wanglab/gogpt-training-data huggingface dataset:
Protein: OCIA domain-containing protein 1 (OCAD1) (Q9W1X9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Maintains stem cell potency. Involved in endocytic pathways that mediate signaling during hematopoiesis.
Subcellular location: Endosome {ECO:0000269|PubMed:22110713}.
Interaction partners:
- ADP-ribosylation factor 1
- peptidyl-tRNA hydrolase
Sequence:
MDSPLNDGSHHPPPHAPHPLADYQFSAEEVKALRECNTESFFQRSLPFGTGLGLLAYFGVKNGYLQGHVKYGAVPKVVMGVILGYFVGKFSYQQKCAEKIMRLPNSHLGELLRQRRQGGGVISSITPDENLGRAFTLAPFSPSSADVYSDEAYQPGRSTSLNLDTESRPTLSGLDDIYRPTLDSGSMLEAELPLEPSKPGQSYEDLRRRNREEYSKHQQSPYSRPYEPPVAVQQRPVEQAQSEPAGRKNQYGDSWTD
Protein: tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase (EC 2.1.1.205) (2'-O-ribose RNA methyltransferase TRM7) (tRNA methylase 7) (P38238)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of tRNA(Phe), tRNA(Trp) and tRNA(Leu(UAA)). Requires TRM732 for methylation of the cytidine at position 32 and RTT10/TRM734 for methylation of the nucleotides at position 34 in substrate tRNAs. Lack of either of these modifications in tRNA(Phe) reduces formation of wybutosine from 1-methylguanosine at position 37.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03162, ECO:0000269|PubMed:14562095}.
Interaction partners:
- tRNA
- tRNA
- Multisite-specific tRNA:
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA dimethylallyltransferase
- tRNA
- Multisubstrate pseudouridine synthase 7
Sequence:
MGKSSKDKRDLYYRKAKEQGYRARSAFKLLQLNDQFHFLDDPNLKRVVDLCAAPGSWSQVLSRKLFDESPSSDKEDRKIVSVDLQPMSPIPHVTTLQADITHPKTLARILKLFGNEKADFVCSDGAPDVTGLHDLDEYVQQQLIMSALQLTACILKKGGTFVAKIFRGRDIDMLYSQLGYLFDKIVCAKPRSSRGTSLEAFIVCLGYNPPSNWTPKLDVNTSVDEFFQGCFLNKLCISDKLSHWNEEERNIAEFMACGSLQSFDSDATYHDLPSSVAGTSSSLDPVQSPTNPPYKKALELKRSGKLTRSV
Protein: Farnesyltransferase, putative (EC 2.5.1.21) (Q57YR9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Lanosterol 14-alpha-demethylase
- NAD
- Squalene monooxygenase
- Farnesyl pyrophosphate synthase
- C-5 sterol desaturase, putative
- Lathosterol oxidase, putative
- Methyltransferase
- Hydroxymethylglutaryl-CoA synthase
- Farnesyl pyrophosphate synthetase, putative
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Sequence:
MDYVSELYAMIRVRWQMRRMAGELQADDEDLRFCYDVLRDVSRSFALVIMQLKAALRDAVCVFYLVLRALDTVEDDMQLPLEFKLRELPLFHTRLHDHTWRLDGVGEGRERELLQKFPHVSAAFSRLDPSFQSVIEDICRRMADGMCDFLQRTDTCKANNKEISEDNCHDGKSEKSAVETREDFDLYCHYVAGLVGLGLTQLFVRSGLEKAALEENMTRANHMGLLLQKTNIIRDFYEDICESPPRVFWPREIWGQYTDDLHAFKGITRPTNGSNDTACGEGRKYSDEEKEIIKSKAVDCLNAMVADALVHLPPVIEYLAELRDPTVFAFCAIPQVMAVATLALVFDNPDVFHSRVKLTRGATCKIIHNATELSAALKLVRTYAQKLLASAHAGVASHEAVAQSLQVAIKTMDEQVLRHNTKLVEGPTRRVLAQYSALGGGLLLKVVDGVFGYLGR
Protein: LIM domain binding 1 (A0A8I6G409)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGSVPFSLSGCSSKSFKLYSPKEPPNGNAFPPFHPGTMLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKEAFHSNFVSLDCDQGSMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQQPSKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQFDAANGIDDEDSFNNSPALGANSPWNSKPPSSQESKSENPTSQASQ
Protein: Snaclec coagulation factor IX/factor X-binding protein subunit B (IX/X-bp subunit B) (P23807)
Organism: Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
Function: When linked to subunit A of IX/X-bp, anticoagulant protein which binds to the gamma-carboxyglutamic acid-domain regions of factors IX (F9) and factor X (10) in the presence of calcium with a 1 to 1 stoichiometry.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MGRFIFMSFGFLVVFLSLSGTAADCPSDWSSYEGHCYKPFSEPKNWADAENFCTQQHAGGHLVSFQSSEEADFVVKLAFQTFGHSIFWMGLSNVWNQCNWQWSNAAMLRYKAWAEESYCVYFKSTNNKWRSRACRMMAQFVCEFQA
Protein: Mitochondrial-processing peptidase subunit alpha (Alpha-MPP) (Inactive zinc metalloprotease alpha) (P-55) (Q10713)
Organism: Homo sapiens (Human)
Function: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P20069}. Mitochondrion inner membrane {ECO:0000269|PubMed:25808372}.
Interaction partners:
- Mitochondrial-processing peptidase subunit beta
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit 1, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
Sequence:
MAAVVLAATRLLRGSGSWGCSRLRFGPPAYRRFSSGGAYPNIPLSSPLPGVPKPVFATVDGQEKFETKVTTLDNGLRVASQNKFGQFCTVGILINSGSRYEAKYLSGIAHFLEKLAFSSTARFDSKDEILLTLEKHGGICDCQTSRDTTMYAVSADSKGLDTVVALLADVVLQPRLTDEEVEMTRMAVQFELEDLNLRPDPEPLLTEMIHEAAYRENTVGLHRFCPTENVAKINREVLHSYLRNYYTPDRMVLAGVGVEHEHLVDCARKYLLGVQPAWGSAEAVDIDRSVAQYTGGIAKLERDMSNVSLGPTPIPELTHIMVGLESCSFLEEDFIPFAVLNMMMGGGGSFSAGGPGKGMFSRLYLNVLNRHHWMYNATSYHHSYEDTGLLCIHASADPRQVREMVEIITKEFILMGGTVDTVELERAKTQLTSMLMMNLESRPVIFEDVGRQVLATRSRKLPHELCTLIRNVKPEDVKRVASKMLRGKPAVAALGDLTDLPTYEHIQTALSSKDGRLPRTYRLFR
Protein: Protein anachronism (Q26307)
Organism: Drosophila melanogaster (Fruit fly)
Function: Negatively regulates proliferation of neuronal precursor cells, thereby controlling the timing of postembryonic neurogenesis.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MASAMRGEKCERSRIRELVLILSLITMAGDSRATPFDPSFFIEGVQSEVVNPFNRTILNRFNLTEEQILSIQNRSNPNMRDDSAQSSNQQYLQQVATQRLNDIFKRVQKAISNEPNGSASKEKAGFPICNAETTNPEDWSLGNNVTLQFASSVFISNNDDRLSSALLRLYKTNPGQTREHNPGQASTQPISTENPGNTAPNCAEQPPVGPQIRVTVSIVHQQRKKQRKKRTCNTAMLSSSSTGWVEIDVKCALAYWEQQHRQQLRQQQPLQPQLTASVVGILMIEVHDDEENLLRPGLYFAPPTCDQADIAVPWSVYRTEPFKSHLASWTLPRKPRLDIFFNGSNSMKNSYNTPKSRAFIESTTSNSPTIDNQLDESGEYESQQRVHAPLVHHRRHHHNHQQPESESESAQLEAEIEAEELMSSASNSEQQMEPISNHHRHRTGHHHPHHQLHQHHHHHHRHTKHHRIPAHKQE
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 (EC 3.1.4.11) (Phosphoinositide phospholipase C-beta-4) (Phospholipase C-beta-4) (PLC-beta-4) (Q15147)
Organism: Homo sapiens (Human)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction.
Subcellular location: Cell membrane {ECO:0000269|PubMed:35284927}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Guanine nucleotide-binding protein subunit alpha-14
- Protein kinase C gamma type
- Guanine nucleotide-binding protein subunit alpha-15
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- Guanine nucleotide-binding protein G
Sequence:
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWRSEGKEGQVLECSLINSIRSGAIPKDPKILAALEAVGKSENDLEGRIVCVCSGTDLVNISFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFMTNTNGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDENAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRLKPEVEKKQLEALRSMMEAGESASPANILEDDNEEEIESADQEEEAHPEFKFGNELSADDLGHKEAVANSVKKGLVTVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGTYVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKKFLSITEKRADQMRAMGIETSDIADVPSDTSKNDKKGKANTAKANVTPQSSSELRPTTTAALASGVEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEMKKETEIKIQTLTSDHKSKVKEIVAQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLLINAHEQQTQQLKLSHDRESKEMRAHQAKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQAKEMQQMVKLEAEMDRRPATVV
Protein: Xylan O-acetyltransferase 1 (EC 2.3.1.-) (Protein ESKIMO 1) (Protein trichome birefringence-like 29) (Q9LY46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Xylan acetyltransferase required for 2-O- and 3-O-monoacetylation of xylosyl residues in xylan. Catalyzes the 2-O-acetylation of xylan, followed by nonenzymatic acetyl migration to the O-3 position, resulting in products that are monoacetylated at both O-2 and O-3 positions. Is necessary for the formation of the functional xylem, which is required for water transport to aerial tissues. Acts as negative regulator of cold acclimation. Involved in water economy as well as salt tolerance. Regulated at the transcriptional level by NAC012/SND1 (Probable).
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
- Protein REDUCED WALL ACETYLATION 2
- Beta-1,4-xylosyltransferase IRX9
- Beta-1,4-xylosyltransferase IRX14
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 2
- Glucuronoxylan 4-O-methyltransferase 3
- Protein IRREGULAR XYLEM 15
- Probable galacturonosyltransferase 12
- Probable beta-1,4-xylosyltransferase IRX10
- Probable galacturonosyltransferase-like 1
Sequence:
MQPWRRKFPLFETGVTMKQRKNSNLSIFVVVFSVFLFGIFMYNEDVKSIAEFPFSTSKPHDVHDEATPITEITTLPVQESIKNSDPIQESIKNADSVQDSVKDVAEPVQEEVSKTEEVKKIELFAATEDEEDVELPPEECDLFTGEWVFDNETHPLYKEDQCEFLTAQVTCMRNGRRDSLYQNWRWQPRDCSLPKFKAKLLLEKLRNKRMMFVGDSLNRNQWESMVCLVQSVVPPGRKSLNKTGSLSVFRVEDYNATVEFYWAPFLVESNSDDPNMHSILNRIIMPESIEKHGVNWKGVDFLVFNTYIWWMNTFAMKVLRGSFDKGDTEYEEIERPVAYRRVMRTWGDWVERNIDPLRTTVFFASMSPLHIKSLDWENPDGIKCALETTPILNMSMPFSVGTDYRLFSVAENVTHSLNVPVYFLNITKLSEYRKDAHTSVHTIRQGKMLTPEQQADPNTYADCIHWCLPGLPDTWNEFLYTRIISRS
Protein: Dimethyladenosine transferase 1, mitochondrial (EC 2.1.1.-) (Mitochondrial 12S rRNA dimethylase 1) (Mitochondrial transcription factor B1) (h-mtTFB) (h-mtTFB1) (hTFB1M) (mtTFB1) (S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 1) (Q8WVM0)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11809803}.
Interaction partners:
- DNA-directed RNA polymerase, mitochondrial
- Transcription factor A, mitochondrial
- GTPase Era, mitochondrial
- Nitric oxide-associated protein 1
- Ribosome assembly protein METTL17, mitochondrial
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein mS38
Sequence:
MAASGKLSTCRLPPLPTIREIIKLLRLQAAKQLSQNFLLDLRLTDKIVRKAGNLTNAYVYEVGPGPGGITRSILNADVAELLVVEKDTRFIPGLQMLSDAAPGKLRIVHGDVLTFKVEKAFSESLKRPWEDDPPNVHIIGNLPFSVSTPLIIKWLENISCRDGPFVYGRTQMTLTFQKEVAERLAANTGSKQRSRLSVMAQYLCNVRHIFTIPGQAFVPKPEVDVGVVHFTPLIQPKIEQPFKLVEKVVQNVFQFRRKYCHRGLRMLFPEAQRLESTGRLLELADIDPTLRPRQLSISHFKSLCDVYRKMCDEDPQLFAYNFREELKRRKSKNEEKEEDDAENYRL
Protein: Splicing factor 1, isoform B (A0A0B4KG60)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSATPPDLLSLAASREVSAAVAVAASANGGSGRSADKERSRSRDRGRDKDKDRDKDRKKRDKDSRDRDSRRRDDRGDRDRDRERDRDSRSHRSKSRNYDDGDRRRKRSRSRDRDRDRKRDRDRDSRSRRSSSRGGRDDYDRSRRRRSRSRSYERRRNDRGSQRDQRDQHSQRSSRERTHVNPFDTSNSRNSLNQDHDQSRIPSLFDRQQGLETIREEGREQRFDLTQTIQELMGNAGGNKGFASFFNSQNSNDSTSNGAFDNSADSAAERKRKRKSRWGGSENDKTFIPGMPTILPSTLDPAQQEAYLVQFQIEEISRKLRTGDLGITQNPEERFDTVLSTPLSLSI
Protein: Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR8 (EC 3.1.3.95) (Myotubularin-related protein 8) (Phosphatidylinositol-3-phosphate phosphatase) (Q96EF0)
Organism: Homo sapiens (Human)
Function: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. In complex with MTMR9, negatively regulates autophagy.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:16787938}.
Interaction partners:
- Myotubularin-related protein 9
- Polyphosphoinositide phosphatase
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Inositol polyphosphate-4-phosphatase type I A
- Phosphatidylinositide phosphatase SAC2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol polyphosphate 4-phosphatase type II
- Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Phosphatidylinositol 3-kinase catalytic subunit type 3
Sequence:
MDHITVPKVENVKLVDRYVSKKPANGILYLTATHLIYVEASGAARKETWIALHHIATVEKLPITSLGCPLTLRCKNFRVAHFVLDSDLVCHEVYISLLKLSQPALPEDLYAFSYNPKSSKEMRESGWKLIDPISDFGRMGIPNRNWTITDANRNYEICSTYPPEIVVPKSVTLGTVVGSSKFRSKERVPVLSYLYKENNAAICRCSQPLSGFYTRCVDDELLLEAISQTNPGSQFMYVVDTRPKLNAMANRAAGKGYENEDNYANIRFRFMGIENIHVMRSSLQKLLEVCELKTPTMSEFLSGLESSGWLRHIKAIMDAGIFITKAVKVEKASVLVHCSDGWDRTAQVCSVASILLDPFYRTFKGLMILIEKEWISMGHKFSQRCGHLDGDSKEVSPIFTQFLDCIWQLMEQFPCAFEFNENFLLEIHDHVFSCQFGNFLGNCQKDREDLRVYEKTHSVWPFLVQRKPDFRNPLYKGFTMYGVLNPSTVPYNIQFWCGMYNRFDKGLQPKQSMLESLLEIKKQRAMLETDVHELEKKLKVRDEPPEEICTCSQLGNILSQHLGSPLTNPLGFMGINGDLNTLMENGTLSREGGLRAQMDQVKSQGADLHHNCCEIVGSLRAINISGDVGISEAMGISGDMCTFEATGFSKDLGICGAMDISEATGISGNLGISEARGFSGDMGILGDTGISKASTKEADYSKHQ
Protein: Peptidyl-prolyl cis-trans isomerase CYP19-1 (PPIase CYP19-1) (EC 5.2.1.8) (Cyclophilin of 19 kDa 1) (Rotamase cyclophilin-3) (Q38900)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in reactive oxygen species production in response to pathogen infection.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24440291}.
Interaction partners:
- UPF0235 protein At5g63440
- Germin-like protein subfamily 1 member 15
- AT4g26130/F20B18_240
- Cysteine proteinase RD21A
- At1g09850
- Probable cysteine protease RD21B
- Probable cysteine protease RD21C
- Nuclear protein
- F14J8.16 protein
- Pre-mRNA-splicing factor SYF2
Sequence:
MATNPKVYFDMTVGGKSAGRIVMELYADTTPETAENFRALCTGERGIGKQGKPLHYKGSSFHRVIPKFMCQGGDFTAGNGTGGESIYGSKFKDENFIKKHTGPGILSMANAGANTNGSQFFICTEKTSWLDGKHVVFGQVVEGLNVVRDIEKVGSDSGRTSKPVVIADCGQIS
Protein: E3 ubiquitin-protein ligase gid2 (EC 2.3.2.27) (GID complex catalytic subunit 2) (Glucose-induced degradation protein 2) (O59668)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- GID complex subunit 9
- GID complex subunit 1
- GID complex subunit 8
- GID complex subunit 7
- GID complex substrate-recognition subunit 4
- SPRY domain-containing protein C285.10c
- GID complex substrate-recognition subunit 10
- Protein yippee-like PJ691.02
- GID complex subunit 5
- Uncharacterized protein C1604.12
Sequence:
MNIDEWQRIEETAPGNKCLAKLNELESILKDAKKSCLKDPTTSMKELVACSEKTQQVFDDLKRTEKKFHTSLNRFGKTLEKKFNFDLEDIKLHSSFESKKREIDTALSLHFFRQGDVELAHLFCKEAGIEEPSESLHVFTLLKSIVQGIRDKDLKLPIEWASQCRGYLERKGSSLEYTLQKYRLVSNYLTTKDIMAAIRYCRTNMAEFQKKHLADIQKTMIALFFCSRNEVLSGTNDSHDSIHHIISNNAQLNIPQEYIDVLDLDWKSLELLFVREFCAALGMSLESPLDIVVNAGAIALPILLKMSSIMKKKHTEWTSQGELPVEIFLPSSYHFHSVFTCPVSKEQATEENPPMMMSCGHVIVKESLRQLSRNGSQRFKCPYCPNENVAADAIRVYF
Protein: Ras GTPase-activating-like protein gapA (IQGAP-related protein gapA) (O00899)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Part of signaling pathway that is required for completion of cytokinesis. gapA and rgaA control cortexillin localization to the cleavage furrow and hence may be involved in cleavage of the midbody in the final stage of cytokinesis by regulating the actin cytoskeleton. Forms a complex by linking activated rac1A to ctxA in the absence of rgaA. Assembly of this complex is necessary for the recruitment of cortexillin to the midzone of the dividing cell.
Interaction partners:
- Myosin-2 heavy chain
- Cortexillin-2
- Cortexillin-1
- Rho-related protein rac1A
- Ras-like protein rasG
- Serine/threonine-protein kinase pakB
- Calmodulin
- Calmodulin-like protein
- Myosin-ID light chain
- Myosin, essential light chain
Sequence:
MEGLEIEDEDVILLDEDDDSSSSSTVNNSSSNIKNNGNTNNNIGNDDSNKVTLMTSLREKGWGSGMLVDKEKNQYGTIKSYKDDKSSPWFEERQVIATLYKARVLLHEMIYTKMNQERLLSGNLCVGEIQSLLNTQKEDVETDWIAEIQELKRNMVAEIRRNHLLERDVNKLDKRIALLIKHRSNIKDLLLEQNKGKKDKKKKGDDKAEYITLDQKQLESYQNLFYLLQTEPHYLAKLVTLIQADQMEDFLDTVFLTLFGDDFSPREEFLILSLFRLAIGQEMSRIKSAGDLLAVESVVPKMIITYTRRKQGHEFLKQIIAPILENNVVNAPDLNLELNAVQVYQNMISEQEIQTGAKSTLNRGLAEDQIIQLKEVQSILEPRVEKCIQICERFFTGIIQSLNRLPYGIRWICKQIQSIAQKNFDSKPDEIAKVIGYFVYYRFINLAIVTPDAFEILDKELSITSRKNLVNIAKVLQNLFTLKTFQNQGSERWMQPLNKWILSKTSIVRQYLEDLIQVTDPSEYLRVDKYNELTLKLNPVVVISLGEISQTHRLLIANLAALKMKEKEDPLELILKALPAPLEVVDENDREIQLTLINRFKENIEKEISISASLLAETKELVISVLRSIPIQQKQQQQQHDDEKRDDLISILQNAIKHGKETNNPQLSSNAEKIINNLKKMEAEGSIQSENNQYEGFIKVIALEVINRQEIREQQRKERMRLTIALRDLRKHQSYLNDQIQHYTSYLKDVLLHYGPKDKKKSTKPMKISFKELTKKGVIVESDIPKLSHGSTSFYISSDAPGIFDIEARIGVASVGTLSLSLDDLLDKSSAGIPYLKLENIVLDVNMTLHLLNRHFLKNI
Protein: Ribulose-phosphate 3-epimerase (EC 5.1.3.1) (Pentose-5-phosphate 3-epimerase) (PPE) (R5P3E) (P0AG07)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
Interaction partners:
- Transketolase 1
- Transketolase 2
- Ribose-5-phosphate isomerase A
- 6-phosphogluconate dehydrogenase, decarboxylating
- Phosphoglycolate phosphatase
- Ribose-5-phosphate isomerase B
- Tryptophan--tRNA ligase
- Xylulose kinase
- Ribulokinase
- L-ribulose-5-phosphate 4-epimerase AraD
Sequence:
MKQYLIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGITAPIDVHLMVKPVDRIVPDFAAAGASIITFHPEASEHVDRTLQLIKENGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRRRIDESGFDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRSELAKVSHE
Protein: tryptophan--tRNA ligase (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (Q8SZU2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MFRFGKLHRSLSKVAKKGQTAVYSQRRCIQARSFLPGLASRTAGTPSATAQVTGGNKQHVHPHGNSVNSGHEEHNTRWPRKVFSGIQPTGSLHLGNYLGAVRKWVQLQNARDDVTVCIVDLHSITMPHNPPLLRENIFTMAATLLACGIDPTKSTLFVQSAVAEHAEFNWILSSLTTMPRLAQLPQFREKSRLLKDVPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQLAQHLARIYNGRYGETFPVCTAIIEDGDASRVLSLRDPSKKMSKSEANPKATINLCDSPDLITQKIKKAVTDFTSDITYNPGKRAGVSNLVNIHAQVTGQSIKTVVNEAATLDTAKYKDRVAEAVVEHLRPIREQIHHHMTKRNEMIYLLEVGAEKARQQARQTLNDVKQRLGLGTSANIPAAVHVAPLLPAPDISKTSASRRMSKDFDGNVHERHERMYGFGDQPSGGAGQSATGEVADMPQAVVPRVIRRAPIVPTQSMRVEKQLGSTRTRHVSRWTPAMLRI
Protein: Cytochrome c oxidase VIII (COX VIII), putative (Q583E7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIRRTAPAVSFTTSHRALMLRTNRPLLSADMHSLERFKVAWDEMPVHLIGASRKQSFEWYWKCMYQLGIRSTYRMTKSRVVMNWCAVFVFMYLTYISVCFSSFYHIYYQDWPEEFKRENARAYAQSKGSDVWAADGKFIKPYFHINPPMLTMTTEDL
Protein: Polypyrimidine tract binding protein (Q3T7F7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADEISATSMVSCYTVTPPQMRGRMVYVQFSNHRELKTDQGHNNSTAHSDYSVQSPASGSPVPLSAAANATSNNANSSSDSNSAMGILQNTSAVNAGGNTNAAGGPNTVLRVIVESLMYPVSLDILHQIFQRYGKVLKIVTFTKNNSFQALIQYPDANSAQHAKSLLDGQNIYNGCCTLRIDNSKLTALNVKYNNDKSRDFTNPALPPGEPGVDIMPTAGGLMNTNDLLLIAARQRPSLSGDKIVNGLGAPGVLPPFALGLGTPLTGGYNNALPNLAAFSLANSGALQTTAPAMRGYSNVLLVSNLNEEMVTPDALFTLFGVYGDVQRVKILYNKKDSALIQMAEPQQAYLAMSHLDKLRLWGKPIRVMASKHQAVQLPKEGQPDAGLTRDYSQNPLHRFKKPGSKNYQNIYPPSATLHLSNIPSSCSEDDIKEAFTSNSFEVKAFKFFPKDRKMVLLQLLSVEEAVLALIKMHNHQLSESNHLRVSFSKSNI
Protein: DMalpha1 (Plp1a protein) (Proteolipid protein 1a) (Q8UUT6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Proteolipid protein 2
- Transcription factor SOX-10
- Myelin protein P0 precursor
- Myelin basic protein
- Oligodendrocyte lineage transcription factor 2.
- 2',3'-cyclic nucleotide 3' phosphodiesterase.
- Oligodendrocyte transcription factor 1
- Glial fibrillary acidic protein
- Myelin regulatory factor.
Sequence:
MGCYECCMRCLGGVPYVSLAATLLCFSGIALFCGCGHQALTESERLIETYFARDNQDYYTLVYLIEYFQYIIYGLASFFFLYCIVLLAEGFYTTSAVRQSLGEFRSTVCGRCLSTTFIVITYFLVVVWLLVFSLSAFPVYFFYNMAKTCQTINFLSETPSSINQLCIDARQYGLLPWTAIPGKACGMTLSNVCKTREFSLTYNLYIAAFAGAGMTVLALLTYTVSTTYNFAVLRYLGRKGISPRC
Protein: Hemagglutinin-esterase (HE protein) (EC 3.1.1.53) (E3 glycoprotein) (P30215)
Organism: Human coronavirus OC43 (HCoV-OC43)
Function: Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-4-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. May become a target for both the humoral and the cellular branches of the immune system.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04207}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04207}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04207}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04207}. Note=In infected cells becomes incorporated into the envelope of virions during virus assembly at the endoplasmic reticulum and cis Golgi. However, some may escape incorporation into virions and subsequently migrate to the cell surface. {ECO:0000255|HAMAP-Rule:MF_04207}.
Interaction partners:
Sequence:
MFLLPRFILVSCIIGSLGFYNPPTNVVSHVNGDWFLFGDSRSDCNHIVNINPHNYSYMDLNPVLCDSGKISSKAGNSIFRSFHFTDFYNYTGEGQQIIFYEGVNFTPYHAFKCNRSGSNDIWMQNKGLFYTQVYKNMAVYRSLTFVNVPYVYNGSAQSTALCKSGSLVLNNPAYIAPQANSGDYYYKVEADFYLSGCDEYIVPLCIFNGKFLSNTKYYDDSQYYFNKDTGVIYGLNSTETITTGFDLNCYYLVLPSGNYLAISNELLLTVPTKAICLNKRKDFTPVQVVDSRWNNARQSDNMTAVACQPPYCYFRNSTTNYVGVYDINHGDAGFTSILSGLLYNSPCFSQQGVFRYDNVSSVWPLYPYGRCPTAADINNPDLPICVYDPLPVILLGILLGVAVIIIVVLLLYFMVDNGTRLHDA