wanglab/gogpt-training-data huggingface dataset:
Protein: Follistatin (FS) (Activin-binding protein) (P47931)
Organism: Mus musculus (Mouse)
Function: Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P19883}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P19883}.
Interaction partners:
- Inhibin beta A chain
- Growth/differentiation factor 8
- Inhibin beta B chain
- Inhibin beta C chain
- Bone morphogenetic protein 7
- Growth/differentiation factor 11
- Inhibin beta E chain
- Bone morphogenetic protein 4
- Bone morphogenetic protein 15
- Chordin
Sequence:
MVCARHQPGGLCLLLLLLCQFMEDRSAQAGNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGKCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPSSSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCGGGKKCLWDSKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSISEETEEEEEEEDQDYSFPISSILEW
Protein: Betaine--homocysteine S-methyltransferase 1 (EC 2.1.1.5) (O35490)
Organism: Mus musculus (Mouse)
Function: Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O09171}. Nucleus {ECO:0000250|UniProtKB:O09171}. Note=Predominantly localized in the cytoplasm with a small fraction detected in the nucleus. Translocates into the nucleus upon oxidative stress. {ECO:0000250|UniProtKB:O09171}.
Interaction partners:
- Dimethylglycine dehydrogenase, mitochondrial
- Cystathionine beta-synthase
- Adenosylhomocysteinase
- S-adenosylmethionine synthase isoform type-1
- Cystathionine gamma-lyase
- S-adenosylmethionine synthase isoform type-2
- Methionine adenosyltransferase 2 subunit beta
- Putative adenosylhomocysteinase 3
- Alpha-aminoadipic semialdehyde dehydrogenase
- S-methylmethionine--homocysteine S-methyltransferase BHMT2
Sequence:
MAPVAGKKAKKGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAAVEHPEAVRQLHREFLRAGSNVMQTFTFYASEDKLENRGNYVAEKISGQKVNEAACDIARQVADEGDALVAGGVSQTPSYLSCKSEVEVKKIFRQQLEVFMKKNVDFLIAEYFEHVEEAVWAVEALKASGKPVAATMCIGPEGDLHGVPPGECAVRLVKAGASIVGVNCHFDPSVSLQTVKLMKEGLEAARLKAYLMSQPLAYHTPDCGKQGFIDLPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCCGFEPYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWIRARARKEYWQNLRIASGRPYNPSMSRPDAWGVTKGAAELMQQKEATTEQQLRELFEKQKFKSAQ
Protein: F-box/SPRY domain-containing protein 1 (F-box synaptic protein 1) (Q18223)
Organism: Caenorhabditis elegans
Function: Component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex which is required for the restriction and/or maturation of synapses in GABAergic neuromuscular junction (NMJ) presynaptic neurons. Promotes NRJ synapse development and synaptic transmission by negatively regulating the daf-2/InsR pathway in muscles. By targeting convertase egl-3 for degradation, negatively modulates insulin-like protein ins-4 and ins-6 processing. May stabilize synapse formation by promoting the down-regulation of scd-2. Regulates axon termination in PLM and ALM neurons.
Subcellular location: Synapse.
Interaction partners:
- E3 ubiquitin-protein ligase rpm-1
- Cullin-1
- Skp1-related protein
- X-linked retinitis pigmentosa GTPase regulator homolog
- mRNA export factor rae-1
- ALK tyrosine kinase receptor homolog scd-2
- Large ribosomal subunit protein uL3m
- Mitogen-activated protein kinase kinase kinase dlk-1
- PHR domain-containing protein
- Probable protein phosphatase 2C T23F11.1
Sequence:
MAENDGETIVPDEQCNLTASTPMKSSGLEQVESPKERKTSMVECDDEGNPSSGTPDESPKQLTPHSIPPRRRRSPRRPEVSASRLPLKVLNQIFQYLPLKDLRSAMLTCHSWNNALSMEDSDIWQYLLGKKLPEAAVSDPFLLAELGSAKKKLRAWYFAWNTSDISRNNYIRTNGFTVHRQPVAQSTDGVRGKRGISKGVHAFDITWDGPLGTVAVVGIATKHAALHCVGYVALLGSDDQSWGWNLVDNVLMHNGAQLGVYPKMNNPPKYEVGDKIRLIIDCDTHVAYFERNSEFLGIAFNHIPPLRLYPAVCAVYGNTEVTMVYVGSPQMG
Protein: Calpain-like cysteine peptidase, putative (Q57XZ8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSSGGLLANGNTSALRTVAVTLPEFNVEDDEMRIVRVTTPLPDLLPRSFEDIERMRKMRQDAESGRKYVAPRVELSPPYVNDDECDEFEDATINTTVEFLSQLKKPGSYLLRGPSVEGKVSNVFEHGMLYKIITSNDAWHFYNDTEKYEMRVRFRFGAKSELQPGDGVEIFAKSNKEIEASLTVYPGETRKLIEGKVNGFKCMAKAVALSNRKRAEFYGPMNGKIQSELEQLAEELHLPSADKLEEEQLLEHCTANQVPYIDCSFRPCDRSLSRPDVDVHNLQSLPWRRPCDYIPKSQLDEVRLFRRSIAPSHVTQGELGDSYFTSAVACLAEMPDKIRDLFRHPVSPSVGKAERRVGAYWVTLNCGGWWRPTVIDDYLPAYREGPEYAHCAVDFRRLWVALLEKAYAKIHHSYSNIASGDPLDPLQDLTGFPITRFDTDWESAVNGDDKLFKRLVMYNKRGYITVLYTPPPAALKAAQPSDTSPTTEARKPRVTCKELGLQAHSGYSVLQVKCFEEMGLFLLQVRNPWSTGEEWKGRWSKSDKLWEEYPSVQSACFPSGMESPKDDNMFWLQWSDALNVFAGGGVCHVRNNWYDYRIRGNFVDGYPTVCLEINVSDPVAAYIVLSQEEECNTADGSQQSAKQQQVQYAALLVSVSRHSGKYEKMECASDVDVEIPGRQLKFNFSRSVALQYTFEPEGGPYFVIPRIHDVNTSKPYVIGLLLDTYAGNGIQVEFKVIHKSCKVFQNMPTFSVKGMLKDVATEYQIRNSRRPTECVASELVDERLKEFDLGE
Protein: Meiotically up-regulated gene 121 protein (Q09688)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MKGFVVISRFILTLFILITPGLAGVVNYAENSEWNVPKYGNVLDSNCQGQKPVTFFGSVTEHVSNSWWIKLYDYMMTFISGEKLCMQNVAYEFEDISLCMDVVGSKCIPTLQSTDIEKVVNSTSAYLENSESDLTLGCFQIQRFQEESTLYIRALKSSEPVSCDTVRCIHFNHIPYV
Protein: Phosphate metabolism protein 8 (P40025)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in phosphate metabolism.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Monoglyceride lipase
- Triacylglycerol lipase 2
- Glycerol-3-phosphate O-acyltransferase 2
- Lysophospholipid acyltransferase
- Triacylglycerol lipase 5
- Triacylglycerol lipase 4
- Putative lipase ATG15
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Triacylglycerol lipase 3
Sequence:
MTIAKDYRTIYRNQIKKQIRLNQEHLQSLTHLGSQINFEVDPPKLPDPDPARKVFFFDIDNTLYRKSTKVQLLMQQSLSNFFKYELGFDDDEAERLIESYYQEYGLSVKGLIKNKQIDDVLQYNTFIDDSLPLQDYLKPDWKLRELLINLKKKKLGKFDKLWLFTNSYKNHAIRCVKILGIADLFDGITYCHYDRPIEEEFICKPDPKFFETAKLQSGLSSFANAWFIDDNESNVRSALSMGMGHVIHLIEDYQYESENIVTKDHKNKQQFSILKDILEIPLIMDVEVYRPSSIAIKEMEELEEEGEAVNWSNQQINVQSS
Protein: Peroxisomal ATPase PEX1 (Peroxin-1) (D3ZZB2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Peroxisomal ATPase PEX6
- Similar to peroxisome biogenesis factor 26.
- Peroxisomal membrane protein PEX13
- Peroxisomal targeting signal 1 receptor
- Peroxisome biogenesis factor 10
- Peroxisomal membrane protein PEX14
- Peroxisome assembly protein 12
- Peroxisomal targeting signal 2 receptor
- PEX5-related protein
- Peroxisomal targeting signal 1 receptor.
Sequence:
MWSSDRLAGAGSGGAVVTVAFTNARDCFLHLPRHLVAQLHLLQNQAIEVTGDHQPTYLSWVEGRHFNDQSENVAEINRQVGQKLGLSSGDQVFLRPCSHVVSCQQVEVEPLSADDWEILELHAISLEEHLLDQIRIVFPKAIVPIWVDQQTYIFIQIVALMPTAPYGRLETNTKLLIQPKTRQAKESTFPKEGDARGQAHNYGREQKGTVKELQTKQLHKNTEAVPVSNGRNPEVPGDSVKPRWWAVLGSMFSFGPDNKQESAWGSLELGAFKNMQSQTVPLDSIFRVCQVQPPSVHNTPANSVFHKHCTVHVFPWDQEYFDVEPSFTVVYGKLVKLHSPKQQQDKSKQGVLLPEKEKQLSQSPGHKRIGSDGSEEAAETCVLKVVWNGLEELKNATEFTKSLEPLHHGKVWIPADLRKRLNIEMHAVVRITPLETTPVIPRALRLQPAENLPRDVSEEEVKAVFSSWLQESATTMFPLIISKQECIKLEIKDGLKEFSLSIVHSQEKEKEQGRTVFVLSPILLQKISVQVLLEPMIGEHSEEIDILLPSLTLSSLGGVSSLSVSAMEHITHSLLGRPLSRQLMALVAGLRNGALLITGGKGSGKSTLAKAICKEAHDALDAHVEMVDCKALRGKRLESIQKALEVAFSEAAWRQPSVILLDDLDLIAGLPSTPEHEHSPEAVQSQRLAHALNNMIKEFVSMGSLVALIATSQLQHSLHPSLVSAQGVHTFQCIQHIQPPDQEQRCEILHSVVKNKLGCDISKSPDLDLKCIAKETEAFVARDFTVLVDRAIHSSLSRQQNPTREGLTLTTADFQKALRGFLPASLRNVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVVARESGMNFISIQGPELLSKYIGASEQAVRDVFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILTVLSKSLPLADDVDLQHVASVTESFTGADLKALLYNAQLEALQGRLLPGGLHDGGSSSDSDLSLSSMVFLNHSSGSDDSAGDGECGLDQSLVSLEMSEILPDESKFNMYRLYFGSSYESELGNGASCDLSSHCLSAPSSMTQDLPATPGKDPLFTQHPVFRTPSQEGSQDLTQEQRDQLRADISIIKGRYQSQSGEDESLNQPGPIKTSFAISQAHLMTALAHTRPSINEDEGKEFAELYENFQNPKKRKNQSGTVFRTGQKVTLA
Protein: Ras-related protein SEC4 (P0CY31)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP-bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with SEC8; it could serve as the attachment site for the SEC8/SEC15 particle (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Rab guanine nucleotide exchange factor SEC2
- Exocyst complex component SEC15
- Rab GDP dissociation inhibitor
- Rab family GTPase
- SNARE-binding exocyst subunit
- Myosin 2
- Probable vacuolar protein sorting-associated protein 16 homolog
- Exocyst complex protein EXO70
- Exocyst subunit
- Exocyst complex component Sec8
Sequence:
MSGKGTSSRAYDMIMKLLLVGDSGVGKSCLLLRFVEDKFNPSFITTIGIDFKIRTIESKGKRIKLQVWDTAGQERFRTITTAYYRGAMGIVLIYDVTDSRSFENVENWFQTVTQHANEDAQIFLVGNKCDDEVNRQVSKEQGQELAAKLNVPFLEASAKSNENVDSIFYELASIIQEKHVEENIGGVGGASGAGGIDVSQNNSGAKNNCC
Protein: Histone H4 [Cleaved into: Osteogenic growth peptide (OGP)] (P62804)
Organism: Rattus norvegicus (Rat)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000269|PubMed:1582415}. Chromosome {ECO:0000269|PubMed:1582415}. Note=Localized to the nucleus when acetylated in step 11 spermatids. {ECO:0000250|UniProtKB:P62806}.; SUBCELLULAR LOCATION: [Osteogenic growth peptide]: Secreted {ECO:0000269|PubMed:1582415}. Note=Osteogenic growth peptide is secreted by a mechanism independent from a hydrophobic signal sequence. The mature peptide may be imported into secretory lysosomes by an ABCA1-related protein. {ECO:0000269|PubMed:1582415}.
Interaction partners:
- Histone H3.1
- Histone H3.3
- Histone H2B
- Histone H3
- Histone H3
- Histone H3
- Similar to H3 histone, family 3B.
- Histone H3
- Histone acetyltransferase type B catalytic subunit
- Similar to centromere protein A
Sequence:
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Protein: Uncharacterized protein (Q38AP3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPEINLDCKAPSRHEVENWLDRIDDITAAVQEILNEDPMEAERKREEREARRREAEARERRDKVKMRYDPRYYSRFENDEFIDTLLKETDGPTCKGKGKNCNKDEALFSRAERVSLDEALRMKEEAAKAVRASDWETAFKLYSNAIGLNVVDASLQVTLHNNRALVQLKLKRYLDAVEDASYVLREEPTNVKALLRRATALRHLRRPLDALRDAEAALQKDVSNQEAADLAQWLRRIKSEHERCAAFQHHYSGDAEQLSNATCDLIAAVKELPNVSEASSEENRENVAEKQGRKRKCMIRVLKAVCRCLKVVQCFHLGAAVLFALRDGMDSLTELILGLLSGSAEERFGVVCAAGAKDMSPEGMVLFASLRLLSLVLVGSEACADELEPSSIHEMANNLTAVLVEAVEGMDKGAARGVNIETCLSLVSGLLQALEGLATRFPNEVHTPCGPVMEKISESVLRGGRPAPQPLYFLCGLLEALLKVEVVAKAMTPTLEKIGVRVVDAALTAGPTLLKEVGLSLAVRVSCTNHTCAKAMSTSSFTCALAQMLPPPKVCASAPLSARAEEGLFALVYNLFLQAESRRDYVKQWCDTMVETGNGKMHFALCAWYVLRDRAQSGGVSTERATVCSKMTGVLSKFSPFDDSLRDAILKDEGTLWSMLDSALSILGGDAVEIYEAEAKRDGLAVDSEGSEAKPSALWEVVEHTTTLLAGFYSKKLLSSVEGLWELERVRALLRVVQLGGDRHAVAVGNAALICSFVPPAGCEHYVALRGVDVLLESLRKVRASLFSLEHEGKNGTPQWCHARAAQKNVAIALSRCCTVESQRERLRELKGFETLHAVLEQQQAS
Protein: Zic family member 6 (Zinc finger protein Zic6) (Q6PWU7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTSLSRFSGCPLSCVNPGESNTEPSVMLPPLAEEHMGHPTGSSLKLCPSQNLRDYHETRASAYVDHSVTHFPDTGYTSHRLEPSPRGIIIGTNLSAAGMPPVTDQLASRPTQHGNIGRYRDLHSYRDGRSHAFFTAYQEQAHGSSDATRDLSSQMMLGLPGDLLSRTHPYGQPVSGPRANSQQLVTQFLEFYKPLNMAMQRGGGDAFLRCSRQNPKHELVCKWSDGQEGTGKPPCARSFGTMYELVTHVTVEHVGGPEHSDYVCHWENCPRDRKPFKAKYKLVNHVRVHTGEKPFPCPFHGCEKVFARSENLKIHKRTHTGEKPFKCEFEGCNRRFANSSDRKKHSHVHSSDKPYTCKVRGCEKCYTHPSSLRKHMKLHCKAYIAKIGEDDEHLVEARSPEVTEHQDTPASTTVTRTMTTPSHETLSPETRNESAVRSRFHHTFENTLDYTAHRPQSLLDPLLLQRGSYRPESAQYSCNQPSHTFAPSHRTFAPNSPFQKSLVNGWYTCHSAVDTFSPKHCNSDL
Protein: T-lymphocyte surface antigen Ly-9 (Cell surface molecule Ly-9) (Lymphocyte antigen 9) (SLAM family member 3) (SLAMF3) (Signaling lymphocytic activation molecule 3) (CD antigen CD229) (Q9HBG7)
Organism: Homo sapiens (Human)
Function: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. May participate in adhesion reactions between T lymphocytes and accessory cells by homophilic interaction. Promotes T-cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A. Promotes recruitment of RORC to the IL-17 promoter. May be involved in the maintenance of peripheral cell tolerance by serving as a negative regulator of the immune response. May disable autoantibody responses and inhibit IFN-gamma secretion by CD4(+) T-cells. May negatively regulate the size of thymic innate CD8(+) T-cells and the development of invariant natural killer T (iNKT) cells (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000305}.
Interaction partners:
- SH2 domain-containing protein 1A
- CD48 antigen
- SH2 domain-containing protein 1B
- T-cell surface antigen CD2
- SLAM family member 6
- Signaling lymphocytic activation molecule
Sequence:
MVAPKSHTDDWAPGPFSSKPQRSQLQIFSSVLQTSLLFLLMGLRASGKDSAPTVVSGILGGSVTLPLNISVDTEIENVIWIGPKNALAFARPKENVTIMVKSYLGRLDITKWSYSLCISNLTLNDAGSYKAQINQRNFEVTTEEEFTLFVYEQLQEPQVTMKSVKVSENFSCNITLMCSVKGAEKSVLYSWTPREPHASESNGGSILTVSRTPCDPDLPYICTAQNPVSQRSSLPVHVGQFCTDPGASRGGTTGETVVGVLGEPVTLPLALPACRDTEKVVWLFNTSIISKEREEAATADPLIKSRDPYKNRVWVSSQDCSLKISQLKIEDAGPYHAYVCSEASSVTSMTHVTLLIYRRLRKPKITWSLRHSEDGICRISLTCSVEDGGNTVMYTWTPLQKEAVVSQGESHLNVSWRSSENHPNLTCTASNPVSRSSHQFLSENICSGPERNTKLWIGLFLMVCLLCVGIFSWCIWKRKGRCSVPAFCSSQAEAPADTPEPTAGHTLYSVLSQGYEKLDTPLRPARQQPTPTSDSSSDSNLTTEEDEDRPEVHKPISGRYEVFDQVTQEGAGHDPAPEGQADYDPVTPYVTEVESVVGENTMYAQVFNLQGKTPVSQKEESSATIYCSIRKPQVVPPPQQNDLEIPESPTYENFT
Protein: Proline-rich transmembrane protein 1 (Dispanin subfamily D member 1) (DSPD1) (Synapse differentiation-induced protein 4) (SynDIG4) (Q99946)
Organism: Homo sapiens (Human)
Function: Required to maintain a pool of extrasynaptic AMPA-regulated glutamate receptors (AMPAR) which is necessary for synapse development and function. Regulates basal AMPAR function and synaptic transmission during development but is dispensable at mature hippocampal synapses. Plays a role in regulating basal phosphorylation levels of glutamate receptor GRIA1 and promotes GRIA1 and GRIA2 cell surface expression.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q6MG82}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6MG82}. Synapse {ECO:0000250|UniProtKB:Q6MG82}.
Interaction partners:
- Decapping and exoribonuclease protein
Sequence:
MSSEKSGLPDSVPHTSPPPYNAPQPPAEPPAPPPQAAPSSHHHHHHHYHQSGTATLPRLGAGGLASSAATAQRGPSSSATLPRPPHHAPPGPAAGAPPPGCATLPRMPPDPYLQETRFEGPLPPPPPAAAAPPPPAPAQTAQAPGFVVPTHAGTVGTLPLGGYVAPGYPLQLQPCTAYVPVYPVGTPYAGGTPGGTGVTSTLPPPPQGPGLALLEPRRPPHDYMPIAVLTTICCFWPTGIIAIFKAVQVRTALARGDMVSAEIASREARNFSFISLAVGIAAMVLCTILTVVIIIAAQHHENYWDP
Protein: Potassium voltage-gated channel subfamily D member 1 (D3ZYK3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- A-type potassium channel modulatory protein KCNIP1
- A-type voltage-gated potassium channel KCND3
- A-type potassium channel modulatory protein DPP6
- Calsenilin
- A-type potassium channel modulatory protein KCNIP2
- Kv channel-interacting protein 4
- Voltage-gated potassium channel subunit beta-1
- Voltage-gated potassium channel subunit beta-2
- Inactive dipeptidyl peptidase 10
- Ubiquitin-like protein FUBI
Sequence:
MAAGVATWLPFARAAAVGWLPLAQQPLPPAPEVKASRGDEVLVVNVSGRRFETWKNTLDRYPDTLLGSSEKEFFYDAESGEYFFDRDPDMFRHVLNFYRTGRLHCPRQECIQAFDEELAFYGLVPELVGDCCLEEYRDRKKENAERLAEDEEAEQAGEGPALPAGSSLRQRLWRAFENPHTSTAALVFYYVTGFFIAVSVIANVVETIPCRGPARWPTKEQPCGDRFPTAFFCMDTACVLIFTGEYLLRLFAAPSRCRFLRSVMSLIDVVAILPYYIGLFVPKNDDVSGAFVTLRVFRVFRIFKFSRHSQGLRILGYTLKSCASELGFLLFSLTMAIIIFATVMFYAEKGTSKTNFTSIPAAFWYTIVTMTTLGYGDMVPSTIAGKIFGSICSLSGVLVIALPVPVIVSNFSRIYHQNQRADKRRAQQKVRLARIRLAKSGTTNAFLQYKQNGGLEDSGSGEGQMLCVRSRSAFEQQHHHLLHCLEKTTCHEFTDELTFSEALGAVSLGGRTSRSTSVSSQPMGPGSLFSSCCSRRGERRAIRLANSTASVSRGSMQELDTLAGLRRSPAPQSRSSLNAKPHDSLDLNCESRDFVAAIISIPTPPANTPDESQPSSPGGGGSGGMANTTLRNSSLATPCLLPETVKISSL
Protein: COP9 signalosome complex subunit 5 (Signalosome subunit 5) (EC 3.4.-.-) (Q54PF3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of E3 ligasew complexes, leading to modify the Ubl ligase activity. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. Csn5 is essential for growth or survival.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 7
- Cullin-4
- Ubiquitin-like protein NEDD8
- DNA damage-binding protein 1
Sequence:
MSKNGAADALKTFELENNIQTIDHDQLFKYDPQQYQQFLQSKPWSKDPHYFKHVKISAIALLKMVMHARSGGKLEVMGMLMGKVENNTMIIMDSFALPVEGTETRVNAQVEAYEYMVEYLELIKQTGRLENALGWYHSHPGYGCWLSGIDVGTQSVNQQYSEPWLGIVIDPTRTVSAGKVEIGAFRTYPQGYKPPNEGPSEYQSIPLSKIEDFGVHCKQYYSLEITYFKSSLDQQLLDKLWNKYWVNTLSSSPIFSNRDYITGQINDLSEKLEQAETQLSHSRSSILDKKKEESLLSKVSKDSSKVTIEQVQGIMSQVFKNSIFNECQTTKQ
Protein: Ubiquitin carboxyl-terminal hydrolase, putative (EC 3.1.2.15) (Q381Y9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase
- Polyubiquitin, putative
Sequence:
MASVLPSAPPGSAVISSKRRSRRGAQRLAGKQPDVKHIGVSQTVIDRLDLMSLHQELLETFSTFDVQGGMRRKGQRGSFASKFNHVPIAKGIVNRTNSCFMNAMLQAIIFTPPLAQLIISASDSELCPTLSALGKWMLSYWTKPANQSISPPQLSVAQSANEGVASTYLLLARMNGYAQEDALEFLQHLLDTINTELCSLEKHYCNRAAIDSGDEKGWTFVHGRERRSLREEKTGPHSILLDAVFGGTIQSHLKGKSRVRSHASVVLDRFFVLQVDVGFNAECTLEEALERTLQTEKVYDDSRAKDLVKTMKLHQLPLVLFAQLRRWAVTAEGELVKLDNIVRFGKTLVLPKSICSDETLSGTARTYQLVAFVAHRGSATGCGHYVTYIVNASLPENARSNSLVTGGEEVLTLCNDVRISHVTMREAIEGEAAYLLVYQRKT
Protein: Protein EARLY STARVATION 1, chloroplastic (OsESV1) (Q8H8C6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Binds preferentially to highly ordered alpha-glucans, such as starch and crystalline maltodextrins (By similarity). Involved in the organization of the starch granule matrix, thus influencing starch turnover by modulating the accessibility of starch polymers to modifying and degrading enzymes. Required for the control of starch degradation in leaves and starch distribution in nonphotosynthetic parts. Promotes gravitropic responses, negative in shoots but positive in roots, by facilitating starch granules (statoliths) formation in hypocotyls and roots columella. Facilitates tight packing of starch granules in grains.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250|UniProtKB:F4I9G2}. Note=Binds to starch granules in chloroplasts. {ECO:0000250|UniProtKB:F4I9G2}.
Interaction partners:
Sequence:
MAACSRGLVARPFDLTARGAAHWPCPAPRRRAIRCCCRAQQEPRRRLSKAAAAAPERTEEWRIDGNKPAAAARGRRRASLTAMPSLPFPSPRSRRQWKQQNFYPRCTPRGPAPQSRDTPPKRDTGIASEKEWGINLLDEAVKESGTNEDGSTWYRESGDDRGDNGYRCRWARMGGQSHDGTTEWKETWWEKSDWTGYKELGAEKSGKNGEGDSWWEKWKEVLYQDEWSNLARIERSAEKQAKSGAENAGWYEKWWEKYDAKGWTEKGAHKYGRLNEQSWWERWGEHYDGRGFVLKWTDKWAETDLGTKWGDKWEEKFFAGIGSRQGETWHVSPGGDRWSRTWGEEHFGNGKVHKYGKSTTGESWDLVVDEETYYEAEPHYGWADVVGDSTQLLSIQPVERPPGVYPTIDFSASSPAPPSDDPPGMPPSPLE
Protein: UPF0225 protein YchJ (P37052)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YecA
- Formyltetrahydrofolate deformylase
- Uncharacterized protein YcfL
Sequence:
MSQLCPCGSAVEYSLCCHPYVSGEKVAPDPEHLMRSRYCAFVMQDADYLIKTWHPSCGAAALRAELMAGFAHTEWLGLTVFEHCWQDADNIGFVSFVARFTEGGKTGAIIERSRFLKENGQWYYIDGTRPQFGRNDPCPCGSGKKFKKCCGQ
Protein: Inactive carboxylesterase-like protein VdtD (Viriditoxin biosynthesis cluster protein D) (A0A443HK52)
Organism: Byssochlamys spectabilis (Paecilomyces variotii)
Function: Inactive carboxylesterase-like protein; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity. The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-CoA units to form the heptaketide monomer backbone of viriditoxin. The product of VdtA is then O-methylated on C7 by the O-methyltransferase VdtC. The O-methyl group is important for the stereoselective coupling of the monomers at the final step of viriditoxin biosynthesis. The short-chain dehydrogenase/reductase VdtF then acts as a stereospecific reductase converting the pyrone to dihydropyrone via the reduction of the C3-C4 double bond. The FAD-binding monooxygenase VdtE then converts the ketone group into a methyl-ester group to yield semi-viriditoxin. Finally, the laccase VdtB is involved in dimerization of 2 semi-viriditoxin molecules to yield the final viriditoxin. VdtB is responsible for the regioselective 6,6'-coupling of semi-viriditoxin, which yields (M)-viriditoxin and (P)-viriditoxin at a ratio of 1:2. The non-catalytic carboxylesterase-like protein VdtD affects the stereochemistical outcome of the coupling. The highly reducing polyketide synthase VdtX is not involved in viriditoxin synthesis, but might possibly play a role in the production of additional metabolites not identified yet.
Interaction partners:
- Glycerophosphoryl diester phosphodiesterase family-domain-containing protein
- Nitrate reductase
Sequence:
MFMTQIVFGIAPTLLKTFSHLTALDLWRPSAPYVFDPVTSSTYLGTIADGVEEFLGIFYGQDTGGSNRFAPPKPYIPSRHSFINASTAGAACPQPYVPLPADPYTVLTNVSEDCLSLRIARPENTKSTAKLPVMVWLYGGGASVGTAYDVSYNPVGLIQQSVVNGSPVIYVAINYRVNLFGHAFSDALLKSKSTNLAMQDQRLGIEWIKNHISAFGGDPDNITLFGEDEGATYIALHILSNHEVPFHRAILQSGAAITHHDVNGNRSARNFAAVAARCNCLSDGDRQVDSQDTVDCLRRVPMEDLVNATFEVAHSVDPVNGFRAFMPAVDGYMIPDEPSNLLSRGQVPANISILAGWTRDESSMSVPTSIRTAADAASFISTQFPLLNASTIHHFLTSLYPESDFTTNSPSSPEKVTPAWRATSALHRDLTLTCPTIFQAWSLRLSSNCTTPVYLYELRQSPFATALNNSGVGYLGIVHFSDVPYVFNELERTYYITDPEENKLAQRMSASWTAFASGAFPLCERSERSLGRWEEAYGGDRVCRDRMPEHVRVKGIGDNGDQDDGDEIGKLMARCGFINRLEY
Protein: Spindle assembly abnormal protein (Q9LJ94)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSAPIYSPIDMQEIVQNPPGFDTEPVPISTYRDNEPVPLSTYRENDSDHLDATQQENDDFWENGFSREEAIEDPEPSQAKENGKRSVDNSAFTHGETDLNQLPAIPPVSTGQGLPYAPVDWPSPGDVWTWRVGRRVTAMGYHQDRFLILPQRLQQKHVPKSFASKPQLARYLESDFPGMDADAFFASFSWKVPALFQPANKVDAASLFEETPKEVQTEVGQNDENAQDGKGNSRYSQRKRKPMPTPQTYEPVEAKPKSTPRGSSNKKKKGATTPATGPQSSTKPKPSRQSGRRTSIQQRGGAVDLNFLNEEESEPATAPKTSNKRKKRGVNYEEEDVSIPHIYVSPMNGVLAVSHSPIDVNPEEFDSYLNSLDNLMQQPPEEVGRDSSVLVSVSSPMREYEWAEARMKISSLLEKDFTTLFLSKDAAEIAALATKLRKDPNLTAEEIVRLKLMEEIPTFSEVFQENKGVIEEADRFFSALELNKAKVASLKYEYSDLKEKLGSIQMEVDTNSETIRQIDDQIAQLQARRSELKRYIGTKEKERVDLSYGQKMVANSIPKVVQEVQSANLKKPEWECKKDNALKREAEILSKFTPLKGFFL