wanglab/gogpt-training-data huggingface dataset:
Protein: 2-oxoglutarate dehydrogenase, mitochondrial (EC 1.2.4.2) (2-oxoglutarate dehydrogenase complex component E1) (OGDC-E1) (Alpha-ketoglutarate dehydrogenase) (O74378)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Probable isocitrate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase subunit 2, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Isocitrate dehydrogenase subunit 1, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Aconitate hydratase, mitochondrial
- Probable pyruvate dehydrogenase protein X component, mitochondrial
Sequence:
MLRFIPSSAKARALRRSAVTAYRLNRLTCLSSLQQNRTFATQPTDDFLTGGAADYVDEMYDAWKKDPNSVHASWQAYFKNVQERGVSPSKAFQAPPLLDYADSYTALDSSLINGNNYADIDVGIYMKVQLLVRAYQSRGHHLAKLDPLGINVNHNRPSELTLEHYGFTESDLNRTIHLGPGILPNFREAGRKTMTLREIVETCEKIYCGSFAVEFTHISSRKRSNWILSHLETPTPFRYSHDQKIMIFDRLSWADSFERFLFTKFPNDKRFGLEGCEAMVPGMKALIDRSVDEGISNIVIGMAHRGRLNLLHNIVRKPAQAIFSEFRGTQDPDDEGSGDVKYHLGMNYQRPTPSGKRVSLSLVANPSHLEAEDPVVLGKVRAIQHYTSDEASHEQSMGILIHGDAAFAAQGVVYETFGLHALPGYSTGGTVHIVINNQIGFTTDPRFARSTPYCTDIAKSMEAPIFHVNGDDVEAVTFICQLAADWRKAFKTDVVVDIVCYRRHGHNETDQPSFTQPRMYKAIAKHPPTFKIYTQQLLQEKTVSKAEVDAQEKRVWDILESSFESSKNYKSDHREWLSNPWVGFASPKDLMTKILPSYPTGVNIDTLKQIGKALYTLPEGFDAHRNLKRILNNRNKSISSGEGIDMPTAEALAFGTLLEEGHHVRVSGQDVERGTFSQRHAVLHDQSSENVYIPLNHLSPNQASFVIRNSSLSEYGVLGFEYGYSLSSPNALVVWEAQFGDFANNAQCIIDQFIAAGETKWLQRTGIVLSLPHGYDGQGPEHSSARMERYLQLCNEDPREFPSEEKLQRQHQDCNIQAIYVTKPSQYFHALRRNIHRQFRKPLVIFFSKSLLRHPAARSTIDEFDEKHGFKLILEEEEHGKSILPPEKIEKLIICSGQVWVALSKAREENKIDNIAITRVEQLHPFGWKQMAANISQYPNLKEIIWCQEEPLNAGAWTYMEPRIYTILKHLGRDLPVRYAGRPPSASVAAGNKQQHLAEQEQFLNDALL
Protein: Collagen alpha-1(IV) chain (P17139)
Organism: Caenorhabditis elegans
Function: Collagen type IV is specific for basement membranes (Probable). Required to restrict presynaptic growth at the neuromuscular junctions (NMJ) in late larval stage and in adult motor neurons. May play a role in axon regeneration in embryos following injury in D-type motor neurons.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane.
Interaction partners:
- Collagen alpha-2
- Integrin beta pat-3
- Basement membrane proteoglycan
- Papilin
- Integrin alpha pat-2
- SPARC
- Laminin-like protein epi-1
- Integrin alpha ina-1
- Fibulin-1
- Putative cuticle collagen 99
Sequence:
MSRLSLLGLTAAVVLLSSFCQDRIHVDAAAACKGCAPPCVCPGTKGERGNPGFGGEPGHPGAPGQDGPEGAPGAPGMFGAEGDFGDMGSKGARGDRGLPGSPGHPGLQGLDGLPGLKGEEGIPGCNGTDGFPGMPGLAGPPGQSGQNGNPGRPGLSGPPGEGGVNSQGRKGVKGESGRSGVPGLPGNSGYPGLKGAKGDPGPYGLPGFPGVSGLKGRMGVRTSGVKGEKGLPGPPGPPGQPGSYPWASKPIEMEVLQGPVGPAGVKGEKGRDGPVGPPGMLGLDGPPGYPGLKGQKGDLGDAGQRGKRGKDGVPGNYGEKGSQGEQGLGGTPGYPGTKGGAGEPGYPGRPGFEGDCGPEGPLGEGTGEAGPHGAQGFDGVQGGKGLPGHDGLPGPVGPRGPVGAPGAPGQPGIDGMPGYTEKGDRGEDGYPGFAGEPGLPGEPGDCGYPGEDGLPGYDIQGPPGLDGQSGRDGFPGIPGDIGDPGYSGEKGFPGTGVNKVGPPGMTGLPGEPGMPGRIGVDGYPGPPGNNGERGEDCGYCPDGVPGNAGDPGFPGMNGYPGPPGPNGDHGDCGMPGAPGKPGSAGSDGLSGSPGLPGIPGYPGMKGEAGEIVGPMENPAGIPGLKGDHGLPGLPGRPGSDGLPGYPGGPGQNGFPGLQGEPGLAGIDGKRGRQGSLGIPGLQGPPGDSFPGQPGTPGYKGERGADGLPGLPGAQGPRGIPAPLRIVNQVAGQPGVDGMPGLPGDRGADGLPGLPGPVGPDGYPGTPGERGMDGLPGFPGLHGEPGMRGQQGEVGFNGIDGDCGEPGLDGYPGAPGAPGAPGETGFGFPGQVGYPGPNGDAGAAGLPGPDGYPGRDGLPGTPGYPGEAGMNGQDGAPGQPGSRGESGLVGIDGKKGRDGTPGTRGQDGGPGYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGEDGLVGFPGLRGEHGDNGLPGLEGECGEEGSRGLDGVPGYPGEHGTDGLPGLPGADGQPGFVGEAGEPGTPGYRGQPGEPGNLAYPGQPGDVGYPGPDGPPGLPGQDGLPGLNGERGDNGDSYPGNPGLSGQPGDAGYDGLDGVPGPPGYPGITGMPGLKGESGLPGLPGRQGNDGIPGQPGLEGECGEDGFPGSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYPGAPGENGDNGNQGRDGQPGLRGESGQPGQPGLPGRDGQPGPVGPPGDDGYPGAPGQDIYGPPGQAGQDGYPGLDGLPGAPGLNGEPGSPGQYGMPGLPGGPGESGLPGYPGERGLPGLDGKRGHDGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQPGIKGPRGDDGFPGRDGLDGLPGRPGREGLPGPMAMAVRNPPGQPGENGYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGTDGYPGPPGLSGMPGHGGDQGFQGAAGRTGNPGLPGTPGYPGSPGGWAPSRGFTFAKHSQTTAVPQCPPGASQLWEGYSLLYVQGNGRASGQDLGQPGSCLSKFNTMPFMFCNMNSVCHVSSRNDYSFWLSTDEPMTPMMNPVTGTAIRPYISRCAVCEVPTQIIAVHSQDTSVPQCPQGWSGMWTGYSFVMHTAAGAEGTGQSLQSPGSCLEEFRAVPFIECHGRGTCNYYATNHGFWLSIVDQDKQFRKPMSQTLKAGGLKDRVSRCQVCLKNR
Protein: D(2) dopamine receptor (Dopamine D2 receptor) (F1N4I3)
Organism: Bos taurus (Bovine)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDPLNLSWYDDDPESRNWSRPFNGSEGKADRPPYNYYAMLLTLLIFVIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMIAIVWVLSFTISCPMLFGLNNTDQNECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRRRRKRVNTKRSSRAFRANLKAPLKGNCTHPEDMKLCTVIMKSNGSFPVNRRRVEAARRAQELEMEMLSSTSPPERTRYSPMPPSHHQLTLPDPSHHGLHSTPDSPAKPEKNGHAKDHPKIAKIFEIQSMPNGKTRTSLKTMSRRKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNIHCDCNIPPVLYSAFTWLGYVNSAVNPIIYTTFNIEFRKAFLKILHC
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (A0A2R8YGG3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XPDHLQMAVQGKRPMPGMQQQMPTLPPPSVSATGPGPGPGPGPGPGPGPAPPNYSRPHGMGGPNMPPPGPSGVPPGMPGQPPGGPPKPWPEGPMANAAAPTSTPQKLIPPQPTGRPSPAPPAVPPAASPVMPPQTQSPGQPAQPAPMVPLHQKQSRITPIQKPRGLDPVEILQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDESRHCSTGSGSASFAHTAPPPAGVNPDLEEPPLKEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKTLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED
Protein: DNA-binding protein RFX6 (Regulatory factor X 6) (Regulatory factor X domain-containing protein 1) (Q8HWS3)
Organism: Homo sapiens (Human)
Function: Transcription factor required to direct islet cell differentiation during endocrine pancreas development. Specifically required for the differentiation of 4 of the 5 islet cell types and for the production of insulin. Not required for pancreatic PP (polypeptide-producing) cells differentiation. Acts downstream of NEUROG3 and regulates the transcription factors involved in beta-cell maturation and function, thereby restricting the expression of the beta-cell differentiation and specification genes, and thus the beta-cell fate choice. Activates transcription by forming a heterodimer with RFX3 and binding to the X-box in the promoter of target genes. Involved in glucose-stimulated insulin secretion by promoting insulin and L-type calcium channel gene transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:25497100}.
Interaction partners:
- Neurogenin-3
- Probable E3 ubiquitin-protein ligase DTX2
- Insulin
- Calcium-responsive transactivator
- Cyclin-K
- Homeobox protein Nkx-6.1
- Neurogenic differentiation factor 1
- Homeobox protein Nkx-6.2
- Motor neuron and pancreas homeobox protein 1
- Hexokinase-4
Sequence:
MAKVPELEDTFLQAQPAPQLSPGIQEDCCVQLLGKGLLVYPEETVYLAAEGQPGGEQGGGEKGEDPELPGAVKSEMHLNNGNFSSEEEDADNHDSKTKAADQYLSQKKTITQIVKDKKKQTQLTLQWLEENYIVCEGVCLPRCILYAHYLDFCRKEKLEPACAATFGKTIRQKFPLLTTRRLGTRGHSKYHYYGIGIKESSAYYHSVYSGKGLTRFSGSKLKNEGGFTRKYSLSSKTGTLLPEFPSAQHLVYQGCISKDKVDTLIMMYKTHCQCILDNAINGNFEEIQHFLLHFWQGMPDHLLPLLENPVIIDIFCVCDSILYKVLTDVLIPATMQEMPESLLADIRNFAKNWEQWVVSSLENLPEALTDKKIPIVRRFVSSLKRQTSFLHLAQIARPALFDQHVVNSMVSDIERVDLNSIGSQALLTISGSTDTESGIYTEHDSITVFQELKDLLKKNATVEAFIEWLDTVVEQRVIKTSKQNGRSLKKRAQDFLLKWSFFGARVMHNLTLNNASSFGSFHLIRMLLDEYILLAMETQFNNDKEQELQNLLDKYMKNSDASKAAFTASPSSCFLANRNKGSMVSSDAVKNESHVETTYLPLPSSQPGGLGPALHQFPAGNTDNMPLTGQMELSQIAGHLMTPPISPAMASRGSVINQGPMAGRPPSVGPVLSAPSHCSTYPEPIYPTLPQANHDFYSTSSNYQTVFRAQPHSTSGLYPHHTEHGRCMAWTEQQLSRDFFSGSCAGSPYNSRPPSSYGPSLQAQDSHNMQFLNTGSFNFLSNTGAASCQGATLPPNSPNGYYGSNINYPESHRLGSMVNQHVSVISSIRSLPPYSDIHDPLNILDDSGRKQTSSFYTDTSSPVACRTPVLASSLQTPIPSSSSQCMYGTSNQYPAQETLDSHGTSSREMVSSLPPINTVFMGTAAGGT
Protein: Lysosomal thioesterase PPT2 homolog (PPT-2) (EC 3.1.2.-) (Q9VKH6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable thioesterase removing fatty acyl groups from various substrates such as S-palmitoyl-CoA. Because of structural constraints, may be unable to remove palmitate from peptides or proteins (By similarity).
Subcellular location: Lysosome {ECO:0000269|PubMed:18719403}.
Interaction partners:
- Long-chain-fatty-acid--CoA ligase
- long-chain-fatty-acid--CoA ligase
- Palmitoyl-protein thioesterase 1
- Very long-chain-fatty-acid--CoA ligase bubblegum
- Long-chain-fatty-acid--CoA ligase heimdall
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
Sequence:
MRLRLQVLVALLTCSSISVSLAYKPVVILHGILSGAESMASLVREIEEFHPGTIVYNCDKFNGWYSLENAWRQVDQVRDYLNEVGKLHPEGIIVLGYSQGGLLARAAIQSLPEHNVKTFISLSSPQAGQYGTSFLHLIFPDLAAKTAFELFYSRVGQHTSVGGYWNDPQRQDLYLKYSEFLPLINNEKKTSNSTSFKMGMVRLNKLVMIGGPNDDVITPWQSSHFGYFDENMDVIPFIRRPIFTSDSIGIRTLQEAGKLIIVVKPHVHHLAWHTRRDVIHEVIFPYLD
Protein: [Pyruvate dehydrogenase (acetyl-transferring)] kinase, mitochondrial (AtPDHK) (Pyruvate dehydrogenase kinase) (EC 2.7.11.2) (Q9SBJ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine protein kinase that inhibits the mitochondrial pyruvate dehydrogenase (PDH) complex (mtPDC) by phosphorylation of the E1 alpha subunit on Ser residues, thus contributing to the regulation of glucose metabolism.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 5 of pyruvate dehydrogenase complex, chloroplastic
- Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 4 of pyruvate dehydrogenase complex, chloroplastic
- Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Dihydrolipoyl dehydrogenase 2, chloroplastic
Sequence:
MAVKKACEMFPKSLIEDVHKWGCMKQTGVSLRYMMEFGSKPTERNLLISAQFLHKELPIRVARRAIELQTLPYGLSDKPAVLKVRDWYLESFRDMRAFPEIKDSGDEKDFTQMIKAVKVRHNNVVPMMALGVNQLKKGMNSGNLDEIHQFLDRFYLSRIGIRMLIGQHVELHNPNPPLHTVGYIHTKMSPMEVARNASEDARSICFREYGSAPEINIYGDPSFTFPYVPTHLHLMMYELVKNSLRAVQERFVDSDRVAPPIRIIVADGIEDVTIKVSDEGGGIARSGLPRIFTYLYSTARNPLEEDVDLGIADVPVTMAGYGYGLPISRLYARYFGGDLQIISMEGYGTDAYLHLSRLGDSQEPLP
Protein: Max dimerization protein 4 (Max dimerizer 4) (Class C basic helix-loop-helix protein 12) (bHLHc12) (Max-associated protein 4) (Max-interacting transcriptional repressor MAD4) (Q14582)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor. Binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing for MAX and suppresses MYC dependent cell transformation (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Max-like protein X
- Carbohydrate-responsive element-binding protein
- Max-binding protein MNT
- Protein max
- MLX-interacting protein
- Paired amphipathic helix protein Sin3a
- Receptor tyrosine-protein kinase erbB-4
- NIF3-like protein 1
Sequence:
MELNSLLILLEAAEYLERRDREAEHGYASVLPFDGDFAREKTKAAGLVRKAPNNRSSHNELEKHRRAKLRLYLEQLKQLVPLGPDSTRHTTLSLLKRAKVHIKKLEEQDRRALSIKEQLQQEHRFLKRRLEQLSVQSVERVRTDSTGSAVSTDDSEQEVDIEGMEFGPGELDSVGSSSDADDHYSLQSGTGGDSGFGPHCRRLGRPALS
Protein: Large ribosomal subunit protein bL19m (54S ribosomal protein subunit img1, mitochondrial) (Q9UT87)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL28m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL32m
- Small ribosomal subunit protein uS9m
Sequence:
MFNAKHFFNLGLGFQWLQKRGIGSLKRPYNFPKPVPGPKHKDVLSLFEKKCRSVLDEQSERFKMFHRSQPNRVRPGAVLLVESYSKYPSKDSVNRFAGYLLRIRHRGPKSSILLRNVVMGVGVEYLLPIYSPQIKRIVVLKENGLSKRPRRAYLSYLRQPRFRLPPVESLVRKYIEQNQHKP
Protein: Solute carrier family 35 member G5 (Acyl-malonyl-condensing enzyme 1-like protein 2) (Q96KT7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAGSHPYFNLPDSTHPSPPSAPPSLRWHQRCQPSGATNGLLVALLGGGLPAGFVGPLSRMAYQGSNLPSLELLICRCLFHLPIALLLKLRGDPLLGPPDIRGWACFCALLNVLSIGCAYSAVQVVPAGNAATVRKGSSTVCSAVLTLCLESQGLGGYEWCGLLGSILGLIIILGPGLWTLQEGTTGVYTTLGYVQAFLGGLALSLGLLVYRSLHFPSCLPTVAFLSGLVGLLGCVPGLFVLQTPVLPSDLLSWSCVGAEGILALVSFTCVGYAVTKAHPALVCAVLHSEVVVALILQYYMLHETVALSDIMGAGVVLGSIAIITARNLSCERTGKVEE
Protein: Meiotic recombination protein REC114 (Q7Z4M0)
Organism: Homo sapiens (Human)
Function: Required for DNA double-strand breaks (DSBs) formation in unsynapsed regions during meiotic recombination. Probably acts by forming a complex with IHO1 and MEI4, which activates DSBs formation in unsynapsed regions, an essential step to ensure completion of synapsis.
Subcellular location: Chromosome {ECO:0000250|UniProtKB:Q9CWH4}. Note=Located in discrete foci on the axes of meiotic chromosomes. The number of foci is highest at leptonema and decreases at zygonema. {ECO:0000250|UniProtKB:Q9CWH4}.
Interaction partners:
- Meiosis-specific protein MEI4
- Ankyrin repeat domain-containing protein 31
- CD151 antigen
- Interactor of HORMAD1 protein 1
- Transcription termination factor 2
- Meiosis inhibitor protein 1
- Meiotic recombination protein SPO11
- Type 2 DNA topoisomerase 6 subunit B-like
- L-fucose kinase
- HORMA domain-containing protein 1
Sequence:
MAEAGKVPLSLGLTGGEAAEWPLQRYARCIPSNTRDPPGPCLEAGTAPCPTWKVFDSNEESGYLVLTIVISGHFFIFQGQTLLEGFSLIGSKDWLKIVRRVDCLLFGTTIKDKSRLFRVQFSGESKEQALEHCCSCVQKLAQYITVQVPDGNIQELQLIPGPPRATESQGKDSAKSVPRQPGSHQHSEQQQVCVTAGTGAPDGRTSLTQLAQTLLASEELPHVYEQSAWGAEELGPFLRLCLMDQNFPAFVEEVEKELKKLAGLRN
Protein: Seed maturation protein PM28 (Q9XES8)
Organism: Glycine max (Soybean) (Glycine hispida)
Interaction partners:
- 51 kDa seed maturation protein
- Protein SLE3
- Seed maturation protein PM30
- Seed maturation protein PM31
- Protein SLE2
- 18 kDa seed maturation protein
- 18 kDa seed maturation protein
- Uncharacterized protein
- Glycinin G2
- Race-specific resistance protein RpsUN1
Sequence:
MAKSKEDITYATSQARLSEDEAVRVAYEHGSPLEGGKIADSQPVDLFSSAHNMPKSGQTTMDSNTSDQSQMQRDTQEGGSKEFTTGAPG
Protein: Vacuolar serine-type carboxypeptidase ATG42 (EC 3.4.16.5) (Carboxypeptidase C) (CPC) (P38109)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Vacuolar serine-type carboxypeptidase involved in vacuolar zymogen activation, breakdown of the autophagic body, and autophagosome-dependent protein synthesis. Plays a key role in phytochelatin (PC) synthesis from glutathione (GSH) by cleaving the Gly from GSH and form the PC-peptides of the structure (gamma-Glu-Cys)2-Gly. Also involved in resistance to xenobiotics via the degradation of glutathione-S-conjugates.
Subcellular location: Vacuole lumen {ECO:0000269|PubMed:29514932}. Note=The vacuolar sorting receptor VPS10 is required for the delivery of ATG42 to the vacuole lumen. {ECO:0000269|PubMed:29514932}.
Interaction partners:
- SCF-associated factor 1
Sequence:
MKYLNLVFVLQLLISIKYASFGRAFSLFEDDTTFANLDKQLKLPQNTQQTLKLDRLNHDDPLFTTFISSVDTDYSLRLRTVDPSKLGIDTVKQWSGYMDYKDSKHFFYWFFESRNDPANDPIILWLNGGPGCSSFTGLLFELGPSSIGADMKPIHNPYSWNNNASMIFLEQPLGVGFSYGDEKVSSTKLAGKDAYIFLELFFEAFPHLRSNDFHIAGESYAGHYIPQIAHEIVVKNPERTFNLTSVMIGNGITDPLIQADYYEPMACGKGGYHPVLSSEECEKMSKAAGRCRRLNKLCYASKSSLPCIVATAYCDSALLEPYINTGLNVYDIRGPCEDNSTDGMCYTGLRYVDQYMNFPEVQETLGSDVHNYSGCDNDVFTGFLFTGDGSKPFQQYIAELLNHNIPVLIYAGDKDYICNWLGNHAWSNELEWINKRRYQRRMLRPWVSKETGEELGQVKNYGPFTFLRIYDAGHMVPYDQPEASLEMVNSWISGNRAFSDLSTLENAS
Protein: RELA proto-oncogene, NF-kB subunit (E9PI38)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLC
Protein: D(1B) dopamine receptor (D(5) dopamine receptor) (D1beta dopamine receptor) (Dopamine D5 receptor) (P21918)
Organism: Homo sapiens (Human)
Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Thyrotropin subunit beta
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
- Pituitary adenylate cyclase-activating polypeptide
- VIP peptides
- Pro-glucagon
- Follitropin subunit beta
- Natriuretic peptides A
Sequence:
MLPPGSNGTAYPGQFALYQQLAQGNAVGGSAGAPPLGPSQVVTACLLTLLIIWTLLGNVLVCAAIVRSRHLRANMTNVFIVSLAVSDLFVALLVMPWKAVAEVAGYWPFGAFCDVWVAFDIMCSTASILNLCVISVDRYWAISRPFRYKRKMTQRMALVMVGLAWTLSILISFIPVQLNWHRDQAASWGGLDLPNNLANWTPWEEDFWEPDVNAENCDSSLNRTYAISSSLISFYIPVAIMIVTYTRIYRIAQVQIRRISSLERAAEHAQSCRSSAACAPDTSLRASIKKETKVLKTLSVIMGVFVCCWLPFFILNCMVPFCSGHPEGPPAGFPCVSETTFDVFVWFGWANSSLNPVIYAFNADFQKVFAQLLGCSHFCSRTPVETVNISNELISYNQDIVFHKEIAAAYIHMMPNAVTPGNREVDNDEEEGPFDRMFQIYQTSPDGDPVAESVWELDCEGEISLDKITPFTPNGFH
Protein: Prion-like-(Q/N-rich) domain-bearing protein 8 (Glutamine/asparagine-rich protein pqn-8) (P34291)
Organism: Caenorhabditis elegans
Interaction partners:
- EB domain-containing protein
- Flo11 domain-containing protein
- ShKT domain-containing protein
- ShKT domain-containing protein
- ShKT domain-containing protein
Sequence:
MPPILLTFLLFSNVYANFMNMLMGSSSAPLQQYRAYAGCSSSGCVPATIVPKSSGFWPNADMIAGLQTEQRSQNQNQNSNNPQQDDPRTSQSTGQINGNVPGSSSSNQQPVIYIARAGSDKYKNSEVTTSTPTPNGFNFGNGFQGGQNQNTGFSSGFFNNQNQNSNQNLNQNNFQQNQNLGASSGFFNNQNQQNSQQNQVNGPTSGFSNQQTSNQNSGFFNNQNQQNGQNFGNSGNQNGVNPYSGAFSNGQNQNQQGFFGNNQNNQQNSNGQVQGSQNNQIWNQNQNPNILPFGPNLVNSNTQFGPQPFQPIQVGSIRQPFSNKDWNFQPGGQAVQFVGGGGSGGAPGSQSVPMTDEAQQIAVQIQAIRDNLSITRNESNYLINQLKLSLPQELQNQLEMV
Protein: Serine/threonine-protein kinase haspin (EC 2.7.11.1) (Germ cell-specific gene 2 protein) (H-haspin) (Haploid germ cell-specific nuclear protein kinase) (Q8TF76)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase that phosphorylates histone H3 at 'Thr-3' (H3T3ph) during mitosis. May act through H3T3ph to both position and modulate activation of AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion, metaphase alignment and normal progression through the cell cycle.
Subcellular location: Nucleus {ECO:0000269|PubMed:15681610}. Chromosome {ECO:0000269|PubMed:15681610}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15681610}. Note=Nuclear during interphase and associates with the chromosomes and spindle apparatus during mitosis.
Interaction partners:
- Aurora kinase B
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Sister chromatid cohesion protein PDS5 homolog A
- Kinesin-like protein KIF2C
- Shugoshin 1
- Serine/threonine-protein kinase PLK1
- Histone H3.1t
- Histone H3.1
- Histone H3.2
- Histone H3.3C
Sequence:
MAASLPGPGSRLFRTYGAADGRRQRRPGREAAQWFPPQDRRRFFNSSGSSDASIGDPSQSDDPDDPDDPDFPGSPVRRRRRRPGGRVPKDRPSLTVTPKRWKLRARPSLTVTPRRLGLRARPPQKCSTPCGPLRLPPFPSRDSGRLSPDLSVCGQPRDGDELGISASLFSSLASPCPGSPTPRDSVISIGTSACLVAASAVPSGLHLPEVSLDRASLPCSQEEATGGAKDTRMVHQTRASLRSVLFGLMNSGTPEDSEFRADGKNMRESCCKRKLVVGNGPEGPGLSSTGKRRATGQDSCQERGLQEAVRREHQEASVPKGRIVPRGIDRLERTRSSRKSKHQEATETSLLHSHRFKKGQKLGKDSFPTQDLTPLQNVCFWTKTRASFSFHKKKIVTDVSEVCSIYTTATSLSGSLLSECSNRPVMNRTSGAPSSWHSSSMYLLSPLNTLSISNKKASDAEKVYGECSQKGPVPFSHCLPTEKLQRCEKIGEGVFGEVFQTIADHTPVAIKIIAIEGPDLVNGSHQKTFEEILPEIIISKELSLLSGEVCNRTEGFIGLNSVHCVQGSYPPLLLKAWDHYNSTKGSANDRPDFFKDDQLFIVLEFEFGGIDLEQMRTKLSSLATAKSILHQLTASLAVAEASLRFEHRDLHWGNVLLKKTSLKKLHYTLNGKSSTIPSCGLQVSIIDYTLSRLERDGIVVFCDVSMDEDLFTGDGDYQFDIYRLMKKENNNRWGEYHPYSNVLWLHYLTDKMLKQMTFKTKCNTPAMKQIKRKIQEFHRTMLNFSSATDLLCQHSLFK
Protein: cDNA FLJ50504, highly similar to Mus musculus zinc finger, MYND domain containing 11 (Zmynd11), mRNA (B7Z2J6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MARLTKRRQADTKAIQHLWAAIEIIRNQKQIANIDRITKYMSRVHGMHPKETTRQLSLAVKDGLIVETLTVGCKGSKAGIEQEGYWLPGDEISIKKKNTNKQEMGTYLRFIVSRMKERAIDLNKKGKDNKHPMYRRLVHSAVDVPTIQEKVNEGKYRSYEEFKADAQLLLHNTVIFYGDSEQADIARMLYKDTCHELDELQLCKNCFYLSNARPDNWFCYPCIPNHELVWAKMKGFGFWPAKVMQKEDNQVDVRFFGHHHQRAWIPSENIQDITVNIHRLHVKRSMGWKKACDELELHQRFLREGRFWKSKNEDRGEEEAESSISSTSNEQLKVTQEPRAKKGRRNQSVEPKKEEPEPETEAVSSSQEIPTMPQPIEKVSVSTQTKKLSASSPRMLHRSTQTTNDGVCQSMCHDKYTKIFNDFKDRMKSDHKRETERVVREALEKLRSEMEEEKRQAVNKAVANMQGEMDRKCKQVKEKCKEEFVEEIKKLATQHKQLISQTKKKQWCYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR
Protein: MPT51/MPB51 antigen (P9WQN7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May have a role in host tissue attachment, whereby ligands may include the serum protein fibronectin and small sugars.
Subcellular location: Secreted.
Interaction partners:
- Carboxylesterase/lipase Culp6
- Alpha-crystallin
Sequence:
MKGRSALLRALWIAALSFGLGGVAVAAEPTAKAAPYENLMVPSPSMGRDIPVAFLAGGPHAVYLLDAFNAGPDVSNWVTAGNAMNTLAGKGISVVAPAGGAYSMYTNWEQDGSKQWDTFLSAELPDWLAANRGLAPGGHAAVGAAQGGYGAMALAAFHPDRFGFAGSMSGFLYPSNTTTNGAIAAGMQQFGGVDTNGMWGAPQLGRWKWHDPWVHASLLAQNNTRVWVWSPTNPGASDPAAMIGQAAEAMGNSRMFYNQYRSVGGHNGHFDFPASGDNGWGSWAPQLGAMSGDIVGAIR