wanglab/gogpt-training-data huggingface dataset:
Protein: cAMP responsive element binding protein 1 (C9J896)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKK
Protein: Protein FAM170B (Acrosome-related protein) (E9PXT9)
Organism: Mus musculus (Mouse)
Function: Plays a role in fertilization through the acrosome reaction.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:26179146}. Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane {ECO:0000269|PubMed:26179146}.
Interaction partners:
Sequence:
MKHHLIEHRGEQTPGTAVGMASPDAAEESTGVCWPGGAMRRNESSPRPGPAFLPDDDIYLAARAQGVLGWSSSPSSQSSSEYQSYSQYQSWDSSKSEEQQETPPESVCALYTHVQTVRGVAVAWETDDGFEPVTRKPLIREAEFIKRQRRKGSSFEMASNTDLRWELEDCKHYCPQTEDPVDCCMQELRAPPDWLVTTNHGLRCVACCRVFPTLEALLDHAQHGIQDGFSCQIFFEEMLERKRTRDQKQDQQPVEEEQSLSDSSECTRLLTKVLPWQQQPQQQPQEQQKQQQQQQQKQRQQEQQQHQQQQQQPQPLKQQQQQQQQQPLQPQPLKQQPLQPLQPQPQPQPQKQQQRQQQRQQQPPRQQQKQQPLQQQGK
Protein: Lissencephaly-1 homolog A (Platelet-activating factor acetylhydrolase IB subunit alpha a) (Q7T394)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. May be required for proliferation of neuronal precursors and neuronal migration.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
Interaction partners:
- Platelet-activating factor acetylhydrolase, isoform Ib, gamma subunit.
- Platelet-activating factor acetylhydrolase IB subunit alpha2
- Platelet-activating factor acetylhydrolase
- Lissencephaly-1 homolog B
- Nuclear distribution protein nudE-like 1-B
- Lysophosphatidylcholine acyltransferase 2
- Lysophosphatidylcholine acyltransferase 4
- Choline/ethanolaminephosphotransferase 1
- Choline/ethanolaminephosphotransferase 1
- Uncharacterized protein.
Sequence:
MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEINIGGPIGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVIVSASEDATIKVWDHETGDFERTLKGHTDSVQDISFDHTGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVATGYCVKTFTGHREWVRMVRPNQDGTLIASSSNDQTVRVWVVATKECKAELREHEHVVECISWAPESAHPTILEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSIGMCLMTLVGHDNWVRGVLVHPGGKYIVSCADDKTLRIWDYKNKRCTKTLSAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR
Protein: 3-hydroxy-4-methylanthranilate adenylyltransferase (EC 2.7.7.97) (4-MHA-activating enzyme) (C0LTL9)
Organism: Streptosporangium sibiricum
Function: Involved in the biosynthesis of the antitumor antibiotic sibiromycin. Activates 4-methyl-3-hydroxyanthranilic acid (4-MHA or 3H4MAA), a precursor of the antitumor antibiotic sibiromycin, as adenylate. The activated substrate is then covalently tethered to the thiolation domain. 4-MHA is the preferred substrate, but it can also use 3-hydroxyanthranilic acid (3HAA) and anthranilic acid (AA). Has lower activity with 5-hydroxyanthranilic acid (5HAA) and 3,5-dihydroxy-4-methylanthranilic acid (3,5DH4MAA).
Interaction partners:
Sequence:
MSALPSLRVPTLPVAFEAAARAAGDRIALEYGSSSITYRELDAAANRFARRLLREGVTPGSRVGLHMTRCLELYIAMIGLLKAGAVVVPLNPSHPVTVRRSVVREADLPLTLRDVPAGLSSVTVERDVHELLAAGADLDDTSPGLCTDPESTAFILFTSGSTGRPRGVRIAHRGIARVASYNGEVEVRPDDCFLQLAPYSFAASTTDIWLSLLHGARVVVLPSQLPSLPKLAHTIKEYGVTFLNLPGGLMNLLIDAHPEAFAKVRTVIVSGDFPSAPHLARVMKAVPGTVYNAFGCTENSALTAVHPMTPEDLQLGVVPIGLPLPGVGLHVLGEDMTPCAPGEVGEMHISGAGLAQGYLGLPEETAAKFPTVDGVRMLRTGDWARTTPAGEVVLVGRTDQMVKIRGFRVELREVELAADQSGLVEKAVVRAVDATDGQKELVLFCTTATGEAPSIEALLADLKSRLPDYMLPARVHHLAELPVNVNGKLDRMALREPRAVLVEPDGTAQQQPVVRDIIATTVTRLLAVVTGREPIGVSDSFLASGANSLQVIQLAASLHDVMGVDVRPEDIFQLDNAESLAGHIRALRQGHREVPA
Protein: SNAP91 protein (A7Z073)
Organism: Bos taurus (Bovine)
Interaction partners:
Sequence:
MSGQTLTDRIAAAQYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDFARVKKGADGVMRTMAPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVAEQVGIDKGDIPDLTQAPSSLMETLEQHLNTLEGKKPGNNEGSGAPSPLSKSSPATTVTSPNSTPAKTIDTSPPVDLFATASAAVPVSTSKPSSDLLDLQPDFSPAGAAAAAPAPAPPSGGATAWGDLLGEDSLAALSSVPSEAQISDPFAPEPTPPATSAETSAAAASASTTTTVTAVTADVDLFGDAFAASPGEAPTASEGATAPAPPTPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSVPVVTPTASTAPPVPATAPSPAPAVAAATAATTAATTAAAATATTSATTTSAPPALDIFGDLFESAPEVAPAPKPEAAPSIDLFGTDAFSSPPQGASPVPESSLTADLLSVDTFVAPSPATTASPAKVDSSGVIDLFGDAFGSSASEPQPAPQAASSSSASADLLAGFGGSFMAPSPSPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPTGQPAPISLVPPSPAMAASKALGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGVAAVPGTQLSPSPTPASQSPKKPPAKDPLADLNIKDFL
Protein: Putative clathrin assembly protein At1g03050 (Q9SA65)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane, clathrin-coated pit {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Note=Colocalized with clathrin in the Golgi area. {ECO:0000250}.
Interaction partners:
- Probable pectinesterase 49
- Expressed protein
- Clathrin interactor EPSIN 2
- Probable pectinesterase 67
- Invertase/pectin methylesterase inhibitor family protein
- At5g50030
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Calcium-transporting ATPase 2, endoplasmic reticulum-type
- Putative clathrin assembly protein At5g65370
- Probable pectinesterase 50
Sequence:
MGSSKFKRAIGAVKDQTSVGLAKVNGRSASLSELDVAIVKATRHEEFPAEEKYIREILSLTSYSRSYINACVSTLSRRLNKTKCWTVALKTLILIQRLLGEGDQAYEQEIFFATRRGTRLLNMSDFRDVSRSNSWDYSAFVRTYALYLDERLDFRMQARHGKRGVYCVGGEADEEEQDQAAADLSTAIVVRSQPIAEMKTEQIFIRIQHLQQLLDRFLACRPTGNARNNRVVIVALYPIVKESFQIYYDVTEIMGILIERFMELDIPDSIKVYDIFCRVSKQFEELDQFYSWCKNMGIARSSEYPEIEKITQKKLDLMDEFIRDKSALEHTKQSKSVKSEADEDDDEARTEEVNEEQEDMNAIKALPEPPPKEEDDVKPEEEAKEEVIIEKKQEEMGDLLDLGNTNGGEAGQAGDSLALALFDGPYASGSGSESGPGWEAFKDDSADWETALVQTATNLSGQKSELGGGFDMLLLNGMYQHGAVNAAVKTSTAYGASGSASSMAFGSAGRPAATMLALPAPSTANGNAGNINSPVPMDPFAASLEVAPPAYVQMNDMEKKQRMLMEEQMMWDQYSRDGRQGHMNLRQNQNQPYSYTPQY
Protein: Uncharacterized protein C186.04c (G2TRL1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- UPF0768 protein PB2B2.18
- Exosome complex component rrp43
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Glycerophosphocholine phosphodiesterase gde1
- cAMP-dependent protein kinase regulatory subunit
- Putative uncharacterized hydrolase C7D4.05
Sequence:
MNTSSRIQLPSSNDAHVYDGRSNEPKASKRSYVNLTRQMRPKDALKMNISSPNLKDLSKFADPDAQQWLEGYLAGKLEDNSKTPRSNFVDPLYEELNARRKPNKPVWSLSGPLPHVLGNSVVEKLEARSRASSVSNSRLNSRTNSSVSLKGMDGSSSWKNKIKNAVSNVTDQSKR
Protein: Zinc transporter ZIP1 (Solute carrier family 39 member 1) (Zinc-iron-regulated transporter-like) (Zrt- and Irt-like protein 1) (ZIP-1) (mZIP1) (Q9QZ03)
Organism: Mus musculus (Mouse)
Function: Mediates zinc uptake. May function as a major endogenous zinc uptake transporter in many cells of the body (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9NY26}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NY26}; Multi-pass membrane protein {ECO:0000255}. Note=Shows a vesicular localization corresponding partially to the endoplasmic reticulum in several epithelial cell lines. {ECO:0000250|UniProtKB:Q9NY26}.
Interaction partners:
- Proton-coupled zinc antiporter SLC30A1
- Probable proton-coupled zinc antiporter SLC30A4
- Zinc transporter ZIP4
- Zinc transporter SLC39A7
- Metal cation symporter ZIP14
- Zinc transporter ZIP11
- Zinc transporter ZIP9
- Zinc transporter ZIP13
- Zinc transporter ZIP10
- Zinc transporter 6
Sequence:
MGPWGEPELLVWRPEAVASEPSVPVGLEVKLGALVLLLLLTLICSLVPVCVLRRSGANHEASASGQKALSLVSCFAGGVFLATCLLDLLPDYLAAIDEALEALHVTLQFPLQEFILAMGFFLVLVMEQITLAYKEQTSPPHPEETRALLGTVNGGPQHWHDGPGIPQAGGTPAAPSALRACVLVFSLALHSVFEGLAVGLQRDRARAMELCLALLLHKGILAVSLSLRLLQSHLRVQVVAGCGILFSCMTPLGIGLGAALAESAGPLHQLAQSVLEGMAAGTFLYITFLEILPQELATSEQRILKVILLLAGFALLTGLLFVQI
Protein: Paired box 5 (E7EQT0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDLEKNYPTPRTSRTGHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAERVCDNDTVPSVSSINRIIRTKVQQPPNQPVPASSHSIVSTGSVTQVSSVSTDSAGSSYSISGILGITSPSADTNKRKRDEGIQESPVPNGHSLPGRDFLRKQMRGDLFTQQQLEVLDRVFERQHYSDIFTTTEPIKPEQGVSFPGVPTATLSIPRTTTPGGSPTRGCLAPPTIIALPPEEPPHLQPPLPMTVTDPWSQAGTKH
Protein: Erlin-2 (Endoplasmic reticulum lipid raft-associated protein 2) (Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2) (SPFH domain-containing protein 2) (O94905)
Organism: Homo sapiens (Human)
Function: Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs) such as ITPR1. Promotes sterol-accelerated ERAD of HMGCR probably implicating an AMFR/gp78-containing ubiquitin ligase complex. Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. May promote ER retention of the SCAP-SREBF complex.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031}; Single-pass type II membrane protein {ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031}. Note=Associated with lipid raft-like domains of the endoplasmic reticulum membrane.
Interaction partners:
- Erlin-1
- Prohibitin 1
- E3 ubiquitin-protein ligase AMFR
- E3 ubiquitin-protein ligase RNF170
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Transmembrane and ubiquitin-like domain-containing protein 1
- E3 ubiquitin-protein ligase RNF185
- FAS-associated factor 2
- E3 ubiquitin-protein ligase synoviolin
- Protein sel-1 homolog 1
Sequence:
MAQLGAVVAVASSFFCASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNIPEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDSAGSVSKQFEGLADKLSFGLEDEPLETATKEN
Protein: Propionate--CoA ligase (EC 6.2.1.1) (EC 6.2.1.17) (A0A8I6AD12)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGLPEERRKSGSGSRAREETGAEGRVRGWSPPPEVRRSAHVPSLQRYRELHRRSVEEPREFWGNIAKEFYWKTPCPGPFLQYNFDVTKGKIFTEWMKGATTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGVQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTDAFYRGEKLVNLKELADESLEKCREKGFPVRCCIVVKHLGRAELGMNDSPSQSPPVKRPCPDVQISWNEGVDLWWHELMQQAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSVAPRHCGKSTGEPGLLLSVPLPRELSTWLNTLPACFKSKGQIG
Protein: Mu-scoloptoxin(15)-Ssm1a (Mu-SLPTX(15)-Ssm1a) (Potassium channel toxin SsTx) (Ssm spooky toxin) (A0A2L0ART2)
Organism: Scolopendra mutilans (Chinese red-headed centipede) (Scolopendra subspinipes mutilans)
Function: Blocks voltage-gated potassium channels Kv7.4/KCNQ4 (IC(50)=2.5 uM), Kv7.1/KCNQ1 (IC(50)=2.8 uM), Kv7.2/KCNQ2 (IC(50)=2.7 uM) and Kv7.5/KCNQ5 (IC(50)=2.7 uM). Targets the pore domain, in particular negatively charged residues 'Asp-266' and 'Asp-288', of KCNQ4 and probably other KCNQ channel family members where these residues are conserved. In vivo, shows vasoconstrictive activity resulting in acute hypertension when injected intravenously in mice. Also induces coronary vasospasms ultimately leading to heart failure. Induces seizures when injected into the hippocampus of mice. Decreases respiratory rate while increasing respiratory amplitude, probably by triggering a contraction of the bronchial ring.
Subcellular location: Secreted {ECO:0000269|PubMed:29358396}.
Interaction partners:
Sequence:
MEKKIIFLVFLVALLALPGFISTEVIKKDTPYKKRKFPYKSECLKACATSFTGGDESRIQEGKPGFFKCTCYFTTG
Protein: MADS17 (Os04g0580700 protein) (cDNA clone:J023057B01, full insert sequence) (Q0JAS4)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDRSEMGRGRVELKRIENKINRQVTFSKRRNGLLKKAYELSVLCDAEVALIIFSSRGKLYEFGSAGINKTLEKYNSCCYNAQGSNSALAGGEHQSWYQEMSRLKTKLECLQRSQRHMLGEDLGPLSIKELQQLEKQLEYSLSQARQRKTQIMMEQVDDLRRKERQLGELNKQLKNKLEAEADSSNCRSAIQDSWVHGTVVSGGRVLNAQPPPDIDCEPTLQIGYYQFVRPEAANPRSNGGGGDQNNNFVMGWPL
Protein: Dipeptide and tripeptide permease C (Dipeptide/tripeptide:H(+) symporter DtpC) (P39276)
Organism: Escherichia coli (strain K12)
Function: Proton-dependent permease that transports di- and tripeptides. Shows significantly higher specificity towards dipeptides than tripeptides. Has a preference for dipeptides with a C-terminal Lys residue. Can bind Ala-Lys, Lys-Ala, Ala-Ala. Can also transport alanine and trialanine.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Lysine--tRNA ligase, heat inducible
- Uncharacterized protein YjdJ
Sequence:
MKTPSQPRAIYYIVAIQIWEYFSFYGMRALLILYLTHQLGFDDNHAISLFSAYASLVYVTPILGGWLADRLLGNRTAVIAGALLMTLGHVVLGIDTNSTFSLYLALAIIICGYGLFKSNISCLLGELYDENDHRRDGGFSLLYAAGNIGSIAAPIACGLAAQWYGWHVGFALAGGGMFIGLLIFLSGHRHFQSTRSMDKKALTSVKFALPVWSWLVVMLCLAPVFFTLLLENDWSGYLLAIVCLIAAQIIARMMIKFPEHRRALWQIVLLMFVGTLFWVLAQQGGSTISLFIDRFVNRQAFNIEVPTALFQSVNAIAVMLAGVVLAWLASPESRGNSTLRVWLKFAFGLLLMACGFMLLAFDARHAAADGQASMGVMISGLALMGFAELFIDPVAIAQITRLKMSGVLTGIYMLATGAVANWLAGVVAQQTTESQISGMAIAAYQRFFSQMGEWTLACVAIIVVLAFATRFLFSTPTNMIQESND
Protein: ABC-type glutathione-S-conjugate transporter (EC 7.6.2.3) (Q7KTB7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Vacuole membrane {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128}.
Interaction partners:
Sequence:
MADDTSSPMDRFCGSTFWNATETWYTNDPDFTPCFEQTALVWTPCAFYWAFVIFDFYYLKASLDRNIPWNKLNVSKALVNLGLLVITALDLIMALVKKGGDSELPLYDLDVWGPIIKFATFLLLFIFIPLNRKYGVQTTGCQFIFWFLLTVLSIPRCRTEVRLDAERQKILNSQQPSEQDFSWEEYQFVSFFIFFTFTSIMLILNCFADGMPRQTKYQRGENEIPELSASFLSRITYQWFDKMALKGYRNPLEEKDLWDLRPQDSCSEVMPIFAHHWNQNVRKNYKNKARVEPKAQFSNGNVTFENPHGEKNGRKKGMASIMPPIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLIDENNVLDATKTFVSLSLFNILRFPLTMLPMLITNLVQTQVSVNRINKFLNSEELDPNSVLHDSSKPHPMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFIIQHLQEGNEEEEELNQIKRQISSTADVPELLGTVEKAIKLARTESLSDSISVTSADSLMGGGGSLRRRTKRQDSHDSVASAASLKKKQEVEGKLIETEKSQTGGVEFAVYKHYIKSVGIFLSVATLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGLRDMYLGVYGAFGFGQGFTSFFSDLAPALGSLHAAKVLHSMLLENVLRAPMTMFDTTPVGRILSRFSKDVESVDQKMPQVINDCIWCAFEVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPWELEQDKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAFYSMAKDANLV
Protein: Glycerol-3-phosphate acyltransferase (Q9TJS6)
Organism: Oryza sativa (Rice)
Interaction partners:
Sequence:
EPFDYYMFGQNYIRPLVDYRNSYVGNISIFQDMEQKLQQGHNVVLMSNPQTEADPAIIALLLERSNPWISENIVYVAGDRVVTGSLCKPFSMGRNLICVYSKKHM
Protein: Frataxin, mitochondrial (Fxn) (EC 1.16.3.1) (Q9ZR07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+). May be able to store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization. Binds to the mitochondrial cysteine desulfurase NIFS1 and increases its activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17092311}.
Interaction partners:
- Iron-sulfur cluster assembly protein 1
- Iron-sulfur cluster assembly protein 2
- Cysteine desulfurase, mitochondrial
- Iron-sulfur cluster assembly protein 3
- Photosystem II protein D1
- At5g61220
- Ferrochelatase-1, chloroplastic/mitochondrial
- Ferrochelatase-2, chloroplastic
- Iron-sulfur cluster co-chaperone protein HscB homolog
- Adrenodoxin-like protein 2, mitochondrial
Sequence:
MATASRFLLRKLPRFLKLSPTLLRSNGVRVSSNLIQDSIEPLDSFWRIGSRIRHDSLTTRSFSSQGPASVDYSSVLQEEEFHKLANFTINHLLEKIEDYGDNVQIDGFDIDYGNEVLTLKLGSLGTYVLNKQTPNRQIWMSSPVSGPSRFDWDRDANAWIYRRTEAKLHKLLEEELENLCGEPIQLS
Protein: Translocator protein (Peripheral-type benzodiazepine receptor) (O76068)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004225}.
Interaction partners:
Sequence:
HGEGLRWYAGLQKPSWHPPHWVLGPVWGTLYSAMGYGSYLVWKELGGFTEKAVVPLGLYTGQLALNWAWPPIFFGARQMGWALVDLLLVSGAAAATTVAWYQVSPLAARLLYPYLAWLAFTTTLNYCVWRDNHGWRGGRRLPE
Protein: Glucagon-like peptide 2 receptor (GLP-2 receptor) (GLP-2-R) (GLP-2R) (Q9Z0W0)
Organism: Rattus norvegicus (Rat)
Function: This is a receptor for glucagon-like peptide 2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Pro-glucagon
- Glucagon-like peptide 1 receptor
- Gastric inhibitory polypeptide
- Dipeptidyl peptidase 4
Sequence:
MRPQPSPAVPSRCREAPVPRVRAQPVGIPEAQGPVPLHSQQMRLLWGPGRPFLALLLLVSIKQVTGSLLKETTQKWANYKEKCLEDLHNRLSGIFCNGTFDRYVCWPHSYPGNVSVPCPSYLPWWNAESPGRAYRHCLAQGTWQTRENTTDIWQDESECSENHSFRQNVDHYALLYTLQLMYTVGYSVSLISLFLALTLFLFLRKLHCTRNYIHMNLFASFILKVLAVLVKDMVSHNSYSKRPDDESGWMSYLSETSVSCRSVQVLLHYFVGTNHLWLLVEGLYLHTLLEPTVFPERRLWPKYLVVGWAFPMLFVIPWGFARAHLENTRCWATNGNLKIWWIIRGPMLLCVTVNFFIFLKILKLLISKLKAHQMCFRDYKYRLAKSTLLLIPLLGVHEVLFTFFPDDQVQGFSKRIRLFIQLTLSSVHGFLVALQYGFANGEVKAELRKSWGRFLLARHWGCRTCVLGKNFRFLGKCSKKLSEGDGSETLQKLRFSTCSSHLASETLGDVGVQPHRGRGAWPRGSSLSESSEGDFTLANTMEEILEESEI
Protein: 5-hydroxytryptamine receptor 6 (5-HT-6) (5-HT6) (Serotonin receptor 6) (P50406)
Organism: Homo sapiens (Human)
Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase. It has a high affinity for tricyclic psychotropic drugs (By similarity). Controls pyramidal neurons migration during corticogenesis, through the regulation of CDK5 activity (By similarity). Is an activator of TOR signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:37327704}; Multi-pass membrane protein {ECO:0000269|PubMed:35714614, ECO:0000269|PubMed:36989299, ECO:0000269|PubMed:37327704}.
Interaction partners:
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 7
- Pro-opiomelanocortin
- VIP peptides
- Pituitary adenylate cyclase-activating polypeptide
- Pro-glucagon
- Thyrotropin subunit beta
- Natriuretic peptides A
- Follitropin subunit beta
- Gastric inhibitory polypeptide
Sequence:
MVPEPGPTANSTPAWGAGPPSAPGGSGWVAAALCVVIALTAAANSLLIALICTQPALRNTSNFFLVSLFTSDLMVGLVVMPPAMLNALYGRWVLARGLCLLWTAFDVMCCSASILNLCLISLDRYLLILSPLRYKLRMTPLRALALVLGAWSLAALASFLPLLLGWHELGHARPPVPGQCRLLASLPFVLVASGLTFFLPSGAICFTYCRILLAARKQAVQVASLTTGMASQASETLQVPRTPRPGVESADSRRLATKHSRKALKASLTLGILLGMFFVTWLPFFVANIVQAVCDCISPGLFDVLTWLGYCNSTMNPIIYPLFMRDFKRALGRFLPCPRCPRERQASLASPSLRTSHSGPRPGLSLQQVLPLPLPPDSDSDSDAGSGGSSGLRLTAQLLLPGEATQDPPLPTRAAAAVNFFNIDPAEPELRPHPLGIPTN
Protein: Polyribonucleotide nucleotidyltransferase (EC 2.7.7.8) (Polynucleotide phosphorylase) (PNPase) (Q1ZJW2)
Organism: Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 / CCUG 15956))
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595}.
Interaction partners:
Sequence:
MNPIVKTFQYGNHTVTLETGVMARQATAAVMVSMDDTSVFVSVVGKKTAVEGQDFFPLTVNYQERTYAAGKIPGGFFKREGRPSEGETLTARLIDRPIRPLFPDDFKNEVQVIATVVSVNPAVSPDIVTMIGTSAALAISGIPFNGPIGAARVGYINDQFVLNPSNVELEESRLDLVVAGTKDAVLMVESEADRLSEEQMLQAVVFGHDQQQVAINAINEFAAEVATPAWDWVAPQENTALKNKIAELAEAKLVDAYQITEKMARYDRIHEIAGEVNDAILAEDAEANSKEIHTIFHDLEKTVVRGRIIAGNPRIDGREKDMVRALDVRTGVLPRTHGSSLFTRGETQALVTATLGTQRDAQIIDGLTGETKDHFLLHYNFPPYCVGETGFVGSPKRREIGHGKLAKRGIAAVMPSVDEFPYTVRVVSEITESNGSSSMASVCGTSLALMDAGVPIKASVAGIAMGLVKEGDDFVVLSDILGDEDHLGDMDFKVAGTDDGITALQMDIKIEGITKEIMQIALNQAKGARKHILSVMDNAINTPREDISEFAPRIHTMKINPEKIKDVIGKGGAVIRALTEETGTTIEIEDDGTVKIAATEGTAAKEAIRRIEEITADVEVGRIYTGKVMRIVDFGAFVSVIGTKEGLVHISQISQDRVEKVSDYLQMGQEVQVKVLEIDRQGRIRLSMKEAVETPAAEAPAQNEQPQG
Protein: Fanconi anemia protein FANCD2 (Q68Y81)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MVSKRKLSKIDAAEESSKTDLQSRCPETKRSRISDKRAPSQGGLENEGVFEELLRTSGIILKVGEGQNEIAVDQTAFQKKLRVALEKHPSYPGVVNEFISGLESHIKDRSQFKNCLLPCTPARTEGSRTLVHSYCESLIKLLLGIKILQPAVVTLLLEKIPEFFFDVVGTFGTNFPRLIVNQFKWLDGLLDSQDLVKKLMQMLSVSPVPIQHDIITSLPEILEDSQQNEVARELSCLLKQGRRLTVPILDALSRLDLDAELLAEVRQSAMTIVPSVKLEDLPVVIKFILHNVKAADAVEVISDLRKSLDLSSCVLPLQLLGSQRKLKSQAQASSSMSQVTTSQNCVKLLFDVIKQAVRFQKDVSEAWIKAIENSTSVSDHKVLDLIVLLLIHSTNSKNRKQTEKVLRSKIRLGCMPEQLMQNAFQNHSMVIKDFFPSILSLAQTFLHSAHPAVVSFGSCMYKQAFAVFDSYCQQEVVCALVTHVCSGNETELDISLDVLTDLVILHPSLLLRYATFVKTILDSMQKLNPCQIRKLFYILSTLAFSQRQEGSYIQDDMHMVIRKWLSSSVPNHKQMGIIGAVTMMGSVALKRNEADGGLLERPELSIECDGQLSTLLDLVGFCCEQTPEVLALYYDELANLIEKQKGNLDLQLLDKFGKSLVEDFPNDFVVDLSPTVDGSFLFPVKSLYNLDEDETQGAIAINLLPLVSQSEPGRVADEMSNSRKRVVSPICLSPCFRLLRLYTGEQNNGSLEEIDALLGCPLYLTDLEVEGKLDSLSKQEREFLCSLLFYALNWFREVVNAFCQQQDAEMKGKVLTRLQNITELQNVLGKCLAATPGYVPPPATFDSEAPEGVPSINAGGPVRKKNGKKRKSDSSKACSAERTQADESSDGNQPDTELSELEKSATEKETGNPLAQLQSYRPYFRELDLEVFSVLHCGLLTKSILDTEMHTEASEVVQLGPAELCFLLDDMCWKLEHVLTPGSTRRVPFLKERGNKDVGFSHLCQRSPKEVAVCVVKLLKPLCNHMENMHNYFQTVIPNQGVVDESGLNIQEYQLMSSCYHQLLLAFRLLFAWSGFSQHENSNLLRSALQVLADRLKPGETEFLPLEELISESFQYLLNFQASIPSFQCAFILTQVLMAISEKPMTGWKREKMASLAKQFLCQSWMKPGGDREKGSHFNSALHTLLCVYLEHTDNILKAIEEISSVGVPELINSAKDGCSSTYPTLSRQTFPVFFRVMMAQLESSVKSIPAGKPSDSGEVQLEKLLKWNIAVRNFHILINLVKVFDSRPVLSICLKYGRLFVEAFLKLAMPLLDHSFKKHRDDVQSLLKTLQLSTRQLHHMCGHSKIHQDLGLTNHVPLLKKSLEQFVYRVKAMLAFNHCQEAFWVGVLKNRDLQGEEILSQASAAPEEDSAEGSEEDTADSAAEEPDGTDSDSGGAGR
Protein: S-layer protein 2 (55 KDa parasporal endotoxin) (P85110)
Organism: Bacillus thuringiensis subsp. konkukian
Function: The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria.
Subcellular location: Secreted, cell wall, S-layer.
Interaction partners:
Sequence:
LDTDLQGTMPEVYASERAAFL