wanglab/gogpt-training-data huggingface dataset:
Protein: CAAX prenyl protease 2 (EC 3.4.26.1) (Farnesylated proteins-converting enzyme 2) (AtFACE-2) (Prenyl protein-specific endoprotease 2) (Protein RAS-CONVERTING ENZYME 1) (AtRCE1) (Q8GW19)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins. The substrate specificity is only partially overlapping with that of FACE1.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18641086}; Multi-pass membrane protein {ECO:0000269|PubMed:18641086}.
Interaction partners:
- CAAX prenyl protease 1 homolog
- Protein-S-isoprenylcysteine O-methyltransferase B
- Protein-S-isoprenylcysteine O-methyltransferase A
- Protein farnesyltransferase subunit beta
- Isoprenylcysteine alpha-carbonyl methylesterase ICME
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL1
- Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL2
- Farnesol kinase, chloroplastic
- Conserved oligomeric Golgi complex subunit 6
Sequence:
MATDGESISMSLAVATCVAMALFYVLILYVPTVILRLPSASSYTEFMIRRFICAAICTVASLVFTAFILPIKSWEASYILGVYGIRKDHLWQGVVYPLLLTSLVYAGSLVLKLFTLLESWKENGGGCSSFNYIRSFFQTIPASVLTSASNVSVWRNFIVAPVTEELVFRSCMIPLLLCAGFRINTAIFLCPVLFSLAHLNHFREMYIRHNRSYLRASLIVGLQLGYTVIFGAYASFLFIRTGHLAAPLFAHIFCNYMGLPVLYANGKGLVSAAFLGGVVGFVLLLFPLTKPLMYNDSTNDCPCWLGYCLWN
Protein: DNA mismatch repair protein MutH (Methyl-directed mismatch repair protein) (P06722)
Organism: Escherichia coli (strain K12)
Function: Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair.
Subcellular location: Cytoplasm.
Interaction partners:
- DNA mismatch repair protein MutL
- DNA helicase II
- DNA adenine methylase
- Negative modulator of initiation of replication
- Exodeoxyribonuclease 10
- Single-stranded-DNA-specific exonuclease RecJ
- DNA mismatch endonuclease Vsr
- UvrABC system protein A
- UvrABC system protein B
- UPF0053 inner membrane protein YgdQ
Sequence:
MSQPRPLLSPPETEEQLLAQAQQLSGYTLGELAALVGLVTPENLKRDKGWIGVLLEIWLGASAGSKPEQDFAALGVELKTIPVDSLGRPLETTFVCVAPLTGNSGVTWETSHVRHKLKRVLWIPVEGERSIPLAQRRVGSPLLWSPNEEEDRQLREDWEELMDMIVLGQVERITARHGEYLQIRPKAANAKALTEAIGARGERILTLPRGFYLKKNFTSALLARHFLIQ
Protein: HTH-type transcriptional regulator GadX (P37639)
Organism: Escherichia coli (strain K12)
Function: Positively regulates the expression of about fifteen genes involved in acid resistance such as gadA, gadB and gadC. Depending on the conditions (growth phase and medium), can repress gadW.
Interaction partners:
- HTH-type transcriptional regulator GadW
- Transcriptional regulator GadE
- Glutamate decarboxylase alpha
- Protein HdeD
- Glutamate decarboxylase beta
- Glutamate/gamma-aminobutyrate antiporter
- Acid stress chaperone HdeA
- Outer membrane protein Slp
- HTH-type transcriptional regulator DctR
- Acid stress chaperone HdeB
Sequence:
MQSLHGNCLIAYARHKYILTMVNGEYRYFNGGDLVFADASQIRVDKCVENFVFVSRDTLSLFLPMLKEEALNLHAHKKVSSLLVHHCSRDIPVFQEVAQLSQNKNLRYAEMLRKRALIFALLSVFLEDEHFIPLLLNVLQPNMRTRVCTVINNNIAHEWTLARIASELLMSPSLLKKKLREEETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQERSAQRLSNRDSAASIVAQGNFYGTDRSAEGIRL
Protein: Uncharacterized protein C29E6.09 (Q09862)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Stress response protein nst1
- Curved DNA-binding protein
- Small ribosomal subunit protein uS9B
- Probable thiamine biosynthetic bifunctional enzyme
- RNA polymerase II-associated protein 1 homolog
- SWR1-complex protein 5
- Small ribosomal subunit protein uS9A
Sequence:
MLSELPEVIFKGTEFEEQLSNLTSDSQANKRVYEDYDFKDETSAKPIPTEKKLKVFKKDDNVETLLSALEIQNEKSKQQVEYSFIPLKQDDGDILTSPGDFENASTSPVSDVTYVNTKLVDFISSVLLEENQGLALHQLTLKLINIGESFHSLLPINLPYEPYVIANYVERQLRSYISDTSSSKQSLLSLKNSSNGTVYVSTTLPCPVELKPNITAIDTAERNSYLWGILQPPEPSAEGPFTWNGASSHEGDINNNDTELGLIENPMNLETPKIDYATPHIKESNTPLFTYNFNISGFDGDSCIEKFTPLDALGIKPSPIDVDAHFQPEMLPPLFETFS
Protein: Phosphatase and actin regulator 3 (Scaffold-associated PP1-inhibiting protein) (Scapinin) (Q96KR7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus matrix. Note=Localized to the nuclear matrix-intermediate filament scaffold. Isoform 2 is also found in some cytoplasmic extensions.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Chemokine-like protein TAFA-4
Sequence:
MAASEDGSGCLVSRGRSQSDPSVLTDSSATSSADAGENPDEMDQTPPARPEYLVSGIRTPPVRRNSKLATLGRIFKPWKWRKKKNEKLKQTTSALEKKMAGRQGREELIKKGLLEMMEQDAESKTCNPDGGPRSVQSEPPTPKSETLTSEDAQPGSPLATGTDQVSLDKPLSSAAHLDDAAKMPSASSGEEADAGSLLPTTNELSQALAGADSLDSPPRPLERSVGQLPSPPLLPTPPPKASSKTTKNVTGQATLFQASSMKSADPSLRGQLSTPTGSPHLTTVHRPLPPSRVIEELHRALATKHRQDSFQGRESKGSPKKRLDVRLSRTSSVERGKEREEAWSFDGALENKRTAAKESEENKENLIINSELKDDLLLYQDEEALNDSIISGTLPRKCKKELLAVKLRNRPSKQELEDRNIFPRRTDEERQEIRQQIEMKLSKRLSQRPAVEELERRNILKQRNDQTEQEERREIKQRLTRKLNQRPTVDELRDRKILIRFSDYVEVAKAQDYDRRADKPWTRLSAADKAAIRKELNEYKSNEMEVHASSKHLTRFHRP
Protein: 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial (EC 1.14.15.18) (25-OHD-1 alpha-hydroxylase) (25-hydroxyvitamin D(3) 1-alpha-hydroxylase) (VD3 1A hydroxylase) (Calcidiol 1-monooxygenase) (Cytochrome P450 subfamily XXVIIB polypeptide 1) (Cytochrome P450C1 alpha) (Cytochrome P450VD1-alpha) (Cytochrome p450 27B1) (O35084)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase involved in vitamin D metabolism and in calcium and phosphorus homeostasis. Catalyzes the rate-limiting step in the activation of vitamin D in the kidney, namely the hydroxylation of 25-hydroxyvitamin D3/calcidiol at the C1-alpha position to form the hormonally active form of vitamin D3, 1alpha,25-dihydroxyvitamin D3/calcitriol that acts via the vitamin D receptor (VDR). Has 1-alpha-hydroxylase activity on vitamin D intermediates of the CYP24A1-mediated inactivation pathway. Converts 24R,25-dihydroxyvitamin D3/secalciferol to 1-alpha,24,25-trihydroxyvitamin D3, an active ligand of VDR. Also active on 25-hydroxyvitamin D2 (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via FDXR/adrenodoxin reductase and FDX1/adrenodoxin.
Subcellular location: Mitochondrion membrane.
Interaction partners:
- Vitamin D 25-hydroxylase
- 1,25-dihydroxyvitamin D
- Retinoic acid receptor RXR-alpha
- Parathyroid hormone
- Fibroblast growth factor 23
- Vitamin D-binding protein
- Sodium-dependent phosphate transport protein 2A
- Vitamin D3 receptor
- Sodium-dependent phosphate transport protein 2C
- Klotho
Sequence:
MTQAVKLASRVFHRIHLPLQLDASLGSRGSESVLRSLSDIPGPSTLSFLAELFCKGGLSRLHELQVHGAARYGPIWSGSFGTLRTVYVADPTLVEQLLRQESHCPERCSFSSWAEHRRRHQRACGLLTADGEEWQRLRSLLAPLLLRPQAAAGYAGTLDNVVRDLVRRLRRQRGRGSGLPGLVLDVAGEFYKFGLESIGAVLLGSRLGCLEAEVPPDTETFIHAVGSVFVSTLLTMAMPNWLHHLIPGPWARLCRDWDQMFAFAQRHVELREGEAAMRNQGKPEEDMPSGHHLTHFLFREKVSVQSIVGNVTELLLAGVDTVSNTLSWTLYELSRHPDVQTALHSEITAGTRGSCAHPHGTALSQLPLLKAVIKEVLRLYPVVPGNSRVPDRDIRVGNYVIPQDTLVSLCHYATSRDPTQFPDPNSFNPARWLGEGPTPHPFASLPFGFGKRSCIGRRLAELELQMALSQILTHFEVLPEPGALPIKPMTRTVLVPERSINLQFVDR
Protein: V(D)J recombination-activating protein 2 (RAG-2) (P55895)
Organism: Homo sapiens (Human)
Function: Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T-lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. DNA cleavage by the RAG complex occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. The chromatin structure plays an essential role in the V(D)J recombination reactions and the presence of histone H3 trimethylated at 'Lys-4' (H3K4me3) stimulates both the nicking and haipinning steps. The RAG complex also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. The introduction of DNA breaks by the RAG complex on one immunoglobulin allele induces ATM-dependent repositioning of the other allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. In the RAG complex, RAG2 is not the catalytic component but is required for all known catalytic activities mediated by RAG1. It probably acts as a sensor of chromatin state that recruits the RAG complex to H3K4me3 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- V
- Histone H3.2
- Histone H3.1
- Histone H3.3
- Histone H3.3C
- Histone H3.1t
- Histone H3-7
- Transmembrane protein 232
- Cytokine receptor common subunit gamma
- T-cell surface glycoprotein CD4
Sequence:
MSLQMVTVSNNIALIQPGFSLMNFDGQVFFFGQKGWPKRSCPTGVFHLDVKHNHVKLKPTIFSKDSCYLPPLRYPATCTFKGSLESEKHQYIIHGGKTPNNEVSDKIYVMSIVCKNNKKVTFRCTEKDLVGDVPEARYGHSINVVYSRGKSMGVLFGGRSYMPSTHRTTEKWNSVADCLPCVFLVDFEFGCATSYILPELQDGLSFHVSIAKNDTIYILGGHSLANNIRPANLYRIRVDLPLGSPAVNCTVLPGGISVSSAILTQTNNDEFVIVGGYQLENQKRMICNIISLEDNKIEIREMETPDWTPDIKHSKIWFGSNMGNGTVFLGIPGDNKQVVSEGFYFYMLKCAEDDTNEEQTTFTNSQTSTEDPGDSTPFEDSEEFCFSAEANSFDGDDEFDTYNEDDEEDESETGYWITCCPTCDVDINTWVPFYSTELNKPAMIYCSHGDGHWVHAQCMDLAERTLIHLSAGSNKYYCNEHVEIARALHTPQRVLPLKKPPMKSLRKKGSGKILTPAKKSFLRRLFD
Protein: Trans-cinnamate:CoA ligase, peroxisomal (Cinnamic acid:CoA ligase) (Ph-CNL) (PhCNL) (EC 6.2.1.-) ((E)-caffeate:CoA ligase CNL) (EC 6.2.1.-) (4-coumarate:CoA ligase CNL) (EC 6.2.1.12) (Protein ACYL-ACTIVATING ENZYME) (PhAAE) (I3PB36)
Organism: Petunia hybrida (Petunia)
Function: Involved in the biosynthesis of floral volatile benzenoid/phenylpropanoid (FVBP) scent (e.g. benzylbenzoate, phenylethylbenzoate, and methylbenzoate). Catalyzes the formation of CoA esters of cinnamic acid, and, with lower efficiency, of 4-coumaric acid and caffeic acid.
Subcellular location: Peroxisome {ECO:0000269|PubMed:22649270, ECO:0000269|PubMed:22771854}. Note=Located in the peroxisomes of flower petal limb cells. {ECO:0000269|PubMed:22771854}.
Interaction partners:
Sequence:
MDELPKCGANYVPLTPLTFLTRAFKSYANRTSIIYAGARFTWEQTYKRCCRLASSLQSLNIVKNDVVSVLAPNVPATYEMHFAVPMAGAVLNTINTRLDPMNIAIILKHSEAKLLFVDYEYLEKARKALELLMSTNFITAQNSKKISMPQVILIDDLYSPTRIQQQDQLEYEQLVHQGNPEYAPENIVDDEWDPIVLNYTSGTTSEPKGVVYSHRGAFLSTLNTIMGWEMGTEPVYLWSLPMFHINGWTLTWGIAARGGTNVCIRNTTAQEIYSNITLHKVTHMCCAPTVFNILLEAKPHERREITTPVQVMVGGAPPPTTLIGKIEELGFHVVHCYGITEAGGTTLVCEWQSEWNKLSREDQANLKARQGISVLALEDVDVKNSKTMQSVPHNGKTMGEICLRGSSIMKGYFKNDKANSQVFKNGWFLTGDVAVIHQDGYLEIKDRCKDIIISGGENISSIEVENAILKHPSVIEAAVVAMPHPRWGETPCAFVIKTKNPEIKEADIIVHCKKELPGFMVPKHVQFLEELPKTGTGKVKKLQLREMAKSFGIFDNANQTSQILDLPARL
Protein: Pre-B-cell leukemia transcription factor 2 (Homeobox protein PBX2) (Protein G17) (P40425)
Organism: Homo sapiens (Human)
Function: Transcriptional activator that binds the sequence 5'-ATCAATCAA-3'. Activates transcription of PF4 in complex with MEIS1.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeobox protein PKNOX1
- Homeobox protein Meis2
- Homeobox protein Hox-A10
- Homeobox protein Hox-A9
- Homeobox protein Hox-B7
- Putative nucleotidyltransferase MAB21L1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- Homeobox protein Hox-C9
- Homeobox protein PKNOX2
- Sodium-coupled neutral amino acid symporter 2
Sequence:
MDERLLGPPPPGGGRGGLGLVSGEPGGPGEPPGGGDPGGGSGGVPGGRGKQDIGDILQQIMTITDQSLDEAQAKKHALNCHRMKPALFSVLCEIKEKTGLSIRSSQEEEPVDPQLMRLDNMLLAEGVAGPEKGGGSAAAAAAAAASGGGVSPDNSIEHSDYRSKLAQIRHIYHSELEKYEQACNEFTTHVMNLLREQSRTRPVAPKEMERMVSIIHRKFSAIQMQLKQSTCEAVMILRSRFLDARRKRRNFSKQATEVLNEYFYSHLSNPYPSEEAKEELAKKCGITVSQVSNWFGNKRIRYKKNIGKFQEEANIYAVKTAVSVTQGGHSRTSSPTPPSSAGSGGSFNLSGSGDMFLGMPGLNGDSYSASQVESLRHSMGPGGYGDNLGGGQMYSPREMRANGSWQEAVTPSSVTSPTEGPGSVHSDTSN
Protein: LD44235p (Veloren, isoform B) (Veloren, isoform D) (Q8MR14)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNDEDFSRGDVRDLSDIPEADQFSASLKCSCVRLVPYRFEITEPVCFTTKGVRIAGILKDKDEKFELNIHKQEVIKVIAHFGNVEPAQPLVTLYLLKTCAEYVKNQLKLPDDQHHEHTGFKTHSYHTRRLILLFDSISVSARGNIKSMFSCVDEISSTDAAEILERIADSDRKTQDKSSQPPPRQLRADEQVSLLMYPPKGTGGLCIRMEDFVCLTKESYLNDIIIDFYLLWLRNTLIPEPQRERTHIFSTFFYKRLTTLTRPADMKQTAAQKRHARVQKWTKGVDIFDKDFIIVPINEQSHWFLAIICYPNLKGPVTFDTNQPVEPQQLKRPRGKKVALQIGNTTITPLTKRAEGGQLPAALTAENVCRIADDESERDEAEGDESDMASEDSENSNSAKEPAATPTSTTASTPSLSSSQPTATGPARNIASDDVPAVKQPLILIFDSLAGASRSRVVATLRDYLTCEYRVKKPDAQAHVFNKDNMPGHCVKVPQQNNFTDCGLYLLQYVEQFFGEPIRDYRLPIKQLTNWFDFLTVTKKREDIANLIQQLMDEGNQQQRLILPVIEFPTLNGQLVEYPEDTESAEFEEEEGHDDEDPASEMHDENNAGTDMEVDPVNEEPALAGKTAALAPASTTAAAPTGKRFVLKRRLHNGAVSSPTNGNGEASSNGGALIPQLVSTAAATTTGVSSGVAHLGPRGPSGGLKIRKIEP
Protein: Pentatricopeptide repeat-containing protein CRR2, chloroplastic (Plant combinatorial and modular protein H54) (AtPCMP-H54) (Protein CHLORORESPIRATORY REDUCTION 2) (Q9STF3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the intergenic processing between chloroplast rsp7 and ndhB transcripts. Necessary for chloroplast NADH dehydrogenase-like (NDH) complex-dependent cyclic electron transport around PSI (CET).
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Protein DAY-LENGTH-DEPENDENT DELAYED-GREENING 1, chloroplastic
- RNA-binding
- Membrane lipoprotein
- KH domain-containing protein At3g08620
- At2g37400
- RNA-binding
- Tetratricopeptide repeat
- Small ribosomal subunit protein uS4m
- U4/U6 small nuclear ribonucleoprotein Prp31 homolog
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
Sequence:
MFLSHPPQVIQPTYHTVNFLPRSPLKPPSCSVALNNPSISSGAGAKISNNQLIQSLCKEGKLKQAIRVLSQESSPSQQTYELLILCCGHRSSLSDALRVHRHILDNGSDQDPFLATKLIGMYSDLGSVDYARKVFDKTRKRTIYVWNALFRALTLAGHGEEVLGLYWKMNRIGVESDRFTYTYVLKACVASECTVNHLMKGKEIHAHLTRRGYSSHVYIMTTLVDMYARFGCVDYASYVFGGMPVRNVVSWSAMIACYAKNGKAFEALRTFREMMRETKDSSPNSVTMVSVLQACASLAALEQGKLIHGYILRRGLDSILPVISALVTMYGRCGKLEVGQRVFDRMHDRDVVSWNSLISSYGVHGYGKKAIQIFEEMLANGASPTPVTFVSVLGACSHEGLVEEGKRLFETMWRDHGIKPQIEHYACMVDLLGRANRLDEAAKMVQDMRTEPGPKVWGSLLGSCRIHGNVELAERASRRLFALEPKNAGNYVLLADIYAEAQMWDEVKRVKKLLEHRGLQKLPGRCWMEVRRKMYSFVSVDEFNPLMEQIHAFLVKLAEDMKEKGYIPQTKGVLYELETEEKERIVLGHSEKLALAFGLINTSKGEPIRITKNLRLCEDCHLFTKFISKFMEKEILVRDVNRFHRFKNGVCSCGDYW
Protein: Ventral anterior homeobox 2 (Ventral retina homeodomain protein) (Q9WTP9)
Organism: Mus musculus (Mouse)
Function: Transcription factor that may function in dorsoventral specification of the forebrain. Regulates the expression of Wnt signaling antagonists including the expression of a truncated TCF7L2 isoform that cannot bind CTNNB1 and acts therefore as a potent dominant-negative Wnt antagonist. Plays a crucial role in eye development and, in particular, in the specification of the ventral optic vesicle. May be a regulator of axial polarization in the retina.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeobox protein SIX6
Sequence:
MGDGGAERDRGPKRREEPGGRSGRHGEHRGAEDLRADTGSASPREIAGTSASSPAGSRESGGDSDGQQALGETDHCRRILVRDAKGTIREIVLPKGLDLDRPKRTRTSFTAEQLYRLEMEFQRCQYVVGRERTELARQLNLSETQVKVWFQNRRTKQKKDQSRDLEKRASSSASEAFATSNVLRLLEQGRLLSVPRAPSLLALTPGLPGLPASHRGTSLVDPRNSSPRLNPMPSASASSPLPPPLPAICFSSAPLLDLPAGYKLGSSAFEPYSRLEQQKVGSPGQSDKKADI
Protein: FAS-associated death domain protein (FAS-associating death domain-containing protein) (Mediator of receptor induced toxicity) (Q61160)
Organism: Mus musculus (Mouse)
Function: Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q13158}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 6
- Tumor necrosis factor receptor superfamily member 10B
- Caspase-8
- Receptor-interacting serine/threonine-protein kinase 1
- CASP8 and FADD-like apoptosis regulator
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Receptor-interacting serine/threonine-protein kinase 3
- Tumor necrosis factor receptor superfamily member 1A
- Tumor necrosis factor ligand superfamily member 6
- TNF receptor-associated factor 2
Sequence:
MDPFLVLLHSLSGSLSGNDLMELKFLCRERVSKRKLERVQSGLDLFTVLLEQNDLERGHTGLLRELLASLRRHDLLQRLDDFEAGTATAAPPGEADLQVAFDIVCDNVGRDWKRLARELKVSEAKMDGIEEKYPRSLSERVRESLKVWKNAEKKNASVAGLVKALRTCRLNLVADLVEEAQESVSKSENMSPVLRDSTVSSSETP
Protein: D-amino-acid oxidase (DAAO) (DAMOX) (DAO) (EC 1.4.3.3) (Q9Y7N4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:C4R4G9}.
Interaction partners:
- Putative glycine dehydrogenase
- Probable serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Probable low-specificity L-threonine aldolase
- L-pipecolate oxidase
- 5-aminolevulinate synthase, mitochondrial
- Mitochondrial 2-methylisocitrate lyase
- Putative 2-hydroxyacid dehydrogenase UNK4.10
- Alanine racemase, catabolic
- Fumarate reductase
Sequence:
MTKENKPRDIVIVGAGVIGLTTAWILSDLGLAPRIKVIAKYTPEDRSVEYTSPWAGANFCSISATDDNALRWDKITYHRFAYLAKTRPEAGIRFADLRELWEYEPKHDKIRSWNTYVRDFKVIPEKDLPGECIYGHKATTFLINAPHYLNYMYKLLIEAGVEFEKKELSHIKETVEETPEASVVFNCTGLWASKLGGVEDPDVYPTRGHVVLVKAPHVTETRILNGKNSDTYIIPRPLNGGVICGGFMQPGNWDREIHPEDTLDILKRTSALMPELFHGKGPEGAEIIQECVGFRPSRKGGARVELDVVPGTSVPLVHDYGASGTGYQAGYGMALDSVMLALPKIKLA
Protein: DNA-directed RNA polymerase 3, chloroplastic (EC 2.7.7.6) (Protein SCABRA 3) (O24600)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nuclear-encoded DNA-dependent RNA polymerase that catalyzes the transcription of DNA into RNA in chloroplasts using the four ribonucleoside triphosphates as substrates (Probable). Required for chloroplast development and leaf mesophyll cell proliferation.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:10205908}.
Interaction partners:
- Ribosomal RNA small subunit methyltransferase, mitochondrial-N
- DNA-directed RNA polymerase subunit beta
- Ribosomal RNA small subunit methyltransferase, chloroplastic
- Ribosomal RNA small subunit methyltransferase-N
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta'
- Protein TPLATE
- DNA-directed RNA polymerase subunit beta''
- RNA polymerase sigma factor sigF, chloroplastic
- RNA polymerase sigma factor sigE, chloroplastic/mitochondrial
Sequence:
MASAAAASPSLSLNPTSHFQHQTSLVTWLKPPPSSALFRRKTLPFFERHSLPISASSSSSSSSSTSLSVHEKPISNSVHFHGNLIESFENQDSSYAGTIKGASLIEELENPVERNGLSGRRRLFMQDPPWISALFLKGLSKMVDQTLKIERKDIDKRKFDSLRRRQVKEETEAWERMVDEYRDLEKEMCEKNLAPNLPYVKHMFLGWFQPLKDVIEREQKLQKNKSKKVRAAYAPHIELLPADKMAVIVMHKMMGLVMSGHEDGCIQVVQAAVSIGIAIEQEVRIHNFLKRTRKNNAGDSQEELKEKQLLRKRVNSLIRRKRIIDALKVVKSEGTKPWGRATQAKLGSRLLELLIEAAYVQPPLTQSGDSIPEFRPAFRHRFKTVTKYPGSKLVRRYGVIECDSLLLAGLDKSAKHMLIPYVPMLVPPKRWKGYDKGGYLFLPSYIMRTHGSKKQQDALKDISHKTAHRVFEALDTLGNTKWRVNRNILDVVERLWADGGNIAGLVNREDVPIPEKPSSEDPEELQSWKWSARKANKINRERHSLRCDVELKLSVARKMKDEEGFYYPHNLDFRGRAYPMHPHLNHLSSDLCRGTLEFAEGRPLGKSGLHWLKIHLANLYAGGVEKLSHDARLAFVENHLDDIMDSAENPIHGKRWWLKAEDPFQCLAACVILTQALKSPSPYSVISHLPIHQDGSCNGLQHYAALGRDSFEAAAVNLVAGEKPADVYSEISRRVHEIMKKDSSKDPESNPTAALAKILITQVDRKLVKQTVMTSVYGVTYVGAREQIKRRLEEKGVITDERMLFAAACYSAKVTLAALGEIFEAARAIMSWLGDCAKIIASDNHPVRWITPLGLPVVQPYCRSERHLIRTSLQVLALQREGNTVDVRKQRTAFPPNFVHSLDGTHMMMTAVACREAGLNFAGVHDSYWTHACDVDTMNRILREKFVELYNTPILEDLLQSFQESYPNLVFPPVPKRGDFDLKEVLKSQYFFN
Protein: SRCR domain-containing protein (Q8C9T4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAFSFLRLWPLLLLTCWTLVPDLALENFVSFLGGDNKCEGQVRLRNGGQWGLMCADGLGMQEASVICRELGCGSVKFMPRYVLTPEEMRQPWLYDAQCHGNESTFLECRLGSWGTISGCKCQCVAVITCSGGTTLQMGLVDGGSPCAGTAQATGASNFALRCDLHEKEAGVVCRQLECGTALQWSRAHDGTNGNQEQKYLTCQGTETNILQCLINVNVLEQCDLLTYTQVVCTGHVEARLLGGVHPCEGRLEVLRGLTWGTVCHDDLDLPMAHVVCRELGCGTAVSILGSSHFGYGSGPLWTEAFRCMGNESLLFHCLREPGHQCGHDQDAALICSGEKFRLVNGSSRCEGRVELLVQDAWQPLCAANWDLADATVLCHQLNCGYAVATPQGGHFGNVEGPIRTDVFHCVGTEPHLLSCPTSTLGAQACALGNSASALCSGECRQP
Protein: Low density lipoprotein-related protein 1 variant (Q59FG2)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
VCFVCLSHLLPPDSVYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSRRITIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNEQHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKHVGSNMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQDDLTCRAVNSSCRAQDEFECANGECINFSLTCDGVPHCKDKSDEKPSYCNSRRCKKTFRQCSNGRCVSNMLWCNGADDCGDGSDEIPCNKTACGVGEFRCRDGTCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCEHGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCADGADESIAAGCLYNSTCDDREFMCQNRQCIPKHFVCDHDRDCADGSDESPECEYPTCGPSEFRCANGRCLSSRQWECDGENDCHDQSDEAPKNPHCTSPEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDSSDERGCHINECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADVDECSTTFPCSQRCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYREQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSSRSVIVDTKITWPNGLTLDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGTNKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGSDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECARFVCPPNRPFRCKNDRVCLWIGRQCDGTDNCGDGTDEEDCEPPTAHTTHCKDKKEFLCRNQRCLSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASICGDEARCVRTEKAAYCACRSGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQAFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAADSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLVNLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCNLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEHCRNGGTCAASPSGMPTCRCPTGFTGPKCTQQVCAGYCANNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGYCENFGTCQMAADGSRQCRCTAYFEGSRCEVNKCSRCLEGACVVNKQSGDVTCNCTDGRVAPSCLTCVGHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEHVFSQQQPGHIASILIPLLLLLLLVLVAGVVFWYKRRVQGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA
Protein: Cysteine peptidase (EC 3.4.22.-) (Q585F0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Inhibitor of cysteine peptidase
Sequence:
MPRTEMVRFVRLPVVLLAMAACLASVALGSLHVEESLEMRFAAFKKKYGKVYKDAKEEAFRFRAFEENMEQAKIQAAANPYATFGVTPFSDMTREEFRARYRNGASYFAAAQKRLRKTVNVTTGRAPAAVDWREKGAVTPVKDQGQCGSCWAFSTIGNIEGQWQVAGNPLVSLSEQMLVSCDTIDSGCNGGLMDNAFNWIVNSNGGNVFTEASYPYVSGNGEQPQCQMNGHEIGAAITDHVDLPQDEDAIAAYLAENGPLAIAVDATSFMDYNGGILTSCTSEQLDHGVLLVGYNDNSNPPYWIIKNSWSNMWGEDGYIRIEKGTNQCLMNQAVSSAVVGGPTPPPPPPPPPSATFTQDFCEGKGCTKGCSHATFPTGECVQTTGVGSVIATCGASNLTQIIYPLSRSCSGPSVPITVPLDKCIPILIGSVEYHCSTNPPTKAARLVPHQ
Protein: BTB/POZ domain-containing protein kctd15-like (Q5XJ34)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- SUMO-conjugating enzyme UBC9-B
- Transcription factor AP-2-alpha
Sequence:
MSRLSLTRSPVSPLAAQGIPLPAQLTKSNAPVHIDVGGHMYTSSLATLTKYPDSRISRLFNGTEPIVLDSLKQHYFIDRDGEIFRYILSYLRTSKLLLPEDFKEFQLLYEEARYYQLTPMVKELERWKQEREQRRSAQPCECLVVRVTPDLGERIAVSGDKSLIEEIFPETGDVMCNSVNAGWNQDPTHVIRFPLNGYCRLNSVQVLERLFQKGFSMVASCGGGVDSSQFSEYILSREDRRCQTSHTPIRIKQEPLD