wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS12m (28S ribosomal protein S12, mitochondrial) (MRP-S12) (S12mt) (Q29RU1)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:24799711}.
Interaction partners:
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein mS25
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS11m
Sequence:
MSWSGLLRGLSMSLNYGLALAPRPWGTRPMATLNQLHRRGPPKFPPSKPGPTEGRPQLKGVVLRTFIRKPKKPNSANRKCCRVRLSTGREAVCFIPGEGHNLQEHHVVLVQGGRTQDLPGVKLKVVRGKYDCGHVQKKK
Protein: DNA-binding protein inhibitor ID-1 (Id1 protein) (Inhibitor of DNA-binding 1, HLH protein) (Q6IQW5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKVVGPTCALKSSKVGGEDVVRCLSDQSLAISKCKIPLLDEQMTMFLQDMNSCYSKLKELVPTLPTNKKASKMEILQHVIDYIWDLQVELESKKNQSSAPRTPLTTLNAELASISVENGCSDDRIMCR
Protein: Abasic site processing protein YMR114C (EC 4.-.-.-) (Peptidase YMR114C) (EC 3.4.-.-) (Q04471)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: forms a stable thiazolidine linkage between a ring-opened abasic site and the alpha-amino and sulfhydryl substituents of its N-terminal catalytic cysteine residue (By similarity). Acts as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity).
Subcellular location: Chromosome {ECO:0000250|UniProtKB:Q96FZ2}. Note=Localizes to replication forks. {ECO:0000250|UniProtKB:Q96FZ2}.
Interaction partners:
Sequence:
MCGRFALAYDSGDLPQLLRDWNLPVNTPKDASSNSQHPHDEEDTKDQPTVSKDIFKASYNISPTNYSAVYRPDTKAIQFMRWGLVPFWTKDVSQFKTYRTFNARLENLQESKMWMRPCEKKRCAVLMSGYFEWKTVGKKKTPYFISRRDGRLMFVAGMYDYVEKDDLYTFTIITAQGPRELEWLHERMPCVLEPGTESWDAWMDVDKTTWSTEELVKLLKPDYDESKLQFYQVTDDVGKTTNTGERLIKPLLKEDSDMFSVKREKEEALLENDNEQGIDNRGVKGDKSLKGEDVFNQKKSLKRNSYDGLKKNEEQEETTLPEEGSIGDRVKREEANLSPKREGNREKRNIVNMLGNQKDSRGKKKIKK
Protein: Fructoselysine 3-epimerase (EC 5.1.3.41) (P45541)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible interconversion of fructoselysine with its C-3 epimer, psicoselysine. Allows E.coli to utilize psicoselysine for growth. Does not act on psicose or fructoselysine 6-phosphate.
Interaction partners:
- Fructoselysine 6-kinase
- Fructoselysine 6-phosphate deglycase
- Probable fructoselysine utilization operon transcriptional repressor
- Probable fructoselysine/psicoselysine transporter FrlA
- Clamp-binding protein CrfC
Sequence:
MKTGMFTCGHQRLPIEHAFRDASELGYDGIEIWGGRPHAFAPDLKAGGIKQIKALAQTYQMPIIGYTPETNGYPYNMMLGDEHMRRESLDMIKLAMDMAKEMNAGYTLISAAHAGYLTPPNVIWGRLAENLSELCEYAENIGMDLILEPLTPYESNVVCNANDVLHALALVPSPRLFSMVDICAPYVQAEPVMSYFDKLGDKLRHLHIVDSDGASDTHYIPGEGKMPLRELMRDIIERGYEGYCTVELVTMYMNEPRLYARQALERFRALLPEDER
Protein: Peptidyl-glycine alpha-amidating monooxygenase (PAM) [Includes: Peptidylglycine alpha-hydroxylating monooxygenase (PHM) (EC 1.14.17.3); Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC 4.3.2.5) (Peptidylamidoglycolate lyase) (PAL)] (P19021)
Organism: Homo sapiens (Human)
Function: Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides. Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monooxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate. The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate. Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P10731}; Single-pass membrane protein {ECO:0000250|UniProtKB:P10731}. Note=Secretory granules. {ECO:0000250|UniProtKB:P10731}.; SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted. Note=Secreted from secretory granules.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted. Note=Secreted from secretory granules.
Interaction partners:
- Kalirin
- Ras association domain-containing protein 9
- Transmembrane ascorbate-dependent reductase CYB561
- Torsin-2A
- Carboxypeptidase E
Sequence:
MAGRVPSLLVLLVFPSSCLAFRSPLSVFKRFKETTRPFSNECLGTTRPVVPIDSSDFALDIRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNNKDCSGVSLHLTRLPQPLIAGMYLMMSVDTVIPAGEKVVNSDISCHYKNYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPPEANIPIPVKSDMVMMHEHHKETEYKDKIPLLQQPKREEEEVLDQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESESDLVAEIANVVQKKDLGRSDAREGAEHERGNAILVRDRIHKFHRLVSTLRPPESRVFSLQQPPPGEGTWEPEHTGDFHMEEALDWPGVYLLPGQVSGVALDPKNNLVIFHRGDHVWDGNSFDSKFVYQQIGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALHQVFKLDPNNKEGPVLILGRSMQPGSDQNHFCQPTDVAVDPGTGAIYVSDGYCNSRIVQFSPSGKFITQWGEESSGSSPLPGQFTVPHSLALVPLLGQLCVADRENGRIQCFKTDTKEFVREIKHSSFGRNVFAISYIPGLLFAVNGKPHFGDQEPVQGFVMNFSNGEIIDIFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTEKLEHRSVKKAGIEVQEIKEAEAVVETKMENKPTSSELQKMQEKQKLIKEPGSGVPVVLITTLLVIPVVVLLAIAIFIRWKKSRAFGDSEHKLETSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKEDDGSESEEEYSAPLPALAPSSS
Protein: Transferrin receptor protein 2 (TfR2) (B2GUY2)
Organism: Rattus norvegicus (Rat)
Function: Mediates cellular uptake of transferrin-bound iron in a non-iron dependent manner. May be involved in iron metabolism, hepatocyte function and erythrocyte differentiation (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Hereditary hemochromatosis protein homolog
- Hemojuvelin
- Hepcidin
- Transmembrane protease serine 6
- Erythropoietin receptor
- Transferrin receptor protein 1
- Ferroportin
- Bone morphogenetic protein 6
- Beta-2-microglobulin
- Serotransferrin
Sequence:
MEQRWGLLRKVQQWSPRPSQTIYRRVEGPQLENLEEEDREEGEELPAQFCPMELKGPERLGSCPGRSIPIPWAAAGRKAAPYLVLTTLLIFTGAFLLGYVAFRGSCQACGDSVLVVGEDVNSEDSSRGTLYWSDLQDMFLRFLGEGRMEDTIRLTSLRERVAGSARMATLVQDILDKLSRQKLDHVWTDTHYVGLQFPDPAHPNTLHWVGADGSVQEQLPLEDPEVYCPYSATGNATGKLVYAHYGRREDLQDLKAKDVELAGSLLLVRAGITSFAQKVAIAQDFGAHGVLIYPDPADFSQDPHKPGLSSDRAVYGHVHLGTGDPYTPGFPSFNQTQFPPVESSGLPNIPAQPISADVADRLLRKLTGPVAPQEWKGRLSDSPYRLGPGPGLRLVVNNHRTSTPISNIFACIEGFAEPDHYVVIGAQRDAWGPGAAKSAVGTAILLELVRTFSSMVSSGFRPRRSLLFISWDGGDFGSVGATEWLEGYLSVLHLKAVVYVSLDNSVLGDGKFHAKTSPLLVSLIENILKQVDSPNHSGQTLYDQVAFTHPSWDAEVIQPLPMDSSAYSFTAFAGVPAVEFSFMEDDRVYPFLHTKEDTYENLHKMLRGRLPAVVLAVAQLAGQLLIRLSHDHLLPLDFGRYGDVVLRHIGNLNEFSGDLKARGLTLQWVYSARGDYIRAAEKLRKEIYSSEQSDERLMRMYNVRIMRVEFYFLSQYVSPADSPFRHIFLGQGDHTLGALVEHLRMLRSDGSGAASSGLSPGLGFQESRFRRQLALLTWTLQGAANALSGDVWNIDNNF
Protein: GPN-loop GTPase 3 (Q57WZ6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GPN-loop GTPase
- Plastid-encoded RNA polymerase subunit alpha
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
Sequence:
MGKYAVVVIGPAGSGKSTLCCTIAEHYATKGRSTHICNFDPAAEELRYSPSIDVRDLISLEDAMEGKGLGPNGGLVFCMEYLLSAGEQWICEQLGDHAEDFIIIDMPGQVEVLSHVPAVPNFVRLLQRVGYNVVVLFLLDALAATVDAGKFVSGCTFALSSMVCFDCPFMTVLTKCDLLPPDVKEGDLEHYCYCNFDHVNLKPLQGRWQEMVRTMASVIHDFNLVSFRPMDITDTAYVSNICQQMDEVLQVVDEAEVNDRDLPGPPGEGDGDIPGEDVMW
Protein: Semaphorin-4A (Semaphorin-B) (Sema B) (Q62178)
Organism: Mus musculus (Mouse)
Function: Cell surface receptor for PLXNB1, PLXNB2, PLXNB3 and PLXND1 that plays an important role in cell-cell signaling. Regulates glutamatergic and GABAergic synapse development. Promotes the development of inhibitory synapses in a PLXNB1-dependent manner and promotes the development of excitatory synapses in a PLXNB2-dependent manner. Plays a role in priming antigen-specific T-cells, promotes differentiation of Th1 T-helper cells, and thereby contributes to adaptive immunity. Promotes phosphorylation of TIMD2. Inhibits angiogenesis. Promotes axon growth cone collapse. Inhibits axonal extension by providing local signals to specify territories inaccessible for growing axons.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12374982, ECO:0000269|PubMed:15780988, ECO:0000269|PubMed:17318185, ECO:0000269|PubMed:20043131}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- T-cell immunoglobulin and mucin domain-containing protein 2
- Plexin-D1
- Plexin-B1
- Plexin-B3
- Plexin-B2
- Neuropilin-1
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Sequence:
MALPSLGQDSWSLLRVFFFQLFLLPSLPPASGTGGQGPMPRVKYHAGDGHRALSFFQQKGLRDFDTLLLSDDGNTLYVGAREAVLALNIQNPGIPRLKNMIPWPASERKKTECAFKKKSNETQCFNFIRVLVSYNATHLYACGTFAFSPACTFIELQDSLLLPILIDKVMDGKGQSPFDPVHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQPVLKTDIFLRWLHADASFVAAIPSTQVVYFFFEETASEFDFFEELYISRVAQVCKNDVGGEKLLQKKWTTFLKAQLLCAQPGQLPFNIIRHAVLLPADSPSVSRIYAVFTSQWQVGGTRSSAVCAFSLTDIERVFKGKYKELNKETSRWTTYRGSEVSPRPGSCSMGPSSDKALTFMKDHFLMDEHVVGTPLLVKSGVEYTRLAVESARGLDGSSHVVMYLGTSTGSLHKAVVPQDSSAYLVEEIQLSPDSEPVRNLQLAPAQGAVFAGFSGGIWRVPRANCSVYESCVDCVLARDPHCAWDPESRLCSLLSGSTKPWKQDMERGNPEWVCTRGPMARSPRRQSPPQLIKEVLTVPNSILELPCPHLSALASYHWSHGRAKISEASATVYNGSLLLLPQDGVGGLYQCVATENGYSYPVVSYWVDSQDQPLALDPELAGVPRERVQVPLTRVGGGASMAAQRSYWPHFLIVTVLLAIVLLGVLTLLLASPLGALRARGKVQGCGMLPPREKAPLSRDQHLQPSKDHRTSASDVDADNNHLGAEVA
Protein: Transcription factor Jra (Jun-related antigen) (Transcription factor AP-1 subunit Jra) (dJRA) (dJun) (P18289)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'. Plays a role in dorsal closure.
Subcellular location: Nucleus {ECO:0000269|PubMed:9224723}.
Interaction partners:
- Stress-activated protein kinase JNK
- Transcription factor kayak, isoforms A/B/F
- Activating transcription factor 3
- Activating transcription factor-2
- Raw, isoform A
- Signal transducer and transcription activator
- Connector of kinase to AP-1, isoform E
- Serine/threonine-protein kinase Wnk
- Pebbled, isoform A
- protein-tyrosine-phosphatase
Sequence:
MKTPVSAAANLSIQNAGSSGATAIQIIPKTEPVGEEGPMSLDFQSPNLNTSTPNPNKRPGSLDLNSKSAKNKRIFAPLVINSPDLSSKTVNTPDLEKILLSNNLMQTPQPGKVFPTKAGPVTVEQLDFGRGFEEALHNLHTNSQAFPSANSAANSAANNTTAAAMTAVNNGISGGTFTYTNMTEGFSVIKDEPVNQASSPTVNPIDMEAQEKIKLERKRQRNRVAASKCRKRKLERISKLEDRVKVLKGENVDLASIVKNLKDHVAQLKQQVMEHIAAGCTVPPNSTDQ
Protein: Cyclin-dependent kinase 1-A (CDK1-A) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog 1) (Cell division control protein 2-A) (Cell division protein kinase 1-A) (p34 protein kinase 1) (P35567)
Organism: Xenopus laevis (African clawed frog)
Function: Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition, and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. May play a role in regulating the amplitude of the cyclic expression of circadian clock genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P06493}.
Interaction partners:
Sequence:
MDEYTKIEKIGEGTYGVVYKGRHKATGQVVAMKKIRLENEEEGVPSTAIREISLLKELQHPNIVCLLDVLMQDSRLYLIFEFLSMDLKKYLDSIPSGQYIDTMLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDSKGVIKLADFGLARAFGIPVRVYTHEVVTLWYRAPEVLLGSVRYSTPVDVWSIGTIFAEIATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNSFPKWKGGSLSANVKNIDKDGLDLLAKMLIYDPAKRISARKALLHPYFDDLDKSSLPDNQIRN
Protein: Alpha-1,4 glucan phosphorylase (EC 2.4.1.1) (Q503C7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Phosphoglucomutase 1
- Glycogen debranching enzyme
- Glucan
- Glucan
- Glucose 1,6-bisphosphate synthase
- Phosphoglucomutase-2
- UTP--glucose-1-phosphate uridylyltransferase
- UTP--glucose-1-phosphate uridylyltransferase
- Alpha-amylase
- Alpha-amylase.
Sequence:
MSKPLSDHDRKKQISVRGLAGVENVADLKTNFNRHLHFTLVKDRNVSTKRDYYFALAHTVRDHLVGRWIRTQQSYYEKDPKRVYYISLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELQEMEEDAGLGNGGLGRLAACFLDSMASLGLAAYGYGIRYEFGIFNQKISNGWQVEEADDWLRYGNPWEKARPEYMRPVHFYGRTEHHPDGVKWVDTQVVLALPYDTPVPGYRNNIVNTMRLWSAKAPCEFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKASKFGSRDIVRTDFSTLPDKVAIQLNDTHPALAIPELMRVLVDEEKLPWEKAWDICVRTCAYTNHTVLPEALERWPIDLFQTLLPRHLEIIYEINRRHMERVASLYPGDMDRLRRMSLIEEGGQKRVNMAHLCIVGAHAVNGVARIHSDILKATVFKDFYEMDPHKFQNKTNGITPRRWLVMCNPGLAEVIAEKIGEDFIRDLDQLQKLRDFVNDEAFIRDIAKVKQENKLKFAVHLEEHYKVKINPNSMFDIQVKRIHEYKRQLLNCLHIITFYNRIKKEPNKQWTPRTIMIGGKAAPGYHTAKMIIRLITAIGEVVNNDPVVGDRLKVIFLENYRVTLAEKAIPAADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVEAMDVKGYNASEYYNRIPELKQAIDQIAGGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEDYIKCQEKVSALYKKPKEWTKKVILNIAGSGKFSSDRTISQYAREIWGVEPTLEKLAAPDDIK
Protein: PPPDE domain-containing protein (Q381Y2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MENLVDVGKSNGTTNGAATRRGKTQCTEWRGKCKRQKVNKQLSGGASIGFPPRLTNEHIVPPSNAAKGGKEPNSTALTESANHGSVPKDVPCFQQSNDSLSCGLASSRITFVLPCSASDENKVVTPVYLHIYELSHGILHRHSKKVTGKYVKGVYHSAVVCYGMEFFFEGGITVTCAGRTRFGEKFDKVEIGHTNKPLSSFLDWAGQRSRSTYIFHSYHPTEHNCHTFTSDAISFLMGPEASLPSYLTETIDTIVKTPVGTGVVELLVHFLGGMKYVAAENQRRRMSERKACLTRARRCIANNVINTTPPASVTLFRVSDPSSCHRTLAAVEPYGRRLLEHKAIEPPAMNFLRCVQGLCAGVEFIDPDYVTEYVNLATYALIHTTPTLRGPILNSLRVAVLHKMVSCTCAFHPLLLCALSETVRNFMNLTAEGRLALLRLLCNMGGSIHGAVALSSAEYSQMWVAAAGQAVMDYRNPAIVYTGAALIANLAVAFVLTENFVSKTVEYPHISDQCQNLITVTLFYLGSWPRERVPEAATTLMLFALFILLSSSFDASRAAKLHPFQLNFDCLIREVRTLESSTLIRMLQDILRCPHA
Protein: Protein BASIC PENTACYSTEINE7 (AtBPC7) (GAGA-binding transcriptional activator BBR/BPC7) (O82286)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator that specifically binds to GA-rich elements (GAGA-repeats) present in regulatory sequences of genes involved in developmental processes.
Subcellular location: Nucleus {ECO:0000269|PubMed:14731261}.
Interaction partners:
- GLABROUS1 enhancer-binding protein-like 3
- Protein S-acyltransferase 21
- Zinc-finger homeodomain protein 3
Sequence:
MNSFPAQNLMLSATNANKDSGLRTSNAHWLHSCIAVPKTTGIDLSQEPPAEGVMVPQSHLFPPPIRDSRNDTETVKQKSVNQSPSKALKPKPQRKKRSVSNKSKKTPSIPETKREKKNLDINIDISSFDTSGVPPPVCSCTGVSRVCYKWGMGGWQSSCCTISISTYPLPMSTTRPGARLAGRKMSNGAYVKLLARLADEGYDLSHPLDLKNHWARHGTNKFVTIK
Protein: Oxysterol-binding protein homolog C23H4.01c (O13944)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein scs2
- Vesicle-associated membrane protein-associated protein scs22
- Phosphatidylinositol 4-kinase stt4
- Regulator of V-ATPase in vacuolar membrane protein 2
- Protein transport protein sec22
- Syntaxin-like protein psy1
Sequence:
METVEIRSKSLLIQWLTVESNSLLSWQLHVKRKSIKFDIYHKKNDTSSLLDGSNKNTDRSILHTKRQHTHEAGIKKLSAAGLELFYQGERCMSEKPSEGSVYIENGGLYAFVFDNTFSKTKPKTVTFLLTAQPYNGPRIPNASVHGSPKQIISGTLLKKRRKKGQGYARRYFTLNMVEGTISYYANENSSVMRGKIPLSIAVISVAAETHEINVDSGVELWNLRAHTHQDWLRWCNALEKAKNSQTSSKLVVDERTQESSSNQLVSIYSRLRECLDIAQLYRTSRIKSASSHNFSVPEIRIQLPGDAKENKETRTSVEITAAENAQAAVTLRKVTRQLGSLLHELECFIQHHEYTKERTAQSSPSSRMSMDSNFEQHWYDAEDYESTTSQLNHYSESGAHAADATKSSVAHNEKVEDISDSDIPIMKTSSNSTSLDADRDSDTSSISDTSSNSSAPHEQLNATSLASTVDESSRSPPLPEVESNKENDIKRKQPFHDLMDSSSPDDSSFANAKSDEEVQKPSVSKNIADGAVISIPKPLTPKPSDSNSLYPLPHSKVGRRKNIPAITVPPPSILSILRKNIGKDISSIPAPVVSNEPCNLLQRCAEDLEYSNMLDKANECDDDIKIFYVAAFAVSNFSNMRHKERSVRKVFSPLLGETFELVREDRNYRFLAEKVCHRPLIIACHAESRNWIWNHSPKPIQKFWGKSVELNTLGPVTIKLACGTEFSFMKPACFLKNVAIGEKYVEPYDHMEIVDETTGDKAVIRFKSGGMFSGRSEDVLVTVIRSNGEEDPKCLQGKWTSHLDFVNTDEGNVIERIWEVGPLVDKPEDHCGMTVFAAQMNEITDLEKDKLPPTDTRLRPDQRYRENNDLDHAEPLKLELEQKQRERRKEMEEKDIKWEPRWFVPSVAGDDEDEDGSGPIWQLKKENNYWESRENSTWSSCPKLW
Protein: Phosphomutase-like protein 3 (Predicted GPI-anchored protein 12) (Q5ACP5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Uncharacterized protein
- Pdc2p
- 2-aminoadipate transaminase
Sequence:
MQQFLTLGALWTLFNVATTISLPKYSSSQTYFAQSDPNIPVSQVDDTNNFGLKSQYSWDDVVSNLASNEKLFFLQRHGQGWHNVAPSNFSRVDWNCYWAEQSGRDGVVWEDAELTPKGVQQIQNLHQRIKDTPDFPQPEKFFVSPLRRTLQTWNITWNGLPHKTPLIKEFAREIYGIDSESKRHNKTFIHNYVPSFEFESGFTEQDENWSPDKSESDQHCDYRAAVLLQDIFNDSPDEKVISVVLHSGIIYCLLDVVGHRYFPMATGGAIPVVIAIENYNTDYPLNDAWDTFKDWCPNPPASISGTATSTATGSA
Protein: Non-secretory ribonuclease (EC 4.6.1.18) (Eosinophil-derived neurotoxin) (RNase UpI-2) (Ribonuclease 2) (RNase 2) (Ribonuclease US) (P47783)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Function: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities.
Subcellular location: Lysosome {ECO:0000305}. Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule.
Interaction partners:
Sequence:
MVPKLFTSQICLLLLLGLMGVEGSLHAKPGQFTWAQWFEIQHINMTSGQCTNAMQVINNYQRRCKNQNTFLLTTFADVVHVCGNPSMPCPSNTSLNNCHHSGVQVPLIHCNLTTPSRRISNCRYTQTTANKYYIVACNNSDPVRDPPQYPVVPVHLDRII
Protein: Actin cytoskeleton-regulatory complex protein PAN1 (Mitochondrial distribution of proteins protein 3) (P32521)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization. Required for the bipolar budding of diploid cells and the correct distribution of chitin at the cell surface.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, actin patch. Note=Cytoplasmic and cortical actin patches.
Interaction partners:
- Actin cytoskeleton-regulatory complex protein END3
- Actin cytoskeleton-regulatory complex protein SLA1
- Proline-rich protein LAS17
- Protein SLA2
- Epsin-1
- Epsin-2
- Actin-binding protein
- Actin-regulating kinase PRK1
- Clathrin heavy chain
- Actin-related protein 2
Sequence:
MYNPYQQQGMGYQQQQQQQQQQPNGFYPQQQQGQSSNQPQGQPQPQQQMAFNQPQATGIGGMPQSFGNSFSSMPQQPQTGYNNNGNNGSVYGNGNFGQQPQQQQQQAKPQHTGYVPNSSMPMMNTTGTMPPPNPAQQPQLQSIQPQGTGYYQAANTANVHSVQPLQSQGTGYYVSTPNLISSNQTQQPLQAQGTGYYQSQPQQVPPPQQAQSLQPLKPQQTGFYLQPQNQAPLEPLKPTATGFVNSFANNGLNNDIKIPAIRLSFITAQDQAKFETLFRSIVTNGSNTVSGANCRKILMRSGLPPSQLARIWTLCDTSKAGELLFPEFALAMHLINDVLQGDTIPYELDSKTKNEVSSFIDAINLSIANQDSSANDAPKTPFDEFITAGVQNLQPQPTGYMPQTSFGIPLQSQITGGGVASALNPQSTGFMAPTTFNMSMNTGTPGLNPQITGGAPASMQPNITGNALQPQTTGMMPQTTGMMPQTTGMMPQTSFGVNLGPQLTGGALQSQYTGGYGSVMPQQSGPASMPNLSFNQQGLQSQLTGLQPQPTGFLPPSNFSATMPLTAQKTGFGNNEIYTKSNFNNNLIDNSSQDKISTEEKSLFYKIFETFDTQNKGLLDSPTAVEIFRKSGLNRADLEQIWNLCDINNTGQLNKQEFALGMHLVYGKLNGKPIPNVLPSSLIPSSTKLLDNLKNQLKTEPTTTKEKPSFGKIDALSYKNNDDDVLPNYRNRRKVYSAKNEEQSSFSSPSAKSVNHSSSTLQTDDISVDKTVEKKTAKPKYAGFSREINLKNIASLENEIKNISNPENCYDSSIPSDLTSRFDAIIAKLPNLFNEISTIDNEITNAKIQLYRKKNPSSIIGSGPNGEITENDRKKAKSRALLRARMSALTGKSTESEDSLSMEDEQQSAEIKRIQQENGKNQEIIKDIRSSISDISASLKSTMTGSNMISNQEFERWEFGIGLEDGVREFLDDLKSNSNKSVTESSPFVPSSTPTPVDDRSSSPSYSQFKTAEERAAYLKEQAKKRMKEKLAKFDKNRRNVTQSSRSISSENSREQPQQIAGSSNLVEPRATPFQEEKYVEVAQPTQPVQSTQPVQPTQPVQPTQPVQPTQPVQPTQPVQPTQPVQNVYNAKQESDDEDEDDEEKRLQEELKRLKLKKKADKEKRLAALRKQIEDAQNESDEEETNGKDNFGGHVNVPQAAPVAPSAAFSQNSTNAPRSVHAAVTPAAGKNSTGLPSTTMGHNPYFKDASASSTSTFDARAAEMQRRIQRGLDEDEDDGWSDEDESNNRVAVDNKVEEAKIGHPDHARAPPVTAAPLPSVTPVPPAVPVPQANTSNEKSSPIPIAPIPPSVTQEPPVPLAPPLPAVDGFQEPPIPSAPAIATAVQKSGSSTPALAGGVLPPPPPLPTQQASTSEPIIAHVDNYNGAEKGTGAYGSDSDDDVLSIPESVGTDEEEEGAQPVSTAGIPSIPPAGIPPPPPLP
Protein: Uncharacterized protein, isoform B (EC 1.11.1.-) (Uncharacterized protein, isoform C) (Q9VEP3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- IP19013p
- RE05851p
- Uncharacterized protein
- IP19120p
- Chorion protein S36
- FI16876p1
- Chorion protein c at 7F
- Chorion protein S38
- Mucin 4B, isoform B
- IP19005p
Sequence:
MRVFLVVLSVLSVAVATKCPYSAMEPSLSRSKRSSFDIRPGVSDGSLDALIKEFMPKYNGNNVHNSWAEPSASQQPLRCGVPPRNCLNDTRNLHYRTLDGSCNNLLYPEFGIAVSRYRRLLPPRQVEQAPNARLISLSLYGEQTRNDRFRTMAAMQWGQFVAHDISQLSTQGAPQDCCAEPRHPRCLPINLPRGGPIAYHTGKTCLHFARSVSDADAICPKVEEPQPEKLTVATAYLDLSSIYGNNPSQNRKVRLFKGGLLKTSYTNGQHWLPVSQNENGECGAKSECYIVPDIRNRFSPTIALLQTLLVREHNRLAENLALINPDHSDERIFQEARKINIAQFQKITYYDWLPLFVGRTYTYLNGLIYPVEPTEYVNDYDETVNPAAYAEFSAAAFRYAHTQIPGWFSLVAPNRRSNRTMRLSDFLDRTETIRLLDTSDNFDALLRGLATQLHKRSDGNIDREIKHYFNRKEFEEYGSDLKSIDIQRARDFGLASYNDVREFCGLRRAVDWADFAHEIPGEKISLLRRLYATPDDVELGVGGTLEYHVPDALFGPTLLCVIGKQFLNTRRGDRFFFERENEGGFSRAQLAEIRKVSLSSLFCSNANYLHLIQPNVFVFPNSHNLLLNCNFIPQIDLSKWQDLRPQLVH
Protein: MKIAA3015 protein (Q6ZPE7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
PNPPEIAGAAGADGGGAPVAEEQLSGERVRYPANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYKQQQQQQQQQPEKQPLSSSPLPPAGSQVAGAPSQCQAGTPQHQGLATPQAPCQLLQPVSHQQGKTQVEMQSSASSKDSSQSKIIRFTLGQKKISRLPGPTARVAAAGSEAKTRGGSAAANNRRSQSFNNYDKSKPVTSPPPPAPPSNHEKEPLASSASSHPGMSENVPAPLENSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVKHTATSAMLSVKPAGPEAPRPTPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERLEILPSFEETEELEATANRALSTVGPASSSPKIALKGIAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKGKDLTKRVSVTDRPDLKEETKADLSGVAVTEMPKKSSKIASFIPKGGKLNSTKKEATAPSHSGIPKPGMKNVSAKSPSAPIPPKEGERSRGKLSSGLPPQKAQLDSRHSSSSSSLASSEGKGPGGTSLNPSISSQTVSGSVGTTQTTGSNTVSVQLPQPQQQYNHPNTATVAPFLYRSQTDTEGNVTAESSSAGVSMEPSHYTKSGQPALEELTEDPEARRLRTVKNIADLRQNLEETMSSLRGTQVTHSTLETTFDTNVTTEISGRSILSLTGRPTPLSWRLGQSSPRLQAGDAPSMGNGYPPRANASRFISAEAGRYVYSAPLRRQLASRGSSICHVDVSDKADDDVDLEGISMDAPGYMSDGDVLSKNIRSDDITSGYMTDGGLGLYTRRLNRLPDGMAVVRETLQRNTSLGLGDADR
Protein: Krishah, isoform B (EC 2.4.2.9) (M9PHI7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRTGSPSSSGSQSEEGSSSSDHQQPQQEAQEQEQQLHTPTHAHAAVPAATSEEILAEYGSNLKLLECNSQVAELLTILRDKNTTRSDFKFYADRLIRLVIEESLNQLPYTHCDVETPTGAIYEGLKYRSGNCGVSIIRSGEAMEQGLRDCCRSIRIGKILVESDANTHEARVVYARFPDDIGSRQVLLMYPIMSTGNTVLQAVNVLREHGVPESCIILSNLFCTPIAARTVVNAFPKLKILTSELHPVAPNHFGQKYFDCI
Protein: DNA 5'-3' helicase (EC 5.6.2.3) (Q38152)
Organism: Bacillus phage SPP1 (Bacteriophage SPP1)
Interaction partners:
Sequence:
MNPEEKTVMLYNEYAEQAVLGSILTEPELIKECPLTPEHFSPGKHFNIYFTMQDLDRKGQSVDFTSIAARVGEKLPQLGGFGYLTELAASVASTTTFKQHCQTVSEYFQKRKAISIAQQIIENVNESDDGPVKPIQEAVSELMEIEASGTDDDDGSIDEALVTVYEEIESADGNITGVPSGFTELDRMTYGYKRRNFVLIAARPSMGKTAFALKQAKNMSDNDDVVNLHSLEMGKKENIKRLIVTAGSINAQKIKAARRDFASEDWGKLSMAIGEISNSNINIFDKAGQSVNYIWSKTRQTKRKNPGKRVIVMIDYLQLLEPAKANDSRTNQISQISRDLKKMARELDVVVIALSQLSRQVEQRQDKRPMLSDLRESGQLEQDADIIEFLYRDDYYDKESESKNIVEVIIAKHRDGPVGTVSLAFIKEYGNFVNLERRFDDR
Protein: C type lectin receptor C (Q68S96)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
- Ubiquitin conjugation factor E4 B
Sequence:
MVDMGSTACDGMYSKLIDKDSQYLDDSELRGHEVHAVSVPSLRAGSRQSGQGPYRLATGCLATLCAVLLLSVIAVSAHYKNLNQSLRNEHLAPLPQNESGGQIQMQRQTTNVTTLTEALSKLQMEKEDLVKERDELLARLAKSEPEQTSPPLLPSPLAPKSTPLPPSTPLTCPPDWLVFNRSCYYISTRSMSWPDSQTWCKEKGGHLAIIHTAEEQTFVWNQLPRGHWNAYWFGISDETAEADWLWVDGTKLVGGFWEEGEPNNHIDEDCGYIVKTRKLERKAVSSWYDAPCQMYWPFICEIEM