wanglab/gogpt-training-data huggingface dataset:
Protein: Type II NADH:quinone oxidoreductase NdhA (EC 1.6.5.9) (Type II NADH dehydrogenase NdhA) (P95200)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Alternative, nonproton pumping NADH:quinone oxidoreductase that delivers electrons to the respiratory chain by oxidation of NADH and reduction of quinones.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15767566}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH-quinone oxidoreductase subunit A
Sequence:
MTLSSGEPSAVGGRHRVVIIGSGFGGLNAAKALKRADVDITLISKTTTHLFQPLLYQVATGILSEGDIAPTTRLILRRQKNVRVLLGEVNAIDLKAQTVTSKLMDMTTVTPYDSLIVAAGAQQSYFGNDEFATFAPGMKTIDDALELRGRILGAFEAAEVSTDHAERERRLTFVVVGAGPTGVEVAGQIVELAERTLAGAFRTITPSECRVILLDAAPAVLPPMGPKLGLKAQRRLEKMDVEVQLNAMVTAVDYKGITIKEKDGGERRIECACKVWAAGVAASPLGKMIAEGSDGTEIDRAGRVIVEPDLTVKGHPNVFVVGDLMFVPGVPGVAQGAIQGARYATTVIKHMVKGNDDPANRKPFHYFNKGSMATISRHSAVAQVGKLEFAGYFAWLAWLVLHLVYLVGYRNRIAALFAWGISFMGRARGQMAITSQMIYARLVMTLMEQQAQGALAAAEQAEHAEQEAAG
Protein: Neurogenic differentiation factor 4 (NeuroD4) (Helix-loop-helix protein mATH-3) (mATH3) (Protein atonal homolog 3) (O09105)
Organism: Mus musculus (Mouse)
Function: Probably acts as a transcriptional activator. Mediates neuronal differentiation. Required for the regulation of amacrine cell fate specification in the retina.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Visual system homeobox 2
- Forkhead box protein N4
Sequence:
MAKMYMKSKDMVELVNTQSWMDKGLSSQNEMKEQERRPGSYGMLGTLTEEHDSIEEDEEEEEDGDKPKRRGPKKKKMTKARLERFRARRVKANARERTRMHGLNDALDNLRRVMPCYSKTQKLSKIETLRLARNYIWALSEVLETGQTLEGKGFVEMLCKGLSQPTSNLVAGCLQLGPQSTLLEKHEEKSSICDSTISVHSFNYQSPGLPSPPYGHMETHSLHLKPQPFKSLGDSFGSHPPDCSTPPYEGPLTPPLSISGNFSLKQDGSPDLEKSYNFMPHYTSASLSSGHVHSTPFQTGTPRYDVPVDLSYDSYSHHSIGTQLNTIFSD
Protein: Raptor N-terminal CASPase-like domain-containing protein (G5EEV7)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEEDRSITPFSSFAERLTVNLWHAQRNVERVTLYLQEPRHVEDIAGSMEDEWDCIEECVNRRKGSDRLRTASVAIIMCLHLGVDPPEAPSRKDAPSRLLSWVDPYKCGAHKAAIEIGLSTQRAYEKWQPKSKTRYKICTDPPIDDVRKVATNLRRISGNDRVLFHYNGHGVPKPTDNGEIWVFNKSFTQYIPLSIFDLQGWLDYPTIYIWETHSAETILHNYRRFGEDQKISWQSRFDRWQEEQRNLPPISSKMTDADQAEALGFPEKYPRYNDCIHLAACSAGQWLPMSNPHLPADLFTSCLTTPIRTSLAFHLSHSEHRDEYPENILDMIPGNLAERRTVLGELNWIFTAITDTIAFTSIDRDSFQKLFRQDLLLATLFRSFLLAQRVMSKFNVLPVSQPPLKDTSMHDLWRCWDQTMDMVLDYCRELIYVKECERALFCGRDVINRSNVFPFLVLIDFEHVLTYNETHQYNTFFTEQLQAFELWLDYGVDEGTPPLQLPMVLQVLLSQAHRVRALRLLARFLDFGRWAIGYSLAVGIFPYVLKLLQSNISDLKISLAFIWAKILAVDPSCQMELFNECIDESATQQQSPAQSQQPSVALKPSSMFANHPPPAQLTMDKRALQINTQTGGRFQTNQNQALDMQLQYAQQQAHQRQMDPSGGQHSPNAQPRQPQPQQPQQLQQQPSQQQQQQSRQPQGIMKPTNAQPQEKKTMLRFQYFLQLLGDPEIKPKQKTVAAFVLAQLTSNNFKLAQKELTNKGYMGICTELMVDDTARSVKLLKLWILIGLGRLWSDYDVARWQGIRLMAHDKMILELSDESAEVRAAAVFALGSLLRNSSRSNEHASAVEENLAGELCSQCVFDSSVLVREELIVALQWFVFDFEKRFVKFLLELSNQIKFKLPRKRNSSENLSEQGLDIAAEMPSNHRRPRAPPVNEFMQPSVIRKKMSTSVFSTAVEETVHEDGIGNVYHIAHEAGNRVEQESEDIEYRERAKVQIKHLEAKTFNEAVAKTWLSLLILSLDPIERVARMAQKIVHRVEAGMPEMQANIDNTMAHLSRKMIARKNSKATVEMPRKPVGPSEEVSTLSERIKRNLEVEKVVEMIPESGVSADGIDFTKLNMQKAKEQRKGGKGGQIKKLQDESKVKFQVGSPGDVNQQHKNALSPGSSFTDETQSSELFSKDDSSDDDENKSANDEKDRATTASGKTVKGAFRKSDIMDAALMEFTPRRTKAVPGDFAVKEESKTLRTVIENPIVSTQFVAWCSKVFVEPILHVITLDEEKSEDWEHEDEDEFMPEQFREKIKDIQKQDRKMHEEKRARDKKEGKKEKSQEDVVVTTTTISDWAIHAMEGMLQSADIEGRDFQSCKYDECLWRVKLTHPARSLTTSKLRRCMYASDGRLMTIIRQDTDTRSFRRFDLTASNPFCPSYVSQLILINDMSREMVIACSTNGVVRIWDPYFLGWCDDYEKPPELVSASFPLESQMKISDETNRCLFDWNQQNGKLLCTGTRSVRIWDAHCEKVCHDVMYSPGSKQQTGPGAKLNTNTLPTAMSGNLDEEGNMVAVGYADGRVDYFDMRMANPKAARCNLAPVNMSKQFNDRPPGIMHLRVNRQGFGTELFAGSQDGSIYKLQLRMFKEATPSIVTPWEYGAHSHMFVHEDSRILASAGGGELAIYDVAQNKLMARILPPGEPNSMRRDKNSSTFGLFSSQRKLSQVQMSGRMSSMSSATVGEDRQPKVISLTMHQMRLLTVAGYDDNTVCVYGSPKPGLTGHYENTQGASSPPSQSL
Protein: Uncharacterized protein (Q57V21)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNVSEFLKVWKDVKVCDDVVADGGSGGCNLDIGVPSLSEVDDGDEVPVEYGDVSRDDFGGDDGGCEVFDEAGSFFYGQRSKRRRYDGLKTDSISLCKPREPYACLKTFSTNEGSYDNFVSGDSGRKRVKVQIAGRGKPRKGSLAAVTALREELLRKKTLLDKSCRQEVVDSSTNEEFPTIAEGESTLDELLLSVEDLVPVGNLATIVEKSLAPAQTSSVEDPTLSAVSTEAETPLKVDEPGERKESTGSAPKAGKLSMFARAKLYVSGGDALEGKANIEDFFGKRFTS
Protein: Olfactory receptor 7D2 (HTPCRH03) (Olfactory receptor 19-4) (OR19-4) (Olfactory receptor OR19-10) (Q96RA2)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MEAGNQTGFLEFILLGLSEDPELQPFIFGLFLSMYLVTVLGNLLIILAISSDSHLHTPMYFFLSNLSWVDICFSTCIVPKMLVNIQTENKAISYMDCLTQVYFSMFFPILDTLLLTVMAYDRFVAVCHPLHYMIIMNPHLCGLLVFVTWLIGVMTSLLHISLMMHLIFCKDFEIPHFFCELTYILQLACSDTFLNSTLIYFMTGVLGVFPLLGIIFSYSRIASSIRKMSSSGGKQKALSTCGSHLSVVSLFYGTGIGVHFTSAVTHSSQKISVASVMYTVVTPMLNPFIYSLRNKDVKGALGSLLSRAASCL
Protein: AT4g02340 protein (AT4g02340/T14P8_15) (Alpha/beta-Hydrolases superfamily protein) (T14P8.15) (O81299)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative acyl-activating enzyme 19
- Pullulanase 1, chloroplastic
- Methionine gamma-lyase
- AT2G24420 protein
- Dem-like protein
- Uveal autoantigen with coiled-coil/ankyrin
- Nuclear protein
- Phospholipase A1-IIdelta
Sequence:
MEKIEHTTISTNGINMHVASIGSGPVILFVHGFPDLWYSWRHQLVSFAALGYRAIAPDLRGYGDSDAPPSRESYTILHIVGDLVGLLDSLGVDRVFLVGHDWGAIVAWWLCMIRPDRVNALVNTSVVFNPRNPSVKPVDAFRALFGDDYYICRFQEPGEIEEDFAQVDTKKLITRFFTSRNPRPPCIPKSVGFRGLPDPPSLPAWLTEQDVRFYGDKFSQKGFTGGLNYYRALNLSWELTAPWTGLQIKVPVKFIVGDLDITYNIPGTKEYIHEGGLKKHVPFLQEVVVMEGVGHFLHQEKPDEVTDHIYGFFKKFRTRETASL
Protein: Protein FMP42 (Q04991)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- V-type proton ATPase subunit H
- Uncharacterized vacuolar membrane protein YML018C
Sequence:
MTSTRTLRYAQVACACIWCLFSAGIIFGFAALKPILISEGVYHELCDPKDGDRLLCTAQDLKLNFIFALSATVTNIMALPVGKILDMYGPRVCGIIGSCLLFLASGNFISAKHLVSLWDPYLVGYTLLAVAGPFVFISCFQLANSFPQRSGTVLALLTGSFDSSSALFLLYRLLYQNWFPTLNVSRFFTLYLIVPVFILACQLTIMPHSSYKTVNHIAKIAVEGLDENGRLIEGDTGSGIIPDEQERQSLIAIEREEDSIPSRPQRRKSVLETYVEDKLQKKSGGIFGVLHGKSAYEQIKSPWFYLMLLFALVAMLRINYFIATVRTQEEYLLNDPDLALKLNSIFDMLLPLGGAVSIPFIGLLLDHTDTLSTLTILFTTSTAIGVFGLIPNSFTWNLIGIVLLVVYRPFYYTVVSDYSSKVFGFDTFGTVYGLLSCICGIFNMSQNLLDKWTHTTFNMNPFPINLTLVILTVVFSLTLTFYIRSQILPKPVNERGLSSNYQTI
Protein: Palmitoyltransferase PFA5 (EC 2.3.1.225) (Protein fatty acyltransferase 5) (Q9C0W9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSTNLEEKQRRFSKLQKTLGVVFPAAILLSTGYTVWVFIALICVDSNIKIRNGYRNLGGGIVLIIFFFITSGLAYFSYFRVLFSSPSFCGNTLYTYYGFDNPIFLCGPNGAPRMCGTCKCWLPDRSHHSRVSMRCIRKFDHYCSFVGKDVCFSNQKFFYQFLFYGFSAACMVLISTAIMISRTYHYRSLPGTWIFVLVFSAFGVLFLGVMLVRHTGYLLLNINSHEAKNWKTRIYSFSVFFPEHMDSRVLVQSDPGDLPWDRGYSENWRAVMGDHWYNWILPLRRSPGDGEHFLYSPSFVSKMQSKALSMNS
Protein: SPI-2 type 3 secretion system ATPase (T3SS-2 ATPase) (EC 7.4.2.8) (P74857)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: ATPase component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Acts as a molecular motor to provide the energy that is required for the export of proteins (By similarity). Required for type III secretion apparatus (T3SA) formation, secretion of a subset of SPI-2 effectors and virulence. May play a critical role in T3SS substrate recognition, disassembly of the effector/chaperone complex and unfolding of the effector in an ATP-dependent manner prior to secretion (Probable). Releases the effector protein SseB from the T3SS-2 specific chaperone SsaE in an ATP-dependent manner.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24722491}. Note=Can associate with the membrane regardless of the presence of the other ATPase-associated components. {ECO:0000269|PubMed:24722491}.
Interaction partners:
- Secretion system apparatus protein SsaV
- Secretion system apparatus protein SsaQ
- Secretion system apparatus lipoprotein SsaJ
- Secretion system apparatus protein SsaT
- Virulence protein YscR
- SPI-2 type 3 secretion system stator protein
- Secretion system apparatus protein SsaL
- Secretion system apparatus protein SsaO
- Secretion system apparatus protein SsaU
- Flagellar biosynthesis protein FlhA
Sequence:
MKNELMQRLRLKYPPPDGYCRWGRIQDVSATLLNAWLPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTDTDKAIDTYPDICTFLRQSKDEVCGPELLIEKLHQILTE
Protein: Transmembrane protein (Q0PBN7)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Interaction partners:
- ATP-dependent zinc metalloprotease FtsH
- Membrane bound ATPase
- Integral membrane protein
- Zinc protease-like protein
- Zinc protease
- AAA family ATPase
- Branched-chain-amino-acid aminotransferase
- Integral membrane protein
- Integral membrane protein
- Chaperone protein DnaK
Sequence:
MPADLNDYFNKKNGNSNNNGNNNRQNFNFKAPEFNFKGFGKFSPFVYGVIIIILFLIVAKPFMVINSGEMGIKSTTGKYDPNPLEPGLHFFLPFVQKITIIDTRVRQINYASIEGSNENLSSGSGVINKNSISVLDSRGLPVSIDVTVQYRLNPLQVPQTIATWSLNWENKIIDPVVRDVVRSVVGKYTAEELPTNRNTIATQIEEGIRKTIEAQPNEPVELRAVQLREIILPSKVKEQIERVQIAKQEAERTKYEVERANQEALKKAALAEGEANATIISAKGKAMAVKIEADAQAYSNKEIANSLNTPLLNLKQIETQKEFNEALKVNQDAKIFLTPGGAVPNIWVDTKDAKKQSAANMN
Protein: Density-regulated protein (DRP) (Protein DRP1) (Smooth muscle cell-associated protein 3) (SMAP-3) (O43583)
Organism: Homo sapiens (Human)
Function: May be involved in the translation of target mRNAs by scanning and recognition of the initiation codon. Involved in translation initiation; promotes recruitmnet of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Plays a role in the modulation of the translational profile of a subset of cancer-related mRNAs when recruited to the translational initiation complex by the oncogene MCTS1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16982740}.
Interaction partners:
- Malignant T-cell-amplified sequence 1
- Mitochondrial fission 1 protein
- Mitochondrial fission factor
- Ubiquitin-like protein FUBI
- Mitochondrial dynamics protein MIEF1
- Mitochondrial dynamics protein MID49
- Small ribosomal subunit protein eS25
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS17
- Small ribosomal subunit protein uS17
Sequence:
MAADISESSGADCKGDPRNSAKLDADYPLRVLYCGVCSLPTEYCEYMPDVAKCRQWLEKNFPNEFAKLTVENSPKQEAGISEGQGTAGEEEEKKKQKRGGRGQIKQKKKTVPQKVTIAKIPRAKKKYVTRVCGLATFEIDLKEAQRFFAQKFSCGASVTGEDEIIIQGDFTDDIIDVIQEKWPEVDDDSIEDLGEVKK
Protein: Nucleoporin SEH1-A (GATOR2 complex protein SEH1-A) (Nup107-160 subcomplex subunit seh1-A) (Q4FZW5)
Organism: Xenopus laevis (African clawed frog)
Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore.
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
Interaction partners:
Sequence:
MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSENGNWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFDRTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGVVRIYEAPDVMNLSQWSLQHEISCKLSCSCISWNPSSSRAHSPMIAVGSDDSSPNIMGKVQIYEYNENTRKYAKAETLMSVSDPVHDIAFAPNLGRSFHILAVATKDVRIFTMKPLRKELSSSGGVTKFEIHTVAQFDNHNSQVWRVSWNITGTVLASSGDDGTVRLWKANYMDNWKCIGVLKGDGNPVGNSYQGFFGSSVGSAGQSLQNSVNGTPSSGRKHS
Protein: MAGUK p55 subfamily member 4 (Discs large homolog 6) (mDLG6) (Q6P7F1)
Organism: Mus musculus (Mouse)
Function: May play a role in retinal photoreceptors development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12859944, ECO:0000269|PubMed:15558731}. Note=Localized at photoreceptor synaptic terminals in retina. Localized in rod and cone photoreceptors at the plasma membrane and at membranes of intracellular vesicles around the subapical region (SAR) and adherens junction, and in the outer plexiform layer (OPL).
Interaction partners:
- Protein PALS1
Sequence:
MRQSDRGAELTNEDRALPTPPDPENGLSGILRLLLQELSLFYSRDVNGLCLLYDLLHSPWLQALLKVYDCLQRFKEKKLVPDTTHAQILACEVLELLPKASGSPEIQELRQVLQAPHCKALLSAHDTVAQKDFEPLLPPLPDNIPDSEEAMRIVCLVKNQQPLGATIKRHEITGDILVARVIHGGLVERSGLLYAGDKLVEVNGVSVEGLDPEQVIHILAMSCGTIMFKVIPVSAPPVSSQKMVYVRAMIDYWPQEDPDIPCMDAGLPFLKGDILQIVDQNDALWWQARKISDLTICAGLIPSNHLLKRKQREFWWSQPYQPHTCLKSTRALSMEEEDSMKIDEKCVEADEETFESEELAEAKDEFVGDGQKFFIAGFRRSMRLCRRKSHFSQLHASLCCSCSCYSAVGAPYEEVVRYQRQPADKHRLIVLVGPSGVGVNELRRQLIGCNPSCFQSAVPHTTRFPKSYEMDGREYHYVSRETFESLMYGHKMLEYGEYKGHLYGTSVNAVHAVLDEGKICIMDLEPQDIQSARTRDLKPYVIFIKPPNTSSMRHSRKNAKITTDYYVDMKFKDEDLQEMEELAQKMESQFGQFFDHVIVNDNLQDACGQLLSAIQKAQEELQWVPEAWVSPDTES
Protein: Beige protein homolog 1 (Q7LKZ7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in protein sorting and cell wall formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- GTP-binding protein ypt4
Sequence:
MDRKANAYSKSVELLSRLEGCPSEKVLLEELRKLRGFIRNDIPSNFFPQLFITDNGFAAIKKAVTKLNFQSLLSLDIFECCLQILGIATSYTILRSWLLSRKHIEAWIELAIRRMFYSFCAIQDDSNISIYAIGTSSKTDSSIQAASPNEDLKSEGAQEIDSQSETVSISSDVDYDEDRKDLKKAKICSAYYLKTRLLLAVLSFAQNDSTFSLLKLVPSLQDNTNASLVELSRVVEAAIQKLSIKPLAFPNVLPQVLLLCPSISIFNLILLHLRALIRSSPENAIKIGYSKTMHFLLTYLFEPPTSFPLSDVSKDLLNEITLHCATFGVSNASTAKVLRTYLKTKSEFLRTWLLKALSHLVAPSFYFNPSTKGYSSIDFTLSSPVMPINGYSVSLWLNIESLMNDDGNYAPTTLFLISDFLKSTLFRLLLDASKKTVVVHIGSSKDTCVVNFSTPITNFFSKIYKDNPSLNPPSWHLITLVHRNEKSSLPNLELYIDGSAVERAACPYPFLSSTLQPLYVSLGPSIGSRNQSTPSTLAPNVAETDALVSENTGAASQKTSKSYKTNDSLKVPPLVPLLIGTTRFFPVPLVSSQIAIISSLGPSYSGCFQGPINDYMTYKASTALTLEIQDSKSNTEDLLHSIQAFSRSPIAFMSCARDYVDIMDLQLSDFCSFSVLETLKKLENQYYSHVYINRAVSSYDKAFSAEQPSFGVSSGSVTPIIMQSISDAIYNIGGSSILLELVGTAETEAELNFGLQVFFSSIEDNWRFSENVEQTHSFEILAQILHSKSHLLVSEETLKIIALMSGVHHTRFKHPLVMNPLLFRYLILDFDLWSKAPNSNLFVQQLGYIVSLIENNDYAGFNVKRLMKMQILKKLLTAMRNCLFHKDLLPILRLLFKVLMTSAFVSENIRSVATYIIYASQATGKSKPIRRSSVSIAVDRSDSNYISIKESGYAICEEFIDLLIKSNGEPSFLRRFSSMITPAWLLFLLRQQDIHYFICGIRLLNQSICSLGSSFLSKFSQKFHGFLILHDNLKDHIHLEELWLNLLFLSLGLGIRSVQFRTDLTYKQKLDFVLKNELDNILPLSEVFPSLFHAIQATLEKVSNVNGKLNSENVAALRYADDTMSFLVTLQTTYSFELTLNYDFSELLTKVVFPFLSPVDTITAEQEMRDLLHNIRQPLPRSSSSKTFGEGIKKSVRKFSMSGSFKRVVTPLGTQLRKDILNDSITDMENTSSFTASFPQSDQALQYFDNFTVQYAEAKDVIKGLLFSILTCIYNRITSGQGFSYSRLLVYLPPSQIEKKSTFFSGILRSTMSKLIEAVKNDKLLLAEPSILANISYIFTKFIRMHLLGYLKGSWLEIVDDLGSLLEEIISRPDFLAKLPKNGRNAAMNMYSCFLDLFLLEVSDLKQTECNAQSDKIIKSITYWQSLLFNSKTYQKDLFSLLWYAVYIMVETTTGVVRLQAVDAWRLLFLHSPGYLSDIAKTCNNDPRFAYEICKTLDNDSDKFVRWLDDNAAEVNQFMLSCFFCRWEDFLKQQHKLADEEASLLQFSRLEHLRKQLAQNTFNENILNESSASYHVWISSLFALECNRFKKMSQDQSDQENFVAAALLSQKNELSHENSILGSKTTSWELDSTEGSERMRKRLMPCLLQSSELDSKLEARSSGARRNRSFDTSVEAPVSLTNEEKQAATLILPSQEETLHDAARSDSNNSMEDEEDDVDEEDKEDKNRTVMRSIESGDSIQDVYNVSRIFGLEATEGILLLGKQYLYLMDNFFLRSDNEIVDVNDNSIIDERDPYLQLLHLQSLSSSGKVRRHISKENNWHWDFIDLSLVLKRFYLLRDVGLELFFKDGRSFLTILSNTKNRDSLYQKLVARAPGADVLSTSHFATSMSRDLGKANGKSNFLSSKLANALSFSTTHPATKRWERREISNFNYLQIVNTLAGRTYNDLTQYPVFPWVIADYTSKELDLNNPKTYRNFCKPMGAQHPERESQFNERYDLLLGLNDSQQQPFHYGTHYSSAMIVCSYLIRLRPFVDSYLALQGGQFDHADRLFYSIEQAWRSSSKENMADVRELIPEFFYLSEMFINGNGFDFGSRQKESTPINDVILPPWAKGDPAIFVQKNREALESKYVSAHLHEWIDLVFGCKQRGDEAVAATNVFHHLSYQGAIDLENIENEFELAAAVGIIHNFGQTPKQVFKKPHPQRGPDFTDTPLGPYLFGRFEDSIHLLFQSCSPIIRICKKVAHIQYDPSKDEVGAFAADYTPLGPNTFLAWGRVDNTVQLISDQLDKQPVMFEELHSEKITHVVACDERTFLTASLDLTLRLWTLSTNKPIKASLKRVLYGHRYRITCVTVCKAFSIIVSGDAGGNLIIWDLNRAEFVSSLSVYKLPIQTIAVNARNAEIAFSTGFYCCVVNVNGKILVKDKLSRIYNENSDENILCSCFYTGANSEWLHKNLFITGHPDGIIRIWEKRLQSNAKLEAEKNNADRPKWRFHLLRQLQHTKGLGRNRVATRQNIITITPNGQARGIFAGDDKGQVFSWMLPDTTSNVHLEKDNTSELCSLCDSRFSLMEWRSQCRACGNSNVCSDCVSMLKDTNIKTCYECYRQMPLCYKN
Protein: F-actin-capping protein subunit beta (Q8I3T2)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU365078}.
Interaction partners:
- F-actin-capping protein subunit alpha
- Dynactin subunit 2, putative
- Dynactin subunit 4
- Dynactin subunit 6
- Dynactin subunit 5
- Dynein intermediate light chain, putative
- Vacuolar protein sorting-associated protein 45
- Actin-related protein
- Actin-like protein, putative
- Cofilin/actin-depolymerizing factor homolog 2
Sequence:
MNNDKMEAALNICNTLPGHVFDDTIKMLSRIDQSITNNILINKEGSIKINYDKEENKYYLGNMFNKEKDSYRSPYTNIYFPEHYINSYVPPEHLRTLEILYNKIFDRYRKAYYMNGLSSVYLWPNPIEDGFVACFLIKKKEIFDKETNIKWEATHLIQVNITNLNVHYQISCTINFEIKKNDNLLLSGNINKALENSKKVTDLYLIKDQYFHMENMGYLIECMENSLRKSIEYIYILKIQDMLNSIKYYNFTNHLTYNNTNKNISNISNSLIFSRENIQKELQTKIKQVRKK
Protein: Heme oxygenase 1 (HO-1) (EC 1.14.14.18) (P32 protein) [Cleaved into: Heme oxygenase 1 soluble form] (P14901)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (By similarity) Affords protection against programmed cell death and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P09601}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}.
Interaction partners:
- NADPH--cytochrome P450 reductase
- Biliverdin reductase A
- Ferrochelatase, mitochondrial
- Flavin reductase
- Ceruloplasmin
- Frataxin, mitochondrial
- Hephaestin
- Nuclear factor erythroid 2-related factor 2
- NAD
- Protoheme IX farnesyltransferase, mitochondrial
Sequence:
MERPQPDSMPQDLSEALKEATKEVHIQAENAEFMKNFQKGQVSREGFKLVMASLYHIYTALEEEIERNKQNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEIIPCTPATQHYVKRLHEVGRTHPELLVAHAYTRYLGDLSGGQVLKKIAQKAMALPSSGEGLAFFTFPNIDSPTKFKQLYRARMNTLEMTPEVKHRVTEEAKTAFLLNIELFEELQVMLTEEHKDQSPSQMASLRQRPASLVQDTAPAETPRGKPQISTSSSQTPLLQWVLTLSFLLATVAVGIYAM
Protein: Aconitate hydratase A (ACN) (Aconitase) (EC 4.2.1.3) ((2R,3S)-2-methylisocitrate dehydratase) ((2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase) (Iron-responsive protein-like) (IRP-like) (Probable 2-methyl-cis-aconitate hydratase) (EC 4.2.1.99) (RNA-binding protein) (P70920)
Organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein (By similarity).
Interaction partners:
- Citrate synthase
- citrate synthase
- citrate synthase
- Citrate synthase
- Isocitrate dehydrogenase
- Isocitrate lyase
- Succinate dehydrogenase iron-sulfur subunit
- Cytochrome b/c1
- Superoxide dismutase
- Fumarate hydratase class II 1
Sequence:
MTSLDSFKCKKTLKVGAKTYVYYSLPTAEKNGLKGISKLPYSMKVLLENLLRNEDGRSVKKADIVAVSKWLRKKSLEHEIAFRPARVLMQDFTGVPAVVDLAAMRNAMQKLGGDAEKINPLVPVDLVIDHSVIVNFFGDNKAFAKNVTEEYKQNQERYEFLKWGQAAFSNFSVVPPGTGICHQVNLEYLSQTVWTKKEKMTVGKKTGTFEVAYPDSLVGTDSHTTMVNGLAVLGWGVGGIEAEACMLGQPLSMLLPNVVGFKLKGAMKEGVTATDLVLTVTQMLRKLGVVGKFVEFFGPGLDHLSVADKATIANMAPEYGATCGFFPVDAAAIDYLKTSGRAAPRVALVQAYAKAQGLFRTAKSADPVFTETLTLDLADVVPSMAGPKRPEGRIALPSVAEGFSVALANEYKKTEEPAKRFAVEGKKYEIGHGDVVIAAITSCTNTSNPSVLIGAGLLARNAAAKGLKAKPWVKTSLAPGSQVVAAYLADSGLQAHLDKVGFNLVGFGCTTCIGNSGPLPEEISKSINDNGIVAAAVLSGNRNFEGRVSPDVQANYLASPPLVVAHALAGSVTKNLAVEPLGEGKDGKPVYLKDIWPTSKEINAFMKKFVTASIFKKKYADVFKGDTNWRKIKTVESETYRWNMSSTYVQNPPYFEGMKKEPEPVTDIVEARILAMFGDKITTDHISPAGSIKLTSPAGKYLSEHQVRPADFNQYGTRRGNHEVMMRGTFANIRIKNFMLKGADGNIPEGGLTKHWPDGEQMSIYDAAMKYQQEQVPLVVFAGAEYGNGSSRDWAAKGTRLLGVRAVICQSFERIHRSNLVGMGVLPLTFEEGTSWSSLGLKGDEKVTLRGLVGDLKPRQKLTAEIVSGDGSLQRVSLLCRIDTLDELDYYRNGGILHYVLRKLAA
Protein: Cysteine protease (Q9NBW3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYLPERTEHQKIERLYDSNRVNAEPGQGLDLNEKLKPPAVYILNHEQFPQDSQLNRKGSSNDVNALRKTFESLKCRVEVISNPALPDVKNKVKEWSAKRFTQDAGFVLFILSHGDRKEKILACDHREYHLDDDVLFPLFRNPTLSGKPKILIVQACKGPLRADAKKMNNEPYIKCYSCSEGYLSYRNENHGSVFIQTLCEVMDQYGLTRDFQSIFKHVKAEVERRSTMTGSKQVPSEESHNFDKPFYFGNYAKNT
Protein: Citrate/malate-proton symporter (CimHbs) (Citrate/malate transporter) (P94363)
Organism: Bacillus subtilis (strain 168)
Function: Proton motive force-driven secondary transporter that catalyzes the uptake of both citrate and malate. Appears to be an electroneutral proton-solute symporter; the number of protons transported is equal to the valence of the transported anions. Is strictly stereoselective, translocating only the (S)-enantiomer of malate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11566984}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sensor protein CitS
- Malate-2H
- Transcriptional regulatory protein CitT
Sequence:
MGELQTHMQLQTDTIHEGVRKENWFAKAMNIKVGIIPLPVYALLFILITVFVMHHDVKSDILTSIAVMAFFGFTFAQIGKSIPIVRSIGGPAILATFIPSAVVYYHLLPNDIVKSTTEFTENSNFLYLFIAGIVVGSILGMKRETLVKAFMKIFIPLIVGSVTAAIVGLAVGTLLGLGFQHTLLYIVIPIMAGGVGEGAIPLSIGYSDIMPISQGEAFALVLPSIMLGSLCAIILAGLLNRIGKKKPEWTGNGKVDRSEEESPALEESQSGQQMFNLSLFASGGILAVSLYLVGMLAHDFFGFPAPVAMLLLAVLIKLFRLVPASIENGAFGVSRFFSTAVTYPLLFAIGVSMTPWDKLVAAFNLSNIITILSVVVTMMAVGFFTGKWLNMYPIETAIINACHSGQGGTGDVAILSAAERLELMPFAQVSTRIGGAITVSLTLLLLHQFY
Protein: Exocyst complex component 6 (Exocyst complex component Sec15) (Q18286)
Organism: Caenorhabditis elegans
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Interaction partners:
- Exocyst complex component 1
- Exocyst complex component 5
- Exocyst complex component 4
- Exocyst complex component 2
- Exocyst complex component 7
- Exocyst complex component 3
- Exocyst component Exo84 C-terminal domain-containing protein
- Rab8
- GDP/GTP exchange factor Sec2 N-terminal domain-containing protein
- RNA polymerase II-associated protein 3
Sequence:
MPNSSSTSQPATTGSETASTSYVNYVEMSAEQEYFLYELETTDSGSMGLVLRAIYDTGDVQSFARALQQRISHYDKNIQKVCSFHYQSFVDAMQELMKLKEQCQDIKEETVAIDAEIQQISQRLCQKKQEIVRYRKLMKNAKTAMDQIAVCLPVLENYAKLQEQMSNRKYYQALKTLEELEHTHLALVEKYRFTQVLAKSMAPVRLEIKEKAYSEFKDFLENIKKVAGRIGKHASKDTAEQHSFGVTDAERAKKIQEEARKNASNVEIEVSADGSIVKKNMSPKRNMKMQVEDDEQVSAQDLIDFTPVHRCCQIFNVLGAKEEFEQYYRQQRKEQCDLVIEPTHKMNNFKHYVEYLDEIVGFFVVEDQILMTQSNLSTTVDKDKLWDNALMKIRQHLDARFGGSPDVLMMLKMKKVILLFILTMKSYGYAVAPLYELLQNFRDQYNEILVKEYCAQFERDLEKDNYTPITVNSEEEFRTIIRKFPFYKRSMEQEPFPRRFPFSPFVTDAYTQAKNYLIGCLKFMDNLQLNTSAVDDTVRRCANVLLGRWAGVLKSFVHKRLSMIQLVQITINLGYLEKSCESLGAFITSKTSGEEAIGTTSHQVVLSEKVFRDVRSEVEQQIDECMRSKVDEIIDLANYDWELPAAAGQASEFISDLINFLQTTFTSFTNLPSGLAKHVCTQTCKHISQSMSDFLLSPETKCISTGALDQFSLDVMQCEMFTTRCPVAGVDPQTLSMTFADLRQLLDLVMSSDWTTFNAEYGKDHAKYLRVKASTAIVVLEKMIEFERKSTGFFGIAKGDRKKLLDTIVRQLKLLEI
Protein: RNA binding motif protein 34 (Q5TCT4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALEGMSKRKRKRSVQEGENPDDGVRGSPPEDYRLGQVASSLFRGEHHSRGGTGRLASLFSSLEPQIQPVYVPVPKQTIKKTKRNEEEESTSQIERPLSQEPAKKVKAKKKHTNAEKKLADSSPFRLMLRPCLSISSNTLYCIYRFTIYFWESALASADLEEEIHQKQGQKRKNSQPGVKVADRKILDDTEDTVVSQRKKIQINQEEERLK