wanglab/gogpt-training-data huggingface dataset:
Protein: Non-structural maintenance of chromosomes element 1 homolog (EC 2.3.2.27) (Q54X37)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368018}.
Interaction partners:
- SP-RING-type domain-containing protein
- Structural maintenance of chromosomes protein 6
- Structural maintenance of chromosomes protein 5
- Non-structural maintenance of chromosomes element 4
- MAGE domain-containing protein
- Probable GH family 25 lysozyme 5
- Probable GH family 25 lysozyme 2
- Chalcone isomerase domain-containing protein
- Probable GH family 25 lysozyme 4
- Structural maintenance of chromosomes protein 3
Sequence:
MSRRSQPQQNSQSQRPQPPSQSRSNNNSNNNYNNRYEPTDGDDDEIEYNAQHRLLLDQFTKRRIISTETLKKLVMTVNRITQVNISLDDYINSLNSKIMEVGLQIKILNTDGINDYILTNLKPDECARYATHYSGDELKFFKLILKMFIESRVGLKKNDILTLGRDELKIKLSDADNLFRKFAEDGWLRLSASKSFTTLTNRALSDMAPLLDGIPNCALCHTICVLLEDESVQCPNEDCAVMHSHCAEGWFKANKNKCPSCSTRMDF
Protein: Uncharacterized protein (E7DN95)
Organism: Pneumococcus phage Dp-1 (Bacteriophage Dp-1)
Interaction partners:
Sequence:
MAKNKKRKKVNVKRKMLIPTNLSKKVNVKAIAYRKVTVKWLPNTDEIQVYFDLYINKNRLTMLGTIDPDKSYFEGIRIVCKKPQPWMTVKELQVARADAPGFFAVLKAYCHTVGDVLDSGAEPTEIVQGIMYKDGELFKDSEIVSLFKYDVKEPYEFPKDLPITLDNFLEFIMSSQHTRALVLRCANIGEFSKNWRKWQKAIQLLLDYAKADDFKVDETVWDFSPGSKAGKVARRKGYEAIQQALEQINK
Protein: Sarcosine oxidase gamma subunit (Q9HTE5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Sarcosine oxidase subunit beta subunit beta)
- Sarcosine oxidase alpha subunit
- Sarcosine oxidase delta subunit
- Formyltetrahydrofolate deformylase
- DgcA, Dimethylglycine catabolism
- 4-vinyl reductase 4VR domain-containing protein
- Glycine betaine monooxygenase oxygenase subunit
- Membrane dipeptidase
- Serine hydroxymethyltransferase 1
- Glycine betaine monooxygenase reductase subunit
Sequence:
MSKANVYQQRPEPGVHAESPLHHAELHKLAGKTAAKAGIVLREKKLLGHLVLRGDAADPAFAAAVHQALGLELPVALTLVASGETSLQWLAPDEWLLIVPGGEEYAVEQRLRQALGEELHYAVVNVSGGQTLLELSGANVRELLMKSTSYDVHPSNFPVGKAVGSIFAKSQCVIRHTGEDTWELVVRRSFADYFWLWLQDASAEYGLQVAA
Protein: RanBP2-type domain-containing protein (Q57ZG1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRPTSYLAHAAPSTTSSSAAAVATALGKTKTRLSPQQSSFTSLTPSHLRHGGPQAAEQLMRLGRVFVPVTYLPGSSGYQTAQTPGVSPTLRRSRRYEPYGSLLQMYMERGFTDLDALLFHPEAPSPMELLLSVLRHRTACLQLTQKALTATISRPRHTSSAGAASYTLQTVYHILKNHCPYLYDTASVRVLLCQALLCERLFSDAIELLQGMPDSWITPGLWQVVMEAAADGKVPHSPLLWKLLTLSPAKTPGEGRVVRTGQRVPEQLRRGMSARAAEVVSRSFVNRGESMDEAAKAHGVHQNSDTVTFSSFEVRPLSIVQITRGGNQLEWCHLSTSEVGYAEQHYRALRNLRGWGHGVLRLGRGDHLMEGVVYGLDAFLASRLMLRANVSFFGQASPLIALHILRRYIRTCHALRKTPARSSVVKGTGSDGTSELGTNSDWLKYHQPSSTSGSPGVSTSDTQASDIEDFIHPSPFLLFFKVVRETRDVLPGGGGTLASAGHSGTSGGVPTAGLPMIHWELVWRYFQTLNRECPNWHTIIPEKAGDLSQYVIDVLCRGADPWMTLNVARAVSSRHIVDGLDMSLWLLHRLDPSHHMEEARDVTRKVFRWLLTDVGVHLLPQLHHNLIPAARVLVRLGLQDELRQLYNGVLDNVYLFAEDFRAEFLHVMMDLVCPSCSSILSAQDVYAERVCSICLTIIPAKDAGSLPSFQLSSEHISRLREKRKVVRLSERKRLHESICCWSKRGENSRETAAGATNVGKHAASPVFPPLDASSVFKKEILSDTAPLLPGVPVAARNVLLLPGGGGADGAGSCVSEGGGPSASFDVYAAMEESSHRLQLQEAARRYALAQRGVVLPARHSAAFPSPVLSTSSVSTSSAHFSPEKQRQGFMIPSMCVDGPWTCVWCHEQNTGWGSRTQCGACGAETGPSALWRHFAYATSTGDIMEEVRARVANSAERPVDAVVAGYLLMVYRRTFLLRATPHDAERIEQLIQRLCQLHERVLAGYTYMRFVPARARSKGSTLFALAHLFGCTDAAYAGLTTQQLRRDEDTFFQTIFTPATCKVCFGQHAWKACPIITRDFSTTKRQSITMSPKEKQEAVLQQLRQAVEAAVQHGAESSRLVVGAYTAFVKSPYRELFSETHSRDVNRLSMLLSRYQQFRRAAFVLCHIPLHLRDDGAYMAMVPYFNVPVEDARELLRKRSPLGVADGTHPNFVQVAVTCCMCLDERHASFECPRLLKWIGEIEELSASQKNGSATSGALVDVVAAQELSKRLRAQVDGWTSAGPERLHAFYRFLLQRIDDFQKDPYDTLQTDGDEHGHRQVDSCVVGSPLNMLQLRRLDMDDPIVYAINKAISKLALAKQEKSAYRLYARSPVVFVSSGVTSTMLRMAGYSEKGIRTLSHNHVDGSGSSQTSLSSSLSASDESSTLGVSTEGARSAAVPMRNCCLLCFDSEHTYFDCPELIAQPTTAAKLEYVVVHVGGIRSVLDGVRAAAAYVYHTYNLGQLTSDLLRAHPSLVRSLLRLVRRCFACGLVGSGVRILRRLPVEMVPPISPYTDLWRAAGLGEEVVISRRAQLQALFAAEGLEPRIETPPARQTYSNRFVSALSHVLHDDLCRHCYQHGHSLATCSVFHAEVSFGRDYVAAYRMSMMSEQLDDDWRDAYLLKLVDFFLMHKVLMPYHIVGVTNALNAIAAMWSFRGEPGIAIRHLLNIPPAYRRRQAFAYILQAVGVPVDEAKRVLANVYFSPSELSSSNKPSGSSASASASASAGSGSGSGAESGSAVAQHLLMPKPAIRDVAMTAVFNQFPDALAALEGSEGRMEAIRRRNATQKITKGSKAEGGNMKTTSVGGAARMAESSLGEEPSVPSVSLSRRPVQSGDITTVRENFDPVLTELELAVGMKLGSRHVLFTSAVDILAAVVAPKETEGGSGKVQQPAVTTTVVVPPQAASPPPSENPASKLSPESTVAIPRSDACGHPHTREEPEIVTVFSGETAGGGGSGRGSHQRWGVGSDGLKPSSSPSNSPGGDHGKYSSSQHFQTQQHYTQKGRYHERQRRRQRERDVGNNGNHARKR
Protein: Glycerol-3-phosphate O-acyltransferase 2 (G-3-P acyltransferase 2) (GPAT 2) (EC 2.3.1.15) (Dihydroxyacetone phosphate acyltransferase 2) (DHAP-AT 2) (EC 2.3.1.42) (Glycerol-3-phosphate / dihydroxyacetone phosphate acyltransferase 2) (P36148)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Dual substrate-specific glycerol-3-phosphate/dihydroxyacetone phosphate sn-1 acyltransferase, catalyzing the first and committed reaction in the de novo synthesis of glycerophospholipids and triacylglycerols (TAGs). Can use both Gly-3-P and dihydroxyacetone phosphate with similar efficiencies and has a broad fatty acyl-CoA specificity profile. Transfers a fatty acid from fatty acyl-CoA to the sn-1 position of glycerol-3-phosphate to produce lysophosphatidic acid (LysoPA). These lipids not only are precursors of glycerolipids, but also are dynamic components of signal transduction systems that control cell physiology.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:22267742, ECO:0000269|PubMed:31421179, ECO:0000269|PubMed:9401016}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19525420, ECO:0000269|PubMed:31421179}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to both perinuclear and cortical endoplasmic reticulum. {ECO:0000269|PubMed:19525420}.
Interaction partners:
- Lysophospholipid acyltransferase
- Lysophosphatidic acid:oleoyl-CoA acyltransferase 1
- NADPH-dependent 1-acyldihydroxyacetone phosphate reductase
- Glycerol-3-phosphate O-acyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Triacylglycerol lipase 5
- Triacylglycerol lipase 4
- Phosphatidic acid phosphohydrolase 1
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase, mitochondrial
Sequence:
MSAPAADHNAAKPIPHVPQASRRYKNSYNGFVYNIHTWLYDVSVFLFNILFTIFFREIKVRGAYNVPEVGVPTILVCAPHANQFIDPALVMSQTRLLKTSAGKSRSRMPCFVTAESSFKKRFISFFGHAMGGIPVPRIQDNLKPVDENLEIYAPDLKNHPEIIKGRSKNPQTTPVNFTKRFSAKSLLGLPDYLSNAQIKEIPDDETIILSSPFRTSKSKVVELLTNGTNFKYAEKIDNTETFQSVFDHLHTKGCVGIFPEGGSHDRPSLLPIKAGVAIMALGAVAADPTMKVAVVPCGLHYFHRNKFRSRAVLEYGEPIVVDGKYGEMYKDSPRETVSKLLKKITNSLFSVTENAPDYDTLMVIQAARRLYQPVKVRLPLPAIVEINRRLLFGYSKFKDDPRIIHLKKLVYDYNRKLDSVGLKDHQVMQLKTTKLEALRCFVTLIVRLIKFSVFAILSLPGSILFTPIFIICRVYSEKKAKEGLKKSLVKIKGTDLLATWKLIVALILAPILYVTYSILLIILARKQHYCRIWVPSNNAFIQFVYFYALLVFTTYSSLKTGEIGVDLFKSLRPLFVSIVYPGKKIEEIQTTRKNLSLELTAVCNDLGPLVFPDYDKLATEIFSKRDGYDVSSDAESSISRMSVQSRSRSSSIHSIGSLASNALSRVNSRGSLTDIPIFSDAKQGQWKSEGETSEDEDEFDEKNPAIVQTARSSDLNKENSRNTNISSKIASLVRQKREHEKKE
Protein: KISS1 receptor b (F1QZU4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Kisspeptin
- KiSS-1 metastasis suppressor
- Progonadoliberin
- KISS1 receptor a
- FMRFamide related peptide 1
- Progonadoliberin
- Lhb protein
- Preprotachykinin 2a
- Follicle-stimulating hormone beta subunit
- Coiled-coil domain-containing 24.
Sequence:
MAETNSTGDAAEHIMCNYDANIYQCNQTDLMRFQNPVPLTDTWLVPLFFTLIMFVGLVGNLIVIYVVIKNQQMKTVTNLYIVNLATTDILFLVCCVPFTATVYVLPSWIFGDFMCRLVNYLQQVTAQATCITLSAMSVDRFYVTVYPLQSLHHRTPQMALSVCTTIWICSSLLSVPIALYQHTESSYWFGPQTYCTETFPSVIHKRVYLLYSFLAVYLLPLITICMCYTFMLKRMAQATVQPVQGCNQISLQTSSERAEAVRSRVSRMVVVMVLLFLLCWGPIQILILLQAFCAEDVSRSYTLYKLKIWAHGMSYSNSSINPVIYAFMGANFRKAFRSVCPLIFKRRSTEPLATYNREMNFLSS
Protein: Ciboulot, isoform C (GEO02096p1) (RE37354p) (Q8IRS7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MAAPAPALKDLPKVAENLKSQLEGFNQDKLKNASTQEKIILPTAEDVAAEKTQQSIFEGITAFNQNNLKHTETNEKNPLPDKEGEGEESVHRRHREL
Protein: Short-chain dehydrogenase/reductase (EC 1.1.1.-) (F4JE70)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAEETPRLFNGFCRYAVVTGANRGIGFEICRQLASEGIRVVLTSRDENRGLEAVETLKKELEISDQSLLFHQLDVADPASITSLAEFVKTQFGKLDILVNNAGIGGIITDAEALRAGAGKEGFKWDEIITETYELTEECIKINYYGPKRMCEAFIPLLKLSDSPRIVNVSSSMGQLKNVLNEWAKGILSDAENLTEERIDQVINQLLNDFKEGTVKEKNWAKFMSAYVVSKASLNGYTRVLAKKHPEFRVNAVCPGFVKTDMNFKTGVLSVEEGASSPVRLALLPHQETPSGCFFSRKQVSEF
Protein: Acetylcholine receptor subunit delta (P02718)
Organism: Tetronarce californica (Pacific electric ray) (Torpedo californica)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MGNIHFVYLLISCLYYSGCSGVNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTSNVWMDHAWYDHRLTWNASEYSDISILRLPPELVWIPDIVLQNNNDGQYHVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYDANEITMDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYPDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLISFLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVIVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRADESEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNHPPAKPFEGDPFDYSSDHPRCA
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q583L3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MTLIPAHASVLLLFVVAATRYSHAADSEALNLAELTTVCSLIKIANDDGTDMPTAQLETDEIAAINEVNFSLADDYWTKAFPTDGIKTKAEAKGCEDVQSKDSCQEQWLAWQHIAHSLANKDKNNKAAKISPMQKTSSVGRAAALAAAAIAAEAATLQARFDAESRPALTDLKQKVLDDLKTAAYGAGKAETLAENKCPGAKGGNRAADCKVATAGNALCIVSVCLCAKNSGDQPNTDVCGATLTQDVTSWNEAGVKAAYRELEPHCLKMPSVKPTGANIRSLLAQLKGLYKTKGGGSGKSVILGTAGTNHDCRAEASAACVDMSASTLLAATGTATKIQWEEKLLEAANKLDAASEAATVAKVINTKLKALRAKADKLYSHLALTKPPIASQEILTPANKDQANNISKDCEAIVIPEECSLKSECEWNDKATEGEKKCKLNTTKVGQAKTQAGETKGNEQTATEKCTGKVEDVCKKEAGCKWEENKCKDSSFLPNKKLAPSMASAFVIW
Protein: BolA-like protein 2 (Altered inheritance rate of mitochondria protein 15) (Fe repressor of activation 2) (P53082)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the regulation of the iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis. May be involved in mitochondrial organization and biogenesis.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Monothiol glutaredoxin-3
- BolA-like protein 1
- Monothiol glutaredoxin-4
- Putative Xaa-Pro aminopeptidase FRA1
- Iron-regulated transcriptional activator AFT2
- Fe-S cluster assembly protein DRE2
- BolA-like protein 3
- Monothiol glutaredoxin-5
- Iron-regulated transcriptional activator AFT1
Sequence:
MTGERIEKVKINDEFAKSHFLTTQWRETKRQRHYKMPVTEQGLRERIESAIPQVYHIIVTDLSYGCGQSFDIVVVSDFFQGKSKLMRSRAVNKAVKEELQEIHAFSCKCYTEEEWSKIVV
Protein: 5-aminolevulinate synthase, erythroid-specific, mitochondrial (ALAS-E) (EC 2.3.1.37) (5-aminolevulinic acid synthase 2) (Delta-ALA synthase 2) (Delta-aminolevulinate synthase 2) (P18080)
Organism: Gallus gallus (Chicken)
Function: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (By similarity). Contributes significantly to heme formation during erythropoiesis (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22557}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22557}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P22557}.
Interaction partners:
Sequence:
MAAFLRCPLLARHPPLARAFATGARCPFMGFAHRAAPELQEDVERPQIPAVEVLEELLRDGGAALNRTVRDCMDEDAFPYEEQFQAQLGALRRTHTYRVVTAVGRRADAPPLGTRGTAPHTSVELWCSSDYLGLSRHPAVLRAARAALDAHGLGAGGTRNIGGTSPLHGALERALALLHRQPRAALFSSCFAANDTALDTLARILPGCQVYSDAGNHASMIQGIRRRGVPKFIFRHNDPHHLEQLLGRSPPGVPKIVAFESLHSMDGSIAPLEELCDVAHAYGALTFVDEVHAVGLYGARGAGIAERDGVQHKVDVVSGTLGKALGAVGGYIAGSEALVDAVRSLGPGFIFTTALPPQRGGGALAALQVVGSAEGAALRRAHQRHAKHLRVLLRDRGLPALPSHIVPVRWDAEANTRLSRALLEEHGLYVQAINHPTVPRGQELLLRIAPTPHHSPPMLENLADKLSECWGAVGLPREDPPGPSCSSCHRPLHLSLLSPLERDQFGVRGAAAG
Protein: Probable diguanylate cyclase DgcT (DGC) (EC 2.7.7.65) (P75908)
Organism: Escherichia coli (strain K12)
Function: Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Overexpression leads to a strong repression of swimming; swimming returns to normal when residues 359-360 are both mutated to Ala. Overexpression also leads to a 20-fold increase in c-di-GMP levels in vivo. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclic di-GMP phosphodiesterase PdeL
- Probable cyclic di-GMP phosphodiesterase PdeC
- Probable cyclic di-GMP phosphodiesterase PdeB
- Probable cyclic di-GMP phosphodiesterase PdeG
- Probable cyclic di-GMP phosphodiesterase PdeD
- Probable cyclic di-GMP phosphodiesterase PdeN
- Probable cyclic di-GMP phosphodiesterase PdeI
- Cyclic di-GMP phosphodiesterase PdeF
- RNase E specificity factor CsrD
- Probable cyclic di-GMP phosphodiesterase PdeK
Sequence:
MEKDYLRISSTVLVSLLFGLALVLVNSWFNQPGVEEVVPRSTYLMVMIALFFIDTVAFIFMQLYFIYDRRQFSNCVLSLAFLSCLIYFVITVIIIQQIIEERLTSSVVQNDIAIYYLFRQMSLCILIFLALVNKVSENTKQRNLFSKKMTLCISLFFVFGGPIVAHILSSHYESYNLHIAELTNENGQVVWKASYVTIMIFMWLTLLSVNLYFNGLRYDIWNGVTVIAFCAVLYNISLLFMSRYSVSTWYISRTIEVVSKLTVMVIFMCHIFSALRVTKNIAHRDPLTNIFNRNYFFNELTVQSASAQKTPYCVMIMDIDHFKKVNDTWGHPVGDQVIKTVVNIIGKSIRPDDLLARVGGEEFGVLLTDIDTERAKALAERIRENVERLTGDNPEYAIPQKVTISIGAVVTQENALNPNEIYRLADNALYEAKETGRNKVVVRDVVNFCESP
Protein: Intraflagellar transport protein 122 homolog (Q8T9D3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
Sequence:
MRGVLKWLERIEFPNSKDNEISVHNVCYAPDGSQLVVAAGDRLLIYDPNDGSLLNTLKAHKDTVNCVAYSRDGKRFASGASDKMVIVWSPQLEGLLKYSHGDSIQCMSFNPVSHHLASCSLSDFAFWSADQKAVQKYKISARVNGCSWTNDGQYLILGLANGTISIRNKLGEEKGRIDRPGGPNSNVFSVQCCPASGPGSVDTIGVVDWSQTLSFHTLSGQMIGKERTLGFDPLCLQYFPNGEFCLVGGCTGGLHFFTREGIRLGTLGDTFDTWIWTVALHPNGQSYTIGCQDGTLACFNIASSTVHALYRERYAFRENMCDVIIQHLISGQKVRIKCRDLVQKIAIYRNRLAVQLPERVVLYELSSGEDQPMHYKVREKIQQKFDCSLLVVCGRHIVLCQEKRLQCLDFMGVLQREWIMDSFIRYIKVTGGPVGREGLMVGLKNGQVFRIFLNNSLPLLITTAVSAVRCLDINSKRSKIAVVDDVGRLVVRDVINDTILYQDTGVNSVTWNTHLDSMLCYTHTTGGLSVRVGNLPPRAPQNMHGVVVGLCGATAFCLRGNIMHNTPLALGSTMWQFIEAGLFDEAYQVACLGVTTSDWEGLAQSALEALHINIARDAYVKVRNLPWLKLIGELRDQQQRSAVPKEVLLAENCAFAGKFKEAARLFLKCGQSSRALEMYTDLRMFDLAQEYIKDGTDQEKKELVRKRAEWAYSVKEPRAAAELLLSAGENQKAIDIVAEQGWADVLYDIGRRLSLTERDSLESVAQNLKTLKALPLAAEIFKKLGDEAQVVQLHIEVRDWPEAFRLAESLPELLPTVHYQHGQWLAETDQFIEAHQAYIKAGRTKEANRLLKQLSNTAIVEERYLDASYFYWLLAKQHLDVYHAKEEQNPVDHHLTEYKNHLRVAKVYYAYSVIYSYMKEPFTTHSPVSLFNVSRFILNEVEQKGVPKGVSMFSVLFTLAKQAKFLQANKLCLLINKRLQSLKPPAGVQEQIDLNFLNSKACKSGFNDPEELLPLCYKCSNYSQHLNSNCCPTCRQDYIFSFVSFEILPLVQFYPEVDISDAEAERLLLAPAKHAEDSDPFNEDVASALPLSLDRNGLRAIDPNHVLILKRRGKNVRNVYYRNILPDLQVTYCPQCLLLFYAEDFELQVLQKGHCPFCHTSSEKLMEDF
Protein: DNA topoisomerase 4 subunit A (EC 5.6.2.2) (Topoisomerase IV subunit A) (Q9HUK1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00936}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00936}.
Interaction partners:
- DNA topoisomerase 4 subunit B
- DNA gyrase subunit B
- YaeQ family protein
- Outer membrane protein OprM
- Multidrug resistance operon repressor
- Cell division topological specificity factor
- Phytase-like domain-containing protein
- HTH-type transcriptional regulator NfxB
- Porin D
- DNA-directed RNA polymerase subunit beta
Sequence:
MSESLDLSLEGVERRSLAEFTEQAYLNYSMYVIMDRALPHIGDGLKPVQRRIVYAMSELGLDADSKHKKSARTVGDVLGKFHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTEARLSRYSEVLLSELGQGTVDWVPNFDGTLDEPAVLPARLPNLLLNGTTGIAVGMATDVPPHNLREVASACVRLLDQPGATVAELCEHVPGPDFPTEAEIITPRADLQKVYETGRGSVRMRAVYRVEDGDIVIHALPHQVSGSKVLEQIAGQMQAKKLPMVADLRDESDHENPTRIVIIPRSNRVDVEELMTHLFATTDLETSYRVNLNIIGLDGKPQVKDLRQLLSEWLQFRIGTVRRRLQFRLDKVERRLHLLDGLLIAFLNLDEVIHIIRTEDQPKAVLMERFELSEVQADYILDTRLRQLARLEEMKIRGEQEELLKEQKRLQTLLGSEAKLKKLVREELIKDAETYGDDRRSPIVARAEARALSETELMPTEPVTVVLSEKGWVRCAKGHDIDAAGLSYKAGDGFKAAAPGRSNQYAVFIDSTGRSYSLPAHSLPSARGQGEPLSGRLTPPPGASFECVLLPDDDALFVIASDAGYGFVVKGEDLQAKNKAGKALLSLPNGSAVVAPRPVRDVEQDWLAAVTTEGRLLLFKVSDLPQLGKGKGNKIIGIPGERVASREEYLTDLAVLPAGATLVLQAGKRTLSLKGDDLEHYKGERGRRGNKLPRGFQRVDSLLVDIPPQD
Protein: 55 kDa erythrocyte membrane protein (p55) (Membrane protein, palmitoylated 1) (P70290)
Organism: Mus musculus (Mouse)
Function: Essential regulator of neutrophil polarity. Regulates neutrophil polarization by regulating AKT1 phosphorylation through a mechanism that is independent of PIK3CG activity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q00013}; Lipid-anchor {ECO:0000250|UniProtKB:Q00013}. Cell projection, stereocilium {ECO:0000269|PubMed:16829577, ECO:0000269|PubMed:17584769}. Note=Colocalizes with WHRN at stereocilium tip during hair cell development (PubMed:16829577). Colocalizes with PALS1 in the retina, at the outer limiting membrane (OLM) (PubMed:17584769). Colocalizes with WHRN in the retina, at the outer limiting membrane (OLM), outer plexifirm layer (OPL), basal bodies, and at connecting cilium (CC) (PubMed:17584769). Colocalizes with NF2 in non-myelin-forming Schwann cells (By similarity). {ECO:0000250|UniProtKB:Q00013, ECO:0000269|PubMed:16829577, ECO:0000269|PubMed:17584769}.
Interaction partners:
- Whirlin
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Epidermal growth factor receptor kinase substrate 8
- Calcium/calmodulin-dependent protein kinase type II subunit delta
- Epidermal growth factor receptor kinase substrate 8-like protein 2
- Calcium/calmodulin-dependent protein kinase type II subunit beta
- Calcium/calmodulin-dependent protein kinase type II subunit gamma
- Unconventional myosin-XV
- Gelsolin
- Glycophorin-C
Sequence:
MTLKSSEGEGGNSMRTALSDLYLEHLLQKRNRPETSLNQSNVTTEDMYTNGSPAPGSPAHAKGQEARRVRLIQFEKITEEPMGITLKLNEKQSCTVARILHGGMIHRQGSLHVGDEILEINGTNVTNHSVDQLQKAMKETKGMISLKVIANQQSRLPALQMFMRAQFDYDPQKDNLIPCKEAGLKFVTGDIIQIINKDDSNWWQGRVEGSSKESAGLIPSPELQEWRVASVAHSAPSEAPSCSPFGKKKKCKDKYLAKHSSIFDQLDVVSYEEVVRLPAFKRKTLVLIGASGVGRSHIKNGLLSHNPEKFAYPAPYTTRPPKKSEEDGKEYHFISTEEMTKNISANEFLEFGSYQGNMFGTKFETVHQIHKQDKIAILDIEPQTLKTVRTAELSPFIVFIAPTDQGTQTEALQQLQKDSEAIRSQYAHYFDLSLVNNSVDETLKKLQEAFDQACSSPQWVPVSWVY
Protein: PHD finger protein ALFIN-LIKE 5 (Protein AL5) (Q5XEM9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:19154204}.
Interaction partners:
- PHD finger family protein / SWIB complex BAF60b domain-containing protein / GYF domain-containing protein
- Cysteine/Histidine-rich C1 domain family protein
- PHD finger protein MALE MEIOCYTE DEATH 1
- Chromatin remodeling protein SHL
- Protein TRAUCO
- Protein RBL
- Multiple organellar RNA editing factor 1, mitochondrial
- PHD finger protein MALE STERILITY 1
- Chromatin remodeling protein EBS
- PHD finger protein ALFIN-LIKE 6
Sequence:
MEGGTAHYSPRTVEEVFRDFKGRRAGIIQALTTDVEDFFQQCDPEKQNLCLYGFPNEVWEVNLPAEEVPPELPEPALGINFARDGMQERNWLSLVAVHSDAWLLSVSFYFGSRFGFDRADRKRLFSMINEVPTVYEVVTGNAEKQTKEMPSSANQNGNRSKSNSKMRGLESKSSKTIHAKDEEEGLELEEGEEEEDEDEDEHGETLCGACGDNYASDEFWICCDMCEKWFHGECVKITPARAEHIKHYKCPTCSNKRARP
Protein: U6 snRNA phosphodiesterase 1 (3'-5' RNA exonuclease USB1) (EC 4.6.1.-) (Cyclic phosphodiesterase USB1) (EC 3.1.4.-) (U six biogenesis protein 1) (Q12208)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: 3'-5' RNA exonuclease that trims the 3' end of oligo(U) tracts of the pre-U6 small nuclear RNA (snRNA) molecule, leading to the formation of a U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate. In a second step acts as a cyclic phosphodiesterase that hydrolyzes a U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate to a U6 snRNA 3'-end-terminated with a 3' phosphate. Participates in the U6 snRNA 3' end processing that prevents U6 snRNA degradation. Could be involved in aerobic respiration.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03040, ECO:0000269|PubMed:14690591}. Mitochondrion {ECO:0000269|PubMed:14690591}.
Interaction partners:
- Pre-mRNA-processing factor 19
- LSM2-LSM8 complex subunit LSM8
- U4/U6 snRNA-associated-splicing factor PRP24
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Pre-mRNA-splicing factor SYF1
- LSM complex subunit LSM2
Sequence:
MEFISADYSSSDGSDTESESSNKSEVQIEYTEKTCIQKADSTDLPAIPDSIILKYHIPPNLQKYEHQDMNMSRFWRSFTYFEWRPTPAIHRQLQKIICKYKETFMKQEYTNPYQLVDFDPLFISHLGAPKPLHVSLTRSLLFETEEQRHVFIQEMRNGLRNNEITPFKLQICSYPKLYISERANTLYLGLPVSECPNKAQISPFKTIIAEALQKSGISNYQDLIVSRQNLHVSIAIASNPSKATLKRYQQLNETMGALLLLNNDFAYKLEFLVNSIYCDENRHSIRIPFN
Protein: Allyl alcohol dehydrogenase, putative (Putative allyl alcohol dehydrogenase) (Zinc-binding dehydrogenase family protein) (Q9C677)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At4g33840/F17I5_30
- Glycosyl hydrolase family 10 protein
- Glycosyl hydrolase family 10 protein
- Glycosyl hydrolase family 10 protein
- At4g38650
Sequence:
MTNAEAVTVTNKQIIFPDYVTGFPKESDLKITTTTIDLRLPEGSTSVLVKNLYLSCDPYMRICMGKPDPLSSSLVPPYKTGVPIIGLGVSKVIDSGHPDYKKGDLLWGLVGWEEYSVITLTTYSHFKIEHTDVPLSYYTGLLGMPGMTAYAGFYEVCSPKKGETVFVSAASGAVGQLVGQFAKLMGCYVVGSAGSKEKVYLLKTKFGFDDAFNYKEEKDFSAALKRYFPEGIDIYFENVGGKMLDAVLINMKLHGRVAVCGMISQYNLVDPEGVHNLPTILYKRIQLQGFGVCDFYDKYPKFLDFVLPYIREGKITYVEDIAEGFESGPSALLGLFEGKNVGKQLFVVARE
Protein: Rab-GAP TBC domain-containing protein (Q7JL36)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLLCTNLCFKRLDQFSAGKIGHEINNNDVSDAWDTRVKVDETLASASAAKVLAAHAAGKTHRDEEIMPPVSAAPTKNSRQQALQRLAIQKEPLPSSVSSTPQTANPIYPKLPEISDQPRSAVPMASAPPHGGDRDQTRFARLRRLFSNGKSSGKNSPPVDVDLEKLREDCWMGIPHKLRPQAWRLLSGYLPTNAERREVTLQCKRDEYWHYVEQYFHSRFDDQNADTFRQINIDIPRMCPLIPLFQQKMVQEMFERILYIWAIRHPASGYVQGINDLVTPFFVVFLSEFIPQDVEVGSFDVSQLPLEQCQLIEADSFWCVSSLLDSIQDNYTFAQPGIQRKVLQLRHLMSRVDRPLHKHLESNGIEYLQFAFRWMNNLLMREIPLRATIRLWDTYLSEPDGFMQFHNYVCAAFLRTWSKQLQAEKDFQGVMILLQNLPTQSWGDREICELTADAFSLQSVFDGARRHLSAQAASP