wanglab/gogpt-training-data huggingface dataset:
Protein: Proctolin receptor, isoform A (Proctolin receptor, isoform B) (Proctolin receptor, isoform C) (Proctolin receptor, isoform D) (Proctolin receptor, isoform E) (RE56254p) (Q9W4H3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- RYamide receptor
- Neuropeptide F receptor
- Sex peptide receptor
Sequence:
MTMSSTSTATATSTATATLDEANATVGEMFSDADMAEVRHVVQRILVPCVFVIGLLGNSVSIYVLTRKRMRCTTNIYLTALAITDIAYLTCQLILSLQHYDYPKYHFKLYWQLYGYFVWLCDSFGYISIYIAVCFTIERFIAIRYPLKRQTFCTESLAKKVIAAVAIFCLLSTLSTAFEHTITIGTRQIDDAYQPCNQTVANISPMPPPPVAVTPPLATPPLPTPATIWQSPDSAMESTTSGSSNQLVDWGSGSGDGEPENIPRHRRHWQSSGFVTLPTLRKTLEEQDQKVADAAQRSGVTESLLQLWRRKRSAENHNINNTDAFAFNVTEYCQNVTYYNHGLSELGYDELYSYLWNLFTLLVFVVFPLLLLATFNSILILLVHRSKNLRGDLTNASSIRRTKRKSNSGLKGSVSQENRVTITLIAVVLMFIVCQLPWAIYLIVNQYMEIQIGTQVVAGNVCNLLASLHAASNFFLYCVLSDKYRKTVRELITGYRYRRRHARNNTSLYVPHTTTTLTQINGDHYGSNYGGAGSRRNRNTGRLIA
Protein: 11S globulin seed storage protein Ana o 2.0101 (11S globulin Ana o 2) (Allergen Ana o 2) (Anacardein) (Cashew major protein) (CMP) (Legumin Ana o 2) (Legumin-like protein Ana o 2) (allergen Ana o 2.0101) [Cleaved into: 11S globulin seed storage protein Ana o 2.0101 acidic chain (11S globulin seed storage protein Ana o 2.0101 large subunit); 11S globulin seed storage protein Ana o 2.0101 basic chain (11S globulin seed storage protein Ana o 2.0101 small subunit)] (Q8GZP6)
Organism: Anacardium occidentale (Cashew)
Function: Seed storage protein.
Interaction partners:
Sequence:
LSVCFLILFHGCLASRQEWQQQDECQIDRLDALEPDNRVEYEAGTVEAWDPNHEQFRCAGVALVRHTIQPNGLLLPQYSNAPQLIYVVQGEGMTGISYPGCPETYQAPQQGRQQGQSGRFQDRHQKIRRFRRGDIIAIPAGVAHWCYNEGNSPVVTVTLLDVSNSQNQLDRTPRKFHLAGNPKDVFQQQQQHQSRGRNLFSGFDTELLAEAFQVDERLIKQLKSEDNRGGIVKVKDDELRVIRPSRSQSERGSESEEESEDEKRRWGQRDNGIEETICTMRLKENINDPARADIYTPEVGRLTTLNSLNLPILKWLQLSVEKGVLYKNALVLPHWNLNSHSIIYGCKGKGQVQVVDNFGNRVFDGEVREGQMLVVPQNFAVVKRAREERFEWISFKTNDRAMTSPLAGRTSVLGGMPEEVLANAFQISREDARKIKFNNQQTTLTSGESSHHMRDDA
Protein: Pumilio homolog 18 (APUM-18) (AtPUM18) (Q9LVG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20214804}.
Interaction partners:
- Pumilio homolog 24
- Pumilio homolog 23
- Putative pumilio homolog 25
Sequence:
MAVADNPFSMSTMFNALPNPKGISGSIPPPGFAPRASATPLHAALFNLMTDGDGVSYFKEMISNSDKTELQRMASLLTSDSDYFMSIVTTKFGSRRVQKLLGKSDDVDAFFCAAILRRFLHITTDKYASYVTIRAMVVFDKVMKKALYERILYHALDLACDQHGCIALNDIITDADDPYYRDQLLELVASNALRLSNDASGNFVVQHVLTLYDSRCIHNIAVNLYGQCIELSFKKYGSYIVEKLLEVEESMVVVVVELLGCDGDRLMRLARNEFGNFVVVKALRFTKMSRMDLFWGLVQKLMPFIRLLRRSHGSNIANILDSFRLRC
Protein: Pectin lyase-like superfamily protein (Putative polygalacturonase) (Q94C86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable pectate lyase 20
- Probable pectate lyase 8
- Pectin acetylesterase 1
- Pectin acetylesterase 9
Sequence:
MKMPVALVWLLAFTILLISGEGNNAICKENFKLDPRPHSVSILEFGAVGDGKTLNTIAFQNAVFYLKSFADKGGAQLYVPPGKWLTGSFNLTSHLTLFLEKGATILASPDPSHWDVVSPLPSYGRGIELPGKRYRSLINGDNLIDVVITGENGTFDGQGAAWWEWLESGSLNYSRPHIIEFVSSKHILISNLTFLNAPAINIHPVYCSQIHIRKVLIETSVDSPHVLGVAPDSSDNVCIEDSTINVGHDAVSLKSGWDQYGIHYGRPTTAVHIRNLRLKSPTGAGISFGSEMSGGVSDVTVERLNIHSSLIGVAFRTTRGRGGYIRNITISDVDLTSVDTAIVANGHTGSHPDDKFDRDALPVVTHIVMRNFTGVDIGVAGNLTGIGESPFTSICLADIHLQTRSEESWICSNVSGFSDDVSPEPCQELMSSPSSCFAGGSIYEGDATAQSYYSW
Protein: RNA-binding E3 ubiquitin-protein ligase MEX3C (EC 2.3.2.27) (RING finger and KH domain-containing protein 2) (RING finger protein 194) (RING-type E3 ubiquitin transferase MEX3C) (Q5U5Q3)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin ligase responsible for the post-transcriptional regulation of common HLA-A allotypes. Binds to the 3' UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17267406}. Nucleus {ECO:0000269|PubMed:17267406}. Note=Predominantly expressed in the cytoplasm and shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. May act as suppressor of replication stress and chromosome missegregation.
Interaction partners:
- E3 ubiquitin-protein ligase TRIM4
- Polyadenylate-binding protein 1
- mRNA-decapping enzyme 1A
- E3 ubiquitin-protein ligase RNF135
- AP-2 complex subunit beta
Sequence:
MPSGSSAALALAAAPAPLPQPPPPPPPPPPPLPPPSGGPELEGDGLLLRERLAALGLDDPSPAEPGAPALRAPAAAAQGQARRAAELSPEERAPPGRPGAPEAAELELEEDEEEGEEAELDGDLLEEEELEEAEEEDRSSLLLLSPPAATASQTQQIPGGSLGSVLLPAARFDAREAAAAAAAAGVLYGGDDAQGMMAAMLSHAYGPGGCGAAAAALNGEQAALLRRKSVNTTECVPVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPIFVVTGRKEDVAMAKREILSAAEHFSMIRASRNKNGPALGGLSCSPNLPGQTTVQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEMHIAMRTGNYIELNEENDFHYNGTDVSFEGGTLGSAWLSSNPVPPSRARMISNYRNDSSSSLGSGSTDSYFGSNRLADFSPTSPFSTGNFWFGDTLPSVGSEDLAVDSPAFDSLPTSAQTIWTPFEPVNPLSGFGSDPSGNMKTQRRGSQPSTPRLSPTFPESIEHPLARRVRSDPPSTGNHVGLPIYIPAFSNGTNSYSSSNGGSTSSSPPESRRKHDCVICFENEVIAALVPCGHNLFCMECANKICEKRTPSCPVCQTAVTQAIQIHS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q381T4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGNGVVRVATRAPTELPTPKTASSSSHTTASDTRSDAQRSNSPPIPVIKTDGYNNKFDPERLSLEDILGEPGSSTALYIKKKMAGRGAFGEAFIVENNPVAPVAKRRGRIGAESLAVNGTERVGDCQSRQFVAKVLNLTCMSDHDRQYAQTEIMCLANADHFAIVRYYEHFYIDDEFQTIVIITEFADKGDLYRNLHHMPSDRFPTEREAGVLFVQLLLGLDHVHRRRMIHRDIKTANIFLTSRGFLKLGDFGFSKQYDTSVSNPIAVTFLGTSYYLSPEMLKGQRYGKKADIWAAGIVLCELLGKRRPFEAHSPAKLKELVLSGDMWLPPTQKSGESNNSAANTDGKASPPCISLEMREFLEYILQLDPDRRPSASQLLKTPLMQHYLHLFKKQVYDMIAADDEVERNYISNPVDCIGDRRRYNLTAKERVLVMRGIVEGENLIMSETEKQIESGIPGHMEGVVFKGTLDGRWKERYLTLADGYLTVTLAKEKCASNCNTRSKRMPLDTIKSVSPMKIFYSPEANSVEKVDCNKKFVFVLSTVHSQSILFATKTEEERDRWLTALMFTLDMG
Protein: V-type proton ATPase 116 kDa subunit a 1 (V-ATPase 116 kDa subunit a 1) (Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit) (Vacuolar adenosine triphosphatase subunit Ac116) (Vacuolar proton pump subunit 1) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1) (P25286)
Organism: Rattus norvegicus (Rat)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for the acidification of various organelles, such as lysosomes, endosomes, the trans-Golgi network, and secretory granules, including synaptic vesicles. In certain cell types, can be exported to the plasma membrane, where it is involved in the acidification of the extracellular environment. Required for assembly and activity of the vacuolar ATPase (By similarity). Through its action on compartment acidification, plays an essential role in neuronal development in terms of integrity and connectivity of neurons (By similarity).
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32165585}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:32165585}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:Q93050}.
Interaction partners:
- V-type proton ATPase subunit
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit C 1
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit S1
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit D
- Renin receptor
- V-type proton ATPase subunit F
Sequence:
MGELFRSEEMTLAQLFLQSEAAYCCVSELEELGKVQFRDLNPDVNVFQRKFVNEVRRCEEMDRKLRFVEKEIRKANIPIMDTGENPEVPFPRDMIDLEANFEKIENELKEINTNQEALKRNFLELTELKFILRKTQQFFDEMADPDLLEESSSLLEPNEMGRGAPLRLGFVAGVINRERIPTFERMLWRVCRGNVFLRQAEIENPLEDPVTGDYVHKSVFIIFFQGDQLKNRVKKICEGFRASLYPCPETPQERKEMASGVNTRIDDLQMVLNQTEDHRQRVLQAAAKNIRVWFIKVRKMKAIYHTLNLCNIDVTQKCLIAEVWCPVTDLDSIQFALRRGTEHSGSTVPSILNRMQTNQTPPTYNKTNKFTHGFQNIVDAYGIGTYREINPAPYTVITFPFLFAVMFGDFGHGILMTLFAVWMVLRESRILSQKNENEMFSMVFSGRYIILLMGLFSIYTGLIYNDCFSKSLNIFGSSWSVRPMFTIGNWTEETLLGSSVLQLNPAIPGVFGGPYPFGIDPIWNIATNKLTFLNSFKMKMSVILGIIHMLFGVSLSLFNHIYFKKPLNIYFGFIPEIIFMSSLFGYLVILIFYKWTAYDAHSSRNAPSLLIHFINMFLFSYPESGNAMLYSGQKGIQCFLIVVAMLCVPWMLLFKPLILRHQYLRKKHLGTLNFGGIRVGNGPTEEDAEIIQHDQLSTHSEDAEEPTEDEVFDFGDTMVHQAIHTIEYCLGCISNTASYLRLWALSLAHAQLSEVLWTMVIHIGLHVRSLAGGLGLFFIFAAFATLTVAILLIMEGLSAFLHALRLHWVEFQNKFYTGTGFKFLPFSFEHIREGKFDE
Protein: Nuclear transport factor 2 (NTF-2) (Q10100)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Facilitates protein transport into the nucleus. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- GTP-binding nuclear protein spi1
- Ran-specific GTPase-activating protein 1
- NTF2-related export protein 1
- mRNA export factor mex67
- Golgi apparatus membrane protein tvp18
- Importin subunit alpha-2
- Nuclear import protein mog1
- DNA topoisomerase 3
- Replication factor A protein 1
- Nucleoporin nsp1
Sequence:
MADYNALATQFTQFYYQTFDSDRSQLSSLYREESMLSFEGAQLQGTKAIVEKLVSLPFQRVQHRISTLDAQPTGTTGSVIVMVTGELLLDEEQMAQRYSQVFHLVNNNGNYYVLNDLFRLNYG
Protein: Ubiquitin-conjugating enzyme variant Kua homologue, putative (Q38C19)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Ethanolaminephosphotransferase, putative
- Ubiquitin/ribosomal protein S27a, putative
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-like protein, putative
- Ubiquitin-conjugating enzyme, putative
Sequence:
MSIDVVPATETAAAATTTATYMDNIISVRKANAKKLAGGYTQTKRIAEICYFSLAVCLWMRNVAIVVLYLLHSSESSSNQLLWSPLMILSAMVLSDFISGVAHWSFDTWGTPETFLFGNFIRSFREHHVNQMAMTKHDFIETNADTTLPLIPVLLIQLYFLGCNSKNNSTFRYNIDNDNAGFHVFFLTFALFIGMTNELHKWAHLPAPHPFARLLMSCRIVLTRKSHRRHHRGSYDRSYCITTGWLNAPLDRVDFWRKAEAVVTALTGAVPRANDRELLGVRHKEETDGEGCNEEFGGL
Protein: F-box only protein 4 (Q9UKT5)
Organism: Homo sapiens (Human)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes ubiquitination of CCND1 and its subsequent proteasomal degradation. Recognizes TERF1 and promotes its ubiquitination together with UBE2D1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8CHQ0}.
Interaction partners:
- S-phase kinase-associated protein 1
- Telomeric repeat-binding factor 1
- Cullin-1
- S-phase kinase-associated protein 2
- G1/S-specific cyclin-D1
- F-box/WD repeat-containing protein 7
- F-box/WD repeat-containing protein 1A
- F-box only protein 2
- F-box/WD repeat-containing protein 11
- F-box/WD repeat-containing protein 8
Sequence:
MAGSEPRSGTNSPPPPFSDWGRLEAAILSGWKTFWQSVSKERVARTTSREEVDEAASTLTRLPIDVQLYILSFLSPHDLCQLGSTNHYWNETVRDPILWRYFLLRDLPSWSSVDWKSLPDLEILKKPISEVTDGAFFDYMAVYRMCCPYTRRASKSSRPMYGAVTSFLHSLIIQNEPRFAMFGPGLEELNTSLVLSLMSSEELCPTAGLPQRQIDGIGSGVNFQLNNQHKFNILILYSTTRKERDRAREEHTSAVNKMFSRHNEGDDQQGSRYSVIPQIQKVCEVVDGFIYVANAEAHKRHEWQDEFSHIMAMTDPAFGSSGRPLLVLSCISQGDVKRMPCFYLAHELHLNLLNHPWLVQDTEAETLTGFLNGIEWILEEVESKRAR
Protein: Bromo domain-containing protein (Q38AM1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Histone acetyltransferase
- histone acetyltransferase
- histone acetyltransferase
Sequence:
MSKNERDTSFNKNGCLVFVSRLWDLDKLGMFHHPVSAEELPDYHTVIKRPVDLSSIRDGIEKGTYATDVDVQNDVARMITNALEYNAKGSTWYQEAMSFRKTYLDLARQSGLVVDDDEAYIPSRSFKDDESTLRRAEKRNKEDLDEVLRGLEAEKDVPLEELRAKYRRVENITEARGADDVDSSEQGEDEESDEEGSDEEDDDEEDSCASEEVEESEGSDYDSS
Protein: DNA-directed RNA polymerase subunit (EC 2.7.7.6) (B2RXC6)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC10
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase III subunit RPC8
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MVKEQFRETDVAKKISHICFGMKSPEEMRQQAHIQVVSKNLYSQDNNHAPLLYGVLDHRMGTSEKDRPCETCGKNLADCLGHYGYIDLELPCFHVGYFRAVIGILQMICKTCCHIMLSQEEKQQFLDFLKRPGLTYLQKRGLKKKISDKCRKKSTCHYCGAFNGTVKKCGLLKIIHEKYKTNKKVVDPIVSNFLQSFETAIEHNKEVEPLLGRAQENLNPLVVLNLFKRIPAEDVPLLLMNPESGKPSDLILTRLLVPPLCIRPSVVSDLKSGTNEDDLTMKLTEIIFLNDVIKKHRISGAKTQMIMEDWDFLQLQCALYINSELSGIPLNMAPKKWTRGFVQRLKGKQGRFRGNLSGKRVDFSGRTVISPDPNLRIDEVAVPVHVAKILTFPEKVNKANINFLRKLVRNGPDVHPGANFIQQRHMQMKRFLKYGNREKMAQELKFGDIVERHLIDGDVVLFNRQPSLHKLSIMAHLARVKPHRTFRFNECVCTPYNADFDGDEMNLHLPQTEEAKAEALVLMGTKANLVTPRNGEPLIAAIQDFLTGAYLLTLKDTFFDRAKACQIIASILVGKDEKIKVRLPPPTILKPVTLWTGKQIFSVILRPSDDNPVRANLRTKGKQYCGKGEDLCVNDSYVTIQNSELMCGSMDKGTLGSGSKNNIFYILLRDWGQNEAADAMSRLARLAPVYLSNRGFSIGIGDVTPGQGLLKAKYELLNAGYKKCDEYIEALNTGKLQQQPGCTAEETLEALILKELSVIRDHAGSACLRELDKSNSPLTMALCGSKGSFINISQMIACVGQQAISGSRVPDGFENRSLPHFEKHSKLPAAKGFVANSFYSGLTPTEFFFHTMAGREGLVDTAVKTAETGYMQRRLVKSLEDLCSQYDLTVRSSTGDIIQFIYGGDGLDPAAMEGKDEPLEFKRVLDNIKAVYPCQTEPALSKNDLTLTAEAIMKKNEFLCCQDSFLQEIKTFIKGVSEKIKKTRDKYGINDNGTTEPRVLYQLDRITPTQIEKFLETCRDKYMRAQMEPGSAVGALCAQSIGEPGTQMTLKTFHFAGVASMNITLGVPRIKEIINASKAISTPIITAQLDKDDDADYARLVKGRIEKTLLGEISEYIEEVFLPDDCFILVKLSLERIRLLRLEVNAETVRYSICTSKLRVKPGDVAVHGEAVVCVTPRENSKSSMYYVLQFLKEDLPKVVVQGIPEVSRAVIHIDEQSGKEKFKLLVEGDNLRAVMATHGVKGTRTTSNNTYEVEKTLGIEAARTTIINEIQYTMVNHGMSIDRRHVMLLSDLMTYKGEVLGITRFGLAKMKESVLMLASFEKTADHLFDAAYFGQKDSVCGVSECIIMGIPMNIGTGLFKLLHKANRDPKPPRRPLIFDTHEFHIPLVT
Protein: P-selectin glycoprotein ligand 1 (PSGL-1) (Selectin P ligand) (CD antigen CD162) (Q14242)
Organism: Homo sapiens (Human)
Function: A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- E-selectin
- P-selectin
- L-selectin
- Intercellular adhesion molecule 1
- Vascular cell adhesion protein 1
- CD40 ligand
- Leukosialin
- Radixin
- Integrin beta-2
- CD44 antigen
Sequence:
MPLQLLLLLILLGPGNSLQLWDTWADEAEKALGPLLARDRRQATEYEYLDYDFLPETEPPEMLRNSTDTTPLTGPGTPESTTVEPAARRSTGLDAGGAVTELTTELANMGNLSTDSAAMEIQTTQPAATEAQTTQPVPTEAQTTPLAATEAQTTRLTATEAQTTPLAATEAQTTPPAATEAQTTQPTGLEAQTTAPAAMEAQTTAPAAMEAQTTPPAAMEAQTTQTTAMEAQTTAPEATEAQTTQPTATEAQTTPLAAMEALSTEPSATEALSMEPTTKRGLFIPFSVSSVTHKGIPMAASNLSVNYPVGAPDHISVKQCLLAILILALVATIFFVCTVVLAVRLSRKGHMYPVRNYSPTEMVCISSLLPDGGEGPSATANGGLSKAKSPGLTPEPREDREGDDLTLHSFLP
Protein: Peroxisome biogenesis protein 12 (Peroxin-12) (AtPEX12) (Pex12p) (Protein ABERRANT PEROXISOME MORPHOLOGY 4) (Q9M841)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10 (By similarity). When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000250|UniProtKB:O00623}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisome biogenesis protein 5
- Peroxisomal membrane protein PEX14
- Peroxisome biogenesis factor 10
- Peroxisome biogenesis protein 7
- Peroxisomal ATPase PEX1
- Peroxisome biogenesis protein 16
- Peroxisomal ATPase PEX6
- Peroxisome biogenesis protein 19-2
- Peroxisome biogenesis protein 19-1
- Peroxisome biogenesis protein 3-1
Sequence:
MLFQVGGEGTRPTFFEMAAAQQLPASLRAALTYSLGVFALRRSFLHKILDYEDEFFAALMLILEGHSLRTTDGSFAESLYGLRRKSARLRLRKDSARKDSSEEVQHSGLEKRQRILSVVFLVVLPYFKSKLHAIYNKEREARLRESLWGAEDQGFDEADFFTGDDSIVSREPSGNEELSVRVQLATKIKKFIAVCYPWIHASSEGLSFTYQLLYLLDATGFYSLGLQALGIQVCRATGQELMDTSSRISKIRNHERERLRGPPWLKTVQGALLSCSYAVLDYAQTGLIAAVFIFKMMEWWYQSAEERLSAPTVYPPPPPPPAPKMAKEGIPLPPDRSLCALCLQKRANPSVVTVSGFVFCYSCVFKYVSKYKRCPVTLIPASVDQIRRLFQDT
Protein: Borrelia P83/P100 antigen (Q45013)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
- Uncharacterized protein
- SH3b domain-containing protein
- Glutamate transporter, putative
- Tetratricopeptide repeat domain protein
- Tetratricopeptide repeat domain protein
- LPS-assembly protein LptD
- LysM domain protein
- GerMN domain-containing protein
- Caax amino protease family
- Tetratricopeptide repeat domain protein
Sequence:
MKKMLLIFSFFLIFLNGFPVSAREVDREKLKDFVNMDLEFVNYKGPYDSTNTYEQIVGIGEFLARPLTNSNSNSSYYGKYFINRFIDDQDKKASVDVFSIGSKSELDSILNLRRILTGYLIKSFDYDRSSAELIAKVITIYNAVYRGDLDYYKGFYIEAALKSLSKENAGLSRVYSQWAGKTQIFIPLKKDILSGNIESDIDIDSLVTDKVVAALLSENEAGVNFARDITDIQGETHKADQDKIDIELDNIHESDSNITETIENLRDQLEKATDEEHKKEIESQVDAKKKQKEELDKKAINLDKAQQKLDSAEDNLDVQRNTVREKIQEDINEINKEKNLPKPGDVSSPKVDKQLQIKESLEDLQEQLKETGDENQKREIEKQIEIKKSDEKLLKSKDDKASKDGKALDLDRELNSKASSKEKSKAKEEEITKGKSQKSLGDLNNDENLMMPEDQKLPEVKKLDSKKEFKPVSEVEKLDKIFKSNNNVGELSPLDKSSYKDIDSKEETVNKDVNLQKTKPQVKDQVTSLNEDLTTMSIDSSSPVFLEVIDPITNLGTLQLIDLNTGVRLKESTQQGIQRYGIYEREKDLVVIKMDSGKAKLQILDKLENLKVVSESNFEINKNSSLYVDSKMILVAVRDKDSSNDWRLAKFSPKNLDEFILSENKIMPFTSFSVRKNFIYLQDEFKSLVILDVNTLKKVK
Protein: Acetylcholine receptor subunit beta (P25109)
Organism: Rattus norvegicus (Rat)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Acetylcholine receptor subunit alpha
- Acetylcholine receptor subunit delta
- Acetylcholine receptor subunit epsilon
- Neuronal acetylcholine receptor subunit alpha-9
- Neuronal acetylcholine receptor subunit alpha-4
- Neuronal acetylcholine receptor subunit alpha-5
- Neuronal acetylcholine receptor subunit beta-3
- Neuronal acetylcholine receptor subunit beta-4
- Neuronal acetylcholine receptor subunit beta-2
- Neuronal acetylcholine receptor subunit alpha-3
Sequence:
MALGALLLILGILGTPLAPGARGSEAEGQLLKKLFSDYDSSVRPAQEVGDRVGVSIGLTLAQLISLNEKDEEMSTKVYLDLEWTDYRLSWDPAEHDGIESLRVTAESVWLPDVVLLNNNDGNFDVALDINVVVSFEGSVRWQPPGLYRSSCSIQVTYFPFDWQNCTMVFSSYSYDSSEVSLKTGPDPDGQERQEIYIHEGTFIENGQWEIIHKPSRLIHLPGDRRGGKEGHREEVIFYLIIRRKPLFYLVNVIAPCILITLLAIFVFYLPPDAGEKMGLSIFALLTLTVFLLLLADKVPETSLAVPIIIKYLMFTMILVTFSVILSVVVLNLHHRSPHTHQMPFWVRQIFIHKLPPYLGLKRPKPERDQLPEPHHSFSPRSGWGRGTDEYFIRKPPCDFLFPKLNRFQPESPAPDLRRFIDGPPRAVGLPQELREVISSISYMARQLQEQEDHDALKEDWQFVAMVVDRLFLWTFIVFTSVGTLVIFLDATYHLPPPEPFP
Protein: Lambda-crystallin (EC 1.1.1.45) (L-gulonate 3-dehydrogenase) (Gul3DH) (P14755)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Functions as crystallin in the rabbit eye lens. Has high L-gulonate 3-dehydrogenase activity. It also exhibits low dehydrogenase activity toward L-3-hydroxybutyrate (HBA) and L-threonate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15809331}.
Interaction partners:
- Acetyl-CoA acyltransferase 1
- Hydroxysteroid dehydrogenase-like protein 2
- Acetyl-CoA acyltransferase 2
- Sterol carrier protein 2
- Acyl-coenzyme A thioesterase 8
- Acetyl-CoA acetyltransferase 2
- Trifunctional enzyme subunit beta, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- Cocaine- and amphetamine-regulated transcript protein
- Trifunctional enzyme subunit beta, mitochondrial
Sequence:
MASPAAGDVLIVGSGLVGRSWAMLFASGGFRVKLYDIEPRQITGALENIRKEMKSLQQSGSLKGSLSAEEQLSLISSCTNLAEAVEGVVHIQECVPENLDLKRKIFAQLDSIVDDRVVLSSSSSCLLPSKLFTGLAHVKQCIVAHPVNPPYYIPLVELVPHPETSPATVDRTHALMRKIGQSPVRVLKEIDGFVLNRLQYAIISEAWRLVEEGIVSPSDLDLVMSDGLGMRYAFIGPLETMHLNAEGMLSYCDRYSEGMKRVLKSFGSIPEFSGATVEKVNQAMCKKVPADPEHLAARREWRDECLKRLAKLKRQMQPQ
Protein: Probable pectate lyase A (EC 4.2.2.2) (A2QV36)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MTNFKWIVAAAGLLSGQVLAAPTATSTHAKRATVSDAAFGYASLNGGTTGGAGGTTTTVSSYAAFTSAVSGDDAKVVYVDGTIKQTADQVKIGSNTSIIGKDANAILEGFGVLVKEKENVIIRNLGVSKVLADNGDAIGVQYSNNVWIDHCDVSSDRDHDKDYYDGLIDITHGSDYVTVSNTFIHDHWKASLVGHSDSNEDEDSGHLTVTYANNYWYNINSRAPSFRFGTGHVYNSYYLDVSDGINTRDGAQLLVESNQFVDSKKALYSTDDGYAVSNDNDFGDSENTAEEGTLTSMPYDYTLLGSANVKAAVVGTAGQTLTF
Protein: TRAP dicarboxylate transporter, DctP subunit, putative (Q5LKU9)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Subcellular location: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
Interaction partners:
Sequence:
MYLNLKTATASALALACGLAAGTASAETTLRLSTYVNEADIRYAGFTHFADLVAEKTGGSVKVEVFPSATLHGWSEGVDSVQGGVSDISWINADNRLPCYAVTSLYPAEVSLEDQTGLDAAYAALIRDEAANAGLVPLFNSNYSYDQEWWFEEPVADIGNLDGKLVRSIGPLVSMMIETWGGEPVFVAPKEVFQSAERGVVDGINMGVATYSSWKLWTVMPYMVNANLFYGNIQYMMNKAKFDALSADEQAALTAAAAETEAWLQPRYEAWVDQQVGNAVMQGGGAAVSISDDQRASLIASVKPKWDETVNAACGGELADSIRALLASHAP