wanglab/gogpt-training-data huggingface dataset:
Protein: Biotin--protein ligase (EC 6.3.4.-) (Biotin apo-protein ligase) [Includes: Biotin--[methylmalonyl-CoA-carboxytransferase] ligase (EC 6.3.4.9); Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase (EC 6.3.4.10) (Holocarboxylase synthetase) (HCS); Biotin--[methylcrotonoyl-CoA-carboxylase] ligase (EC 6.3.4.11); Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)] (P50747)
Organism: Homo sapiens (Human)
Function: Biotin--protein ligase catalyzing the biotinylation of the 4 biotin-dependent carboxylases acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, and methylcrotonyl-CoA carboxylase.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:7842009}. Mitochondrion {ECO:0000305|PubMed:7842009}.
Interaction partners:
- Biotinidase
- Pyruvate carboxylase, mitochondrial
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Acetyl-CoA carboxylase 1
- Acetyl-CoA carboxylase 2
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
Sequence:
MEDRLHMDNGLVPQKIVSVHLQDSTLKEVKDQVSNKQAQILEPKPEPSLEIKPEQDGMEHVGRDDPKALGEEPKQRRGSASGSEPAGDSDRGGGPVEHYHLHLSSCHECLELENSTIESVKFASAENIPDLPYDYSSSLESVADETSPEREGRRVNLTGKAPNILLYVGSDSQEALGRFHEVRSVLADCVDIDSYILYHLLEDSALRDPWTDNCLLLVIATRESIPEDLYQKFMAYLSQGGKVLGLSSSFTFGGFQVTSKGALHKTVQNLVFSKADQSEVKLSVLSSGCRYQEGPVRLSPGRLQGHLENEDKDRMIVHVPFGTRGGEAVLCQVHLELPPSSNIVQTPEDFNLLKSSNFRRYEVLREILTTLGLSCDMKQVPALTPLYLLSAAEEIRDPLMQWLGKHVDSEGEIKSGQLSLRFVSSYVSEVEITPSCIPVVTNMEAFSSEHFNLEIYRQNLQTKQLGKVILFAEVTPTTMRLLDGLMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPFVQHLMSVAVVEAVRSIPEYQDINLRVKWPNDIYYSDLMKIGGVLVNSTLMGETFYILIGCGFNVTNSNPTICINDLITEYNKQHKAELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKVSIVGLDDSGFLQVHQEGGEVVTVHPDGNSFDMLRNLILPKRR
Protein: Magnesium-chelatase subunit ChlI-1, chloroplastic (Mg-chelatase subunit I-1) (EC 6.6.1.1) (Mg-protoporphyrin IX chelatase subunit ChlI-1) (Protein CHLORINA 42) (P16127)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The magnesium-chelatase is a complex of three subunits, CHLI, CHLD and CHLH. The reaction takes place in two steps, with an ATP-dependent activation followed by an ATP-dependent chelation step. Possesses high affinity for ATP and may play a major role in chlorophyll biosynthesis. Does not bind abscisic acid (ABA), but is a positive regulator of ABA signaling.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Magnesium-chelatase subunit ChlH, chloroplastic
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
- Magnesium-chelatase subunit ChlD, chloroplastic
- Protoporphyrinogen oxidase 1, chloroplastic
- Protoporphyrinogen oxidase 2, chloroplastic/mitochondrial
- Ferrochelatase-1, chloroplastic/mitochondrial
- Ferrochelatase-2, chloroplastic
- Geranylgeranyl diphosphate reductase, chloroplastic
- Magnesium-chelatase subunit ChlI-2, chloroplastic
- E3 ubiquitin-protein ligase WAVH1
Sequence:
MASLLGTSSSAIWASPSLSSPSSKPSSSPICFRPGKLFGSKLNAGIQIRPKKNRSRYHVSVMNVATEINSTEQVVGKFDSKKSARPVYPFAAIVGQDEMKLCLLLNVIDPKIGGVMIMGDRGTGKSTTVRSLVDLLPEINVVAGDPYNSDPIDPEFMGVEVRERVEKGEQVPVIATKINMVDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDVLLDSAASGWNTVEREGISISHPARFILIGSGNPEEGELRPQLLDRFGMHAQVGTVRDADLRVKIVEERARFDSNPKDFRDTYKTEQDKLQDQISTARANLSSVQIDRELKVKISRVCSELNVDGLRGDIVTNRAAKALAALKGKDRVTPDDVATVIPNCLRHRLRKDPLESIDSGVLVSEKFAEIFS
Protein: Neurabin-1 (H2KYW1)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
- Rho GTPase-activating protein syd-1
- Liprin-alpha
- Serine/threonine kinase SAD-1
Sequence:
MTTASELLSDDARARFSHTKALFEQLERQQDVPSFYSPRLQRQPPPPLPPKPPSQCPPSPMSQVERNFSDLAADLDRIQSSPATSRFIQNKSSTLPSSYSDSTQQYSFENTVATSQYGGLQTNNNNNNINMNSFEPYWRNGSIYRRQFEGNGKPFGEENDGISPTTNGVKHTTYAVVKTPKETELETTSENRGLMETRRGLSPERPDVDLTNRKVSFSTAPIPVFSAFSVEDYDRKNEDIDPVASCAEYELERRLERMDLFEVDLEKGAEGLGVSIIGMGVGADSGLEKLGIFVKSITPGGAVHRDGRIRVCDQIVSVDGKSLVGVSQLYAANTLRSTSNRVTFTIGREQNLEESEVAQLIQQSLEHDRMRMMGDEEDDIEEPPPPPSQMPQLPIEQDRPTTSMITKEEIEIRSKIAALELELDVTHKKAEQYHEVLSSTKSHCDQLEKQNEQANYMIKNYQEREKELLNREENHVEQLRDKDVHYASLVRQLKERIDELESKLEEAEERRHSIQNLELIELREKLKEKVEKRNEGMAYRPGGELPHEDKAVMVNLETITPSTKKDAEVSVGSSWTEEYSSPCESPVPRISEPASPALPHKLTHRKLLFPLRKKYAENEFWRATCQPVGLQALHWTVDDVCQLLVSMGLDKYVPEFTINKIDGAKFLELDGNKLKAMGIQNHSDRSLIKKKVKGMKNKIERERKQLERESRTRVIAHTIPM
Protein: Matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (GELB) [Cleaved into: 67 kDa matrix metalloproteinase-9; 82 kDa matrix metalloproteinase-9] (P14780)
Organism: Homo sapiens (Human)
Function: Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves NINJ1 to generate the Secreted ninjurin-1 form. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:2551898}.
Interaction partners:
- Metalloproteinase inhibitor 1
- CD44 antigen
- Metalloproteinase inhibitor 2
- Neutrophil gelatinase-associated lipocalin
- Thrombospondin-1
- Metalloproteinase inhibitor 3
- Cathepsin G
- Dentin matrix acidic phosphoprotein 1
- Elastin
- Interstitial collagenase
Sequence:
MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED
Protein: Proteasome 26S subunit, ATPase 6 (A0A8I5ZU65)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MADPRDKALQDYRKKLLEHKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQIVGEVLKQLTEEKFIVKATNGPRYVVGCRRQLDKSKLKPGTRVALDMTTLTIMRYLPREVDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAVRKVADSKKLESKLDYKPV
Protein: Arginyl-tRNA--protein transferase 2 (Arginyltransferase 2) (R-transferase 2) (EC 2.3.2.8) (Arginine-tRNA--protein transferase 2) (AtATE2) (Q9C776)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Component of the N-end rule pathway with ATE1 and PRT6. The N-end rule pathway regulates seed after-ripening, seedling sugar sensitivity, seedling lipid breakdown, and abscisic acid (ABA) sensitivity of germination. The end-rule pathway regulates various aspects of leaf and shoot development. Involved in the oxygen-dependent N-arginylation of RAP2-12, an activator of hypoxic gene expression. This N-terminal modification leads to ubiquitination by PRT6 and subsequent degradation of RAP2-12 under aerobic conditions. Involved in disease resistance. The end-rule pathway plays a role in regulating the timing and amplitude of the immune response following infection with the bacterial pathogen Pseudomonas syringae pv tomato. Regulates the biosynthesis of plant-defense metabolites such as glucosinolates, and the biosynthesis and response to the phytohormone jasmonate (JA), which plays a key role in plant immunity.
Interaction partners:
- E3 ubiquitin-protein ligase PRT6
- E3 ubiquitin-protein ligase PRT1
- Plant cysteine oxidase 1
- Protein N-terminal glutamine amidohydrolase
- Protein N-terminal asparagine amidohydrolase
- Ethylene-responsive transcription factor RAP2-2
- Ethylene-responsive transcription factor RAP2-12
- Plant cysteine oxidase 4
- Probable nucleoside diphosphate kinase 5
- Plant cysteine oxidase 5
Sequence:
MSSKKAKTKNEASSSRGGIGGESIVADCGRNKSTCGYCKSSTRFSISHGLWTERLTVNDYQALLDSGWRRSGCYLYKPEMEKTCCPSYTIRLKASDFVPSKEQQRVRRRIERFLDGELDAKPSEQTEDQDVSFSREVSVSVKKSLGAAKREKNNELEPIMKDLSEQIDNAVQKCIQSGEFPSNVQIPKASVKKVFSAKRKKLAEGSEDLLYTSNIAFPIVAAMKHTQTLEKGKNVEENRLSPEAVSEKLLSAMNKVGEFTGFSVKVSKGHINFLSATQVTSSDRNEGEESLCATTIKSSSNKLHARKRKLEMHLKRSSFEPEEYELYKRYQMKVHNDKPESISETSYKRFLVDTPLTEVPSSGYDDEEKIPLCGFGSFHQQYRVDDRLIAVGVIDILPKCLSSKYLFWDPDFASLSLGNYSALQEIDWVKQNQAHCSTLEYYYLGYYIHSCNKMRYKAAYRPSELLCPLRYQWVPFEVAKPLLDKKPYSVLSNISKVSSSSSSPQASETLLESTSEHEDMEQGDTNDDDDEMYNSDEDSDSDSSSSRNRSDITNILISLNGPRLRYKDIPRFKNPVVQKQLESMLVSYRKVVGAELSEIMVYELR
Protein: FMN-dependent NAD(P)H:quinone oxidoreductase 1 (EC 1.6.5.-) (Azo-dye reductase 1) (FMN-dependent NADH-azo compound oxidoreductase 1) (FMN-dependent NADH-azoreductase 1) (EC 1.7.1.17) (Q9I5F3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Shows a preference for benzoquinones.
Interaction partners:
- Guanidinium exporter
- Probable nitroreductase
- Probable acyl carrier protein
Sequence:
MSRILAVHASPRGERSQSRRLAEVFLAAYREAHPQARVARREVGRVPLPAVTEAFVAAAFHPQPEQRSLAMQADLALSDQLVGELFDSDLLVISTPMYNFSVPSGLKAWIDQIVRLGVTFDFVLDNGVAQYRPLLRGKRALIVTSRGGHGFGPGGENQAMNHADPWLRTALGFIGIDEVTVVAAEGEESGGRSFEDSCDEAEQRLLALARSA
Protein: Phosphatidylinositol glycan anchor biosynthesis class S (SD10476p) (Q9VC10)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Phosphatidylinositol glycan anchor biosynthesis class T
- Putative GPI-anchor transamidase
- Glycosylphosphatidylinositol anchor attachment 1
- LD37974p
- Prolyl 3-hydroxylase sudestada1
- GPI inositol-deacylase
- GPI ethanolamine phosphate transferase 3
- Phosphatidylinositol glycan anchor biosynthesis class F
- Uncharacterized protein, isoform B
- Davis-cup
Sequence:
METSSSSPVKPRRKDKDEDKFRIGATLAFIVVIIGIGVPMWWRTTTVYRVNLPSTEILSLSKIPIKTAVQVAIYTQQTSRGQLLIAELQNAFSDNEIWSVEFKQLSPTPMTQEAHTPAALEKLLLENHVQSVGDFMFIEWPKLQEELLLTTERSALMRSDTPSNKIAQLLHAKILQTYRINQILSTDERMGAKSEAPQPAYDVIVSVLNPKPRLTHAKWNIAMAVKTYIEPWLAKVSGVSNYTVRSQWKYRVAIEADLKQVRDQSKLGRHYALQETALPHLLTSIAQNLSASTTDKPAINLVVYIPPCHIAPLHIYNSKDQRLTRNDVDAFISPPWGGFIIANPPEHVCLAAMSDQEAVPYHVSTTDNMQVMLDQLHKLLDISSELQMEGVKVVDIEQLEPRRWEYEAYLRRSAIRHISTASSTLQSLIKLLDQISYIVIDDEVGAAITNSYADILAAKAALLEHRLADASVLAKRAFVASERGFFDASLLAQLYFPDEQKYAIYIPLFLPIMVPVLSSFNMLRGVLQARRKEKQS
Protein: F-box/LRR-repeat protein 7 (F-box and leucine-rich repeat protein 7) (F-box protein FBL6/FBL7) (Q9UJT9)
Organism: Homo sapiens (Human)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. During mitosis, it mediates the ubiquitination and subsequent proteasomal degradation of AURKA, causing mitotic arrest (By similarity). It also regulates mitochondrial function by mediating the ubiquitination and proteasomal degradation of the apoptosis inhibitor BIRC5.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5BJ29}. Note=Localizes to the centrosome during spindle formation. {ECO:0000250|UniProtKB:Q5BJ29}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- F-box/LRR-repeat protein 18
- Cyclin-F
Sequence:
MGANNGKQYGSEGKGSSSISSDVSSSTDHTPTKAQKNVATSEDSDLSMRTLSTPSPALICPPNLPGFQNGRGSSTSSSSITGETVAMVHSPPPTRLTHPLIRLASRPQKEQASIDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIRLTGETINVDRALKVLTRRLCQDTPNVCLMLETVTVSGCRRLTDRGLYTIAQCCPELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSGCSKVTCISLTREASIKLSPLHGKQISIRYLDMTDCFVLEDEGLHTIAAHCTQLTHLYLRRCVRLTDEGLRYLVIYCASIKELSVSDCRFVSDFGLREIAKLESRLRYLSIAHCGRVTDVGIRYVAKYCSKLRYLNARGCEGITDHGVEYLAKNCTKLKSLDIGKCPLVSDTGLECLALNCFNLKRLSLKSCESITGQGLQIVAANCFDLQTLNVQDCEVSVEALRFVKRHCKRCVIEHTNPAFF
Protein: ATP synthase-coupling factor 6, mitochondrial (ATPase subunit F6) (A8MUH2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|PIRNR:PIRNR002455}. Mitochondrion inner membrane {ECO:0000256|PIRNR:PIRNR002455}.
Interaction partners:
Sequence:
MILQRLFRFSSVIRSAVSVHLRRNIGVTAVAFNKELDPIQKLFVDKIREYKSKRQTSGGPVDASSEYQQELERELFKLKQMFGNADMNTFPTFKFEEHFSQHLRSWQPSRDDDILILSS
Protein: V-type proton ATPase subunit d (V-ATPase subunit d) (V-ATPase 39 kDa subunit) (V-ATPase subunit M39) (Vacuolar proton pump subunit d) (P32366)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments. This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector. Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- V-type proton ATPase subunit H
- V-type proton ATPase subunit c''
- V-type proton ATPase subunit B
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit C
- V-type proton ATPase subunit F
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit D
- V-type proton ATPase subunit G
- V-type proton ATPase subunit E
Sequence:
MEGVYFNIDNGFIEGVVRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSSESLTTSLIQEYASSKLYHEFNYIRDQSSGSTRKFMDYITYGYMIDNVALMITGTIHDRDKGEILQRCHPLGWFDTLPTLSVATDLESLYETVLVDTPLAPYFKNCFDTAEELDDMNIEIIRNKLYKAYLEDFYNFVTEEIPEPAKECMQTLLGFEADRRSINIALNSLQSSDIDPDLKSDLLPNIGKLYPLATFHLAQAQDFEGVRAALANVYEYRGFLETGNLEDHFYQLEMELCRDAFTQQFAISTVWAWMKSKEQEVRNITWIAECIAQNQRERINNYISVY
Protein: Growth hormone receptor isoform 2 (Q3Y4E0)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Growth hormone 2
- Somatotropin
- Somatolactin
- Somatolactin beta
- Suppressor of cytokine signaling 2
- Suppressor of cytokine signaling 2
Sequence:
MATSHILFICLLVSLTVVSQESPTSEQALPQIRPQITGCVSHDMNTFRCRWNVGTFQNLTEPRDLRMFYYINNKNISPKEWSECPNYMADRIDECFFNESYTKVWMTYSVQLRSGDQDNLYDEVIFTVEDIVEPDPPIALNWTLLNVGLTGSHFDIMVSWEPPHSADVPMGWMTLQYEVQYREVNSTLWRMVDLEKGMQRSLYGLRTNTDHEVRVRCKTLAFRNFGEFSDSIVIHIPTKESRFPVTVLLVFAALGLAVILILVIYSQQQKLMMILLPPIPGPKIKGIDPELFKKGKLAELTSILGGHPDLRPELYCEDPWVEFIELDMEEPNDRLTELDTQCLMDRSPSSDCPPLTIGFGDDDSGRASCCDPDLPEPEAFPFHPLLSNTSLEPSGASTEASSPVQTPTTGKNLWAVPGREDLYTQVSEVRPTGEVLLMPEEQSKVEKDAEEKAEGKEKEKPRKEFQLLVVNADGGGYTTELDAEKMSAKLPTGRGNQPARTEDSRLAQGQPFGEYQSLYFEAEMPPIPPASPVSPLPPVSVYTMVEEVDRQNSLILKPSPPPAPQPVLIKLPLPTPEGYLTPDLLGNITP
Protein: Missing-in-metastasis, isoform J (A0A0B4K7T1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDLSLERDSSALGSLFQQIINDMKNTSPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGASKEIGTALTRVCLRHKAVETRLKTFTSTIMDCLVQPLQERIEDWKRTVATIDKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQTDGLQSLMDSHMQDVTLRRAELEEVEKKSLRAAMVEERLRYCSFVHMLQPVVHEECEVMSELGHLQEAMQSIALVTKEPSVLPQASEELIHDAKASINLYPESPGGGSGSQGGGCSNSLGSRKSSVCSISSMNSSGSSNSPGHHHYPRSLSQFVTPAIRLKPGESSDSGFCSSPALTTQTSNATNQTANVSTWPPHSQDGVDTLPPTADRPHTISTAYEKGHQRPPLTVYTFQNPETIHESGSCLNNGTAAPNGQPLSGQATPATQKSPAASLSRPPLPVRCSSLERPLSAQSNHRQGSGNNLLQRQCPSPIPAHITKELSAAHHAQQQQQQQNQQPQTPPTYVNMSELATMAALKQTNQQQKPSTPPLQQQSSIDSTSSQHSNDSTGSHQLLQQQQQHHQSQQNHHSATATRSHSISSTASSLHSHPSIDSTVACGSLVGQHNHSTSTNTNTTSPSSGSSTPQNHYSPLLTNSPTSTAAGTPSGSSLGPGSGLGFVYQVSSPTPPSSEVLKITEQAAAGQDQGPANSVADETDERSRASVLQKASMFEKAAAAAAVSPPAPMQIASGSPASGGGTRRSEAEQQEMDKSFEDSIQALNNLIGELDSFQREIDEGKVKPPSNIISGSTTSSNNNNTTTSSISSSDNNNLPATSNIEPCAISNQTNSSGCGTDISDTTSDELAGDDMDVRRRDRDRDRDLLGASDSELSRCYVSETSSLTGGLTAGGYENPTFAHFAANANREDAVSLASDSVCLGQPRHAYVDTCSDSGSAVVVIYDHQIPNTPDIEFVKQNSEIVVLRTKDPQPHALQLHEMRELQQLPANLAGSPDSSPDSAGGQAPPTATVAPAKQRLSSFRATSEQQLQLLGRGSPQRGKTPSEQAVQSRPQDQHFPQTQQQDIDGSSPPVELARRQLPPKPTSLSIFNGPVPTAGDRPVVPRKSDFKADLDAKIRRQKQKVKQQLQQQQQQQQQEQQETQQQQQAPQEQQHSPQSPQTRNCNVTNQQAANITASASAFATATASTDPYPNPNHRMPNQNQTATSNHTQCKTPTMALSPSSPRGHLPLSSSSLSSLPLPATTSSPSNARPSMLPASDRPPAHPYVCSNAPANPHHANSISNANAHLKPCITPRPASLSGGAAGGGSTRIGRRSSINQSKPPPPVRRSSSVTPSPNASVGLQQQPQHATLSQQNHQLSSSSEHLPPPPPFMLDAMPQIPSSALKVSETVRALAAMRHQPASPVSLRRMQQQQQQQLQQQQQQQVQQQQPLLQTFRTSSPAAGGGGGGGIYAQPKLVNSMSSFRTSSPSPNGHAHPLPPTQPKANPNLIAQLNARLSGKQQQHQQQQHIEGIYGNQQAPGGESIYMRSGLSMSQPQQQQHFDAAQSPNMRQAHSHQHHQPPQQQHYTCPPPLEDPPPPPIYAAGASATMPKKMARPPTGQNATHSSAYAAASSTATLPKNMMQQQQRLQHQQQYQQPAGMGIGNGNGHLGQRPQLPLPQQKLRAAQQQHLAEQQHQQQQEQQQHHQQHQQHQQRQPPIPSRHSSVQQKIFVSTNPFIQTTAVKFHSPSASPTCGSPVTGSLASIYATTSRGGHHHQQQQAQQQQHYYRDAAGGNSNGGAAYYNHNAHAHSQAHHPNYATSTNIEKTGSIRAKTKAEFLENLNAKLAKQGMSGRAFAVRNLINSKALMYQNPQKLSRPSAQYRRPPTYPNTSTTTNATCEDQC
Protein: Krueppel-like factor 3 (Kruppel-like factor 3 (basic)) (A2BG67)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- C-terminal-binding protein 1
- C-terminal-binding protein 1
Sequence:
MLTCDPKPDMSLYQPYSTLIKSHETFGMVLPPAVVSGAHLYPSHYHPSYQLPYSHRQSQDVHQAQIEPVDLSIGNKSSGSSPSSSLASSSPRASPPSPYEAHSPASRCSQNRQLSPSLTLPIPAVTQVLTPFVSSPGMIPVIPMPLSVLYPPSLHLSPSIIISPVTPEDPANHKHFSVIKSENTSDHHELLKPIKSEPHPEHTQDNHSQEKSVITALPNYNDRGNTQSPKVESPDLLKKRRIHRCDFNGCNKVYTKSSHLKAHRRTHTGEKPYKCMWEGCTWKFARSDELTRHYRKHTGVKPFHCPDCDRTFSRSDHLALHKKRHLLV
Protein: ADAM metallopeptidase domain 3A (Transmembrane protein tMDC I) (P70534)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MLPLFLVLSCLGQLIAVGKDIETPLIQITVPEKIETNIKDAKESETQVTYVIRIEGKAYTLQLEKQSFLHPHFVTNLHNKLGTLQPYFSLVKSHCFYQGHAVEIPASTVTLSTCSGLRGLLQLENVTYGIEPLESSTTLEHILYEIQNHKIDYSPLKENYTNSQDESGSYRILVKPLKSSNSKLRKRILTVKIIMDKGMFDHVGSEVGVATQKVVQMFGLINTMFSQLKMTVMLNSLEIWSEENKIETNGDADEVLQRFLLWTHKEMPQTTKEITYLLLYKDHPDYVGATYHGMACNPKFTAGIALHPKTLGVEGFAIVLSQLLGINLGLTYDDIYNCFCRGSTCIMNPSAIHSEGIKVFSSCSMDEFRQLASQPDLDCLLKTQETEVVALPQAAKVCGNYILEPPEQCDCGPAERCSHKKCCKSEDCTLLSDAECGSGACCDKRTCKIAERGRLCRKSTDQCDFPEFCNGTSEFCVADIKAADLEPCNNETAYCFKGVCQDRDRQCTDLFGKYAKGPNYVCAQEVNLQNDKFGNCHGRCNYSALFCGKAVCYWSFAELVKTDVFDVQYTYLGGQVCVSAHLRVRNDETKDDTYVRDGTICGNGQVCYRGECLRVHVLRGDRECEADDKCQGHGICNNQNNCQCEAGFAPPECDMTPSSPGGSMDDGFWLPLDKSTPLVIKRPGTQYKKGLLISFYVFLPFLIVTAIMVVKQNISKMFGQGEEEFSEGSISEEINDSKQS
Protein: Prohibitin (Q5AND0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273, ECO:0000256|RuleBase:RU366048}.
Interaction partners:
- Prohibitin
- Prohibitin
- Mitochondrial inner membrane protease ATP23
- Elongation factor Tu
- mitochondrial processing peptidase
- Cytochrome b-c1 complex reductase subunit, mitochondrial
- Slp2p
- AAA family ATPase
- FACT complex subunit POB3
- M-AAA protease subunit
Sequence:
MNDQNWKNLSNELRRRAEQARSSSNMKSPKSPLGIFGGIGGLLLLGGATMFIQNALFNVDGGQRAILYSRLDGVQSKIYPEGTHFVIPWFQRPIIYDVRAKPKEIASLTGTKDLQMVNITCRVLYKPDIWQLPTIYRTLGLKYEEKVLPSIVNEVLKSVVAQFNASQLITQREKVSRLVRENLVRRASKFNVLLDDVSITYMTFSPEFSQAVEAKQIAQQDAQRAAFVVDKAIQEKQQLVVKAQGEAKSAELIGEAIKKSKDYVELKRLDTAREIANILAASPNRIILDNDTLLLNTVTDNRK
Protein: Interleukin-3 receptor subunit alpha (IL-3 receptor subunit alpha) (IL-3R subunit alpha) (IL-3R-alpha) (IL-3RA) (CD antigen CD123) (P26951)
Organism: Homo sapiens (Human)
Function: Cell surface receptor for IL3 expressed on hematopoietic progenitor cells, monocytes and B-lymphocytes that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells. Ligand stimulation rapidly induces hetrodimerization with IL3RB, phosphorylation and enzyme activity of effector proteins such as JAK2 and PI3K that play a role in signaling cell proliferation and differentiation. Activation of JAK2 leads to STAT5-mediated transcriptional program (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:38702781}; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-3
- Cytokine receptor common subunit beta
- Granulocyte-macrophage colony-stimulating factor
- C-type lectin domain family 4 member C
- Interleukin-5
- GTPase NRas
- GTPase KRas
- GTPase HRas
- Interleukin-2
- B-lymphocyte antigen CD19
Sequence:
MVLLWLTLLLIALPCLLQTKEDPNPPITNLRMKAKAQQLTWDLNRNVTDIECVKDADYSMPAVNNSYCQFGAISLCEVTNYTVRVANPPFSTWILFPENSGKPWAGAENLTCWIHDVDFLSCSWAVGPGAPADVQYDLYLNVANRRQQYECLHYKTDAQGTRIGCRFDDISRLSSGSQSSHILVRGRSAAFGIPCTDKFVVFSQIEILTPPNMTAKCNKTHSFMHWKMRSHFNRKFRYELQIQKRMQPVITEQVRDRTSFQLLNPGTYTVQIRARERVYEFLSAWSTPQRFECDQEEGANTRAWRTSLLIALGTLLALVCVFVICRRYLVMQRLFPRIPHMKDPIGDSFQNDKLVVWEAGKAGLEECLVTEVQVVQKT
Protein: Protein REVEILLE 4 (Myb transcription factor LHY/CCA1-like 1) (Q6R0G4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:17363273}. Cytoplasm {ECO:0000269|PubMed:17363273}. Note=Actively translocating nucleo-cytoplasmic shuttle protein.
Interaction partners:
- Protein LNK2
- Protein LNK1
- Two-component response regulator-like APRR1
- Two-component response regulator-like APRR5
- Protein EARLY FLOWERING 4
- WD repeat-containing protein LWD2
- WD repeat-containing protein LWD1
- Two-component response regulator-like APRR9
- Transcription factor LUX
- Two-component response regulator-like APRR7
Sequence:
MTSTNPVVAEVIPAETSTDATETTIATTEAGEAPEKKVRKAYTITKSRESWTEGEHDKFLEALQLFDRDWKKIEDFVGSKTVIQIRSHAQKYFLKVQKNGTLAHVPPPRPKRKAAHPYPQKASKNAQMSLHVSMSFPTQINNLPGYTPWDDDTSALLNIAVSGVIPPEDELDTLCGAEVDVGSNDMISETSPSASGIGSSSRTLSDSKGLRLAKQAPSMHGLPDFAEVYNFIGSVFDPDSKGRMKKLKEMDPINFETVLLLMRNLTVNLSNPDFEPTSEYVDAAEEGHEHLSS
Protein: Large ribosomal subunit protein uL13A (60S ribosomal protein L16-A) (O42848)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongation factor 3
- mRNA export factor elf1
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein eS10B
- Small ribosomal subunit protein uS13B
- Small ribosomal subunit protein eS24B
- Small ribosomal subunit protein eS19A
- Small ribosomal subunit protein uS9A
- Large ribosomal subunit protein uL23A
- Small ribosomal subunit protein eS28A
Sequence:
MSEFQKVVVIDAKGHLLGRLASVVAKQLLGGQKVVVVRCEELNISGHFFRNKLKYLAYLRKACRYNPSRGAFHFRAPSRIFQKAVRGMLPHKTARGQAALEHLQAVEGIPPPFDKQKRVVVPAALRVLRLKPGRKYCTVGRLSSEVGWKYSDIVSKLEERRKVKSAAFYQAKLAKQKKIASAKAASSVNGKLAEFGY
Protein: Scavenger receptor (Q58SM6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
TCDRDGRLRGEKPFCASRGCARPEDPENGHVENLSLRADVVCHDGYVLVGGRTAYCDGERWSTQLGSCRRSNHTRDHSCDFESEDQCGWEAETTFRRPWKRVSTVSDIHSLRTGPRHDHTFKNESGGHYMRMETQMGAYGSYHLLSPIYPRSLTLKTACCFRFHYFMFGAGVDNLVVSVKPVSMPMATMWNRFRANCSKFEISGQQGTQWLEHTISIDEMQEDFQVIFTATDARSQFGDIAIDDVQLMTGSECGTNGFTTTTEPTAPTGSNEQPLVYDMMSCSGRCGTSISASNITNNGIVMGCGCNDECLSDETCCLNYLEECTKELLTTTEDDISSLPPTVTSTSTSTTRKSTTTTTTSTTTTSTTTTKRPTTTTTTTKATTTKRTTTTKKPTTTSTTPKPTTTTSTTPKSTTSTTSTTSTTPTTTTTINVFTTKKTTIMIPTSSTEKTTGINTTMKTRKRITWNVDPQDIEGHMDTSGSTPNPALVVLYLLLAIVLVVVLANVVNRWIIPITGSKTSSEKAVRFKKAFDSLKKQRKRNSMDDQPLCDSDNDDVEYFEEMGVDIRHRTDL