wanglab/gogpt-training-data huggingface dataset:
Protein: Protein Rep68 (EC 3.6.4.12) (P03132)
Organism: Adeno-associated virus 2 (isolate Srivastava/1982) (AAV-2)
Function: Plays an essential role in the initiation of viral DNA synthesis. Binds specifically to an inverted terminal repeat element (ITR) on the 3' and 5' ends of the viral DNA, where it cleaves a site specifically to generate a priming site for initiation of the synthesis of a complementary strand. Also plays a role as transcriptional regulator, DNA helicase and as key factor in site-specific integration of the viral genome. Inhibits the host cell cycle G1/S and G2/M transitions. These arrests may provide essential cellular factors for viral DNA replication.
Subcellular location: Host nucleus {ECO:0000255|PROSITE-ProRule:PRU01366}.
Interaction partners:
Sequence:
MPGFYEIVIKVPSDLDGHLPGISDSFVNWVAEKEWELPPDSDMDLNLIEQAPLTVAEKLQRDFLTEWRRVSKAPEALFFVQFEKGESYFHMHVLVETTGVKSMVLGRFLSQIREKLIQRIYRGIEPTLPNWFAVTKTRNGAGGGNKVVDECYIPNYLLPKTQPELQWAWTNMEQYLSACLNLTERKRLVAQHLTHVSQTQEQNKENQNPNSDAPVIRSKTSARYMELVGWLVDKGITSEKQWIQEDQASYISFNAASNSRSQIKAALDNAGKIMSLTKTAPDYLVGQQPVEDISSNRIYKILELNGYDPQYAASVFLGWATKKFGKRNTIWLFGPATTGKTNIAEAIAHTVPFYGCVNWTNENFPFNDCVDKMVIWWEEGKMTAKVVESAKAILGGSKVRVDQKCKSSAQIDPTPVIVTSNTNMCAVIDGNSTTFEHQQPLQDRMFKFELTRRLDHDFGKVTKQEVKDFFRWAKDHVVEVEHEFYVKKGGAKKRPAPSDADISEPKRVRESVAQPSTSDAEASINYADRLARGHSL
Protein: Receptor-like kinase TMK4 (EC 2.7.11.1) (BAK1-associating receptor-like kinase 1) (Leucine-rich repeat receptor-like kinases TMK4) (Transmembrane kinase 4) (Q9LK43)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in auxin signal transduction and cell expansion and proliferation regulation. May be involved in brassinosteroid-mediated plant growth and development via auxin regulation. May be involved in microspore and pollen development.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At5g01110
- Transmembrane protein
- Plant intracellular Ras-group-related LRR protein 7
- Plant intracellular Ras-group-related LRR protein 4
- Plant intracellular Ras-group-related LRR protein 6
- Plant intracellular Ras-group-related LRR protein 8
- Plant intracellular Ras-group-related LRR protein 5
- Plant intracellular Ras-group-related LRR protein 3
Sequence:
MEAPTPLLLLVLLTTITFFTTSVADDQTAMLALAKSFNPPPSDWSSTTDFCKWSGVRCTGGRVTTISLADKSLTGFIAPEISTLSELKSVSIQRNKLSGTIPSFAKLSSLQEIYMDENNFVGVETGAFAGLTSLQILSLSDNNNITTWSFPSELVDSTSLTTIYLDNTNIAGVLPDIFDSLASLQNLRLSYNNITGVLPPSLGKSSIQNLWINNQDLGMSGTIEVLSSMTSLSQAWLHKNHFFGPIPDLSKSENLFDLQLRDNDLTGIVPPTLLTLASLKNISLDNNKFQGPLPLFSPEVKVTIDHNVFCTTKAGQSCSPQVMTLLAVAGGLGYPSMLAESWQGDDACSGWAYVSCDSAGKNVVTLNLGKHGFTGFISPAIANLTSLKSLYLNGNDLTGVIPKELTFMTSLQLIDVSNNNLRGEIPKFPATVKFSYKPGNALLGTNGGDGSSPGTGGASGGPGGSSGGGGSKVGVIVGVIVAVLVFLAILGFVVYKFVMKRKYGRFNRTDPEKVGKILVSDAVSNGGSGNGGYANGHGANNFNALNSPSSGDNSDRFLLEGGSVTIPMEVLRQVTNNFSEDNILGRGGFGVVYAGELHDGTKTAVKRMECAAMGNKGMSEFQAEIAVLTKVRHRHLVALLGYCVNGNERLLVYEYMPQGNLGQHLFEWSELGYSPLTWKQRVSIALDVARGVEYLHSLAQQSFIHRDLKPSNILLGDDMRAKVADFGLVKNAPDGKYSVETRLAGTFGYLAPEYAATGRVTTKVDVYAFGVVLMEILTGRKALDDSLPDERSHLVTWFRRILINKENIPKALDQTLEADEETMESIYRVAELAGHCTAREPQQRPDMGHAVNVLGPLVEKWKPSCQEEEESFGIDVNMSLPQALQRWQNEGTSSSTMFHGDFSYSQTQSSIPPKASGFPNTFDSADGR
Protein: Transcriptional corepressor Atro (Q8T9N4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAASTQGEIRVGPGHQVNDVYAKLPDYNPISSFPIDKETDERELEESRWSPGVVADGDLLMFLRAARSMAAFQGMCDGGLEDGCLAASRDDTTINALDVLHDSGYDPGKALQALVKCPVSKGIDKKWTEDETKKFIKGLRQFGKNFFRIHKDLLPHKDTPELVEFYYLWKKTPGANNNRPHRRRRQSALRRNRVTRANNSNSNTPPKKEDTPEPQTATTATAAATAASETASRSSPAVSKEENSSLTEDDASECDSDSSLTHKRDESPSRMRTRNKQQNNNSSTSSGNNTAGNGGGNATSISSGSTGGGAAGGNSSSKDQSANAVANGKRPKRGSETPDVSGGASVDSPKTPTKAVAESSANKRKGGKQDTPNKKKRTEQESNEPSAHEENAIKEKRKRPDSPVESMNSDSRPDSVLDDGESNTTDTTTAEQQSTKDSKETVSCKEEREMVTNDLEAKAEEKAIKAEALAEDSKDSAIKNMDEETNIQAPSSADTSLVDGPNPNALPSPVAAPITMKVPTIATVEALNASVDRKEAIEKMESCDSDPEMLKKLATIKQEVSPQQQQHMQQQSQQQMQQQLAPVGIPQPPSCPPSESVYIKKEPMEDSMDATCNQNSNEPQDLKVKIEIKNEDALKHSAGGLPPSGPCAPPSALHPLSGAPVESGQEPLHLQHMPHGQVTTQPPPGYLIDGQLKYGPSGQGVPPQPPQLHSDAAGGVSGAPPGAPTTPQKYPPEMEMKFAPQDLKYPPPPPLDALKYSQEMQAAAAAAAAAGKYDMKYMMEQQGKYNVELSAAHQPPSKPGYQDSLKIPDIKPGFGHLPHNVGSPLDAAHKYGPPPTSQESQQQQPQPPAHQVPPGATPPPGIAMPKPHYQHDVQTPPLGRPFEPTGLMLKYGDPLAAKYGPPQDLKYPMPPVSQAGPADVKPYGGENLIKSSPYGPPPESPIDASARSTPGQDSQGSNSNSQPPSMPPQPQQFQSPHPSPHMPSPAGGGLPPGMHPQNLIHGPPPGAAGGSGPQPPPPPTSLHQPTPTSAGPPSLQHGLHPGHQHSQLSAASSIPPSSIGIPPTLSTMAPSHMHPHLHPHAHLQGLHRPHDLPPSMHPHAPMPLSLQGHPQHGHGLPPSHTSQQQQQQQQQQQPGGPAGTVRTPSPAQQPPRSMHDPQSSREPPTSQPSTTMAGSSGPGGPPPQQSPHAHRTSPLPGLAGSGPPPPGLIGHPMAIHPHLAHLPPGHPAHAALAHPGHHLLSHSIAGLGPGGGPIALLAGPGGLGGIPESALSRRTPPSHLPHSHASSAPLTAHSVASMTSTSMSLTTSTVPSSAFSRASPSVQISSSGGGPSGPGSVGPGGMPNSSAAAAAAAAAHRAASPASSVSSLSRQSPLHPVPQSPLSHHPSSSALSAAAAAVAERDRHALMRQQSPHMTPPPVSNASLMASPLSKMYAPQPGQRGLGTSPPPHLRPGASPPVIRHPQMPLPLPLIAPGGGIPQIGVHPGQSPYPHPLLHPSVFYSPHHHPFNSPYGYAPYGPGFPAYMKPPPQPGQLDPAAVMAAHHAGLQGPPPQQMRQDEQNAAAAAAQAAAEKQHQAAAAAAAQQHKAPQQQQPGGMPPNKPPTPKTPQGPGGGMPPGMGGPGTPTGLPPGAYPGSHMPGYPQGPPHGSPFAPQDGQPHGLKPTSHMDALRAHAHSANSAGMGGGHHPTEPLPIDIEPDPEPEIPSPTHNIPRGPSPEAKPDDTECHRSQSAIFVRHIDRGDYNSCTRTDLIFKPVADSKLARKREERDRKLAEKERERRQQQQQQQQQQQQQQAAAAQQAAQQAKMKAELKPPYADTPALRQLSEYARPHVAFSPVEQMVPYHHPMGPMYRERELEEIKNAQAAAASQSRLDPHWMEYYRRGIHPSQFPLYANPAISQMERERLGIPPPHHVGLDPGEHMPQPPEAGFQLPPNVGQYPRPNMLIPREPHSDVLLRMSYADQLQYLQAAEFQRQSLHDQYFRQRPR
Protein: F-actin-capping protein subunit alpha-3 (CapZ alpha-3) (Q9WUV6)
Organism: Rattus norvegicus (Rat)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the morphogenesis of spermatid.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A0PFK5}.
Interaction partners:
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha-1
- F-actin-capping protein subunit alpha-2
- Dynactin subunit 2
- Actin-related protein 10
- Dynactin subunit 1
- Dynactin subunit 4
- Dynactin subunit 5
- Actin-related protein T2
- Capping protein regulator and myosin 1 linker 2
Sequence:
MSLSVLSRQDKEKVIHRLLIQAPPGEFVNAFDDLCLLIRDEKLMHHQGECAGHQHCQKYCVPLCIDGNPVLLSHHNVMGDFRFFDYQSKLSFRFDLLQNQLRDIQSHGIIRNENEYLRSVVMCALKLYVNDHYPNGNCNVLRKTVKNKEFLIACIEKHSYDNGECWNGLWKSKWIFQVNPFLTQVTGRIFVQAHYFRCVNLHVEVSKDLKESLEVVNQAQLALSFARLVEEQENKFQAAVIEELQELSNEALRKILRRDLPVTRTLIDWQRILSDLNLVMYPKLGYVIYSRSVLCNWII
Protein: Palmitoyltransferase ZDHHC4 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 4) (DHHC-4) (Zinc finger protein 374) (Q9NPG8)
Organism: Homo sapiens (Human)
Function: Palmitoyltransferase that could catalyze the addition of palmitate onto protein substrates including the D(2) dopamine receptor DRD2.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21926431}; Multi-pass membrane protein {ECO:0000305|PubMed:21926431}. Golgi apparatus membrane {ECO:0000269|PubMed:26535572}; Multi-pass membrane protein {ECO:0000305|PubMed:21926431}. Cell membrane {ECO:0000269|PubMed:26535572}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Acyl-CoA wax alcohol acyltransferase 2
Sequence:
MDFLVLFLFYLASVLMGLVLICVCSKTHSLKGLARGGAQIFSCIIPECLQRAVHGLLHYLFHTRNHTFIVLHLVLQGMVYTEYTWEVFGYCQELELSLHYLLLPYLLLGVNLFFFTLTCGTNPGIITKANELLFLHVYEFDEVMFPKNVRCSTCDLRKPARSKHCSVCNWCVHRFDHHCVWVNNCIGAWNIRYFLIYVLTLTASAATVAIVSTTFLVHLVVMSDLYQETYIDDLGHLHVMDTVFLIQYLFLTFPRIVFMLGFVVVLSFLLGGYLLFVLYLAATNQTTNEWYRGDWAWCQRCPLVAWPPSAEPQVHRNIHSHGLRSNLQEIFLPAFPCHERKKQE
Protein: Lymphocyte antigen 6D (Ly-6D) (E48 antigen) (Q14210)
Organism: Homo sapiens (Human)
Function: May act as a specification marker at earliest stage specification of lymphocytes between B- and T-cell development. Marks the earliest stage of B-cell specification.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
Sequence:
MRTALLLLAALAVATGPALTLRCHVCTSSSNCKHSVVCPASSRFCKTTNTVEPLRGNLVKKDCAESCTPSYTLQGQVSSGTSSTQCCQEDLCNEKLHNAAPTRTALAHSALSLGLALSLLAVILAPSL
Protein: GTP:AMP phosphotransferase AK3, mitochondrial (EC 2.7.4.10) (Adenylate kinase 3) (Q9WTP7)
Organism: Mus musculus (Mouse)
Function: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q9UIJ7, ECO:0000255|HAMAP-Rule:MF_03169}.
Interaction partners:
- Adenylate kinase 9
- Adenosine kinase
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase
- Nucleoside diphosphate kinase, mitochondrial
- Nucleoside diphosphate kinase B
- Pyruvate kinase PKM
- Nucleoside diphosphate kinase 3
- Ribonucleoside-diphosphate reductase large subunit
- Nucleoside diphosphate kinase A
Sequence:
MGASGRLLRAVIMGAPGSGKGTVSSRITKHFELKHLSSGDLLRQNMLQGTEIGVLAKTFIDQGKLIPDDVMTRLALHELKTLTQCSWLLDGFPRTLPQAEALDKVYQIDTVINLNVPFEVIKQRLTARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDDKPETVIKRLKAYEAQTEPVLQYYQKKGVLETFSGTETNKIWPHVYSFLQTKVPETTQKASVTP
Protein: Uncharacterized protein (Q384E2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
Sequence:
MSGPVSQLSNERLRELRAAVHSFLQDSSVYSSIRDIIDTYVTENPEGSVTASSSADVMKIIRERGLVQELLNKLQDEKRADAKNTITPCHLWKLLPGEYYLHVRLAGGKAFVDNLDIAPSVAQDYHMYVALQFGPHRYRSVSQDVSVDPPFRDEFLIHLDYKAFGTSALDLIEISTPFNLAVIREDRFLSTATMVGENVVDWRKVLRTGYLGLTVELCGENPGIPAGIIELQIEILPNKAPRFTDEEIVRRIELQRSGITSADREFLLYARRWWKEFQDIRPGHKQRRVKVFASTPSGRMVPTAHFVSVIRSERGIETPFDAARFVSLFAVTTEEHLTQEVLSGSGGNSSGATWVSLLTFLSQRRGDVCNHSTLLCSLLLGFGLDAYCAVGSDRKGKTTMFVVTRRRVVAGTFEVTLWEPTSGSRFLLTEPHPFETIGCMFTHRSFYANIQQSDFVVTTSFDVDNEELWKPMNPLKLRMVPKSPNPSLLWVSRDVKKLENELQGSLVREITNYRDARGIVSNIDERLSYVLSQALCAYENHRRRGTPEDLSLFESCVKGTIGDGKTFRGVPVNVTHLNSHKILAAFGESTSGREILELSADGLTLGIQVKVFPFPEEVLSVWVMLAAAYRSP
Protein: GTPase activating protein, putative (Q57XM7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ras-related protein Rab-7b
Sequence:
MDVGSKVFVDQLLSRVSFSDIISSHAHIVIEAHRGSGKKSPAGMLMLVRDDKHMNWASGRNKNSNNNTYVDISATAAELPSRGQPPREGSSQNVPAHTEDIFLVWVPYSYIPRECPKLLPAFPRNSPILGVTVVGKPGDSSTELSHITCIEMKCIDKIRRVASVGGKSVIEVYRLDSAEIVMLSFCQGGLTSFLAEMRVLSPMSQSHLDTNDFIVYGHHPKNLTTKFSSSEEERTTVMSHLNKLRSYTRSSFLNELWGTASGTGTPTALQPPTHETGDTRDMQIMLYGKKDSNPLATVATKLTNVFNSLLEPSPNSRDEFASNVEVDPSLLFPCSDTPPKGDERGDFFHGEGGVAAQISQVELQVPRISRCENLRQMGPRLTANEWNTCFVGDERRVDVERFEHAKIVAYMGGIDSDIRLEVWCFMLDVYGCHTSSTESQRQRVRDEYRRRYEVLTGQWKSIFPEQEENFTVFREARVAVEKDVLRTDRFLPAYADECGEKLCMLRNVLLSRVMLNLDLGYCQGMSDILSPIALLAQDEVEAFMIFSCFIANHCCNDILKDVKRGMEQHLTALRALVAFSAPLLFNHLRIQGADDMFFCFRWLLVLFKREFPVEDAMLLWDVIICCPYTPRFEIFVAAALLKAFTPQILEMNLSHDELLKFVNSASCQLDVRHVIVLSQDFYLEVAKHVTTLGGGMVFRRGRLPTLEEVLQILEGNTT
Protein: LIM zinc finger domain containing 2 (H0Y592)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XGVPICGACRRPIEGRVVNALGKQWHVEVSQAGGHVASGWGVPQLRVMHFVCAKCEKPFLGHRHYEKKGLAYCETHYNQLFGDVCYNCSHVIEGDVVSALNKAWCVSCFSCSTCNSKLTLKNKFVEFDMKPVCKRCYEKFPLELKKRLKKLSELTSRKAQPKATDLNSA
Protein: Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 2 (GGPP synthase 2) (GGPS2) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase 2) (Dimethylallyltranstransferase 2) (EC 2.5.1.1) (Farnesyl diphosphate synthase 2) (Farnesyltranstransferase 2) (EC 2.5.1.29) (Geranyltranstransferase 2) (EC 2.5.1.10) (O04046)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heterodimeric geranyl(geranyl)-diphosphate (GPP) synthase large subunit. In vitro, the large subunit catalyzes mainly the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate while the small subunit alone is inactive. Upon association of the two subunits, the product profile is not changed.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:10759500}.
Interaction partners:
- Phytoene synthase 1, chloroplastic
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Geranylgeranyl diphosphate reductase, chloroplastic
- Dehydrodolichyl diphosphate synthase 4
- Isopentenyl phosphate kinase
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- (Z)-gamma-bisabolene synthase 1 (Terpenoid synthase 12) (AtTPS12)
- Ent-copalyl diphosphate synthase, chloroplastic
- Farnesyl pyrophosphate synthase 1, mitochondrial
Sequence:
MEPQILFLYLSLFILSLNFFFTNLKPRLVRLFQPSLESRVKTALLSRKEVAAFLDSPIVEDEEGEEREEEEEGGIVSNANFTFEFDPYMMSKAESVNKALEEAIPVGEPLKIHEAMRYAILAAGKRVRPILCLASCELVGGQENAAMPAACAVEMIHTMSLIKDDLPCMDNDDLRRGKPTTHKVYGEGVAILSGGALLSLAFEHMTTAEISSERMVWAVRELARSIGTRGLVAGQAMDISSEGLDLNEVGLEHLEFIHVHKTAVLLETAAVLGAIIGGGSDEEIESVRKFARCIGLLFQVVDDILDETKSSEELGKTAGKDQLAGKLTYPKLIGLEKSKEFVKRLTKDARQHLQGFSSEKVAPLVALTTFIANRNK
Protein: Diacylglycerol O-acyltransferase 2 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase 2) (Q96PD7)
Organism: Homo sapiens (Human)
Function: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides (By similarity). Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14521909, ECO:0000269|PubMed:27184406}; Multi-pass membrane protein {ECO:0000269|PubMed:14521909}. Lipid droplet {ECO:0000269|PubMed:27184406}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27184406}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Long-chain fatty acid transport protein 1
- Phospholipid phosphatase 2
- Phospholipid phosphatase 3
- Phospholipid phosphatase 4
- Phospholipid phosphatase 5
- 2-acylglycerol O-acyltransferase 2
- 2-acylglycerol O-acyltransferase 1
- Patatin-like phospholipase domain-containing protein 2
- 2-acylglycerol O-acyltransferase 3
Sequence:
MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLNRSKVEKQLQVISVLQWVLSFLVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHTMYMEALVKLFDKHKTKFGLPETEVLEVN
Protein: Cytochrome P450 (EC 1.14.14.1) (Q9DEW9)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Interaction partners:
Sequence:
MLGSWLLVVFCVCLLFLFIRIQRPKNFPPGPRPIPIFGNLFQFNIKNPLKDFEKLAEQYGNICSLYIGTKPAVVLNGLKVIREALVTKSADFSGRPQNMLKDVTEGKGIVIADYGRQWKEHRRFALMTLRNFGLGKQSMENRILGEIEHLVAKLEKYAGSSMYPQTLFHDAASNIIYLVLFGTRYDYGDETLKVYVRLYSENAKLANGTWSIIYDALPILRSLPLPFKKAFDNYSTLKILTANMINKHRTTRVPGKPRDLVDCYLDEIDKKDNESTFSEEQLVVYIMNLHIAGTDTTSNTLLTSILYLMAHPDIQKRCQKEIDVVLEGNSQPSFEDRHNMPYTQAVVHECQRIARTVPLSVFHCTTRDTELMGYTIPKGTMIIPNLSSVLSEEGQWKFPHDFNPSNFLNEQGQFEKPEAFIPFSAGPRVCLGEGLARMELFLFLVTLLRRFQFIWPEDAGEPDFTPIFGLTLTPKPYRMGVKLRQPAREK
Protein: Possible oxidoreductase (O69692)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS14A
- Large ribosomal subunit protein uL4
Sequence:
MQNATMRVLVTGGTGFVGGWTAKAIADAGHSVRFLVRNPARLKTSVAKLGVDVSDFAVADISDRDSVREALNGCDAVVHSAALVATDPRETSRMLSTNMAGAQNVLGQAVELGMDPIVHVSSFTALFRPNLATLSADLPVAGGTDGYGQSKAQIEIYARGLQDAGAPVNITYPGMVLGPPVGDQFGEAGEGVRSALWMHVIPGRGAAWLIVDVRDVAALHAALLESGRGPRRYTAGGHRIPVPELAKILGGSPAPRCWPSRCPIPRCVSRDRCWIKPGPICLSILRSPRQVCSTTHRCRSPTIRRAKKN
Protein: U2 snRNP auxiliary factor small subunit (A8MRI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MYQRPDMITPGVDAQGQPLDPRKIQEHFEDFFEDLFEELGKFGEIESLNICDNLADHMIGNVYVQFKEEDQAAAALQALQGRFYSGRPIIADFSPVTDFREATCRQYEENNCNRGGYCNFMHVKLVSRELRRKLFGRYRRSYRRGSRSRSRSRSISPRNKRDNDRRDPSHREFSHRDRDREFYRHGSGKRSSERSERQERDGSRGRRQASPKRGGSPGGGREGSEERRARIEQWNREREEKEEGGA
Protein: Male germline specific protein (Q0GYU3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPHKKTKHLKAVVPGMISLEGEQFDPWEIPFPLPEQEDPSMCRDEYLKDLIREHESRVASLVVRSTVRDVSIVKRPVELQDTDVKEAEAMVVLQMAQKRQRTSVRRTMEEVIASIRLRSTIIADLIRQVQKAAIEFLSVRLLRQLRLFSMPWPGDLEETPNNLFSWSLDDFLLRLDVKQIYLDVLNRERSVKDLDCVKFCKDLSEIEHLIHEIRRDFRDDVDLCENSLHLLKNAQYHMNAPWVKSLNDNIENLASSASVALLNEQSGSLTSLRRNSSAMIVFERKSALNPIETRYQINWFKSCTDQRLTRMNERNVEIKRELQDLEVQAVQDEKVQYSSGLMYELEVGKLRESIRNWQDRLDTDLEHADVMCTVSRLALQKVKDDLKFYMEQKDMYLQRIKEVQALIDQERMIREERELAALKRMSRGSLRKSVPKSTKNFQKKSKGKSEKKSELKSEIKSDTKPEMKTERKSDLKAERKSKTMAEKSQRKSTNSKME
Protein: Signal transducer and activator of transcription 4 (Q14765)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator mainly expressed in hematopoietic cells that plays a critical role in cellular growth, differentiation and immune response. Plays a key role in the differentiation of T-helper 1 cells and the production of interferon-gamma. Participates also in multiple neutrophil functions including chemotaxis and production of the neutrophil extracellular traps (By similarity). After IL12 binding to its receptor IL12RB2, STAT4 interacts with the intracellular domain of IL12RB2 and becomes tyrosine phosphorylated. Phosphorylated STAT4 then homodimerizes and migrates to the nucleus where it can recognize STAT target sequences present in IL12 responsive genes. Although IL12 appears to be the predominant activating signal, STAT4 can also be phosphorylated and activated in response to IFN-gamma stimulation via JAK1 and TYK2 and in response to different interleukins including IL23, IL2 and IL35. Transcription activation of IFN-gamma gene is mediated by interaction with JUN that forms a complex that efficiently interacts with the AP-1-related sequence of the IFN-gamma promoter (By similarity). In response to IFN-alpha/beta signaling, acts as a transcriptional repressor and suppresses IL5 and IL13 mRNA expression during response to T-cell receptor (TCR) activation.
Subcellular location: Cytoplasm. Nucleus {ECO:0000269|PubMed:35614130, ECO:0000269|PubMed:37256972}. Note=Translocated into the nucleus in response to phosphorylation. {ECO:0000269|PubMed:35614130}.
Interaction partners:
- Interleukin-12 receptor subunit beta-2
- Signal transducer and activator of transcription 1-alpha/beta
- Interleukin-12 receptor subunit beta-1
- Tyrosine-protein kinase JAK1
- Interferon gamma
- Tyrosine-protein kinase JAK2
- Interferon regulatory factor 9
- Signal transducer and activator of transcription 3
- Non-receptor tyrosine-protein kinase TYK2
- Tyrosine-protein kinase JAK3
Sequence:
MSQWNQVQQLEIKFLEQVDQFYDDNFPMEIRHLLAQWIENQDWEAASNNETMATILLQNLLIQLDEQLGRVSKEKNLLLIHNLKRIRKVLQGKFHGNPMHVAVVISNCLREERRILAAANMPVQGPLEKSLQSSSVSERQRNVEHKVAAIKNSVQMTEQDTKYLEDLQDEFDYRYKTIQTMDQSDKNSAMVNQEVLTLQEMLNSLDFKRKEALSKMTQIIHETDLLMNTMLIEELQDWKRRQQIACIGGPLHNGLDQLQNCFTLLAESLFQLRRQLEKLEEQSTKMTYEGDPIPMQRTHMLERVTFLIYNLFKNSFVVERQPCMPTHPQRPLVLKTLIQFTVKLRLLIKLPELNYQVKVKASIDKNVSTLSNRRFVLCGTNVKAMSIEESSNGSLSVEFRHLQPKEMKSSAGGKGNEGCHMVTEELHSITFETQICLYGLTIDLETSSLPVVMISNVSQLPNAWASIIWYNVSTNDSQNLVFFNNPPPATLSQLLEVMSWQFSSYVGRGLNSDQLHMLAEKLTVQSSYSDGHLTWAKFCKEHLPGKSFTFWTWLEAILDLIKKHILPLWIDGYVMGFVSKEKERLLLKDKMPGTFLLRFSESHLGGITFTWVDHSESGEVRFHSVEPYNKGRLSALPFADILRDYKVIMAENIPENPLKYLYPDIPKDKAFGKHYSSQPCEVSRPTERGDKGYVPSVFIPISTIRSDSTEPHSPSDLLPMSPSVYAVLRENLSPTTIETAMKSPYSAE
Protein: SCL-interrupting locus protein homolog (Q60988)
Organism: Mus musculus (Mouse)
Function: Immediate-early gene. Plays an important role in embryonic development as well as in cellular growth and proliferation; its long-term silencing affects cell survival and cell cycle distribution as well as decreases CDK1 activity correlated with reduced phosphorylation of CDK1. Plays a role as a positive regulator of the sonic hedgehog pathway, acting downstream of PTCH1. Plays an important role in the regulation of centriole duplication. Required for the onset of procentriole formation and proper mitotic progression. During procentriole formation, is essential for the correct loading of SASS6 and CENPJ to the base of the procentriole to initiate procentriole assembly (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q15468}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q15468}. Note=Localizes at the leading edge. {ECO:0000250|UniProtKB:Q15468}.
Interaction partners:
- Serine/threonine-protein kinase PLK4
- Spindle assembly abnormal protein 6 homolog
- Centrosomal P4.1-associated protein
- Centrosomal protein 192
- Centrosomal protein of 152 kDa
- Abnormal spindle-like microcephaly-associated protein homolog
- Centrosomal protein of 135 kDa
- WD repeat-containing protein 62
- Rotatin
- Microcephalin
Sequence:
MNTRFPSSKMVPFHFPPSKLALWNPMPIGECIYLHLSYYRKPKLMVTEKAIRLAYRHAKQNKKNVPCFLLGSLTVDEDEEGVTLTIDRFDPGREIPECLERTPTASLPGDFLIPCRVHIQGLGSRDVIVHNADDFSSALKALQYHVCSKDFLDCGKLLCLRAQITPRESLDGVDFNLQWTAVTLANSFKCVPVKPIPIIPTALARNLSSNLNISQVQGTYKHGYITMDETRKLLLLLQSDPKVSSLPLVGIWLAGIIHVYSPQVWACCLRYMFSSSIQERVFSESGNFIIVLYSLTHKEPEFYECLPCESRTPDLQFQLLTNKETLHLFNNVEPSGKNPIHFELSAESQDAEAEAEVLSKISKTLPVKRSSQKLSPGKIPINKHDTDLEDEDFSPRPIPSPHPVSQKISKVQPSVPELSLVLDNNFTESSNQSNPLEMMTVENPLLIKPSQPELCDAKHSSEATTGEPFRRGPTNQLSQDTALRQSRGKQSSTCKKESLQFRNTNAKPSLSVPSPDVAEKLQAVSAGSMQKEDYPVRPSTLDSRQPSLAPQAQPHNLVFSTHNSTRPMELQVPTPSLPSYYPTNVCSCCQHHGHIQYSTINSWQGNTVGSIQDLRSESLPKHAFFHSSGCPSLCPNAIYSSSSPVSMKQGGMGAYSPHSNGEPSPVAGPSHVDSCVPHPCAMCMHTPNTAPDNGMMGLSPDAYRFVTEQDRQLRLLQAQIQRLLEAQSLDPGSHKTVATVEDTVKAAKQMELVSMEAQSSPGLHMRKSVSIAVSTGASLFWNAAGDDQEPDSQPKQDDTKISSEDMNFSVDINNEATSLPGSASSLKAVDIPSFEESNLAVEEVNQPLPESNSSSEQSKEPGVPVFFPNALLAESVSMCLQTAPTEGASNSTELPQGTKDEPYRPSDNQKIYQDLLGQVNHLLSNASQETEEPPTKAVVTNRECAKTQNTHHARKKRHNSGLVDKDCVLSATIKQLRSLGVKIDSPTKVKKNEQKVDHASVLACISPEAVISGLNYMSFGNVGMSSLSPTGVDLSMEANAIALKYLSENQLSQLSLARSKQNNGDSSVGLLHINSDRSTVGLSLVSPSNMSFATKKYMKRYGLLQSSDNSEDEEEPPSHADSESDHVLNRNPACRPVQCGHEKEPSWNACEIAQCSDCGSADTRTDVPVLRNITNQAVQPRATEHLNEDSAISLRNLKPNPAMNLRTGKAEFTHHPEKENERDIAVFPGTLPSPETLKQMNSMDSVGTFLDVKRLRQLPKLF
Protein: Beta-cubebene synthase (Mg25) (EC 4.2.3.128) (B3TPQ6)
Organism: Magnolia grandiflora (Southern magnolia)
Function: Sesquiterpene synthase converting farnesyl diphosphate into beta-cubebene (24.5%), alpha-muurolene (19.3%), delta-cadinol (18.6%), delta-elemene (16.0%), tau-muurolene (10.8%), and beta-elemene (10.8%). No activity with geranyl diphosphate or geranylgeranyl diphosphate.
Interaction partners:
Sequence:
MDSPTTQRPNMEIGRAFVNYHPSIWGEHFIAASPDVMRLDAHKGRGEELKEVVRNMFSTVNDPLLKMNLIDAIQRLGVAYHFEMEIDKALGQMYDDHINGKDDGFDLQTLALQFRLLRQQGYNVSSGVFAKFKDDEGNFSSILSKDTHGLLSLYEAAFLGTHGDDILDEAITFTTVHLKSTLPHVSAPLTKLVELALEIPLHRRMERLQTRFYISIYEEDRERNDVLLEFSKLEFLRLQSLHQRELRDISLWWKEMDLLAKLPFTRDRVLEGYFWTVGVYFEPHYSRARMIMTKMIAFATVMDDTYDVYGTLEELELLTATIERWNRGDMDQLPDYMKVIFIALLDGVDATEDDLTGEGKSYRIYYLKEAVKDLAKAYLAEARWVSSGYVPTSEEYMKVALISAVYPMLFVAFLIGMDEVVTKEVLEWAIHMPTMLRTCSIVARLMDDIPSNKLEQERKHVSSSVECYMKEHGTSYHESIQKLREMVASGWKDINKECLKPTPVPTAVINVILNFTRVLEIIYQHRDGYTDASVETKEHIASLFVDPIPL