wanglab/gogpt-training-data huggingface dataset:
Protein: Plexin A (O96681)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MNFVLSVLLIAILKDKYDYWLPSRTGCQTLAANIWSDKTTAQNEPINLTNANAPIKNAKNLNSTITNVAAFDTKLNHLLVDTITGRVFVGGVNRLYQLSPDLELSETVKTGPQNDSVECSILDCPLNAVRSPTDNYNKVLLIDRATSRLIACGSLFQGTCTVRNLQNVSIIEHEVPDAVVANDANSSTVAFIAPGPPQHPVTNVMYVGVTYTNNSPYRSEIPAVASRSLEKTKMFQIASSAVTTGTRTFINSYARETYFVNYVYGFSSERFSYFLTTQLKHSHHSSPKEYITKLVRICQEDSNYYSYTEIPVECISDAQGGTKFNLVQAGFLGKPSSNLAQSLGISIQNDVLFAVFSKGEGNTPTNNSALCIYSLKSIRRKFMQNIKSCFNGSGMRGLNFISPSMPCVLTKLQTIGEDFCGLDVNSPLGGETPITSVPVAMFNTKLTSVAATSTSGYTVVFVGTSDGFLKKVVIESSSIANEYASFAVDLGSEINRDMQFDNQNLYIYVMSKTKVSKVKVFDCSDYKTCGDCLGARDPYCGWCSLENKCSPRSNCQDDANDPFYWVSYKTGKCTTITSVVPHQLQRTTARTLELIIDHLPQLKENLICAFTTEDKALFTNATKKRNGVNCTTPRTDMLPQIEQGKHHFTAKLSVRTRNGPDLVSTDFTFFDCSTHSSCTRCVSSEFPCDWCVEAHRCTHDTAENCRNDILVTGVSRIGPSYRSGPGFCPTINATGDGSEVLVAGGTSKSIKVKVHIIGQFIVQTRFVCQFNIEGRVTSLNAQLLGDTIYCDSMEFQYTSRSPNLTATFAVIWGGSKPLDNPHNIHVVIYRCREMADSCGICLALSEKYNCGWCSSTNTCEVEEQCNKNKEGKTDWLNRSEICPNPEIHTFQPKTGPWEGGTNITIRGINLGKNYNDIYSGVRIAGINCMPFPQFYIDTKQIVCTVDSPGEQMYRNGKIVVQIGDYRGESKEDYEFVDPKILDFNPKFGPTSGGTEIHITGKHLNAGSRIQASINDHLPCKILSTDSSQAICRTSASPGIIEGRLKMSFDNGPREFNDYNFKYVLDPTVEHVSSGPSGQIKVPKGIPAGGIRISVTGTQFTSIQNPNIYVVYNGEMYASPCRVQSDTEMECASPVVDVDSHVIEAERPILLEYGFLMDNVLRVQNLSKVHNNHFELYPNPEYFIFEERVKYFKSXYLTINGRNLDRACKESDVEVKIGNGFCNITSLSRQQLTCRPPSEATATKSMNGPEVIVRIGTSLEYRIGILSYESSNIILDWGENVIFAVIATIVILLLIFVALLVAYKKKSSESSRVLRNMQEQMDILELRVAAECKEAFAELQTEMTDLTGDLTSGGIPFLDYRSYAMKILFPNHEDHIVLQWERPELLRKEKGLRIFGQLIMNKTFLLLFIRTLESNRYFSMRERVNVASLIMVTLQSKLEYCTDILKTLLGDLIEKCIEGKSHPKLLLRRTESVAEKMLSAWFTFLLYKFLKECAGEPLYMLFRAVKGQVDKGPVDACTHEARYSLSEEKLIRQSIDFRPMNVYASIIQQPIFCNNLDMLPSHTENVSVKVLDCDTIGQVKEKCLETIYRNIPSSPRPPKDDLDLEWRTGATGRVILYDEDVTSKTESEWKKLNTLQHYNVPDGAGLSLVPKQSSIYNFSILSDKNEKSHKYETLNISKYTSSSPTFSRAGSPLNNDMHENGLRYWHLVKHHDSDMQKEGERVNKLVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDDQAQLHGITDPEVVHTWKSNSLPLRFWVNLIKNPNFVFDIHKSNIVDSCLSVVAQTFMDSCSTSDHRLGKDSPSSKLLYAKDIPEYRKWVDRYYRDIRDMSPISDQDMNAMLAEESRLHTTEFNTNCALHELYTYAVKYNEQLTVTLEEDEFSQKQRLAFKLEQVHNIMSSE
Protein: Mannosyl phosphorylinositol ceramide synthase SUR1 (EC 2.4.1.370) (P33300)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the synthesis of mannosyl phosphorylinositol ceramide. Catalyzes the addition of mannosyl to phosphorylinositol ceramide. Suppressor of RVS161 mutation.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Mannosyl phosphorylinositol ceramide synthase regulatory protein CSG2
- Copper-transporting ATPase
- Inositolphosphotransferase 1
- Sphingolipid C4-hydroxylase SUR2
- Mannosyl phosphorylinositol ceramide synthase CSH1
- Ceramide very long chain fatty acid hydroxylase SCS7
- Inositol phosphorylceramide synthase catalytic subunit AUR1
- Fatty acid elongase 2
- Sterol 24-C-methyltransferase ERG6
Sequence:
MRKELKYLICFNILLLLSIIYYTFDLLTLCIDDTVKDAILEEDLNPDAPPKPQLIPKIIHQTYKTEDIPEHWKEGRQKCLDLHPDYKYILWTDEMAYEFIKEEYPWFLDTFENYKYPIERADAIRYFILSHYGGVYIDLDDGCERKLDPLLAFPAFLRKTSPLGVSNDVMGSVPRHPFFLKALKSLKHYDKYWFIPYMTIMGSTGPLFLSVIWKQYKRWRIPKNGTVRILQPAYYKMHSYSFFSITKGSSWHLDDAKLMKALENHILSCVVTGFIFGFFILYGEFTFYCWLCSKNFSNLTKNWKLNAIKVRFVTILNSLGLRLKLSKSTSDTASATLLARQQKRLRKDSNTNIVLLKSSRKSDVYDLEKNDSSKYSLGNNSS
Protein: RUN domain-containing protein 3A (F1LRZ9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Mitochondrial glutathione transporter SLC25A39
- Transmembrane and ubiquitin-like domain-containing protein 2
- Dephospho-CoA kinase domain-containing protein
- Ataxin-7-like protein 3
Sequence:
MEASFVQTTMALGLPSKKASSRNVIVERRNLITVCRFSVKTLLEKYTAEPIDDSSEEFVNFAAILEQILSHRFKACAPAGPVSWFSSDGQRGFWDYIRLACSKVPNNCVSSIENMENISTARAKGRAWIRVALMEKRMSEYITTALRDNRTTRRFYDSGAIMLREEATVLTGMLIGLSAIDFSFCLKGEVLDGKTPVVIDYTPYLKFTQSYDYLTDEEERHSAESSTSEDNSPEHPYLPLVTDEDSWYNKWHKMEQKFRIVYAQKGYLEELVRLRESQLKDLEAENRRLQLQLEEAAAQNQREKRELEGVILELQEQLPDPPPPPRTGLIPGDHAPLAQGSKELTTALVNQWPSLSTLSRPEGASNSKLFRRHSFMSTEPLSAEASLSSDSQRLGEGKRDEEPWGPIGKDPTPSMLGLCGSLASIPSCKSLASFKSNECLVSDSPEGSPALSPS
Protein: Zinc finger CCCH domain-containing protein 14 (Q9V3H9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nuclear cap-binding protein subunit 2
- Polyadenylate-binding protein
- Transportin-1
- Polyadenylate-binding protein 2
- Importin N-terminal domain-containing protein
- ATP-dependent RNA helicase WM6
- mRNA export factor Gle1
- Heterogeneous nuclear ribonucleoprotein 27C
- FI20028p1
- RNA-binding protein Musashi homolog Rbp6
Sequence:
MECNLGSEIGQKMRSAVKAKLLELGTGGSAGFIDDELPDYVMVMVANKRTKQQMNAELNLFLGDQTDLFVTWLHEVLQKLQEVTLPTSSASSKKRKSRGQEKDKKGSKKDKRPHRKSGDELSEPQPSSSDAMPIVSSITDVFAEELLEKAKKTMDIDLSAKDEILHKKKNRKSIEDEDASANRALDVPAVSEIISTTIGVNRQKDLAELAEIQKKIHAAKKHLRQIGEIGDESDEYDEDLLNLSAREESVDQEPEEDPPKLEAPPRKAKSPIIFNRREKTPEKRPEAEPEIDSRQEEAEEKSPKKDSSADKAKEDRSERRSVHDRLGSKAQTPADRSQRNQKELYVPTHRRRSEPEATKERSQRERTRERRSSRDTSRDTNRNQRQRRSPSPEAPSTKQRIVSQVIVAVNKPPEPSDDEDMAEKPVNSVIKVKPRPNVSPRRQACKNLLLRAVADAQRSTILAKTSTQKEDEDVGKIISSLGKRKSEDKNDQIRKRNRERKRRKRSAQGNELFRRTTRELVVNVTQRDGKRERRSNERRAEIKVVEEEYTPSLMTEGVETYVPQLLTNVDELDLHISSHDEPSPNSGALKTQFVVTLNGDKALGGKNVKGGASRKRPSNSRKRSTSPVSTPQVSSSNIEPTSTTVDKRRRSNRDRSFSPSPRQSSGSPSLPTTRSINRNEVRRQPQEIKKIIIKNDTDEDDEMHGSPKKRSPNKRQPAAANGHKDNKDKGKIEEGSTTPPLPAKPKARAEKKASSKEKSVRSNSAETSSAAKSVSASTSVSTTTKAKHTPIRFTLKSEDEPSASKKRRSGSPDRDVAAPERRRVSIRNPEDRKYDNLPALSAVSVDSTVLKVNKPKERCKYHPNCTKQFCEYYHPTAPCKSFPNCKFADKCMYSHPKCKFDMACMSIDCNYAHGGQRDLSHVQLAAPPLSSHVIPVQNYKSISAPVTSTTATTMCKYYPNCSKLGCTFYHPKPCRFGKNCVNKLECIFYHPEMQSKFKWVASLG
Protein: Small ribosomal subunit protein eS32 (60S ribosomal protein L41) (Large ribosomal subunit protein eL41) (P62947)
Organism: Mus musculus (Mouse)
Function: Interacts with the beta subunit of protein kinase CKII and stimulates phosphorylation of DNA topoisomerase II alpha by CKII.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
Sequence:
MRAKWRKKRMRRLKRKRRKMRQRSK
Protein: SMAD5 antisense gene protein 1 (10.3 kDa proline-rich protein DAMS) (SMAD5 antisense RNA 1) (SMAD5 opposite strand protein) (Q9Y6J3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MHKQPKLLPPPATPPPPPQSSSWSGNIVFTIKINIWLRVFSHSSPTGLPKPHSPMPSPPEPEHSVGKPANVQIPQVSSPEFCNQKSVLATEHAQT
Protein: RNA helicase (EC 3.6.4.13) (Q95XY1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNTQYYANHNGQQQPPQQQQGQGWSSSYSQQSNNMPAGGVFYNGFANGTPSNNGSSGYNNFADSGNGFNNKRYSGAESNQWGGAPAEYSESNLFHRTDSGINFDKYENIPVEVSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMVKPPAFTNGRRTYYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPKTARTTAMFSATFPKEIQVLAKDFLKDNYIFLAVGRVGSTSENIEQRLLWVNEMEKRSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDKNRGIGRDLKNLIVESNQEVPEWLHQVAAEGRIGGGQRGGNRRFGATDYRVGRGGGGSFGGNFSNYNSGGATGGFGSGPAYGGSFGGGAPRRPFTNGGFGAHSSLSSTSNSGGGGGFSGPRRGGFNSGMNRQGGGGGGFYSNPGQAPIDHWQAPQA
Protein: Ethylene-responsive transcription factor ERF054 (Transcription factor QRAP2) (Q9M0J3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- At5g46710
Sequence:
MDFDEELNLCITKGKNVDHSFGGEASSTSPRSMKKMKSPSRPKPYFQSSSSPYSLEAFPFSLDPTLQNQQQQLGSYVPVLEQRQDPTMQGQKQMISFSPQQQQQQQQYMAQYWSDTLNLSPRGRMMMMMSQEAVQPYIATKLYRGVRQRQWGKWVAEIRKPRSRARLWLGTFDTAEEAAMAYDRQAFKLRGHSATLNFPEHFVNKESELHDSNSSDQKEPETPQPSEVNLESKELPVIDVGREEGMAEAWYNAITSGWGPESPLWDDLDSSHQFSSESSSSSPLSCPMRPFF
Protein: Phosphoinositide-interacting protein (Q8BFY0)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of TRPV1, a molecular sensor of noxious heat and capsaicin. Positively regulates TRPV1 channel activity via phosphatidylinositol 4,5-bisphosphate (PIP2). Binds various phosphoinositide, including phosphatidylinositol 4,5-bisphosphate (PIP2), but not phosphatidylinositol (PI).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- START domain-containing protein 10
Sequence:
MEVLPKALEVDERSPESKDLLPSQTASSLCISSRSESVWTTTPKSNWEIYHKPIIIMSVGAAILLFGVAITCVAYILEEKHKVVQVLRMIGPAFLSLGLMMLVCGLVWVPIIKKKQKQRQKSNFFQSLKFFLLNR
Protein: Suppressor of Ty 3 (Q8I8U9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSHKCVTLSFIPNDRPSLSQRVLSILTKSAVAIEVVTLFVNKMNYNAKRVMRQNSVCVGSNDMAASPIMIGPAPPSAPSTPQLQTTEDIKPLLVQRQVILLQSGSIPTNPSPQQINLAGHNVAGGASGSNVANVLIPDDAPVSLLTEIADIMRSFGDSDQPRTGSVKLVEQILQQQLRGIFNEASLVAMRRKQNPCPSQADFEFLMRNHPVKIARMRKHLKDMRILKRFLSIRTGRPQDFMDDLEQQEEDEELAIDVYELHDEDRMRRLFRADRISQILTGQQYLEFNEARKTSFYCRHGEKIKNKFRRFLDLPADLRIPTPTMNILAYLAHETIAAIVDYSILTRLNSDNRATEPYSRVTSAGGSPAMMHVCPEVTQGRGMEVVKPISVPEIHEAMRRFRQMSSRKIGRYRNSCDIDFRRSFLAI
Protein: Protein tyrosine phosphatase type IVA 2 (EC 3.1.3.48) (HU-PP-1) (OV-1) (PTP(CAAXII)) (Protein-tyrosine phosphatase 4a2) (Protein-tyrosine phosphatase of regenerating liver 2) (PRL-2) (Q12974)
Organism: Homo sapiens (Human)
Function: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Promotes tumors. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB.
Subcellular location: Cell membrane. Early endosome. Cytoplasm.
Interaction partners:
- Metal transporter CNNM3
- Geranylgeranyl transferase type-2 subunit beta
- 6-pyruvoyl tetrahydrobiopterin synthase
- Protein tyrosine phosphatase type IVA 1
- Metal transporter CNNM4
- Metal transporter CNNM2
- Metal transporter CNNM1
- Interleukin-17 receptor D
Sequence:
MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDWLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFRDTNGHCCVQ
Protein: Synaptosomal-associated protein 47 (SNAP-47) (Synaptosomal-associated 47 kDa protein) (A6QP11)
Organism: Bos taurus (Bovine)
Function: May play a role in intracellular membrane fusion.
Subcellular location: Endomembrane system {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Appears to be exclusively membrane-bound. {ECO:0000250}.
Interaction partners:
- Syntaxin-3
- Vesicle-associated membrane protein 2
- Syntaxin-4
- Vesicle-associated membrane protein 8
- Vesicle-associated membrane protein 7
- Syntaxin-7
- Synaptosomal-associated protein 29
- Synaptosomal-associated protein
- Vesicle-associated membrane protein 1
- Syntaxin-12
Sequence:
MSGDTCVQTWPCSYYLELEKRWVPGRLSLTSLSLKFMTDKTRETLVSFPLSSIIEIKKEASHFIFSSITILERDHSKHWFSSLQPSRNAVFSVIEHFWRELLLSESGAAAEAASSSMTKGKELTCLMACTQKRLEDTARVLHHQGEQLDGISRGLDKMESDLDVADRLLTELESPSWWPFSSKLWKTPSETKPKWDASMADSKAFGKEGIVIQVPAVISQRTESHVKPGRLTVLVSGLEIYNSDSLLMHRFEREDVDDIKVHTPYEISICQRFIGKPDISYRLISAKMPEVIPILEVQFSKKIELLEVAMMLGSTRTSSLAEKGYSVWHAASGLMDQATHCEPSSGSQEGRPLQLQTSEPVISEEDTQELGQILRKLKGLALDTETELERQDEALDGITEAVDRATLTIDKHNRRMKKLT
Protein: Zinc finger CCCH domain-containing protein 57 (AtC3H57) (Zinc finger type domain-containing protein ZFN3) (Q8L7N8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Small RNA degrading nuclease 3
- Small RNA degrading nuclease 2
- Protein GLUTAMINE DUMPER 3
- Large ribosomal subunit protein P2y
- Glutaredoxin-C3
- Small RNA degrading nuclease 1
Sequence:
MDFDSISRESTFLSPLLNQNAMWQMNLGSDDTMGVDGSYPERHGEPDCAYYIRTGLCRFGSTCRFNHPHDRKLVIATARIKGEYPERIGQPECEFYLKTGTCKFGVTCKFHHPRNKAGIDGSVSVNVLSYPLRPNEDDCSYFLRIGQCKFGGTCKFNHPQTQSTNLMVSVRGSPVYSALQSLTGQPSYSWSRTSFVANPPRLQDPSGFASGSQGGLFSSGFHSGNSVPLGFYALPRENVFPERPGQPECQFYMKTGDCKFGTVCKFHHPRDRQTPPPDCVLSSVGLPLRPGEPLCVFYSRYGICKFGPSCKFDHPMRVFTYNNNTASPSPSSSLHQETAITTELRNLLVSSSVEAKPTSLPETTSAKDTIVDAQH
Protein: Proline and serine rich coiled-coil 1 (Q5T2Z1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MEDLEEDVRFIVDETLDFGGLSPSDSREEEDITVLVTPEKPLRRGLSHRSDPNAVAPAPQGVRLSLGPLSPEKLEEILDEANRLAAQLEQCALQDRESAGEGLGPRRVKPSPRRETFVLKDSPVRDLLPTVNSLTRSTPSPSSLTPRLRSNDRKGSVRALRATSGKRPSNMKRESPTCNLFPASKSPASSPLTRSTPPVRGRAGPSGRAAASPPTPIRSVLAPQPSTSNSQ
Protein: Biogenesis of lysosome-related organelles complex 1 subunit 2 (BLOC-1 subunit 2) (F4K657)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex that mediates the vacuolar degradative transport via the intracellular vesicle trafficking from the endosome to the vacuole.
Subcellular location: Cytoplasm {ECO:0000250}. Endosome {ECO:0000305}.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Sorting nexin 2B
- Sorting nexin 2A
- Sorting nexin 1
- At5g57860
- Vacuolar protein sorting-associated protein 35C
- Vacuolar protein sorting-associated protein 35A
- Vacuolar protein sorting-associated protein 35B
- 1-phosphatidylinositol-3-phosphate 5-kinase FAB1A
- F18C1.6 protein
Sequence:
MADSRDDLAESLQNLFTSVSSMVKSELQGTNNHLDLLEKMNLRVASEYDDMGDVAAGLRVFAEQMKSKSGGLDEFVGQMDAIEKQVSEFEAVISVLDRYVSVLESKIRAEYRHPHHQRRSNDSVVTD
Protein: General transcription factor IIF subunit 1 (General transcription factor IIF 74 kDa subunit) (Transcription initiation factor IIF subunit alpha) (TFIIF-alpha) (Transcription initiation factor RAP74) (P35269)
Organism: Homo sapiens (Human)
Function: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.
Subcellular location: Nucleus.
Interaction partners:
- RNA polymerase II subunit A C-terminal domain phosphatase
- Transcription initiation factor IIB
- TATA-box-binding protein
- DNA-directed RNA polymerase II subunit RPB9
- General transcription factor IIF subunit 2
- Transcription initiation factor IIE subunit beta
- DNA-directed RNA polymerase II subunit RPB2
- General transcription factor IIE subunit 1
- Transcription initiation factor TFIID subunit 1
- DNA-directed RNA polymerase II subunit RPB7
Sequence:
MAALGPSSQNVTEYVVRVPKNTTKKYNIMAFNAADKVNFATWNQARLERDLSNKKIYQEEEMPESGAGSEFNRKLREEARRKKYGIVLKEFRPEDQPWLLRVNGKSGRKFKGIKKGGVTENTSYYIFTQCPDGAFEAFPVHNWYNFTPLARHRTLTAEEAEEEWERRNKVLNHFSIMQQRRLKDQDQDEDEEEKEKRGRRKASELRIHDLEDDLEMSSDASDASGEEGGRVPKAKKKAPLAKGGRKKKKKKGSDDEAFEDSDDGDFEGQEVDYMSDGSSSSQEEPESKAKAPQQEEGPKGVDEQSDSSEESEEEKPPEEDKEEEEEKKAPTPQEKKRRKDSSEESDSSEESDIDSEASSALFMAKKKTPPKRERKPSGGSSRGNSRPGTPSAEGGSTSSTLRAAASKLEQGKRVSEMPAAKRLRLDTGPQSLSGKSTPQPPSGKTTPNSGDVQVTEDAVRRYLTRKPMTTKDLLKKFQTKKTGLSSEQTVNVLAQILKRLNPERKMINDKMHFSLKE
Protein: Acyl-CoA synthetase (EC 6.2.1.3) (Q7KQL7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGIILNIYIFFIYLIYVRSHFSQPTSSEYEGYSEICEKARNANESSVYCMKDYKRNSSKYMYKHIMRMFIEKHNLNDNKIALIEHECGEPQNYMTYDTFLRKILSFNNSLNKYDGINIPEKIYNEEMNNGKFKLLGLYGSNSINWLVADLGAMLSGVTTLVMHSKFSMDVIVGILNETKLEWLCLDLDLVEGLMERINELPHLKNLIILDTVAKQGIINSTIEKNKNINLKGNGNLNNMNNKKGNDLSKNLEDVRLGPIKYDKEKLEKFKSLKERYHKYLEKFLLLDDVINNENTNFKIKNEDPNFVTSIVYTSGSSGMPKGAMLSNKNLYNQLYSLYNHSVRKTYNLQYHLSYLPISHVFERTIAYSIIFLRGTVHIWSKNLNYFSKDILNSNSVIMTGVPKVFSRIYTNIMTEINNLSPFKRCIIKKIISLKKSNKKRWLVNFLENLFHISSKIKEKVNPNLEIILNGGGKLSPDVASELCNLLNIKYCQGYGLTETGGAIFGKHVEDLNFECIGGPICPNTKYKVRSWETYKATDTLPKGELLIKSDSIFRGYFLEKEYTKNAFTNDGYFKTGDVVQINKNGTLTFLDRSKGLVKLSQGEYIETDLLNNLYSQISFINNCVVYGDDSMDGPLAIISVDKYLLFLSLKDDNMLEMTGVNEQNYLDKLTDDNINNNIFLDYVKEKMLEVYKETNLNRYNIINNIYLTSKVWDTNNYLTPTFKVKRFYVFKDYAFFISQVKEIYNNKLKGCAPISVNSENKDEEKKNDSKKKEEKDSEKLSNESTSNQNKNDMGKHEKYVENKKVKLGATYGTRQKEMNK
Protein: Putative heat shock protein HSP 90-beta 2 (Heat shock protein 90-beta b) (Heat shock protein 90Bb) (Q58FF8)
Organism: Homo sapiens (Human)
Function: Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MPEEVHLGEKEVETFAFQAEIAQLMSLIINTFYSNKEIFLWELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNTQEHTLTLVDTGIGMTKADLINNLGTIAKFQDQTEYLEEMQVKEVVEKHSQFLGYPITLYLEKEREKEISDGKAEEEKGEKEEENKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNTEDITQEEYGEFYKSLTNDWKDHLAVRYFSVEEYVSRMKEIQKSIYYITGESKEQVANSAFVEQVWKRDSRVVYMTEPIDGYQLKEFDGKSLVSVTKEGLELPEDGEEKKRMEERKAKFENLCKFMKETLDKKVEMVTVSNRLVSSSCCIVTSTYSWTANMEQIMKA
Protein: CAAX prenyl protease 1 homolog (EC 3.4.24.84) (Farnesylated proteins-converting enzyme 1) (FACE-1) (Prenyl protein-specific endoprotease 1) (Zinc metalloproteinase Ste24 homolog) (Q80W54)
Organism: Mus musculus (Mouse)
Function: Transmembrane metalloprotease whose catalytic activity is critical for processing lamin A/LMNA on the inner nuclear membrane and clearing clogged translocons on the endoplasmic reticulum. Proteolytically removes the C-terminal three residues of farnesylated proteins. Plays also an antiviral role independently of its protease activity by restricting enveloped RNA and DNA viruses, including influenza A, Zika, Ebola, Sindbis, vesicular stomatitis, cowpox, and vaccinia. Mechanistically, controls IFITM antiviral pathway to hinder viruses from breaching the endosomal barrier by modulating membrane fluidity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O75844}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:O75844}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:O75844}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:O75844}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein-S-isoprenylcysteine O-methyltransferase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- CAAX prenyl protease 2
- Protein farnesyltransferase subunit beta
- Prelamin-A/C
Sequence:
MGMWASVDAMWDFPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTRVPAELEQIMDSDTFEKSRLYQLDKSTFSFWSGLYSEVEGTFILLFGGIPYLWRLSGQFCSSAGFGPEYEIIQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNHQTLEFFMKDAIKKFIVTQCILLPVSALLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKQEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVPNKDNQEESGMEARNEGEGDSEEVKAKVKNKKQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRRELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSTWHYSHPPLLERLQALKNAKQD
Protein: Proliferating cell nuclear antigen (Q38F34)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU000641}.
Interaction partners:
- DNA polymerase eta
- Replication factor C, subunit 3, putative
- DNA polymerase
- Protein artemis
- Flap endonuclease 1
- Replication factor C, subunit 5, putative
- DNA polymerase delta subunit 2, putative
- Replication factor C, subunit 4, putative
- Mismatch repair protein MSH8, putative
- Replication factor C, subunit 2, putative
Sequence:
MLEAQVLHANLWKRLIECINGLVNEANFDCNPGGLSIQAMDTSHVALVHMLLRDDCFTKYQCERNSVLGLNLASLSKVLKIVEATDSLTLRHEDDSDVVTLTSENGERSRKCEYQLKLLEIETEAMGIPEMDYKSIVTLSSQEFAKIVRDMTVFGDTVNIEILKESVKFSSCGDVGEGYALLRASHAPTVDPRSKGESDVKTEDEEADACSVRTHSAKGKDGPLGIGVDVRTNEPITLSFALRFMNIFAKGATLSDRVSLKFAKESPCMVEYSIDQVGYLRYYLAPKVDDAE
Protein: Enterobactin synthase component D (4'-phosphopantetheinyl transferase EntD) (EC 2.7.8.-) (Enterochelin synthase D) (P19925)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Subcellular location: Membrane {ECO:0000269|PubMed:2526281}.
Interaction partners:
- Enterobactin synthase component F
- Enterobactin synthase component B
- Enterobactin synthase component E
- 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
- Ferrienterobactin receptor
- Isochorismate synthase EntC
- Iron
- Proofreading thioesterase EntH
- Enterobactin biosynthesis protein YbdZ
- Colicin I receptor
Sequence:
MKTTHTSLPFAGHTLHFVEFDPANFCEQDLLWLPHYAQLQHAGRKRKTEHLAGRIAAVYALREYGYKCVPAIGELRQPVWPAEVYGSISHCGTTALAVVSRQPIGIDIEEIFSVQTARELTDNIITPAEHERLADCGLAFSLALTLAFSAKESAFKASEIQTDAGFLDYQIISWNKQQVIIHRENEMFAVHWQIKEKIVITLCQHD
Protein: UPF0494 membrane protein PB2B2.07c (Q9HDU8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSNPESAKKQVDPPGYNELFMVRDTRNVDLERGLELCKPEKVNKQNLFTNIIKPQKDKINIKTDKIKFFLNNLFTEFSKFHDSCYPDGRISTRSKLRWPLLIIWCILIVFAIDKNFEVKDFLSIWINESFINENRFYSEIWGPIAIYICLFILLLLGLICMFPLHLCRVCVLALRETGMIIAVLGAALGMIIAALGATITGLLYFSHWALYKVVILALDLKIEPFKDEIAFLTLPTHNGETLSIRDNNQS
Protein: 2-aminomuconic semialdehyde dehydrogenase (EC 1.2.1.32) (Aldehyde dehydrogenase 12) (Aldehyde dehydrogenase family 8 member A1) (Q9H2A2)
Organism: Homo sapiens (Human)
Function: Catalyzes the NAD-dependent oxidation of 2-aminomuconic semialdehyde of the kynurenine metabolic pathway in L-tryptophan degradation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
- Bifunctional epoxide hydrolase 2
- Delta-1-pyrroline-5-carboxylate synthase
- Hydroxysteroid dehydrogenase-like protein 2
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
Sequence:
MAGTNALLMLENFIDGKFLPCSSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMDIPRSVQNFRFFASSSLHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAMAAGNTVIAKPSELTSVTAWMLCKLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKLSLPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITVKH
Protein: E3 ubiquitin-protein ligase RMA (EC 2.3.2.27) (Protein RING membrane-anchor) (RING-type E3 ubiquitin transferase RMA) (P93744)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU369090}; Single-pass type IV membrane protein {ECO:0000256|RuleBase:RU369090}.
Interaction partners:
- Expressed protein
- Chaperone DnaJ-domain superfamily protein
- Nudix hydrolase 23, chloroplastic
- At2g42060
- Chaperone DnaJ-domain superfamily protein
- Tetratricopeptide repeat
- Shaggy-related protein kinase iota
- Protein ABIL2
- Chaperone DnaJ-domain superfamily protein
Sequence:
MGEEISSTVNLDLNLGPDPELGLEPATNYARSDWGNGLAARESESLRRFRSRYRSRFRRIDMLPVLAETHSPAMELSQLLITSGNVVALPAGEGSMASGERVIEDSKKCENGSKVMAEDNVTEEKRDVEKSVGSDGSFFDCYICLDLSKDPVVTNCGHLYCWSCLYQWLQVSEAKECPVCKGEVSVKTVTPIYGRGIQKRESEEVSNTKIPSRPQARRTESLRTTLNRSGHIPTEIFRHLQDRLERESSTGERRARPSLNRFMTSRGVRAEENQSSEALVEPSSDEINDIDLILNNAPENEEENENLSSSRALATQRRWAQMYGRVSSFTLSSAERLADTYLITHALGRNQEQNSSPPVGVEDRDSFSSIVGVINSESQVETAAEINSMLTVSTSSSVRRHENSSRVSDVDSADSRPLRRRRRLA