wanglab/gogpt-training-data huggingface dataset:
Protein: PD-(D/E)XK endonuclease-like domain-containing protein (Q38C24)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSRVPHPSGVDILFDSKWHQYKIGNCALRSVSKLLDKHFPFDEKRALAAVAKKTGQTTEEVKASWNRQALLGKNIHEYIECKLRGLPPPTWTLLLKKKRRKEDVFRHQDIREGSKKKKKDKKSDGDSEGSEGSDGKKHASRGSKSLIDTLLHGEEEAYMVVADRVVETIECNYDIIAVEQVIASVPWGIAGTVDLIARNKRTGRLLIGDWKTSGTVASSFRFSPFETPCTGCLLHLPNSRFHRYAMQVAIYGEILKNDQYLEKGFFGKKIEPLNKDIGEINLSPAMVNEALEYGIVQMQKNDAGSVCVEFKEVKESTVMPVDATDCTFLQLLHSVMRG
Protein: Sodium channel regulatory subunit beta-2 (P54900)
Organism: Rattus norvegicus (Rat)
Function: Crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the sodium channel. The subunit beta-2 causes an increase in the plasma membrane surface area and in its folding into microvilli. Interacts with TNR may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22992729}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O60939}. Cell projection, axon {ECO:0000269|PubMed:22992729}. Note=Clusters at the axon initial segment and node of Ranvier, the specialized neuronal subcellular domains involved in action potentials generation and propagation. {ECO:0000269|PubMed:22992729}.
Interaction partners:
- Sodium channel regulatory subunit beta-1
- Sodium channel regulatory subunit beta-3
- Sodium channel protein type 2 subunit alpha
- Sodium channel protein type 3 subunit alpha
- Sodium channel protein type 1 subunit alpha
- Sodium channel protein type 9 subunit alpha
- Sodium channel protein type 5 subunit alpha
- Sodium channel protein type 8 subunit alpha
- Sodium channel protein type 4 subunit alpha
- Sodium channel protein type 10 subunit alpha
Sequence:
MHRDAWLPRPAFSLTGLSLFFSLVPSGRSMEVTVPTTLSVLNGSDTRLPCTFNSCYTVNHKQFSLNWTYQECSNCSEEMFLQFRMKIINLKLERFGDRVEFSGNPSKYDVSVTLKNVQLEDEGIYNCYITNPPDRHRGHGKIYLQVLLEVPPERDSTVAVIVGASVGGFLAVVILVLMVVKCVRRKKEQKLSTDDLKTEEEGKTDGEGNAEDGAK
Protein: Innexin inx5 (Q9VWL5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Structural component of the gap junctions.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction {ECO:0000250}.
Interaction partners:
Sequence:
MFSAVKPLSKYLQFKSIRIYDSVFTIHSRCTVVILLTCSLLLSARQYFGDPIQCISEEKNIEYIQSYCWTMGTYILKLDDFGDQEQALVSPNQEVSYNSAFFSSATTNAPQSSSRVRTRPHFRSSLRRIGEYNEAYARSLSIAEGVGPEIRGQTERQYLRYYQWVIILLLFQSFVFYFPSCLWKVWEGRRLKQLCSEVGDALLSEETYNTRLRMLVKYFTTDYEDMHFCYMAKYVFCEVLNFLISVVNIIVLEVFLNGFWSKYLRALATIPFYDWDRWNRVSSSVFPKIAKCEVLKFGGSGTANVMDNLCILPLNILNEKIFVFLWAWFLLMALMSGLNLLCRLAMICSRYLREQMIRSQLRFMTKRHVKRALRDLTIGDWFLMMKVSVNVNPMLFRDLMQELCELRTSASGSTLESPV
Protein: Acid-sensing ion channel 1A (ASIC1-A) (Acid-sensing ion channel 1.2-A) (Amiloride-sensitive cation channel 2-B, neuronal-A) (ZASIC1.2) (Q708S7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Proton-gated sodium channel; it is activated by a drop of the extracellular pH and then becomes rapidly desensitized. Generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Can also transport potassium ions, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14970195}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q1XA76}. Postsynaptic cell membrane {ECO:0000305|PubMed:14970195}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6NXK8}.
Interaction partners:
Sequence:
MKTSVMDLKVEPMDIDFDQPPPLQVFAHTSTLHGISHIFSYEKITAKCCLWVVFFLSSLTFLMYVCIDRIQFYLEYPHVTKLDEITTPVMVFPAVTICNLNSIRFSRITRNDLYHAGELLALLNSRHEVREAHLVEESVMEVLKSKTDFRSFKPRHFNMWEFYNRTGHDIKDMLLSCQFRGSPCRPEDFSVVFTRYGKCYTFNSGETGPPRVSVKGGMGNGLEIMLDIQQDEYLPVWGESDESSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVSCQEQRLVYLPAPWGSCKSTPPSSDYFRAYSISACRTDCETRYLVENCNCRMVHMPGDAPYCTPVLYKECAHPALDFLVETDSDYCSCETPCNITRYSKELSFVKIPSKASVKYLAKKYSKSEKYITENVMVLDVFFEALNYETIEQRKAYEVAGLLGDIGGQMGLFIGASILTILELFDYLYEVMKYRLCRCSNKKHHNNNNNTDHNAVFSLDDVNCHVSKFH
Protein: Spermatogenesis-defective protein 39 (SPE-39) (VPS33B-interacting protein in polarity and apical restriction) (Q23288)
Organism: Caenorhabditis elegans
Function: Proposed to be involved in endosomal maturation implicating in part vps-33.2. May play a role in epithelial polarization through stabilization of apical membrane protein content. May play a role in transcriptional regulation (By similarity). Plays a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes. Essential for vesicular trafficking during spermatogenesis; required during spermiogenesis or sperm activation for the morphogenesis of specialized Golgi-derived fibrous body-membranous organelle (FB-MO) complexes. Required for the processing of internalized proteins in oocytes and coelomocytes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14504223}. Cytoplasmic vesicle {ECO:0000250}. Early endosome {ECO:0000250|UniProtKB:Q9H9C1}. Recycling endosome {ECO:0000250|UniProtKB:Q9H9C1}. Late endosome {ECO:0000250|UniProtKB:Q9H9C1}. Note=Localizes in both residual bodies and budding spermatids (PubMed:14504223). {ECO:0000269|PubMed:14504223}.
Interaction partners:
- Vacuolar protein sorting-associated protein 33B
- Vacuolar protein sorting-associated protein 33A
- Vacuolar protein sorting-associated protein 16 homolog
- Vps8 domain-containing protein
- Vacuolar protein sorting-associated protein 45
- V-type proton ATPase subunit B 2
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 39 homolog
Sequence:
MALRRKFTFELPEDSYWNESDSNSSGLFDDLQSKQLQARAAVDNLFGGDETPKPYVRPQNPTPTPTNVPLQIDGRAAAVSDKANIRITDTSPRASGKIVDDFLNMKFAENVNVAPVIQTAPSVVSEASASSLPSEAQRLDLDYNRLRQEHRKLKDQHEVLRHERFQPLTIEASIKRMLQGHTVTLDYYRSLRDKTQLLKQAVATYDNNTIFKIVIFLERTLKENIFCKIMDGQKSACRVYTRHLQITGEWDKMNKFLRSIGQYQHASVIEFEATRKYKRNPDKRVPLLRTMLHGSFSIPEMKFEARQMEALMRNYEIQLQMEKMDAGDKGEHFRKFPKTSSLIGLPALSSLYYSAMYHYDDSPTSAASLPSVQTLIRFNDRLATQTIVSALTRLSRWPDIDKLLQPKTITMTFSAAKSVFKGKKSTSKWGVSINNHNLLTIVKRSHPSPPTDFIYRILKGESDAQERLRLALLFDVPEMVIECLTQKGDRLSLASYAKSLKTNSVESFKAVAALNNPSIKWK
Protein: LD01876p (Q86M55)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASSSNNSSSTANNHGGHNPLNRLSLKSAGKRNQESMSHSQPNGGWINVETLNNGNGLLHSPPHNHQQQQQQQQRGGGGASPAGGGGGPSAAADHNIQITQPISAPSSPLASPGALNSSGSSSGGGAGSAGGISGSPTAFCLPSSSAAAAVAAISATPTSGSGSYVCSAGTNWHFAAVAASNAIDTADPNWQASKATVLERNAAMFNNELMSDVKFIVGGEFDIDPIQTIPAHKYILATGSSVFYAMFYGGLAENKQEIKVPDVEPTAFLTLLRYLYCDEIKLEPEHILATLYAAKKYIVPHLARACVNYLEVKLTAKKRLPTSQSIASVRGARADATLLGSDRRPGRDGG
Protein: Odorant receptor Or1 (AgOr1) (Q8WTE7)
Organism: Anopheles gambiae (African malaria mosquito)
Function: Odorant receptor which plays a critical role in the anthropophilic host-seeking behavior; establishes the host preference to transmit malaria. May participate in the phenomenon of decreased host-seeking behavior in disease vector mosquitoes after blood feeding.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Odorant receptor coreceptor
Sequence:
MKLNKLNPRWDAYDRRDSFWLQLLCLKYLGLWPPEDTDQATRNRYIAYGWALRIMFLHLYALTQALYFKDVKDINDIANALFVLMTQVTLIYKLEKFNYNIARIQACLRKLNCTLYHPKQREEFSPVLQSMSGVFWLMIFLMFVAIFTIIMWVMSPAFDNERRLPVPAWFPVDYHHSDIVYGVLFLYQTIGIVMSATYNFSTDTMFSGLMLHINGQIVRLGSMVKKLGHDVPPERQLVATDAEWKEMRKRIDHHSKVYGTMYAKVTECVLFHKDILSFGDEVQDIFQGSIFAQVCASVIIICMTLLQATGDDVTMADLLGCGFYLLVMTSQVFIFCYVGNEISYTTDKFTEFVGFSNYFKFDKRTSQAMIFFLQMTLKDVHIKVGSVLKVTLNLHTFLQIMKLSYSYLAVLQSMESE
Protein: (S)-coclaurine N-methyltransferase (PsCNMT) (EC 2.1.1.140) (Q7XB08)
Organism: Papaver somniferum (Opium poppy)
Function: Involved in the biosynthesis of benzylisoquinoline alkaloids. N-methyltransferase methylating (S)-coclaurine. 4'-O-methylcoclaurine and norlaudanine can also be used as substrates.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16813579}.
Interaction partners:
Sequence:
MQLKAKEELLRNMELGLIPDQEIRQLIRVELEKRLQWGYKETHEEQLSQLLDLVHSLKGMKMATEMENLDLKLYEAPMEFLKIQHGSNMKQSAGYYTDESTTLDEAEIAMLDLYMERAQIKDGQSVLDLGCGLGAVALFGANKFKKCQFTGVTSSVEQKDYIEGKCKELKLTNVKVLLADITTYETEERFDRIFAVELIEHMKNYQLLLKKISEWMKDDGLLFVEHVCHKTLAYHYEPVDAEDWYTNYIFPAGTLTLSSASMLLYFQDDVSVVNQWTLSGKHYSRSHEEWLKNMDKNIVEFKEIMRSITKTEKEAIKLLNFWRIFCMCGAELFGYKNGEEWMLTHLLFKKK
Protein: Leucine-rich repeat neuronal protein 2 (Glioma amplified on chromosome 1 protein) (Leucine-rich repeat neuronal protein 5) (O75325)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MRLLVAPLLLAWVAGATAAVPVVPWHVPCPPQCACQIRPWYTPRSSYREATTVDCNDLFLTAVPPALPAGTQTLLLQSNSIVRVDQSELGYLANLTELDLSQNSFSDARDCDFHALPQLLSLHLEENQLTRLEDHSFAGLASLQELYLNHNQLYRIAPRAFSGLSNLLRLHLNSNLLRAIDSRWFEMLPNLEILMIGGNKVDAILDMNFRPLANLRSLVLAGMNLREISDYALEGLQSLESLSFYDNQLARVPRRALEQVPGLKFLDLNKNPLQRVGPGDFANMLHLKELGLNNMEELVSIDKFALVNLPELTKLDITNNPRLSFIHPRAFHHLPQMETLMLNNNALSALHQQTVESLPNLQEVGLHGNPIRCDCVIRWANATGTRVRFIEPQSTLCAEPPDLQRLPVREVPFREMTDHCLPLISPRSFPPSLQVASGESMVLHCRALAEPEPEIYWVTPAGLRLTPAHAGRRYRVYPEGTLELRRVTAEEAGLYTCVAQNLVGADTKTVSVVVGRALLQPGRDEGQGLELRVQETHPYHILLSWVTPPNTVSTNLTWSSASSLRGQGATALARLPRGTHSYNITRLLQATEYWACLQVAFADAHTQLACVWARTKEATSCHRALGDRPGLIAILALAVLLLAAGLAAHLGTGQPRKGVGGRRPLPPAWAFWGWSAPSVRVVSAPLVLPWNPGRKLPRSSEGETLLPPLSQNS
Protein: Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide I) (P00399)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00401}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00401}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4
- Cytochrome c oxidase subunit 2
- Cytochrome b
- Cytochrome c oxidase subunit 3
- NADH-ubiquinone oxidoreductase chain 5
- NADH-ubiquinone oxidoreductase chain 2
- NADH-ubiquinone oxidoreductase chain 1
- Cytochrome c oxidase subunit 5A, mitochondrial
- ATP synthase subunit a
Sequence:
SRQWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALSLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNNKWLKSHFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNIVSTIGSTISLLGILFFFFIIWESLVSQRQVIYPIQLNSSIEWYQNTPPAEHSYSELPLLTN
Protein: Guanine deaminase (Guanase) (Guanine aminase) (EC 3.5.4.3) (Guanine aminohydrolase) (GAH) (P76641)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Interaction partners:
- Putative xanthine dehydrogenase FAD-binding subunit XdhB
- Putative xanthine dehydrogenase molybdenum-binding subunit XdhA
- Adenine phosphoribosyltransferase
- Putative xanthine dehydrogenase iron-sulfur-binding subunit XdhC
- Hypoxanthine phosphoribosyltransferase
- Pyrimidine/purine nucleoside phosphorylase
- Purine nucleoside phosphorylase 2
- Pyrimidine-specific ribonucleoside hydrolase RihB
- Xanthine-guanine phosphoribosyltransferase
- Purine nucleoside phosphorylase DeoD-type
Sequence:
MMSGEHTLKAVRGSFIDVTRTIDNPEEIASALRFIEDGLLLIKQGKVEWFGEWENGKHQIPDTIRVRDYRGKLIVPGFVDTHIHYPQSEMVGAYGEQLLEWLNKHTFPTERRYEDLEYAREMSAFFIKQLLRNGTTTALVFGTVHPQSVDALFEAASHINMRMIAGKVMMDRNAPDYLLDTAESSYHQSKELIERWHKNGRLLYAITPRFAPTSSPEQMAMAQRLKEEYPDTWVHTHLCENKDEIAWVKSLYPDHDGYLDVYHQYGLTGKNCVFAHCVHLEEKEWDRLSETKSSIAFCPTSNLYLGSGLFNLKKAWQKKVKVGMGTDIGAGTTFNMLQTLNEAYKVLQLQGYRLSAYEAFYLATLGGAKSLGLDDLIGNFLPGKEADFVVMEPTATPLQQLRYDNSVSLVDKLFVMMTLGDDRSIYRTYVDGRLVYERN
Protein: UPF0658 Golgi apparatus membrane protein C23H3.04 (O13938)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MFWDFKHRIEQSVTNFRETTYEAFSRCKLFLKTLPKTSIFFLTVIILECLLIICFEGYCIGQFRTVELLKNLGIDSLPISLTLFIFACFFILYLCVEALSSKNIIEIIGLLCIHVALFIYSIVQISELAEIQKVFLSKTQSSLNPITLILNRHEAGNEGIYFILEVPKRIKPFLIALPVILGVASVMLGFLAHGMNKAYGWVIYKKIGPELRMRRRYLVYKIYVTLLKIDIYFFLGVTVQYVMVLPEDAVVEFVLTILVLPLTVLILTLSFNSVSSENMFLMMTVQFFYVCGIPYILFKIIRMYTSTQKEYYASSKQMITTFSVITLLLLLFTIAIGFACSHNFKKGLKEYCM
Protein: Ankyrin repeat domain-containing protein 54 (Lyn-interacting ankyrin repeat protein) (Q6NXT1)
Organism: Homo sapiens (Human)
Function: Plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Midbody {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm during the cell cycle. EPO stimulation induces nuclear accumulation (By similarity). {ECO:0000250}.
Interaction partners:
- Lipoyl synthase, mitochondrial
- Tubby-related protein 3
Sequence:
MAAAAGDADDEPRSGHSSSEGECAVAPEPLTDAEGLFSFADFGSALGGGGAGLSGRASGGAQSPLRYLHVLWQQDAEPRDELRCKIPAGRLRRAARPHRRLGPTGKEVHALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLNILQEGHAQCLEAVRLEVKQIIHMLREYLERLGQHEQRERLDDLCTRLQMTSTKEQVDEVTDLLASFTSLSLQMQSMEKR
Protein: glucan 1,4-alpha-glucosidase (EC 3.2.1.3) (1,4-alpha-D-glucan glucohydrolase) (Glucan 1,4-alpha-glucosidase) (Q2ULP9)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Glycosyl hydrolase family 13 catalytic domain-containing protein
- alpha-amylase
- Alpha-amylase A type-1/2
- Glycosyl hydrolase family 13 catalytic domain-containing protein
- Alpha-glucosidase
- Glycosyl hydrolase family 13 catalytic domain-containing protein
- Alpha-1,4 glucan phosphorylase
- 1,4-alpha-glucan-branching enzyme
- Glycogen debranching enzyme
- Probable alpha/beta-glucosidase agdC
Sequence:
MRNNLLFSLNAIAGAVAHPSFPIHKRQSDLNAFIETQTPIAKQGVLNNIGADGKLVEGAAAGIVVASPSKSNPDYFYTWTRDAGLTMEEVIEQFIGGDATLESTIQNYVDSQAKQQAVSNPSGGLSDGSGLAEPKFYVNISQFTDSWGRPQRDGPALRASALIAYGNSLISSDKQSVVKANIWPIVQNDLSYVGQYWNQTGFDLWEEVQGSSFFTVAVQHKALVEGDAFAKALGEECQACSVAPQILCHLQDFWNGSAVLSNLPTNGRSGLDTNSLLGSIHTFDPAAACDDTTFQPCSSRALSNHKLVVDSFRSVYGINNGRGAGKAAAVGRYAEDTYQGGNPWYLTTLVAAELLYDALYQWDKQGQVNVTETSLPFFKDLSSNVTTGSYAKSSSAYESLTSAVKTYADGFISVVQEYTPDGGALAEQYSRDQGTPVSASDLTWSYAAFLSAVGRRNGTVPASWGSSTANAVPSQCSGGTVSGSYTTPTVGSW
Protein: Acyl-coenzyme A thioesterase 1 (Acyl-CoA thioesterase 1) (EC 3.1.2.-) (CTE-I) (CTE-Ib) (Inducible cytosolic acyl-coenzyme A thioester hydrolase) (Long chain acyl-CoA thioester hydrolase) (Long chain acyl-CoA hydrolase) (Palmitoyl-coenzyme A thioesterase) (EC 3.1.2.2) (Q86TX2)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16940157}.
Interaction partners:
- Cytosolic acyl coenzyme A thioester hydrolase
- Acyl-coenzyme A thioesterase 2, mitochondrial
- Acyl-coenzyme A thioesterase 8
- Acyl-coenzyme A thioesterase THEM5
- Acyl-coenzyme A thioesterase THEM4
- Fructose-1,6-bisphosphatase isozyme 2
- ATP-dependent 6-phosphofructokinase, muscle type
- Very-long-chain enoyl-CoA reductase
- ATP-dependent 6-phosphofructokinase, liver type
- Peroxisomal succinyl-coenzyme A thioesterase
Sequence:
MAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLGELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGRLLCRVRHERYFLPPGVRREPVRAGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLLAGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAVNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSVANVGGTLRYKGETLPPVGVNRNRIKVTKDGYADIVDVLNSPLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPETGHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIPSKV
Protein: Venom prothrombin activator omicarin-C catalytic subunit (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Omicarin-C catalytic subunit light chain; Omicarin-C catalytic subunit heavy chain] (Q58L95)
Organism: Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota)
Function: Snake prothrombin activator that attacks the hemostatic system of prey. This catalytic subunit is functionally similar to blood coagulation factor Xa. It requires a non-catalytic subunit present in the venom, which is similar to coagulation factor Va, to be fully active (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MAPQLLLCLILTFLWSLPEAESNVFLKSKVANRFLQRTKRANSLFEEFRSGNIERECIEERCSKEEAREVFEDDEKTETFWNVYVDGDQCSSNPCHYRGTCKDGIGSYTCTCLFGYEGKNCERVLYKSCRVDNGNCWHFCKPVQNDIQCSCAEGYLLGEDGHSCVAGGNFSCGRNIKTRNKREASLPDFVQSQNATLLKKSDNPSPDIRIVNGMDCKLGECPWQAVLVDEKEGVFCGGTILSPIYVLTAAHCINQTEKISVVVGEIDKSRVETGHLLSVDKIYVHKKFVPPKKGYKFYEKFDLVSYDYDIAIIQMKTPIQFSENVVPACLPTADFANQVLMKQDFGIISGFGRIFEKGPKSNTLKVLKVPYVDRHTCMVSSESPITPTMFCAGYDTLPRDACQGDSGGPHITAYRDTHFITGIVSWGEGCAKKGKYGIYTKVSKFILWIKRIMRQKLPSTESSTGRL
Protein: DUF4185 domain-containing protein (O69675)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MLRIGPTAGTGTPTGDYGIGATDLCEFVEFPSQLLQVCGDSFAGQGVGFGGWYAPVALHVDTESIDDPAGVRYTGVTGVGTPLLADPTPPGDSQLPAGVVQINRRNYLMVTTTKDLQPQNSRLVRAEAARGGWQTVSGSRRNAAYQDGRQTQISGYYDPVPTPDSPTGWVYIVADSFTRGEPAVLYRATPESFTDRSRWQGWAGGPDGGWNKPPTPLWPDQLGEMSIRQIDGQTVLSYFNASTGNMEVRVAHHPTSLGAAPVTTVVRHDEWPEPAESLPPPYDNRLAQPYGGYISPGSTIDELRIFVSQWDTRARQNGPYRVIQFAVNPFKPWSDP
Protein: Slr0848 protein (Q55436)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Phosphopantetheine adenylyltransferase
- Penicillin-binding protein 1B
- Ribosomal RNA small subunit methyltransferase G
- Penicillin-binding protein 1A
- Penicillin-binding protein 1B
- Pyridoxal phosphate homeostasis protein
Sequence:
MTRRESANPEVTENSAVVPGQTVDFDIQQQLAELQELLYDSFHIPLTAWSVVDEEKILDQIDVIAEFIPGAVHRAIAILEREQQILQGAELEAQRMIEVAHQEAQRIKDESGIIQKAQYEADQYKAQVQQDCDALQRQVQQECEALQRQTQQECDTLRRQTMGELEQIKQVTHQEIQQFRQQTVQECEALQKQTEQEATEMQRDVDTYADRLLSRLEGELGQMMRSVSQSRQILYENSAEHNATITNRPPVATPSPVLPPSPGPKPPRGDRPRRRSR
Protein: 5-hydroxytryptamine (Serotonin) receptor 2A, isoform A (Q9VN38)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MEMQSYSGRGPSTGTSETATATAAVASASASDTAATFTLRHFNCRLEEADWPGPRQPFIDCEGSHTNSTSYTPSSLPTSKNLIEGPNNTFQCARQAIDEAEHNAFYSCDGESPLSENCTLRLKARLLRWPYEAYEHIRLAINGALSDYASDKLSDSSSCDEGGMVLQCKLGQAHELLLCHLQQLEREPLREVGSAEESFSNDSLLQAFQIELGAERDGLWSFLNLSELMEPDHGFLGIMNVTNTSLDMFLPNLTALNTTSTASTADMATEFAVTKSFLDYSPHGYDFLFLFVVFFIFAGGLGNILVCLAVALDRKLQNVTNYFLFSLAIADLLVSLFVMPMGAIPAFLGYWPLGFTWCNIYVTCDVLACSSSILHMCFISLGRYMGIRNPLGSRHRSTKRLTGIKIAIVWVMAMMVSSSITVLGLVNEKNIMPEPNICVINNRAFFVFGSLVAFYIPMLMMVTTYALTIPLLRKKARFAAEHPESELFRRLGGRFTLRPQHSQQQLQMFSSFSGSNNKFLSMGDGNRNFNTEGEMEEGGAPSRRSGVEPAERPLMQQRTASSRSMGTVSFRNVVNGTSGAAGSGRRTTGTAHSSFRFSGAGIFRHSSSSPASSCHSTSTSRSSSFWRKHGGYPNLMDRLAIHLRLSLVPPSSHPNRRASVRVTISQPQLGYPTNVGGNGGRTVGATEVGAGGNGSSAGRTSNSSLGGTSLMKIATIQGPILNQSQAAGGNHMVQKVKPTALKPEEPQRNKVRPFKFAFNRVATPTLNLRFLNNRSKRNSLSANAVATEQKATKVLGLVFFTFVLCWSPFFILNIIFAACPECQVPEHVVNTCLWLGYVSSTINPIIYTIFNRTFRAAFIRLLKCNCKR
Protein: CUGBP Elav-like family member 3 (CELF-3) (Bruno-like protein 1) (CUG-BP- and ETR-3-like factor 3) (ELAV-type RNA-binding protein 1) (ETR-1) (RNA-binding protein BRUNOL-1) (Trinucleotide repeat-containing gene 4 protein) (Q8CIN6)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein involved in the regulation of pre-mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Activates the splicing of MAPT/Tau exon 10. Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MKEPDAIKLFVGQIPRHLEEKDLKPIFEQFGRIFELTVIKDKYTGLHKGCAFLTYCARDSALKAQSALHEQKTLPGMNRPIQVKPADSESRGDRKLFVGMLGKQQTDEDVRKMFEPFGTIDECTVLRGPDGTSKGCAFVKFQTHAEAQAAINTLHSSRTLPGASSSLVVKFADTEKERGLRRMQQVATQLGMFSPIALQFGAYSAYTQALMQQQAALVAAHSAYLSPMATMAAVQMQHMAAISANGLIATPITPSSGTSTPPAIAATPVSAIPAALGVNGYSPVPTQPTGQPAPDALYPNGVHPYPAQSPAAPVDPLQQAYAGMQHYTAAYPAAYSLVAPAFPQPPALVAQQPPPPPQQQQQQQQQQQQQQQQREGPDGCNIFIYHLPQEFTDSEILQMFVPFGHVISAKVFVDRATNQSKCFGFVSFDNPASAQAAIQAMNGFQIGMKRLKVQLKRPKDANRPY
Protein: NADP-dependent alkenal double bond reductase P2 (EC 1.3.1.74) (Q39173)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reduction of the 7-8 double bond of phenylpropanal substrates, such as p-coumaryl aldehyde and coniferyl aldehyde (in vitro). Has activity towards toxic substrates, such as 4-hydroxy-(2E)-nonenal (in vitro) (By similarity). May play a distinct role in plant antioxidant defense and is possibly involved in NAD(P)/NAD(P)h homeostasis.
Interaction partners:
- NADPH-dependent alkenal/one oxidoreductase, chloroplastic
- DNA polymerase V family
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- At1g25420/F2J7_16
Sequence:
MTTNKQVIFKDHVSGFPKESDFNFTTTTVELRVPEGSKSVLVKNLYLSCDPYMRSRMGKPDPSSALAQAYAPGKPIYGYGVSRVIESGHPDYKKGDLLWGIVGWEEYSVITPMAHMHFKIQHTDVPLSYYTGLLGMPGMTAYAGFYEVCSPKKGETVYVSAASGAVGQLVGQFAKMMGCYVVGSAGSKEKVDLLKTKFGFDDAFNYKEESDLSAALKRCFPKGIDMYFENVGGKMLDAVLLNMNPHGRIAVCGMISQYNLENQEGVHNLSNIIYKRIRIQGFVVADFYDKYPKFLELVLPRIKEGKITYVEDVADGLEKAPEALVGLFHGKNVGKQVVVIARE
Protein: Cutinase 1 (EC 3.1.1.74) (Cutin hydrolase 1) (P00590)
Organism: Fusarium vanettenii (Neocosmospora pisi)
Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (Ref.4).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P11373}.
Interaction partners:
Sequence:
MKFFALTTLLAATASALPTSNPAQELEARQLGRTTRDDLINGNSASCRDVIFIYARGSTETGNLGTLGPSIASNLESAFGKDGVWIQGVGGAYRATLGDNALPRGTSSAAIREMLGLFQQANTKCPDATLIAGGYSQGAALAAASIEDLDSAIRDKIAGTVLFGYTKNLQNRGRIPNYPADRTKVFCNTGDLVCTGSLIVAAPHLAYGPDARGPAPEFLIEKVRAVRGSA