wanglab/gogpt-training-data huggingface dataset:
Protein: N-acetylgalactosaminide beta-1,3-galactosyltransferase (EC 2.4.1.122) (Q7K509)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MTSASLLSRSLLTEAPRSKNRSVFTLIAGLVVGYCLAQIFSSIAPHESLYPYLSRRFSDSQVATGGQLAPEQSGLKHDHRNDNVSVAEQLKKEVRILCWVMTNPTNHKKKARHVKRTWGKRCNILLFMSSGADEELPTVKLDVGEGRENLWAKVKEAFKYVYHHHYNDADFFYKADDDTYAVIENMRYMLYPYNPETPVHFGFKFKPFVKQGYMSGGAGYILSREALRRFVVEGIPNPKMCLPGTVVNEDIEIGRCMENLNVTAGDSRDEIGRGRMFPFIPEHHLIPAKADKNFWYWNYLYYKTDDVSFA
Protein: Histone acetyltransferase mst1 (EC 2.3.1.48) (Protein 2-hydroxyisobutyryltransferase mst1) (EC 2.3.1.-) (Protein acetyltransferase mst1) (EC 2.3.1.-) (Protein crotonyltransferase mst1) (EC 2.3.1.-) (O94446)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac (By similarity). The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination. Recruitment to promoters depends on H3K4me (By similarity). Also acetylates non-histone proteins (By similarity). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively.
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16199868}. Chromosome {ECO:0000269|PubMed:20299449, ECO:0000269|PubMed:33723569}. Note=Localizes to pericentric heterochromatin (PubMed:20299449). Following DNA damage, localizes to sites of DNA damage, such as double stand breaks (DSBs) (PubMed:33723569). {ECO:0000269|PubMed:20299449, ECO:0000269|PubMed:33723569}.
Interaction partners:
- Enhancer of polycomb-like protein 1
- Chromatin modification-related protein png1
- Chromatin modification-related protein vid21
- SWR1-complex protein 4
- Actin-related protein 4
- Chromatin modification-related protein eaf3
- Actin
- NuA4 acetyltransferase complex subunit Tra2
- Protein AF-9 homolog
- Probable chromatin modification-related protein eaf7
Sequence:
MSNDVDDESKIETKSYEAKDIVYKSKVFAFKDGEYRKAEILMIQKRTRGVVYYVHYNDYNKRLDEWITIDNIDLSKGIEYPPPEKPKKAHGKGKSSKRPKAVDRRRSITAPSKTEPSTPSTEKPEPSTPSGESDHGSNAGNESLPLLEEDHKPESLSKEQEVERLRFSGSMVQNPHEIARIRNINKICIGDHEIEPWYFSPYPKEFSEVDIVYICSFCFCYYGSERQFQRHREKCTLQHPPGNEIYRDDYISFFEIDGRKQRTWCRNICLLSKLFLDHKMLYYDVDPFLFYCMCRRDEYGCHLVGYFSKEKESSENYNLACILTLPQYQRHGYGKLLIQFSYELTKREHKHGSPEKPLSDLGLISYRAYWAEQIINLVLGMRTETTIDELANKTSMTTNDVLHTLQALNMLKYYKGQFIICISDGIEQQYERLKNKKRRRINGDLLADWQPPVFHPSQLRFGW
Protein: Acyl-CoA dehydrogenase, putative (O53550)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MDFTTTEAAQDLGGLVDTIVDAVCTPEHQRELDKLEQRFDRELWRKLIDAGILSSAAPESLGGDGFGVLEQVAVLVALGHQLAAVPYLESVVLAAGALARFGSPELQQGWGVSAVSGDRILTVALDGEMGEGPVQAAGTGHGYRLTGTRTQVGYGPVADAFLVPAETDSGAAVFLVAAGDPGVAVTALATTGLGSVGHLELNGAKVDAARRVGGTDVAVWLGTLSTLSRTAFQLGVLERGLQMTAEYARTREQFDRPIGSFQAVGQRLADGYIDVKGLRLTLTQAAWRVAEDSLASRECPQPADIDVATAGFWAAEAGHRVAHTIVHVHGGVGVDTDHPVHRYFLAAKQTEFALGGATGQLRRIGRELAETPA
Protein: Periodic tryptophan protein 2 homolog (Q9C1X1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized WD repeat-containing protein C2E1P5.05
- U3 small nucleolar RNA-associated protein 4
- Probable U3 small nucleolar RNA-associated protein 7
- U3 small nucleolar RNA-associated protein 6
- Uncharacterized WD repeat-containing protein C3D6.12
- U3 small nucleolar RNA-associated protein 10
- rRNA biogenesis protein rrp5
- U3 small nucleolar RNA-associated protein 22
- Probable U3 small nucleolar RNA-associated protein 18
- U3 small nucleolar RNA-associated protein 21 homolog
Sequence:
MKTEFGFSNLVGTIFSKGNLVFTPDGFSILSPVGNRVSVYNLKDNTSYTFPFENHKNISHIALSPTSTLLLSVDEEGRCILCNFLRRSVLHYFNFKSPVGAIEFSPNGKFFAVSLGKLIQVWRTPNSLEEREFAPFVLHREYTGHFDDIVSISWSADSRFFISTSKDLTARLHSVDPIEGFHPCALTGHKNTVVSGFFSKDQQTIYTVSKDGALFVWKYSPLFQAGEVIDEEAEENKTRTHIWLIKERHYFNQNSKLRCAAFHPTSNLLVVGFSSGLFGIYELPSFTMLYQLSITQSNIDTLTVNSTGDWIAIGSSKLGQLLVWEWQSESYVLKQQSHYDALSTLQYSSDGQRIITGADDGKIKVWDMNSGFCIVTFTQHTSAVSGLCFSKRGNVLFSSSLDGSVRAWDLIRYRNFRTFTAPSRVQFSCIAVDPSGEIVCAGSQDSFEIFMWSVQTGQLLETLAGHEGPVSSLSFNSSGSLLASGSWDKTVRIWDIFSRSGIVEPLPIPSDVLSLAFHPDGKEVCVASLDGQLTFWNVQEGKQTSLIDGRKDLSGGRRFDDARTAENSSLNKTFTSICYSADGSCVLSAGTSKYVCLYDIITGVLIKKFQLSKNESLQGVQEMLNSRKMTEAGSIELIDTQGEESDLEDRIDRTLPGARRGDLSARKTRPEIICHGVQFSPSGGAFAAATTEGLMIYSLYNDFLFDPINLDMDITPSTTLTMCAEGEFLISLVMALRLNEYKVVQKVYESIPITDVEHVVQELPVSYLANFMGYLSSFAAETPHIEFHLRWMKSVLTYHGEYLRRKNFEFASQLTSLQKSIVVLSKRLSQLSSNNEFQLSFLLDKMHLRLENTA
Protein: Adenosylhomocysteinase (EC 3.13.2.1) (A5PMG3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNHGYDFPRIQFANQEDKQEFSKFPTKTGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPREKSQVNSKGSSDFCVKNIKQAEFGRREIEIAEQDMSALISLRKRAQGEKPLAGAKVAGCTHITAQTAVLIETLVALGAQCRWTACNIYSTQNEVAAALAESGVSVFAWKGESEDDFWWCIDRCVNMDGWQANMILDDGGDLTHWVYKKYPSVFKKVRGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCSALKALGAIVCVTEIDPICALQACMDGFRVVKLNEVVRQMDMVITCTGNKNVVTREHLDRMKNGCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRVILLAEGRLLNLSCSTVPSFVLSITATTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPNFDAHLTELSDEQAKYMGLNKNGPFKPNYYRY
Protein: Peptide methionine sulfoxide reductase B1, chloroplastic (OsMSRB1) (EC 1.8.4.12) (Peptide-methionine (R)-S-oxide reductase) (Q0DC89)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Involved in abiotic stress response. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantiomer.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19415325}.
Interaction partners:
- Peptide methionine sulfoxide reductase A4, chloroplastic
- Peptide methionine sulfoxide reductase A5
- Peptide methionine sulfoxide reductase A2-1
- Peptide methionine sulfoxide reductase A2-2
- Thioredoxin reductase NTRC
- 50S ribosomal protein L20
- 50S ribosomal protein L20
- Large ribosomal subunit protein bL20c
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Large ribosomal subunit protein bL33c
Sequence:
MAMRQYAAATAASSSFRARPRARPSCLPAAALPLAPCCGVAWSRASYRRASVRAMGAASSSSSSSSSSPSPQGQAQAQAQGKPNYSTSLTDEEWRKRLTKDQYYITRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYQPIGDNVKCKLDMSIIFMPRTEVLCAVCDAHLGHVFDDGPRPTGKRYCINSASLKLKKTQ
Protein: Reticulon-2 (Neuroendocrine-specific protein-like 1) (NSP-like protein 1) (Neuroendocrine-specific protein-like I) (NSP-like protein I) (NSPLI) (O75298)
Organism: Homo sapiens (Human)
Function: Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity. Enhances trafficking of the glutamate transporter SLC1A1/EAAC1 from the endoplasmic reticulum to the cell surface (By similarity). Plays a role in the translocation of SLC2A4/GLUT4 from intracellular membranes to the cell membrane which facilitates the uptake of glucose into the cell (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22232211}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q6WN19}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O70622}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O70622}. Note=Localizes to intermediate filaments in mononucleated myoblasts and to Z lines in mature myotubes. {ECO:0000250|UniProtKB:O70622}.
Interaction partners:
- Atlastin-1
- Receptor expression-enhancing protein 5
- Reticulon-1
- Spastin
- Reticulon-4
- Receptor expression-enhancing protein 1
- Receptor expression-enhancing protein 2
- Beta-secretase 1
- Atlastin-3
Sequence:
MGQVLPVFAHCKEAPSTASSTPDSTEGGNDDSDFRELHTAREFSEEDEEETTSQDWGTPRELTFSYIAFDGVVGSGGRRDSTARRPRPQGRSVSEPRDQHPQPSLGDSLESIPSLSQSPEPGRRGDPDTAPPSERPLEDLRLRLDHLGWVARGTGSGEDSSTSSSTPLEDEEPQEPNRLETGEAGEELDLRLRLAQPSSPEVLTPQLSPGSGTPQAGTPSPSRSRDSNSGPEEPLLEEEEKQWGPLEREPVRGQCLDSTDQLEFTVEPRLLGTAMEWLKTSLLLAVYKTVPILELSPPLWTAIGWVQRGPTPPTPVLRVLLKWAKSPRSSGVPSLSLGADMGSKVADLLYWKDTRTSGVVFTGLMVSLLCLLHFSIVSVAAHLALLLLCGTISLRVYRKVLQAVHRGDGANPFQAYLDVDLTLTREQTERLSHQITSRVVSAATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLLILGVIGLFTIPLLYRQHQAQIDQYVGLVTNQLSHIKAKIRAKIPGTGALASAAAAVSGSKAKAE
Protein: Thromboxane A2 receptor (Prostanoid TP receptor) (K7ER80)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MWPNGSSLGPCFRPTNITLEERRLIASPWFAASFCVVGLASNLLALSVLAGARQGGSHTRSSFLTFLCGLVLTDFLGLLVTGTIVVSQHAALFEWHAVDPGCRLCRFMGVVMIFFGLSPLLLGAAMASERYLGLHRPDSAAKPACHEPRRAAVPHHGEGAAHLLARGHLEPDPGPLGVYPVPPRRAPASPASPQHPAQVAVPPAPAHAALRAAVGSGQSAPPAPFRGALGPSDSPSACSEDSGAGGAGWTVGISSRVLG
Protein: DNA-directed DNA polymerase (EC 2.7.7.7) (Q8MWB2)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MLRRLFKPQLMVPWSRQPPTCCSSQIINIISRGLSQRGEPLGAAAPSSVSSVSVPPVASLHTPVMHSNAFAASEVKKLLAKAQYSLFTLGWNPGTDDYCIYCATTNELVRAKKDTLWKAIFWMEGRIGDDYIAGLLFPSDGTPALTEVAAMVREKCRRQVVVAPDTWGICYLTLKNQRDFVRGMELPASLEHAAFLLMRAMFNSSLIEPSVFDVTSGAYISASCADSVSAARDCLVSWWVLFNVHKKFGTSGSRKLIDPVEQIVRRVVKTVNVFVVDINVRVGKGTISEGFTMIVTIYDAQRRSQSVHMIRSLAEESAKRNTLNGLLFGEGTSAISLFVPTDRTKSSQLLAFARSCRPSCPFFVTEPSSLTPFFSGAPVTDGLSEQSDPRSTWALIRTNCFAQCPGRRLEEVLDRKLLQGFTAVANRLYSDRLHRVSPALMSAASSIPLREEPRVAWERVASLVEEERKNPVAHVNKSAFLNNVTITDAEVVFRLQQWHSTIYESPDRLEREREALEGLQRYLVVDLETTTVRRYKRVANPFTKENYVVLSGARDYRGQVFMPSRYYSRNVALRYDDLHVTSTHSLVKGSSKHSLFLPPLDDYDVLVGHNIKFDLLHMWRDVELRRFLKRGGKIWDTMYAEYLLTGHEVKLGHGAGLEEVAKSYGGQTPKLDAVKQAWSSGKDTCEIPYRTLTQYLHGDLENTELIFKKHIERALAQRQVVIILARMDGLLCTTEMEYNGLKTNVQLALSQSNELMCKVKELRRHLDNSIPKEISIDCRKYFNWASNQHLIAFFFGGKLKLSTNARESRLLPGEVFERHTLYARPEDYDKTEFPKGVFLRPPVYVVGPADCLMATGVSLDKGTKFFKMYFEAYVKQAGFRKSSSVTDSLRRAMVSVSRIDQEKCSNPDALVNLLPKRHLFLFAAFTPTSDGTISKLFLKNAITGESLTIAGDCANKVERLRAFMEGQVEAHTEMLVDADGDGSAPANNNAFADAHITILARDAPFSCARLLHSDEGISAYLSLHDGLNPQEDVGQRYVITLADTVSTLSYYRYMYGSDTEAAYADKTKVDESKLVVPMKALPRPCSSRGATSEAFKKKLVQEAAMKPEDWCNLYIDIFLHIGHAALCRESLETEAGSKKARKSKGKGGIRTPGDLPILLRERSAFIGYYNSLPDDERKKLALMTMLGRTCGTAFDAFAVMCSHDDIVEVNIGGRLNQYVPSQLDAEQVMRKFRSPTTRQLQVGEDSLTYFKKTHGDKTAETILELRAMEKLIGTYYENTDDGTGMVSLVHDDDSCIHHELIHNKTNTGRLASANPNCQNIPKEDKSPLREMFVSRYGEKGMCIEADYSQLEVVALAVLANDQQMLEDLRSNVDFHCKRVAMMRPDLQYTEILKKAKKDKEPEFVKLRQQAKIFSFQRQYGAGVKMISESTGLTQDQVRHLIEKERETYRGVDVFNSMVALSANKFDASLQNGSRNVRGHQIFKGMFPVITGSRYIFTESDVPEGLLRNKSLAVKSTNFSPTHLKNYPVQGFAGEIVQIMLGVLWRHFLRKDNYGGLAVLINTVHDCVWIDCHMDVLQDVVLETDGIMSSVRDVLNRLYPEMEVSVDFPCDVVAGENMGALRPVVIEETL
Protein: Bifocal, isoform E (M9PHL6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004232}. Rough endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004269}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004269}.
Interaction partners:
Sequence:
MESQKRPSLDLHTDVPAGLAAGGSGLGAAAEMSPTSGFLPDMPQWKKDLIQRRKTNVARTQAASITSPTDGSCGALAEANAAPGAIADFTEPATISSTSQKRNMIGSEEKSEKSSISNTNSDSTGGHHSVVAVSLSPDAAATTNVTVTPIPKQRSSLLNTRSQEREMVRYILSESGERDGELESGEQPAGVVSNSRCGEVETGTIGSPSSSANQNPNPNHLKTKCKPGQSVAEGKPSAKETIVDNSKSCSKTKSISDKLQSNKFIIQQQQQQQQQQQQQQQLSPTKVTVKPTMVAMQEMKKTTKQNGQHRHLAGKIGSVAGGDVDPQHPPTNPIPDSLDTGEDLSYGPGIVSKLRCRYLSLALRESRQQSSKQRLQRSTSLNTLLDRDDDEVEVEEPEMTNSQVRAKSTPPPILGAKPTPKPSSQHQRPVSLGANGAGSAVNPPSNSDQAQTGAVANGGAGSGQRSRHFKRGNEVMKRARSVEALLCEKSPWNSQRISTAGAAAAAAPSPPAPKATAAAPSPVTSPTCVTIEDKIHNARERLHSGTDTAPPKRLTSIIDDTERPPPDLVKQTLKMFEASANRRPRAAHRSNGVGGVASKVANYKSIIKDQKQPSSAAATPPPTGMGFASSTPLRHVHPDIIPRQVDSPVSALSVMMRRMELQEPETPERETRDAEATPQSEALSETERNDRDEGDGEVDDDNHNNNDDDHDDGDDGSDNNEQRDKMGAAAAGDKPKPPAESAAGGAQRSFAASTENAHVASGSSSSTSASVRKLSNNNDSSSGPAVTKQIGVIRPLFNSQGAGSTPLTSREIEKNRINEMKKSTATDAGGSVSGSGTVAGAGSGTSPTTSLDSVINTKEAASSETDASASPLWTLRKLRNQSQTAGGGSGPSSSLHSTENTSMVFNFSKSTKEVPDYIESDVVIYRRKRELPKPNEPGFVLLGDLSVETSTDTDYDDYSMCPPSPCDVEFENANIVIDGKSSIRQKPKESSFRVQFNDTLTSTFEYPSEASMTIEDPPYADPFGHVSKHHQMLLAEQMHLLQHQEQLELEQMHQLGLAPEQHHHVTVDEIIELPTSTAGHGHGIGLGHRSGAAGGGGTMLGNLPLGK
Protein: Ribose 1,5-bisphosphate phosphokinase PhnN (EC 2.7.4.23) (Ribose 1,5-bisphosphokinase) (P16690)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). Accepts ATP but not GTP as a phosphoryl donor, and uses ribose 1,5-bisphosphate but not ribose, ribose 1-phosphate, or ribose 5-phosphate as a phosphoryl acceptor.
Interaction partners:
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL
- Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
- Putative phosphonates utilization ATP-binding protein PhnK
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH
- Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase
- Probable transcriptional regulator PhnF
- Phosphonates-binding periplasmic protein
Sequence:
MMGKLIWLMGPSGSGKDSLLAELRLREQTQLLVAHRYITRDASAGSENHIALSEQEFFTRAGQNLLALSWHANGLYYGVGVEIDLWLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEINARLARAARYTPQDCHTLNNDGSLRQSVDTLLTLIHQKEKHHACL
Protein: Sex-determination protein fem-3 (Cb-FEM-3) (Q8I8U6)
Organism: Caenorhabditis briggsae
Function: Required for male development. In XO (male) animals, fem-3 directs male differentiation in all tissues. In XX (hermaphrodite animals), it specifies the first 80 or so germ cells to be sperm. Negatively regulates male development when bound to tra-2.
Interaction partners:
- Protein CBR-FEM-2
- Protein CBR-FEM-1
- Sex-determining transformer protein 2
- Protein CBR-CUL-2
- FOG-3
- Sex-determining transformer protein 1
- Protein CBR-GLD-1
- Protein CBG02702
- Protein CBG13460
- RNA helicase
Sequence:
MVPDDVEPMEVDDDGALIVDLNETVEEDEETKKEKKRRKRFREKLKRFDHYSQFSGISIAQIDWPLIQGRSLQRSPLTGQSFNADENIFRIDEWPRETFLQITSTLTFCAGAALLSNEKITLFVFQRTMKTLVAYCNFMYHRAITHNRRQINRIDVHELISRNPLRFHMFLQKFLPHPDINRTHFNNEFLYYFHNLYFQDETCRLLYHDVARYSPIINQQGTRMSLQHQIYYPDVMRNPAFDALWFTSFINPSGYSFSRFHAYRFHEALGMPPLESELIIVLDWLAKLIICDIGYKVLAWRDARGFQGLPDLLSFQMAMLEEGDPLFDLDIDYTAPPTRLFSEPTRFQTYPKFQPRRRIDFPSRFDGFYKKRRLERGLEEIQESFIMNHFPTKPLRTVYVYTHPEERRR
Protein: Heat shock protein hsp9 (P50519)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Catalase
- Stress response protein ish1
- Heat shock protein 16
- Heat shock protein 104
- Protein lsd90
- Nuclear bridge Ish domain protein les1
- Glutathione peroxidase-like peroxiredoxin gpx1
Sequence:
MSDPARKSFTEQGKEKMTPDSSKSTLDKAKESITGAYDKVASAFTSDEDKSTSQEAHDKAQRFVDDKL
Protein: Probable serine/threonine-protein phosphatase PP2A regulatory subunit (Protein phosphatase PP2A regulatory subunit A) (Q09543)
Organism: Caenorhabditis elegans
Function: Acts as a scaffolding protein for phosphatase let-92 and its regulatory subunits (Probable). Probably together with let-92 and regulatory subunit sur-6, regulates centriole duplication, microtubule outgrowth and mitotic spindle stability during early embryonic cell division by preventing the degradation of sas-5 and kinase zyg-1. During vulva development, may play a role with phosphatase let-92 and regulatory subunit sur-6 in the induction of vulva cell precursors by positively regulating let-60/Ras-MAP kinase signaling, probably by promoting lin-45 activation. Plays a positive role in axon guidance probably by inhibiting phosphatase let-92.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23336080}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23336080}. Note=Localizes to P granules in embryonic cells. {ECO:0000269|PubMed:23336080}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit
- Serine/threonine-protein phosphatase 2A regulatory subunit sur-6
- Serine/threonine protein phosphatase 2A regulatory subunit
- Serine/threonine-protein phosphatase 2A regulatory subunit pptr-1
- Serine/threonine-protein phosphatase 2A regulatory subunit rsa-1
- Serine/threonine-protein phosphatase 2A activator
- EF-hand domain-containing protein
- Striatin N-terminal domain-containing protein
- Probable protein phosphatase methylesterase 1
- EF-hand domain-containing protein
Sequence:
MSVVEEATDDALYPIAVLIDELRNEDVTLRLNSIRKLSTIALALGVERTRNELIQFLTDTIYDEDEVLLVLAEQLGNFTPLVGGPDHVHCLLLPLENLATVEETVVRDKAVESLRKIADKHSSASLEEHFVPMLRRLATGDWFTSRTSACGLFSVVYPRVSPAIKSELKSMFRTLCRDDTPMVRRAAAAKLGEFAKVFEKTAVIEGLHSSLTDLHVDEQDSVRLLTVESAIAFGTLLDKANKKKLIEPILIELFDDKSWRVRYMVAEKLIEIQNVLGEDMDTTHLVNMYTNLLKDPEGEVRCAATQRLQEFALNLPEDKRQNIICNSLLNVAKELVTDGNQLVKSELAGVIMGLAPLIGKEQTVSELLPIYMQLLNDQTPEVRLNIISSLDKVNEVIGAAQLSTSLLPAIVGLAEDGKWRVRLAIVQFMPLLASQLGQEFFDEKLLPLCLNWLTDHVFSIREASTLIMKELTQKFGGQWASTNIVPKMQKLQKDTNYLQRMTCLFCLNTLSEAMTQEQILKEIMPIVKDLVEDDVPNVRFNAAKSLKRIGKNLTPSTLTSEVKPLLEKLGKDSDFDVRYFSEEAKNSLGL
Protein: Rac-like GTPase (Ras-related C3 botulinum toxin substrate 1) (G5EBV3)
Organism: Caenorhabditis elegans
Interaction partners:
- CRAL-TRIO domain-containing protein
- Serine/threonine-protein kinase pak-1
- NCK adaptor protein family
- GLH-binding kinase 1
- Probable rho GDP-dissociation inhibitor
- Stress-activated protein kinase JNK
- Stress-activated protein kinase jnk-1
- Serine/threonine-protein kinase max-2
- CRIB domain-containing protein
- Ras-related protein rac-2
Sequence:
MSSPSRQIKCVVVGDGTVGKTCMLISYTTDSFPVQYVPTVFDNYSAQMSLDGNVVNLGLWDTAGQEDYDRLRPLSYPQTDVFILCFSVVSPVSFDNVASKWIPEIRQHCPDAPVILVGTKLDLRDEAEPMRALQAEGKSPISKTQGMKMAQKIKAVKYLECSALTQQGLTQVFEDAVRSILHPKPQKKKKSCNIM
Protein: 4E-interacting protein (E9AFM3)
Organism: Leishmania major
Interaction partners:
- Putative eukaryotic translation initiation factor eIF-4E
- Uncharacterized protein
- Uncharacterized protein
- Integral membrane protein
- PB1 domain-containing protein
- Proteophosphoglycan ppg4
Sequence:
MPSVRTMYTREELLRIATLASAMDLGPEVLRKFDVIEVAEPVPTPKRRDAESNFKGSVFTDNFSTSTTITNLGPNGGGNSGGKGGHNSGMNGGGSSSNHPGSSSTPVYGSGGGRGGDNRRGGGGGGGNGGRDDSSNSNSVRQSGYDRFAPPEGRFNRGNRNQETFEEGIEYELRQSALQKKRVAETMEREDRKGENLRQALEKFKQEGNDAEAAEAEKETDEIERLLAGITIVDDAPKAVVRSRFFSAQGPTATSAEHPATTQPSPPPPQASTTLSFGAPASSIAPATTGTPQASVLPTPANSGTQGYARGPWSSMKSDSNLWSTAPSMASALKQSLQHSLPPADASPSVPIKPPQPASQQSQPSSCPASTSHQATSMGAAAANASANSTGAPSASGPASFGVPAPAPASPPAPPQSSVLGPANGHSSTNIATAMGAKTGVSSSAAQPQAPPHTPPQTPHHSQSQPSRPAPATAIKAAPRSSGSTGVPTGAWSAADLELLLKKGATMISSAPAPPPSTAASATAAPKTQPITAAELESMLMQRARQGRGVTGNGMSTVPPSPPQFQQPPPPRQAPLLFANPSKTPPMPANSNPTSAPLSSPQQLPASMKMAPNGAMLQPKQPHQQQQPLPPPPPPMPSQMPAHSQPQSQPQPQPQIQPQIQPQQHQTPWMAMPRPPQAPPAPQPNSNGSPMHNTPPLQPLAAKMPQPAPMMQNGLQMPMQMNAQGQYFVDPAQLQRVYMTGQPMMFRRPDGTVFMQAHPMPQPQPQQAPPQQQPPFNPFGTNAQFLFQQQQQQQRR
Protein: Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (EC 6.2.1.4) (GTP-specific succinyl-CoA synthetase subunit beta) (G-SCS) (GTPSCS) (Succinyl-CoA synthetase beta-G chain) (SCS-betaG) (B1H270)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03221}.
Interaction partners:
Sequence:
MASAVAIAAQAGKLLRERSLRPRLLAVRSQAGHLTPRRWLNLQEYQSKKLMSEHGVRVQRFFVASTAKEAQEAAKRLNAKEIVLKAQILAGGRGKGVFDSGLKGGVHLTKDPKVVGQLAQQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSHNGPVLVGSPQGGVDIEEVAASSPELIFKEQIDIFEGIKDSQAQRMAENLGFLGSLKNQAADQIKKLYHLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAARYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKESQVYQAFKLLTSDPKVEAILVNIFGGIVNCAIIANGITKACQELELKVPLVVRLEGTNVQEAQNILKSSGLPITSAVDLEDAAKKAVASVAKK
Protein: Type II secretion system protein N (T2SS protein N) (General secretion pathway protein N) (Protein XcpP) (Q51575)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins (By similarity). Required for the translocation of a variety of enzymes across the outer membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:8763961}; Single-pass type II membrane protein {ECO:0000269|PubMed:8763961}.
Interaction partners:
- Secretin XcpQ
- Type II secretion system protein M
- Type II secretion system protein L
- Secretion protein XqhA
- Type II secretion system protein E
- XphA
- Type II secretion system core protein G
- Type II secretion system protein K
- Type II secretion system protein F
- Type II secretion system protein GspC N-terminal domain-containing protein
Sequence:
MIPRRSSDITIKTRSDVLPFSGASSRWLQRYAPALLAVALIIAMSISLAWQAAGWLRLQRSPVAVAASPVSHESIRSDPTRLARLFGTSAQDPNAPPPATNLDLVLKGSFVQSDPKLSSAIIQRQGDKPHRYAVGGEISDGVKLHAVYRDRVELQRGGRLESLPFPHRSGGLLASADDITSENDSIEQLQSLQDENAAALRERLDALRQQMEATPIAEPAEEDSSEPTTTPTESD
Protein: Metallocarboxypeptidase inhibitor (MCPI) (Carboxypeptidase inhibitor) (NvCI) [Cleaved into: Metallocarboxypeptidase inhibitor c (Carboxypeptidase inhibitor c) (NvCIc)] (P86912)
Organism: Nerita versicolor (Four-tooth nerite) (Sea snail)
Function: Metallocarboxypeptidase inhibitor. Has an inhibitory effect on bovine CPA1 and CPB2, human CPA1, CPA2, CPA4, CPB1 and CPB2, and porcine CPB1. Does not inhibit D.melanogaster svr (carboxypeptidase D). Shows no activity against serine proteases subtilisin or bovine trypsin, cysteine protease papain, and aspartyl protease porcine pepsin.
Interaction partners:
Sequence:
FHVPDDRPCINPGRCPLVPDATCTFVCKAADNDFGYECQHVWTFEGQRVGCYA
Protein: DNA polymerase epsilon subunit B (DNA polymerase II subunit 2) (P24482)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: As accessory component of the DNA polymerase epsilon complex participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA replication complex GINS protein SLD5
- DNA polymerase epsilon subunit C
- DNA polymerase epsilon catalytic subunit A
- DNA replication complex GINS protein PSF3
- DNA replication complex GINS protein PSF1
- DNA replication licensing factor MCM3
- Minichromosome maintenance protein 5
- Cell division control protein 45
- DNA polymerase epsilon subunit D
- DNA replication complex GINS protein PSF2
Sequence:
MFGSGNVLPVKIQPPLLRPLAYRVLSRKYGLSIKSDGLSALAEFVGTNIGANWRQGPATIKFLEQFAAVWKQQERGLFIDQSGVKEVIQEMKEREKVEWSHEHPIQHEENILGRTDDDENNSDDEMPIAADSSLQNVSLSSPMRQPTERDEYKQPFKPESSKALDWRDYFKVINASQQQRFSYNPHKMQFIFVPNKKQNGLGGIAGFLPDIEDKVQMFLTRYYLTNDRVMRNENFQNSDMFNPLSSMVSLQNELSNTNRQQQSSSMSITPIKNLLGRDAQNFLLLGLLNKNFKGNWSLEDPSGSVEIDISQTIPTQGHYYVPGCMVLVEGIYYSVGNKFHVTSMTLPPGERREITLETIGNLDLLGIHGISNNNFIARLDKDLKIRLHLLEKELTDHKFVILGANLFLDDLKIMTALSKILQKLNDDPPTLLIWQGSFTSVPVFASMSSRNISSSTQFKNNFDALATLLSRFDNLTENTTMIFIPGPNDLWGSMVSLGASGTLPQDPIPSAFTKKINKVCKNVVWSSNPTRIAYLSQEIVIFRDDLSGRFKRHRLEFPFNESEDVYTENDNMMSKDTDIVPIDELVKEPDQLPQKVQETRKLVKTILDQGHLSPFLDSLRPISWDLDHTLTLCPIPSTMVLCDTTSAQFDLTYNGCKVINPGSFIHNRRARYMEYVPSSKKTIQEEIYI