wanglab/gogpt-training-data huggingface dataset:
Protein: WD repeat-containing protein WDS homolog (Protein will die slowly homolog) (Q9FND4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22676313}. Note=Associates predominantly in the form of large cytoplasmic complexes. {ECO:0000269|PubMed:22676313}.
Interaction partners:
- Ran-binding protein M homolog
- Protein GID8 homolog
- Protein RMD5 homolog
- SPla/RYanodine receptor
- At4g09200
- Protein MAEA homolog
- ARM repeat superfamily protein
- E3 ubiquitin-protein ligase UPL4
- E3 ubiquitin-protein ligase UPL3
- Protein yippee-like
Sequence:
MENGLWEVLGSKGLLKKHEFIRILVQCLYSLGFKNSASCLEFESKILYKTADSEFLEKQVLSGNWDSCVQVLDRIFDNSMDDTRNTALYLVFKQCLLEYLKRGDVSLALNVLRKQAPLLRMGKEKIHRLACDIVYSKEMESGEVDNCLVLDLRRKLLVELEKLIPLPIVIPERRLEHLVETAVMDQIDTCMYHNSCDAVSLYKDHCCGRDQIPSETVQILVAHKNEVWFVQFSNSGKYLATASSDCTAIIWKVLDDNKVELKHTLESHQNPVSFVSWSPDDTKLLTCGNAEVLKLWDVDTGVLRHTFGNNNTGFTVSSCAWFPDSTRLVCGSSDPERGIVMWDTDGNEIKAWRGTRIPKVVDLAVTPDGESMITVFSDKEIRILNLETKVERVISEEQPITSLSISGDGKFFIVNLSCQEIHLWDLAGEWKQPLKFSGHRQSKYVIRSCFGGLDSSFIASGSEDSQVYIWNLKNTKPLEVLSGHSMTVNCVSWNPKNPRMLASASDDQTIRIWGPGKPNKPLN
Protein: Tribbles homolog 1 (TRB-1) (G-protein-coupled receptor-induced gene 2 protein) (GIG-2) (SKIP1) (Q96RU8)
Organism: Homo sapiens (Human)
Function: Adapter protein involved in protein degradation by interacting with COP1 ubiquitin ligase. The COP1-binding motif is masked by autoinhibitory interactions with the protein kinase domain. Serves to alter COP1 substrate specificity by directing the activity of COP1 toward CEBPA. Binds selectively the recognition sequence of CEBPA. Regulates myeloid cell differentiation by altering the expression of CEBPA in a COP1-dependent manner (By similarity). Controls macrophage, eosinophil and neutrophil differentiation via the COP1-binding domain (By similarity). Interacts with MAPK kinases and regulates activation of MAP kinases, but has no kinase activity.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 1
- CCAAT/enhancer-binding protein alpha
- RIB43A-like with coiled-coils protein 2
- E3 ubiquitin-protein ligase COP1
- Early growth response protein 1
- Serine/threonine-protein kinase 40
- DET1 homolog
- Fos-related antigen 2
- Protein FosB
- Tribbles homolog 2
Sequence:
MRVGPVRSAMSGASQPRGPALLFPATRGVPAKRLLDADDAAAVAAKCPRLSECSSPPDYLSPPGSPCSPQPPPAAPGAGGGSGSAPGPSRIADYLLLPLAEREHVSRALCIHTGRELRCKVFPIKHYQDKIRPYIQLPSHSNITGIVEVILGETKAYVFFEKDFGDMHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTAPEILLHPWFESVLEPGYIDSEIGTSDQIVPEYQEDSDISSFFC
Protein: Calmodulin (CaM) (O16305)
Organism: Caenorhabditis elegans
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Interaction partners:
- Calcium/calmodulin-dependent protein kinase type II
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Calcium/calmodulin-dependent protein kinase type 1
- Probable 3',5'-cyclic phosphodiesterase pde-1
- Protein kinase domain-containing protein
- Protein phosphatase 2B regulatory subunit cnb-1
- Calponin-homology
- Actin
- cAMP-dependent protein kinase catalytic subunit
- Calcium/calmodulin-dependent protein kinase kinase
Sequence:
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVTMMTTK
Protein: Cytochrome c2 (P86321)
Organism: Afifella marina (Rhodobium marinum) (Rhodopseudomonas marina)
Function: Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.
Subcellular location: Periplasm {ECO:0000269|PubMed:20697695}.
Interaction partners:
Sequence:
QXGDLVAAGKKVYRQCHACHSVGEGAKNRVGPEQNNLFGRVAGSLPDFRYSKAMKSAGENGLVWTDKSLHEYLKNPRAYVPKTKMIFAGLKKPEDIDAVVAYLKTFDTDGMPDPDASTYTPPNG
Protein: Uncharacterized protein (Q580J9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQRLVSALSRCIQGRAVTTLVPTATEGVDTLEASLRSLSKSSGLIDIKQLGKLMRKLIQCSDSRKARLCKEACRMAHAAGLHAECAEMFFSCRKMGPVTLNDLVINAAACTLDPEYLQKCLSNSDGTSLTRGLASHEAVIVLRIFWQSTRCFVCIERSRKEWSEDRGERGAAKQRETVLGRYRAVSEEAFRLLKLPDDVLFSDWWARVKRLVLYHQKDKGEAAVYEQFFSCWENYHGEEFLKWVEPPCLVAMLRSCVKGERWDLAGRYVNVSRDCLLSRANHPDDTLLQHCLTYFSSSSFSKAGVVWFGRIREALVGYIPSAMVIHSAARLAGDAGDGELAVWCLQALLSERQPSSPSPHSIFPCLVALAKCRVKDFKKVLRTLEESGHVKQTGEEYLYLDLLYSRHNLFLGEELVQRVEKHLTHVDGCLSRAGFSVRNATLFLRIVQEMEHVSFFKYYMVLKRELQADASDYARAQWLSIALKWVLTQPTLKNSDYETLMMEARALLNDGKTTGAGPPLVGYSLNSKITSRLAAIHQLQGKEAPRGLVDEATVVAPIMRFTRQRHRLPRSQPPWIEAVKPPRQRELWQVRRTLEALAQREWRERVQR
Protein: Elongation factor G 1 (EF-G 1) (P28371)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein uL11
Sequence:
MEKDLTRYRNIGIFAHVDAGKTTTTERILKLTGRIHKLGEVHEGESTMDFMEQEAERGITIQSAATSCFWKDHQLNVIDTPGHVDFTIEVYRSLKVLDGGIGVFCGSGGVEPQSETNWRYANDSKVARLIYINKLDRTGADFYRVVKQVETVLGAKPLVMTLPIGTENDFVGVVDILTEKAYIWDDSGDPEKYEITDIPADMVDDVATYREMLIETAVEQDDDLMEKYLEGEEISIDDIKRCIRTGTRKLDFFPTYGGSSFKNKGVQLVLDAVVDYLPNPKEVPPQPEVDLEGEETGNYAIVDPEAPLRALAFKIMDDRFGALTFTRIYSGTLSKGDTILNTATGKTERIGRLVEMHADSREEIESAQAGDIVAIVGMKNVQTGHTLCDPKNPATLEPMVFPDPVISIAIKPKKKGMDEKLGMALSKMVQEDPSFQVETDEESGETIIKGMGELHLDIKMDILKRTHGVEVEMGKPQVAYRESITQQVSDTYVHKKQSGGSGQYAKIDYIVEPGEPGSGFQFESKVTGGNVPREYWPAVQKGFDQSVVKGVLAGYPVVDLKVTLTDGGFHPVDSSAIAFEIAAKAGYRQSLPKAKPQILEPIMAVDVFTPEDHMGDVIGDLNRRRGMIKSQETGPMGVRVKADVPLSEMFGYIGDLRTMTSGRGQFSMVFDHYAPCPTNVAEEVIKEAKERQAAA
Protein: Centrin, putative (Q584G1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-repair protein, putative
- Dynein heavy chain, putative
Sequence:
MSSSRPATGNRLAVPIRTNLPVPAPRKRRFELTDEQRQEIREAFELFDSDKNGLIDAHEMKVSMRALGFDAKKEEVLRMMQDCAARDQHNNPLMDLAGFTDLMTERFAQRDPRQEMIKAFQLFDENNTGKISLRSLRRVARELGENMTDEELQAMIDEFDTDQDGEINLDEFLAIMLEDDDY
Protein: Tubulin beta-4B chain (Tubulin beta-2C chain) (P68372)
Organism: Mus musculus (Mouse)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37295417, ECO:0000269|PubMed:37865089, ECO:0000269|PubMed:37989994}.
Interaction partners:
- Tubulin alpha-4A chain
- Tubulin alpha-1B chain
- Tubulin alpha-1A chain
- Tubulin alpha-1C chain
- Tubulin alpha-3 chain
- Tubulin alpha-8 chain
- Tubulin alpha chain-like 3
- Gap junction alpha-1 protein
- Tubulin beta-5 chain
- Microtubule-associated protein
Sequence:
MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGKYVPRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEFEEEAEEEVA
Protein: Transcriptional regulatory protein WalR (I6L8Z5)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- histidine kinase
- Metallo-beta-lactamase domain-containing protein
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- UDP-N-acetylglucosamine 2-epimerase
- Glucosyltransferase-SI
- Glucosyltransferase-S
- histidine kinase
Sequence:
MKKILIVDDEKPISDIIKFNLAKEGYDTITAFDGREALSKYEEENPDLIILDLMLPELDGLEVAKEVRKNSHVPIIMLSAKDSEFDKVIGLEIGADDYVTKPFSNRELLARVKAHLRRTENIESAVAEENASGIPEIIIGDLQILPDAFVAKKRGTEVELTHREFELLHHLATHTGQVMTREHLLETVWGYDYFGDVRTVDVTVRRLREKIEDTPSRPEYILTRRGVGYYMKSYD
Protein: Neuropeptide Y receptor type 6 (NPY6-R) (Pancreatic polypeptide receptor 2) (PP2) (Q61212)
Organism: Mus musculus (Mouse)
Function: Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is NPY = PYY >= NPY (2-36) = [Leu-31, Pro-34] NPY > NPY (13-36) > PP. The activity of this receptor is mediated by G proteins that inhibits adenylate cyclase activity.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Pro-neuropeptide Y
- Peptide YY
- Proto-oncogene tyrosine-protein kinase Src
- Pancreatic polypeptide prohormone
- Tyrosine-protein kinase HCK
- RAC-alpha serine/threonine-protein kinase
- Tyrosine-protein kinase Fyn
Sequence:
MEVLTNQPTPNKTSGKSNNSAFFYFESCQPPFLAILLLLIAYTVILIMGIFGNLSLIIIIFKKQREAQNVTNILIANLSLSDILVCVMCIPFTVIYTLMDHWVFGNTMCKLTSYVQSVSVSVSIFSLVLIAIERYQLIVNPRGWKPRVAHAYWGIILIWLISLTLSIPLFLSYHLTNEPFHNLSLPTDIYTHQVACVEIWPSKLNQLLFSTSLFMLQYFVPLGFILICYLKIVLCLRKRTRQVDRRKENKSRLNENKRVNVMLISIVVTFGACWLPLNIFNVIFDWYHEMLMSCHHDLVFVVCHLIAMVSTCINPLFYGFLNKNFQKDLMMLIHHCWCGEPQESYENIAMSTMHTDESKGSLKLAHIPTGI
Protein: Multidrug transporter QDR2 (Clotrimazole exporter QDR2) (Drug:H(+) antiporter QDR2) (DHA QDR2) (Q6FSQ7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Multidrug resistance transporter involved in resistance to the antifungal drugs miconazole, tioconazole, clotrimazole, and ketoconazole; as well as to quinidine. Decreases the intracellular accumulation of clotrimazole in and plays a role in the extrusion of this antifungal from preloaded cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23629708}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MMEDQQSLHSFISDYDQRSHAVEKYDGPDLSEVDSEDNDKMIKTNEDEAVKEPIYRTRSNQTEPDIANAPPYSRFDAKYKMALVLQCAYTGLFSTMAGAIYYPVLSVIEKQFHITEELVNITVVVYFIFQGIAPTLMGGLADSLGRRPVVLFAVTVYFGACIGLACAQTYAQIVVLRCLQAAGISPVIAINSGIIGDVTTRAERGGYVGYISGFQVLGSAFGALIGAGLSSRWGWRSIFWFLAIGSGVCLVFSIIMLPETKRTIVGNGSVTPRNYLNRAPLLMFPLIRRKLHLDDPEYETLEPRTQLSLLAPLSILKVKEISILLVTAGIQFATWSTHQTALSTVLSKNYHLSVAKIGLCYLPTGICTLISIVTSGRYLNWSYRRRFAKHKVWLKEQEEILVKENGYSREEVQNIINNDPKYVFNLVQTRLHAAFVTLLLSSSGFVAFGWCIDVKAPLASVLVMSGFASLFSNCILTFSTTLIVDIFPSKTSTATGCLNLFRCLLSALFIGCLSKMATSMTYGGVFTFLGALTALSACPLFYLLKNGREITLKRKRKEDASRAFALSVANEKAEAEGKAEESR
Protein: Mediator of RNA polymerase II transcription subunit 2 (Mediator complex subunit 2) (Q12124)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 3
- Mediator of RNA polymerase II transcription subunit 15
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 5
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 17
- Meiotic mRNA stability protein kinase SSN3
Sequence:
MVVQNSPVSSVHTANFSERGSNTRTMTYKNKLTVCFDDILKVGAEMMMQQQLKNVQLDSYLVNGFSQSQQKLLKEKVKLFHGILDDLETSLSQSSSYLETLTALGKEKEKEREEAEKKRAEQENMRKVREQEELKKRQELEEASQQQQLQQNSKEKNGLGLNFSTTAPANTTDANGSKENYQELGSLQSSSQTQLENANAANNGAAFSPLTTTRIQSQQAQPSDVMFNDLNSMDISMFSGLDSTGFDSTAFNATVDETKGFDDNDSGNNYNDINISSIENNINNNINSTKNGKDNNNESNKNNNGDEKNKNNNEDNENNNNSSEKNNNNNNNNNNNNDDNGNNNNNNSGNDNNNTTNNDSNNKNNSITTGNDNENIVNNDLPTTVVSNPGDNPPPADNGEEYLTLNDFNDLNIDWSTTGDNGELDLSGFNI
Protein: T. brucei spp.-specific protein (Q385I9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDYRGKHVASVNYDNFLQEAPRFNPREKLKRSGSPLFYSRSFREHIPTFPTVAGAFRPSSAITWVKGKNEFDRQLQSHRRYHSLLENRRNVDKLRHVLSTKAATLSSKEAQEAHESTVALLSTRSNSVVTTLGPLSSCNTTFNSDTSTFSTPQRLKSVDSIVADLTIIREAAECQSSSRQLRSNTNGSLCSEGCTGLTHLPTFCVRHGCLFVNSRANRRTEQTFVDRFTSSELPAEIPMGHDNSFTQMMGNKCGSRHIDERLLTLLRARDVSA
Protein: Peptide Im-5 (Im5) (C0HL58)
Organism: Isometrus maculatus (Lesser brown scorpion) (Scorpio maculatus)
Function: Probably forms pores in target membranes. Has antibacterial activity against Gram-negative bacterium E.coli NBRC 3972 (MIC=10 uM) and against Gram-positive bacteria S.aureus NBRC 13276 (MIC=2.5-5 uM) and B.subtilis NBRC 3009 (MIC=0.5-1 uM). Toxic to cricket A.domestica. Has hemolytic activity against sheep erythrocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:28941793}. Target cell membrane {ECO:0000305|PubMed:28941793}.
Interaction partners:
Sequence:
MKYRKQLLVLFFAYFLVVNESEAFLGSLFSIGSKLLPGVIKLFQRKKQRALMKRDLQDRMDPYQRNLKLDRYLKQLALD
Protein: Tropomyosin 1 (B7Z596)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEGKILSSVFSLILMVEYQPGKTIFQFKGIHIDTLLCTCTFFLCVLWGFSLWLLNS
Protein: Zinc finger protein kinase (Q965D1)
Organism: Trypanosoma brucei brucei
Interaction partners:
Sequence:
MLSKLFRYDTKLQGKQELSTADHRSLLELSMTDNITSVEIPQYRVRGTFVENVIECTKRNMTWQVFRRYQQFKALDQSLKQLCSRGSSRHCDYGVIPVLCGSHWTEVTNQSIDLVEKRRRHLEIYLRQLLVPGNVFYVAKTVIYDFLHDGAVPAQHQRRAIRPLIGFATPDSLADLHLENRNGEGSASRLGAASTLNDKSISMLGPSAVGESDRVDDGVGDEEEEPCKSPPGETVESGEECEDLPSADNSEAEDVRVPPPGSLCRQCNAEFSSVLYPHRCFFCRQQFCRDCLHPVELEEGEVARSCVQCYENFARKTCKPQYPPTPMASTPILQCAPAGGALDPLNLLGSTSHVRTDVTLSDFKLVTTVGRGTFGKVMKVIFREDGKVYAMKVLNKCVIHKRRMIEYIREEKNIMSSLPSHPYIVTCHFAFQTDYHLFFVLDYLPGGDMHSRVYPKLKLTESDVRLYIAELVLALQHLHRHDIAHRDVKLENIVLGEDGHLKLTDFGLARMNFSRQRRRSFVGSPEYLPPETIQGKYQTKAVDWWSAGVMLYEMLSGKTPFYSAYNCEIYNNVLKAELDLTAPCFTPEAASLIEQLLQSHPKARLQDAGAIKAHPYFASIDWAALEGKKISAPIQLDLMGNDMKYIKWKFTAEWAVIYKPPGVTRATIDLLINRFSNFAHVSEGTPPTPHLPIGQQQEEVSDGVTNPPDITGVWNVVKVEMQTEDGKITHPWGSAVCGVLAYFPEGQFSMQLTSYMRPHLRQQFVDRAVREDLVEMCNSYAGSFGKYQIKPGSNIITHRLHGCLCPNLTGSTQKYFFEVRERKENGAKVLKLFTACNALPGEDISAQTVLTWERTGSC
Protein: Fc fragment of IgG binding protein (E9Q9C6)
Organism: Mus musculus (Mouse)
Interaction partners:
- Trefoil factor 3
- Calcium-activated chloride channel regulator 1
- Ubiquitin-like protein FUBI
- Zymogen granule membrane protein 16
Sequence:
MGSPWKWWALWAGATLLWALLTPAEASCQGIQCASGQRCQMVSGKARCVAESTAVCRAQGDPHYTTFDGRRYDMMGTCSYTMAELCGSDETLPAFSVEAKNEHRGSRQVSYVGLVTVYAYSHSVSLVRGEIGFVRIDNQRSRLPASLSEGRLRVHKSGTRGVIEMDFGLVVTYDWDGQLTLSLPKRFQDQVCGLCGNYNGDPADDFLTPDLDQAPDALEFANSWKLDDGDYLCDDGCHNSCPSCTPGQTQHYKGDRLCGMLTLSTGPFSACHEFLDPKPFLDDCVFDLCVTGGERLSLCRSLSAYAQACVELGVTLENWRLPASCPMSCPANSCYDPCSPACPPSCNSEAVPTNCSSRPCVEGCVCLPGFVASGGDCVPVSSCGCIYQGRLLAPGQEVFDDDRCRRRCTCDGATQKVTCRDTTGCPSGERCNVQNGLLGCYPDNFASCQASGDPHYVSFDGKRFDFMGTCTYLLVGSCGQNAALPAFKVLVENEHRGSQTVSYTRAVRVVAHGVEVAVRRENPGRVLIDGVLQYLPFQAAGGKIQVYRQGNDAIVSIDFGLTVTYNWDAHVTAKVPSSYAKDVCGLCGNFNGNPDDDLALKGGGQASNVLDFGNSWQEEIIPGCGATEPGDCPQLDSLVTQQIQDKKECGILADPEGPFRECHKLLNPQGAIRDCVYDLCLLPGQSGPLCDALAAYAAACQAAGGTVHPWRSEELCPLTCPPNSHYEQCSYGCPLSCGDLPVQGGCGSECREGCVCNEGFALSGESCVPLASCGCVHEGAYHAPGETFYPGPGCDSLCHCEEGGLVSCEPSSCGPQEACQPSNGVLGCVAVGTTTCQASGDPHYVTFDGRRFDFMGTCVYVLAQTCGNRPGLHQFTVLQENEAWGNGKVSVTKVITVLVANYTLRLEQSQWKVKVNGVDTKLPVMLDGGKIRVSQHGSDVVIETDFGLRVAYDLVYYVRVTIPGNYYKQMCGLCGDYNGDPKDDFQKPDGSQTTDPSDFGNSWEEAVPDSPCAPVPPCTGDDCDTECSPELQDKYHGEQFCGLLTSPTGPLAACHKLLDPQGPLQDCVFDLCLGGGNQSILCNIIHAYVSACQAAGGQVEPWRTETFCPMECPPHSHYEVCADTCSLGCWALNTPQQCPEGCAEGCECDSGFLYNGKACVPIEQCGCYHNGVYYEPEESVLIENCQQHCVCQPGKGMMCQDHSCKPGQVCEPSGGVLTCVTKDPCHGITCRPQETCKVQGGEGVCVPNYNSTCWLWGDPHYNSFDGWSFDFQGTCNYLLAGTLCPGVNAEGLTPFTVTTKNENRGSPAVSYVRQVTVTTLNTNISIHKNEIGKVRVNGVLMALPVYLAGGRISVINGGSKAVLETDFGLQVTYDWNWRVDVTLPSSYHGAVCGLCGNMDKNHQNDQVFPNGTMAPSIPTWGGSWQVPGWDPLCWHECQGSCPTCPEDRVEEYEGPGFCGPLAPGTGSPFTSCHAHVPPESFFKGCVLDVCLGGGSKDILCQALAAYAAACQAAGIKIEDWRTQAGCEITCPDNSHYELCGPPCPASCPPPARHTAPTVCDGPCVEGCQCDEGFVLSADQCVPLDGGCGCWVNGTYYEAGTEFWADTTCSKRCHCGPGGDSLVCKPASCGLGEECALLPSGEIGCQPTSITECQAWGDPHYTTLDGHRFDFQGTCEYLLSAPCHEPPTGTEYFNVTVANEHRGSQAVSYTRSVTLQIYGLSLTLSAQWPRKLQVNGEFVALPFHLDQKLSVYISGADVVVNTASGVSLAFDGDSFVRLRVPAAYAGTLCGLCGNYNKNPNDDLTAVGGKPEGWKVGGAPGCDQCEPEPCPKPCTPEEQEPFRGPDACGIITAPEGPLAPCHSLVPPTQYFEACLLDACQVQGHPGGLCPAIATYVAACQAAGAQLGEWRKPDFCPLQCPAHSHYQLCGDSCPVSCPSLSAPVGCETICREGCVCDAGFVLSGDTCVPVGQCGCLYQGRYYVLGATFYPGPECERLCECGPDGQVTCQEGADCEPYEECRIENGVQACHPTGCGHCLANGGLHYVTLDGRVYDLHGSCSYVLASVCHPKPGDEEFSIVLEKNSAGDPQRVVVTVAGQVVGLARGPQVTVDGEVVTLPVATGHVSVTAEGRNIVLQTNKGMKVLFDGDAHILMSIPSSFRGRLCGLCGNFNGNWSDDFVLPSGAVAPNVEAFGTAWRAPGSSLGCGEGCGPQGCPVCLAEETQAYEKNDACGKIRDPHGPFAACHKVLSPLEYFRQCVYDMCAHKGDKAYLCRSLAAYTAACQAAGAAVKPWRTDSVCPLQCPAHSHYSICTRSCQGSCAALSGLTGCTTRCFEGCECDDHFLLSHGVCIPAQDCGCVHNGQYMPVNSSLMSSDCSERCFCSPNNGLTCHEAGCPSGHVCEIQAGVRECQAARGLCSISVGANLTTFDGAHNAISSPGVYELSSRCPGLQKNVPWYRVLADVQPCHNNDKIVSKVHIFFQDGLVTVIPSKGAWVNGLRVDLPATVLTSVSVRRMPDGSMLVHQKAGVTVWLGKDGLLDVMVGDDLAAMLCGACGNFDGDQTNDAYGSQGKTPIEKWRAQDFSPCSN
Protein: Intestinal-type alkaline phosphatase (IAP) (Intestinal alkaline phosphatase) (EC 3.1.3.1) (P09923)
Organism: Homo sapiens (Human)
Function: Alkaline phosphatase that can hydrolyze various phosphate compounds.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P15693}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P15693}.
Interaction partners:
- Thiamine pyrophosphokinase 1
- Cancer-related nucleoside-triphosphatase
- 6-pyruvoyl tetrahydrobiopterin synthase
- GTP cyclohydrolase 1
- Acetylcholine receptor subunit delta
- Inhibin alpha chain
- Alkaline phosphatase, germ cell type
Sequence:
MQGPWVLLLLGLRLQLSLGVIPAEEENPAFWNRQAAEALDAAKKLQPIQKVAKNLILFLGDGLGVPTVTATRILKGQKNGKLGPETPLAMDRFPYLALSKTYNVDRQVPDSAATATAYLCGVKANFQTIGLSAAARFNQCNTTRGNEVISVMNRAKQAGKSVGVVTTTRVQHASPAGTYAHTVNRNWYSDADMPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPADASQNGIRLDGKNLVQEWLAKHQGAWYVWNRTELMQASLDQSVTHLMGLFEPGDTKYEIHRDPTLDPSLMEMTEAALRLLSRNPRGFYLFVEGGRIDHGHHEGVAYQALTEAVMFDDAIERAGQLTSEEDTLTLVTADHSHVFSFGGYTLRGSSIFGLAPSKAQDSKAYTSILYGNGPGYVFNSGVRPDVNESESGSPDYQQQAAVPLSSETHGGEDVAVFARGPQAHLVHGVQEQSFVAHVMAFAACLEPYTACDLAPPACTTDAAHPVAASLPLLAGTLLLLGASAAP
Protein: ATP-dependent RNA helicase (EC 3.6.4.13) (Q389Z8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA-binding protein, putative
- Ribosome biogenesis protein NSA1
- Nucleolar protein, putative
- NLE domain-containing protein
- ATP-dependent DEAD/H RNA helicase, putative
- Nop14-like protein
- RNA helicase
- rRNA biogenesis protein, putative
- Pumilio/PUF RNA binding protein 8, putative
- Ribosome biogenesis protein BOP1 homolog
Sequence:
MSLKKKTLKQRLRKNEMRQRQKVSKDVRKRVRTGRRQCNRFDDIESGSRPLQELVEEIAAGSAAPTREVALDPRSLTDLLLQTSASLSNTNSGGKTAAKPNVGRGNSESDGKPRLVLPEAPLPEDHPLALPEVQLGEDELGGGKDTNSVPGGKNQYRHHGDPYVFWERVGLHPLLLKALRTMRFTHPTPVQEEVLPSVLSQNVDGRAVGGKEKITPGKGKSGGRGWEKDVIISAETGSGKTLAFAIPILQHVLTNVLVNEVTQGPDGKIGNEETANAAKGKEGKGKKTKGGGKSTERGKSESFKKSRKRLREGEEEGEQLTTAPPTTTFKLQGRLMQALIVSPTRELALQISEAMQQLVQHAPQVIVGCVVGGMAPEKQQRVLNRHPHVLICTPGRLWELMQKNEGCYLGHSLSRRLSYVVLDEADKLLQSGRFEELKNLLERIHCEILPAGYVQEREEGAEAGDAELEAGFWDAEKQKFVPFPKDSPTGDDDKKETPQLRTSRKDEPRLIPMPPDPPEGHRVTTFVTSATLSLQTNYVRRDMRAKKTVIRTSNEDTMGKVLQQLEIKPSNAHVFTISPKVDVAAKIHETYLRCPGDSKDLYLYYFLKMYRERSIVFVNAISMLRRLVKLLEVLGIPVAGLHASLQQRQRLKFIDKFRKGEKRVLVATDIASRGLDVEGVRYVVHFQVPRSTDAYIHRCGRTARCGGTGLSLLMVNAQEHVSFTKLMGSLGRSTGDLEVFALQPTIVHQLHAHLKVALQIDKLQKEIDKSRANNNWARRMSREADVDVDDLIDDDADTENKAKEKAIKILRRRLMLLGEKDMGTSGGKGSFRSSAQAIGAKQAESKLVERAQLQVTQKPKKGSKVVKKAGARKNTEKE
Protein: acetyl-CoA C-acyltransferase (EC 2.3.1.16) (Q9W1H8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Trifunctional enzyme subunit alpha, mitochondrial
- Hydroxymethylglutaryl-CoA synthase
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase 1
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MSLQNVCRKGNAFNLLNVARKVQCRALSAAVANPQPKQKNSQNIVLVDGVRTPFLTSGTTYSKLMPHELARHSLLSLLQKNRLDKELIDYIVYGSVIQEVKTSNIAREAALAAGFSNKTPAHTVTMACISSNAAITTGMGLIATNTYDVIVAGGVEFMSDVPIRHSRKMRSLLLKANKAKTLGQRLALLSTFRPDFLAPELPAVAEFSSGETMGHSADRLASAFNVSRSEQDEYALRSHTLAKEAQEKGYFTDLVPFKVSGVDQIVDKDNGIRVSSPESLAKLRPAFVKPYGTVTAANASFLTDGASACIIMTEEKAKQLGLKPKAYLRDFLFVSQDPVNQLLLGPAYGIPKLLKKAGLTLKDIDSWEIHEAFAGQIVANLKALDSDWFCKTYLGLNEKVGTPDLSKWNNWGGSLSIGHPFAATGVRLCMHTANRLVREDGKLGVVAACAAGGQGVAMLIERYPGATAD
Protein: TNF receptor-associated factor (EC 2.3.2.27) (Q6DEG0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PIRNR:PIRNR015614}.
Interaction partners:
- Serine/threonine-protein kinase TBK1
- TRAF family member-associated NFKB activator.
- Mitochondrial antiviral-signaling protein
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Inhibitor of nuclear factor kappa B kinase subunit epsilon
- TIR domain-containing adapter molecule 1
- Mitogen-activated protein kinase kinase kinase 14
- Receptor-interacting serine-threonine kinase 2.
- OTU domain-containing protein 5-A
- Interferon regulatory factor 3
Sequence:
MSAGRNVEQQIPLQQRPPSLAMPSMAQRPRPEPGFSPLHGGFRDHFVTTPEPKYCCETCRLVLCNPRQTECGHRFCESCINELLSKPNPVCPADLLPLFEDKIFRDVCCNREIMALKVYCRSEKNGCKEQMCLQQVMEHLVICPYFEVPCPLGKCKEKMMRKDMPEHLSRKCKHREVTCEFCSLKMALTELQKHKETVCPAFPVACPNHCSFSSILRSELSSHQHDCPKAQVTCSFIRYGCSYKGLNQEMREHESSFASEHLRMMAVRNTTLEAKVEDVKSELMERYKVLPSLSSRLAEVERQYEEMREKNRQLEQKLVSMQMLMSSHSEKLLEVEMELRELRPLRAMREEVETLRGSVESMRSMVSSLDSSCVNSASGSHTLASLEQQLTRHDDLMSVHDVRLAEMDLKLQVLETASFNGTLIWKIRDYKRRKQEAVVSKTLSLYSQPFYTGYFGYKMCARVYLNGDGMGKGTHLSLFFVVMRGEYDALLQWPFKQKVTLMLMDQGPARKHLGDAFKPDPSSSSFRRPTGEMNIASGCPLFVAQTVLENGTYIKDDTIFIKVTVDTSDLPDP