wanglab/gogpt-training-data huggingface dataset:
Protein: Actin cytoskeleton-regulatory complex protein SLA1 (P32790)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization.
Subcellular location: Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, actin patch. Note=Cytoplasmic and cortical actin patches. Is associated with cortical actin patches in its dephosphorylated form and dissociates upon phosphorylation by PRK1.
Interaction partners:
- LAS seventeen-binding protein 3
- Actin cytoskeleton-regulatory complex protein END3
- Proline-rich protein LAS17
- Actin cytoskeleton-regulatory complex protein PAN1
- Actin-binding protein
- Protein ECM25
- Protein SLA2
- Protein YSC84
- Verprolin
- Polyubiquitin
Sequence:
MTVFLGIYRAVYAYEPQTPEELAIQEDDLLYLLQKSDIDDWWTVKKRVIGSDSEEPVGLVPSTYIEEAPVLKKVRAIYDYEQVQNADEELTFHENDVFDVFDDKDADWLLVKSTVSNEFGFIPGNYVEPENGSTSKQEQAPAAAEAPAATPAAAPASAAVLPTNFLPPPQHNDRARMMQSKEDQAPDEDEEGPPPAMPARPTATTETTDATAAAVRSRTRLSYSDNDNDDEEDDYYYNSNSNNVGNHEYNTEYHSWNVTEIEGRKKKKAKLSIGNNKINFIPQKGTPHEWSIDKLVSYDNEKKHMFLEFVDPYRSLELHTGNTTTCEEIMNIIGEYKGASRDPGLREVEMASKSKKRGIVQYDFMAESQDELTIKSGDKVYILDDKKSKDWWMCQLVDSGKSGLVPAQFIEPVRDKKHTESTASGIIKSIKKNFTKSPSRSRSRSRSKSNANASWKDDELQNDVVGSAAGKRSRKSSLSSHKKNSSATKDFPNPKKSRLWVDRSGTFKVDAEFIGCAKGKIHLHKANGVKIAVAADKLSNEDLAYVEKITGFSLEKFKANDGSSSRGTDSRDSERERRRRLKEQEEKERDRRLKERELYELKKARELLDEERSRLQEKELPPIKPPRPTSTTSVPNTTSVPPAESSNNNNSSNKYDWFEFFLNCGVDVSNCQRYTINFDREQLTEDMMPDINNSMLRTLGLREGDIVRVMKHLDKKFGRENIASIPTNATGNMFSQPDGSLNVATSPETSLPQQLLPQTTSPAQTAPSTSAETDDAWTVKPASKSESNLLSKKSEFTGSMQDLLDLQPLEPKKAAASTPEPNLKDLEPVKTGGTTVPAAPVSSAPVSSAPAPLDPFKTGGNNILPLSTGFVMMPMITGGDMLPMQRTGGFVVPQTTFGMQSQVTGGILPVQKTGNGLIPISNTGGAMMPQTTFGAAATVLPLQKTGGGLIPIATTGGAQFPQTSFNVQGQQQLPTGSILPVQKTANGLISANTGVSMPTVQRTGGTMIPQTSFGVSQQLTGGAMMTQPQNTGSAMMPQTSFNAVPQITGGAMMPQTSFNALPQVTGGAMMPLQRTGGALNTFNTGGAMIPQTSFSSQAQNTGGFRPQSQFGLTLQKTGGIAPLNQNQFTGGAMNTLSTGGVLQQQQPQTMNTFNTGGVMQELQMMTTFNTGGAMQQPQMMNTFNTDGIMQQPQMMNTFNTGGAMQQPQQQALQNQPTGFGFGNGPQQSRQANIFNATASNPFGF
Protein: Neutrophil cytosol factor 1 (Neutrophil cytosolic factor 1) (Q4Z8P3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAETYVRHVELLGFEKRFFPSQHYVYMLLVKWSDQSEKLVYRRYPEVHTLHKTLKEMFPIEAGDIDEKDRIIPTLPAPKWLDNQKTTETRQATLAEYCRSLLNLPANISRCQLIRDFFKMRPEDETPPAPHPYKRNETFIMSTNRVRSNTTSEITGPIMLETYRVIADYSKSSKYELTLKMGDMVDIVEKSPNGWWFCQCESRRGWVPASYLEPLDGADESEEPEPNYAGELYKTTRGYKAVEQDEMTLEAGVIIEVIHKLLDGWWVVRKGEETGFYPSMFLCRTGEKKEVDAERDVVRRATPPPRRSTIRNAQSIHSTVRRRISQDSYRKQSRRFLQQRGRLNSHSRIGTRSPLQERRTNRENIEKSSAPQAEDEDKSVPVVPPRPSPQLILERCTENTSKRMSMQEAD
Protein: Catalase-peroxidase (CP) (EC 1.11.1.21) (Catalase-2) (Peroxidase/catalase) (Q7Z7W6)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May be involved in protection from the host during host infection.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03108}.
Interaction partners:
- Transaminase A
- Aromatic-L-amino-acid decarboxylase, putative
- histidinol-phosphate transaminase
- Kynureninase 2
- aspartate transaminase
- Kynureninase 1
- Aspartate aminotransferase
- aromatic-amino-acid transaminase
- 3-hydroxyanthranilate 3,4-dioxygenase 1
- aspartate transaminase
Sequence:
MTQDKCPFKEQSSQPNFAGGGTSNKDWWPDRLKLNILRQHTAVSNPLDADFDYAAAFNSLDYEGLKKDLRALMTDSQDWWPADFGHYGGLFIRMAWHSAGTYRVFDGRGGAGQGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGNKISWADLLILTGNVALESMGFKTFGFAGGRPDTWEADEATYWGRETTWLGNDARYAKGFSGSDKRGSLIADEESHKTTHSRELETPLAAAHMGLIYVNPEGPDGNPDPVAAAHDIRDTFGRMAMNDEETVALIAGGHTFGKTHGAAPADNVGKEPEAAGLEAQGLGWANKHGSGKGPHTITSGLEVTWTKTPTQWNNNFLEYLFKFEWELTKSPAGAHQWVAKNADEIIPDAYDASKKHKPTMLTTDLSLRFDPAYEKIARRFLEHPDQFADAFARAWFKLTHRDMGPRARYLGPEVPSEVLIWQDPIPAVNHPLVDASDIAALKDEILASGVPPRSFISTAWAAASTFRGSDKRGGANGARIRLAPQRDWEVNNQPWLREALSALEAVQSRFNARGDSKKVSLADLIVLAGCAAVEKAAQDAGHPIKVPFVPGRMDASQEETDVQSFNHMEPFADGFRNFAKGPARPRAEHYLVDKAQLLNLSAPEMTVLVGGLRVLNTNYDGSTHGVFTSRPGALTNDFFVHLLDMNTAWKDVGNGELFEGSDRKTGGKKWTATRADLVFGSNAELRAIAEVYASNDGDMKFVKDFVAAWNKVMNLDRFDLKGKQTIPARL
Protein: Conidiophore development regulator abaA (E9RD40)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (By similarity). Essential for differentiation and functionality of phialides as conidiogenous cells. Regulates autolysis and cell death. Positively regulates expression of the gliotoxin biosynthetic gene cluster in actively growing vegetative cells, and likely bridges morphological and chemical development during the life-cycle. Negatively regulates expression of the melanin biosynthetic gene cluster.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:I1S4T3}. Note=localizes to the nuclei of phialides and terminal cells of mature conidia (By similarity). {ECO:0000250|UniProtKB:I1S4T3}.
Interaction partners:
- Sexual development transcription factor SteA
- C2H2 type master regulator of conidiophore development brlA
- Developmental regulatory protein wetA
- Developmental and secondary metabolism regulator veA
- Cell pattern formation-associated protein stuA
- Secondary metabolism regulator laeA
- Velvet domain-containing protein
- Orotidine 5'-phosphate decarboxylase
- rRNA-processing protein efg1
Sequence:
MATDWQPECIAPQHQSGLENIGHHTDRALQNTSGNVQSYSDAILHGGMSGRDDHLQHLAYKYSHAPVHPQPMQTATTLHPHHILNARVQAKKLRRVQSLGPNHAGARRGRSYLKSQKYLEYRARPRRDTGKDGEPVWSDELEDAFQQALEANPPMGRRKWSERGKSYGRNELIAEYIYKVTGKKRTRKQVSSHLQVLDSFLKGDPDWERLVREQPADRSGNQHQPVGPKWRTSLDHPLPSHYGGHMHATYHDHLSPVQPYVGELPPPHYTLGSNMHERSTDTIHGFNFDMWVSAPQQANQGDKAFHVYTCLQGDQYHPVAPPMPLENVRDWRTTFPHLNSVMEELDGPLDCEIILLEASLKLMNDFPPPGSKLGIQLDIDFAPPGMTDATVLSQMDNWTCSTYIYEDGNRLSKADHNLARPLSTKVKPPFESSWWAKLFTELTQDKQMAEKSGRHQNADDHIRQFFRSLSAVQEIRAISQNSRRVSQGSGHPGDCSKRMAILLWKFRQTLPDEVGLTTWRKLIPPPDRTMMNSPKPATGIDLPPLSLDSILLKPQPPNVYQNPQGHDLLHQNGTSQPHWPLYPPPHESMSNMYHSTGSFDFLNSVSKAEDGLPDRTAVTSILDSFPAMPPQETSQPSSLNVSSGGPVMLNVHDMSLSHHNLAGYALSHDNHYVPSQQHGVSVHDSSNVLNNIFGPGSQPMDEIGNSQSAWGPPIPSTTIPSDVGSNHYTHLPYHHHDHQTSASRESHPPNGFEGLMGPDDLMDKIVGSMPDDPGMNGAGPDHASAAYADTNATEAVQ
Protein: Phosphatidylserine decarboxylase proenzyme 2, mitochondrial (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 2 beta chain; Phosphatidylserine decarboxylase 2 alpha chain] (Q9UTB5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity). Together with psd1 and psd3, responsible for the majority of phosphatidylethanolamine synthesis. Plays a role in lipid droplet biogenesis at the endoplasmic reticulum membrane.
Subcellular location: [Phosphatidylserine decarboxylase 2 beta chain]: Mitochondrion {ECO:0000305|PubMed:16823372, ECO:0000305|PubMed:34818062}. Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Nucleus envelope {ECO:0000269|PubMed:16823372}.; SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 2 alpha chain]: Mitochondrion {ECO:0000305|PubMed:16823372, ECO:0000305|PubMed:34818062}. Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Nucleus envelope {ECO:0000269|PubMed:16823372}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}.; SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:34818062}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:34818062}.
Interaction partners:
- Uncharacterized CDP-alcohol phosphatidyltransferase class-I family protein C22A12.10
- Lysophospholipid acyltransferase
- Phosphatidylserine decarboxylase proenzyme 3
- Phosphatidylethanolamine N-methyltransferase
- Phospholipase D1
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Triacylglycerol lipase ptl3
- ERMES regulator 1
Sequence:
MRPRQRFRRFHPRWSKVNLRGFGGVGALKGVKALNGMNVRVSMRLKWISNRIHRIRRSRRLGRLSISVRPNGSWQVYLLSSLPLRSLSRVWGQFNRAHLPTFLRTPGFKLYAWVFGCNLSELKDPDLTHYRNFQDFFCRELRPETRPVDPVSPVVSPVDGRIVCQGVVDNNRIQHVKGLSYSLEALLGGISSSNPLVVNFEDEITPDLIQKHEQFAEQHSISLNSNNRYRKADASAAVVDEHSDEEALLCAFTDHPHFYLNDSRNSLNYFCPFSAFEDISNSVRSSCGKRLSPSSNFDLNNLGGDDDLRSESSSDFESAPASILEHEPTNWDDWVQEADVTDIDSLPWHNIRPGNKLFYSVIYLAPGDYHRFHSPADWVIESRRHFSGELFSVSPFLARRLHNLFVLNERVALLGRYEHGFMSMIPVGATNVGSIVINCDPTLSTNRLVLRKKSLGTFQEAVYKNASPVLDGMPVSRGEQVGGFQLGSTVVLVFEAPADFEFSTYQGQYVRVGEAL
Protein: rRNA methyltransferase 2, mitochondrial (EC 2.1.1.-) (16S rRNA (uridine(1369)-2'-O)-methyltransferase) (16S rRNA [Um1369] 2'-O-methyltransferase) (Protein ftsJ homolog 2) (Q9UI43)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:24036117, ECO:0000269|PubMed:25009282}.
Interaction partners:
- Mitochondrial ribosome-associated GTPase 1
- 5-cytosine rRNA methyltransferase NSUN4
- Mitochondrial ribosome-associated GTPase 2
- Mitochondrial assembly of ribosomal large subunit protein 1
- Transcription termination factor 4, mitochondrial
- rRNA methyltransferase 1, mitochondrial
- Large ribosomal subunit protein uL24m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL4m
Sequence:
MAGYLKLVCVSFQRQGFHTVGSRCKNRTGAEHLWLTRHLRDPFVKAAKVESYRCRSAFKLLEVNERHQILRPGLRVLDCGAAPGAWSQVAVQKVNAAGTDPSSPVGFVLGVDLLHIFPLEGATFLCPADVTDPRTSQRILEVLPGRRADVILSDMAPNATGFRDLDHDRLISLCLTLLSVTPDILQPGGTFLCKTWAGSQSRRLQRRLTEEFQNVRIIKPEASRKESSEVYFLATQYHGRKGTVKQ
Protein: Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase (EC 2.4.1.265) (Asparagine-linked glycosylation protein 8) (Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl alpha-1,3-glucosyltransferase) (Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase) (P40351)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:3536907}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dol-P-Glc:Glc
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dol-P-Man:Man
- Dol-P-Man:Man
- Dolichyl-phosphate beta-glucosyltransferase
- GDP-Man:Man
- Glucosidase 2 subunit alpha
- UDP-N-acetylglucosamine transferase subunit ALG13
- Mannosyl-oligosaccharide glucosidase
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
Sequence:
MKGDRSRQNMAVTKKAKLKKNDEPKKVLKTAATEKGEGSKRYSLWNFWISTLFLKLLLIPDYFSTDFDVHRNWLAITNKLPISEWYYEHTSQWTLDYPPFFAYFEWFLSQFVPKSVRDDGCLDIVEIGKFGLPTIVFQRLTVIFSEILLFVILQIYINTTKLSERSQSFVVASSIVLSPGFLIIDHIHFQYNGFLFAILIGSIVAAKNKRYILCAVLYTTAICFKHIFLYLAPCYFVFLLRAYVLNVNNFKFKSYKDFLFLIRWANLLKLATVVVGIFTICFLPFAHQMPQVLSRLFPFSRGLTHAYWAPNFWALYSFMDKILTTVMLKLPYVHTFATKFIKPPLIPQNIKEINERLAANNNGSKGLVQDVFFVILPQIPPKLTFILTIFYQVLAVLPLLFDPSFKRFVGSLTLCGLASFLFGWHVHEKAIMLVIIPFTFLVGFDRRLLVPFMLVASAGYVSLYPLLYKGQDFFIKTLYTYVWCIIYFAAFRKTTKISSSVERRIFFLDRLALTYIFSLLPIVTVLQILDEVKWRYSFLQKFEFLGLMIYSVYCSLGIISSWFALSWLYNFDELLWQ
Protein: UPF0696 protein C11orf68 (Basophilic leukemia-expressed protein Bles03) (Protein p5326) (Q9H3H3)
Organism: Homo sapiens (Human)
Interaction partners:
- Eukaryotic translation initiation factor 4H
Sequence:
MAAAAAAAVAGVGRGGGGAEPRQERSRARGWAGVERSEGRRMEPGEELEEEGSPGGREDGFTAEHLAAEAMAADMDPWLVFDARTTPATELDAWLAKYPPSQVTRYGDPGSPNSEPVGWIAVYGQGYSPNSGDVQGLQAAWEALQTSGRPITPGTLRQLAITHHVLSGKWLMHLAPGFKLDHAWAGIARAVVEGQLQVAKVSPRAKEGGRQVICVYTDDFTDRLGVLEADSAIRAAGIKCLLTYKPDVYTYLGIYRANRWHLCPTLYESRFQLGGSARGSRVLDRANNVELT
Protein: Kinesin-like protein KIF11 (Kinesin-related motor protein Eg5) (Q6P9P6)
Organism: Mus musculus (Mouse)
Function: Motor protein required for establishing a bipolar spindle during mitosis. Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P52732}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P52732}.
Interaction partners:
- Disks large-associated protein 5
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Abnormal spindle-like microcephaly-associated protein homolog
- Centromere-associated protein E
- Kinesin-like protein KIF23
- Dual specificity protein kinase TTK
- Centrosomal protein of 55 kDa
- Cyclin-A2
- Protein regulator of cytokinesis 1
- Mitotic checkpoint serine/threonine-protein kinase BUB1
Sequence:
MASQPSSLKKKEEKGRNIQVVVRCRPFNLAERKANAHSVVECDHARKEVSVRTAGLTDKTSKKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSPNEVYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLSPSSDVSERLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFSVTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHIPYRESKLTRILQDSLGGRTRTSIIATISPASFNLEETLSTLEYAHRAKNIMNKPEVNQKLTKKALIKEYTEEIERLKRDLAAAREKNGVYISEESFRAMNGKVTVQEEQIVELVEKIAVLEEELSKATELFMDSKNELDQCKSDLQTKTQELETTQKHLQETKLQLVKEEYVSSALERTEKTLHDTASKLLNTVKETTRAVSGLHSKLDRKRAIDEHNAEAQESFGKNLNSLFNNMEELIKDGSAKQKAMLDVHKTLFGNLMSSSVSALDTITTTALESLVSIPENVSARVSQISDMILEEQSLAAQSKSVLQGLIDELVTDLFTSLKTIVAPSVVSILNINKQLQHIFRASSTVAEKVEDQKREIDSFLSILCNNLHELRENTVSSLVESQKLCGDLTEDLKTIKETHSQELCQLSSSWAERFCALEKKYENIQKPLNSIQENTELRSTDIINKTTVHSKKILAESDGLLQELRHFNQEGTQLVEESVGHCSSLNSNLETVSQEITQKCGTLNTSTVHFSDQWASCLSKRKEELENLMEFVNGCCKASSSEITKKVREQSAAVANQHSSFVAQMTSDEESCKAGSLELDKTIKTGLTKLNCFLKQDLKLDIPTGMTPERKKYLYPTTLVRTEPREQLLDQLQKKQPPMMLNSSEASKETSQDMDEEREALEQCTEELVSPETTEHPSADCSSSRGLPFFQRKKPHGKDKENRGLNPVEKYKVEEASDLSISKSRLPLHTSINL
Protein: GH14088p (Ser7 (EC 3.4.21.-)) (Q9W314)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI01422p
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Cyclin-dependent kinase 7
- Cyclin-dependent kinase 12
- Cyclin-dependent kinase 9
- DNA-directed RNA polymerase II subunit RPB3
- Transcription elongation factor SPT5
Sequence:
MLLLIPLFLTLLGAEAQQFGKAIMHFGNCNSVEFGRGTCIEKKDCDFYAVDKLMELASKQQCFSRQRPDLVCCPRETNIIPPLAPRISNGTTNATSSTTTLKLLPRTTPRPPSGIDQLPEHPYCGSAFSFRLVGGHNTGLFEFPWTTLLEYETVSGGKDYACGASFIAQRWLLTAAHCIHTMGRNLTAAILGEWNRDTDPDCENDLNGVRECAPPHIRVTIDRILPHAQYSELNYRNDIALLRLSRPVNWLQMQNLEPVCLPPQRGRYANQLAGSAADVSGWGKTESSGSSKIKQKAMLHIQPQDQCQEAFYKDTKITLADSQMCAGGEIGVDSCSGDSGGPLTVEANTASGNRYVYLAGVVSIGRKHCGTALFSGIYTRVSSYMDWIESTIRANRI
Protein: T-complex protein 1 subunit delta (TCP-1-delta) (CCT-delta) (P50999)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- T-complex protein 1 subunit epsilon
- Probable T-complex protein 1 subunit beta
- T-complex protein 1 subunit zeta
- Probable T-complex protein 1 subunit eta
- T-complex protein 1 subunit gamma
- Probable T-complex protein 1 subunit theta
- T-complex protein 1 subunit alpha
- Uncharacterized protein C17C9.14
- Probable prefoldin subunit 5
- Phosducin-like protein C2A9.09
Sequence:
MSKAATVPVAFQDREKPQEVRLSNIMAARSVADAIRTSLGPKGMDKMIQTGKGEVILTNDGATILKHLSVLHPAAKMLVDLSAAQDVEAGDGTTSVVILAGSMLACAEKLLKKGIHPTVIAESFQRAAGFTVDCMKENALAIELSDRESLLRAATTSLNSKIVSQYSNLLAPIAVDAVLKVIDPRVATNVDLKDIRIVKKLGGIIDDTELIPGLALTQTAVKSAGGPTRIEKANIALIQFQLSPPKPDMENQVVVNDYRQMDKILKEERQYLLNMCKKIKKAGANVILIQKSILRDAVNDLALHFLAKLKIMVIKDIERDEVEFICKSTGCKPIADIESFAEDKLGHADLVEETSSSGEKIVKFSGVKNAGKTVSILCRGANLLTLEEAERSLHDALCVIRCLVKQRALIAGGGSPEIEAAQRLLEHARQLEGREAICIRAFSEALEIIPVTLAENAGLNAIQVVTELRSRHANGEKTAGINVRKGIVTNILEENVLQPLLVNISAIQLAAETTKMIMKIDDITLAR
Protein: Psalmotoxin-1 (PcTx1) (Pi-theraphotoxin-Pc1a) (Pi-TRTX-Pc1a) (P60514)
Organism: Psalmopoeus cambridgei (Trinidad chevron tarantula)
Function: This toxin is a gating modifier that acts principally as an inhibitor on ASIC1a (ASIC isoform 2) and a potentiator on ASIC1b (ASIC isoform 3). This toxin potently and selectively inhibits rat, mouse and human ASIC1a (IC(50)=0.35-3.7 nM). The blockade is rapidly reversible. The toxin acts by shifting its steady-state desensitization to more alkaline pH (0.27 pH unit). At higher concentrations, it potentiates rat and human ASIC1b and activates chicken ASIC1 by stabilizing the open state of these subtypes. The toxin binds most tightly to the open and the desensitized states of ASIC1a (promoting desensitization), whereas it binds most tightly to the open state of ASIC1b (promoting opening). The toxin also inhibits mouse ASIC1a-ASIC2b (IC(50)=2.64 nM) and rat ASIC1a-ASIC2a. It binds to the extracellular domain at subunit interfaces in the acidic pocket with the majority of contacts on the thumb domain of the channel. It is also noteworthy that calcium competes with the toxin, probably by inhibiting binding of the toxin to the channel.
Subcellular location: Secreted {ECO:0000269|PubMed:10829030}.
Interaction partners:
Sequence:
EDCIPKWKGCVNRHGDCCEGLECWKRRRSFEVCVPKTPKT
Protein: Gamma-crystallin F (Gamma-F-crystallin) (Q9CXV3)
Organism: Mus musculus (Mouse)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Gamma-crystallin B
- Alpha-crystallin A chain
Sequence:
MGKITFYEDRSFQGRHYECSTDHSNLQPYFSRCNSVRVDSGCWMLYEQPNFAGCQYFLRRGDYPDYQQWMGFSDSVRSCHLIPHSTSHRIRIYEREDYRGQMVEITDDCSHLQDRFHFSDFHSFHVMEGYWVLYEMPNYRGRQYLLRPGEYRRYHDWGAMNARVGSLRRIMDFY
Protein: 65-kDa microtubule-associated protein 3 (AtMAP65-3) (Protein PLEIADE) (Q9FHM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Microtubule-associated protein that plays a critical role in organizing the mitotic microtubule array during both early and late mitosis in all plant organs. Essential for the cytokinesis, especially in roots, by maintaining the integrity of the overlapped microtubules in the phragmoplast. Required during root morphogenesis. Needed for giant cell development during root knot nematode infection, where cytokinesis is initiated but not completed.
Subcellular location: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, phragmoplast. Note=Locates only to the mitotic MT arrays. Present in MT cortical arrays just before mitosis. Associates to MT in preprophase band, during anaphase, and in phragmoplast, including midzone. Distributed diffusely through the cytoplasm during metaphase only. At the end of cytokinesis, present only at the cell periphery, forming a ring around the newly formed cell plate. During root knot nematode infection, targeted to the giant cell mini cell plate.
Interaction partners:
- Kinesin-like protein KIN-7A
- Kinesin-like protein KIN-10A
- Kinesin-like protein KIN-12D
- Serine/threonine-protein kinase Aurora-1
- Microtubule-associated protein RP/EB family member 1C
- Kinesin-like protein KIN-12C
- Protein ENDOSPERM DEFECTIVE 1
- Uncharacterized protein family
- At4g28310
- Putative defensin-like protein 270
Sequence:
MASVQKDPILQVETTCGSLLFELQIIWDEVGETETDRDQMLLELERECLEVYRRKVDQANRCRAQLRQAIADAEAQLAAICSAMGERPVHIRQSDQSVGSLKQELGRILPELEEMQKRKVERRNQFIVVMEQIDSITNDIKGQGELVHSEPLIDETNLSMRKLEELHCQLQVLQKEKIDRVETIRKHLCTLYSHCSVLGMDFNEVVGQVNPTLSDPEGPRSLSDHTIEKLGAAVQKLMEVKIQRMQRLQDLATTMLELWNLMDTPIEEQQEYQHITCNIAASEHEITEANSLSEDFIKYVEAEVVRLDEVKASKMKELVLKKRSELEEICRKTHLLPVSDSAIDQTIVAIESGIVDATMVLEHLEQHISKIKEEALSRKEILERVEKWLSACDEESWLEEYNRDDNRYNAGRGAHLTLKRAEKARNLVTKLPGMVEALASKTIVWEQENGIEFLYDGIRLLSMLEEYNILRQEREEEHRRQRDQKKLQGQLIAEQEALYGSKPSPSKPLGGKKAPRMSTGGASNRRLSLGAAMHQTPKPNKKADHRHNDGALSNGRRGLDIAGLPSRKQSMNPSEMLQSPLVRKPFSPISTTVVASKANIATTTTQQLPKNNAVNEISSFATPIKNNNILRNLEEEKMMTMMMQTPKNVAAMIPIPSTPATVSVPMHTAPTPFTNNARLMSEKPEVVEYSFEERRLAFMLQSECRLV
Protein: Duplicated homeodomain-like superfamily protein (MYB transcription factor) (Putative MYB family transcription factor) (Q8GXN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At5g15300
- F-box/kelch-repeat protein SKIP6
- AT5g43460/MWF20_18
- AT4g05070 protein
- Transmembrane protein
- Transmembrane protein
- Secreted transmembrane peptide 5
- AT1G25275 protein
- At3g13845
- Small polypeptide DEVIL 10
Sequence:
MNRGIEVMSPATYLETSNWLFQENRGTKWTAEENKKFENALAFYDKDTPDRWSRVAAMLPGKTVGDVIKQYRELEEDVSDIEAGLIPIPGYASDSFTLDWGGYDGASGNNGFNMNGYYFSAAGGKRGSAARTAEHERKKGVPWTEEEHRQFLMGLKKYGKGDWRNIARNFVTTRTPTQVASHAQKYFIRQVNGGKDKRRSSIHDITTVNIPDSPDAAAADNATANAPCSPPSVGGNQRETSEWEGQTLYDETAAAFYNQNAFSETLLGMSSTPYMAKLQEQSFLNASQFESYNAYLQM