wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein 105 (O88412)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTTELKETMGRASWDPEKVKMEEDDESVISQASSQQVYYENDKDCAPGEGPYGSISVSEDEEKGQEMFREMAVVLKATQEAAAASPFGSYSLAGTLAESQILELHGNPTPTGAKSKNLELLIPKKEISDDSEKPPMILGRIQKGDLQGPELGESCEKGNVLKGLRIKEEKGDLGEATVKDCPLSESFRDEEESKKSRGKYSLRSTPGKNQKIQPGQKPFTCSECGKGFSQSANLVVHQRIHTGEKPFECHECGKAFIQSANLVVHQRIHTGQKPYVCGKCGKAFTQSSNLTVHQKIHSLEKTFKCSECEKAFSYSSQLARHQKVHITEKCYECNECGKTFTRSSNLIVHQRIHTGEKPFACSDCGKAFTQSANLIVHQRSHTGEKPYKCKDCEKAFSCFSHLIVHQRIHTAEKPYDCSECGKAFSQLSCLIVHQRIHSGDLPYVCNECGKAFTCSSYLLIHQRIHNGEKPYSCNECGKAFRQKSSLTVHQRTHTGEKPYECAKCGAAFISNSHLMRHHRTHLVE
Protein: Zinc finger protein 395 (E5RG59)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASVLSRRLGKRSLLGARVLGPSASEGPSAAPPSEPLLEGAAPQPFTTSDDTPCQEQPKEVLKAPSTSGLQQVAFQPGQKVYVWYGGQECTGLVEQHSWMEGQVTVWLLEQKLQVCCRVEEVWL
Protein: Enolase 1 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 1) (2-phosphoglycerate dehydratase 1) (Q6FTW6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phosphoglycerate mutase
- Fructose-bisphosphate aldolase
- Glucose-6-phosphate isomerase
- Pyruvate kinase 2
- Pyruvate kinase 1
- Phosphoglycerate kinase
- Phosphoglycerate mutase
- Triosephosphate isomerase
- Transketolase
- Phosphoenolpyruvate carboxykinase
Sequence:
MSVTKVHARTVYDSRGNPTVEVEVYTKDGMFRAIVPSGASTGSHEALELRDGDKSKWEGKGVTKAVSNVNDIIGPKLIESKLDVKDQKAIDEFMIKLDGTKNKSKLGANAILGVSLAVARAGAAAKGVPLYQHIAELADMKKEPYVIPCPFFNVLNGGVHAGGNLALQEFLIAPVGAESFHEALRLGSEVYHKLKALAKKRIGSSAGNVGDEGGIAPSLSTPFEALDLIYDAIKEAGHEGKVKIAMDPASSEFFQGDKYDLDFKNPHPDAKNKLSGAQLGDYYKTILEKYPIVSLEDPFAEDDWEAWTNFFPKAGVQIIADDLTVTNPERIQTAIDKKTADCLLLKVNQIGSLTESINSAKLAYGAGWGVQVSHRSGETEDTFIADLVVGLRTGQIKSGSLARSERLAKWNQILRIEEELGASNTIFAGAKFHKGQLL
Protein: CRISPR-associated protein, Cse2 family (Q47PJ2)
Organism: Thermobifida fusca (strain YX)
Interaction partners:
- CRISPR-associated protein, Cse4 family
- CRISPR-associated protein, Cas5e family
- CRISPR-associated protein, Cse3 family
- CRISPR-associated protein, Cse1 family
- CRISPR-associated helicase, Cas3 family
- CRISPR-associated protein, Cse2 family
- CRISPR-associated endonuclease Cas1
Sequence:
MNSDYILQHADALVKRVSKLIVNEPAARAALRRGVGLAPEDPRMLAAHRVVAPYVPVPTDYDVDRRRAASLWDVHAVERAFYAVAAIMAAQPRSARDQEAEATEEQTGEPQDSEALTEPTPAEESSATKDGKPDRRPNLGVSLAQAVFDKGLNADSTEQRLHLIARQNLDGVHRHLPRLVLYLRSDQVHIDWGILIRDLARWGHTPRHVAREWVQDYHRTLETLTRQAEQKNKNNTTDEEAEAA
Protein: Mutagen-sensitive 101 (Q9VY97)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cell cycle checkpoint control protein Rad9
- CDC45L
- PAX-interacting protein 1
- Serine/threonine-protein kinase ATR
- Checkpoint protein Hus1-like
- DNA replication licensing factor Mcm5
- DNA replication licensing factor Mcm3
- Claspin
- DNA polymerase epsilon catalytic subunit 1
- Rad17
Sequence:
MSISMSMDETICAYFVNNLKPGDGGVQEADTLQQFEAARELLGQQLAETQIRQIKPSEGYPLIAAGNLTKKDVFVLTQFEGEFFEQLQQTRALILGPPCLITCLRRNEPIPEGSSAIYSTAMRDLQVSATGITPQKKEELSRLINWMGGIYFQSFGHRTTHLISNTIKSSKYEQATLNGVPVMHVDWVQYVWDQSRRSQREGIMATDPDFDKYRLPIFFGANITCSGLDVARKDQVMRLVNDNGGIYHRAFRSQVVDIVITEQTKTDTEKYKAAIRYKKDVLLPEWIFDSCNRGYALPTKDYEVRPGKTSSTPTKTTRPGAAPGADQTHLSDLSRISFVSGSRRMCSDLSTVNESVSSVGSSSPAKQLLKQATSSGRNYQQVLAEIEPRQAKKAGAFLDGCCVYLSGFRSEEREKLNRVLNTGGATRYDEANEGISHIIVGQLDDAEYRQWQRDGLMGSVHVVRLDWLLESIRAGRVVSELVHRVSMPQNREPDVASPASKRTLRSMNHSFKQPTLPIKKKLFDQEPDPVQEQEHEEPDHTLLDQYSQDQGAVAQLPPADVSLLQPAASSTQMDIRQRVSVANPKPPAEGLQLPDLSASTLSIDFDKLDYFAGVSVYVHRECFNEEFFNQMLTECEAAQGLLVPSSFSDEVDFAIVSFEVAFDVKQLPVKARHVVTELFLESCMKKNQLLPIEYYHKHVPATALRQPLKGMTIVVSIYAGLERDFINATAELLGASVNKTFIKKEKPLLVCPSAEGSKYEGAIKWNYPVVTSDWLVQCARTGQKLPFVGYLVGKSPEDFPISPRLRDSNSRTARRPNESTLVAQPDVTMEEAENQPAGSVTPVTAGSPGAPELTPLRNKRVSELAGIPGGSALHRGSNSTSSPDSPCTPLSQVGAQQYNLDFLEQFVQRLDTEEGKDCVREIIREMRENQTPELERIRRQACTPVSRKHQRPAPGIPDFCLTPEFQQRMADDFERRWRLPTMKIKPDTPLAVIRQRVMRITCETLGIEYEESNAKTPTLSESPSTVKKKPPTRTTQATKLNFDRSPKTPKLSLGKKTPLRVSMGSPRSGTQSPFVPNTQSPIEAAPPRRSDGPTLSEEGQSTINFDKISFEESAVPVLAPDVPTVAPDVKQITDYLKNCESRRNSLKRSHDNDMDCGESEVQYVQPFESEGFALGTEDMVDWRDPAEFNAAKRRSSGGSPKMQYAGIPCFSISCGDDDEKRAELIARITQLGGKVCENLVNYDDSCTHLLCERPNRGEKMLACIAAGKWILNIQYIEQSHARGDFLDETLYEWGNPKAINLPTLAPEEEPIAAAVHRWRTELSACGGGAFSDHRVILSMNERSGAPIRNVLRAGGACILEPTTPFSKDPVAKSASHCFVDVKKAPLSTQDMEYLHKCGVQVLSQIAINAYLMNGRDADLGKYQLL
Protein: Ephrin type-B receptor 1 (EC 2.7.10.1) (ELK) (EPH tyrosine kinase 2) (EPH-like kinase 6) (EK6) (hEK6) (Neuronally-expressed EPH-related tyrosine kinase) (NET) (Tyrosine-protein kinase receptor EPH-2) (P54762)
Organism: Homo sapiens (Human)
Function: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. In addition to its role in axon guidance also plays an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively. Involved in the maintenance of the pool of satellite cells (muscle stem cells) by promoting their self-renewal and reducing their activation and differentiation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:18034775}; Single-pass type I membrane protein {ECO:0000269|PubMed:18034775}. Early endosome membrane {ECO:0000269|PubMed:18034775}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8CBF3}.
Interaction partners:
- Ephrin-B2
- Ephrin-B1
- Ephrin-B3
- Ephrin-A4
- Ephrin-A5
- Tyrosine-protein kinase ABL1
- Ephexin-1
- Ephrin-A1
- Ras GTPase-activating protein 1
- Ephrin-A2
Sequence:
MALDYLLLLLLASAVAAMEETLMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWSEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYGACMSLLSVRVFFKKCPSIVQNFAVFPETMTGAESTSLVIARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGRCTCKPGYEPENSVACKACPAGTFKASQEAEGCSHCPSNSRSPAEASPICTCRTGYYRADFDPPEVACTSVPSGPRNVISIVNETSIILEWHPPRETGGRDDVTYNIICKKCRADRRSCSRCDDNVEFVPRQLGLTECRVSISSLWAHTPYTFDIQAINGVSSKSPFPPQHVSVNITTNQAAPSTVPIMHQVSATMRSITLSWPQPEQPNGIILDYEIRYYEKEHNEFNSSMARSQTNTARIDGLRPGMVYVVQVRARTVAGYGKFSGKMCFQTLTDDDYKSELREQLPLIAGSAAAGVVFVVSLVAISIVCSRKRAYSKEAVYSDKLQHYSTGRGSPGMKIYIDPFTYEDPNEAVREFAKEIDVSFVKIEEVIGAGEFGEVYKGRLKLPGKREIYVAIKTLKAGYSEKQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLAEMNYVHRDLAARNILVNSNLVCKVSDFGLSRYLQDDTSDPTYTSSLGGKIPVRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPMDCPAALHQLMLDCWQKDRNSRPRFAEIVNTLDKMIRNPASLKTVATITAVPSQPLLDRSIPDFTAFTTVDDWLSAIKMVQYRDSFLTAGFTSLQLVTQMTSEDLLRIGITLAGHQKKILNSIHSMRVQISQSPTAMA
Protein: Ras oncogene (Q5CCJ5)
Organism: Bombyx mori (Silk moth)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046278}; Lipid-anchor {ECO:0000256|ARBA:ARBA00046278}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00046278}.
Interaction partners:
Sequence:
MSRAGDRPNQAQTYKLVVVGGGGVGKSAITIQFIQSYFVTDYDPTIEDSYTKQCVIDDIPAKLDILDTAGQEEFSAMREQYMRSGEGFLLVFSVADHASFDELYKFHKQILRVKDREEFPMLIVGNKADLETQRVVSLEEAQALSRQLKVPYIECSAKARMNVDQAFHELVRLVRRFQEAERMNTKNYYESGKKKKCTIL
Protein: Cryptic protein (P97766)
Organism: Mus musculus (Mouse)
Function: Nodal coreceptor involved in the correct establishment of the left-right axis. May play a role in mesoderm and/or neural patterning during gastrulation.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Secreted {ECO:0000250}.
Interaction partners:
- Activin receptor type-2B
- Activin receptor type-1B
- Nodal
- Left-right determination factor 2
- Embryonic growth/differentiation factor 1
- Left-right determination factor 1
- Forkhead box protein H1
- Zinc finger protein ZIC 3
Sequence:
MRANSPTQGISLKMHQARPLFLVTVALQLIGLGYSYQSEGDGAREVSNILSPVIPGTTLDRTLSNSSRKNDIPEGARLWDSLPDSSTLGESAVPVSRCCHNGGTCVLGSFCVCPAYFTGRYCEHDQRRRDCGALGHGAWTLHSCRLCRCIFSALYCLPHQTFSHCDLKSFLSSGARGSRECSIPSLLLLVLCLLLQGVAGKG
Protein: Leucine rich melanocyte differentiation associated (A0A087WWI0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGLVVRGTQVSYIGQDCREIPEHLGRDCGHFAKRLDLSFNLLRSLEGLSAFRSLEELILDNNQLGDDLVLPGLPRLHTLTLNKNRITDLENLLDHLAEVTPALEYLSLLGNVACPNELVSLEKDEEDYKRYRCFVLYKLPNLKFLDAQKVTRQEREEALVRGVFMKVVKPKASSEDVASSPERHYTPLPSASRELTSHQGVLGKCRYVYYGKNSEGNRFIRDDQL
Protein: Calsequestrin (C0KTH9)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Sarcoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004564}.
Interaction partners:
Sequence:
MLALWLLLLPCLSLLPLVQTEKGLEFPRYDGKDRVIDINNKNHQKAMKKYIMTCLLYHKPIPDGKELQKQHLMTEMVLELAAQVMEEKEIGFGMVDSHKDTKVAKKLGLVEEGSVYVFKADRVIEFDGMLSADTLVEFLLDLLEEPVEVIGNALELRAFDRMEEDIRLIGYFKNEDSEHYSAFKEAAEQFQPYIKFFATFEKAVAKELTLKMNEVDFYEPFMEEPVTLPDRPNSEEEIVAFVTEHRRPTLRKLRAEDMFETWEDVVEGSHIVAFAEEEDPDGYEFLELLKEVARDNTHHPGLSIIWIDPDDFPLLIPYWEKTFQVDLFKPQIGVVNVADADSIWLEMEEQDLLTAQKLADWIENVLSGKVNTEDDDDDNDDDEEEDDDDDDDDDSDDDSDDDSDDSDDSDDEEDEDDD
Protein: TATA-box binding protein associated factor 4 (A0A2I3BPN6)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAGSDLLDEVFFNSEVDEKVVSDLVGSLESQLAASAAHHHHLAPRTPELRAAAAGALGNHVVSGSPAGAAGAGPAASAEGAPAAAPEPPPAGRARPAGGGPRRPGSSSPRRLLVPAGPAPAPAKLRPLPEASAGPCPAAAAAAAATAAAVAGPDPAAAAPPAGPGASKPGPPGPPGPGAAQTLNGSAAPPTAPHAAPAVSPVNNGPAPPPAAGSVIQAAPAPAAPSPPAAPAPAAPPPPAPPAPVAPARPPGHPAAPAPPVSPAAAAAAAAAAAAAQNGAAPAPAAASGGAAGLGQPGAGAQGAKAEAPKPGPGPGPGPAAAAAAAGVAGGGAAGSVLLGPAMPGALPGPAPGTPAGLAKGAAAATPSLPRTPAATTGAIRATLTPTVLAPRLPQPPQNPTNIQNFQLPPGMVLVRSENGQLLMIPQQALAQMQAHAQAQPQSTMAPRPATPTGAPPVQISTVQAPGTPIIARQVTPTTIIKQVSQAQTTVQPTTTLQRSPGVQPQLVLGGSAQPASLGTATAVQTGTPQRTVPGASTTSTAATETMENVKKCKSFLSTLIKLASSGKQSTETAANVKDLVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDSAAFIQQSQQQQPPASQATTALTAVVLSSSVQRTAGKTAASVTSALQPPVISLTQPTQVIQQPPKPGALIRPPQVTLTQTPMVALRQPHNRIMLTTPQQIQLNQLQPVPVVKPTVLPGTKALSTVSAQAAAAQKNKLKEPGGGSFRDDDDINDVASMAGVNLSEESARILATNSELVGTLTRSCKDDTFLLPAPLQRRILEIGKKHGITELHPDVVSYVSHATQQRLQNLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFEQLDQIEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQKAKEMQQQELAQMRQRDANLTALAAIGPRKKRKVDCTGPGSGAEGSGPGAAVPGGSGVGTPRQFTRQRITRVNLRDLIFCLENERETSHSLLLYKAFLK
Protein: Dynein regulatory complex protein 1 (Coiled-coil domain-containing protein 164) (Q96MC2)
Organism: Homo sapiens (Human)
Function: Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes (By similarity). Plays a critical role in the assembly of N-DRC and also stabilizes the assembly of multiple inner dynein arms and radial spokes. Coassembles with CCDC65/DRC2 to form a central scaffold needed for assembly of the N-DRC and its attachment to the outer doublet microtubules.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:P0DL09}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:P0DL09}.
Interaction partners:
- Dynein regulatory complex subunit 2
- Dynein regulatory complex subunit 4
- Coiled-coil domain-containing protein 40
- Coiled-coil domain-containing protein 39
- Dynein regulatory complex subunit 7
- Dynein axonemal assembly factor 19
- Dynein axonemal intermediate chain 1
- Outer dynein arm-docking complex subunit 1
- Dynein axonemal intermediate chain 2
- Radial spoke head protein 9 homolog
Sequence:
MNPPGSLEALDPNVDEHLSTQILAPSVHSDNSQERIQARRLRIAARLEARRREALGEYLDGKKESEEDQSKSYKQKEESRLKLAKLLLCGTELVTNIQVAIDIREIHRRVEEEEIKRQRIEKLENEVKTSQDKFDEITSKWEEGKQKRIPQELWEMLNTQQLHCAGLLEDKNKLISELQQELKTKDDQYVKDLKKQSDDICLLLERMEEQVKNVMKTFREELYNIEKAFEVERQELLASNKKKWEQALQAHNAKELEYLNNRMKKVEDYEKQLNRQRIWDCEEYNMIKIKLEQDVQILEQQLQQRKAIYQLNQEKLEYNLQVLKKRDEESTVIKSQQKRKINRLHDILNNLRSKYAKQIKQFQEENQSLTSDYKRLVMQFKELQKAMRHFALIDDEKFWEIWLMNEEEAKDLIARAFDVDRIIHTHHLGLPWAAPDFWFLNNVGPISQQPQKSATQIVEEMLMRSEEEEAEEAAAEPESYLDLPKQISEKTTKRILMLLCDESGFLIESKLLSLLLPLEQNECYLLRLDAIFSALGIESEDDLYKLVNFFLKYRAHRLSSSLQIKPCSQASMEKASMEETSTRSELELAEQTEMEGEKEESLVEGEKEEEEETPPSPWVIHPNDVLKILEAFVMGLKKPRDSRAPLRVQKNVRDNSKDSEYWQALTTVIPSSKQNLWDALYTALEKYHLVLTQRAKLLLENSSLEQQNTELQALLQQYLNSKINSELQVPPTQVLRVPTK
Protein: Aminomethyltransferase, mitochondrial (EC 2.1.2.10) (Glycine cleavage system T protein) (GCVT) (Glycine decarboxylase complex subunit T) (P48015)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine.
Subcellular location: Mitochondrion.
Interaction partners:
- Serine hydroxymethyltransferase, mitochondrial
- Glycine dehydrogenase
- Glycine cleavage system H protein, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Methylenetetrahydrofolate dehydrogenase [NAD
- Alanine--glyoxylate aminotransferase 1
- Bifunctional purine biosynthesis protein ADE17
- C-1-tetrahydrofolate synthase, mitochondrial
- Methylenetetrahydrofolate reductase 1
Sequence:
MSIIKKIVFKRFNSTLKKTALHDLHVSLGGTMVPYAGYSMPVLYKGQTHIESHNWTRTNAGLFDVSHMLQSKLSGPHSVKFLQRVTPTDFNALPVGSGTLSVLLNPQGGVVDDTIITKENDDNEFYIVTNAGCAERDTEFFHDELQNGSTLDCQWKIIEGRSLLALQGPKAKDVLEPLLSKTAPGKDLKELFFGQRHEFALKDGSLVQIARGGYTGEDGFEISIANEKAVEFAEQLLANPVMKPIGLAARDSLRLEAGMCLYGHELDESITPVEAALNWVISKSRRDLVDQKYWFNGYAKIMDQLNNKTYSKVRVGFKYLKKGPAARNGVKIFLPDAETEVGLVTSGSASPTLNNINIGQAYVQKGYHKKGTKLLVQVRNKFYPIELAKMPLVPTHYYKQ
Protein: Meiotic spindle formation protein mei-1 (EC 5.6.1.1) (Katanin p60 ATPase-containing subunit A1) (Katanin p60 subunit A1) (p60 katanin) (P34808)
Organism: Caenorhabditis elegans
Function: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays. Required specifically for meiotic spindle formation in the female germline; the presence of this protein is inimical to the formation of mitotic spindles. In body wall muscles, regulates organization of myosin thick filaments.
Subcellular location: Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:10809666, ECO:0000269|PubMed:12781129, ECO:0000269|PubMed:8027178}. Chromosome {ECO:0000269|PubMed:12781129, ECO:0000269|PubMed:16338136}. Cytoplasm {ECO:0000269|PubMed:16338136}. Note=Localizes to the spindle poles and condensed chromatin during female meiosis (PubMed:10809666, PubMed:12781129, PubMed:16338136, PubMed:8027178). This localization requires mei-2 (PubMed:10809666). Also localizes to the polar body (PubMed:12781129). Ser-92 phosphorylated mei-1 is first detected on the maternal chromatin in anaphase of meiosis I, then localizes to the cytoplasm during meiosis II and quickly disappears between pronuclear formation and the first cell division, except in the polar bodies (PubMed:16338136). {ECO:0000269|PubMed:10809666, ECO:0000269|PubMed:12781129, ECO:0000269|PubMed:16338136, ECO:0000269|PubMed:8027178}.
Interaction partners:
- Meiotic spindle formation protein 2
- Katanin_con80 domain-containing protein
- WD_REPEATS_REGION domain-containing protein
- Protein maternal effect lethal 26
- Dual specificity tyrosine-phosphorylation-regulated kinase mbk-2
- Kinesin motor domain-containing protein
- Calponin-homology
- Protein tyrosine phosphatase-like protein egg-3
- Kinesin-like protein
- CCCH-type zinc finger protein oma-1
Sequence:
MNGDVQSVIRGYLERAQVAKTMSDAGRWNEAGDLLRQLMTDVKSCKISASNRDEHDARNTFLRALEANLKLVQQNVRDEDDLHEAMTRQSGSPEPPADPDVWSKPSPPLPSSSKFGATKKGVGAAGPRPREISKSTSSMSTNPADVKPANPTQGILPQNSAGDSFDASAYDAYIVQAVRGTMATNTENTMSLDDIIGMHDVKQVLHEAVTLPLLVPEFFQGLRSPWKAMVLAGPPGTGKTLIARAIASESSSTFFTVSSTDLSSKWRGDSEKIVRLLFELARFYAPSIIFIDEIDTLGGQRGNSGEHEASRRVKSEFLVQMDGSQNKFDSRRVFVLAATNIPWELDEALRRRFEKRIFIPLPDIDARKKLIEKSMEGTPKSDEINYDDLAARTEGFSGADVVSLCRTAAINVLRRYDTKSLRGGELTAAMESLKAELVRNIDFEAALQAVSPSAGPDTMLKCKEWCDSFGAM
Protein: LD29161p (Myoglianin, isoform A) (Myoglianin, isoform C) (Myoglianin, isoform D) (Q9V4F4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- receptor protein serine/threonine kinase
- Serine/threonine-protein kinase receptor
- Mothers against decapentaplegic homolog
- Follistatin, isoform A
- Protein screw
- receptor protein serine/threonine kinase
- receptor protein serine/threonine kinase
Sequence:
MLANSCCGWRKYKTHDQHHRTLKKKTRQNTSDTTVHIEVNSNEIQFPGSYRFNLDSKKINIGRMNILGHKRGNFRVTRYVTVTVLLILSTAVNAYAQPENKSFSNSSNNDSPEMVMLSNETNNSAKVLSEKNGSSSISADDKINENMGIFQMKVQSKPGKKSTPLAKVSEHGDLSRVQSVSLYRNTLINIESMLQRQLREKAKVDSIESIKMHILMRLNLKKLPNITKPISVPQNIIDNFYRDYNASSKTTVWNRMESIDESHLSINDTYGDHIMTDFFDESSSSQMQGDDANTVNEFLIDLNKNQAKKSDIPINTNDEEYESILSHISSIYIFPEEIQPHVRHNRKVDVFRFQIDSSYSDLSYATLHLYLRGWDWISAHQPGLLEEIKKQPRKDIVVTIHRAIRVANTTSFNPKVKMFEFRHSIPSGLGQWVAVDLKSLLGNLGSNMTQEILIKGAETWMKSLVVTTDNTSKNPLTVHIEIGSQKKHRRKRSVYMDCTENDHDMRCCRYPLKVNFTSFGWHFVVAPTSFDAYFCSGDCKVGYLEQYPHTHLAALTTSATPCCSPTKMSSLSLLYFDDNHNLVLSVIPNMSVEGCSCS
Protein: Cysteine protease atg4da (EC 3.4.22.-) (Autophagy-related protein 4 homolog D-A) (R4GER2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (By similarity). The protease activity is required for proteolytic activation of ATG8 family proteins to reveal a C-terminal glycine (By similarity). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (By similarity). In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (By similarity). Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (By similarity). ATG4D plays a role in the autophagy-mediated neuronal homeostasis in the central nervous system.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q86TL0}.
Interaction partners:
- GABA
- GABA
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Uncharacterized protein LOC100000242
- Map1lc3b protein
- Ubiquitin-like-conjugating enzyme ATG3
- MAP1 light chain 3-like protein 2
- Ubiquitin-like modifier-activating enzyme ATG7
- Microtubule-associated protein 1 light chain 3 alpha
- Phosphatidylinositol 3-kinase catalytic subunit type 3
Sequence:
MNSVSPSAVQYIVGGGAHEDKASASSKRHLGHGAVPDGIREGSGEPDEVDRLKAKFMSAWNNVKYGWTVKSKTSFNKSSPLILLGQSFLFNNEDEVERFRQTFVSCVWLTYRREFPQLDGSSLTTDCGWGCMLRSGQMMLAQGLLLHLMPTDWRWSDCHALTDVDFEVLKPRSPSRPAGMSMPSFSSSWSSSIPQINPSPGITEAHRRAPARCPSASPDPQVDALHRKVVSCFGDHPSAPFGVHQLVELGKESGKRAGDWYGPSVVAHMLRKAVARAAEFEDLAVYVAQDCTVYKEDVMSLCESSGVGWKSVVILVPVRLGGESLNPSYIECVKNILKLKCCIGIIGGKPKHSLFFVGFQDEQLLYLDPHYCQPVVDVTQANFSLESFHCNSPRKMNFSRMDPSCTIGLYARSKTDFESLCTAVSEALSSSKEKYPIFTFVEGRGQIYGMEGPSGGSVDAPAHIFTCSRLSRNNKRGSTDEFVLL
Protein: Acyl-coenzyme A oxidase 1 (EC 1.3.3.6) (Q7KML2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. First enzyme of the fatty acid beta-oxidation pathway.
Subcellular location: Peroxisome {ECO:0000250}. Nucleus {ECO:0000269|PubMed:32169171}.
Interaction partners:
- Sterol carrier protein 2
- Probable enoyl-CoA hydratase, mitochondrial
- acetyl-CoA C-acyltransferase
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase 2
- Peroxisomal multifunctional enzyme type 2
- Trifunctional enzyme subunit alpha, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase 1, isoform A)
- HL08109p)
Sequence:
MPAKPVNPDLQKERSTATFNPREFSVLWAGGEERFKEKKALEKLFLEDPALQDDLPISYLSHKELYEHSLRKACIIGEKIRKLRADGEDGVDTYNALLGGSLGSAILKEGNPLALHYVMFVPTIMGQGTMDQQVEWLSKAWDCEIIGTYAQTELGHGTFLRGLETRADYDASTQEFVINTPSLSAYKWWPGGLGHTANHAVVVAQLYTKGEFRGLAPFIVQLRDSDTHRPMPGIDIGDIGTKLGMKGVNNGYLGLKNVRVPLNNMLMKNQQVLPDGTYVAPKNSVLTYGTMMFVRCALIRDTAQSLAKASTIATRYSAVRRQSPIDPNQPEPQIMDHTTQQLKLFPQIAKAIVFKTTGDGIWNMYNVISGEIEQGNLDRLPEMHALSCCLKAICSADAAAGVETCRLSCGGHGYMDCSNFPTIYGMTTAVCTYEGENTVMLLQTARYLVKVYGQALNGEKLVPTVSYISDAINQTKFVNFDGSLRSIVKAFQFVAANKTRIAYEQIELRRKQGYGTEVAANLCGTFLTAAADLHGRAFLAQTAYTELLALSREVSPELAEVLKVVLELYLVDACLNRIGDFLRFIDLTDQDVTKLEVRLENCLKRFRPNAVSLVDSFDLHDRVLDSALGAYDGNVYEHIFESTKKNPLNKEPVNGAFHKYLKPFMKAHL
Protein: procollagen-proline 4-dioxygenase (EC 1.14.11.2) (A0A1P6BZ71)
Organism: Brugia malayi (Filarial nematode worm)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
- BMA-PHY-2, isoform j.
- Pyrroline-5-carboxylate reductase
Sequence:
MIATVVFILALRSTTHADLFTSIAEMELLLEADKRIPDLLDMYIERFQQRLDQIRQLSVGKKQLGNRSLGNDIRLLSNPVSAYLLIKRLIEEWDDIKRLAGSDIGEELLKEISELRAMNYVKNPTTEDLVGAAIALLRLQDTYRLNVKEIADGKILNASGVQPFTARDCFDIGRAAYNVNDYYHTLIWMEEAQERLRDEAPHETVQLKEILEYLAFALFKQGNLKRALLLTEQLHTIDPNHPRAKNNIKWYEDLLAEEGLKPIDYRRNIPPVTNPRPTTGLETAEHDIYEALCRNEIPVSIKVTSKLYCYYKMDRPFLRLAPFKVEILRFNPLAVLFRDVITDEEVTMIQMLATPRLRRATVQNSITGELETASYRTSKSAWLKDEEHEVVHRINKRIDLMTNLEQETSEELQVGNYGIGGHYDPHFDFARREEVNAFQSLNTGNRLATLLFYMTQPESGGATVFTEVKTTVMPSKNDALFWYNLLRSGEGDLRTRHAACPVLTGTKWVSNKWIHERGQEFRRPCGLSRSVEEQFVGDLSA
Protein: Cell adhesion molecule L1-like (A0A8I6A9A6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MELPLGGRGLILSLIFLLLKLSTAEIPLSVHQVPTIVKQSYVQVAFPFDEYFQIECEAKGNPEPKFSWTKDDKPFDLSDPRIIAFNNSGTFRIPNEGHISHFQGKYRCFASNRLGTAISEEIEFIVPGVPKFPKEKIEPIDVEEGDSIVLPCNPPKGHPPLHIYWMNIELEHIEQDERVYMSQKGDLYFANVEEKDSRNDYCCFAAFPKLRTIVQKMPMKLTVNSLKHANDSSSSTEISNQANSIKQRKPKLLLPPAQIGSASSKTVLKGDTLLLECFAEGLPTPQIEWSKLGSELPKGRATIEIHEKTLKIENVSYQDRGNYRCTANNLLGKASHDFHVIVEEPPRWKKKPQSAVYSTGSNGILLCEAEGEPQPTIKWRVNGLPIENHPFPGDVMFPREISFTNLQPNHTAVYQCEASNIHGTILANANIDVVDVVPLIQTKNEENYETVVGYSAFLHCEYFASPKATVVWEVADETHPLEGGRYHTHENGTLEIERTTEEDAGSYSCWVDNTMGKAVITANLDIRNATKLRVFPKNPRIPKSHVLELYCESQCDSHLKHSLKLSWSKDGEAFEMNGTEDGRIVIDGANLTISNISGEDQGIYSCSAQTALDSTSGKTQVTVLGVPDPPRNLLLSERQNRSVRLSWEAGDDHNSKISEYIVEFEGNREEPGKWEELTRVRGEETDVVLPLAPYVRYQFRVTAVNEVGKSHSSQPSDHHETPPAAPDKNPHNIRVQASQPKEMIIKWEPLKSMEQNGPGLEYRVSWKPQGAPEEWEEETVTNHTLRVMTPTVYAPYDVQVQAINQLGSGPEPQPVTLYSGEDYPSTAPVIHRVDVMNSTLVKVTWSSIPKETVHGLLRGYQINWWKTKSLLDGRTHPKEVNILRFSGQRNSGMVPSLEPFSEFHLTVLAYNSKGAGPESEPYIFQTPEGVPEQPSFLKVIKVDKDTATLSWGLPKKLNGNLTGYLLQYQIINDTYELGELNEINVTTPSKSSWHLSNLNATTKYKFYLKACTSRGCGKPISEEGATLGEGKYAGLYDDISTQGWFIGLMCAIALLTLILLTVCFVKRNRGGKYSVKEKEDLHPDPEVQSAKDETFGEYSDSDEKPLKGSLRSLNRNMQPTESADSLVEYGEGDQSIFNEDGSFIGAYTGAKEKGSVESNGSSTATFPLRA