wanglab/gogpt-training-data huggingface dataset:
Protein: Hypoxia-inducible factor 3-alpha (HIF-3-alpha) (HIF3-alpha) (Basic-helix-loop-helix-PAS protein MOP7) (Class E basic helix-loop-helix protein 17) (bHLHe17) (HIF3-alpha-1) (Inhibitory PAS domain protein) (IPAS) (Member of PAS protein 7) (PAS domain-containing protein 7) (Q9Y2N7)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional regulator in adaptive response to low oxygen tension. Acts as a regulator of hypoxia-inducible gene expression. Functions as an inhibitor of angiogenesis in hypoxic cells of the cornea. Plays a role in the development of the cardiorespiratory system. May also be involved in apoptosis (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16775626, ECO:0000269|PubMed:19694616}. Cytoplasm {ECO:0000269|PubMed:19694616}. Nucleus speckle {ECO:0000250|UniProtKB:Q0VBL6}. Mitochondrion {ECO:0000250|UniProtKB:Q0VBL6}. Note=In the nuclei of all periportal and perivenous hepatocytes. In the distal perivenous zone, detected in the cytoplasm of the hepatocytes. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Colocalizes with BAD in the cytoplasm. Colocalizes with EPAS1 and HIF1A in the nucleus and speckles (By similarity). Localized in the cytoplasm and nuclei under normoxia, but increased in the nucleus under hypoxic conditions (PubMed:19694616). Colocalized with HIF1A in kidney tumors (PubMed:19694616). {ECO:0000250|UniProtKB:Q0VBL6, ECO:0000250|UniProtKB:Q9JHS2, ECO:0000269|PubMed:19694616}.
Interaction partners:
- Aryl hydrocarbon receptor nuclear translocator
- Endothelial PAS domain-containing protein 1
- Hypoxia-inducible factor 1-alpha
- Aryl hydrocarbon receptor nuclear translocator 2
- Prolyl hydroxylase EGLN2
- Egl nine homolog 1
- Prolyl hydroxylase EGLN3
- von Hippel-Lindau disease tumor suppressor
- Erythropoietin
- Elongin-B
Sequence:
MALGLQRARSTTELRKEKSRDAARSRRSQETEVLYQLAHTLPFARGVSAHLDKASIMRLTISYLRMHRLCAAGEWNQVGAGGEPLDACYLKALEGFVMVLTAEGDMAYLSENVSKHLGLSQLELIGHSIFDFIHPCDQEELQDALTPQQTLSRRKVEAPTERCFSLRMKSTLTSRGRTLNLKAATWKVLNCSGHMRAYKPPAQTSPAGSPDSEPPLQCLVLICEAIPHPGSLEPPLGRGAFLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGGRGPQSESIVCVHFLISQVEETGVVLSLEQTEQHSRRPIQRGAPSQKDTPNPGDSLDTPGPRILAFLHPPSLSEAALAADPRRFCSPDLRRLLGPILDGASVAATPSTPLATRHPQSPLSADLPDELPVGTENVHRLFTSGKDTEAVETDLDIAQDADALDLEMLAPYISMDDDFQLNASEQLPRAYHRPLGAVPRPRARSFHGLSPPALEPSLLPRWGSDPRLSCSSPSRGDPSASSPMAGARKRTLAQSSEDEDEGVELLGVRPPKRSPSPEHENFLLFPLSLSFLLTGGPAPGSLQDPSTPLLNLNEPLGLGPSLLSPYSDEDTTQPGGPFQPRAGSAQAD
Protein: Tripeptidyl-peptidase 2 (EC 3.4.14.10) (Tripeptidyl-peptidase II) (TPPII) (F4JVN6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine protease of the proteasome pathway that may function with the 20S proteasome to degrade oxidized proteins generated by environmental stress.
Interaction partners:
- Probable carboxylesterase 7
- Probable thimet oligopeptidase
- Prolyl endopeptidase
- Probable cytosolic oligopeptidase A
- Protein S40-4
- Subtilisin-like protease SBT1.8
- Subtilisin-like protease SBT1.4
- Subtilisin-like protease SBT5.5
- Subtilisin-like protease SBT3.8
- Subtilisin-like protease SBT2.5
Sequence:
MDLSLQLQIHGALINKGPSCTSYWASSSSLSLPRDFISSSTFLLHRRLRRRSCSRSRGIRLRRSGFSAMPCSSSDTLTASRVGCGGGGGGGAVGGGAENASVANFKLNESTFIASLMPKKEIRADCFIEAHPEYDGRGVVIAIFDSGFDPSAAGLHVTSDGKPKVLDVIDCTGSGDIDTSTVVKANEDGHIRGASGATLVVNSSWKNPTGEWRVGSKLVYQLFTDDLTSRVKKERRKSWDEKNQEEIAKAVNNLYDFDQKHSKVEDAKLKKTREDLQSKVDFLKKQADKYEDKGPVIDAVVWHDGEVWRVALDTQSLEEDPDSGKLADFSPLTNYRIERKYGVFSRLDACSFVANVYDEGKVLSIVTDSSPHGTHVAGIATAHHPEEHLLNGVAPGAQIISCKIGDSRLGSMETGTGLTRALIAALEHNCDLVNMSYGEPALLPDYGRFVDLVTEAVNKRRLIFVSSAGNSGPALTTVGAPGGTTSSIIGVGAYVSPAMAAGAHSVVEPPSEGLEYTWSSRGPTSDGDLGVCISAPGGAVAPVPTWTLQRRMLMNGTSMASPSACGAIALLLSAMKAEGIPVSPYSVRRALENTSTPVGDLPEDKLTTGQGLMQVDKAYEYLKQFQDYPCVFYQIKVNLSGKTIPTSRGIYLREGTACRQSTEWTIQVDPKFHEGASNLKELVPFEECLELHSTDEGVVRVPDYLLLTNNGRGFNVVVDPTNLGDGVHYFEVYGIDCKAPERGPLFRIPVTIIIPKTVANQPPVISFQQMSFISGHIERRYIEVPHGATWAEATMRTSGFDTTRRFYIDTLQVCPLRRPIKWESAPTFASPSAKSFVFPVVSGQTMELAIAQFWSSGLGSREPTIVDFEIEFHGVGVDKEELLLDGSEAPIKVEAEALLASEKLVPIAVLNKIRVPYQPIDAQLKTLSTGRDRLLSGKQILALTLTYKFKLEDSAEVKPYIPLLNNRIYDTKFESQFFMISDTNKRVYAMGDVYPESSKLPKGEYKLQLYLRHENVELLEKLKQLTVFIERNMGEIRLNLHSEPDGPFTGNGAFKSSVLMPGVKEAFYLGPPTKDKLPKNTPQGSMLVGEISYGKLSFDEKEGKNPKDNPVSYPISYVVPPNKPEEDKKAASAPTCSKSVSERLEQEVRDTKIKFLGNLKQETEEERSEWRKLCTCLKSEYPDYTPLLAKILEGLLSRSDAGDKISHHEEIIEAANEVVRSVDVDELARFLLDKTEPEDDEAEKLKKKMEVTRDQLADALYQKGLAMARIENLKGEKEGEGEEESSQKDKFEENFKELTKWVDVKSSKYGTLTVLREKRLSRLGTALKVLDDLIQNENETANKKLYELKLDLLEEIGWSHLVTYEKQWMQVRFPKSLPLF
Protein: 11S globulin seed storage protein 1 (11S legumin) (Allergen Car i 4) (Pec11S-1) (allergen Car i 4.0101) [Cleaved into: 11S globulin seed storage protein 1 acidic chain; 11S globulin seed storage protein 1 basic chain] (B5KVH4)
Organism: Carya illinoinensis (Pecan)
Function: Seed storage protein.
Interaction partners:
Sequence:
MAKPILLSIYLCLIIVALFNGCLAQSGGRQQHKFGQCQLNRLDALEPTNRIEAEAGVIESWDPNHQQLQCAGVAVVRRTIEPNGLLLPHYSNAPQLVYIARGRGITGVLFPGCPETFEESQRQSQQGQRREFQQDRHQKIRHFREGDIIAFPAGVAHWCYNDGSSPVVAIFLLDTHNNANQLDQNPRNFYLAGNPDDEFRPQGQQEYEQHRRQQQHQQRRGEHGEQQRDLGNNVFSGFDAEFLADAFNVDTETARRLQSENDHRGSIVRVEGRQLQVIRPRWSREEQEHEERKERERERESESERRQSRRGGRDDNGLEETICTLSLRENIGDPSRADIYTEEAGRISTVNSHNLPILRWLQLSAERGALYSDALYVPHWNLNAHSVVYALRGRAEVQVVDNFGQTVFDDELREGQLLTIPQNFAVVKRARDEGFEWVSFKTNENAMVSPLAGRTSAIRALPEEVLVNAFQIPREDARRLKFNRQESTLVRSRSRSSRSERRAEV
Protein: Interferon alpha-9 (IFN-alpha-9) (P09235)
Organism: Mus musculus (Mouse)
Function: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Subcellular location: Secreted.
Interaction partners:
- Interferon alpha/beta receptor 1
- Interferon 1ai2
- Interferon alpha-5
- Interferon alpha-12
- Interferon alpha-11
- Tyrosine-protein kinase JAK2
- Interferon regulatory factor 7
- Interferon regulatory factor 3
- Epidermal growth factor receptor
- Interferon alpha/beta receptor 2
Sequence:
MARPFAFLMVLVVISYWSTCSLGCDLPQTHNLRNKKILTLLAQMRRLSPLSCLKDRKDFGFPQEKVDAQQIQEAQAIPVLSELTQQILTLFTSKDSSAAWNATLLDSFCTGLHQLLNDLQGCLMQLVGMKELPLTQEDSQLAMKKYFHRITVYLREKKHSPCAWEVVRAEVWRALSSSVNLLARLSEEKE
Protein: Y+L amino acid transporter 2 (Solute carrier family 7 member 6) (y(+)L-type amino acid transporter 2) (Y+LAT2) (y+LAT-2) (Q8BGK6)
Organism: Mus musculus (Mouse)
Function: Heterodimer with SLC3A2, that functions as an antiporter which operates as an efflux route by exporting cationic amino acids such as L-arginine from inside the cells in exchange with neutral amino acids like L-leucine, L-glutamine and isoleucine, plus sodium ions and may participate in nitric oxide synthesis (By similarity). Also exchanges L-arginine with L-lysine in a sodium-independent manner (By similarity). The transport mechanism is electroneutral and operates with a stoichiometry of 1:1 (By similarity). Contributes to ammonia-induced increase of L-arginine uptake in cerebral cortical astrocytes leading to ammonia-dependent increase of nitric oxide (NO) production via inducible nitric oxide synthase (iNOS) induction, and protein nitration (By similarity). May mediate transport of ornithine in retinal pigment epithelial (RPE) cells (By similarity). May also transport glycine betaine in a sodium dependent manner from the cumulus granulosa into the enclosed oocyte.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q92536}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Amino acid transporter heavy chain SLC3A2
- Amino acid transporter heavy chain SLC3A1
- Large neutral amino acids transporter small subunit 4
- Large neutral amino acids transporter small subunit 3
- Sodium- and chloride-dependent neutral and basic amino acid transporter B
Sequence:
MEAQELGSPTPTYHLLPKANQHTVKEDAGSPSQGSPETMQLKKEISLLNGVSLVVGNMIGSGIFVSPKGVLKYTASYGLSLIVWAIGGLFSVVGALCYAELGTTITKSGASYAYILEAFGGFIAFIRLWVSLLIVEPTSQAIIAITFANYIIKPSFPTCDPPYVACRLLAAACVCLLTFVNCAYVKWGTRVQDTFTYAKVLALIAIIIMGLVKLCQGHTEHFQDAFKGSSWNVGDLSLALYSALFSYSGWDTLNFVTEEIKNPERNLPLAIGISMPIVTLIYILTNVAYYTVLNIQDVHKSDAVAVTFADQTFGMFSWTIPIAVALSCFGGLNASIFASSRLFFVGSREGHLPNLLSMIHIERFTPVPALLFNCTMTLIYLVVKDVFLLINYFSFSYWFFVGLSVVGQLYLRWKEPDWPRPLKLSLFFPIVFCVCSLFLVAVPLFSDTINSLIGIGIALSGVPVYFLGVYLPESRRPLFIRNVLATVTRVTQKLCFCVLTELDVTEEKNVERKTD
Protein: Sisters unbound (Q9VTM9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Sister chromatid cohesion protein solo
- Structural maintenance of chromosomes protein
- Crossover suppressor on 2 of manheim
Sequence:
MEFVSAISTVGNTETVAREFAIAFLQAVTSDPDNWIVKVSHQFVGQCFRVLGLNFNVSVQAFSQTQDHPYRDANPNYIFDPVPLVMTELDKFLDRLPRLLAQVGELLAKDSQGTRFDELTQPLPCYLNLILKWIKVVQAMCKNMQLSNSTSVDRYICEPLARMSFSILGGLAKLLPKYENFSGFKGICLALTVDVRYGIFYQETCDVVVPPMLDIFRKHYKTFCGPEKSALDFVYCILTVVMSEDDCYIKAYEFLESMIRQFAENSQHSHHLRCFTNELITVKYVVLQFETLKDSNSKPLLLATLKYLMTLQRNVASAECFTKRFHEELLHLVLRMSVSSATVASMAAKVYITLSQRQHQEQEIEQHILETYVKIPQNPRKNITYEQFRNELTRYLKTLIQYFPPLQEFDFYARVLTARNVRIELSLIAAQCASIIFEMHMAEYTSLPVARDQVNELLRVWSRILKASSKQNGTRPLIYSIYDLIDFDSVAECDADLLLNLESSCLENFLNDDTIIESEFQRLYVNISRSVGATGNIQIHTTTSRALRDEQAALQLRLNNTDPESPEMQQLLKEYAFSYMRIHAVLMVNKLHVRYVADIYETLAKFVLEMPTLNENITLYGSESLANMLVLLHGDLKDSDGEMIDKVSGLVKQLQDFCVSELRKEKLNLKRAKFFVCSTLIMHINQLPYLSLDSAAYDKILEVLTSPPRESPPELPSNTYVADMHYMFRLLIKTEEFDLPTNRVWKLLMKYKMSSIKCLDTEIEDLINVFIKYRIESYIHYMSVIQLHIYKDSNVNKKGSIALTAHLRLIDMNCSALDSWLLRYIIFKESLSLLIKNMRIRRSEVTNSSQRNRLLPLKYILNMVVNLRLDEAQFLSIAKLLHVLKDETIGPQENSEIENFITQISTYKYQAEDEHLEATKNEYYEGRLTPLPSGPLNLWQIKTIHNTTDLTD
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A0G2JTD8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}.
Interaction partners:
Sequence:
MSSRTALAPGNDRNSDTHGTLGSGRSSDKGPSWSSRSLGARCRNSIASCPEEQPHVGNYRLLRTIGKGNFAKVKLARHILTGREVAIKIIDKTQLNPSSLQKLFREVRIMKGLNHPNIVKLFEVIETEKTLYLVMEYASAGEVFDYLVSHGRMKEKEARAKFRQIVSAVHYCHQKNIVHRDLKAENLLLDAEANIKIADFGFSNEFTLGSKLDTFCGSPPYAAPELFQGKKYDGPEVDIWSLGVILYTLVSGSLPFDGHNLKELRERVLRGKYRVPFYMSTDCESILRRFLVLNPAKRCTLEQIMKDKWINIGYEGEELKPYTEPEEDFGDTKRIEVMVGMGYTREEIKEALTNQKYNEVTATYLLLGRKTEEGGDRGAPGLALARVRAPSDTTNGTSSSKGSSHNKGQRTSSSTYHRQRRHSDFCGPSPAPLHPKRSPTSTGDTELKEERLPGRKASCSAAGSGSRGLPPSSPMVSSAHNPNKAEIPERRKDSTSTPNNLPPSMMTRRNTYVCTERPGSERQSLLPNGKENSSGTSRVPPASPSSHSLAPPSGERSRLARGSTIRSTFHGGQVRDRRAGGGSGGGVQNGPPASPTLAHEAAPLPSGRPRPTTNLFTKLTSKLTRRVTDEPERIGGPEVTRDHVVDGLAFFQLLLHLHHKLYAIHHQLHLFDLGRAQPIGVGDVEHGAHRSGVHATCAGADITEALNKSRDAGTALCPTANASESRCSQVTGSHYWTLHAWTLG
Protein: Putative uncharacterized protein encoded by LINC00526 (Q96FQ7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSHSYKKAISDEALRPFQMDYFGGLPPGQYATRMTGQVHGSGCHLRSAPCDLGASQRKLSSNFSEIDAGLFSQGKSAAYTDIGATKPVEQRETAS
Protein: Cdc42 effector protein 2 (Binder of Rho GTPases 1) (Q8JZX9)
Organism: Mus musculus (Mouse)
Function: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner (By similarity).
Subcellular location: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Cdc42 effector protein 5
- Rho-related GTP-binding protein RhoQ
- Cell division control protein 42 homolog
Sequence:
MSTKVPIYLKRGSRKGKKEKLRDLLSSDMISPPLGDFRHTIHIGSGGGDDMFGDISFLQGKFHLLPGTAVEEAEEDGSFDLPFQFTRTTTVCGRELPDGLSPLLKNAISLPVIGGPQALTLPTAQAPPKPPRLHLESPQPSPQPSPQGAGNVDVWRIPEAGSPHNGMSPEPEAEEPFLSHASSLLSLHVDLGPSILDDVLQIMDHDLGRVQIPT
Protein: Sucrose transport protein SUT1 (Sucrose permease 1) (Sucrose transporter 1) (OsSUT1) (Sucrose-proton symporter 1) (Q10R54)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Responsible for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). Can also transport other glucosides such as maltose, salicin, helicin, and alpha-phenylglucoside. Probably required for apoplastic phloem sucrose loading in source tissues (e.g. leaves) in order to transport it to sink tissues (e.g. roots, flowers). Probably not involved in transport of sugars across the symplastic discontinuity between the endosperm and the embryo. Essential for normal pollen germination, but not for pollen maturation or starch accumulation in pollen.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MARGSGAGGGGGGGGGGLELSVGVGGGGGARGGGGGEAAAAVETAAPISLGRLILSGMVAGGVQYGWALQLSLLTPYVQTLGLSHALTSFMWLCGPIAGMVVQPCVGLYSDRCTSKWGRRRPYILTGCVLICLAVVVIGFSADIGYAMGDTKEDCSVYHGSRWHAAIVYVLGFWLLDFSNNTVQGPARALMADLSGRHGPGTANSIFCSWMAMGNILGYSSGSTNNWHKWFPFLKTRACCEACANLKGAFLVAVIFLSLCLVITLIFAKEVPFKGNAALPTKSNEPAEPEGTGPLAVLKGFRNLPTGMPSVLIVTGLTWLSWFPFILYDTDWMGREIYHGDPKGTDPQIEAFNQGVRAGAFGLLLNSIVLGFSSFLIEPMCRKVGPRVVWVTSNFLVCIAMAATALISFWSLKDFHGTVQKAITADKSIKAVCLVLFAFLGVPLAVLYSVPFAVTAQLAATRGGGQGLCTGVLNISIVIPQVVIALGAGPWDELFGKGNIPAFGLASGFALIGGVAGIFLLPKISKRQFRSVSMGGGH
Protein: Cabut (Q4R0P9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDMDTLLPSPPATPPLRENKLEIVAKDEQQVNENLLKAKLKLVAQKSQKNGGIITPNPSDTEDEAPEIAVPNKKPRLEQPAMSMTPPPDQKLDDDQKAERVSVIMRVNSSGAVSSSSQDENSSSSTSCCSSSSNTNTSTSSVPPTVEDDYPEANVWRNLKFKMNRKRAAEVALPPVQTPETPVAKLVAPPAPAECIKEEEIKPILTPIYVSPVASSASQLILLSTVAAQQSPTPVPKTPTMSEEKLTTRITAAQAAATRSRIYECSFPDCGKNYFKSSHLKAHQRVHTGERPFICKWENCDKRFSRSDELSRHKRTHTGEKKFQCSVCQKKFMRSDHLSKHVKRHNKDKANGVNRHVSLANNNTSASVAASLCDASLHLRAIAPAGSSDSSSPISSASLQVYSAQDLLRLQQQASSFTFGGTLLQVQR
Protein: Rho-GAP domain-containing protein (D3YT54)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MERLEARSASIGEALGKHGISLKSASVGSASERNGSFTTENGGSQNHHLLEERRSKARRIGGIVTKSPDDRPRPKLFGGSLDEYVEATGEEIPLLVQSAIAYLSRYSLRNQGLFRVSGSQSEINRFREAYERGEDLFQYLDDGSDANSAAGVLKLYFRELREPIFPIFMFEQFCDCAKSESPTEFVRRARELVSKLPVSHVLLLRFLFAFLSHLCEFADENMMEPHNLAICFGPTLLPIPEGKDQVFYHNYVNELVRNLIIHADDVFPRDLAGPVYDKYAMQRYMDGNFIEENDLISEDDEAHEKLSLPPSRHMMIDSTYESADRILLSSPILSQANTSTPNGISPSNGAESSTHNEIDYAPIASSRSSNRSKASGSIDLAMRSEMPHRIANELNNIFKNSSLSSEGSKGISVLRHSHVEPSWTDNREHLNMRSMSTDPDEEREYVSPPPPLLSTKYVSAASCSISPAPRTIDIKERKDSRDLLYAPITRATTVPANSGSNTEMNSTGVRPIGKSSLRDQLQLMRKENSTEMKPSTSLNGSTKKLDSETTILDARSTDKSTESSRRTSLEDDKSPEPFAQPDIINSARPRGKSPTLDDILNSLKVATSISP
Protein: Phosphatidylinositol 4-kinase type 2-alpha (EC 2.7.1.67) (55 kDa type II phosphatidylinositol 4-kinase) (Phosphatidylinositol 4-kinase type II-alpha) (Q99M64)
Organism: Rattus norvegicus (Rat)
Function: Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9BTU6}; Lipid-anchor {ECO:0000250|UniProtKB:Q9BTU6}. Membrane raft {ECO:0000250|UniProtKB:Q9BTU6}. Endosome {ECO:0000269|PubMed:21998198}. Endosome membrane {ECO:0000250|UniProtKB:Q9BTU6}. Cytoplasmic vesicle {ECO:0000269|PubMed:21998198}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q2TBE6}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q2TBE6}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q2TBE6}. Mitochondrion {ECO:0000250|UniProtKB:Q2TBE6}. Membrane {ECO:0000269|PubMed:11244087}; Lipid-anchor {ECO:0000269|PubMed:11244087}. Cell membrane {ECO:0000250|UniProtKB:Q9BTU6}. Perikaryon {ECO:0000250|UniProtKB:Q2TBE6}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q2TBE6}. Note=Found in subdomains of the plasma membrane termed non-caveolar membrane rafts. Transported from neuronal cell body to neuron projections and neurite tips in a BLOC-1- and AP-3-complexes-dependent manner. {ECO:0000250|UniProtKB:Q2TBE6}.
Interaction partners:
- Phosphatidylinositol 4-kinase alpha
- Phosphatidylinositol 4-kinase beta
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol-3-phosphatase SAC1
- Phosphatidylinositol 3-kinase catalytic subunit type 3
Sequence:
MDETSPLVSPERAQPPEYTFPSVSGAHFPQVPGGAVRVAAAGSGPSPPCSPGHDRERQPLLDRARGAAAQGQTHTVAAQAQALAAQAAVAVHAVQTHRERNDFPEDPEFEVVVRQAEIAIECSIYPERIYQGSSGSYFVKDSQGRIIAVFKPKNEEPYGNLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFNRIGLPPKVGSFQLFVEGYKDADYWLRRFEAEPLPENTNRQLLLQFERLVVLDYIIRNTDRGNDNWLIKYDYPMDNPNCRDTDWVMVREPVIKVAAIDNGLAFPLKHPDSWRAYPFYWAWLPQAKVPFSQEIKDLILPKISDPNFVKDLEEDLYELFKKDPGFDRGQFHKQIAVMRGQILNLTQALKDNKSPLHLVQMPPVIVETARSHQRSSSESYTQSFQSRKPFFSWW
Protein: Deoxyribonuclease-2 (EC 3.1.22.1) (Deoxyribonuclease II) (DNase II) (Q17778)
Organism: Caenorhabditis elegans
Function: Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Implicated in apoptosis.
Interaction partners:
- Cell-death-related nuclease 7
- Cell death-related nuclease 6
- Exosome complex component RRP46 homolog
Sequence:
MGLSPAAVLIFLLLGVSQTYAAFSCKDQSGNDVDWFAVYKMPIEKDDGSVTGLAGGVAWYYVDVNKKGTLTPSAKTLDDNDQAIAYTLQQYYDKQNDKTIFHVMYNDEPWGSKSTSGIKLEEILSNRVYSNYTHEDDSTSTAFGHTKGTIFFDGTSGVWLVHSVPLFPNPTKYEYPVSGHDYGQTMLCMTFKYAQLKSIGTQLFFNRPNIYSSNLPTNMAADNADLAKAIAGQYQKGQPFQSVIELETMAGYSFTNFAKSKEFNADLYDTLVAPTLKTDLVVETWRRGSEIPLDCKLTYHANDALSIHVGSTTAFSYTKDHSKMAHSADMTKPWVCIGDINRMTSQYVRGGGTTCISSSFLWKAYSVIATQNNCA
Protein: Distal tail protein pb9 (DTP-pb9) (Dit) (Tail protein pb9) (Q6QGE8)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Distal tail protein which forms a hexameric ring located at the tail tube end.
Subcellular location: Virion {ECO:0000269|PubMed:36961893}. Note=Component of the tail (PubMed:24198424, PubMed:36961893). Located between the baseplate tube protein p140, the collar protein p132 ring and the baseplate hub protein pb3 trimer (PubMed:36961893). {ECO:0000269|PubMed:24198424, ECO:0000269|PubMed:36961893}.
Interaction partners:
Sequence:
MRLPDPYTNPEYPGLGFESVNLVDNDPMIRDELPNGKVKEVKISAQYWGINISYPELFPDEYAFLDSRLLEYKRTGDYLDVLLPQYEAFRVRGDTKSVTIPAGQKGSQIILNTNGTLTGQPKAGDLFKLSTHPKVYKITNFSSSGNVWNISLYPDLFITTTGSEKPVFNGILFRTKLMNGDSFGSTLNNNGTYSGISLSLRESL
Protein: Cadherin domain-containing protein (Q3UTP0)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MYLSICCCFLLWAPALTLKNLNYSVPEEQGAGTVIGNIGKDARLQPGLPPAERGSGSGRSKSGSYRVLENSAPHLLDVDADSGLLYTKQRIDRESLCRHNAKCQLSLEVFANDKEICMIKVEIQDINDNAPSFPSDQIEMDISENAAPGTRFPLTSAHDPDAGENGLRTYLLTRDDHGLFALDVKSRGDGTKFPELVIQKALDRELQNHHTLVLTALDGGEPPRSATVQINVKVIDSNDNSPVFEAPSYLVELPENAPLGTVVIDLNATDADEGPNGEVLYSFSSYVPDRVRELFSIDPKTGLIRVKGNLDYEENGMLEIDVQARDLGPNPIPAHCKVTVKLIDRNDNAPSIGFVSVRQGALSEAAPPGTVIALVRVTDRDSGKNGQLQCRVLGGGGTGGGLGGPGSVPFKLEENYDNFYTVVTDRPLDRETQDEYNVTIVARDGGSPPLNSTKSFAVKILDENDNPPRFTKGLYVLQVHENNIPGEYLGSVLAQDPDLGQNGTVSYSILPSHIGDVSIYTYVSVNPTNGAIYALRSFNYEQTKAFEFKVLAKDSGAPAHLESNATVRVTVLDVNDNAPVIVLPTLQNDTAELQVPRNAGLGYLVSTVRALDSDFGESGRLTYEIVDGNDDHLFEIDPSSGEIRTLHPFWEDVTPVVELVVKVTDHGKPTLSAVAKLIIRSVSGSLPEGVPRVNGEQHHWDMSLPLIVTLSTISIILLAAMITIAVKCKRENKEIRTYNCRIAEYSHPQLGGGKG
Protein: Csl4 (RE36848p) (Q9VKJ4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- FI01414p
- Exosome complex exonuclease RRP44
- FI07225p
- Exosome complex component RRP4
- Ribosomal RNA-processing protein 42
- Exosome complex component RRP45
- Nuclear nucleic acid-binding protein C1D
- Exosome complex component 10 homolog
- FI06805p
- Combover, isoform A
Sequence:
MSEQQDETVVCLPGERLCRTEDSIVLGIGTYEQNGYIYASKSGIVNIEDSGDKCQVVSVHKPGFHLTIPATGDVVTARVLVTTPKFAKCAIFCVRNVLLESSYRGLLRKEDVRETEKDRVDIYKSFRPGDVILARVINQLEQSFLLTTAENELGVVIAYASDYRKTRVPMVPVGWSEMQCPQTTIKEPRKVAKVLPESSINAVK
Protein: Enoyl-[acyl-carrier-protein] reductase, mitochondrial (EC 1.3.1.104) (2-enoyl thioester reductase) (Nuclear receptor-binding factor 1) (HsNrbf-1) (NRBF-1) (Q9BV79)
Organism: Homo sapiens (Human)
Function: Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Displays a preference for medium-chain over short- and long-chain substrates. May provide the octanoyl chain used for lipoic acid biosynthesis, regulating protein lipoylation and mitochondrial respiratory activity particularly in Purkinje cells (By similarity).
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:12654921, ECO:0000269|PubMed:37653044}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:25031892}. Nucleus {ECO:0000269|PubMed:25031892}.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Fatty acid synthase
- Hydroxyacyl-thioester dehydratase type 2, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 3
- Trifunctional enzyme subunit alpha, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MWVCSTLWRVRTPARQWRGLLPASGCHGPAASSYSASAEPARVRALVYGHHGDPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEEELRRPEMKNFFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEASMKPFISSKQILTM
Protein: Peroxisomal membrane protein PEX14 (Peroxin-14) (Peroxisomal membrane protein PER10) (P78723)
Organism: Pichia angusta (Yeast) (Hansenula polymorpha)
Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:9009266}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53112}; Cytoplasmic side {ECO:0000250|UniProtKB:P53112}.
Interaction partners:
Sequence:
MSQQPATTSRAELVSSAVEFLLDQSIADSPLAKKVEFLESKGLTQQEIEEALQKARTGTVQASPSQQSVVPPRPPVPDYYPSAPPLPERDWKDYFIMATATAGISYGVYQFVKRYVVPKILPPSKTQLEQDKAAIDHEFQRVESLLEKFEADQKEFYQKQEAKSKKIDETLQEVDEIINKTNEKNLNNEETLKYLKLEIENIKTTLLKTLDSQKATLNAELSAMEKQLQDIKFDIKTSGIAVAPQLSTPPSESTSRQSPAAEAKPKINLNIPPTTSIPSLRDVLSREKDKDVNSDSIAQYEQRTANEKDVERSIPAWQLSASNGGSSTTSGVAGDEQKEPKRGIPAWQLNA
Protein: Telomere-binding protein 1 (Protein RTBP1) (Q9LL45)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Binds the telomeric double-stranded 5'TTTAGGG-3' repeat and regulates telomere length and structure.
Subcellular location: Chromosome, telomere {ECO:0000305}.
Interaction partners:
- Os04g0589400 protein
Sequence:
MVLQKRLDYGSHGHRAPIKPRVATLAPVKRSTRIRKKQMYALDLLATAAEKLLADQDNLSSGPNINETPEGYVTSMKPVKAEQFDEAFPLRSVAVKKDDCKGCTVGCAGICGFLRQANMCLAENSSTQNLADSVLESLTAKPDVLAKDSFVSSKKSCRLGFGLGTIPEYGSVGVCQPWSTRSAEVKQVHRARPTAIRSQEDSDAAALCALVETMDLDTKPLAEASSGSNSGVHICGPDRGHNSHPSCLAKVQHAADRDDDENSSGCVHPSTSGNNRGYIPHYIGDRRIRRLFASRLRKAARNRICGEMSCKGNKLSLCEKKMPTTRRRVQQTTLKRKRLAQLYSEKSSDEVKLTIKSFNIPELLIEIPENATVGSLKKTVSDAVTTIIERGLRVGILLQGKNIQNDNKTLRQAGICRGKKLNDIGFTLECEAGQDSHPGVIVPEEMDFVGASVVDKSATVKCEEPAENQQLMQDFPGCSLSDPGSVDYPVEWSTQETSASSQAIVPFADPNSLALANVPLSRSKRPDFGQRRIRRPFTVAEVELLVEAVEHLGTGRWRDVKFRAFENVHHRTYVDLKDKWKTLVHTASIAPQQRRGAPVPQELLDRVLAAQAYWSEQQAKLHGDPPVPEICPT