wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit (GPI-GlcNAc transferase complex subunit ERI1) (GPI-GnT subunit ERI1) (Endoplasmic reticulum-associated Ras inhibitor protein 1) (P62651)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable component of the GPI-GlcNAc transferase (GPI-GnT) complex in the endoplasmic reticulum, a complex that catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI-anchors for cell surface proteins. Ras may inhibit the enzyme activity of the GPI-GnT complex via the association between ERI1 and RAS2.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12832483}; Multi-pass membrane protein {ECO:0000269|PubMed:12832483}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- ERMES regulator 1
Sequence:
MRPRDQGFLVLGFTYSVLLISLATFYWLRNNDSFLHYWCVLLLCPATLWLWALIAWCDSEMFASSKDE
Protein: ETS-related transcription factor Elf-3 (E74-like factor 3) (Epithelial-restricted with serine box) (Epithelium-restricted Ets protein ESX) (Epithelium-specific Ets transcription factor 1) (ESE-1) (P78545)
Organism: Homo sapiens (Human)
Function: Transcriptional activator that binds and transactivates ETS sequences containing the consensus nucleotide core sequence GGA[AT]. Acts synergistically with POU2F3 to transactivate the SPRR2A promoter and with RUNX1 to transactivate the ANGPT1 promoter. Also transactivates collagenase, CCL20, CLND7, FLG, KRT8, NOS2, PTGS2, SPRR2B, TGFBR2 and TGM3 promoters. Represses KRT4 promoter activity. Involved in mediating vascular inflammation. May play an important role in epithelial cell differentiation and tumorigenesis. May be a critical downstream effector of the ERBB2 signaling pathway. May be associated with mammary gland development and involution. Plays an important role in the regulation of transcription with TATA-less promoters in preimplantation embryos, which is essential in preimplantation development (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10391676, ECO:0000269|PubMed:15169914, ECO:0000269|PubMed:17060315}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237, ECO:0000269|PubMed:10391676, ECO:0000269|PubMed:15169914, ECO:0000269|PubMed:17060315}. Note=Localizes to the cytoplasm where it has been shown to transform MCF-12A mammary epithelial cells via a novel cytoplasmic mechanism. Also transiently expressed and localized to the nucleus where it induces apoptosis in non-transformed breast epithelial cells MCF-10A and MCF-12A via a transcription-dependent mechanism. {ECO:0000269|PubMed:10391676, ECO:0000269|PubMed:15169914, ECO:0000269|PubMed:17060315}.
Interaction partners:
- ETS-related transcription factor Elf-4
- Mediator of RNA polymerase II transcription subunit 23
- Protein kinase C iota type
- Small proline-rich protein 2A
- Homeobox protein ESX1
- POU domain, class 2, transcription factor 3
- Histone acetyltransferase p300
- TATA-box-binding protein
Sequence:
MAATCEISNIFSNYFSAMYSSEDSTLASVPPAATFGADDLVLTLSNPQMSLEGTEKASWLGEQPQFWSKTQVLDWISYQVEKNKYDASAIDFSRCDMDGATLCNCALEELRLVFGPLGDQLHAQLRDLTSSSSDELSWIIELLEKDGMAFQEALDPGPFDQGSPFAQELLDDGQQASPYHPGSCGAGAPSPGSSDVSTAGTGASRSSHSSDSGGSDVDLDPTDGKLFPSDGFRDCKKGDPKHGKRKRGRPRKLSKEYWDCLEGKKSKHAPRGTHLWEFIRDILIHPELNEGLMKWENRHEGVFKFLRSEAVAQLWGQKKKNSNMTYEKLSRAMRYYYKREILERVDGRRLVYKFGKNSSGWKEEEVLQSRN
Protein: Probable nitrilase C965.09 (EC 3.5.-.-) (O59829)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MKANIACVQMAPKVCDVKHNLQKMSSYVHEVMESNPSTNLILFPELITSGYECGNTFTQIAEIAGEGPSFKTMSNLAAKYHVNIIYGFPEKEEKQSNIIYNSCIYITENGNLGGVYRKVHLFDTERKHFKKGSDFPIFETSFGKLGVMICWDTAFPEVARIHALNGADLLVVATNWENPYSDDWDLVTKARAFENCIPLVAANRVGTDEKLSFFGHSKIIGPTGKVIKALDEEKEGVISYTVDLDDAKPLRKNYYTFFEDRMPDLYKRLLSP
Protein: Low-density lipoprotein receptor-related protein 8 (LRP-8) (Apolipoprotein E receptor 2) (Protein LR8B) (Q98931)
Organism: Gallus gallus (Chicken)
Function: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. Also binds alpha2-macroglobulin. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q14114}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Transcobalamin 2.
- Reelin
- DAB1, reelin adaptor protein
- Apolipoprotein B
Sequence:
MCRPALARLLLLQLLLLKLYLGKGAMKECDKDQFQCRNERCIPAVWACDEDNDCSDNSDEADCPKKTCAETDFACDNGHCIPDRWKCDGEEECSDGSDESEAACTKQVCPAEKISCGDLSNKCIPSSWRCDGQKDCESGIDEAGCAPACSPDEFQCSNKTCISINFVCDGYNNCGDGSDEKKCSPLTCSPNEFQCNNSVCIPQLWVCDNQADCEDHSDESIERCGYDAKAFNTCAAHEFQCGNGECILLNWKCDGDEDCKDKSDEQDCPLVTCRPDEFQCGDGTCIHGAKQCDKVHDCPDNSDEAGCVQESACESPSKFQCKSGECIDGGKVCDLHRDCRDWSDEPLKECGINECSLNNGGCSHICKDLKIGYECECPPGYKLLDKKTCGDIDECENPDACSQICINYKGDYKCECYEGYEMDTLSKNCKAVGKSPYLIFTNRHEVRKIDLVKRDYSRIIPMLKNVVALDVEVATNRIYWCDLFYRKIYSAYIDKASDTAEQVILIDSQLNSPEGVAIDWVHKNIYWTDSGNKTISVATADGSRRRTVFNSDLSEPRAIAVDPTRRFMYWSDWGDKAKIEKAGLNGVGRQVLVSDNIEWPNGITLDLLNQRLYWVDSKLHSLSCIDFNGSNREVLISSIDDLSHPFGLAVFEDRVFWTDLENEAIFSANRLSGLDISVLAENLNNPHDIVVFHELKQPKAPDSCELSPQPNGGCEYLCLPAPHISPRSPKFTCACPDNMWLGPDMKKCYKELPTTPATVEVPTTTTSHPAATSTVTVTGSANTTTAVIPRAVSEATTAIPSSHSTTSLLIDSEMTTGNSNLSQHYSNNGQGFDSTVTAAVIGIVIPVVVIGLLCMGGYLIWRNWKRKNTKSMNFDNPVYRKTTEEEDEDEIHIGRTAQIGHVYPARVALSLEDDGLP
Protein: CRP-like protein Clp (Catabolite activation-like protein) (CAP-like) (Q8PQ45)
Organism: Xanthomonas axonopodis pv. citri (strain 306)
Function: Global transcriptional regulator that regulates virulence factors production by activating or repressing the expression of a large set of genes in diffusible signal factor (DSF) pathway.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MSPGNTTVVTTTVRNATPSLALDAGTIERFLAHSHRRRYPTRTDVFRPGDPAGTLYYVISGSVSIIAEEDDDRELVLGYFGSGEFVGEMGLFIESDTREVILRTRTQCELAEISYERLQQLFQTSLSPDAPKILYAIGVQLSKRLLDTTRKASRLAFLDVTDRIVRTLHDLAKEPEAMSHPQGTQLRVSRQELARLVGCSREMAGRVLKKLQADGLLHARGKTVVLYGTR
Protein: Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial (Glu-AdT subunit A) (EC 6.3.5.7) (O94509)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Subcellular location: Mitochondrion.
Interaction partners:
- Glutamyl-tRNA
- Asparagine--tRNA ligase, mitochondrial
- Probable glutamine--tRNA ligase
- Probable asparagine--tRNA ligase, cytoplasmic
- tRNA nucleotidyltransferase cca1
- Chromatin assembly factor 1 subunit A
- Aspartate--tRNA ligase, cytoplasmic
- Serine/threonine-protein kinase rio2
- Glutamate--tRNA ligase, mitochondrial
- Uncharacterized protein C777.11
Sequence:
MSNKYNNLLKEVAAKYASIILNDAKIKSLTSINSAEYLYDSFVEISKLPLEKKLPLKWKLITVKENICTKTNLTTAASNMLKDYNSPFDASIVESLKKAGGIILGKTNMDEFAMGVKSENNLFGRTVNPVVKDSNYDVGGSSGGAAAAIAADICYASVGSDTGGSIRLPAAYVGCVGFKPSFGRISRYGMLAFANSFDTVGIAANNVKGVTKVFNVLDHPDINDSTCLTKEARYFVKEQHKKLSRKPIKIGIPIDWNVSETHPNVLDKWNEFISLLKSNGYLVQEIQLPISLYANSVYSTMAYAEATSNLAKYNTIAFGNCLDEKFEEEIISSTARSFFLGDEVKKRLLLGAYSLARMNSSDLFSKARYVRRAIQLEFNKNFFLPSFSVDDPRGDIDFIVTPSFFNSSQPIETPSSYSHLSDTMLVPANMAGIPSVSIPFGTLNNGLPMGIQIMAQYLNDEDLLSFAGQFA
Protein: Tyrosine-protein kinase YwqD (EC 2.7.10.2) (P96716)
Organism: Bacillus subtilis (strain 168)
Function: May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB.
Interaction partners:
- Probable capsular polysaccharide biosynthesis protein YwqC
- Tyrosine-protein phosphatase YwqE
- Uncharacterized protein YveK
- Low molecular weight protein-tyrosine-phosphatase YfkJ
- HTH-type transcriptional repressor FatR
- UDP-glucose 6-dehydrogenase YwqF
- Serine/threonine-protein kinase YabT
- Protein-arginine-phosphatase
- UDP-glucose 6-dehydrogenase TuaD
- Iron-sulfur cluster carrier protein
Sequence:
MALRKNRGSRMQRNVIAMTEPKSLNSEQYRTIRTNIEFASVDRQMKSVMITSACPGEGKSTTAANLAVVFAQQGKKVLLIDADLRKPTVHTAFFLENTVGLTSVLLKKSSMEQAVQASNEKHLDVLTSGPIPPNPAELLSSKWMKELAYEACAAYDMVIFDTPPILAVADAQILGNVADGSVLVISSGKTEKEQAAKAKEALATCKSKLLGAIMNGKKLSKHSEYGYYGTKDNFMQK
Protein: Coatomer subunit beta' (Beta'-coat protein) (Beta'-COP) (O62621)
Organism: Drosophila melanogaster (Fruit fly)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit epsilon
- Coatomer subunit delta
- Coatomer subunit alpha
- Coatomer subunit zeta
- Coatomer subunit beta
- Coatomer subunit gamma
- ADP-ribosylation factor GTPase activating protein 3, isoform H
- Protein transport protein Sec31A
- Bifunctional glutamate/proline--tRNA ligase
- Alpha-mannosidase 2
Sequence:
MPLKLDIKRRLTSRSDRVKCVDLHPAEPWMLCALYNGHVHIMNYENQQMVKDFEVCDVPVRSARFVARKNWILTGSDDMQIRVFNYNTLEKVHSFEAHSDYLRCIAVHPTQPLVLTSSDDMLIKLWNWEKMWACQRVFEGHTHYVMQIVFNPKDNNTFASASLDRTVKVWQLGSNFANFTLEGHEKGVNCVDYYHGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNISAVCFHPELPIVLTGSEDGTVRIWHSGTYRLETCLNYGFERVWTISSMRGTNNVALGYDEGSIIIKVGREEPAMSMDVVGSKIIWAKHSEMQQVNLKTIADGTEIKDGERLPVATKDMGACEIYPQTIAHNPNGRFVVVCGDGEYIIYTSMALRNKAFGSAQEFVWALESNEYAIRENNGTVRLFRNFKERKSFTPEYGAESIYGGYYFGVKTSSGLAFYDWETLQLVRRIEVQPKNVFWNESGSLVCLATDDSYFVLGVDTAQVANAVETKEGLEDDGVESAFNVLGEVSECVKTGLWVGDCFIYTNSVNRINYYVGGEIVTVSHLDRTMYLLGYVPKDNRIYLGDKELNVISFCLQLSVLEYQTAVMRRDFERADVVLPTIPKEHRTRVAHFLEKQGFKSQALQVSTDADHKFDLALQIGDLEIALKLARESENSQKWSQLADVASSKNNMSLVKECMQKANDLSGLLLLSTASGDAQLLEVVGAAGSAQGHHNLAFLSAFLRSDVERCLEILIETNRLPEAAFFARTYLPSQMSRIVELWREKLGKVNEKAGQSLADPAQYTNLFPGLGDALRVEQHLQEERARKAPARLAANLPLNSERHPLQELFAAEQGAAGQHLEEKVKPAYVPAQAVVSSSQVAEPTSAADDDDDLDLEIDGITLDDNIDTTDVNLDDDFLSDD
Protein: Dihydroxyacetone phosphate acyltransferase (DAP-AT) (DAPAT) (DHAP-AT) (EC 2.3.1.42) (Acyl-CoA:dihydroxyacetonephosphateacyltransferase) (Glycerone-phosphate O-acyltransferase) (O15228)
Organism: Homo sapiens (Human)
Function: Dihydroxyacetonephosphate acyltransferase involved in plasmalogen biosynthesis.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:15687349}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9ES71}; Matrix side {ECO:0000250|UniProtKB:Q9ES71}. Note=Exclusively localized to the lumenal side of the peroxisomal membrane. {ECO:0000250|UniProtKB:Q9ES71}.
Interaction partners:
- Alkyldihydroxyacetonephosphate synthase, peroxisomal
- Fatty acyl-CoA reductase 1
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase 1-like protein
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Peroxisomal targeting signal 1 receptor
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
Sequence:
MESSSSSNSYFSVGPTSPSAVVLLYSKELKKWDEFEDILEERRHVSDLKFAMKCYTPLVYKGITPCKPIDIKCSVLNSEEIHYVIKQLSKESLQSVDVLREEVSEILDEMSHKLRLGAIRFCAFTLSKVFKQIFSKVCVNEEGIQKLQRAIQEHPVVLLPSHRSYIDFLMLSFLLYNYDLPVPVIAAGMDFLGMKMVGELLRMSGAFFMRRTFGGNKLYWAVFSEYVKTMLRNGYAPVEFFLEGTRSRSAKTLTPKFGLLNIVMEPFFKREVFDTYLVPISISYDKILEETLYVYELLGVPKPKESTTGLLKARKILSENFGSIHVYFGDPVSLRSLAAGRMSRSSYNLVPRYIPQKQSEDMHAFVTEVAYKMELLQIENMVLSPWTLIVAVLLQNRPSMDFDALVEKTLWLKGLTQAFGGFLIWPDNKPAEEVVPASILLHSNIASLVKDQVILKVDSGDSEVVDGLMLQHITLLMCSAYRNQLLNIFVRPSLVAVALQMTPGFRKEDVYSCFRFLRDVFADEFIFLPGNTLKDFEEGCYLLCKSEAIQVTTKDILVTEKGNTVLEFLVGLFKPFVESYQIICKYLLSEEEDHFSEEQYLAAVRKFTSQLLDQGTSQCYDVLSSDVQKNALAACVRLGVVEKKKINNNCIFNVNEPATTKLEEMLGCKTPIGKPATAKL
Protein: Storkhead-box protein 1 (Winged-helix domain-containing protein) (Q6ZVD7)
Organism: Homo sapiens (Human)
Function: Involved in regulating the levels of reactive oxidative species and reactive nitrogen species and in mitochondrial homeostasis in the placenta. Required for regulation of inner ear epithelial cell proliferation via the AKT signaling pathway (By similarity).
Subcellular location: [Isoform A]: Cytoplasm {ECO:0000269|PubMed:22253775}. Nucleus {ECO:0000269|PubMed:22253775}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:22253775}. Note=In epithelial cells, diffusely expressed in the cytoplasm, particularly in peri-membrane cortical regions (By similarity). Concentrated at centrosomes during metaphase (PubMed:22253775). {ECO:0000250|UniProtKB:B2RQL2, ECO:0000269|PubMed:22253775}.; SUBCELLULAR LOCATION: [Isoform B]: Nucleus.; SUBCELLULAR LOCATION: [Isoform C]: Nucleus, nucleolus.
Interaction partners:
Sequence:
MARPVQLAPGSLALVLCRLEAQKAAGAAEEPGGRAVFRAFRRANARCFWNARLARAASRLAFQGWLRRGVLLVRAPPACLQVLRDAWRRRALRPPRGFRIRAVGDVFPVQMNPITQSQFVPLGEVLCCAISDMNTAQIVVTQESLLERLMKHYPGIAIPSEDILYTTLGTLIKERKIYHTGEGYFIVTPQTYFITNTTTQENKRMLPSDESRLMPASMTYLVSMESCAESAQENAAPISHCQSCQCFRDMHTQDVQEAPVAAEVTRKSHRGLGESVSWVQNGAVSVSAEHHICESTKPLPYTRDKEKGKKFGFSLLWRSLSRKEKPKTEHSSFSAQFPPEEWPVRDEDDLDNIPRDVEHEIIKRINPILTVDNLIKHTVLMQKYEEQKKYNSQGTSTDMLTIGHKYPSKEGVKKRQGLSAKPQGQGHSRRDRHKARNQGSEFQPGSIRLEKHPKLPATQPIPRIKSPNEMVGQKPLGEITTVLGSHLIYKKRISNPFQGLSHRGSTISKGHKIQKTSDLKPSQTGPKEKPFQKPRSLDSSRIFDGKAKEPYAEQPNDKMEAESIYINDPTVKPINDDFRGHLFSHPQQSMLQNDGKCCPFMESMLRYEVYGGENEVIPEVLRKSHSHFDKLGETKQTPHSLPSRGASFSDRTPSACRLVDNTIHQFQNLGLLDYPVGVNPLRQAARQDKDSEELLRKGFVQDAETTSLENEQLSNDDQALYQNEVEDDDGACSSLYLEEDDISENDDLRQMLPGHSQYSFTGGSQGNHLGKQKVIERSLTEYNSTMERVESQVLKRNECYKPTGLHATPGESQEPNLSAESCGLNSGAQFGFNYEEEPSVAKCVQASAPADERIFDYYSARKASFEAEVIQDTIGDTGKKPASWSQSPQNQEMRKHFPQKFQLFNTSHMPVLAQDVQYEHSHLEGTENHSMAGDSGIDSPRTQSLGSNNSVILDGLKRRQNFLQNVEGTKSSQPLTSNSLLPLTPVINV
Protein: Vacuolar H ATPase (Q9XTY9)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}. Vesicle {ECO:0000256|ARBA:ARBA00004373}.
Interaction partners:
- V-type proton ATPase subunit S1
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C
- V-type proton ATPase subunit B 1
- V-type proton ATPase subunit e
- Probable V-type proton ATPase subunit H 2
- Probable V-type proton ATPase subunit F
Sequence:
MKFVLLVSALVAACAASSLEIIAAPASLKFPDADATLKTTLISTLNENILGLSARQVDGFSVSVDMFSRPRALAVVTVIGADNLNLGGKTYSTKSDGVENVGFDQDMALIFGADRENVQVSAGGITGSMLALAAQQEAVDATVIKTKRSTLVKELEAVYQLAAAIKSAGVQMDNNADVFRVSITGLVGITESAQKEEAVADVKAAIEALTASINNAYGGQAVIELLAFEAESGAAEKSTESREIPNHNIQKRDTKSKTPTQLARENLQVTVPVSSDYPAIFAIFLGLVVILVVALIYIVVGMASIDPEKDSIIYRMTTTRMKKD
Protein: Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase) (P21550)
Organism: Mus musculus (Mouse)
Function: Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. Appears to have a function in striated muscle development and regeneration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11229603}. Note=Localized to the Z line. Some colocalization with CKM at M-band (By similarity). {ECO:0000250}.
Interaction partners:
- Phosphoglycerate mutase 2
- Pyruvate kinase PKM
- Glucose-6-phosphate isomerase
- Pyruvate kinase PKLR
- Bisphosphoglycerate mutase
- Phosphoglycerate mutase 1
- Triosephosphate isomerase
- Phosphoenolpyruvate carboxykinase, mitochondrial
- Phosphoenolpyruvate carboxykinase, cytosolic
- Fructose-bisphosphate aldolase A
Sequence:
MAMQKIFAREILDSRGNPTVEVDLHTAKGRFRAAVPSGASTGIYEALELRDGDKARYLGKGVLKAVEHINKTLGPALLEKKLSVVDQEKVDKFMIELDGTENKSKFGANAILGVSLAVCKAGAAEKGVPLYRHIADLAGNPDLVLPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFKEAMRIGAEVYHHLKGVIKAKYGKDATNVGDEGGFAPNILENNEALELLKTAIQAAGYPDKVVIGMDVAASEFYRNGKYDLDFKSPDDPARHISGEKLGELYKNFIQNYPVVSIEDPFDQDDWATWTSFLSGVDIQIVGDDLTVTNPKRIAQAVEKKACNCLLLKVNQIGSVTESIQACKLAQSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEALGDKAVFAGRKFRNPKAK
Protein: Brain-derived neurotrophic factor (proBDNF) (K4MNE5)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU364086}.
Interaction partners:
Sequence:
MTILFLTMVISYFSCMKAAPMKEASVRGHGSLAYPGLRTHGTLESLTGPNAGSRGLTSLADTFEHVIEELLDEDQDIQPSEENKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSTSEWVTAAEKKTAVDMSGATVTVLEKVPVPKGQLKQYFYETKCNPKGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDNKKRVGWRFIRIDTSCVCTLTIKRGR
Protein: Chaperone DnaJ-domain superfamily protein (Q8L763)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Chaperone DnaJ-domain superfamily protein
- At3g13310
- At2g17880
- Eukaryotic LigT
- Heat shock protein DnaJ with tetratricopeptide repeat-containing protein
- Chaperone DnaJ-domain superfamily protein
- Chaperone DnaJ-domain superfamily protein
- AT4g39960/T5J17_130
- Heat shock protein DnaJ with tetratricopeptide repeat-containing protein
- Chaperone protein dnaJ C76, chloroplastic
Sequence:
MFRLRSLLSLKSSSIVELSSQNVTEAIRFAPFHSTSVLSEKSRSRFGSARDSEGERSSKNSSIRFTCTVKEKGRTSAKKTVDKLLFHRGINDPLQNEWHFGPSPLIRDRHMKKKSPPGRGKKPRDKKTKRWHREGNPDDDFGTDANNTFENKWRERWTAQSQKASYSKDSTAGFEWREGWSWTTQSQRSKSWNKESFDEPLNVEFRSERIVLGLPLDGPIKVDDVKNAFRSSALKWHPDKHQGPSQVAAQEKFKLCVDAYKSLCSALA
Protein: Severin (P10733)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Severin blocks the ends of F-actin and causes the fragmentation and depolymerization of actin filaments in a Ca(2+) dependent manner.
Interaction partners:
- Leucine-rich repeat protein lrrA
- Cofilin-1A
- Profilin-1
- Profilin-2
- Gelation factor
- Profilin-3
Sequence:
MIKNRKLDITSTNVAGIGTDLDKKCRLDAASTEAQWKGVGQAPGLKIWRIENFKVVPVPESSYGKFYDGDSYIILHTFKEGNSLKHDIHFFLGTFTTQDEAGTAAYKTVELDDFLGGAPIQYRQCQSYESPSFLSLFPKYFILSGGVESGFNHVKPTEYKPRLLHISGDKNAKVAEVPLATSSLNSGDCFLLDAGLTIYQFNGSKSSPQEKNKAAEVARAIDAERKGLPKVEVFCETDSDIPAEFWKLLGGKGAIAAKHETAPTKSEKVLYKLSDASGSLKFSEVSRGKINKSSLKSEDVFIIDLGNEIYTWIGSKSSPNEKKTAFSHATQYLVNNKRCEYTPIVRVLENGTNQSFETLLSA
Protein: Lissencephaly-1 homolog (DLis-1) (Dlis1) (Lissencephaly1) (Q7KNS3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as nuclear migration during cell division, mitotic spindle formation and the removal of mitotic checkpoint proteins from kinetochores at the metaphase to anaphase transition. Required for several aspects of neurogenesis including neuroblast proliferation, neuronal cell differentiation, dendritic growth, branching and maturation and axonal transport. Required for synchronized cell divisions in the germline, fusome integrity and oocyte differentiation. Acts together with BicD, Egl, dynein and microtubules to determine oocyte identity during oogenesis. Also required for nurse cell to oocyte transport during oocyte growth and for the positioning of the nucleus in the oocyte.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle pole. Chromosome, centromere, kinetochore. Note=Localizes to the plus end of microtubules. Also localizes to the mitotic spindle poles from late prophase through to telophase and to kinetochore microtubules in metaphase. Localization to kinetochore microtubules is reduced in anaphase and telophase. In oocytes, it concentrates in the cortex from stage 5 of oogenesis.
Interaction partners:
- Platelet-activating factor acetylhydrolase IB subunit beta homolog
- Nuclear distribution protein nudE homolog
- Dynein heavy chain, cytoplasmic
- GXIVsPLA2, isoform A
- phospholipase A2
- phospholipase A2
- Lysophosphatidylcholine acyltransferase
- Phospholipase A2
- Phospholipase A2
- Phospholipase A2
Sequence:
MKMVLSQRQREELNQAIADYLGSNGYADSLETFRKEADLSTEVEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKFSLTGHRASITRVIFHPIFALMVSASEDATIRIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECIKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDQTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKTIRIWDVSVGLCLLTLSGHDNWVRGLAFHPGGKYLVSASDDKTIRVWDLRNKRCMKTLYAHQHFCTSIDFHKAHPYVISGSVDQTVKVWECR