wanglab/gogpt-training-data huggingface dataset:
Protein: 6-phosphogluconate dehydrogenase, decarboxylating 1 (OsG6PGH1) (EC 1.1.1.44) (Q9LI00)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Ribulose-phosphate 3-epimerase, cytoplasmic isoform
- Glucose-6-phosphate 1-dehydrogenase
- Ribulose-phosphate 3-epimerase, chloroplastic
- Glucose-6-phosphate 1-dehydrogenase
- Os01g0926300 protein
- Os08g0154300 protein.
- Glucose-6-phosphate 1-dehydrogenase
- Glucose-6-phosphate 1-dehydrogenase
- Glucose-6-phosphate 1-dehydrogenase
- Probable 6-phosphogluconolactonase 4, chloroplastic
Sequence:
MAVTRIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETVQRAKVEGNLPVYGFHDPASFVNSIQKPRVVIMLVKAGAPVDQTIATLAAHLEQGDCIIDGGNEWYENTERREKAMEERGLLYLGMGVSGGEEGARNGPSLMPGGSFEAYKYIEDILLKVAAQVPDSGPCVTYIGKGGSGNFVKMVHNGIEYGDMQLISEAYDVLKSVGKLTNSELQQVFSEWNKGELLSFLIEITADIFSIKDDQGSGHLVDKVLDKTGMKGTGKWTVQQAAELSVAAPTIEASLDSRFLSGLKDERVEAAKVFQGDFSSNLPVDKAQLIEDVRQALYASKICSYAQGMNIIKAKSMEKGWSLNLGELARIWKGGCIIRAIFLDRIKKAYDRNSDLANLLVDPEFAQEIMDRQAAWRRVVCLAINNGVSTPGMSASLAYFDSYRRDRLPANLVQAQRDYFGAHTYERVDMPGSFHTEWFKIARAAKM
Protein: Large ribosomal subunit protein uL18B (60S ribosomal protein L5-B) (O74306)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000250|UniProtKB:P26321}.
Interaction partners:
- Elongation factor 3
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL28
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL29
Sequence:
MPFIKAVKSSPYFSRYQTKYRRRREGKTDYYARKRLIAQAKNKYNAPKYRLVVRFSNRFVTCQIVSSRVNGDYVLAHAHSSELPRYGIKWGLANWTAAYATGLLVARRALAKVGLADKYEGVTEPEGEFELTEAIEDGPRPFKVFLDVGLKRTSTGSRVFGAMKGASDGGLFIPHSPNRFPGFDIETEELDDETLRKYIYGGHVAEYMEMLIDDDEERYQKQFSGLIADGIESDQLEDIYAEAYAKIREDPSFQKSGKDAAAFKAESLKYTQRKLTAEERKERFNAKVIEAGRA
Protein: Endoglin (A0A8I6A813)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGPAPWVTLPLVDSLAERVGCDLQRVDSTRGEVTYTTSQVSEGCVAQVANAAHEVHVLFLNLSRRKSEVELTLQASKQNGTETREVFLVFISNENVLVKLQAPEIPLHLVYNSSLEVFKGPKVNSTPLPSFTSKTQILDWAATKGTITSIAALDDPKSIVLRLGQDPKAPPFCFPEAQKDMGVTLEWQPRTQTPVQGCHLEGVTGHKEAYVLRIRSGSEAGPRTVTVTVKLSCTSGDAVLILQGPPYVSWLIDTNHNMQIWTTGEYSIKIFPENNIKGFELPDTPQGLIGEARKLNASIVTFVEIPLTSDVSLTVSSCGGGLQTSPAPVVTTPPKDTCSPELLMSLIQPKCGNDVMTLALNKKLVQTLQCTITGLAFWDSSCQAKDQDGHLVLSSTYSSCGMKVTDHVISNEVRLGIRKKKVQCIDMDSLSFQLGLYLSPHFLQASNTIELGQQGFVQVSMSPLTSEVTVQLDSCHLDLGPEGDMVELIQSRAAKGSCVSLLSPSPEGDPRFSFLLRVYMVPTPAAGTLSCNLALHPSTLSQEVYKTVSMRLNIVSPDLSGKGLVLPSVLGITFGAFLIGALLTAALWYIYSHTRAPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA
Protein: Sporulation-specific protein 12 (P17123)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: It is required for meiosis I chromosome division during sporulation. A component of the FEAR (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase.
Interaction partners:
- Cell cycle protein kinase DBF2
- Tyrosine-protein phosphatase CDC14
- Separin
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Kinetochore protein SLK19
- Guanine nucleotide exchange factor LTE1
- Protein TEM1
- Securin
- G2/mitotic-specific cyclin-2
- Cell division control protein 15
Sequence:
MSNKASDQSARTASILKTDITRENTITRSSSSNNDNYHHHNNINNYNESAKTGEDANKENIPNLEEEIAAFRIFRKKSTSNLKSSHTTSNLVKKTMFKRDLLKQDPKRKLQLQQRFASPTDRLVSPCSLKLNEHKVKMFGKKKKVNPMKLNFKGNLAADSEDVEIDEDEEYFY
Protein: Flavin prenyltransferase UbiX (EC 2.5.1.129) (Q9HX08)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
Interaction partners:
- Pyrrole-2-carboxylic acid decarboxylase
- 3-octaprenyl-4-hydroxybenzoate carboxy-lyase
- 4-hydroxybenzoate octaprenyltransferase
- Probable FAD-dependent monooxygenase
- UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase
- YceK/YidQ family lipoprotein
- 3-dehydroquinate dehydratase 2
- Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE
- Probable protein kinase UbiB
Sequence:
MSGPERITLAMTGASGAQYGLRLLDCLVQEEREVHFLISKAAQLVMATETDVALPAKPQAMQAFLTEYCGAAAGQIRVFGQNDWMAPPASGSSAPNAMVICPCSTGTLSAVATGACNNLIERAADVALKERRPLVLVPREAPFSSIHLENMLKLSNLGAVILPAAPGFYHQPQSVEDLVDFVVARILNTLGIPQDMLPRWGEQHLVSDE
Protein: HLA class I histocompatibility antigen, C alpha chain (HLA-C) (HLA-Cw) (Human leukocyte antigen C) (P10321)
Organism: Homo sapiens (Human)
Function: Antigen-presenting major histocompatibility complex class I (MHCI) molecule with an important role in reproduction and antiviral immunity. In complex with B2M/beta 2 microglobulin displays a restricted repertoire of self and viral peptides and acts as a dominant ligand for inhibitory and activating killer immunoglobulin receptors (KIRs) expressed on NK cells. In an allogeneic setting, such as during pregnancy, mediates interaction of extravillous trophoblasts with KIR on uterine NK cells and regulate trophoblast invasion necessary for placentation and overall fetal growth. During viral infection, may present viral peptides with low affinity for KIRs, impeding KIR-mediated inhibition through peptide antagonism and favoring lysis of infected cells. Presents a restricted repertoire of viral peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-C-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected cells, particularly in chronic viral infection settings such as HIV-1 or CMV infection. Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (By similarity). Typically presents intracellular peptide antigens of 9 amino acids that arise from cytosolic proteolysis via proteasome. Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9. Preferentially displays peptides having a restricted repertoire of hydrophobic or aromatic amino acids (Phe, Ile, Leu, Met, Val and Tyr) at the C-terminal anchor.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18420581, ECO:0000269|PubMed:20972337, ECO:0000269|PubMed:28649982}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:18420581}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Killer cell immunoglobulin-like receptor 2DL3
- Beta-2-microglobulin
- Killer cell immunoglobulin-like receptor 2DL1
- Natural killer cells antigen CD94
- HLA class I histocompatibility antigen, A alpha chain
- HLA class I histocompatibility antigen, B alpha chain
- Leukocyte immunoglobulin-like receptor subfamily B member 1
- Killer cell immunoglobulin-like receptor 3DL1
- T-cell surface glycoprotein CD8 alpha chain
- HLA class I histocompatibility antigen, alpha chain F
Sequence:
MRVMAPRALLLLLSGGLALTETWACSHSMRYFDTAVSRPGRGEPRFISVGYVDDTQFVRFDSDAASPRGEPRAPWVEQEGPEYWDRETQKYKRQAQADRVSLRNLRGYYNQSEDGSHTLQRMSGCDLGPDGRLLRGYDQSAYDGKDYIALNEDLRSWTAADTAAQITQRKLEAARAAEQLRAYLEGTCVEWLRRYLENGKETLQRAEPPKTHVTHHPLSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGQEQRYTCHMQHEGLQEPLTLSWEPSSQPTIPIMGIVAGLAVLVVLAVLGAVVTAMMCRRKSSGGKGGSCSQAACSNSAQGSDESLITCKA
Protein: Activity-dependent neuroprotector homeobox protein 2 (ADNP homeobox protein 2) (Zinc finger protein 508) (Q6IQ32)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation. May play a role in neuronal function; perhaps involved in protection of brain tissues from oxidative stress. May be involved in erythroid differentiation (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Chromobox protein homolog 1
- Chromobox protein homolog 3
Sequence:
MFQIPVENLDNIRKVRKKVKGILVDIGLDSCKELLKDLKGFDPGEKYFHNTSWGDVSLWEPSGKKVRYRTKPYCCGLCKYSTKVLTSFKNHLHRYHEDEIDQELVIPCPNCVFASQPKVVGRHFRMFHAPVRKVQNYTVNILGETKSSRSDVISFTCLKCNFSNTLYYSMKKHVLVAHFHYLINSYFGLRTEEMGEQPKTNDTVSIEKIPPPDKYYCKKCNANASSQDALMYHILTSDIHRDLENKLRSVISEHIKRTGLLKQTHIAPKPAAHLAAPANGSAPSAPAQPPCFHLALPQNSPSPAAGQPVTVAQGAPGSLTHSPPAAGQSHMTLVSSPLPVGQNSLTLQPPAPQPVFLSHGVPLHQSVNPPVLPLSQPVGPVNKSVGTSVLPINQTVRPGVLPLTQPVGPINRPVGPGVLPVSPSVTPGVLQAVSPGVLSVSRAVPSGVLPAGQMTPAGQMTPAGVIPGQTATSGVLPTGQMVQSGVLPVGQTAPSRVLPPGQTAPLRVISAGQVVPSGLLSPNQTVSSSAVVPVNQGVNSGVLQLSQPVVSGVLPVGQPVRPGVLQLNQTVGTNILPVNQPVRPGASQNTTFLTSGSILRQLIPTGKQVNGIPTYTLAPVSVTLPVPPGGLATVAPPQMPIQLLPSGAAAPMAGSMPGMPSPPVLVNAAQSVFVQASSSAADTNQVLKQAKQWKTCPVCNELFPSNVYQVHMEVAHKHSESKSGEKLEPEKLAACAPFLKWMREKTVRCLSCKCLVSEEELIHHLLMHGLGCLFCPCTFHDIKGLSEHSRNRHLGKKKLPMDYSNRGFQLDVDANGNLLFPHLDFITILPKEKLGEREVYLAILAGIHSKSLVPVYVKVRPQAEGTPGSTGKRVSTCPFCFGPFVTTEAYELHLKERHHIMPTVHTVLKSPAFKCIHCCGVYTGNMTLAAIAVHLVRCRSAPKDSSSDLQAQPGFIHNSELLLVSGEVMHDSSFSVKRKLPDGHLGAEDQRHGEEQPPILNADAAPGPEKVTSVVPFKRQRNESRTEGPIVKDEALQILALDPKKYEGRSYEEKKQFLKDYFHKKPYPSKKEIELLSSLFWVWKIDVASFFGKRRYICMKAIKNHKPSVLLGFDMSELKNVKHRLNFEYEP
Protein: Transmembrane protein (G5EEV8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSLVTTRGGFILLLLFATLASPKKAVVVDEDTIIFDDYTPGMGNSASAKQVADQVAYGVISCITVGVLIVMLYMSVFGQRVRATAVRWHVLNCSLWGILHLISYASFAEKAPWPNYITNQNWRDTARQVECFTRSVFPAGMVFVYLEQIILTIAPKLANSIVFNAIFFILLIPFLNGLMIFLYYAHFMDIVWWYEPIDLFNLATYLIFTTFTFIYFLFCLFGTCLCCATMTSKKPSSRTTGTFADMWLLFPYGLIPSIMYGPSFGMTSVSFAMQHLLTWVLESGLLTGGGGSSSGGSFIDMNLLMQVATNAILAMPWFVLLFPLVQSILALVCLRMFREQFFFMISCGRIFEGKRAKIGMTEWNVTSIGPPPLYPNSPSEKQEA
Protein: V-type proton ATPase subunit a (Q9CTA9)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
GVSAVAHRIPCQDMPPTLIRTNRFTSSFQGIVDAYGVGRYREVNPAPYTIITFPFLFAVMFGDVGHGLLMFLFALAMVLTENRPAVKAAQNEIWQTFFGGRYLLLLMGLFSVYTGFIYNECFSRATTIFPSGWSVAAMANQSGWSDEYLSQHSMLTLNPNITGVFLGPYPFGIDPIWSLATNHLSFLNSFKMKMSVILGVTHMAFGVFLSIFNHVHFGQAHRLLLETLPELIFLLGLFGYLVFLIVYKWVNVSAASASSAPSILIHFINMFLFSQNPTNHLLFHGQEVVQYVLVVLALATVPILLLGTPLYLVRQHRHRRNTQRRPAGQQDEDTDKLLASPDASTLENSWSPDEEKAGSPGDEETEFVPSEIFMHQAIHTIEFCLGCISNTASYLRLWALSLAHAQLSEVLWAMVMRIGLGMGREIGVAAVVLVPVFAAFAVLTVAILLVMEGLSAFLHALRLHWVEFQNKFYSGTGYKLSPFTFTVDSD
Protein: RE19290p (Q8SX41)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAEIREDEEEKKSGISILPGPELLALPGFDTRASIASAALSDVPSDVIIKSRIRYGSPLSACKGLLLEYAKSTTIHGIRYIFEVHRPIYEKLYWLFFTCISVYFAVSLIWDTYLKWQESPVILGFDETLVPVHKIPFPTITICPEIKMERNVFDYTNVSRQLWEEYKQNGNISDLDDEDLARMAVAMHICDSEVVQRFTPLLSQLNPPNVDVTQTLIDLSISKNETGPFCKWNGRFYFCDKIFDFVATDEGICYQFNGLRPKDIYRDEKFISYVDPDVVDFNKYFDVDLPPWNNITGNWSLDTGFVDQGQNAYPQRTVFSSVKNGFFAFLQGLQHNFDYDCRSFKQGYKVFLNSPESVPLTTGNYILVPHGDEVLVSVLPAYVVSTDNLHEITPEKRQCLFDDERSLRFFRSYSQSNCQTECLANYTVSKCGCAKFWMPKPLGTPVCGLKDISCYTSAQDELYTLMQNQTMAKSIDESVDITCNCMPACTSLEYNFEISRAKYDVAKTIRAFREEYEHTDAIGSRLSVYFKEHQFTAIKRTILFGVSTLISNCGGICGLFMGISCLSFLELIYFFCMRICGSCRDRRKHKIQQQNSVDLPEEKSEN
Protein: Solute carrier family 35 member E3 (Bladder cancer-overexpressed gene 1 protein) (Q7Z769)
Organism: Homo sapiens (Human)
Function: Putative transporter.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- UPF0235 protein C15orf40
- Nuclear pore complex protein Nup107
- E3 ubiquitin-protein ligase Mdm2
Sequence:
MALLVDRVRGHWRIAAGLLFNLLVSICIVFLNKWIYVYHGFPNMSLTLVHFVVTWLGLYICQKLDIFAPKSLPPSRLLLLALSFCGFVVFTNLSLQNNTIGTYQLAKAMTTPVIIAIQTFCYQKTFSTRIQLTLIPITLGVILNSYYDVKFNFLGMVFAALGVLVTSLYQVWVGAKQHELQVNSMQLLYYQAPMSSAMLLVAVPFFEPVFGEGGIFGPWSVSALLMVLLSGVIAFMVNLSIYWIIGNTSPVTYNMFGHFKFCITLFGGYVLFKDPLSINQALGILCTLFGILAYTHFKLSEQEGSRSKLAQRP
Protein: 3-hydroxykynurenine transaminase (EC 2.6.1.63) (3-hydroxykynurenine transaminase and alanine--glyoxylate aminotransferase) (Ae-HKT/AGT) (Alanine--glyoxylate aminotransferase) (EC 2.6.1.44) (Q0IG34)
Organism: Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
Function: Catalyzes the pyridoxal 5'-phosphate-dependent transamination of both 3-hydroxykynurenine and L-kynurenine to xanthurenic acid and kynurenic acid, respectively, preferentially using the alpha-ketoacid pyruvate, glyoxylate or oxaloacetate as the amino group acceptor. The affinity and catalytic efficiency for 3-hydroxykynurenine is higher than for L-kynurenine. Involved in the detoxification of cytotoxic metabolite 3-hydroxykynurenine generated by the hydroxylation of L-kynurenine, an intermediate in the tryptophan catabolism pathway. Also catalyzes, although with a lesser efficiency, the transamination of alanine with glyoxylate as an amino group acceptor. May play a role in the detoxification of glyoxylate, a toxic plant metabolite from the diet (Probable).
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:P21549}.
Interaction partners:
- malate synthase
- Serine hydroxymethyltransferase
- AAEL005819-PA
- Phosphoserine phosphatase
- Glyoxylate reductase/hydroxypyruvate reductase
- Glyoxylate reductase/hydroxypyruvate reductase
- Glyoxylate reductase/hydroxypyruvate reductase
- Aminomethyltransferase
- (S)-2-hydroxy-acid oxidase
- (S)-2-hydroxy-acid oxidase
Sequence:
MKFTPPPSSLRGPLVIPDKIMMGPGPSNCSKRVLAALNNTCLSNFHDELFQVIDEVKDGLRYIFQTENRTTMCITGSAHTGMEALLCNLLEEGDIVLIANNGIWAERAINMATRYGADVRVLGGPADKPFSMTDFKKAIEQHRPKCLFVVHGDSSSGLLQPLEGLGKICHDYDCLLLVDAVASLCGVPFYMDKWEIDGVYTGSQKVLGAPPGITPISISPKALEVIRSRKTPSKVFYWDLLILGNYWGCYDEQKRYHHTVPSNLIFALREAIAQIAEEGLEPVIRRRQECAEQMYRGLQAMGLEIFVKDPEYRLPTVTCIMIPKGVNWWKVSEYAMNNFSLEIQGGFGPTMGIAWRAGIMGESSTLQRVNFYLYAFKESLKATHPDYVFEKKNGQTNGTK
Protein: Eukaryotic translation initiation factor 1 (eIF1) (Protein translation factor SUI1 homolog) (P48024)
Organism: Mus musculus (Mouse)
Function: Necessary for scanning and involved in initiation site selection. Promotes the assembly of 48S ribosomal complexes at the authentic initiation codon of a conventional capped mRNA (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P41567}.
Interaction partners:
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit G
- Ubiquitin-like protein FUBI
- Eukaryotic translation initiation factor 2 subunit 2
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 1A
- Eukaryotic translation initiation factor 3 subunit A
Sequence:
MSAIQNLHSFDPFADASKGDDLLPAGTEDYIHIRIQQRNGRKTLTTVQGIADDYDKKKLVKAFKKKFACNGTVIEHPEYGEVIQLQGDQRKNICQFLIEIGLAKDDQLKVHGF
Protein: Phosphotransferase (EC 2.7.1.-) (A0A5F9ZGW4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVA
Protein: Pachytene arrest protein SAE3 (Sporulation in the absence of SPO11 protein 3) (P89114)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in meiotic DNA-break repair. Required for the recruitment of DCM1 to meiosis recombination hot spots.
Subcellular location: Nucleus {ECO:0000269|PubMed:15579681, ECO:0000269|PubMed:15620352, ECO:0000269|PubMed:16341884}. Note=Localizes at chromosomal foci at leptotene and zigotene.
Interaction partners:
- Meiosis protein 5
- Meiotic recombination protein DMC1
- Meiotic nuclear division protein 1
- DNA repair protein RAD57
- Meiosis-specific protein SPO11
- DNA repair protein RAD55
- DNA repair and recombination protein RDH54
- DNA repair protein RAD51
- SRP-independent targeting protein 2
- Meiosis-specific protein HED1
Sequence:
MNYLETQLNKKQKQIQEYESMNGNLIKMFEQLSKEKKNDETPKKISSTYIKELKEYNELRDAGLRLAQIIADEKQCKIKDVFEEIGYSMKD
Protein: Protein SCAR4 (AtSCAR4) (Protein WAVE3) (Q5XPJ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex. Regulates trichome branch positioning and expansion.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Protein SCAR3
- Protein SCAR1
- Protein BRICK 1
- F-box/kelch-repeat protein At5g39560
- Protein SCAR2
- Protein NAP1
- Protein SPIRRIG
- Putative acyl-activating enzyme 19
- Protein ABIL1
Sequence:
MALTRYQIRNEYGLADKELYQSADKEDPEALLEAASMAGLVGVLRQLGDLSEFAAEVFHCLHEQLMTTAARGHGLAMRLQHLEADFPSVEIPILSQTDHSTFFYEPGLEWHSDLQTKEDLISPRNLPRCIMDSYEECHGPPQLFLLDKFDVAGSGSCLKRYSDPSLLKTHTTSAVVATSKLGKDKRLRQSKKKGSHTTIKETPEDSRTSHAKLHQLFFLEHVENGHRNPEFHVKLKRRQLNGPPINSSSGASYMEKFLKNSSPYCERVHGTMDQSSPAMETEVTVCSEQEDLPIPSLVYSNSGGTRKYNEMEIESIAGHEILEIPFVPHEITVNEKSPVVCLESSSSVNLCCKTNNDADSPASTESEVKEAGSDDKAGCDHGFPGFGQPQICTNAEVNQTEVLTQFSNVLRHSPEEGESSLLCTDIQRASPESKPHKAEEAAVDLDESFSQMTPDIDSAGMGTLEILQTPFSLSCYESPANLPEDSGSHLELQSNKANAEACEVFEVRRDPMLNISPETHLLKVTQVPQDAYEGGTNDVHSQHVFSVETASEISVSALVEDQFSSITNQEIEALESEDISSEAGHFIPDTKKSLNETSVALESDFLLPNHYISTFDNFEDLSLSADAQDYAAPKEDETNSQDGSSMNPAQSKHISTSEISSENGTLMSDTPRDLHTGYGSLSASSCLEDGLANPDLAEISSYSGQEDPQTMSIVSDDSSDPEVPIPDGTCFAGDVDHDNQTGLNNKAIETVPQKELETISDPQESLLGTEECLSSEYCLQIQNQRQESPSETGSANSRTSSDESPPTQNGSVGVQSSPLDVFPSSITEIEALHAPYQEIFTSLNDHISESVLSKGLTDEEDFLNVSPESILPLSTSLHETPQANPEITPPLPPLPPTQWWMGKLVESTEMPSLAGSGNNSFNIQRDENTQNGSVQANEAQYPSEVSVTDGENHNFHIYTEESKATEEQSPSGVNGTSDTYMESKHKCLNRTPEDSFSLAESAQGLEADWRTEAMALEWFSQNLREHNNPHPAKLEEEEPQVDHPLEKPGQTKFRQTLRDNNSYNQNQKAGKLKRDEDTLVIGIDRSMLRKVSEGNRTHVGARVDENDSLLEIIRSKSFNLRPADASGRPNFQVAVPKTNLKVAAILEKANTLRQAMAGSDDEHDSDSWSE
Protein: Paired box 6 (A0A1W2PPH0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MGADGMYDKLRMLNGQTGSWGTRPGWYPGTSVPGQPTQDGCQQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPVSSFTSGSMLGRTDTALTNTYSALPPMPSFTMANNLPMQPPVPSQTSSYSCMLPTSPSVNGRSYDTYTPPHMQTHMNSQPMGTSGTTSTGLISPGVSVPVQVPGSEPDMSQYWP
Protein: Ubiquitin-like domain-containing protein (Q5AZV1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Ulp1 protease family protein
- NEDD8-activating enzyme E1 catalytic subunit
- NEDD8-conjugating enzyme UBC12
- mRNA-nucleus export ATPase
- JmjC domain-containing histone demethylation protein 1
- NEDD8-activating enzyme E1 regulatory subunit
- COP9 signalosome complex subunit 5
- RING-box protein 1
- ZZ type zinc finger domain protein
- Elongation factor 3
Sequence:
MLIKVRTLTGKEIELDIEPDYKVSRIKERVEEKEGIPPVQQRLIFGGKQMADDKTAQDYNLEGGATLHLVLALRGGCAALQ
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12 (Q9UBI6)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-12
- B2 bradykinin receptor
- Muscarinic acetylcholine receptor M2
- 5-hydroxytryptamine receptor 7
- C-X-C chemokine receptor type 4
Sequence:
MSSKTASTNNIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLIGIPTSENPFKDKKTCIIL
Protein: Claudin-5 (Q2HJ22)
Organism: Bos taurus (Bovine)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space.
Subcellular location: Cell junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Occludin
- Cadherin-5
- Endothelial cell adhesion molecule
- Zona occludens protein 1
- SRY
- von Willebrand factor
- Junctional adhesion molecule A
- Claudin-12
- Claudin-3
- Claudin-16
Sequence:
MGSAALEILGLVLCLVGWVGLILACGLPMWQVTAFLDHNIVTAQTTWKGLWMSCVVQSTGHMQCKVYDSVLALSPEVQAARALTVGAVLLALVALFVTLAGAQCTTCVAPGPAKARVALTGGALYALCGLLALVPLCWFANIVVREFYDPTVPMSQKYELGAALYIGWAASALLMCGGGLVCCGAWVCTGRPDFSFPVKYSASRRPTATGDYDKKNYV
Protein: Toxin YoeB (EC 3.1.-.-) (Putative endoribonuclease YoeB) (Putative mRNA interferase Yoeb) (P69348)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type II toxin-antitoxin (TA) system. Its mode of function is controversial; it has been proposed to be an mRNA interferase but also an inhibitor of translation initiation. When overproduced in wild-type cells, inhibits bacterial growth and translation by cleavage of mRNA molecules while it has a weak effect on colony forming ability. Overproduction of Lon protease specifically activates YoeB-dependent mRNA cleavage, leading to lethality. YefM binds to the promoter region of the yefM-yeoB operon to repress transcription, YeoB acts as a corepressor.
Interaction partners:
- Antitoxin YefM
- mRNA interferase toxin RelE
- mRNA interferase toxin YafQ
- Antitoxin DinJ
- Ribonuclease toxin YhaV
- Endoribonuclease toxin ChpB
- Endoribonuclease toxin MazF
- mRNA interferase toxin MqsR
- Antitoxin RelB
- Antitoxin MazE
Sequence:
MKLIWSEESWDDYLYWQETDKRIVKKINELIKDTRRTPFEGKGKPEPLKHNLSGFWSRRITEEHRLVYAVTDDSLLIAACRYHY