wanglab/gogpt-training-data huggingface dataset:
Protein: Protein FixB (P31574)
Organism: Escherichia coli (strain K12)
Function: Required for anaerobic carnitine reduction. May bring reductant to CaiA.
Interaction partners:
- Protein FixA
- Crotonobetainyl-CoA reductase
- Ferredoxin-like protein FixX
- Protein FixC
- Probable acyl-CoA dehydrogenase YdiO
- Putative electron transfer flavoprotein subunit YdiQ
- Putative electron transfer flavoprotein subunit YgcR
- Putative metabolite transport protein YaaU
- Carnitinyl-CoA dehydratase
- L-carnitine CoA-transferase
Sequence:
MNTFSQVWVFSDTPSRLPELMNGAQALANQINTFVLNDADGAQAIQLGANHVWKLNGKPDDRMIEDYAGVMADTIRQHGADGLVLLPNTRRGKLLAAKLGYRLKAAVSNDASTVSVQDGKATVKHMVYGGLAIGEERIATPYAVLTISSGTFDAAQPDASRTGETHTVEWQAPAVAITRTATQARQSNSVDLDKARLVVSVGRGIGSKENIALAEQLCKAIGAELACSRPVAENEKWMEHERYVGISNLMLKPELYLAVGISGQIQHMVGANASQTIFAINKDKNAPIFQYADYGIVGDAVKILPALTAALAR
Protein: Heat shock 70kDa protein 1A variant (Q59EJ3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
LRSCCDSPLPFSRVTPVVPRLPRANLCGCRHRRVEFPASGRTELFSRIQCSVSSPQSQSRADREQGTGMAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGDTKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIESMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD
Protein: Small ribosomal subunit protein mS31 (28S ribosomal protein S31, mitochondrial) (MRP-S31) (S31mt) (P82925)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11279123, ECO:0000269|PubMed:24799711}.
Interaction partners:
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS23
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS39
- Small ribosomal subunit protein bS21m
Sequence:
MFPRVSAVLPFRPLSRLPLCSAGPEASAATVVPLASPHGTVRTKCNIQRYFGTNSVIYSKKDDKSVPACEISKETENQGSTKENKKKDLVNIIKGMKVELSTVNVQTTKPPNRGQLKSLEAAIRRLQKSPEDAPQKSKSLSPELVAAATAVADSLPFDKQTTKSELLRQLRQHEEDSKAQKDGEKPKISFSNIISDMKVARSSTARASTRPVHQIQFDEGADDFVDREETADLRKRFRKNIFKGKRLNIFELKPVTEEAPETEAAPSLWDVEFAKQLAAVTEQPFQNGFEEMIQWTKEGKLWEFPINNEAGFDDDGSEFHEHIFLDKYLEGFPKQGPIRHFMELVTCGLSKNPYLSVKQKVEHIEWFRNYFNEKQDILKESGINFS
Protein: At2g27090 (BZIP transcription factor (DUF630 and DUF632)) (Q9ZVD1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGASTSRIDEDKALQLCRERKKFVQQALDGRCLLAAAHVSYVQSLKSTGTALRKFSETEVPVESSLYTSTSATPEQPLALIEKSVSHLSYSPPPASHSHHDTYSPPPSPPSTSPFQVNHMKFKGFSSKKVEEKPPVSIIATVTSSSIPPSRSIEKMESTPFEESSSMPPEAPWDYFGLSHPIDNQFSSSHVGNGHVSRSVKEEDGTPEEEDDGEDFSFQEREESRDSDDDEFDEPTSDTLVRSFENFNRVRRDHSTLPQREGVESDSSDAEKSKTPELSPPVTPLVATPVNKTPNKGDHTENKLPPRDFLSSMKEIELLFVKASETGKEVPRMLEANKLHFRPIVPSKESGSGASSLFKTCLSCGEDPKDVPEEPAQNSVKYLTWHRTESSRSSSSRNPLGGMNSDDVEELNSNLFENICMIAGSHASTLDRLYAWERKLYDEVKGSQTVRREYDEKCRILRELESEGKGSQRIDKTRAVVKDLHSRIRVAIHRIDSISRRIEELRDNELQPQLEELIEGLSRMWEVMLECHKVQFQLIKACYRGGNIKLNMQSELHRQVTSHLEDELCALASSFTKWITGQKSYIQAINEWLVKCVALPQRSKRKRRAPQPSLRNYGPPIYATCGIWLEKLEVLPTKEVSGSIKALASDVARFLPRQEKNRTKKHRSGENKNDLTAHMLQDETLEDCGPGFDRFRTSLEGFVGQLNQFAESSVKMYEELKEGIHGAKNNYEQLKKAYSSQGK
Protein: Protein huluwa (E9QDC5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Key maternal determinant of the dorsal organizer and body axis formation in vertebrates that acts by promoting stabilization of beta-catenin (ctnnb1). Localizes on the plasma membrane of the future dorsal blastomeres in early blastulas and binds to and promotes the tankyrase-mediated degradation of axin (axin1 and axin2). Axin degradation results in stabilization and nuclear translocation of beta-catenin (ctnnb1) for activating organizer-specific target gene expression.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30467143}; Single-pass membrane protein {ECO:0000255}. Note=Enriched on the plasma membrane of blastomeres only in a small region in which the dorsal organizer will form. {ECO:0000269|PubMed:30467143}.
Interaction partners:
Sequence:
MSQLGSAVPSSNLPEGLPVSSLALLILVLIPCVLLLLLLNCLFVGYKLFRMTRRKRDRYGSEMSLMHSSYSTRQRITRFSDEPPVAPNRKTNYVSVSEPMLAPPITSSLTSSAERRATGQRAMFLRPDGATYAGSESLRVPHWRTSAPVLVQSSDSDMERVNTVPPNSPVLRVTPNGFSVPMTSLRRSSTMELESTSLDKIHVECESASIIPQENSCYVVSSSSSARGSGLDSDFGASAGVSLRILSMDSDGFPGSAWASALEWDYYDPSYVTQNHVPKHRPQAPPITTKQYWV
Protein: Hydroxymycolate synthase MmaA4 (EC 2.1.1.-) (Mycolic acid methyltransferase) (MA-MT) (S-adenosylmethionine-dependent methyltransferase) (AdoMet-MT) (SAM-MT) (Q79FX8)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC).
Interaction partners:
- Methoxy mycolic acid synthase MmaA3
Sequence:
MTRMAEKPISPTKTRTRFEDIQAHYDVSDDFFALFQDPTRTYSCAYFEPPELTLEEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVERFDVNVIGLTLSKNQHARCEQVLASIDTNRSRQVLLQGWEDFAEPVDRIVSIEAFEHFGHENYDDFFKRCFNIMPADGRMTVQSSVSYHPYEMAARGKKLSFETARFIKFIVTEIFPGGRLPSTEMMVEHGEKAGFTVPEPLSLRPHYIKTLRIWGDTLQSNKDKAIEVTSEEVYNRYMKYLRGCEHYFTDEMLDCSLVTYLKPGAAA
Protein: H6 family homeobox 4 (B7ZD71)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MSKEDASCRPASLKFTIDNILNSKTSSRNFDSCHSRASLVVCRDGCLHHPGESEDPCKEGSDARLHGIDKLNREGDATVDALKAVDMRSESADSCDDAQQKNNGKKNKLMTKKKTRTIFSKRQIFQLESTFDMKRYLSSAERACLANSLQLTETQVKIWFQNRRNKLKRQLSTELEGPNSEFGDIGKTVPLPALYKENNLLGRCMLPMPLPVVYPGGSAPYFYFSNASKYFSLFDGDI
Protein: 60S ribosomal protein L32 (Q8I3B0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 40S ribosomal protein S7
- Ribosomal protein S27a, putative
- 60S ribosomal protein L30e, putative
- 40S ribosomal protein S10, putative
- 40S ribosomal protein S17, putative
- Small ribosomal subunit protein uS2
- 60S ribosomal protein L10, putative
- 40S ribosomal protein S4
- 40S ribosomal protein S19
- 40S ribosomal protein S19
Sequence:
MAVKKVGKIIKKRTKKFTRFQSNRFMRVKPAWRKPRGIDCRVRRRYKGTNLMPSIGYGSNKKTKFLLPNNKYKYVVKNVKEMEPLIMNHTKYCVQIAHNVSSKKRKQIIERAKQMNVSVINAKARLQKTEE
Protein: Adenosine kinase (AK) (EC 2.7.1.20) (Adenosine 5'-phosphotransferase) (Q54MB5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
Interaction partners:
- Probable adenine phosphoribosyltransferase
- Adenylosuccinate lyase
- AMP deaminase
- Adenosine deaminase 2
- Probable adenosine deaminase
- Adenylate kinase
- Probable adenylate kinase B
- 3',5'-cyclic-AMP phosphodiesterase 4
- Adenylate kinase isoenzyme 6 homolog
- 3',5'-cyclic-nucleotide phosphodiesterase regA
Sequence:
MSNIKILCAGNPLLDLSTHVEMAILDKYELKLGNAILAEDKHLPLYGEIKSGKVEYIPGGAAQNTSRVCQWMLKDKQTVCYTGCVGTDENATILKTATESNGVVTKYQVDSSAPTGACAVLINHKERSMVTNLGAANNFKIAHFQTEEMKAIVNSAQFFYLVGYFLTVSPDSAVHLGKHAAENDKPFLYGLAAPFLIDFFFDKVSELLPYVDIVFANESEAATLGRKMNWGEDLTVIAEKLAAWEKVNTKRTRTVVFTQGPDATLVFQNGVLTKYNPIKVATEDILDLNAAGDSFCGGFLAAYSNGQEIAKCVEAGHYASWEIIRQNGATVPASEPKIQF
Protein: Cytochrome c oxidase subunit 2 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide II) (P68530)
Organism: Bos taurus (Bovine)
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:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Multi-pass membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}.
Interaction partners:
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 7A1, mitochondrial
- Cytochrome b
- NADH-ubiquinone oxidoreductase chain 2
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 6C
- Cytochrome c oxidase subunit 7C, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4
Sequence:
MAYPMQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSELKPGELRLLEVDNRVVLPMEMTIRMLVSSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSSRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML
Protein: DNA ligase 3 (EC 6.5.1.1) (DNA ligase III) (Polydeoxyribonucleotide synthase [ATP] 3) (Q9C1W9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Flap endonuclease 1
- ATP-dependent DNA helicase II subunit 2
- ATP-dependent DNA helicase II subunit 1
- DNA ligase 1
- Exodeoxyribonuclease 1
- Proliferating cell nuclear antigen
- Probable tyrosyl-DNA phosphodiesterase
- Inheritance of peroxisomes protein 2
- Uncharacterized protein C12G12.16c
- Aprataxin-like protein
Sequence:
MPPKKRMKNGSSLKSTSKKGEKSRNIITIQDLFSKREAQLTDTPNKLLTDHDQSASDYAYALKLQQLFDSENQATAPEKLPKDVIIPEEEYHTDTFNVVKESNDKPKENLVTSEECKASFFSTDSVNKDSTIDYDALQKDPLTYVKSCRARFVSKDTKSFSYSSLANTFSLISSTKSRIRIVTLLTNFLLTLLYADPDSLIATVWLCTNSIAPNFYGKNLGVGPAMYSKALKEVCGITASALKNLWNKYGDPGDVAFEAKVSVRTLSRPEPLTIKKVYSTLLKIADSNGNGAQNRKLELTKFLLISSNAEEVRYIGRSIMQNLRIGAVQNTMLASLSKAFFIFDNQNEIFNFNSDSLQQQFRQGEEIVKQSFFQVPDYNILVATLLREGIENLKDNMSIRPGIPVKPMLGSITKNLQHMLERLTDHNFSCEFKYDGQRAQIHCDRLGNIKIFSRHLEEITGRFPDVIEVAQLALKHSCDFIIEGELVAIDKSNGQILDFQKLSTRERKKVTVADITIDVCVFVFDIMFCDGKSCLQMPLIERRRMFFEHFNLIPNRFQFVSSLETNEEQSIQEFFSLAITNKCEGLMVKVLNGTNSKFPSTYEPDKRGEGWIKVKQDYDDEFESLDLVPIGAWYGNGRKAGWFSPILLAVYNPDTGAYEAVCKCMSGFSDQFYKELTQKYSLESGNSSLKPIYNFCETGKVTPQIYFAPQEVWEIKGAQITSSPAYKAALGLIQDDRGLSIRFPRFIRVRSDKGPEDASTNSILADMYMKQLNT
Protein: Uncharacterized protein (Q383X5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKTYSELLAVCTEFRENFAALSEKYAGVTHELQSERERSERLVKQLEAAKNNEDRLNSGMRELKKELEEALAYKDRYLAATVSVEHLKGRLENARHAVADNLLEQEQQMDQLRAQIKDLQQRLNVSADVTVVQQLKRQVSELEERCAVQNGQLLEERERFSQQLLTAHNALREQQGRQLEVEQRCRSMEAELLQMRSLVRRSSDLQNDAAVSREKCVSDARKAALQVETLTAELRDAQVRLCEAESRHAEELEALRVEDAEEKARLLERVSQLSAAADEAAAQRVQEQEKYSALQRSVHQQLETVRADAREEVAAVQKLLADSRSEQQQQGWRVEQTRSELEESKRLLRQREAKLESYAAECKQLRTQMETLTQREEWLTAERDHLSQHLAAARKQVQDLVASHKGQEESGLEVERLRIQLRFREEELQEARRLVEVSETHVKDLEDAADRRVRLVRQELKRIKKQAKVESSQAETVRRRLVHALLERDMELRPCYSLETMERKPPQREQRVPSTYAHAFPTAPSGLDVMTLLRGQTEQAEALHQRLVELSK
Protein: AAA family ATPase (A0A1D8PU31)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Ist1p
- ESCRT-III subunit protein
- Uncharacterized protein
- Tubulin beta chain
- Tubulin alpha chain
- Vacuolar protein-sorting-associated protein 46
Sequence:
MFLRKKPPQISTLDELQQTYNDCCNLTIKNLTLEEENNVEDALKGWKSLHTSLLYKLDIFDKMSSKLNPEEKTILGELKGIRDENIKHLIRVQLRLDEVNRRKHREANHGAPPPPPPPRSTVSNSTSNINVPSTLRNSSSQSTSAGGAASRPMMKSLRPHSNGHSASSSSSLSKTHARLKPKSVQEASTAASASWTKPITSQQKYQISKSNLKSKKDDLFQDFDQDTYTPNRNDSGNWEKFANSRSSSGLSEYSNEEDGGDYNLIDLDDYNGNGSLSHSMDDLTIKPVISPKDASSSSAYTSIPAQQHHTPVQSKSSAGNANKSNGLLRPSQQMEHISKSTSDIRTKPKIPYVYTKPKPMNIQRLMRQSASQSKSSPSSSSPSNKPVTTSKVAATTAGKTAKPKPKSNITYNFVRAPAPGKLKAANSTPTTTSRPRTNGASAGTVNKQGSKQPSTSVRRPSKPAEDEQINSPTMDDLLSGYEDNPQNDLDEDDNSKNLILTNEKHQDKLIASIRGIDPTAAKQILNDVVVHGDEVYWDDIVGLEGAKNSLKEAVVYPFLRPDLFRGLREPTRGMLLFGPPGTGKTMLARAVATESNSTFFSISSSSLTSKYLGESEKLVKALFLLAKKLAPSIVFMDEIDSLLGARTEGEIESTRRIKNEFLVQWSELSSAAAGRETDDGDVSRVLILGATNLPWSIDEAARRRFVRRQYIPLPEDEARISQIKKLLKYQKNTLDDSDYNKLIELTKGFSGSDITALAKDSAMGPLRSLGDKLLSTPTEQIRPISLEDFENSLKYIRPSVSSDGLKEYEDWASKFGSSGA
Protein: Myosin-3 (Myosin heavy chain A) (MHC A) (P12844)
Organism: Caenorhabditis elegans
Function: Essential for muscle contraction. Involved in ovulation likely by regulating the contraction of gonadal myoepithelial sheath cells.
Subcellular location: Cytoplasm, myofibril {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:6352051}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:6352051}. Note=In myoepithelial sheath cells, forms filaments assembled in a nonstriated meshwork. Colocalizes with unc-15/paramyosin and with unc-89 to M line-like structures. Does not colocalize with beta integrin pat-3. {ECO:0000269|PubMed:17326220}.
Interaction partners:
- Myosin, essential light chain
- Myosin-4
- Troponin T
- Tropomyosin isoforms a/b/d/f
- Troponin I 2
- Myosin regulatory light chain 1
- Alpha-actinin, sarcomeric
- Troponin I 1
- Cuticle collagen rol-6
- Myosin regulatory light chain
Sequence:
MSGNPDAFENDPGFPFLGISREARAATAARPFDSKKNCWIPDPEDGFVAAEIQSTTGEQVTVVTVKGNQITVKKDQCQEMNPPKFDKTEDMANLTFLNEASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGESGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAELTIEGMDDKEEMRLTQEAFDIMGFEDNETMDLYRSTAGIMHMGEMKFKQRPREEQAEPDGEEDALNAAAMLGIQAEEFLKALTKPRVRVGTEWVNKGQNLEQVNWAVSGLAKAIYARMFKWIITRCNKTLDAKEIERKHFIGVLDIAGFEIFDLNSFEQLWINFVNERLQQFFNHHMFVLEQEEYKREGIAWTFIDFGLDLQACIELIEKPLGIISILDEECIVPKATDMTYAQKLLDQHLGKHPNFQKPKPPKGKQGDAHFAIVHYAGTVRYNATNFLEKNKDPLNDTAVALLKHSTDNSLMLDIWQDYQTQEEAAEAAKAGQTAGGKRGKSSSFATVSMIYRESLNNLMNMLYQTHPHFIRCIIPNEKKASGVIDSALVLNQLTCNGVLEGIRICRKGFPNRMLYPDFKHRYAILAADAAKESDPKKASVGILDKISVDGNLTDEEFKVGETKIFFKAGVLAKLEDLRDEILSRIVTMFQSRIRSYLAKAEVRRRYEQQTGLLVVQRNVRAWCTLRTWEWFKLFGKVKPMLKAGKEQEAMGELAVKIQKLEEAVQRGEIARSQLESQVADLVEEKNALFLSLETEKANLADAEERNEKLNQLKATLESKLSDITGQLEDMQERNEDLARQKKKTDQELSDTKKHVQDLELSLRKAEQEKQSRDHNIRSLQDEMANQDEAVAKLNKEKKHQEESNRKLNEDLQSEEDKVNHLEKIRNKLEQQMDELEENIDREKRSRGDIEKAKRKVEGDLKVAQENIDEITKQKHDVETTLKRKEEDLHHTNAKLAENNSIIAKLQRLIKELTARNAELEEELEAERNSRQKSDRSRSEAERELEELTERLEQQGGATAAQLEANKKREAEIAKLRREKEEDSLNHETAISSLRKRHGDSVAELTEQLETLQKLKAKSEAEKSKLQRDLEESQHATDSEVRSRQDLEKALKTIEVQYSELQTKADEQSRQLQDFAALKNRLNNENSDLNRSLEEMDNQLNSLHRLKSTLQSQLDETRRNYDEESRERQALAATAKNLEHENTILREHLDEEAESKADLTRQISKLNAEIQQWKARFDSEGLNKLEEIEAAKKALQLKVQELTDTNEGLFAKIASQEKVRFKLMQDLDDAQSDVEKAAAQVAFYEKHRRQFESIIAEWKKKTDDLSSELDAAQRDNRQLSTDLFKAKTANDELAEYLDSTRRENKSLAQEVKDLTDQLGEGGRSVAELQKIVRKLEVEKEELQKALDEAEAALEAEEAKVLRAQIEVSQIRSEIEKRIQEKEEEFENTRRNHQRALESMQATLEAETKQKEEALRIKKKLESDINDLEIALDHANRAYADAQKTIKKYMETVQELQFQIEEEQRQKDEIREQFLASEKRNAILQSEKDELAQQAEAAERARRNAEAECIELREQNNDLNAHVSALTGQRRKLEGELLAAHAELEEIANELKNAVEQGQKASADAARLAEELRQEQEHSMHIERIRKGLELQIKEMQIRLDDAENAALKGGKKIIAQLEARIRAIEQELDGEQRRHQDTEKNWRKAERRVKEVEFQVVEEKKNEERLTELVDKLQCKLKIFKRQVEEAEEVAASNLNKYKVLTAQFEQAEERADIAENALSKMRNKIRASASMAPPDGFPMVPSASSALIRSSSNARFL
Protein: Zinc finger protein 417 (Q8TAU3)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription intermediary factor 1-beta
Sequence:
MAAAAPRRPTQQGTVTFEDVAVNFSQEEWCLLSEAQRCLYRDVMLENLALISSLGCWCGSKDEEAPCKQRISVQRESQSRTPRAGVSPKKAHPCEMCGLILEDVFHFADHQETHHKQKLNRSGACGKNLDDTAYLHQHQKQHIGEKFYRKSVREASFVKKRKLRVSQEPFVFREFGKDVLPSSGLCQEAAAVEKTDSETMHGPPFQEGKTNYSCGKRTKAFSTKHSVIPHQKLFTRDGCYVCSDCGKSFSRYVSFSNHQRDHTAKGPYDCGECGKSYSRKSSLIQHQRVHTGKTAYPCEECGKSFSQKGSLISHQRVHTGERPYECREYGKSFGQKGNLIQHQQGHTGERAYHCGECGKSFRQKFCFINHQRVHTGERPYKCGECGKSFGQKGNLVQHQRGHTGERPYECKECGKSFRYRSHLTEHQRLHTGERPYNCRECGKLFNRKYHLLVHERVHTGERPYACEVCGKLFGNKNCVTIHQRIHTGERPYECNECGKSFLSSSALHVHKRVHSGQKPYKCSECGKSFAECSSLIKHRRIHTGERPYECTKCGKTFQRSSTLLHHQSSHRRKAL
Protein: Mitogen-activated protein kinase kinase kinase 6 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 2) (O95382)
Organism: Homo sapiens (Human)
Function: Component of a protein kinase signal transduction cascade. Activates the JNK, but not ERK or p38 kinase pathways.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 3
- Dual specificity mitogen-activated protein kinase kinase 6
- Mitogen-activated protein kinase kinase kinase 5
Sequence:
MAGPCPRSGAERAGSCWQDPLAVALSRGRQLAAPPGRGCARSRPLSVVYVLTREPQPGLEPREGTEAEPLPLRCLREACAQVPRPRPPPQLRSLPFGTLELGDTAALDAFYNADVVVLEVSSSLVQPSLFYHLGVRESFSMTNNVLLCSQADLPDLQALREDVFQKNSDCVGSYTLIPYVVTATGRVLCGDAGLLRGLADGLVQAGVGTEALLTPLVGRLARLLEATPTDSCGYFRETIRRDIRQARERFSGPQLRQELARLQRRLDSVELLSPDIIMNLLLSYRDVQDYSAIIELVETLQALPTCDVAEQHNVCFHYTFALNRRNRPGDRAKALSVLLPLVQLEGSVAPDLYCMCGRIYKDMFFSSGFQDAGHREQAYHWYRKAFDVEPSLHSGINAAVLLIAAGQHFEDSKELRLIGMKLGCLLARKGCVEKMQYYWDVGFYLGAQILANDPTQVVLAAEQLYKLNAPIWYLVSVMETFLLYQHFRPTPEPPGGPPRRAHFWLHFLLQSCQPFKTACAQGDQCLVLVLEMNKVLLPAKLEVRGTDPVSTVTLSLLEPETQDIPSSWTFPVASICGVSASKRDERCCFLYALPPAQDVQLCFPSVGHCQWFCGLIQAWVTNPDSTAPAEEAEGAGEMLEFDYEYTETGERLVLGKGTYGVVYAGRDRHTRVRIAIKEIPERDSRFSQPLHEEIALHRRLRHKNIVRYLGSASQGGYLKIFMEEVPGGSLSSLLRSVWGPLKDNESTISFYTRQILQGLGYLHDNHIVHRDIKGDNVLINTFSGLLKISDFGTSKRLAGITPCTETFTGTLQYMAPEIIDQGPRGYGKAADIWSLGCTVIEMATGRPPFHELGSPQAAMFQVGMYKVHPPMPSSLSAEAQAFLLRTFEPDPRLRASAQTLLGDPFLQPGKRSRSPSSPRHAPRPSDAPSASPTPSANSTTQSQTFPCPQAPSQHPPSPPKRCLSYGGTSQLRVPEEPAAEEPASPEESSGLSLLHQESKRRAMLAAVLEQELPALAENLHQEQKQEQGARLGRNHVEELLRCLGAHIHTPNRRQLAQELRALQGRLRAQGLGPALLHRPLFAFPDAVKQILRKRQIRPHWMFVLDSLLSRAVRAALGVLGPEVEKEAVSPRSEELSNEGDSQQSPGQQSPLPVEPEQGPAPLMVQLSLLRAETDRLREILAGKEREYQALVQRALQRLNEEARTYVLAPEPPTALSTDQGLVQWLQELNVDSGTIQMLLNHSFTLHTLLTYATRDDLIYTRIRGGMVCRIWRAILAQRAGSTPVTSGP
Protein: Chaperone protein HtpG (Heat shock protein HtpG) (High temperature protein G) (P42555)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Molecular chaperone. Has ATPase activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
Interaction partners:
- Chaperone protein DnaK
- Heat shock protein 70
- Chaperonin GroEL
- Co-chaperonin GroES
- Heat shock protein
- Chaperonin, putative
- Chaperone protein DnaJ
- Protein GrpE
- ATP-dependent protease subunit HslV
- ATP-dependent protease ATPase subunit HslU
Sequence:
MKKQFDTEVNDLLYLIIHSLYSHKEIFLRELISNASDAIDKLKFLSLTNEKFKNIALEPKIEISFDDKSILIKDNGIGMDEQDLTNHLGVIAKSGTKEFINNLKQDEKKSASLIGQFGVGFYSAFIVSEKVEVTSKKALESDAYIWSSDGKTGYEIEKAKKEESGTEIKLYLNKEGLEYANKWKIQEIIKKYSNHINYPIYIKYSEPIMKDGKQEGIEEKEEKLNETTALWTKNKSEIKAEEYNEFYKNTTFDYENPLMHIHTKAEGNLEYTNLFYVPSKAPYDLYYPNTKPGVKLFINRIFITDSEGSLLPNYLRFIKGIIDCQDLPLNVSREILQQNKILSKIKSSSVKKILSELEKLSKKNPEKFSEFSKEFGRCIKEGVYSDFENREKLISLIRFKSSSVDGFVSFKEYKERMNESQKSIYYITGGKENILKENPIVAAYKEKGFEILIMDDELDEAILNLIPEYEGLKLKAINKNETSNELKDENFKKIEEEFKDTLTKVKEILKDHIKEVNLSATLIKEPSAIIIDSNDPTYQMQKIMLSMGQEVKEIKPILELNPNNKIVQNLKNLEPEKLEKISILLFEEAMLTSGMPSKNPGKFINIINEFIEKDFL
Protein: Tyrosine kinase-like protein (EC 2.7.10.2) (Q8IIF4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Gametocyte-specific protein
Sequence:
MSKSLKLMEDKNLEKNAVEAFKQKMEKKKQEYLRFNLSRNGENMKEGDEKKKEIDINNNHNFNINNHHVNDKHINNKYINNYMNNRHIKNIHVNNDHINNIHVSNNHINNIHVSNNHINNNHIKNNNDINRKNSNRHKNRKVVYIETYDTYDKYILNMYDEENEIYEDEINRENVESRTPNEGMEFNRIEKREENIFIPLKILSNKYDFNDLVEATNNFSEYNRIAKGGNGTVYKGVLKNCINVAIKVLKKNENNGFENEIIIMSRYRHNNILSLLGYATNKNNFYLIYEYVNLGDLRTLLFNHYYYYNSKNKENPELSYYNISCYENYLRKKKSSSSCSSTNYYTSTFYKQNIFPYFNNSKYSPFQQNSFDNNTPLFLSFNIRINILVQIINVLCYLHTSSPIVYHRDLKSANILIDDQFNAKLGDFGLSFVYMNNNNVFNLTGGTPGYADPYYISTHEINEQTEIYSFGALILEMLVSKSPAIHVGKNYNCIYSKNEKCPIFYHKKKHDHDDNVFDYLVNHLNMSDYKSIYSILDYSVNFPDFLVEKLTKLSFLCLNPNIKNRPSSKLVNLILLEIQKECDLFMKKQQETFKRKFNCINMYLEDMERGEQKQNKKKIYNNNNINSHNNSCNSNIIQKNETKFSESKGNNKNKKFKSEDSNKLEENYNIFLKKIKEINYNTLKKSFYNFVYPMFKNENIYNFSEHIMHKRNKKCPVEHIKQHMENAKKVSSTMEYNELNMNDIPTPDYIRFKYNTISNLCNIKECILHRMHKDFFSKNYILNSFSFNLMNCYFLKFISNYLKYVNMPNGSNSLLIKDGDDDDDDDNEHDEEDYDDEKEEGEYEQVHLSKKKYIEDKYKEEIYKEEIYKEEIYKEEIYKEEIYKEEIYKEEIYKEEIYKGEIYKEEIYKEEIYKEEKYKDDIHDEEKYKDDIHNEEKYKNDIHNEENKEGKPSSSFKTPIERLFKIYQEDIHNNMNNKLKKKKTMKEQIQQKKKNNNISNINHIDNSNNVDNNKENVNNKKNKQMNLEENNIYNNNNNNNNNADNNQNIYNKNINYHNNISNNPFKGIEKDYIDKNNMINVIPKCPLKNPNLNNIYANYANNQNDVRYQVPFNNNDYLLNNHNFLEPNPDHINNINNNNNNNYYYYYNNNQIYMNNCYMNNKYNNMNMEHMKNYYNNGYNNEYYNHINLSNIPYNNIQLQNGHFHNINMNNQNMIPFQNINNTLYASNQVKINNEHIINDVHNNICNNMQNISKNVGKSSSSDINHEINDAQNILSNSNEQYLKGNYRNNTPKISFHLNKEKNNEQDIKEACLNNKENISKNLENLRKLHNDIQKEKDVNNIKETDEDTYCNSSSLLRDYNIHKKNMNNNDLLLSDDNFMMSPYDNINDTHILYISNFVNFINLENNKNINDSNTCAWFNKNVFEVLIDEHKFFSSVTFLDILYEFNVFNVKRDGHVFIEHDNEYVLQGKWCDYDPNKNNSTSVNFEENFCFEIAISEDNENNTHSVFLLKSNQLKYTDNIQNDNTITKKIWVSEYLGRRNEFLEKILKRNISNILYECISRKHCLFLLEVLMKKINKPTSYDNKVKGNFSYFYFEYNIKVLCNSENCIFTNNHILHKNNTYSYKLPNNILSLLVFSEDKLIKGKYHPENQINTTQKVHFPLYPFFVNINFYNEK
Protein: Increased copper sensitivity protein 3 (P47034)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ataxin-10 homolog
Sequence:
MHISLPTRNKSYFRIRTRTYQIGLYHSDSSPIRDISVLHLLIATLCTIFFPIFFSLSKVQVVQWQGTTISKNCIALTMSFPLNAIPGMYLIIAFPRLQTVIPLQRNTPVRITKSVIVKGAVSVPRISSPMH
Protein: Tissue factor (TF) (Coagulation factor III) (Thromboplastin) (CD antigen CD142) (P13726)
Organism: Homo sapiens (Human)
Function: Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade.
Subcellular location: [Isoform 1]: Membrane {ECO:0000269|PubMed:12652293}; Single-pass type I membrane protein {ECO:0000269|PubMed:12652293}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:12652293}.
Interaction partners:
- Coagulation factor X
- Tissue factor pathway inhibitor
- Coagulation factor VII
- Prothrombin
- Coagulation factor IX
- Thrombomodulin
- von Willebrand factor
- Antithrombin-III
- Coagulation factor VIII
- Plasminogen
Sequence:
METPAWPRVPRPETAVARTLLLGWVFAQVAGASGTTNTVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIVKDVKQTYLARVFSYPAGNVESTGSAGEPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNVTVEDERTLVRRNNTFLSLRDVFGKDLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVECMGQEKGEFREIFYIIGAVVFVVIILVIILAISLHKCRKAGVGQSWKENSPLNVS