wanglab/gogpt-training-data huggingface dataset:
Protein: Mitochondrial genome maintenance exonuclease 1 (EC 3.1.-.-) (Q9CXC3)
Organism: Mus musculus (Mouse)
Function: Metal-dependent single-stranded DNA (ssDNA) exonuclease involved in mitochondrial genome maintenance. Has preference for 5'-3' exonuclease activity but is also capable of endoduclease activity on linear substrates. Necessary for maintenance of proper 7S DNA levels. Probably involved in mitochondrial DNA (mtDNA) repair, possibly via the processing of displaced DNA containing Okazaki fragments during RNA-primed DNA synthesis on the lagging strand or via processing of DNA flaps during long-patch base excision repair (By similarity). Specifically binds 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03030}.
Interaction partners:
- Twinkle mtDNA helicase
- DNA replication ATP-dependent helicase/nuclease DNA2
- DNA polymerase subunit gamma-2
- DNA polymerase subunit gamma-1
- DNA-directed RNA polymerase, mitochondrial
- Ribonuclease H1
- Deoxyguanosine kinase, mitochondrial
Sequence:
MKLPLTFCRLLSRLNRFSVKASPPVSFSTFSYLCSQKKKNSYEAVDQAKYSRLVRSVLSRGPAQTPESLFKEDDVLYGPVSKHKAAEPEPQARVPQHCFPIFNEERTGKPHTDASSSPLKIPLQRNSIPSVTRILQQTMPPEQSFFLERWKERMVLELGEDGFAEYTSNVFLQGKQFHKALESILSPQENLTGGEEHPQCGYIESIQHILTEISGVQALESAVQHEALKYVGLLDCVAEYRGKLCVIDWKTSEKPKPLIRNTYDNPLQVVAYMGAVNHDAHYSFQVQCGLIVVAYKDGSPAHPHFMDEELCSKYWAKWLLRLEEYTEKQKNLSAPEPA
Protein: Nucleoprotein (Nucleocapsid protein) (Protein N) (P89216)
Organism: Thogoto virus (isolate SiAr 126) (Tho)
Function: Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication.
Subcellular location: Virion {ECO:0000305}.
Interaction partners:
Sequence:
MATDQMDISGPPPKKQHVDTESQIPKMYEMIRDQMRTLASTHKIPLNIDHNCEVIGSIIMAACTNNRDLRPVDKYWFLMGPAGAEVMTEVEIDIQPQLQWAKGAVHDPKYKGQWYPFLALLQISNKTKDTILWQKYPVTQELEISNSLEIYANGHGIKDRLKNSRPRSVGPLVHLLHLKRLQENPPKNPKTKKPLESPAVNGIRKSIVGHLKRQCIGETQKAMINQFEMGRWESLSTFAASLLAIKPRIENHFVLTYPLIANCEDFAGATLSDEWVFKAMEKISNKKTLRVCGPDEKWISFMNQIYIHSVFQTTGEDLGVLEWVFGGRFCQRKEFGRYCKKSQTKVIGLFTFQYEYWSKPLKSAPRSIEGSKRGQISCRPSFKGKRPSYNNFTSIDALQSASGSQTVSFYDQVREECQKYMDLKVEGTTCFYRKGGHVEVEFPGSAHCNTYLFG
Protein: Kappa-casein [Cleaved into: Casoxin-C; Casoxin-6; Casoxin-A; Casoxin-B; Casoplatelin] (P02668)
Organism: Bos taurus (Bovine)
Function: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
Subcellular location: Secreted.
Interaction partners:
- Beta-lactoglobulin
- Beta-casein
- Alpha-S1-casein
- Alpha-S2-casein
- Alpha-lactalbumin
- Chymosin
- Glycosylation-dependent cell adhesion molecule 1
- Lactotransferrin
- Albumin
- Polymeric immunoglobulin receptor
Sequence:
MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYGLNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHPHPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEINTVQVTSTAV
Protein: LD21041p (Q8MQQ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
GTRQNPPGQVAAPTVAVPQSAPIAPPPGTSSTSVAPPLTASIANPPPTSGFASVPLFAAPTISSTPIPFFNPQPTGAEVTTGLSQQENEATASTTLEGLVQGPAPTLSASQFFDTPLPTGTQPENQVASVSSERENLVQEPISNQGIPFFAPPQTNIFTPQLQQEFIAPAEDSKRSEIQEEFLSAPPQESNLSTELREDTHTGPPVIEPVLEETPASSSESSVPPASKVDQEDIVYPEPSAPVEQEIPLFVPVPGLPGLSQDIPLYPPPPTGSTTASSIFAAPPVASSAPLFVPVPGPPSVSSLFSPSQVDSTSSLFAPPPTSANTTILTPAPDTTSTLFANNIPTTTPSIPDIVPTTSAELVDAPPGFQGSSDDTATNLFQGNTETQTVFSPFAQTKATPLVQETKPELVPPPIGFFAPKSESEVLSQPPLAPSPLQSFFSTAPETATTTDFNFFGSPAPGSVFPDLPVQQGIAPPPLALESPPQNSVSNIATSAIGFDLLNQTQQASSLVENSNQNSSVNSFDGYFGGPSASAAQTFANETTNALVAPAINCDPVNFFDQVPQTQSQIQQANEDQRIQNFFNNPPLQDQPAVPGELKYDIVHSGVAVKQLQERSQTPVSNLVEPPSSACSEFSTLAPAPTQTDRQSGDDLLQQHLGELPEDILRELRMASASSEKGQVATPPVAIPYSPVVAHWFYKRSVDTKFIWTPFSHYDSALLETSLNLDDSTLIIPVEGGRYDVNIKERTKTPVYWEGKAIEVRRCSWFYKGVDSKYVPYTEDTAALLEAEYKRSAETGEWHQKIMLANGEQVVFHGPTVIVHFLPQQNADTWGASTQGSMRPRVVKRDLDDFTIEQGESQRVDHLLFMVHGIGSACDLKMRSVEEVVDDFRVIAQQLVQSHYKNSTDMGLVGRVEVLPISWHGHLHSEELGIDEKLKSITLESIPRLRNFTNDTLLDVLFYTSPKYCQKIMNTVADALNDVYLKYRMRHPEFNGGVSLAGHSLGSLILFDLLCHQEPLKESEEENKENPDQLPQKQSSQKVQLPTSDPLPKQVSYAMGPEGTGQPVITYTQLIFHPKKFFALGSPIGMFVTIRGIDKLGLDFHLPTCPGFYNIFHPFDPVAYRIEALVNPDMNGIRPVLIPHHKGRKRMHLELKETMTRVGADIKQRFMDTFKTTLDSVNFLTTVTKVKKEAEESLEKETSQTSSQAFQKQTEDQDESSVASSSCKLRNRTDSNSTTASDPEFIELDFPLGKLNDSKRVDYVLQEAPLEFINEYIFALSSHVCYWGSEDTILFVMKEIYASLGISTDSQVPQSSMTIERPVSHESSVSHSLLPM
Protein: Ataxin-2-like protein (Ataxin-2 domain protein) (Ataxin-2-related protein) (Q8WWM7)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of stress granule and P-body formation.
Subcellular location: Membrane {ECO:0000269|PubMed:11784712}; Peripheral membrane protein {ECO:0000269|PubMed:11784712}. Cytoplasm {ECO:0000269|PubMed:23209657}. Nucleus speckle {ECO:0000269|PubMed:23209657}. Cytoplasmic granule {ECO:0000269|PubMed:23209657}. Note=Predominantly cytoplasmic but is also detected in nuclear speckles (PubMed:23209657). Component of cytoplasmic stress granules (PubMed:23209657). Inhibition of methylation alters nuclear localization (PubMed:25748791). Methylation does not seem to be required for localization to stress granules under stress conditions (PubMed:25748791). {ECO:0000269|PubMed:23209657, ECO:0000269|PubMed:25748791}.
Interaction partners:
- Protein LSM12
- Ataxin-2
- Probable ATP-dependent RNA helicase DDX6
- Ataxin-3
- Polyadenylate-binding protein 1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- FMR1-interacting protein NUFIP2
- Ataxin-3-like protein
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
Sequence:
MLKPQPLQQPSQPQQPPPTQQAVARRPPGGTSPPNGGLPGPLATSAAPPGPPAAASPCLGPVAAAGSGLRRGAEGILAPQPPPPQQHQERPGAAAIGSARGQSTGKGPPQSPVFEGVYNNSRMLHFLTAVVGSTCDVKVKNGTTYEGIFKTLSSKFELAVDAVHRKASEPAGGPRREDIVDTMVFKPSDVMLVHFRNVDFNYATKDKFTDSAIAMNSKVNGEHKEKVLQRWEGGDSNSDDYDLESDMSNGWDPNEMFKFNEENYGVKTTYDSSLSSYTVPLEKDNSEEFRQRELRAAQLAREIESSPQYRLRIAMENDDGRTEEEKHSAVQRQGSGRESPSLASREGKYIPLPQRVREGPRGGVRCSSSRGGRPGLSSLPPRGPHHLDNSSPGPGSEARGINGGPSRMSPKAQRPLRGAKTLSSPSNRPSGETSVPPPPAVGRMYPPRSPKSAAPAPISASCPEPPIGSAVPTSSASIPVTSSVSDPGVGSISPASPKISLAPTDVKELSTKEPGRTLEPQELARIAGKVPGLQNEQKRFQLEELRKFGAQFKLQPSSSPENSLDPFPPRILKEEPKGKEKEVDGLLTSEPMGSPVSSKTESVSDKEDKPPLAPSGGTEGPEQPPPPCPSQTGSPPVGLIKGEDKDEGPVAEQVKKSTLNPNAKEFNPTKPLLSVNKSTSTPTSPGPRTHSTPSIPVLTAGQSGLYSPQYISYIPQIHMGPAVQAPQMYPYPVSNSVPGQQGKYRGAKGSLPPQRSDQHQPASAPPMMQAAAAAGPPLVAATPYSSYIPYNPQQFPGQPAMMQPMAHYPSQPVFAPMLQSNPRMLTSGSHPQAIVSSSTPQYPSAEQPTPQALYATVHQSYPHHATQLHAHQPQPATTPTGSQPQSQHAAPSPVQHQAGQAPHLGSGQPQQNLYHPGALTGTPPSLPPGPSAQSPQSSFPQPAAVYAIHHQQLPHGFTNMAHVTQAHVQTGITAAPPPHPGAPHPPQVMLLHPPQSHGGPPQGAVPQSGVPALSASTPSPYPYIGHPQGEQPGQAPGFPGGADDRIREFSLAGGIWHGRAEGLQVGQDARVLGGE
Protein: Probable lipase C16A3.12c (EC 3.1.1.-) (P78898)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable lipase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Vacuole {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Multifunctional tryptophan biosynthesis protein
Sequence:
MSGFNKNQIYWGDYVGVIAAFVGVYTELVARIFIYMIPERVREWFRVRIIVLYHYYISSKTTDGMTDAVQKCRNIYEICEAFGYRVEEHLVRTQDNFILCLHRITHPKQSQHKREVVYCHHGLMTNSELWVAVNESERSLPFVLIESGYDVWLGNNRGNKYSRKHITYKPKDEEFWNFSLDDMAMFDIPDTVDYILRETGREKLNYIGFSQGTAQAMAALSINPDLNDKVNIFIGLAPAYAPKGFSNYFVDYIVKVNPKIMYHLFGRRCLLPSVTFWQNICYPPIFVKIVDVSLKILFNWDLSNISLNQKLCGYAHLYSFSSVKSVVHWLQIIKNCTFQLYDDDMALLAGYGSRHYQVPLFPTNNIKCPMLILWGGKDTLINMEVMRTALPPHAKEVSIAHYEHLDFLWGQDVKEEVFPVVIDALKHHSLGKAKHFVKQNGFH
Protein: Sugar transporter family protein (AFU_orthologue AFUA_7G05550) (Q5AYC7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MADDQVKAQAGHIEAPEEHRPLTFKACFQYLKDRVPTLKPPMRKAPNPFKALTLLNRQQWLFFAVAFLGWTLDALDFFTVSLTTSELAEEFGKEISDISWGITLVLMLRSVGAITFGIASDRWGRKWPFIINNLLFIALEIGTGFTQTYQQFLAVRALFGIAMGGLYGNVAATALEDCPKEARGIVSGLLQQGYAFGYLLAAAFARALVGTTSHGWRPFYWFAGCLPVLAIVFRLFLPETNAYRQRQELRAEMPGNVTSAFISEGKVALKRHWLLLIYLVLLMAGFNFMSHGSQDLYPTLVQRQYGFSRDAVTVTQVVANLGALTGGTLCGWGSQIFGRRFSIIVISIVGGALLYPYTFISSHKIMAPAFFEQFCVQGAWGVIPIHLMELSPGSIRTFTVGTAYQLGNLVSSASSTIESTIGERFPLPPTEEGEERYDYGKVICIFMGCVYAYVIIVTFFGPERLGRDFDVENDEDVGEVRAERGVIDDMEKGRN
Protein: CENP-B homolog protein 1 (CBHP-1) (O14423)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds to centromeric K-type repeat DNA and ARS3002 DNA. The CBH-binding consensus sequence is Py-Pu-A-T-A-T-Py-Pu-T-A.
Subcellular location: Nucleus. Chromosome, centromere.
Interaction partners:
- ARS-binding protein 1
Sequence:
MPPIRQAVSLAEKKAIRDYYNQSAHRIPQKEVTEWFRKTYNKDLSQSTISEILSPKYSYLDDGSVRLGDIKKIRAPKFPLLDNAVYEWLQQREVEGLPISGDMIKQAATRFWSKIPAYASLPLPDFSNGWLDKFRRRHYIQQSAVNQALESIKFEVFREYPVHIQEFIRPYAQKDIFCVGGTSLFWKLTPNKQNLDYQEIQGMKRGKAKVSLIMCCNADGSERLPLWIVGYAQNPRSFEQCGIFPKSMNFEWKWNGRASISPIIMEEWLRWFDTRMQGRKVLLMLESNDTYQFGVESVRRFKGGFQNTSVFRIPEKTLDIKSPFEQGIVDTFKANYRRYWLQYSLNQINILRDPLKAVNVLKAIRWMLWSWNFGVSEKTIQASFLRSGLLGPHSEAEGQGMESYQKAIMEIGNLISSKGSEAVKQINEYIRPSEEDETKLHQDAVDTVAAEFLEERRFESDEEEDVEPQISNVEAAMAFEVLIKYFEQHENGDPSFVLDLYRRQRVIAPNNLIA
Protein: Immunoglobulin-like domain-containing receptor 1 (Angulin-2) (Q8CBR1)
Organism: Mus musculus (Mouse)
Function: Maintains epithelial barrier function by recruiting MARVELD2/tricellulin to tricellular tight junctions (tTJs). Crucial for normal hearing by maintaining the structural and functional integrity of tTJs, which are critical for the survival of auditory neurosensory HCs. Mediates fatty acids and lipoproteins-stimulated CCK/cholecystokinin secretion in the small intestine. In the inner ear, may regulate alternative pre-mRNA splicing via binding to TRA2A, TRA2B and SRSF1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23239027, ECO:0000269|PubMed:25217574}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000269|PubMed:23239027, ECO:0000269|PubMed:25217574}. Nucleus {ECO:0000269|PubMed:28785060}. Cytoplasm {ECO:0000250|UniProtKB:Q86SU0}. Note=Localizes to tricellular tight junctions (tTJs) between epithelial cells. {ECO:0000269|PubMed:23239027, ECO:0000269|PubMed:25217574}.
Interaction partners:
- MARVEL domain-containing protein 2
Sequence:
MGCGLLAAGLLLFTWLPAGCLSLLVTVQHTERYVTLFASVTLKCDYTTSAQLQDVVVTWRFKSFCKDPIFDYFSASYQAALSLGQDPSNDCSDNQREVRIVAQRRGQSEPVLGVDYRQRKITIQNRADLVINEVMWWDHGVYYCTIEAPGDTSGDPDKEVKLIVLHWLTVIFIILGALLLLLLIGVCWCQCCPQYCCCYIRCPCCPTRCCCPEEALARHRYMKQVQALGPQMMEKPLYWGADRSSQVSSYAMNPLLQRDLSLQSSLPQMPMTQMAAHPPVANGVLEYLEKELRNLNPAQPLPADLRAKSGHPCSMLSSLGSAEVVERRVIHLPPLIRDPPSSRTSNPSHQQRLNAVSSRHCDLSERPRQRHHSDFLRELQDQGMRPWAPGRGELDPHWSGRHHRSRPSESSMPWSDWDSLSECPSSSEAPWPPRRPEPREGAQRRERRRHRSYSPPLPSGPSSWSSEEEKESLPRNWGAQRRHHHRRRRSQSPNWPEEKPPSYRSLDVTPGKNNRKKGNVERRLERESSHSGRSVVI
Protein: Lysosome-associated membrane glycoprotein 1 (LAMP-1) (Lysosome-associated membrane protein 1) (120 kDa lysosomal membrane glycoprotein) (LGP-120) (CD107 antigen-like family member A) (CD antigen CD107a) (P14562)
Organism: Rattus norvegicus (Rat)
Function: Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, autophagy, and cholesterol homeostasis (By similarity). Also plays an important role in NK-cells cytotoxicity. Mechanistically, participates in cytotoxic granule movement to the cell surface and perforin trafficking to the lytic granule. In addition, protects NK-cells from degranulation-associated damage induced by their own cytotoxic granule content. Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis (By similarity).
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Cytolytic granule membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane (By similarity). Colocalizes with OSBPL1A at the late endosome (By similarity). {ECO:0000250|UniProtKB:P05300, ECO:0000250|UniProtKB:P11279}.
Interaction partners:
- Lysosome-associated membrane glycoprotein 2
- Cathepsin D
- Serine/threonine-protein kinase mTOR
- NPR2-like, GATOR1 complex subunit
- Early endosome antigen 1
- Regulatory-associated protein of mTOR
- GATOR complex protein NPRL3
- GATOR2 complex protein WDR24
- DEP domain containing 5, GATOR1 subcomplex subunit
- Kaptin
Sequence:
MAAPGARRPLLLLLLAGLAHSAPALFEVKDNNGTACIMASFSASFLTTYDAGHVSKVSNMTLPASAEVLKNSSSCGEKNASEPTLAITFGEGYLLKLTFTKNTTRYSVQHMYFTYNLSDTQFFPNASSKGPDTVDSTTDIKADINKTYRCVSDIRVYMKNVTIVLWDATIQAYLPSSNFSKEETRCPQDQPSPTTGPPSPSPPLVPTNPSVSKYNVTGDNGTCLLASMALQLNITYMKKDNTTVTRAFNINPSDKYSGTCGAQLVTLKVGNKSRVLELQFGMNATSSLFFLQGVQLNMTLPDAIEPTFSTSNYSLKALQASVGNSYKCNSEEHIFVSKALALNVFSVQVQAFRVESDRFGSVEECVQDGNNMLIPIAVGGALAGLVLIVLIAYLIGRKRSHAGYQTI
Protein: Protein lifeguard 4 (Transmembrane BAX inhibitor motif-containing protein 4) (Z-protein) (Q9DA39)
Organism: Mus musculus (Mouse)
Function: Anti-apoptotic protein which can inhibit apoptosis induced by intrinsic and extrinsic apoptotic stimuli. Can modulate both capacitative Ca2+ entry and inositol 1,4,5-trisphosphate (IP3)-mediated Ca2+ release (By similarity).
Subcellular location: Golgi apparatus membrane; Multi-pass membrane protein.
Interaction partners:
- Pancreatic secretory granule membrane major glycoprotein GP2
- Antiviral innate immune response receptor RIG-I
Sequence:
MADTDPGYPRSSIEDDFNYGSCVASASVHIRMAFLRKVYSILSLQVLLTTVTSALFLYFQALRTFVHESPALIVVFALGSLGLIFALTLHRHTHPLNLYLLFAFTLSESLAVAAVVTFYDVYLVLQAFIMTTAVFLGLTAYTLQSKRDFTKFGAGLFAGLWILCLAGFLKLFFYSETMELVLASLGALLFCGFIIYDTHSLMHRLSPEEYVIAAISLYMDIINLFLHLLKFLEAVNKK
Protein: Spastin (EC 5.6.1.1) (A0A2R8Y4I8)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Membrane {ECO:0000256|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03021}. Midbody {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000256|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. Localizes to endoplasmic reticulum tubular network. {ECO:0000256|HAMAP-Rule:MF_03021}.
Interaction partners:
Sequence:
MNSPGGRGKKKGSGGASNPVPPRPPPPCLAPAPPAAGPAPPPESPHKRNLYYFSYPLFVGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPAPASASAPAPVPGGEAERVRVFHKQAFEYISIALRIDEDEKGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLESGAVPKRKDPLTHTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNKPSTPTTATRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
Protein: p-aminobenzoyl-glutamate hydrolase subunit B (EC 3.5.1.-) (PABA-GLU hydrolase) (PGH) (P76052)
Organism: Escherichia coli (strain K12)
Function: Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p-aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified.
Interaction partners:
- p-aminobenzoyl-glutamate hydrolase subunit A
- p-aminobenzoyl-glutamate transport protein
- HTH-type transcriptional regulator AbgR
- Methylated-DNA--protein-cysteine methyltransferase
- Uncharacterized protein YahE
Sequence:
MQEIYRFIDDAIEADRQRYTDIADQIWDHPETRFEEFWSAEHLASALESAGFTVTRNVGNIPNAFIASFGQGKPVIALLGEYDALAGLSQQAGCAQPTSVTPGENGHGCGHNLLGTAAFAAAIAVKKWLEQYGQGGTVRFYGCPGEEGGSGKTFMVREGVFDDVDAALTWHPEAFAGMFNTRTLANIQASWRFKGIAAHAANSPHLGRSALDAVTLMTTGTNFLNEHIIEKARVHYAITNSGGISPNVVQAQAEVLYLIRAPEMTDVQHIYDRVAKIAEGAALMTETTVECRFDKACSSYLPNRTLENAMYQALSHFGTPEWNSEELAFAKQIQATLTSNDRQNSLNNIAATGGENGKVFALRHRETVLANEVAPYAATDNVLAASTDVGDVSWKLPVAQCFSPCFAVGTPLHTWQLVSQGRTSIAHKGMLLAAKTMAATTVNLFLDSGLLQECQQEHQQVTDTQPYHCPIPKNVTPSPLK
Protein: Transmembrane 9 superfamily member 3 (P40071)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: With EMP70 and TMN2, plays a critical role in the late stages of a nutrient-controlled pathway notably regulating FLO11 gene expression. Acts downstream of RAS2 and TOR. Essential for cell adhesion and filamentous growth. May play a role as effector of cellular copper homeostasis.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Lipid phosphate phosphatase 1
Sequence:
MRVRPKRSVITLMAIVVVMLILRNQFYSSRTRGHGQEPVISSSQKNLYDGWITPNFYRKGDPLELIVNKVESDLTQLPYAYYDLPFTCPPTMHKKPLHLSLNEIIRGDRKWESDYKLKFGEDNPCETLCARKTTKEGMQTLDKLVREGYVVQWLIDDELPAATTFISTTDHKKYYASGFPLGFIDPDTDKTYLHNHVMLVIRFHASDNDKNTIVGFEVYPRSVSDYHCPGASKNYEQYEIVIPEDENELTYLPFTYSVYWREEFEVDWNHRWDYFLNAGELSDEQSIQFHWMSLANSVGIVLSISFITLIIYVRVMYTDKSNSKSPKYMINIEGIETEDDLDDDKYGKYSVYTVAKDWIQNGRPNLFGLKVLILLVSFGVQFLFTIIGSLTISCSMNKLHNVRNSVLTMAILFFVLGAFMASFVGTRLSMVTKTKRTKANYLDDNRYLKDYKKFSPIFTILCGSSLPGIVMVSTFLLNSIVWAHDSTSALPFKTIVFFMSIYFIVCIPLSLFGGIVANNIPLPQYWLSGITKDESNSDGNGLFVPKSRAKFNPLVYCGIYLCGIFPLLVIYVEMQYVYKSLWLEKTTFYYFYGFLFLSIILLCVLTMEISIIGSYLLMRFCFEDKVVRNNWRWKCFEMGFSGGVYMELYSLYYIFAVLNIHGFSSILISICYSLIFNVMCSLGLGALSYLTASWFINKIYHQKVNL
Protein: Isocitrate dehydrogenase [NADP] cytoplasmic (IDH) (IDH1) (EC 1.1.1.42) (Cytosolic NADP-isocitrate dehydrogenase) (IDPc) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase) (O88844)
Organism: Mus musculus (Mouse)
Function: Catalyzes the NADP(+)-dependent oxidative decarboxylation of isocitrate (D-threo-isocitrate) to 2-ketoglutarate (2-oxoglutarate), which is required by other enzymes such as the phytanoyl-CoA dioxygenase. Plays a critical role in the generation of NADPH, an important cofactor in many biosynthesis pathways. May act as a corneal epithelial crystallin and may be involved in maintaining corneal epithelial transparency (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12031902}.
Interaction partners:
- Aconitate hydratase, mitochondrial
- Cytoplasmic aconitate hydratase
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Isocitrate dehydrogenase subunit
- Isocitrate dehydrogenase subunit gamma 1, mitochondrial
- Probable isocitrate dehydrogenase gamma 2, mitochondrial
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- Glutamate dehydrogenase 1, mitochondrial
- Citrate synthase, mitochondrial
Sequence:
MSRKIQGGSVVEMQGDEMTRIIWELIKEKLILPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKYNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVTGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPKDGTQKVTYMVHDFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKKYKSQFEAQKICYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLICPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWSRGLAHRAKLDNNTELSFFAKALEDVCIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKAKLAQAKL
Protein: At4g09970 (Transmembrane protein) (Q6DBH2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASLHLGGASLINEVVFGSSLIGFRSKRFKRASERCRFCVQQMSENEQRTKHELARSAKRSESLRRILKQYGVSVENPEESKTSSRLDDLDCEEKHDAVTSSVIDDDSKMNTTEELPDLRRVEKYTETVGTADNLSGQNHQILPHLNTGVLLTSLLPVLGFCIICIIGTLHTIISRKTSQGHHHGSERWRTALMDWNEPLASDGHDSMSPEYRVASTNQEATATDEMNEAYSRVELEYKRFLLECGVGES
Protein: Uncharacterized protein, isoform K (H9XVM8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDSTLNIENVNDPTSIASDLSAENTKADLVSLNEPKTYEPTTIAPDLKMENTKNSIPSPIKPNVNDQTSSASDLTAENTKADHDSLNKPKDFNNQILNIISDIDINIKAQEKITQLKEQELKLIQKQNDLANEIHKQQILAKQLSAQNQLKQNECQSGELDLHSQYQNERGGPTSTLYQEKNIASKESANVSKTVDLRKIFTPATDAAEILPKNRKLYASSAFYSPTLHPTVEDQVELARRISHSLSDISNQTSKGQSMYVNRKKRSDKWVHEGGSQGNDAINPFKENSETKSTMEVAKLEKIPLKLIMNPNGKVRDYNSLKDLINVEAGLLSPDNCAELITALQLHQGRGAELFAKRRRKADNWVVDESHSGTQYHPSGIPDFQQYQQRPVLSPNILPAYSDAGKHRVQLNIHQNQLIEKYSKPGLQVVQSPWKAALQTGSASSAFLEDTKSFSPPALTPIPSSQAGSKDWTDANEPMPHGSSRRNTNAVASSPRSVIVPSNPQRDLAYTPCVAQGWGGRSVELPKDSFQSNESQSSWQTEPHIGRADDSNPSFNNYIFGERLTSNFAFDVQNRLHSLENFQKYFLEYQRLELEILRNRESSRVLQHDAYESLLDFTPQNEFKVISGEDLKVNCDLDEKVNVRELIQSFEKQNTTDLRHDAAPIEGLYVPKEISLSSYAAPSQQCEIHSKHFERPYEDTFPRTFPRNNYSANNNFPGNDGIGEFPLSKPTGLTTGTLHQQPYSPTSYKKTVPGLEKVENFARYEQPDRKRLTSGSPQYLNALQNSQVRNASPIPFGTSLNEQTSWPPRSVLLQGGSPSPLPNHVQTFNKCAKGWGSIPVKQQSYSSQYNLPGNLPYSDF
Protein: Endonuclease MutS2 (EC 3.1.-.-) (Ribosome-associated protein quality control-upstream factor) (RQC-upstream factor) (RqcU) (EC 3.6.4.-) (O25338)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity (Probable). Also involved in repairing oxidative DNA damage. Has ATPase activity. Binds DNA.
Interaction partners:
- Uncharacterized protein
- Small ribosomal subunit protein uS4
- UDP-N-acetylmuramate--L-alanine ligase
- Solute-binding signature and mitochondrial signature protein
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein bS21
- Large ribosomal subunit protein bL20
- Large ribosomal subunit protein bL35
- Large ribosomal subunit protein bL28
- Small ribosomal subunit protein uS15
Sequence:
MSDAPKRSLNPTLMMNNNNTPPKPLEESLDLKEFIALFKTFFAKERDTIALENDLKQTFTYLNEVDAIGLPTPKSVKESDLIIIKLTKLGTLHLDEIFEIVKRLHYIVVLQNAFKTFTHLKFHERLNAIVLPPFFNDLIALFDDEGKIKQGANATLDALNESLNRLKKESVKIIHHYARSKELAPYLVDTQSHLKHGYECLLLKSGFSGAIKGVVLERSANGYFYLLPESAQKIAQKIAQIGNEIDCCIVEMCQTLSHSLQKHLLFLKFLFKEFDFLDSLQARLNFAKAYNLEFVMPSFTQKKMILENFSHPILKEPKPLNLKFEKSMLAVTGVNAGGKTMLLKSLLSAAFLSKHLIPMKINAHHSIIPYFKEIHAIINDPQNSANNISTFAGRMKQFSALLSKENMLLGVDEIELGTDADEASSLYKTLLEKLLKQNNQIIITTHHKRLSVLMAENKEVELLAALYDEEKERPTYTFLKGVIGKSYAFETALRYGVPHFLIEKAKTFYGEDKEKLNVLIENSSALERELKQKNEHLENALKEQEYLKNAWLLEMEKQKEIFHNKKLELEKSYQQALNILKSEVASKDTSSMHKEIHKASEILSKHKTNQEIPQIITNFQANEKARYKNESVLIVQILDKGYYWIETELGMRLKAHGSLLKKIQKPPKNKFKPPKTTIPKPKEASLRLDLRGQRSEEALDLLDAFLNDALLGGFEEVLICHGKGSGILEKFVKEFLKNHPKVVSFSDAPINLGGSGVKIVKL