wanglab/gogpt-training-data huggingface dataset:
Protein: Rho GDP-dissociation inhibitor 3 (Rho GDI 3) (Rho-GDI gamma) (Rho-GDI2) (Q62160)
Organism: Mus musculus (Mouse)
Function: Inhibits GDP/GTP exchange reaction of RhoB. Interacts specifically with the GDP- and GTP-bound forms of post-translationally processed Rhob and Rhog proteins, both of which show a growth-regulated expression in mammalian cells. Stimulates the release of the GDP-bound but not the GTP-bound RhoB protein. Also inhibits the GDP/GTP exchange of RhoB but shows less ability to inhibit the dissociation of prebound GTP.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Transforming protein RhoA
- Tumor necrosis factor receptor superfamily member 16
- RIKEN cDNA 4930544G11 gene
- Rho-related GTP-binding protein RhoB
- Cell division control protein 42 homolog
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Rho GDP-dissociation inhibitor 1
- Rho GDP-dissociation inhibitor 2
- Rho-related GTP-binding protein RhoG
Sequence:
MLGLDACELGEQLLELLRLALCARVLLADKDGESTPSDEVLDEIVPEYQAPGKKSMLAIWQLDPGDVSLVKYKQALLGPLPPIMDPSLPNVQVTRLTLLTEQAPGPIIMDLTGDLDALKNQVFVLKEGIEYKVKITFKVNKEIVSGLKCLHHTYRRGLRVDKAIFMVGSYGPRAQEYEFVTSVEEAPRGALARGLYVVRSLFTDDDRLNHLSWEWHLHVCQDWKD
Protein: Agglutinin-like protein 9 (Adhesin 9) (A0A1D8PQ86)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections. Allele ALS9-2 contributes to endothelial cell adhesion, whereas ALS9-1 does not.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor. Secreted, cell wall. Note=Identified as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. {ECO:0000305|PubMed:12845604}.
Interaction partners:
Sequence:
MLPQFLLLLLYLTVSTAKTITGVFNSFDSLTWTRSVEYVYKGPETPTWTAVLGWSLNSTTADAGDTFTLIMPCVFKFITSQTSVDLTADGVSYATCDFNAGEEFTTFSSLSCTVNSVSVSYDKASGTVKLPITFNVGGTGSSVDLTDSKCFTAGKNTVTFMDGDTKISTTVDFDASPVSPSGYITSSRIIPSLNKASSLFVSPQCENGYTSGIMGFVTSQGATIDCSNINIGISKGLNDWNFPVSSESFTYTKTCSSSGIIVEYENVPAGYRPFVDAYISSENVEQYTLTYANEYTCKNGNTVVDPFTLTWWGYKNSEADSNGDIIVVTTKTVTASTTAVTTLPFNPTVDKTETIEVLQPIPTTTITTSYIGISTSYETFTATIGGTATVIVDTPYHITTTVTTFWTGSVTTTTTYSNPTGSIDTVIVQIPSPDPTTTITEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTPSVSSFESKTFYSSEAQSSLEIDSSNTFMTSISVSTASSYDESSTIVSSAFPTLHISSYSLSTSFVPPVTLPRYVNTTISSSPSFESSSMYSSVTSAVTSIDNDREVPTSTTTYLHSKLYSESISTVIQTKSSDWSLSLGNSNKPESASTVSEESLHYLSTPGPSSSEYSISFTSEKEGHVSSYVPRVSYTSSVKVSISSTMSSENGMSATHTFGISTNTIPSSTETSIKSATVTTPVSESTNTGMSIFMSTTTESKTTDITTETSVSGEVNLGSATVKVSSSEFISKGTVTRIMPTELTNSESTFTASPSFVLTSTESSVIETPATIEMSSRSSSYSVPLSKLRSEGETTRVIPTSSTATGSTVIGSPSSVSTSNESIITGSSSFVSTTAETISTRSIVTESIVAGSPSLVLTTTVLDTTETTITETSIVGESSSRSLTFKASSLSKGEITGTVTPEMSVSTSKATTGTTSEVSIKESLTTKVPTFTSTTIKPETSETQHSESRTTQIPYSETKGSQLSTANSQVSQTGSSKSSIFESAISKDESTFVSATVKSITTPAVTQYQTSLPNPAVSVSEESGKKSSIIESQTENSATQHSIYFDSIETSTLSNTLANTLVSGAMKNSETTSELTTSDKAIGFSTTTETSIPGATNSALSPSVDSGKSSMLGWSGGIVSTVSTSTRLEDSTATSSSITAANQDSLNPSTVSKYPHGSETIDNGSNGSSHSSSALASTISASHSIKFSAHQTTLSQSLISSSTKTVIASTYDGSGSVIKLHSWFYGLVTIFFLFI
Protein: Odorant receptor 43a (P81917)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. Complexes with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. They are necessary and sufficient to promote functional reconstitution of odor-evoked signaling in sensory neurons that normally respond only to carbon dioxide. Involved in the behavioral responses to acetophenone, benzaldehyde, benzyl alcohol, cyclohexanone, and cyclohexanol.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 23a
- Odorant receptor 88a
- Odorant receptor coreceptor
- Odorant receptor 47b
- Putative odorant receptor 83c
- Odorant receptor 85a
- Odorant receptor 13a
- Odorant receptor 9a
- Putative odorant receptor 69a, isoform A
- Odorant receptor 47a
Sequence:
MTIEDIGLVGINVRMWRHLAVLYPTPGSSWRKFAFVLPVTAMNLMQFVYLLRMWGDLPAFILNMFFFSAIFNALMRTWLVIIKRRQFEEFLGQLATLFHSILDSTDEWGRGILRRAEREARNLAILNLSASFLDIVGALVSPLFREERAHPFGLALPGVSMTSSPVYEVIYLAQLPTPLLLSMMYMPFVSLFAGLAIFGKAMLQILVHRLGQIGGEEQSEEERFQRLASCIAYHTQVMRYVWQLNKLVANIVAVEAIIFGSIICSLLFCLNIITSPTQVISIVMYILTMLYVLFTYYNRANEICLENNRVAEAVYNVPWYEAGTRFRKTLLIFLMQTQHPMEIRVGNVYPMTLAMFQSLLNASYSYFTMLRGVTGK
Protein: Golgi reassembly-stacking protein 2 (GRS2) (Golgi reassembly-stacking protein of 55 kDa) (GRASP55) (Q9R064)
Organism: Rattus norvegicus (Rat)
Function: Key structural protein of the Golgi apparatus (By similarity). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (By similarity). Acting in concert with GORASP1/GRASP65, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (By similarity). However, other studies suggest that GORASP2 plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after breakdown during mitosis and meiosis. May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA (By similarity). Required for normal acrosome formation during spermiogenesis and normal male fertility, probably by promoting colocalization of JAM2 and JAM3 at contact sites between germ cells and Sertoli cells (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10487747, ECO:0000269|PubMed:11739401}; Lipid-anchor {ECO:0000269|PubMed:10487747}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H8Y8}. Golgi apparatus {ECO:0000250|UniProtKB:Q9H8Y8}. Note=Detected in the intermediate Golgi, membrane-associated (PubMed:10487747). ER stress triggers its relocalization from Golgi to ER membrane (By similarity). {ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000269|PubMed:10487747}.
Interaction partners:
- Golgin-45
- Junctional adhesion molecule C
- Junctional adhesion molecule 2.
- Ras-related protein Rab-2A
- Golgin subfamily A member 2
- Golgin subfamily A member 5
- Golgi SNAP receptor complex member 1
- Syntaxin-5
- small monomeric GTPase
- General vesicular transport factor p115
Sequence:
MGSSQSVEIPGGGTEGYHVLRVQENSPGHRAGLEPFFDFIVSISGSRLNKDNDTLKDLLKANVEKPVKMLIYSSKTLELREASVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGADTVMNESEDLFSLIETHEAKPLKLYVYNTDTDNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPTRPFEEGKKISLPGQMTGTPITPLKDGFTQVQLSSVSPPSLSPPGTAGVEQSLSGLSISSAPPAVSNVLSTGVPTVPLLPPQVNQSLASVPPMNPAATLPSLMPLSAGLPNLPNLPSLSNFNLPAPHIMPGVGLPELGKPGLPPLPSLPPRNVPGIAPLPMPSDFLPSFPLVPEGSSAASAGEPLSSLPAMGPPSDPVMTTAKADTSSLTVDVMSPASKVPTTVEDRVSDCTPAMEKPVSAVTDANASGAS
Protein: Uncharacterized RING finger protein C57A7.09 (P87139)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSYYQIIVCILASISYIILLEVIALDLGVLDNIFIPKRFAASTDVAIQLPDRNVTLWSRQAVFGKHFTNASATTVINLYLPSNFQEDMSGCPNRNDTDASYFYENDIIDYDIEYIEQKSYSSKPSARVQKDDGGESKDEAILDFLLVQRGKCTYFDKALEAQRLGFKGVIVGDNRSPSSFRLHYMVAPDKVDESKVHIPSLFVSTSSYNLLWSDLLHSYRQPLKLYAKPEELGDMFWPFLLCFSPSIIMLITVQALAIRKFIRTYRTKSKTRRFIEDLPSRTISREGFYSEEEEIENSTQNGELVPLMDESTRRATFGVECVICLESFTKGDKVVALPCKHEFHRPCIAKWIVDYRHACPTCNTEVPPPKPF
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (O77294)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMKKLLSNGSNKNKTLKFDEGINLDQIIAKLKLIGEIGSVIQISVREIEAVCSRAREVLLKQPTLLEIPAPINLLGDIHGQYLNLLRYFESNGYPPDSVYLLLGDYVDRGKQSIETLTLLLALKARYPTKFYLLRGNHECSSINHFYGFYDECKRRYTVKLWRTFVDCYNCLPLAAIIEENIFCCHGGLSPHLFSMQQIREIRRPIEIPESGLICDILWSDPDLRIMGWGPNERGVSHTFGSDVVSAFLHRFKLNLICRGHQVVEDGYEFFAKRQLITIFSAPNYCGEFDNAGAMMCINQDLLCTFRVQRPILSEQRRLSDISV
Protein: CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase) (P9WHK7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Is essential for M.tuberculosis growth in vitro and ex vivo. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity).
Interaction partners:
- ADP-ribose pyrophosphatase
- Tyrosine recombinase XerD
- GMP synthase
- Large ribosomal subunit protein uL6
- Nucleoside diphosphate kinase
- Large ribosomal subunit protein uL5
- dCTP deaminase, dUMP-forming
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein uS2
Sequence:
MRKHPQTATKHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDRNLPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAQPDADGNRPDVVITEIGGTVGDIESQPFLEAARQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVISTPDAPSIYDIPKVLHREELDAFVVRRLNLPFRDVDWTEWDDLLRRVHEPHETVRIALVGKYVELSDAYLSVAEALRAGGFKHRAKVEICWVASDGCETTSGAAAALGDVHGVLIPGGFGIRGIEGKIGAIAYARARGLPVLGLCLGLQCIVIEAARSVGLTNANSAEFDPDTPDPVIATMPDQEEIVAGEADLGGTMRLGSYPAVLEPDSVVAQAYQTTQVSERHRHRYEVNNAYRDKIAESGLRFSGTSPDGHLVEFVEYPPDRHPFVVGTQAHPELKSRPTRPHPLFVAFVGAAIDYKAGELLPVEIPEIPEHTPNGSSHRDGVGQPLPEPASRG
Protein: Pentatricopeptide repeat-containing protein 8, mitochondrial (O94615)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial RNA-binding protein involved in mitochondrial translation. The cox1 mRNA is one target but it is not clear if ppr8 has a single or multiple targets.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:21727087}.
Interaction partners:
- Pentatricopeptide repeat-containing protein 2
- Pentatricopeptide repeat-containing protein 6
- Pentatricopeptide repeat-containing protein 7
- Pentatricopeptide repeat-containing protein 5
- Uncharacterized protein C106.19
- Mitochondrial cox1 translation regulator ppr4
- DNA-directed RNA polymerase, mitochondrial
Sequence:
MQGFGSQIFRKLLRSSNAKVSDALLQNTRTLFTAPPLHSGLQTSFTAETQQHVRQNSQNLLKQLNDEMKARKYTETVATFSSLKPFGILDSQTINRYILFLVDRIKMLNGRGNVDEATLDKLDDILRYAIEHQEIASARFWRIMLQSYIDLNLFDKASLIADMSLSHMEFLPKDERVLGNLYISALQAKILGGASFEQCGKIGSAIHEQLEGKEVVNELVAVYLIYTVFKDQGISSKAHKALVQFNGLTSFHSDVIISVFVNKGLVDQAAAYLKNSNLNERNLPTIYTTVWLLQRLFEAHHSLDPLLTIFDYYLSVSPKDITRLTNAILSLSMKQFERDRDIKKATDFITTFINKMSDVKEFKPSISTANTLFSIASRLKDVKWLSAGFDMIDKYGLKPTHVTYRSLLKAYCLLPSTCEQISQAWVNLEYRLEAISISVADKEINLLKDCILSQPDRDDQQSCLQFLNMVLSKYGKHIRSP
Protein: Chromatin-binding protein (A0A1D8PNH8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Serine/threonine-protein kinase RAD53
- Protein kinase activating protein
- Serine/threonine-protein kinase MEC1
- Serine/threonine-protein kinase TEL1
- Esc4p
- Serine/threonine protein kinase
- DNA helicase
- DNA damage checkpoint protein LCD1
- DNA repair and recombination protein RAD52
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MDTQVDQHVLPQSASSKNSQFQHQQQGQDLGQGQGQVHSTVNVNLEPTQKDSSIFKDYEDHNSSLIFGGNIINDDTELLPTIEDETIGDKTIEDITEADDDTISPFSKKLQEMINQEGQNNGIRTHSEYLKSYSCESSKDGGGNGNDDTQVLIQRHYHSDDNYNIESFNDTIQKQRSNSKLFIQDNIDTQDDQMGDTQIIRKPLPDTQIIGKALSDTQVINNALPDTQVIGKVLPDTQIIQKVLPDTQVIKKALPDTQIIQKALPDTQVIPKRLPDTQVIPKLLPDTQVIQKNNIPDTQVIQLPETQSQSLLYYDSQKVLHSSPADQSQIASKSPSHNNKNKKTFKSQTQVLNTQDLSDISTSEDTLQEHTTQSVIEIQTDSDDNDDDDDDDDNEDEKIESNYYDDSLTAHQFKRKLSLSPQKIKRRNTELIPSRTNKSSLSTTSLSSSLLSNNNNNNNNRDFLKTPGLRQYSVPLVLASPTNPLSSSSPLKKKLKLKLNNKGEVEEEEEEEEEVDKSIQTDKIEEDTTSIDIIAPLPSSPNKGGRGRGGGGGVKISFEEEHEPSDLEEFDIDSDQIKKKNQDFIEIDDDEEEEEEDEVVEDDDDDDDDDDDDDDDDDDNSESKKQSDEIIPIIAPKSRIKKRIIDLQSMNSNTNDEEEDIDSIIEEEEEDNNNTEPNILRQEKSNTLTEDDIINHDSVWAIYNLKMYTGKIVAKYIEDSNIEFYEGTYNIKNVDLNVLDIRIGDTVNIKGNRHKYIVTGLSTLTTNGGGDIKCMRGYNVVYLRRCQQKPNSGKLSKEISVILSDCFMELSDWIIHQQKFKLIIGNYNIFNDEGILLPSTPKKLQKYKLPSTPLKSIKYTNNNNNSEIIKPNSNSLVAESESGLFQGMIFCITSIDGDRKLQLKSMIETNGGILWDKEIHELFSYHERERKRKRKQEQPLRKGSEISISLYLSCDLEIVETFNFIALISNNFCRSAKYLQALALGWPIISDIYIDDCLKNNHHKSKWINYLLPSGLSKKLNTIKSIDIFKFKQNYDMGKKLIDQFNNNHHVFQGLNILILQNKSINYNSMETCKFIFYAFGAKSLQYFTKTDQIIKCIKEDFSPILEVDPNITIYDESNDMVQVLTNITNNTRNNTQNKSNKSNYSIKLIDWEWVVQCVINGTILECSKYTLSI
Protein: NAD(P)H-quinone oxidoreductase subunit J, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit J) (NADH-plastoquinone oxidoreductase subunit J) (Q6ENH1)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01357}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01357}; Stromal side {ECO:0000255|HAMAP-Rule:MF_01357}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- NAD
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Uncharacterized protein
- Plus3 domain-containing protein
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NAD
- NADH dehydrogenase iron-sulfur protein 4
- NADH:quinone oxidoreductase/Mrp antiporter transmembrane domain-containing protein
Sequence:
MQQGWLSNWLVKHEVVHRSLGFDHRGIETLQIKAEDWDSIAVILYVYGYNYLRSQCAYDVAPGGSLASVYHLTRIQYGIDNPEEVCIKVFAQKDNPRIPSVFWIWRSSDFQERESFDMVGISYDNHPRLKRILMPESWIGWPLRKDYITPNFYEIQDAH
Protein: Histone H3 methyltransferase DOT1 variant d (Q679P4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
PAAAGLVHVSSTATRLTNSHTMGSFSSGVAGGTVGGVFTHAVPSASAHPFGAGVGSGAVCSSATLGLSPLQAAASTSASSFQAAASVETRPPPPPPLLPPQHLGRPPAGPPVLHAPPPPNVALPPPPALLASNPEPVLLQSLASLPANNAFLPPSSAASLQPANASLSVKLASLPHKVSRPSFTVHHQPLPRLALAQAAPAAPQASTSGPSAVWVSLGMPPPYAAHLSGVKPR
Protein: Chromobox protein homolog 6 (O95503)
Organism: Homo sapiens (Human)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Possibly contributes to the target selectivity of the PRC1 complex by binding specific regions of chromatin. Recruitment to chromatin might occur in an H3K27me3-independent fashion (By similarity). May have a PRC1-independent function in embryonic stem cells (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:18927235}. Chromosome {ECO:0000269|PubMed:18927235}. Note=Uniformely distributed in the nucleoplasm (PubMed:18927235). Localizes to the inactivated X chromosome in females (By similarity). {ECO:0000250|UniProtKB:Q9DBY5, ECO:0000269|PubMed:18927235}.
Interaction partners:
- E3 ubiquitin-protein ligase RING1
- E3 ubiquitin-protein ligase RING2
- Polycomb complex protein BMI-1
- Chromobox protein homolog 8
- Polyhomeotic-like protein 2
- Polyhomeotic-like protein 3
- Polycomb group RING finger protein 2
- Polycomb group RING finger protein 1
- E3 SUMO-protein ligase CBX4
- Polyhomeotic-like protein 1
Sequence:
MELSAVGERVFAAESIIKRRIRKGRIEYLVKWKGWAIKYSTWEPEENILDSRLIAAFEQKERERELYGPKKRGPKPKTFLLKARAQAEALRISDVHFSVKPSASASSPKLHSSAAVHRLKKDIRRCHRMSRRPLPRPDPQGGSPGLRPPISPFSETVRIINRKVKPREPKRNRIILNLKVIDKGAGGGGAGQGAGALARPKVPSRNRVIGKSKKFSESVLRTQIRHMKFGAFALYKPPPAPLVAPSPGKAEASAPGPGLLLAAPAAPYDARSSGSSGCPSPTPQSSDPDDTPPKLLPETVSPSAPSWREPEVLDLSLPPESAATSKRAPPEVTAAAGPAPPTAPEPAGASSEPEAGDWRPEMSPCSNVVVTDVTSNLLTVTIKEFCNPEDFEKVAAGVAGAAGGGGSIGASK
Protein: Uncharacterized transporter C576.17c (O74899)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MNDTNDVMHVHSESISPKKNDLDIELGESVVEPHLSNNSIAKLDTYELEENEDISDYAYKLAGISNEHPAHPQNWGWWKKAYIVLLSTSLQMYVFWTPNFYPGVQDSVMELWHLSSQVSLLGQSMFVLGVALGPLFLGPLSDLLGRKLVYIGSLIIYVCFCISCALARNYAQLVISMLIMGVVGSTALGNVAGAVADVLGDEDSNWGMYMFIFMCSVASVGSPMGTGVAENPKLTWRWLYWIDVIVGGFFIILFVFTPETLPAIVIQRYEQKRQGLPVSWFPQFSLKKLAKDTYFVFFMAIKIFFSEPIVSSLGIYNGFVNGLLYFFLQAIWPVYFSIYKMSDMAASCTYMAAMPACVILLWFEPLQCWLYKRDKRKHQNRLRPEARFIMTLFYVWGFPIGIFMFAFCSKVHIHYIVSLIGLTIFNIADYHIWQAMLLYVTDAYPNVSASAVAAFELPSNLGAVGFIHLSALMFSRMNVHWATAVVGFASLPLIALIYALYFYGDRIRARSKLASQRVPINTAAH
Protein: RH31156p (Receptor expression enhancing protein A, isoform K) (Q9W1X3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHRTQDELDDVMMSSMTSSAVVMRSTATGARLLRPRNQTPVGRSGSGTRHSTGMYFTEVDVTAKNAGDFNYNIRSQDDISSGYSSAEPVSGLSRTSSMTNASKARAKSKRNELLEEMRDEVYLDNQLYFQGVQRKSSVPEAEELKIVESSESIQSQELEKVLKEENIDAEDEAFFETLPLIEEHINEVVANYGRDEKLLPQERKHNSIEEEQFEDALFEEPQKCVSDEVDAKNIEEILTDRSQNQTPNGSAETTDSGTPSQNKPYVHPPIDPFLLVLSASASAPDPFMPERPRPMSPREMRETLEEIKHSFRAQLEAEPSVSASPSPSLRPKANHGKGRAPPPPLPPKKHSLSPQPDAISQTSTGSVERKSGIGQLFKNIKANVLRNKANPSQQQPEDEQLAAKETQI
Protein: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex component E2) (OGDC-E2) (Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex) (P0AFG6)
Organism: Escherichia coli (strain K12)
Function: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Interaction partners:
- 2-oxoglutarate dehydrogenase E1 component
- Dihydrolipoyl dehydrogenase
- Succinate--CoA ligase subunit alpha
- Succinate--CoA ligase subunit beta
- Succinate dehydrogenase flavoprotein subunit
- Succinate dehydrogenase iron-sulfur subunit
- Aconitate hydratase B
- Citrate synthase
- Succinate dehydrogenase cytochrome b556 subunit
- Isocitrate dehydrogenase
Sequence:
MSSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSAGKETSAKSEEKASTPAQRQQASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPALAARSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLLDV
Protein: Extracellular superoxide dismutase [Cu-Zn] (EC-SOD) (EC 1.15.1.1) (O09164)
Organism: Mus musculus (Mouse)
Function: Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
Subcellular location: Secreted, extracellular space. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:16371425}.
Interaction partners:
- Copper transport protein ATOX1
- Superoxide dismutase, mitochondrial
- Copper chaperone for superoxide dismutase
- Catalase
- Glutathione peroxidase 3
- Glutathione peroxidase 1
- Parkinson disease protein 7 homolog
Sequence:
MLAFLFYGLLLAACGSVTMSNPGESSFDLADRLDPVEKIDRLDLVEKIGDTHAKVLEIWMELGRRREVDAAEMHAICRVQPSATLPPDQPQITGLVLFRQLGPGSRLEAYFSLEGFPAEQNASNRAIHVHEFGDLSQGCDSTGPHYNPMEVPHPQHPGDFGNFVVRNGQLWRHRVGLTASLAGPHAILGRSVVVHAGEDDLGKGGNQASLQNGNAGRRLACCVVGTSSSAAWESQTKERKKRRRESECKTT
Protein: Beta-catenin/armadillo-related protein 1 (Protruding vulva protein 1) (Suppressor of polyray 1) (Q18825)
Organism: Caenorhabditis elegans
Function: Participates in the Wnt signaling pathway which affects cell fate and may regulate the stem cell divisions of seam cells during larval development. Functions as a transcriptional activator but is dependent on the interaction with pop-1. Involved in maintaining lin-39 Hox expression and regulating glr-1 abundance at the synapses. Required for mab-5 expression during Q neuroblast migration and for oxidative stress-induced daf-16 signaling. Has roles in egg laying, vulva precursor cell fate determination, Q neuroblast migration, posterior ectodermal cell P12 specification, movement, body length, male tail development and dauer induction. Functionally redundant to wrm-1 and hmp-2. In the intestine, plays a role in probiotic-mediated protection against infections by pathogens such as S.enterica.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15820693, ECO:0000269|PubMed:9716532}. Nucleus {ECO:0000269|PubMed:15820693, ECO:0000269|PubMed:9716532}. Membrane {ECO:0000269|PubMed:15820693, ECO:0000269|PubMed:9716532}. Cell junction {ECO:0000269|PubMed:15820693, ECO:0000269|PubMed:9716532}. Note=Mostly cytoplasmic. {ECO:0000269|PubMed:15820693, ECO:0000269|PubMed:9716532}.
Interaction partners:
- Protein pop-1
- Axin-like protein pry-1
- F-box/WD repeat-containing protein lin-23
- Glycogen synthase kinase-3
- Adenomatous polyposis coli protein-related protein 1
- Casein kinase I isoform alpha
- Protein kinase domain-containing protein
- RuvB-like 1
- Beta-catenin-like protein hmp-2
- Armadillo repeat-containing protein wrm-1
Sequence:
MDLDPNLVINHDDTNLSEASFTMEQHTSSYSDIHMGSTPCTGHRKVDMWRNHNFDSGFQTMNHSEAPSIISSLHPSSHLSGMSSMADYEPIPTLSDQQKQKFDGITQNQADGQYNTVRAIPELTMLMKDQDNEVVHKAVILMQNIAKMECDPMRRQNEARIVDPRVIFTLRDLLRDKVEFPNIIRCTLGTFFHICNRQEGIDLVTRAIAEQPDIIPNLIRHIGTYPSSIYKYAILTMHSILSDKQRGGQSVIIARQQDAITHVTPWLEAEKSEKLLPVIVDLIRVLCEKNTEQKIKFVKMGGPQKLLMLLQHRVYENLLWRTTQLLKTFSNFDAPNLVAFGGRQILANLLSHGSPRLVQSTLETLRNISDVPSKIKEDLLLKSLLELVNSRNTTIRLYSAQIMSNLVANNRHNKEFMCGNNGVVILVRALTIATKEMGDLRDKEAQQMEDYIESLICTLRHLCVGHPMSDKVQAFVFRDPALFLHKLLTMRPVLLKHTLSLLLKVVSQHALLAPFRSCRIGDKGFVEQLIHILRVACTQLNVQESIEGVRVKDIIHLCIQILRWITRDQDILNEVVFFLQTPENSRMGDGHTLPIFVLQKANVEENTKSSALALIYNLMHHEQMANVLDRDDVLVKMLQNVQMQSQTHPELASLANNILKMMYEKREKTRNTLPRYNSYLESQFGHMSMTTPRSEALNSSGEVCEGAGEQWSTPLTDDTMMDSYCNSSGRDSSKPYNSPMYHSPPAMYPEYSIGPPETYLDPHATASCYPRPTPPQYNSYDRSPPVYNDLPSNPGPSSHSSDYYPSRNSRF
Protein: Potassium channel subfamily K member 5b (Potassium channel, subfamily K, member 5) (Q6PFU3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MADKGPILTSVIIFYLSIGAAIFQILEEPNLNSAVDDYKNKTNNLLKKYPCLSKEVLGEIIEVVAEATGQGVTVTKEAQFNNWNWENAVIFAATVITTIGYGNVAPKTTGGRLFCILYGLCGIPLCLTWISELGTFFGSRTKRLSQLLLHSGLNVRKVQFICTIVFLLWGFLVHLIIPAFVFMFFENWTYLEGLYFSFTTLTTVGFGDYVAGVDPSVNYPTLYRFFVQLWIYLGLAWLSLFFSWNVHMVVEAHKVLKKRRMRRHRLPTDDVPEKKEVKKTPKPPPRSGVIDIFEFMSEKVEDYSDVIRAIGADEKRRKKKQEEELARSKSCSDLLQGLVIPLDHSPRLQRRFSVSANMCMAISDESVDGLNNNNCKQEDDTLTKVRHKDQKVNRERAENPARCAWDSRSSDPSIFQSSTVTNSTNRGSRFSVSKVSEDRSLGKRKSFG