaxin-3
- Beta-soluble NSF attachment protein
- Synaptotagmin-1
- Complexin-1
Sequence:
MSATAATVPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLKMMIILGVICAIILIIIIVYFST
Protein: Retbindin (Q8QZY4)
Organism: Mus musculus (Mouse)
Function: Riboflavin-binding protein which might have a role in retinal flavin transport.
Subcellular location: Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix {ECO:0000269|PubMed:25542898}. Cell membrane {ECO:0000269|PubMed:25542898}; Peripheral membrane protein {ECO:0000269|PubMed:25542898}.
Interaction partners:
Sequence:
MAHEGHSQHSGLVWALRPILAWIFLVACGWSHPLQTRSWGHPGLAAKVRTGQLQPAGHPQSSVLPSYPRIQVPGSQTPPVPVPCCTAEIDRPESLLESCGAPSPECEFFLGQLQGALRDRFHPQLFGARPVQPLCPELCQIWFTTCQADFICGPTWLQSSGERGCEPSCRTYGQTFANATDLCHSVLGHVLRVAAPGSSHCLNVSISSPGARRRPRAWISNVVGSGSGSGSGDSPEPMFGFQYVSLP
Protein: Periostin (A0A8I6AK89)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MVPLLPLSALLLLFLCDVDPANANSYYDKVLAHSRIRGRDQGPNVCALQQILGTKKKYFSSCKNWYQGAICGKKTTVLYECCPGYMRMEGMKGCPAVMPIDHVYGTLGIVGATTTQHYSDVSKLREEIEGKGSYTYFAPSNEAWDNLDSDIRRGLENNVNVELLNALHSHMVNKRMLTKDLKHGMVIPSMYNNLGLFINHYPNGVVTVNCARVIHGNQIATNGVVHVIDRVLTQIGTSIQDFIEAEDELSSFRAAAITSDLLESLGRDGHFTLFAPTNEAFEKLPRGVLERIMGDKVASEALMKYHILNTLQCSEAITGGAVFETMEGNTIEIGCEGDSISINGIKMVNKKDIVTKNGVIHLIDEVLIPDSAKQVIELAGKQQTTFTDLVAQLGLASSLKPDGEYTLLAPVNNAFSDDTLSMDQRLLKLILQNHILKVKVGLSDLYNGQILETIGGKQLRVFVYRTAICIENSCMVRGSKQGRNGAIHIFREIIQPAEKSLHEKLRQDKRFSIFLSLLEAADLKDLLTQPGDWTLFAPTNDAFKGMTNEEREILIGDKNALQNIILYHLTPGVYIGKGFEPGVTNILKTTQGSKIYVKGVNETLLVNELKSKESDIMTTNGVIHVVDKLLYPADIPVGNDQLLELLNKLIKYIQIKLNFVHAPLSLLSATKIITKLVEPKIKVIQGSLQPIIKTEGPAMTKIHIEGEPDFRLIKEGETVTEVIHGEPVIKKYTKIIDGVPVEITEKETREERIITGPEIKYTRISTGGGETEETLQKFLQKEVSKVTKFIEGGDGHLFEDEAIKRLLQGDTPAKKIQANKRVQGSRRRSREGRSQ
Protein: Palmitoleoyl-protein carboxylesterase notum1' (EC 3.1.1.98) (A0A0D3QS98)
Organism: Xenopus laevis (African clawed frog)
Function: Carboxylesterase that acts as a key negative regulator of the Wnt signaling pathway by specifically mediating depalmitoleoylation of WNT proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors. Functions in the prospective ectoderm and is required for neural induction.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9VUX3}.
Interaction partners:
Sequence:
MAGTLCVTLLLLLSTIAVGGRKTWRRRSQQIVPSSWERSEGGGESFPLDFTAVEGNMDNFMNQIKSLAQSLYPCSAQRLDDEMKLHSLHNKSVTCNDGSPAGYYLKESKGSRRWLVFLEGGWYCISRENCDIRYDTMRSLMSSRAWPPSKTASGILSTQPEENPHWWNANIVFIPYCSSDVWSGVSPKTEKSGYAFMGSLIIQEVVKELLGKGLDTAKLLLLAGSSAGGTGVLLNVDMVANLLEELGYPGIEVRGLSDSGWFLNNKQYWRTDCTDIITCAPTEAIQRGIRYWNSMVPERCKQQFKEGEEWNCFFGYKIYPTLRSPVFVVQWLFDEAQLTVDNVHLSRQPVQESQWLYIQNLGRELRNTLKDVGASFAPACLAHEVITRSHWTEIQVRGTSLPRALHCWDRSLQEPNKNSKVQLKGCPFHLMDSCPWPQCNPTCPSIRDHFTGQEMSVVQFLMHLGFDVQKMASQQGMEPGKLLGVLSS
Protein: Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase) (P34556)
Organism: Caenorhabditis elegans
Function: Plays a key role in the control of the eukaryotic cell cycle (By similarity). Required for entry into S-phase and mitosis (By similarity). Acts as a component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II (By similarity). May function in concert with npp-16 to arrest prophase blastomeres in response to anoxia.
Subcellular location: Nucleus {ECO:0000269|PubMed:20053678}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P06493}. Cytoplasm {ECO:0000269|PubMed:20053678}. Chromosome {ECO:0000269|PubMed:20053678}. Note=Localization to chromosomes is enhanced in embryos exposed to anoxia (PubMed:20053678). When phosphorylated, localized to the nuclei of blastomeres during interphase, but not during late prophase (PubMed:20053678). {ECO:0000269|PubMed:20053678}.
Interaction partners:
- G2/mitotic-specific cyclin-B1
- G2/mitotic-specific cyclin-B
- Cyclin N-terminal domain-containing protein
- G2/mitotic-specific cyclin-A1
- Cyclin-like domain-containing protein
- Cyclin-dependent kinases regulatory subunit
- G2/mitotic-specific cyclin-B3
- Separin homolog sep-1
- separase
- Mitotic checkpoint protein bub-3
Sequence:
MDPIREGEVAHEGDSVYTLNDFTKLEKIGEGTYGVVYKGKNRRTNAMVAMKKIRLESEDEGVPSTAVREISLLKELQHPNVVGLEAVIMQENRLFLIFEFLSFDLKRYMDQLGKDEYLPLETLKSYTFQILQAMCFCHQRRVIHRDLKPQNLLVDNNGAIKLADFGLARAIGIPIRVYTHEVVTLWYRAPEILMGAQRYSMGVDMWSIGCIFAEMATKKPLFQGDSEIDELFRIFRVLGTPTELEWNGVESLPDYKATFPKWRENFLRDKFYDKKTGKHLLDDTAFSLLEGLLIYDPSLRLNAKKALVHPYFDNMDTSKLPAGNYRGELELF
Protein: Ribonuclease H2 subunit B (Ribonuclease HI subunit B) (A0A2R8Y7R8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAGVDCGDGVGARQHVFLVSEYLKDASKKMKNGLMFVKLVNPCSGEGAIYLFNMCLQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEKGNPEIDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVSSRVQSTAFFSGDQASTDKEEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKKIKLSDEPVEAKEDYTKFNTKDLKTEKKNSKMTAAQKALAKVDKSGMKTRSTNWSFCDGSTKTEKGQVMVVAPRKAWRFSLQLQTLPEDSDFFFCTFLENRQVPKGAF
Protein: Cytochrome c1, heme protein, mitochondrial (EC 7.1.1.8) (Complex III subunit 4) (Complex III subunit IV) (Cytochrome b-c1 complex subunit 4) (Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit) (Cytochrome c-1) (P08574)
Organism: Homo sapiens (Human)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of 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. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07143}; Single-pass membrane protein {ECO:0000250|UniProtKB:P07143}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Cytochrome b-c1 complex subunit 10
- Cytochrome b-c1 complex subunit 9
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
Sequence:
MAAAAASLRGVVLGPRGAGLPGARARGLLCSARPGQLPLRTPQAVALSSKSGLSRGRKVMLSALGMLAAGGAGLAMALHSAVSASDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCASCHSMDFVAYRHLVGVCYTEDEAKELAAEVEVQDGPNEDGEMFMRPGKLFDYFPKPYPNSEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIAMAPPIYTDVLEFDDGTPATMSQIAKDVCTFLRWASEPEHDHRKRMGLKMLMMMALLVPLVYTIKRHKWSVLKSRKLAYRPPK
Protein: Glycoprotein (Q85422)
Organism: Lyssavirus rabies
Subcellular location: Virion membrane {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004563}.
Interaction partners:
Sequence:
MVPQVLLFVLLLGFSLCFGKFPIYTIPDKLGPWSPIDIHHLRCPNNLVVEDEGCTNLSGFSYMELKVGYISAIKVNGFTCTGVVTEAETYTNFVGYVTTTFKRKHFRPTPDACRAAYNWKMAGDPRYEESLQNPYPDYHWLRTVRTTKESLIIISPSVTDLDPYDKSLHSRVFPGGKCSGITVSSTYCSTNHDYTIWMPENPRPGTPCDIFTNSRGKRASNGNKTCGFVDERGLYKSLKGACRLKLCGVLGLRLMDGTWVAMQTSDETKWCSPDQLVNLHDFRSDEIEHLVVEELVKKREECLDTLESIMTTKSVSFRRLSHLRKLVPGFGKAYTIFNKTLMEADAHYKSVRTWNEIIPSKGCLKVGGRCHPHVNGVFFNGIILGPDDRVLIPEMQSSLLRQHMELLESSVIPLMHPLADPSTVFKEGDEAEDFVEVHLPDVYKQISGVDLGLPNWGKYVLMTAGAMIGLVLIFSLMTWCRRANRPESKQRSFGGTGGNVSVTSQSGKVIPSWESYKSGGEIRL
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial (Complex I-30kD) (NADH-ubiquinone oxidoreductase 30 kDa subunit) (D3ZG43)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH:ubiquinone oxidoreductase subunit V3
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 2
Sequence:
MASAAARVWCRGLLGAASVARGAGRPSVLLQQRVRRESAAADKRPTVRPSSDVTHKRLSAFGEYVAEILPKYVQQVQVTCFDELEICIHPDGVIPTITFLKDHTNAQFKSLADLTAVDVPTRQNRFEIVYNLLSLRFNSRIRVKTYADELTAIDSIVSVHIAANWYEREVWDMFGVFFFNHPDLRRILTDYGFEGHPFRKDFPLTGYVELRYDDEVKRVVAEPVELAQEFRKFDLNSPWEAFPAYRQPPEHLKLEAGDKKPEAK
Protein: Deoxyribose operon repressor (P0ACK5)
Organism: Escherichia coli (strain K12)
Function: This protein is one of the repressors that regulate the expression of deoCABD genes, which encode nucleotide and deoxy ribonucleotide catabolizing enzymes. It also negatively regulates the expression of nupG (a transport protein) and tsx (a pore-forming protein). The inducer is deoxyribose-5-phosphate.
Interaction partners:
- Putative undecaprenyl-diphosphatase YbjG
- HTH-type transcriptional regulator UlaR
- HTH-type transcriptional regulator GntR
- L-fucose operon activator
- Lactose operon repressor
- HTH-type transcriptional repressor CytR
- Arabinose operon regulatory protein
Sequence:
METRREERIGQLLQELKRSDKLHLKDAAALLGVSEMTIRRDLNNHSAPVVLLGGYIVLEPRSASHYLLSDQKSRLVEEKRRAAKLAATLVEPDQTLFFDCGTTTPWIIEAIDNEIPFTAVCYSLNTFLALKEKPHCRAFLCGGEFHASNAIFKPIDFQQTLNNFCPDIAFYSAAGVHVSKGATCFNLEELPVKHWAMSMAQKHVLVVDHSKFGKVRPARMGDLKRFDIVVSDCCPEDEYVKYAQTQRIKLMY
Protein: Protein HBT1 (HUB1 target protein 1) (Q07653)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Polarity-determining protein which forms a conjugate with the ubiquitin-like modifier HUB1. Involved in bud site selection and cellular morphogenesis during conjugation. Required for survival during stationary phase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- SUR7 family protein FMP45
- Reticulon-like protein 2
- Transketolase 2
- Meiotic sister chromatid recombination protein 1
- ULP1-interacting protein 4
- Phosphate metabolism protein 7
- Protein GRE1
- Transaldolase NQM1
- Ubiquitin-like modifier HUB1
Sequence:
MNMNESISKDGQGEEEQNNFSFGGKPGSYDSNSDSAQRKKSFSTTKPTEYNLPKEQPESTSKNLETKAKNILLPWRKKHNKDSETPHEDTEADANRRANVTSDVNPVSADTKSSSGPNATITTHGYSYVKTTTPAATSEQSKVKTSPPTSHEHSNIKASPTAHRHSKGDAGHPSIATTHNHSTSKAATSPVTHTHGHSSATTSPVTHTHGHASVKTTSPTNTHEHSKANTGPSATATTHGHINVKTTHPVSHGHSGSSTGPKSTAAAQDHSSTKTNPSVTHGHTSVKDNSSATKGYSNTDSNSDRDVIPGSFRGMTGTDVNPVDPSVYTSTGPKSNVSSGMNAVDPSVYTDTSSKSADRRKYSGNTATGPPQDTIKEIAQNVKMDESEQTGLKNDQVSGSDAIQQQTMEPEPKAAVGTSGFVSQQPSYHDSNKNIQHPEKNKVDNKNISERAAEKFNIERDDILESADDYQQKNIKSKTDSNWGPIEYSSSAGKNKNLQDVVIPSSMKEKFDSGTSGSQNMPKAGTELGHMKYNDNGRDNLQYVAGSQAGSQNTNNNIDMSPRHEAEWSGLSNDATTRNNVVSPAMKDEDMNEDSTKPHQYGLDYLDDVEDYHENDIDDYSNAKKNDLYSKKAYQGKPSDYNYEQREKIPGTFEPDTLSKSVQKQDEDPLSPRQTTNRAGMETARDESLGNYEYSNTSGNKKLSDLSKNKSGPTPTRSNFIDQIEPRRAKTTQDIASDAKDFTNNPETGTTGNVDTTGRMGAKSKTFSSNPFDDSKNTDTHLENANVAAFDNSRSGDTTYSKSGDAETAAYDNIKNADPTYAKSQDITGMTHDQEPSSEQKASYGSGGNSQNQEYSSDDNIDVNKNAKVLEEDAPGYKREVDLKNKRRTDLGGADASNAYAAEVGNFPSLIDPHVPTYGFKDTNTSSSQKPSEGTYPETTSYSIHNETTSQGRKVSVGSMGSGKSKHHHNHHRHSRQNSSKGSDYDYNNSTHSAEHTPRHHQYGSDEGEQDYHDDEQGEEQAGKQSFMGRVRKSISGGTFGFRSEI
Protein: Alpha-amylase 1B (EC 3.2.1.1) (P0DTE7)
Organism: Homo sapiens (Human)
Function: Calcium-binding enzyme that initiates starch digestion in the oral cavity. Catalyzes the hydrolysis of internal (1->4)-alpha-D-glucosidic bonds, yielding a mixture of maltose, isomaltose, small amounts of glucose as well as small linear and branched oligosaccharides called dextrins.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL
Protein: Suppressor of variegation 2-10, isoform J (A0A0B4JD03)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVQMLRVVELQKILSFLNISFAGRKTDLQSRILSFLRTNLELLAPKVQEVYAQSVQEQNATLQYIDPTRMYSHIQLPPTVQPNPVGLVGSGQGVQVPGGQMNVVGGAPFLHTHSINSQLPIHPDVRLKKLAFYDVLGTLIKPSTLVPRNTQRVQEVPFYFTLTPQQATEIASNRDIRNSSKVEHAIQVQLRFCLVETSCDQEDCFPPNVNVKVNNKLCQLPNVIPTNRPNVEPKRPPRPVNVTSNVKLSPTVTNTITVQWCPDYTRSYCLAVYLVKKLTSTQLLQRMKTKGVKPADYTRGLIKEKLTEDADCEIATTMLKVSLNCPLGKMKMLLPCRASTCSHLQCFDASLYLQMNERKPTWNCPVCDKPAIYDNLVIDGYFQEVLGSSLLKSDDTEIQLHQDGSWSTPGLRSETQILDTPSKPAQKVEVISDDIELISDDAKPVKRDLSPAQDEQPTSTSNSETVDLTLSDSDDDMPLAKRRPPAKQAVASSTSNGSGGGQRAYTPAQQPQQSEDNDENCMAKAKEDSVIDLLDSP
Protein: Homeobox protein ttx-1 (Abnormal thermotaxis protein 1) (OTX homeobox homolog ttx-1) (Q9U2Z0)
Organism: Caenorhabditis elegans
Function: Probable transcription factor. Binds to a motif including the sequence 5'-TAA[TG]-3' in regulatory promoter elements. Modulates expression of its own, and of various other, genes in the AFD thermosensory neurons or AMsh amphid sheath glia, incuding the nuclear hormone receptor nhr-38, the LIM homeobox ceh-14, cyclic nucleotide-gated channel tax-2, receptor-type guanylyl cyclase gcy-8 and VEGF-related protein ver-1. Required for the development and cell fate of AFD neurons. In concert with ceh-14, perhaps as components in a complex, specifies identity of AFD neurons, acting by synergistically regulating gcy-8, gcy-18 and other genes. Involved in thermosensory behavior, thereby regulating entry and exit into the dauer larval stage of development. Required in amphid sheath AMsh glia remodeling during entry into dauer stage, acting by positively regulating the expression of ver-1 in AMsh of amphid sensory neurons. May be essential for early development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|RuleBase:RU000682, ECO:0000269|PubMed:11580895}.
Interaction partners:
- LIM/homeobox protein ceh-14
- Receptor-type guanylate cyclase gcy-8
- Protein ver-1
- Zinc finger protein ztf-16
- Receptor-type guanylate cyclase gcy-18
- Transcription factor che-1
Sequence:
MSLTSSSAPSDSIVELIQSQNLSGSGSGTGGNTGSTTMNSGNFIPTPSLTGTGASQSSGSASSGNFVSPDETDTKPSPSLMDHNDPTSSLSQQLAQGATLTSPYSTTTVDPSSLYFQLSPMSYIPNVSSATTVAAANMSAYFNQKSAYPTSHLGFPSNVGSHSFLQSNMYIPSSLSDCPTATMGSMSWNANQPGFSRKQRRERTTFTRNQLEILESYFVKTRYPDIFMREDMAHKIQLPESRVQVWFKNRRAKARQQKKTLAPSNSGVTCSGNNGSTGGGSSNGSTGSEVQPSSPATTDSELKFSEVIKEECDEQSISPSADDQKGVNSYINPISSSSGTTSYNGTSSFRPQAQYPYASYPAYDFQYSQSNTNSTNTYTLDGNSTWKFQMS
Protein: Proteasome subunit beta (Q9BMX8)
Organism: Trypanosoma brucei
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR001213}. Nucleus {ECO:0000256|PIRNR:PIRNR001213}.
Interaction partners:
Sequence:
MASGGSVIGLKYNGGVLLASDTLLSYGSLAKWPNIPRIKIIGPHTAVCATGDYADFQDMTEQLESHVERQRRYINDVLRPDEIFCYLHRHIYHKRSNFEPCLCSFVVCGCQGGVPFLGGIDSVGTQWRDDCVATGYGAYIAIPLLRKALEKPGGLSREEAVEVIKNCLRVLFYRECRAINKFQIADATNDAVEIGKPFEVETNWEYEGFCFEKTAIIR
Protein: MHC class I polypeptide-related sequence A (MIC-A) (Q29983)
Organism: Homo sapiens (Human)
Function: Seems to have no role in antigen presentation. Acts as a stress-induced self-antigen that is recognized by gamma delta T-cells. Ligand for the KLRK1/NKG2D receptor. Binding to KLRK1 leads to cell lysis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10363723, ECO:0000269|PubMed:18287244, ECO:0000269|PubMed:21928280, ECO:0000269|PubMed:8901601}; Single-pass type I membrane protein {ECO:0000269|PubMed:10363723, ECO:0000269|PubMed:18287244, ECO:0000269|PubMed:8901601}. Cytoplasm {ECO:0000269|PubMed:10363723, ECO:0000269|PubMed:18287244, ECO:0000269|PubMed:8901601}. Note=Expressed on the cell surface in gastric epithelium, endothelial cells and fibroblasts and in the cytoplasm in keratinocytes and monocytes. Infection with human adenovirus 5 suppresses cell surface expression due to the adenoviral E3-19K protein which causes retention in the endoplasmic reticulum. {ECO:0000269|PubMed:10363723, ECO:0000269|PubMed:18287244, ECO:0000269|PubMed:8901601}.
Interaction partners:
- NKG2-D type II integral membrane protein
- MHC class I polypeptide-related sequence B
- Immunoglobulin heavy variable 3-43D
- Probable non-functional immunoglobulin heavy variable 3-16
- UL16-binding protein 2
- UL16-binding protein 1
Sequence:
MGLGPVFLLLAGIFPFAPPGAAAEPHSLRYNLTVLSWDGSVQSGFLTEVHLDGQPFLRCDRQKCRAKPQGQWAEDVLGNKTWDRETRDLTGNGKDLRMTLAHIKDQKEGLHSLQEIRVCEIHEDNSTRSSQHFYYDGELFLSQNLETKEWTMPQSSRAQTLAMNVRNFLKEDAMKTKTHYHAMHADCLQELRRYLKSGVVLRRTVPPMVNVTRSEASEGNITVTCRASGFYPWNITLSWRQDGVSLSHDTQQWGDVLPDGNGTYQTWVATRICQGEEQRFTCYMEHSGNHSTHPVPSGKVLVLQSHWQTFHVSAVAAAAIFVIIIFYVRCCKKKTSAAEGPELVSLQVLDQHPVGTSDHRDATQLGFQPLMSDLGSTGSTEGA
Protein: BZIP domain-containing protein (H2L0F7)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MQQNIQYTYSSDPRSGGNQNQQLHGISQFQQNSYQPTTYSNSNANNFHSSNSATFIPNSVTQTPQRRMGEEKSLVNMLDAYFIDSTTPSTSTSWNNQQPVQMSSIQQSVGSYNQQIPQLKVGDVDLQVEGMNVKLSSSPDKGEKDRVKKARQAEAARMRYHRLSNEEKRELNLKRTLAQKRKRQREKEMEELESILRETNDIQEDPDITEQLREKRMRAKWAEAARTRYARMTPEERRAHNTRRRMRQMQNAMSAIKACGMATGDPQKDDEAVRLHIKTQNAKKAEAARQRYHRMNDDEKRVYNQRRTEAFRRRRMEEEMLLAMPIGRINGEALDRAQQIVVRNAKRAEAARLRYQRMTPDQRKSYNQKRYTPKRRRNEMDDMISAGQMAVGSSGTITMGTGTPAKKDDMDALSSLERDVVKRTQHAQQILLRQRANQSSGTPRSVTPPPQAYIISNGQQQHQQLVGNQGNNGIGQHQVLHQGHMQQQQIQVSHQDFQQSSQSIPQNIYTSGMIIQNQGQQQQGQQQQQGQSQQILNNPYRT
Protein: CRISPR-associated endonuclease Cas2 (EC 3.1.-.-) (Q9KFX8)
Organism: Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans)
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Involved in the integration of spacer DNA into the CRISPR cassette (By similarity). Functions as a dsDNA-specific endonuclease, acting on circular and linear DNA; has no activity on ssRNA or ssDNA.
Interaction partners:
- CRISPR-associated endonuclease Cas1
- CRISPR-associated exonuclease Cas4
- BH0339 protein
- BH0336 protein
- pre-crRNA processing endonuclease
- BH0338 protein
- Ferredoxin
- Ferredoxin
- Ferredoxin
Sequence:
MLVLITYDVQTSSMGGTKRLRKVAKACQNYGQRVQNSVFECIVDSTQLTSLKLELTSLIDEEKDSLRIYRLGNNYKTKVEHIGAKPSIDLEDPLIF
Protein: Protein amnionless [Cleaved into: Soluble protein amnionless] (Q9BXJ7)
Organism: Homo sapiens (Human)
Function: Membrane-bound component of the endocytic receptor formed by AMN and CUBN. Required for normal CUBN glycosylation and trafficking to the cell surface. The complex formed by AMN and CUBN is required for efficient absorption of vitamin B12. Required for normal CUBN-mediated protein transport in the kidney (Probable).
Subcellular location: [Isoform 1]: Apical cell membrane {ECO:0000269|PubMed:14576052}; Single-pass type I membrane protein {ECO:0000305|PubMed:30523278}. Cell membrane {ECO:0000269|PubMed:14576052, ECO:0000269|PubMed:29402915, ECO:0000269|PubMed:30523278}; Single-pass type I membrane protein {ECO:0000305}. Endosome membrane {ECO:0000305|PubMed:14576052}. Membrane, coated pit {ECO:0000305|PubMed:14576052}.; SUBCELLULAR LOCATION: [Soluble protein amnionless]: Secreted {ECO:0000269|PubMed:14576052}.
Interaction partners:
- Cubilin
- Low-density lipoprotein receptor-related protein 2
- Cobalamin binding intrinsic factor
- Apolipoprotein A-I
- Transcobalamin-2
- Disabled homolog 2
Sequence:
MGVLGRVLLWLQLCALTQAVSKLWVPNTDFDVAANWSQNRTPCAGGAVEFPADKMVSVLVQEGHAVSDMLLPLDGELVLASGAGFGVSDVGSHLDCGAGEPAVFRDSDRFSWHDPHLWRSGDEAPGLFFVDAERVPCRHDDVFFPPSASFRVGLGPGASPVRVRSISALGRTFTRDEDLAVFLASRAGRLRFHGPGALSVGPEDCADPSGCVCGNAEAQPWICAALLQPLGGRCPQAACHSALRPQGQCCDLCGAVVLLTHGPAFDLERYRARILDTFLGLPQYHGLQVAVSKVPRSSRLREADTEIQVVLVENGPETGGAGRLARALLADVAENGEALGVLEATMRESGAHVWGSSAAGLAGGVAAAVLLALLVLLVAPPLLRRAGRLRWRRHEAAAPAGAPLGFRNPVFDVTASEELPLPRRLSLVPKAAADSTSHSYFVNPLFAGAEAEA