wanglab/gogpt-training-data huggingface dataset:
Protein: Endonuclease 5 (AtENDO5) (EC 3.1.30.1) (Deoxyribonuclease ENDO5) (Single-stranded-nucleate endonuclease ENDO5) (F4JJL3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes, with low efficiency, only single-stranded DNA and RNA without apparent specificity for bases. Endonuclease that recognizes and cleaves some mismatches with high efficiency, including heteroduplex double-stranded DNA; mostly efficient on T/G, A/G and G/G mismatches, less efficient for T/T and poorly efficient for C/C, A/A, T/C and A/C.
Interaction partners:
- GDSL esterase/lipase At3g50400
- Staphylococcal-like nuclease CAN2
- Staphylococcal-like nuclease CAN1
- Formin-like protein 2
Sequence:
MRLWIVSVLVLTHLVHGALCWGKDGHYTVCKLAEGFFEDDTIAAVKKLLPESVDGGGLADFCSWPDEIKKLSQWQWTSTLHYVNTPEYRCNYEYCRDCHDTHKHKDWCVTGAIFNYTNQLMSASENSQNIVHYNLTEALLFLSHYMGDVHQPLHTGFLGDLGGNTIIVNWYHNKSNLHHVWDNMIIDSALETYYNSSLPHMIQALQAKLKNGWSNDVPSWKSCHFHQKACPNLYASESIDLACKYAYRNATPGTTLGDEYFLSRLPVVEKRLAQGGIRLAATLNRIFSAKPKLAGL
Protein: ADP-polyphosphate phosphotransferase 1 (EC 2.7.4.-) (Polyphosphate kinase PPK2 1) (Q92SA6)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Function: Uses inorganic polyphosphate (polyP) as a donor to convert ADP to ATP. Can also convert GDP to GTP, with lower efficiency. Cannot dephosphorylate ATP in the presence of polyP.
Interaction partners:
Sequence:
MALDEAPAEARPGSRAVELEIDGRSRIFDIDDPDLPKWIDEEAFRSDDYPYKKKLDREEYEETLTKLQIELVKVQFWMQATGKRVMAVFEGRDAAGKGGAIHATTANMNPRSARVVALTKPTETERGQWYFQRYVATFPTAGEFVLFDRSWYNRAGVEPVMGFCTPDQYEQFLKEAPRFEEMIANEGIHLFKFWINIGREMQLKRFHDRRHDPLKIWKLSPMDIAALSKWDDYTGKRDRMLKETHTEHGPWAVIRGNDKRRSRINVIRHMLTKLDYDGKDEAAIGEVDEKILGSGPGFLR
Protein: Integral membrane protein 2A (Protein E25) (Q61500)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVKIAFNTPTAVQKEEARQDVEALVSRTVRAQILTGKELRVVPQEKDGSSGRCMLTLLGLSFILAGLIVGGACIYKYFMPKSTIYHGEMCFFDSEDPVNSIPGGEPYFLPVTEEADIREDDNIAIIDVPVPSFSDSDPAAIIHDFEKGMTAYLDLLLGNCYLMPLNTSIVMTPKNLVELFGKLASGKYLPHTYVVREDLVAVEEIRDVSNLGIFIYQLCNNRKSFRLRRRDLLLGFNKRAIDKCWKIRHFPNEFIVETKICQE
Protein: Peroxisomal trans-2-enoyl-CoA reductase (EC 1.3.1.38) (Q9JIF5)
Organism: Cavia porcellus (Guinea pig)
Function: Participates in chain elongation of fatty acids. Catalyzes the reduction of trans-2-enoyl-CoAs of varying chain lengths from 6:1 to 16:1, having maximum activity with 10:1 CoA. Has no 2,4-dienoyl-CoA reductase activity.
Subcellular location: Peroxisome {ECO:0000269|PubMed:10811639}.
Interaction partners:
- Acetyl-CoA acyltransferase 1
- Acyl-coenzyme A oxidase
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Malonyl-CoA-acyl carrier protein transacylase, mitochondrial
- Peroxisomal targeting signal 1 receptor
- Peroxisomal bifunctional enzyme
- Peroxisomal bifunctional enzyme
- Alpha-methylacyl-CoA racemase
- Isochorismatase domain-containing protein 1
- Fatty acid synthase
Sequence:
MGSWTKCQSCLAPGLLQNRAAIVTGGGTGIGKAIAKELLHLGCNVVIASRKFDRLRAAAEELKATLPPSNKAEVTPIQCNIRKEEEVNNLMKSTLALYGKIDFLVNNGGGQFWSSPEHISSKGWHAVIETNLTGTFYMCKAAYNSWMKEHGGAIVNIIILLNGQPFVAHSGAARGGVYNLTKSLALGWARSGIRINCVAPGTVYSQTAMDNYGDMGKTLFADAFQKIPAKRLGVPEEVSSLVCFLLSPAASFITGQLVNVDGGQSLYCQNHDIPDHDNWPEGVGDLSTVKKMKESFKQKAKL
Protein: TeaA receptor TeaR (Eurofung) (C8V4B8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- mRNA-nucleus export ATPase
- Elongation factor 3
- Small ribosomal subunit protein uS2
- 40S ribosomal protein S8
- 40S ribosomal protein S15
- 40S ribosomal protein S3
- 40S ribosomal protein S10a
- 40S ribosomal protein S17, putative
- 40S ribosomal protein S10b
- 40S ribosomal protein S14
Sequence:
MAGTATATFSADVWTSASTIDASAQPWDFAVPVNQENRHRSKSRTSRKSRDRGSKSSRSSSLSKQIYGHEQSHFAPRGRRDASLSRKEFDSGGVQDTAATSHINGSRKSDIKDDEENDENWIHRDKLARIESEELQQAAILFQRRPGTGSTRGRGRSRDHHHGSVSGTTVISATHHEPLEPWPDLQEDQQNNTASAALAGGDDITEDERQYWDLRRPEEIAAERGSSTSSIYRNPGLRKSSSRIPIPTSSPVPLSPPTIDREYFTSRSRAPTSENEEVSSNARPRRASEPLTVDSASNSDPTSESRPGSRGWPASQNATTKKTAAKPATTNRKTSAPNPKKPSPRSRATSSNANQRPTTRSGEARPPMSINRPEGDPPWLATMYKPDPRLPPDQQILPTHARKMQQEQWEKEGKTPTMYDREFAPLAIAPDQPQPEVKTEKEAEKESQQQEHLKPEGLGLQPPPKSPEPSRPGTSTGYSPMPKVQETPPTGLTPRFNSQTVVTAQGPPPEDEKAEKGCGCCIVM
Protein: 4-hydroxybenzoate polyprenyltransferase, mitochondrial (4-HB polyprenyltransferase) (EC 2.5.1.39) (4-hydroxybenzoate nonaprenyltransferase) (Para-hydroxybenzoate--polyprenyltransferase) (PHB:PPT) (PHB:polyprenyltransferase) (F4JPA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03189}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03189}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03189}.
Interaction partners:
Sequence:
MAFFGLSRVSRRLLKSSVSVTPSSSSALLQSQHKSLSNPVTTHYTNPFTKCYPSWNDNYQVWSKGRELHQEKFFGVGWNYRLICGMSSSSSVLEGKPKKDDKEKSDGVVVKEASWIDLYLPEEVRGYAKLARLDKPIGTWLLAWPCMWSIALAADPGSLPSFKYMALFGCGALLLRGAGCTINDLLDQDIDTKVDRTKLRPIASGLLTPFQGIGFLGLQLLLGLGILLQLNNYSRVLGASSLLLVFSYPLMKRFTFWPQAFLGLTINWGALLGWTAVKGSIAPSIVLPLYLSGVCWTLVYDTIYAHQLHHHRFLFQLLFHVSCKCIHFDDKEDDVKVGVKSTALRFGDNTKLWLTGFGTASIGFLALSGFSADLGWQYYASLAAASGQLGWQIGTADLSSGADCSRKFVSNKWFGAIIFSGVVLGRSFQ
Protein: [Thr6]-bradykinyl-Val,Asp (Bradykinin-related peptide RD-11) [Cleaved into: [Thr6]-bradykinin] (L0PJV8)
Organism: Agalychnis callidryas (Red-eyed tree frog) (Phyllomedusa callidryas)
Function: Induces relaxation of rat smooth muscle from tail artery (EC(50)=16.8 nM) and contraction of that from ileum (EC(50)=205 nM), urinary bladder (EC(50)=895 nM) and uterus (EC(50)=60.3 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2).
Subcellular location: Secreted {ECO:0000255, ECO:0000269|PubMed:24394432}.
Interaction partners:
Sequence:
MSFLKKSLFLVLFLGLVSFSICEEEKRETEEEENEDEMDKESEEKRESPERPPGFTPFRVD
Protein: Protein Dok-7 (Downstream of tyrosine kinase 7) (Q18PE0)
Organism: Mus musculus (Mouse)
Function: Probable muscle-intrinsic activator of MUSK that plays an essential role in neuromuscular synaptogenesis. Acts in aneural activation of MUSK and subsequent acetylcholine receptor (AchR) clustering in myotubes. Induces autophosphorylation of MUSK.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16794080}; Peripheral membrane protein {ECO:0000269|PubMed:16794080}. Synapse {ECO:0000269|PubMed:16794080}. Note=Accumulates at neuromuscular junctions.
Interaction partners:
- Muscle, skeletal receptor tyrosine-protein kinase
- Agrin
- 43 kDa receptor-associated protein of the synapse
- Acetylcholinesterase collagenic tail peptide
- Acetylcholine receptor subunit epsilon
- Acetylcholine receptor subunit delta
- Acetylcholine receptor subunit beta
- Adapter molecule crk
- Acetylcholine receptor subunit alpha
Sequence:
MTEAALVEGQVKLRDGKKWKSRWLVLRKPSPVADCLLMLVYKDKCERSKGLRERSSLTLEDICGLEPALPYEGLAHTLAIICLSQAVMLGFDSHEAMCAWDTRIRYALGEVHRFHVTVAPGTKLESGPATLHLCNDILVLARDIPPTVMGQWKLSDLRRYGAVPNGFIFEGGTRCGYWAGVFFLSSAEGEQMSFLFDCIVRGISPTKGPFGLRPVLPDPSSGGPSASEERVAQEALEALQLEKRLSLLSHSGRPGSGGDDRSLSSSSSEASHSDISASSRLTAWPEQSSSSAGTSQEGPGLVAAQGPGEAMLGASRPPLKPLRPRQLQEVGRQSSSDSGIATGSHSSYSGSFSSYAGSNLDVWRAGEEFGSLLSLPPGASAPEPRLCACPPGAAEYQVPTSLRHHYDTPRSLRQAPRDPSPASQGSSDHGSATDLGGQAPTGCPSSWLGARRRGQATEGPGSDAALPSPSPGESWEAGSPHAGPPPAFFLSCSICGGLKVKPPP
Protein: D-erythrulose kinase (EC 2.7.1.210) (A0QXE4)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the phosphorylation of D-erythrulose to D-erythrulose-4P. Involved in the degradation pathways of erythritol and D-threitol, that allow M.smegmatis to grow on these compounds as the sole carbon source.
Interaction partners:
- Phosphocarrier protein HPr
- D-erythrulose-4-phosphate isomerase 1
- D-threitol dehydrogenase
- Erythritol/L-threitol dehydrogenase
- Muconate cycloisomerase
- Erythritol/L-threitol-binding protein
- Transporter
- Trehalose import ATP-binding protein SugC
- ABC transporter, permease protein
- Trehalose import ATP-binding protein SugC
Sequence:
MTKLFNDPARFTEDMLVGFLDANSRYVVGVPGGVVRAQTTRPGKVAVVIGGGSGHYPAFCGTVGPGFADGAVVGNIFTSPSAEEAASVARAAHSDAGVLLTTGNYAGDVMNFNLAVDQLRSEGIEAQYFAVTDDVASAERGQEAKRRGIAGDFTVFKCASAAAEEGLDLAGVVRVAEAANAATRTLGVAFDGCTLPGADHPLFTVPEGHMGLGLGIHGEPGVSEEKMPTAAGLAATLVDGVLGDRPDAPEKRIAVILNGLGRTKYEELFVVWGEVSRLLRDRGYTIVEPEVGELVTSLDMAGCSLTVMWLDEELERYWAAPADTPAYKKGAAQQHVSGERRSEATARSASSGPKLAELSDEDGRAGARLVARAFDAMAEALADAEEELGRIDAVAGDGDHGRGMVKGSSAAREAAASALSEGAGQGSVLNAAGKAWAAKAGGTSGVLWGALLTALGARLGDTGRPDSSVIAAGVRDAYDALIRLGGAAPGDKTMLDAMLPFTEELERRVAQDESWQSAWRAAADVATEAARATADLRPKIGRARPLAERSVGTPDAGATSLALCARTVADCVTLSTQGEN
Protein: Cathepsin D (Cathepsin D, isoform B (EC 3.4.23.-)) (Cathepsin D, isoform C) (SD07085p) (Q7K485)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cathepsin B, isoform A)
- Cathepsin L1
- FI04419p
- cathepsin L
- Cathepsin F
- Battenin
- Vacuolar protein sorting-associated protein 35
- BcDNA.GH08312
- Autophagy protein 5
Sequence:
MQKVALLLVAFLAAAVAHPNSQEKPGLLRVPLHKFQSARRHFADVGTELQQLRIRYGGGDVPEPLSNYMDAQYYGPIAIGSPPQNFRVVFDTGSSNLWVPSKKCHLTNIACLMHNKYDASKSKTYTKNGTEFAIQYGSGSLSGYLSTDTVSIAGLDIKDQTFAEALSEPGLVFVAAKFDGILGLGYNSISVDKVKPPFYAMYEQGLISAPVFSFYLNRDPASPEGGEIIFGGSDPNHYTGEFTYLPVTRKAYWQIKMDAASIGDLQLCKGGCQVIADTGTSLIAAPLEEATSINQKIGGTPIIGGQYVVSCDLIPQLPVIKFVLGGKTFELEGKDYILRVAQMGKTICLSGFMGLDIPPPNGPLWILGDVFIGKYYTEFDMGNDRVGFADAK
Protein: Large ribosomal subunit protein mL42 (39S ribosomal protein L31, mitochondrial) (L31mt) (MRP-L31) (39S ribosomal protein L42, mitochondrial) (L42mt) (MRP-L42) (Q9Y6G3)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11279123, ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein mL66
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS7m
Sequence:
MAVAAVKWVMSKRTILKHLFPVQNGALYCVCHKSTYSPLPDDYNCNVELALTSDGRTIVCYHPSVDIPYEHTKPIPRPDPVHNNEETHDQVLKTRLEEKVEHLEEGPMIEQLSKMFFTTKHRWYPHGRYHRCRKNLNPPKDR
Protein: Solute carrier family 12 member 1 (Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 1) (BSC1) (Kidney-specific Na-K-Cl symporter) (Na-K-2Cl cotransporter 2) (NKCC2) (P55016)
Organism: Rattus norvegicus (Rat)
Function: Renal sodium, potassium and chloride ion cotransporter that mediates the transepithelial NaCl reabsorption in the thick ascending limb and plays an essential role in the urinary concentration and volume regulation. Electrically silent transporter system.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P55014}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP-sensitive inward rectifier potassium channel 1
- Sodium/hydrogen exchanger 3
- Aquaporin-2
- STE20/SPS1-related proline-alanine-rich protein kinase
- Barttin
- Epithelial sodium channel subunit gamma
- Serine/threonine-protein kinase OSR1
- Uromodulin
- Sodium-dependent phosphate transport protein 2A
- Epithelial sodium channel subunit alpha
Sequence:
MSVNIPSNSVPSGASRFQVHVINEGHGSGAAMSDSTDPPHYEETSFGDEAQNRLKISFRPGNQECYENFLQTGETAKTDTTFHAYDSHTNTYYLQTFGHNTMDAVPKIEYYRNTGSVSGPKVNRPSLQEIHEQLAKNVAVAPGSADRVANGDGMPGDEQAENKEEDVTGVVKFGWVKGVLVRCMLNIWGVMLFIRLSWIVGEAGIGLGVIIIGLSVVVTTLTGISMSAICTNGVVRGGGAYYLISRSLGPEFGGSIGLIFRFANAVRVAMYVVGFAETVVDLLKESDSMMVDPTNDIRIIGSITVVILLGISVAGMEWEAKAQVILLVILLIGIANFFIGTVIPSNNEKKSRGFFNYQASIFAENFGPSFTEGEGFFSVFAIFFPAATGILAGANISGDLEDPQDAIPRGTMLAIFITTVAYIGVAICVRACVVRDATGSMNDTVVSGMNCNGSAACGLGYDFSRCQHEPCQYGLMNNFQVMSMVSGFGPLITAGIFSATLSSALASLVSAPKVFQALCKDNIFKGLQFFAKGYGKNNEPLRGYFLTFVIAMAFILIAELNVIAPIISNFFLASYALINFSCFHASYAKSPGWRPAYGIYNMWVSLFGAILCCAVMFVINWWAAVITYVIELFLYIYVTYKKPDVNWGSSTQALSYVSALDNALELTTVEDHVKNFRPQCIVLTGGPMTRPALLDITHAFTKNSGLCICCEVFVGPRKLCVKEMNSGMAKKQAWLMKNKIKAFYAAVAADCFRDGVRSLLQASGLGRMKPNTLVIGYKKNWRKAPLSELENYVGIIHDAFDFEIGVVIVRISQGFDISPVLQVQDELEKLEQERLALEAAIKDNDCEEGKGGIRGLFKKAGKLNITKPAPKKDSNISTIQSMHVGEFNQKLVEASAQFKKKQGKGTIDVWWLFDDGGLTLLIPYILTLRKKWKDCKLRIYVGGKINRIEEEKISMASLLSKFRIKFADIHIIGDINIKPNKESWKVFEEMIEPYRLHESHKDLTTAEKLKRESPWKITDAELEAVKEKSYRQVRLNELLQEHSRAANLIVLSLPVARKGSISDLLYMAWLEILTKNLPPVLLVRGNHKNVLTFYS
Protein: Cohesin subunit rad21 (Double-strand-break repair protein rad21) (SCC1 homolog) (P30776)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by cut1 and dissociates from chromatin, allowing sister chromatids to segregate. Also involved in the DNA double-strand-break (DSB) repair system.
Subcellular location: Nucleus {ECO:0000269|PubMed:11069892}. Chromosome, centromere {ECO:0000269|PubMed:11069892}. Note=Associates with chromatin. Cohesin complex mainly associates with broad centromere region. Also associates with mating-type heterochromatic region.
Interaction partners:
- Sister chromatid cohesion protein pds5
- Sister chromatid cohesion protein mis4
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 1
- Cohesin subunit psc3
- Meiotic recombination protein rec11
- Separin
- Serine/threonine-protein kinase plo1
- Meiotic recombination protein rec8
- Structural maintenance of chromosomes protein 4
Sequence:
MFYSEAILSKKGPLAKVWLAAHWEKKLSKVQTLHTSIEQSVHAIVTEETAPMALRLSGQLMLGVVRIYSRKARYLLEDCTEALMRLKMSFQPGQVDMIEPATALQSLKGKDAVTQSANLTLPETITEFDLLVPDSTFDFQWSQLLRTPSRSSNTLELHSLPISSSPSFPSSQLSIEAGRNAQVESGFSLGESFAHVGNDMQFHLPISNSGAATPRSVHSDNQSQISIEVGRDAPAAAATDLSGIIGPQMTKSPASSVTHFSTPSMLPIGGTSLDDELLAPVDDLNLDLGLDDLLGDEQGANAPAIEADEQAETSSIHLPSDIMEDDSSRPAAAGVEEGQVVESATAPQQEKINPQKTVRRQRAIIDPVTELSSKQMKKQLADTSSITSPLCLNTSSIVFNATVNFTRNGKFNTSIFSSNLNPKVNELLQADFKQAILRKRKNESPEEVEPAKHQRTDTSTENQETAEVLDPEEIAAAELANITEAAIATLPQETVVQPEGEAPELGSPMGFPVTALESADDSLFDAPPVMLDEADLLGSERLDSSVSEALPSSQTAKDSLRNKWDPYTEGEKVSFQTLSAGCNREEAVQLFFDVLVLATKDVISVKQDVAIQNEITLTAKRGMLLSSL
Protein: Kinetoplastid membrane protein 11 (KMP-11) (Q9U6Z1)
Organism: Trypanosoma cruzi
Function: May be involved in the regulation of the cytoskeleton through interaction with the subpellicular microtubules. May be involved in parasite mobility and attachment to the surface of the host cell. Behaves as a strong immunogen during infection.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10668791}. Note=Associated with microtubules.
Interaction partners:
Sequence:
MATTLEEFSAKLDRLDAEFAKKMEEQNKKFFADKPDESTLSPEMKEHYEKFEKMIQEHTDKFNKKMHEHSEHFKAKFAELLEQQKNAQFPGK
Protein: OxyR (Q9HTL4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- ATP-dependent DNA helicase RecG
- Alkyl hydroperoxide reductase subunit F
- Catalase HPII
- Alkyl hydroperoxide reductase C
- RNA polymerase sigma factor RpoS
- Redox-sensitive transcriptional activator SoxR
- Catalase
- OhrR
- Superoxide dismutase
- Superoxide dismutase
Sequence:
MTLTELRYIVTLAQEQHFGRAAERCHVSQPTLSVGVKKLEDELGVLIFERSKSAVRLTPVGEGIVAQAQKVLEQAQGIRELAQAGKNQLAAPLKVGAIYTIGPYLFPHLIPQLHRVAPQMPLYIEENFTHILRDKLRTGELDAIIIALPFQEADVLTKPLFDEPFYVLMPADHPWTAKASIDSELLNDKSLLLLGEGHCFRDQVLEACPTVRKGDENKHTTVESSSLETIRHMVASGLGVSVLPFSAVDSHHYAPGVIEVRPFSAPVPFRTVAIAWRASFPRPRAIEVLADSIRLCSVARPQTQEQPQIA
Protein: Axotactin (M9PE65)
Organism: Drosophila melanogaster (Fruit fly)
Function: May have serine protease inhibitor activity (Probable). Might play a role in the glial-neuronal signaling pathway that is important in establishing the electrical properties of axonal membranes.
Subcellular location: Cell projection, axon {ECO:0000269|PubMed:10037607}. Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to longitudinal axon tracts as well as to an axonal scaffold in the brain (PubMed:10037607). A secreted form might exist (Probable). {ECO:0000269|PubMed:10037607, ECO:0000305|PubMed:10037607}.
Interaction partners:
Sequence:
MAFPYIWALLPLICSASGLSLPNMTSTDAVVAGGGILPILVAGNPGNLGSSNMSLSGGGGLAGSSTGGQSLPDTGGGNSAGGSPAGGSSGTGGGGSNSGISGNNSAMIQGQKSNQYEKCAGPGDPGPCKQYIYKWRYEPTTNECTNFIWGGCEGNPQNRFGTEAECLFHCIGGPHTLPPFLQSTTREPSTTESSMLLGLPYTQSPAQSPDGMGGAEGGDGTTPVPIEQRGPELTFAETGQGKTFIFAKNNTFIQMDGDIIQTFQLRLCREISFQFRTRLPHGLLVYHNVKNPDRINLDPYALYVIVEKGQLKVVHVFGKHSTSVTVGESLNRDEWHSVMVRIDVHGARLIARVDNSQEEVYLKGLNHEYNYGVSTNLPSVVLVGGLSSEEKLHGVKYITESFVGCIRNVVLSSGKAASDLLPIAPLVATKHENVNEGCSDMCESRHNLCFVGSRCINHYGGISCDCFGTHYEGEHCDIYTATIITLRGASYVSYRIYDWKDRVHSSTRRISLMFRTNFDDSALFYASGESLKHQYIAASIKNQSVHVEMDFGDNVMSTVLTDDLTRGYWHNLTILHEQRTVSIILDQQQKVLELPATASGNMLFDPEIYFGGGPELHKKKGLASHNNFVGSLKYVYYNDISILYELQRGNPKVHYHGVLEAEFVENEVNVIPITYPFATSHIWWPINHAEEFNIKFDFRSSRPGAVLAYSDVTTSAGNGFWEIRLTSDKLSFDLVPDVNNNVTHSTTIKINRATSWHSVELDYKLGEIRFTVDYRHTLSQMYGLTFNIGDKLIIGSSLKSAAMGLVGCIRDIEINGHLIEPRHVVKTERVVGEVALDNCNYIDPCKRPNTCEHGGKCFVKDDRVTCDCKHTGYIGKNCHFTKYRKTCEELALLGFTKSDVYLIDIDGNGVFPPAHVKCDFQSLENATKTIVEHNLPSQVDVRSARESDFSFNIRYREFSPHMLQELISHSLYCTQYIKYDCYRAQLELHSATWFTSSAKNLTVDFLGNVKRGACPCSVNKTCVDPNQSCNCDVKENKWNSDEGYYQDPQSLGITNMYFLQQKDMDDEAQGRITLGPLECVETNTQKYVVTFTTSQSYIEVPGWRKGDIAFSFRTTGEKAILLFQPPIRPHYPSFMVALTGDDQLTFTFTLSTGTTRELVINSHRRLNGGEWHKIWIDYNQYHVRFMINTDYQMLDLLPEEEFGPFEGSMYIGGATFDLLKKLSVKAGLIGCFRGLVVNGEILDIYSYMSVHLSEIIKDCKPSCVPSPCRNGAQCKELWSSFKCVCNNPWAHIGEFCETNINEKALTFINRESFLMRNYLSVGATPVILMHGINGERDVLKGILNQDLLINLRTYDTNALVLYANDHYNNFVHLYISLNREIVFLYNYGDEIVNLTLLDDTLMASLKSIQVAIVRGEQETRMHVNEHSVSIDRGTLLLDEYANKPWSNPEKEVLSPHRPPAPPTEYFQFHVGGYDPANLLRPNVDAPALEGYIGCVRGLKIGAQLIDLADINERNIAPTQEGVLPNCQIKCDAEPCKNGGTCQEHFAEQLSTCDCEHTSFLGEFCSEEKGADFSGESTLQRKFELPGTGRVDYVRLQLAFSSFDLRRANRIMLLMQTEAERSYYLLLAITSDGYLQLEEDRDNGQTVGARIDRNFLNSARHSVYYVRNGTQSQLFIDREQVPLSEFAARVLTTGGDAGSNRVQIGGINSTDSRFAVFKSYSGCLSNIYIQVNGHVMKPLEEYMLFTKSGADNITVINPQGVRSAQCNAKFDVSEQPTQEPMVNVSMIPEPWVEEPPARVPYIPRFVYDENKQEDSTQVVFLTLTSVFVIIVICCLLEVYRSHLAYKKRIERETDEDIIWSKEQATKMHESPGVKAGLLGGVTAGSGNGLPPYTYKALPQEDKKPGNGAPLVGILKNGSATPSQPGTPTALSKNGDIASRIEEEEEEEDEAPAQKAAEKSGENEEPPAKDTTASEIKESQAQPPEQLAKDTTDASAAPKASKETEAQAEPSEPSSQLNSAQNGQLAQMEQAARGDEVQVPSLPHPIQPPDAIFMPNLPQKAQQRQPQEHKSRHKATDDTEAPKQQQQQQQQQQSFDVATNANGSSLPASRVKNPEEPGGKSPLVPMRQHHSKVTRPPPPPTLFLENSLLQRQFANPISYLGGPRLQPRSNRTSIDSILSLD
Protein: Small ribosomal subunit protein RACK1 (Guanine nucleotide-binding protein subunit beta-2-like 1) (Q21215)
Organism: Caenorhabditis elegans
Function: Required for the expression of antimicrobial peptide nlp-29 in response to fungal infection or physical injury.
Interaction partners:
- Ribosomal Protein, Small subunit
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein uL4
- Elongation factor 2
- Small ribosomal subunit protein uS4
Sequence:
MVQEQMKLTGTLEGHTGWVTQIATYTRNDKTTVLSSSRDKTILVWDVDSVAPVDEGPIGRPVRSLTGHNHFVSDVVISSDGQFALSGSWDKTLRLWDLNQGVSTRQFISHTKDVLSVAFSADNRQIVSGSRDKSIKLWNTLAQCKYTITDDCHTDWVSTVRFSPSNRDPVIVSAGWDKVVKVWNLGNCRLKTNHIGHTGYVNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLPGNDVINAMSFSPNRYWLCAAVGSSIKIWDLEDKKEIEELKPEIASSGSSRGSSPQCISLAWSQDGQTLFAGYTDNIIRVYQVSIRASN
Protein: Serine aminopeptidase S33 domain-containing protein (O05805)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit D
- Mycothione reductase
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit C
- NADH-quinone oxidoreductase subunit B
- Conserved protein
- NADH-quinone oxidoreductase subunit H
Sequence:
MTGWVPDVLPGYWQCTIPLGPDPDDEGDIVATLVGRGPQTGKARGDTTGAHHTVLAVHGYTDYFFHTELADHFANRGFAFYALDLRKCGRSRAPGQTPHFITDLARYDTELEHSLSIINEQNRSAKVLVYGHSAGGLIVSLWLDRLRQRGEITRAGVTGLVLNSPFLDLQGPAILRLPLTSAFFAAMARMRPKWVARPPKEGGYGCTLHRDYDGEFDYNLQWKPVGGFPVTFGWIHASRRGHARLHRGIDVGVPNLILCSDHTVREKADPATLHRGDAVLDVTHITRWAGCIGNRSTVIAVADAKHDVFLSLPQPRQMAYRRLDLWLDDYLGTHNDTDASASSGKG
Protein: Transcription factor VHR2 (VHT1 regulator 2) (P40041)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor that regulates ERG9, but seems to have a more global function in transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Anaphase-promoting complex subunit 4
- Mitotic spindle checkpoint component MAD2
- Anaphase-promoting complex subunit CDC16
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit DOC1
Sequence:
MIDDTENSKIHLEGSHKTGKYTGYGTTHKIRAQLNFNDEKKWKKFSSRRLELIDSFGLSQHKASEQDDNIRQIATILRSEFEYPDTFSAEFEKLVTAAVQSVRRNRKRSKKKLLDSKKKIARGKVQKIPLSPPSSSNMGSCSASNASSSDEEASVKEEPAEHALPSLNTITSQKLLPYPNGRTLPPVPTQVRSLLKKNASLLRDPSAPYAHGGDEKLQKFDIEDQPLESEQEYDFIAKSIIVEIVNNAIPLPEQIQRDKFIRPNLTKKKGCQSKVVISNNLRKLILSKIHNSRTCLEMSKDERNLDSFANLETLGKNSLMASISLVVENSFSHLPSSTKQYLTERLSSIEFLTILSQRLFMPATRQLFADLSQEKIQVRVLNLILGSLVKDYGFDASLAPINEIIYHMTLHQYPLVCSNKQSNPMRPHSTSEVLSAHSSTKDASTPGKEEPRVTRSSTSADSTIITLPSIEVPNTYDDDRLKMLSAISLQIENSTFSKPFSTISK
Protein: Rabphilin, isoform C (M9PJH7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MWKKSGAWFFKGLPKYDMPRSASATPIPNPGPGSMAGDTRAVQSCHATPTRPARVKKLTIRVNDSSSSSSGHSEPEDEVDTGVGIGVGVVGGGMAKGIASTRLQREDSFRLRAYGSIRSFIDGGERKLSNSFFFNRQQSQRPSECPEYDSVSMSKLRRESSFLRRGSVSSSWSISDSSGSGSNNSGNSQTQSQYQQHQQQLQQHCRDPLLGWLEIAISYREAFHSLDCTMVRARDLPAMDAAGLADPYCKLNIITPEAHTKYTRWQRTKTVHKTRNPEFNETLQFVGVEPEELGNSLIYVALFDDDKYGHDFLGAAKVCLSTHVAVPDFGATRRGGPVQQRGGDGPELAQWQDASLALLQHQAKGVGGECETVHQPDGHGQQRQLRSLRQDPTQAGCAQEQEAQDQRQMAHAQSHLQRGVLLRGKSARPQQGDAHPDRVGQGSRQEQRLPGQPAIGRPKQRRTPAAVARLHPIARSLPREMALPRPRQSRPLSSPIRSQRQPIPSPIDSILSLPIWMFFL
Protein: Trehalose-phosphatase (EC 3.1.3.12) (Trehalose synthase complex catalytic subunit tps2) (Trehalose-6-phosphate phosphatase) (TPP) (O14145)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Phosphatase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cytosolic neutral trehalase
- Alpha,alpha-trehalose-phosphate synthase
- Putative alpha,alpha-trehalose-phosphate synthase 100 kDa subunit
- Putative alpha,alpha-trehalose-phosphate synthase 106 kDa subunit
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Trehalose-phosphatase
- Probable thiamine biosynthetic bifunctional enzyme
Sequence:
MPSGAQGNTQSAAYKRIVNVSRNFQFKAALNKDTREWTFQHRSSGTALYSAIASLGDPSSPWDAVYVASPGPVQISEGNDHTVETKIDEAAVVHRSSSIVISPEDQEIFLKKATEYYRKKNIEADIVPVWGKVQRVPQAKSSSATITPSVSNKLSTAYQSIKSEALKDGPMYADSVLWDVLHYRIPTLDGYQQHNLWKNFTRWSQYFADNIVSNYRPGDLILIHDYSLFLLPRLIRKQLSDAPIVFFLHAPFCTSEVFRCLSKRAEILKGVLASNVIAMQTDSYTRHFLSTCSNVLGLETTSTHIDTSDGFRVVVFSSHVSIDVPRVYSRCNSKPVSLKIQQLKSLYPSDKKLIVGRDQLTKACGVTHKLRAFRELLIHFPKWRGHVVLIQITSLPVGNNYSNEELKKTENLVAQINSEFGSLDYTPVIHFHQLLDPDEYYALLSVANIACVSSVRDSMNTMALEYVACQQKNKGSLILSEFSGTAELLLSAYLVNPYDYSRFAETINYCLNMTEKERERRFSSLWKQATSQSSQQWIYKLINRAAYEVKALESHMTTPLLTYNILIKPYRNAKRRLFLLDYDGTLIESARNSIDAVPTDRLLRTLKRLASDSRNIVWILSGRSQKFMEEWMGDISELGLSSEHGSAIRPPLAGSWSSCAENLDLSWKDTVRDFFQYYVERTPGSYIEEKKHSISWCYQNANTTYSKFQSLECQTNLEDMLKHYDVEISPAKSFLEVHPNYLNKGSIVRRILKRSGSVDFVFCAGDDKTDENMFEVFLPTAFSNSHLIDEIDSTEYSGSHHTDDNSDANKVENVKVATFRVHIGLTDKPTLSDYHLPAPRDLGELLHNL