wanglab/gogpt-training-data huggingface dataset:
Protein: Signal recognition particle subunit SRP54 (EC 3.6.5.4) (Signal recognition particle 54 kDa protein) (P61011)
Organism: Homo sapiens (Human)
Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane. Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes. Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA. Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA. SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER. Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA (By similarity). Plays a role in proliferation and differentiation of granulocytic cells, neutrophils migration capacity and exocrine pancreas development.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:14729963}. Cytoplasm {ECO:0000269|PubMed:14729963, ECO:0000269|PubMed:29914977}. Endoplasmic reticulum {ECO:0000269|PubMed:29914977}.
Interaction partners:
- Signal recognition particle 14 kDa protein
- Signal recognition particle receptor subunit alpha
- Large ribosomal subunit protein uL23
- Signal recognition particle 9 kDa protein
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP68
- Signal recognition particle 19 kDa protein
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL18
Sequence:
MVLADLGRKITSALRSLSNATIINEEVLNAMLKEVCTALLEADVNIKLVKQLRENVKSAIDLEEMASGLNKRKMIQHAVFKELVKLVDPGVKAWTPTKGKQNVIMFVGLQGSGKTTTCSKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIASEGVEKFKNENFEIIIVDTSGRHKQEDSLFEEMLQVANAIQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNELKLDDNEALIEKLKHGQFTLRDMYEQFQNIMKMGPFSQILGMIPGFGTDFMSKGNEQESMARLKKLMTIMDSMNDQELDSTDGAKVFSKQPGRIQRVARGSGVSTRDVQELLTQYTKFAQMVKKMGGIKGLFKGGDMSKNVSQSQMAKLNQQMAKMMDPRVLHHMGGMAGLQSMMRQFQQGAAGNMKGMMGFNNM
Protein: Glutamate receptor 1.2 (Ligand-gated ion channel 1.2) (Q9LV72)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glutamate-gated receptor that probably acts as non-selective cation channel. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Nonsense-mediated mRNA decay-like protein
- Putative cyclic nucleotide-gated ion channel 7
- Mechanosensitive ion channel protein 8
- AGAMOUS-like 41
- Cyclic nucleotide-gated ion channel 18
- Probable LRR receptor-like serine/threonine-protein kinase At5g37450
- Nucleobase-ascorbate transporter 6
- Beta-galactosidase 15
- Serine racemase
Sequence:
MVRICIQTPILLSFLLVLLFFISNCFASSQNNDDDKRIRVRVGLVLDLGSVEGKIVRSSVSMALSDFYDNHNDYKTRLSLLVRDSHGEPLLALDSVVDLLQTEGVQAIIGGNSLLEAKLLAELGEKARVPVISLNSPMSLSLSKYTHLIQATHNSASEVKGITAFLHGFDWNSVALVLEDHDDWRESMHFMVDHFHENNVHVQSKVAFSVTSSEDSLMDRLRELKDLGTTVFVVHLSEVIATRLFPCAEKLGMMGEGFAWILTSRSMSSFHDQFIDDLTKEAMEGVVGFKSYIPMSKELHNFTLRWRKTLPVEEVTGSEITRLSISGVWAHDVAWSLASAAEVTRMPTVTSTLLEAIKESRFKGLSGNFQLDDMKLLSDKFEIVNMIGSGERRVGFWNSNGSFSNRRQLSSTHDNLETIIWPGGSAQSPKGRSLRESGRKKLRVLVTSSNRFPRLMKVETDPITHEITIVEGFCIEVFQASIAPFNYEVEYIRWLNGTNYTKLAYALHSQKDKYDAAVGDITITSDRSMYVDFTLPYTEMGLGIVAAKERSMWVFFQPLTPNLWITSAAFFVLTGIIVWLIERAENKEFQGSWPQQIGVVIWFGFSTLVYAHREKLQHNLSRFVVTVWVFAVLILVTSYTATLTSMMTVQQIRFNANEDYVGHLSGSLIANAALTNSSLRAMRLLGLNTSEDYAQALMNKSVSYIVSELPYLKILLGENPGHFLMVKTQSTTNGFGFMFQKGSELAPNVSREIAKLRTSERLNEMERRWFDKQLPYTTDDTSNPITLYRFRGLFMITGVSFAFALAVLLILWLRERWEILVNSVNIYFSQRLRHFRILFTRTIHPSPLGLDNPIGENAVQMAQRNRR
Protein: ATP synthase F(0) complex subunit C2, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase membrane subunit c locus 2) (ATP synthase proteolipid P2) (ATPase protein 9) (ATPase subunit c) (P07926)
Organism: Bos taurus (Bovine)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
Subcellular location: Mitochondrion membrane; Multi-pass membrane protein.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MYTCAKFVSTPSLIRRTSTVLSRSLSAVVVRRPETLTDESHSSLAVVPRPLTTSLTPSRSFQTSAISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM
Protein: Interleukin-1 beta (IL-1 beta) (Q63264)
Organism: Rattus norvegicus (Rat)
Function: Potent pro-inflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P01584}. Secreted {ECO:0000250|UniProtKB:P01584}. Lysosome {ECO:0000250|UniProtKB:P01584}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P10749}. Note=The precursor is cytosolic. In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted. Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1 during maturation. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10. {ECO:0000250|UniProtKB:P01584}.
Interaction partners:
- Interleukin-1 receptor type 1
- Interleukin-1 alpha
- Interleukin-1 receptor type 2
- Caspase-1
- Interleukin-1 receptor accessory protein
- Interferon gamma
- NACHT, LRR and PYD domains-containing protein 3
- Granulocyte-macrophage colony-stimulating factor
- Interleukin-2
- Interleukin-5
Sequence:
MATVPELNCEIAAFDSEENDLFFEADRPQKIKDCFQALDLGCPDESIQLQISQQHLDKSFRKAVSLIVAVEKLWQLPMSCPWSFQDEDPSTFFSFIFEEEPVLCDSWDDDDLLVCDVPIRQLHCRLRDEQQKCLVLSDPCELKALHLNGQNISQQVVFSMSFVQGETSNDKIPVALGLKGLNLYLSCVMKDGTPTLQLESVDPKQYPKKKMEKRFVFNKIEVKTKVEFESAQFPNWYISTSQAEHRPVFLGNSNGRDIVDFTMEPVSS
Protein: Peroxynitrite isomerase 2 (EC 5.99.-.-) (Ferric nitrobindin) (Nb(III)) (P9WFG9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate. Therefore, this protein likely plays a role in peroxynitrite sensing and in the detoxification of reactive nitrogen and oxygen species (RNS and ROS, respectively). Is able to bind nitric oxide (NO) in vitro, but may act as a sensor of peroxynitrite levels in vivo.
Interaction partners:
- Heparin-binding hemagglutinin
- Conserved protein
- Conserved protein
Sequence:
MSSGAGSDATGAGGVHAAGSGDRAVAAAVERAKATAARNIPAFDDLPVPADTANLREGADLNNALLALLPLVGVWRGEGEGRGPDGDYRFGQQIVVSHDGGDYLNWESRSWRLTATGDYQEPGLREAGFWRFVADPYDPSESQAIELLLAHSAGYVELFYGRPRTQSSWELVTDALARSRSGVLVGGAKRLYGIVEGGDLAYVEERVDADGGLVPHLSARLSRFVG
Protein: FERM domain-containing protein 1 (Q8N878)
Organism: Homo sapiens (Human)
Interaction partners:
- FERM domain-containing protein 6
- Protein KIBRA
- Merlin
Sequence:
MAVPPRGRGIDPARTNPDTFPPSGARCMEPSPERPACSQQEPTLGMDAMASEHRDVLVLLPSREQLRLAVGVKATGRELFQQVCNVASIRDAQFFGLCVVRNNEYIFMDLEQKLSKYFSKDWKKERNEGNEKPRAPFVAFLRVQHYVENGRVISDHRARHLYYCHLKERVLRSQCAHREEAYFLLAACALQADLGEHRESAHAGRYFEPHSYFPQWIITKRGIDYILRHMPTLHRERQGLSPKEAMLCFIQEACRLEDVPVHFFRLHKDKKEGRPTVILGLALRGVHIYQGKKLEIQLDGLPAAQKLVYYTGCTWRSRHLLHLLRASHQLHLRVRPTLQQLRQREEAEEKQHYRESYISDELELDLASRSFPGSGVSSQHCPHCLSRHSADSHGSSYTSGIKANSWLRESREMSVDVPLEVHGLHEKEPSSSPRTSRSHPSTRGDSQATRQEPCTQVRTRGQSAEAVHQIQEMTAGVSEEQHSHGLDDMQLHQLALHPAPTSLSHTFHRALDCRLAGPCETRATLPSKRSSNCLALDLFGEAPPQEFVV
Protein: Site-specific recombinase, phage integrase family (Q5LLE0)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Interaction partners:
Sequence:
MKRKLTTKFIESQKPNPSKRLDFRDELMPGLVLRISTSGTKTFCLHKRISGKMRRLTIGRFGVVSLAEARERVRKVLYEIETGRFEDRTGVEVETKPTLGDVIPDYIEKHAKVHNRDWKRKEALLAKFAALHVKRIDEIKRADVVKACDLIHKSAPVSANRALAHLKHLMGWCVERGMIDASPIAGMKPLSKERSRERVLTDDELGALWTACDAEGYPFGDCMKLLILSGQRRAEVAEMRWTELDLEKRLWTLPSQRAKNGRQHTVPITDAMIDVLRRVPRFLGSDYVFTTTGKSPVSGFGRLKDRLDKALPEGTEPWIIHDLRRTMSTNMAMLGVPQPVTEALLNHKTGVVSGVAAIYNVYSYTDEKCEALEQWNRHLTKMTQGHSDRLAGKMSAQFSA
Protein: High affinity immunoglobulin epsilon receptor subunit beta (FcERI) (Fc epsilon receptor I beta-chain) (IgE Fc receptor subunit beta) (Membrane-spanning 4-domains subfamily A member 2) (P13386)
Organism: Rattus norvegicus (Rat)
Function: High affinity receptor that binds to the Fc region of immunoglobulins epsilon. Aggregation of FCER1 by multivalent antigens is required for the full mast cell response, including the release of preformed mediators (such as histamine) by degranulation and de novo production of lipid mediators and cytokines. Also mediates the secretion of important lymphokines. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators responsible for the manifestations of allergy.
Subcellular location: Membrane {ECO:0000269|PubMed:21746961}; Multi-pass membrane protein {ECO:0000269|PubMed:21746961}.
Interaction partners:
- High affinity immunoglobulin epsilon receptor subunit alpha
- High affinity immunoglobulin epsilon receptor subunit gamma
- Tyrosine-protein kinase Lyn
- Tyrosine-protein kinase SYK
- Ig-like domain-containing protein.
- Tyrosine-protein kinase Fyn
- Mast cell carboxypeptidase A
- Fc of IgG, low affinity IIIa, receptor.
- T-cell surface glycoprotein CD3 zeta chain
- Solute carrier family 45, member 3
Sequence:
MDTENKSRADLALPNPQESPSAPDIELLEASPPAKALPEKPASPPPQQTWQSFLKKELEFLGVTQVLVGLICLCFGTVVCSTLQTSDFDDEVLLLYRAGYPFWGAVLFVLSGFLSIMSERKNTLYLVRGSLGANIVSSIAAGLGIAILILNLSNNSAYMNYCKDITEDDGCFVTSFITELVLMLLFLTILAFCSAVLLIIYRIGQEFERSKVPDDRLYEELHVYSPIYSALEDTREASAPVVS
Protein: Stall, isoform C (Stall, isoform E (EC 3.4.24.-)) (Q9W1Z6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTVAAIGSNRHRRLALIVLTTLWLLIGASSSSSSTSSTNPKSVNIELRRKRSLHYNGIELDKNTLVGHLREHERALIFGSRSPEEAPEFKLVHLAQQRPEEQQRLEERKRPGEAEQHGGNPHQRRQRRSLPSEDGNGPLPPEEEEQEAGEDVEARLQLQQSPQLIDDAFIFIRRTENGTQFVEHSPQLLKRLERCFYRSPAAALDLCEPGNVRGVFQQNGSDLVIHPLPARFGTGTHVLYQARVDKSGGGYSEASSRRTASPLDSQLQFEPDAEEFNEPRRRLRAQSQLQSPLRLRFQPRHHHPHQHHQQRRRRYIGDAPRSRWSDIPEELFIETAIFVDSDLYAHMQKNFPTNTESKVVSFLLAMINGVQLLYHHPTLGRRINFVLKRLEIWKSWDPPGLVRSRDVENYLNSFCKWQEKLNPFSDADPLHYDHALVLTGLDLVTYDKGKANSQVVGMATVKGMCTSIYSCTINEAKHFESVFVVAHEIGHNLGMRHDAKEISCDPTMHIMSPKLGSGKVTWSKCSRTYLEDFLMDPQAECLFDRDSFAGPWDHTAGGRLPGERFNANQQCMLRFGKNFMQASTQSKMEICRDLHCRQDGLPWTSHPALEGTECGPNMWCRGGTCEARSSKQGSYSALKSWPPEHIPEATHEKIIRHEPNRIPPLLHDYNPMDNELPGSPSNWGEWSEPSACESGCLYGQSRRLLEGSTGLRTLNRSCLNFPSRCIGRDRRFVTCNTPQCHKVPVQTINDFATQVCMQARKSDPELTGEGQQLPSTLDASCKIFCRTRTNGTKSRRWTFPDGTTCKAKQHNPEDITYCISGRCERFSCDNSTSNFFKMDSSFCEARSVRPTRDSSDQESRQQTNRQRYAERQEGKPQKNHYENEVAKRPSYGQGNHINAPASPYKRRNYHKPYPPEIPRPPPPASASLIALDRSSSSESEWVAHPGCHSNCMTDSKGVQGVTSRLTGVESIQLCSYRIQPCERLQTAAEYAEQTCARYRQKVRGLSGHGAQISASIDEPDRSCRVGCQDEFIKYRYYLVNGRNGHFPPGTRCSPVGKRYCVYGRCLEFGDDDLPLDKTHISLGQLRTRRKRSSISNDLFNITEIFIKPSHSDISAENIEFTQPIHVSADELSSKSR
Protein: Negative regulator of sexual conjugation and meiosis (EC 2.7.11.1) (P08092)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: This protein is a negative regulator of both sexual conjugation and meiosis. It phosphorylates mei2. It blocks the onset of meiosis until conjugation takes place.
Interaction partners:
- Meiosis protein mei2
- Meiosis inducing protein mei3
- Transcription factor ste11
- DNA repair protein rhp51
- Meiotic recombination protein rec12
- Cyclin puc1
- Meiosis-specific transcription factor mei4
- M-phase inducer phosphatase
- Checkpoint signal transducer rad24
- Cell division cycle-related protein res1/sct1
Sequence:
MMRENPELLLGQVLGDSLRFVSIIGAGAYGVVYKAEDIYDGTLYAVKALCKDGLNEKQKKLQARELALHARVSSHPYIITLHRVLETEDAIYVVLQYCPNGDLFTYITEKKVYQGNSHLIKTVFLQLISAVEHCHSVGIYHRDLKPENIMVGNDVNTVYLADFGLATTEPYSSDFGCGSLFYMSPECQREVKKLSSLSDMLPVTPEPIESQSSSFATAPNDVWALGIILINLCCKRNPWKRACSQTDGTYRSYVHNPSTLLSILPISRELNSLLNRIFDRNPKTRITLPELSTLVSNCKNLTRRLRPAPLVSSRYLAYQQQQQQQQMNLQQGIQGYPHQGYMPTQNIGFPWPPTPQFVSNWNHCATPTIPVSLQVLTPNSSLKVDPTTPLTAPIHATESFWPSAAAAAAAVHNNANSYMPITPTPYPNNAKIFGYPNQPPLTPIPFTGFVLHPAPVGRAADAVDPSRKSL
Protein: adenylate cyclase (EC 4.6.1.1) (O16880)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit
- Guanine nucleotide-binding protein G
- cAMP-dependent protein kinase regulatory subunit
Sequence:
MSTVMEMSTTRAEIRSVLVKHWRSLDKARLHTIHLWLLLYAAAQIFIEYYFSEVYAVLMLEADDRPQSKENHEKVKKWSPFCFYASIFFIAYLILTCFAIRIRQPKEGMGLVLVSLSLCVLLPAFSWILHLPVVIFVSRERIHTNEHDHSALYTSLCIASVIQFFILPRHRRIFFVVAVSWIVANFLLIVAINWDALNVNTLFMCSCLSLFLHQGVIALVGVVADSNEAGNRAEIARKLTEAVYRRTELETLKDRQEQLLLSVIPAYLADQVSKSIIQSSSTGSTVEVPRTGKNNTKNHKLFHDLHVQVHDNVSILFADIVNFTVLAAQLTAKDLVRTLNELYSKFDRDAQRLQCMRIKFLGDCYYCVSGMPVNRPNHADMCVVMGLEMINTIKQVRIATGVDVNMRIGVHTGSVLCGIMGLRKWQFDIWSDDVTLANHMESAGVPGAVHITKSTKDMLLGDYCIVDANTDDPHVVSYGQPTYHILPDKTSAIERTASIYRNSRLSTSPALQSRMSMKAKVSKMVEFWGAETPFANFTKKKFSASHDPALITDEIARRPTYINTIPSMTLIENNLTNFSFNNINSMFNCELPTIPASPKLLWPFSRKSITCNLSDCVLLTFVCIPSAFANLLLCSLYCPSDVLQQISLQQFFTIIGLAMLSLLGRVCSYAGPLITMVAFLLSSCIPIGPHIIIKKSKLEGVMAFNSLIFLPSCVSHLVSVFILYRLPYSHRCFLFFADFVIFQVLLSLFPAYGAEVYVGYMGYHLSVVSISLSLLVVLLFFIDWITNYERKRESACHVSFQNEERDVETMQDINKILIENILPSSVAAKFLSPDRAVNELYARQHENVCVMFASIPNFKDFWSEWDTNRKLECLRLLNEIVCEFDKLLSKPKFSSVEKIKTVGSTYMAAAGLNESEADYDDIYLEKQNSGKYNNNIRHGNMAFRNANLMIEFALAMSQILDALNRDSFQNFELRIGMSVGPLVAGVIGAQKPQYDIWGNTVNLASRMDTHGEPRKIHATTDMGRVLQTGGYRVQSRGKIRVKGVKEPMETFLIEVDSKRNSSVSGEQQNHSNNNNCHSTL
Protein: Electron transfer flavoprotein beta subunit lysine methyltransferase (EC 2.1.1.-) (ETFB lysine methyltransferase) (ETFB-KMT) (Protein N-lysine methyltransferase METTL20) (Q8IXQ9)
Organism: Homo sapiens (Human)
Function: Protein-lysine methyltransferase that selectively trimethylates the flavoprotein ETFB in mitochondria. Thereby, may negatively regulate the function of ETFB in electron transfer from Acyl-CoA dehydrogenases to the main respiratory chain.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23349634}. Mitochondrion matrix {ECO:0000269|PubMed:25023281, ECO:0000305|PubMed:25416781}. Note=Concentrated in cytoplasmic granular foci. {ECO:0000269|PubMed:23349634}.
Interaction partners:
- Electron transfer flavoprotein subunit beta
- Methyltransferase-like protein 22
- EEF1A lysine methyltransferase 2
- Protein N-lysine methyltransferase METTL21A
Sequence:
MALSLGWKAHRNHCGLLLQALRSSGLLLFPCGQCPWRGAGSFLDPEIKAFLEENTEVTSSGSLTPEIQLRLLTPRCKFWWERADLWPHSDPYWAIYWPGGQALSRYLLDNPDVVRGKSVLDLGSGCGATAIAAKMSGASRILANDIDPIAGMAITLNCELNRLNPFPILIQNILNLEQDKWDLVVLGDMFYDEDLADSLHQWLKKCFWTYRTRVLIGDPGRPQFSGHSIQHHLHKVVEYSLLESTRQENSGLTTSTVWGFQP
Protein: DUF2304 domain-containing protein (O06375)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MNWIQVLLIASIIGLLFYLLRSRRSARSRAWVKVGYVLFVLAGIYAVLRPDDTTVVANWFGVRRGTDLMLYALVMAFSFTTLSTYMRFKDLELRYARIARALALEGAQAPEQCR
Protein: Xyloglucan endotransglucosylase/hydrolase protein 9 (At-XTH9) (XTH-9) (EC 2.4.1.207) (Q8LDW9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues. Involved in internodal cell elongation.
Subcellular location: Secreted, cell wall {ECO:0000305}. Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Expansin-B3
- Expansin-B1
- Dof zinc finger protein DOF5.4
Sequence:
MVGMDLFKCVMMIMVLVVSCGEAVSGAKFDELYRSSWAMDHCVNEGEVTKLKLDNYSGAGFESRSKYLFGKVSIQIKLVEGDSAGTVTAFYMSSDGPNHNEFDFEFLGNTTGEPYIVQTNIYVNGVGNREQRLNLWFDPTTEFHTYSILWSKRSVVFMVDETPIRVQKNLEEKGIPFAKDQAMGVYSSIWNADDWATQGGLVKTDWSHAPFVASYKEFQIDACEIPTTTDLSKCNGDQKFWWDEPTVSELSLHQNHQLIWVRANHMIYDYCFDATRFPVTPLECQHHRHL
Protein: Regulator of fusion ref-1 (G5EEQ5)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16376329}.
Interaction partners:
- Helix-loop-helix protein 26
- BHLH domain-containing protein
- Helix-loop-helix protein 25
Sequence:
MVLISTPPPAYAHNRKTSQEKKRRDEINAKIKELQLLIQNESDNEKMTQGDVLNRAVEVVSRMETESPGPSSNPNRKGFFDGFRSIESLTYSFIKSLGVNSDVCQDFVQRAKQFFDRERSSLLSTVSGKSKRRSESEILHSSMSYRSQSSSPSTSESGITIDRKEVKKNREQDRRDRQGEAFDALKNFIIENKLMTSHQVEKMQRLNTLDIIIAYIQNKKHNFVSRSDQEQSLYAHAIAEGKKTAKNIAFQFFKSDRHLVVRCADLEKFFEFSLSPKPLFGFPSMPIPIPPPSFPIFPFRPFPFFPMPMAPMATSPKSQQSPSYSLDSPPPSSDTSSSSIETPSTPNENSNSNPKASRKSKLFRPWE
Protein: ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) (M0RAD5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- ATP-dependent clpX-like chaperone, mitochondrial
- Mitochondrial disaggregase
- Lon protease homolog, mitochondrial
- 10 kDa heat shock protein, mitochondrial
- Stress-70 protein, mitochondrial
- 60 kDa heat shock protein, mitochondrial
- ATP-dependent zinc metalloprotease YME1L1
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Elongation factor Tu, mitochondrial
- GTPase Era, mitochondrial
Sequence:
MGQRRGFSLFIRTPINEDPTHRLTPPSSAPPISFSEVDEPAAPAKHAGCCSSGNQAWMHGGMWPRVLLRDGRAAAGGCRALLSRFAVRFSPPWSTGSDSPLRSNLHGTATRAFPLIPIVVEQTGRGERAYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPIHMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGSPGMRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKRQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPELVQKETTTAPADPPAPAGT
Protein: Collectin-10 (Collectin liver protein 1) (CL-L1) (Q8CF98)
Organism: Mus musculus (Mouse)
Function: Lectin that binds to various sugars: galactose > mannose = fucose > N-acetylglucosamine > N-acetylgalactosamine. Acts as a chemoattractant, probably involved in the regulation of cell migration.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9Y6Z7}. Golgi apparatus {ECO:0000269|PubMed:28301481}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6Z7}.
Interaction partners:
- Collectin-11
- Ficolin-2
- Mannan-binding lectin serine protease 1
- Mannose-binding protein C
- Mannan-binding lectin serine protease 2
- Myeloid cell surface antigen CD33
- Ficolin-1
- Interleukin-3 receptor subunit alpha
- Mannose-binding protein A
Sequence:
MNGFRVLLRSNLSMLLLLALLHFQSLGLDVDSRSAAEVCATHTISPGPKGDDGERGDTGEEGKDGKVGRQGPKGVKGELGDMGAQGNIGKSGPIGKKGDKGEKGLLGIPGEKGKAGTICDCGRYRKVVGQLDISVARLKTSMKFIKNVIAGIRETEEKFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEVVNTLIADYVAKSGFFRVFIGVNDLEREGQYVFTDNTPLQNYSNWKEEEPSDPSGHEDCVEMLSSGRWNDTECHLTMYFVCEFVKKKK
Protein: Myotubularin-related protein 12 (Inactive phosphatidylinositol 3-phosphatase 12) (Q80TA6)
Organism: Mus musculus (Mouse)
Function: Acts as an adapter for the myotubularin-related phosphatases. Regulates phosphatase MTM1 protein stability and possibly its intracellular location. By stabilizing MTM1 protein levels, required for skeletal muscle maintenance but not for myogenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9C0I1}. Sarcoplasmic reticulum {ECO:0000269|PubMed:23818870}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:23818870}. Note=Localizes to punctate vesicles when associated with MTM1 (By similarity). Localizes to triads, a structure formed by a T tubule and two sarcoplasmic reticulum terminal cisterna (PubMed:23818870). In skeletal muscles, co-localizes with MTM1 in the sarcomere (PubMed:23818870). Partially localizes to the sarcoplasmic reticulum in skeletal muscles (PubMed:23818870). {ECO:0000250|UniProtKB:Q9C0I1, ECO:0000269|PubMed:23818870}.
Interaction partners:
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2
- Myotubularin
Sequence:
MLGKGGVGGGGGTKAPKPSFVSYVRPEEIHTDEKEVTEKEVTLHLLPGEQLLCEASTVLKYVQEDSCQRGVYGRLVCTDFKISFLGDEDSALDNGGEAQFKNKIIGVNDVPLHCVDQIYGVFDEKKKPLFGQLKKYPEKLVIHCKDLRVLHFCLRYTKEEEVKRIVSGIIHHTQSPKLLKRLFLFSYAAAVHGTATDSRNCTVMFDTPKDWCWELERTKGSVKYRTVSVNEGYRVSDRLPAYFVVPTPLPEDDVRRFQGHGIPIWCWSCHNGSALLKMSALPKEQDDGALQVQKSFLDGIYKTIHRPPYEMVKTEDLSSNFLSLQEIQSAYCKFKQLFLIDNSSEFWDTDIKWFSLLESSSWLDIIRRCLKKAIEITECLEAQNVNVLLLEENASDLCCLLSSLVQVMMDAHCRTRTGFQSLIQKEWVMGGHSFLDRCNHLHQSDKEEVPIFLLFLDCVWQLVHQYPPAFEFTETYLTVLSDSLYIPIFSTFFFNSPHQKDTNMGRENLDAQSKPLTLLTVWDWSVQFEPKAQTLLRNPLYVEKPKLDRGQQKGSRFKHQRQLSLPLTQSKSSPKRGFFREETDHLIKNLLGKRISKLINSSDDLQDSSREFYDSWHSKPTDYHGLLLPHIEGPEIKVWAQRYLRWIPEAQILGGGRVATMGKLLEMMEEVQSLQEKIEARHHRQEAVHAEAPGLLRNSVRLSSLFPFALLQRHSAKPVLPTSGWKALGGEDDLAKREDEFVDLGDV
Protein: Transmembrane emp24 domain-containing protein 7 (p24 family protein gamma-3) (p24gamma3) (p27) (Q9Y3B3)
Organism: Homo sapiens (Human)
Function: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Appears to play a role in the biosynthesis of secreted cargo including processing and post-translational modifications.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Cycles between compartments of the early secretatory pathway.
Interaction partners:
- Transmembrane emp24 domain-containing protein 2
- Transmembrane emp24 domain-containing protein 10
- Protein transport protein Sec23A
- Protein transport protein Sec24A
- Protein SEC13 homolog
- Small COPII coat GTPase SAR1A
- Protein transport protein Sec24D
- Coatomer subunit beta'
- Coatomer subunit zeta-1
- Protein transport protein Sec24B
Sequence:
MPRPGSAQRWAAVAGRWGCRLLALLLLVPGPGGASEITFELPDNAKQCFYEDIAQGTKCTLEFQVITGGHYDVDCRLEDPDGKVLYKEMKKQYDSFTFTASKNGTYKFCFSNEFSTFTHKTVYFDFQVGEDPPLFPSENRVSALTQMESACVSIHEALKSVIDYQTHFRLREAQGRSRAEDLNTRVAYWSVGEALILLVVSIGQVFLLKSFFSDKRTTTTRVGS