wanglab/gogpt-training-data huggingface dataset:
Protein: Fumitremorgin C monooxygenase (EC 1.14.14.119) (Cytochrome P450 monooxygenase ftmP450-3) (Fumitremorgin biosynthesis protein G) (B9WZX6)
Organism: Aspergillus fumigatus (Neosartorya fumigata)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
METLDAIQLPYLGVVGASLIVILGIILLFPLGSDPFITINQHPRDLFQTKAKQQFEYNAAALLNEGLQTGHSAFRLVTNMVTYLILKDQYAEEIKNDSRFGAHEAVDPVLLVDLPGLESMFQGSLHNQVPPMAVRALNKELVHLTPSLSEEAMNCLQTRWTDSTEWHGVSIPETVLALIAQMTTRALLGPELCRNPEWLDIAKSFTTNRAIAVAAVQSWPSFLQPVIHWFLPPCRALRRQIQCARNIILPALERERRAYCSDQPTKREFSNLVFIDQYAKGARYDATMAQLRIIAVAFQTTSDLVEKVIARLCKHPELIEPLREEVVSVVGNRGLHRHSLRKLTLMESVMKETQRLEPAVIIGMFRLAKEKVTLKDGTVVPKGTNIAFANDLRFDPEMYLEPETFDGYRFQRMREDPAKIDLAPFTKTRMSHLAFGHGKHACPGRFLACDEAKLILCHILLNYDIRAVEGSPPELRARGMFVQLDPGAMMSVRRRRGTETAPHG
Protein: UDP-glucuronosyltransferase 1A6 (UGT1A6) (EC 2.4.1.17) (A1) (P-nitrophenol-specific UDPGT) (UDP-glucuronosyltransferase 1-6) (UDPGT 1-6) (UGT1*6) (UGT1-06) (UGT1.6) (P08430)
Organism: Rattus norvegicus (Rat)
Function: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.
Subcellular location: Microsome. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MACLLPAARLPAGFLFLVLWGSVLGDKLLVVPQDGSHWLSMKEIVEHLSERGHDIVVLVPEVNLLLGESKYYRRKSFPVPYNLEELRTRYRSFGNNHFAASSPLMAPLREYRNNMIVIDMCFFSCQSLLKDSATLSFLRENQFDALFTDPAMPCGVILAEYLKLPSIYLFRGFPCSLEHIGQSPSPVSYVPRFYTKFSDHMTFPQRLANFIANILENYLYHCLYSKYEILASDLLKRDVSLPALHQNSLWLLRYDFVFEYPRPVMPNMIFIGGTNCKKKGNLSQEFEAYVNASGEHGIVVFSLGSMVSEIPEKKAMEIAEALGRIPQTLLWRYTGTRPSNLAKNTILVKWLPQNDLLGHPKARAFITHSGSHGIYEGICNGVPMVMMPLFGDQMDNAKRMETRGAGVTLNVLEMTADDLENALKTVINNKSYKENIMRLSSLHKDRPIEPLDLAVFWVEYVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAIVLTVVFIVYKSCAYGCRKCFGGKGRVKKSHKSKTH
Protein: Renin receptor (ATPase H(+)-transporting lysosomal accessory protein 2) (ATPase H(+)-transporting lysosomal-interacting protein 2) (Renin/prorenin receptor) [Cleaved into: Renin receptor extracellular fragment; Renin receptor cytoplasmic fragment] (Q9CYN9)
Organism: Mus musculus (Mouse)
Function: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (By similarity). May mediate renin-dependent cellular responses by activating ERK1 and ERK2 (By similarity). By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS) (By similarity). Through its function in V-type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26376863}; Single-pass type I membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:26376863, ECO:0000269|PubMed:30985297}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:26376863}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, dendritic spine membrane {ECO:0000269|PubMed:26376863}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:26376863}. Endosome membrane {ECO:0000269|PubMed:30985297}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase 21 kDa proteolipid subunit c''
- Renin-1
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit S1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit C 1
- Ribonuclease kappa
- V-type proton ATPase subunit d 2
- V-type proton ATPase subunit B, brain isoform
Sequence:
MAVLVVLLFFLVAGALGNEFSILRSPGSVVFRNGNWPIPGDRIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATIMVMVKGVDKLALPAGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSLLNSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDELGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLVRKSRTILEAKQENTQSPYNLAYKYNLEYSVVFNLVLWIMIGLALAVIITSYNIWNMDPGYDSIIYRMTNQKIRID
Protein: Mediator of RNA polymerase II transcription subunit 18 (Mediator complex subunit 18) (p28b) (Q9BUE0)
Organism: Homo sapiens (Human)
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. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 20
- Cyclin-C
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 26
- Mediator of RNA polymerase II transcription subunit 28
Sequence:
MEAPPVTMMPVTGGTINMMEYLLQGSVLDHSLESLIHRLRGLCDNMEPETFLDHEMVFLLKGQQASPFVLRARRSMDRAGAPWHLRYLGQPEMGDKNRHALVRNCVDIATSENLTDFLMEMGFRMDHEFVAKGHLFRKGIMKIMVYKIFRILVPGNTDSTEALSLSYLVELSVVAPAGQDMVSDDMKNFAEQLKPLVHLEKIDPKRLM
Protein: Terminal nucleotidyltransferase 5D (EC 2.7.7.19) (Non-canonical poly(A) polymerase FAM46D) (Q8NEK8)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of one adenosine molecule from an ATP to an mRNA poly(A) tail bearing a 3'-OH terminal group.
Interaction partners:
Sequence:
MSEIRFTNLTWDQVITLDQVLDEVIPIHGKGNFPTMEVKPKDIIHVVKDQLIGQGIIVKDARLNGSVASYILASHNGISYKDLDVIFGVELPGNEEFQVVKDAVLDCLLDFLPKDVKKEKLSPDIMKDAYVQKLVKVCNGHDCWSLISLSNNTGKNLELKFVSSLRRQFEFSVDSFQIVLDPMLDFYSDKNAKLTKESYPVVVAESMYGDFQEAMTHLQHKLICTRKPEEIRGGGLLKYCSLLVHGFKPACMSEIKNLERYMCSRFFIDFPHIEEQQKKIESYLHNHFIGEGMTKYDYLMTLHGVVNESTVCLMSYERRQILHLITMMALKVLGELNILPNTQKVTCFYQPAPYFAAEARYPIYVIPEPPPVSFQPYHPLHFRGSNGMS
Protein: Netrin unc-6 (Uncoordinated protein 6) (P34710)
Organism: Caenorhabditis elegans
Function: Component of an extracellular matrix cue that guides dorsoventral migrations on the epidermis. Required for the guidance of pioneer axons and migrating cells along the body wall. In particular, it is required for the guidance of axons from neurons, including SubL neurons and AIY interneurons, into the nerve ring. During gonad morphogenesis, involved in distal tip cell (DTC) migration from the dorsal side of the hermaphrodite body to the midbody to allow for formation of gonad arms. Its association with either unc-40 or unc-5 receptors will lead to axon attraction or repulsion, respectively. Involved in dendritic morphogenesis; may act by association with unc-40 at the tips of growing dendrites for interaction with unc-5 on the apposing branch to induce mutual repulsion. Involved in the positioning of ray 1, the most anterior ray sensilium, in the male tail. Required for the formation of synapses between the AVA interneurons and the PHB sensory neurons.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Epidermal basal lamina.
Interaction partners:
- Netrin receptor unc-5
- Netrin receptor unc-40
- Protein sax-3
- Slit homolog 1 protein
- Ras-related protein ced-10
- E3 ubiquitin-protein ligase TRIM9
- UNC-34
- Ig-like and fibronectin type-III domain-containing protein C27B7.7
- BMP-like protein unc-129
- Abnormal cell migration protein 10
Sequence:
MITSVLRYVLALYFCMGIAHGAYFSQFSMRAPDHDPCHDHTGRPVRCVPEFINAAFGKPVIASDTCGTNRPDKYCTVKEGPDGIIREQCDTCDARNHFQSHPASLLTDLNSIGNMTCWVSTPSLSPQNVSLTLSLGKKFELTYVSMHFCSRLPDSMALYKSADFGKTWTPFQFYSSECRRIFGRDPDVSITKSNEQEAVCTASHIMGPGGNRVAFPFLENRPSAQNFENSPVLQDWVTATDIKVVFSRLSPDQAELYGLSNDVNSYGNETDDEVKQRYFYSMGELAVGGRCKCNGHASRCIFDKMGRYTCDCKHNTAGTECEMCKPFHYDRPWGRATANSANSCVACNCNQHAKRCRFDAELFRLSGNRSGGVCLNCRHNTAGRNCHLCKPGFVRDTSLPMTHRKACKSCGCHPVGSLGKSCNQSSGQCVCKPGVTGTTCNRCAKGYQQSRSTVTPCIKIPTKADFIGSSHSEEQDQCSKCRIVPKRLNQKKFCKRDHAVQMVVVSREMVDGWAKYKIVVESVFKRGTENMQRGETSLWISPQGVICKCPKLRVGRRYLLLGKNDSDHERDGLMVNPQTVLVEWEDDIMDKVLRFSKKDKLGQCPEITSHRY
Protein: Probable low-specificity L-threonine aldolase 2 (EC 4.1.2.48) (Threonine aldolase 2) (Q9FPH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Threonine aldolase involved in threonine degradation to glycine. May play a role in the removal of L-allo-threonine.
Interaction partners:
- Threonine dehydratase biosynthetic, chloroplastic
- Serine--glyoxylate aminotransferase
- Glycine dehydrogenase
- Glycine dehydrogenase
- Probable sarcosine oxidase
- Threonine synthase 1, chloroplastic
- Threonine synthase 2, chloroplastic
- Serine hydroxymethyltransferase 7
- Serine hydroxymethyltransferase 6
- Serine hydroxymethyltransferase 5
Sequence:
MVTPTTIRTVDLRSDTVTKPTESMRSAMANAEVDDDVLGNDPTALRLEKEVAEIAGKEAAMFVPSGTMGNLISVLVHCDERGSEVILGDDSHIHIYENGGVSSLGGVHPRTVKNEEDGTMEIGAIEAAVRSPKGDLHHPVTKLICLENTQANCGGRCLPIEYIDKVGELAKKHGLKLHIDGARIFNASVALGVPVKRIVQAADSVSICLSKGIGAPVGSVIVGSKKFITKARWLRKTLGGGMRQIGVLCAAALVALHENVAKLEDDHKKARVLAEGLNRIERLRVNVAAVETNIIYVDIPEDPKFGAEEACKSLEDVGVLVIPQATFRIRIVLHHQISDVDVEYVLSCFEKIFHS
Protein: DNA-directed RNA polymerase subunit Rpo7 (EC 2.7.7.6) (DNA-directed RNA polymerase subunit E) (DNA-directed RNA polymerase, subunit E') (Q980A3)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00865}.
Interaction partners:
- DNA-directed RNA polymerase subunit Rpo6
- DNA-directed RNA polymerase subunit Rpo5
- DNA-directed RNA polymerase subunit Rpo12
- DNA-directed RNA polymerase subunit Rpo3
- DNA-directed RNA polymerase subunit Rpo11
- DNA-directed RNA polymerase subunit Rpo10
- DNA-directed RNA polymerase subunit Rpo1C
- DNA-directed RNA polymerase subunit Rpo1N
- Transcription elongation factor Spt4
- DNA-directed RNA polymerase subunit Rpo4
Sequence:
MYKLIKARSIVRIPPNEFGKPLNEIALNELRQQYQEKILKDLGLVLAILNVKTSEEGILVFGDGATYHEVEFDMITYVPVVQEVVEGEVLQVDNYGIFVNLGPMDGLVHISQITDDTLKYDNVRGIIFGEKSKKVIQKGDKVRARVISVASTVTGRLPRIALTMRQPYLGKLEWITQTKK
Protein: RRM domain-containing protein (Q9XU67)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Bms1-type G domain-containing protein
- Brix domain-containing protein ZK795.3
- Periodic tryptophan protein 2 homolog
- Guanine nucleotide-binding protein-like 3 homolog
- Ribosome biogenesis protein WDR12 homolog
- rRNA biogenesis protein RRP5
- Nucleolar complex protein 2 homolog
- Pre-rRNA-processing protein pro-1
- Protein BFR2
- WD repeat-containing protein 74
Sequence:
MTTRLIVKNLPSTCTEQQLRKFFEKYGQISDASLKYTKEGKFRGFAFVGFLDEGSASNALAKSNQTFFNSKKLTVEECRPFGDANKPRAWSKYAKDSSAYKRTHGEKEEANPGKSDETEEPAPKKQKDDAKFDQFLEAKGVVVEKEVKLSKDKSAEAKKLMAELMDGIGGDTSLSLIFSGLPSSAKGKNIKEWLNPIRVKAMKIARNEDVAAAFVTFNRPPDVRRALQKDGQFLGGFKIGIEKIETPEPEHEVIEEHGASLESRDKEEETVREKILETGRLFLRNLPYATKEDDLQFLFKKYGEVSEVQVVIDKKTGACKGFAIVEFVFPEAAVAAYSALDGYVFKGRMMHILPGDEKRTKEGEEESEVVPDDPDNPLKAEAKKEKKKKSFKEEKDEQKKASAGKTAHSWNALFLGANAIADTLAQRLNVKKSDLLTSDQGESAGVRLALAETRLVRETRDFFLENGVKLDAFSKPAEKRSDTVMLAKNLPAGVESEELQRMFEKFGDCTKVLMPTEGGVSALVIMGNPVDAKKAFRALAYSRFRSQPLYLEWAPYDVMGATAPPAEDKTAEVADKPKLSKREMTYEEKRKERKNRQQGITEEEKDDGEVIEEEEKPKEVEAEDKKKSSKKQSEKEIESGSTLFVKNLAFDTTDGSLEFLFRKRYGDLVKSAQISKKLNPAEPTKPLSMGFGFVQFYTAFDAKTALKDMQGELLDGHSLELKISHRENADKGALKRKEVKQKEQGECTKLLVRNLPFEASVKEVETLFETFGAVKTIRIPKKPGQKQQHRGFGFVDFISADEAHRAFDSLVHSTHLYGRRLVLEWAKDDETVEELREKTAEKFAGNKKGVKKSKAQTEEFQQQLQIADDEKD
Protein: Thymosin beta-4 (T beta 4) [Cleaved into: Hemoregulatory peptide AcSDKP (N-acetyl-SDKP) (AcSDKP) (Seraspenide)] (P20065)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P62328}.
Interaction partners:
- Actin, cytoplasmic 2
- LIM and senescent cell antigen-like-containing domain protein 1
- Actin, cytoplasmic 1
- Scaffold protein ILK
- Profilin-4
- Profilin-1
- Profilin-2
- Profilin-3
- Profilin
Sequence:
MLLPATMSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (Q8AWF1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGCACCKQRKASKAVSNQNSCDAFNGTQASEPSRYIPDPTFNSGIPNFNDFSNPLTPPTSIINPARPPGLTGGGVTLFIALYEYDARTEDDLSFQKGEKFHIINNTEGDWWEARSLDTGKSGYIPSNYVAPVDSIQAEEWYFGKMGRKDAERQLLAQNNPRGTFLIRESETTKGAYSLSIRDWDDAKGDHVKHYKIRKLDNGGYYITTRTQFDTVQQLVEHYTGSNDGLCCYLTKACPNTTPQTMGLGRDAWEIARDTLKLNRKLGQGCFGDVWMGMWNGTTKVAVKTLKPGTMSPEAFLDEAQIMKRLRHDKLVQLYAVVSEEPIYIITEFMSQGSLLDFLKDGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELMLQCWRKDPDERHTFEYLQSFLEDYFTATEPQYQPGENL
Protein: Protein scribble homolog (Scribble1) (Q4H4B6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Scaffold protein involved in different aspects of polarized cells differentiation regulating epithelial and neuronal morphogenesis. Regulates the caudal migration of the nVII motor neurons. Required for convergent extension movements during gastrulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15829519}; Peripheral membrane protein {ECO:0000269|PubMed:15829519}. Cell junction {ECO:0000250|UniProtKB:Q14160}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q14160}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q14160}. Cytoplasm {ECO:0000250|UniProtKB:Q14160}. Postsynapse {ECO:0000250|UniProtKB:Q14160}. Presynapse {ECO:0000250|UniProtKB:Q14160}.
Interaction partners:
- LLGL scribble cell polarity complex component 2
- LLGL scribble cell polarity complex component 1.
- Vang-like protein
- Vang-like protein 2
- Cadherin EGF LAG seven-pass G-type receptor 1
- Prickle homolog 1b
- Prickle homolog 1a
- Protein tyrosine kinase 7a
- Frizzled-3
- Cadherin, EGF LAG seven-pass G-type receptor 2.
Sequence:
MLKCIPLWRCNRHVESVDKRHCSLTAVPDEIYRYNRSLEELLLDANQLRELPKPFFRLHNLRKLGLSDNEIQKLPPDVANFTQLVELDISRNDISEIPENIKFCQSLEIADFSGNPLTRLPDGFTQLRGLAHLSLNDVSLQSLPNDIGNLSNLVTLELRENLLKSLPSSLSFLVKLEQLDLGSNVLEVLPDTLGALPNLRELWLDRNQLSSLPPELGNLRQLVCLDVSENRLSELPTEISGLIALTDLLLSENLLEILPDSIGSLKKLSILKVNQNRLVHLTDSIGECENLTELMLTENLLQSLPRSLGKLKKLTNLNVDRNRLSSVPAELGGCVSLNVLSLRDNRLGKLPPELANATELHVLDVAGNRLQNLPFALANLNLKAMWLAENQSQPMLKFQTEDDEQTGEKVLTCYLLPQQPSSSLENLLERSVDEAWPTDTNLNRVSVIQFRDDSKHEEEDDETAADKRGLQRRATPHPSELKVMKNVIEARRNEAYTARPDEDLESPDAEEKRLSGLSNQSHDSQASSSTTSATSHEDKQGINSTGVELNDGQVQEEEDLDEMEVEYTEPTVHFAEEPIIRGGDEDDDYDNDDDDAERSDEVSQTPSFPAEKQRLIRKDTPHYKKHFKITKLPKPETVAALLQGFSHDGLSPTAHTPENERDGEDDEEEEEDEDEEDDLHTPFQHRLDAAELEDIRMSQMNSSLQPVKGVSFDQVNNLLIEPARIEEEELTLSILRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAARAGVKVGDKLLEVNGVDLHGAEHHTAVEALRNSGAAVVMTVLRERMVEPENAITTTPLRPEDDYFPRERRSSGLPFLLDPDCPAVSTGPAQRLATCLIRNDKGLGFSIAGGKGSTLYRVGDTGIFISRIAEGGAAHRDNILQVGDRVISINGVDMTEARHDQAVALLTGTSPTITLVVDREQSSVGGASPRTRPHSPPPPEPSDSPEQEDGGDEHLGNHLNCPMEDEYPIEEVTLIKAGGPLGLSIVGGSDHASHPFGINEPGVFISKVIPNGLASQSGLRVGDRILEVNSIDLRHATHQEAVRALLSNKQEIRMLVRRDPSPPGMQEIVIHKQPGEKLGISIRGGAKGHAGNPFDPTDEGIFISKVSSNGAAARDGRLRVGMRILEVGNNSLLGMTHTEAVRVLRASGDSLVMLICDGFDPKSASTIEASPGVIANPFAAGIVRKNSMESISSVDRDLSPEEIDIMQKEVEMVRETSQWEREEMEKVSLSSGPLKLDYKTLAALPTTSLQKVNRASPSEPFRIDSPVRDAAHSPHNSQSNIHFPSNANTKDNASTKPGAIQPLSRVRPPVSPASQDGHSSPNPFQHGLSPINSQTTDLYSPRNNVSAKQPSPETPSPLGRHSPEQRSFKDRQKYFEIDVKQQTPDKPKPRISLVGEDDLKKMKEEEAKRIEQRAREFMLDEDEEEEEEDLAKQVAHMKAHGKVVLDGVEYKVESLGSPTSRQCATPPNYSATPPSHCGSSGPSSIDGKGDSQRNSVEDSFRLEQRPNSMTGLIPVYPGESAAPIRTAKAERRHQDRLRMQSPELTVALDKELSPAEKRALEAEKRAMWRAARMKSLEQDALKAQMVIAKSKEGKKRGTLDQLSESPSPAPTPSPTPMEDISPRTVTSPGRLSPGAADDVHFMDESSSNAVSVIDPEVPVAATSALEEMALYSNKRKLRQGRRSLEAPVPT
Protein: Alkaline protease 1 (ALP) (EC 3.4.21.63) (Aspergillopeptidase B) (Aspergillus proteinase B) (Elastase) (Elastinolytic serine proteinase) (Oryzin) (Q00208)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Secreted alkaline protease that allows assimilation of proteinaceous substrates.
Subcellular location: Secreted {ECO:0000269|PubMed:25043916}.
Interaction partners:
- P/Homo B domain-containing protein
- Neutral protease 2 homolog AN7962
- Probable dipeptidyl-peptidase 5
- 60S ribosomal protein L23
- Neutral protease 2
- Neutral protease 2 homolog AN3393
Sequence:
MHSFKRSLLLLGALLPAVFGAPVEPRRAAEKVPGKYIVTFKSGLNVDQIDAHTSWASNVHKRNLERRGLAERDQYSGIEKNYKINKFAAYSGSFDDATIEEIRNSADVAHVEEDQIWYIDALTSQSGAPWGLGAISHKGEASTTYVYDTSAGEGTYAYVVDTGINADHEEFGGRASLAYNAVGGQHVDSVGHGTHVAGTIGGETYGVSKKANLLSVKVFQGESSSTSIILDGFNWAANDIVSKGRTGKSAINMSLGGGYSYAFNQAVEDAYDEGVLSVVAAGNDNIDASDSSPASAPNALTVAASTKSNTRASFSNYGSVVDIFAPGQDILSAWIGSTTATNTISGTSMATPHVVGLSLYLIALEGLSSASAVVSRIKELATQGVLSNVQGSPNLLAYNGADE
Protein: Calmodulin (CaM) (P62152)
Organism: Drosophila melanogaster (Fruit fly)
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+) (By similarity). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases (By similarity). In photoreceptor cells, light-induced Ca(2+) influx activates calmodulin, which in turn is likely to promote Crag activity in trafficking of newly synthesized ninaE (Rh1) from the trans-Golgi network to rhabdomere membranes. Together with Akap200, regulates PKA activity and ethanol-induced sensitivity and tolerance.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:18331716}.
Interaction partners:
- Neither inactivation nor afterpotential protein C
- Inactivation-no-after-potential D protein
- Transient receptor potential protein
- Myosin-VIIa
- Dilute class unconventional myosin, isoform C
- Calmodulin-related protein 97A
- Transient-receptor-potential-like protein
- Unc-13, isoform E
- Myosin heavy chain 95F
- Peptidyl-prolyl cis-trans isomerase Fkbp12
Sequence:
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVTMMTSK
Protein: LIM domain and actin binding 1 (F8VS07)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEQKENVPPGPEVCITHQEGEKISANENSLAVRSTPAEDDSRDSQVKSEVQQPVHPKPLSPDSRASSLSESSPPKAMKFQAPARETCVECQKTVYPMERLLANQQVFHISCFRCSYCNNKLSLGTYASLHGRIYCKPHFNQLFKSKGNYDEGFGHRPHKDLWASKNENEEILERPAQLANARETPHSPGVEDAPIAKVGVLAASMEAKASSQQEKEDKPAETKKLRIAWPPPTELGSSGSALEEGIKMSKPKWPPEDEISKPEVPEDVDLDLKKLRRSSSLKERSRPFTVAASFQSTSVKSPKTVSPPIRKGWSMSEQSEESVGGRVAERKQVENAKASKKNGNVGKTTWQNKESKGETGKRSKEGHSLEMENENLVENGADSDEDDNSFLKQQSPQEPKSLNWSSFVDNTFAEEFTTQNQKSQDVELWEGEVVKELSVEEQIKRNRYYDEDEDEE
Protein: Flagellum transition zone component (Q38G01)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSCFPACLRVLSTTSRFCCCIPFYCKKKMCVKKFTIRKGKEKVRSMSSNSSDVYVIEDSHSSSSPRDSSYSSTAGSGADIVGNQAGLTRTSDANACSFAQASRMQIDTGTNTEEILESDAIGRLTGVVAELFHSVTGSTYQNKLSQGACNDVEGQITSSGNLTLLNLSQRLLELARRPPPSGHVKEALTDSSAAAYMDDEPEWLGAIQHSMERTRQVFSELDLTGAKIGLNTAFVATPTSSEADTTYRAPSGRPLSLAPEPLQCETEAVGNIKEELCKLQDSTAEVRLVLNKEGVDSIIPLYNELLALRSERRQNVVSSAEALRAYLITQEECFNQRLVVAEGRELLLSREINRNCAGGDGSTIETLARDVEKLSELSRELKRLRDEHQRHAEGQGLFYHSVSETGPERKRQRTSDEGFKTLLARQLQADEQVASLRRAAESYKSEVLEWKRRYELAVRSIDRPQDSAVFNSLLEEVRRSLLQETMQRSSSLCQLFGWKLISLDGNSASIALIGNPGIQLTLPVSESLSDERSSLATGIVLARKVMESCSLVRESQQGCCGVQQGSNRAEAGAQQESTQAELSGDADNCETAINVADEVCEGLDKASDVDVCEEAKPAETVEVTEVEAELADSKVDEAPDKHTMSEAGAFYSGGLWEE
Protein: F18O14.9 (Membrane protein) (Q9LN61)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MADPLNGKSFFICFSLLFSFTLLFISPLYATESPVIEDVSTDVAVSVSETNREAVLLHNLEELVKNLTELVANLDAKLSATPLKEKNEISVDDDIGEEKERGRAKAFSVTKYSPFWSERFQFTSAVKLNSDATCINVLPFRDFEGSSKYFAIGDSKGRVYVFLRNGDVLIEFFTTVDSPVTAMVSYSSVFKNSSFVVTGHQNGAVLLHRIHEGSNGEDWNSNSVSMEHVGKFDVDDSADPVTLLEVHHVGRVRYILATDLSGKLTVLTENRTVYGSVIPSSRPLVFLKQRLLFLTESGAGSLDLRSMKIRETECEGLNHSLARTYVFDAAERSKAYGFTSEGEIIHVLLHGDIMNFKCRVRSKKKFQMEEPVALQSIKGYLLVINEEKVFAFNVSTQHYVRTAGPRLLFSAGLEEIRSAFLSHRESSSRTTTVVKTRPLIASDRENLLVIGLENGYFAVYKSKLPTLKGDFNTMLWSSPVFFFILFLFGAWHFFAKKKESLTAWGPDDPFTPTGAQNSSAKEPTFTEPSRRNDDLMDLRRRYAGGSYRSVGANDPSSRAPVDGNYRTTAQDHNNYRGGGSGLDSNGFGNRRDHLFGNNKVLDNES
Protein: RAS p21 protein activator (GTPase-activating protein) 1a (Ras GTPase-activating protein 1 isoform X1) (F1R3X3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- GTPase NRas
- Rho GTPase-activating protein 35
- HRas proto-oncogene, GTPase a.
- small monomeric GTPase
- small monomeric GTPase
- RAS-related 2
- RAS-related
- Muscle RAS oncogene homolog
- Ras-related protein M-Ras
- RAS p21 protein activator
Sequence:
MEVRGEDRGSDGSRGPDSTHFPLYSKPARVRVPVPDPDMMIYPSAGGEELAGRAAAATGCESPSSDGPGSSRMSPTDGPTVFPPLPPPPPSGLGGQGSVDESDQQDGPEYEEEEVVFPLSAPPTNQWYHGMLDRTIAEERLRQARTPGSYLIRESDRRPGSFVLSFLSVTSVVNHFRIIAMCGDYYIGGRRFSSLSDLIGYYSYVSCLLKGEKLSSPVAPPEPVEDRRRVRAILPYTKVPETDEISFLKGDMFIVHNELEDGWMWVTNVRTEEQGLIVDDLVEEVGREEDPHEGKIWYHRKISKQEAYNLLLTVGQVCSFLVRPSDNTPGDYSLFFRTNENIQRFKISPTPNNQYMMGGRYYNSVDDIIERYRKEQIVEGYTLKDPVPVQQKEQVLSDLVDGREIYNTIRRKTKDAFYKNIVKKGYLLFNKGKGKRWKHLYFILEGNDAHLIYFESEKRATKPKGLIDLSVCSVYGVHDSLFGRPNCFQIVVQHFSEEQYIFYFAGETPEQAQDWMKCLQTFCNNLRKPLQTTYNKRLRQVSSLVLYVEEAHKLPIKHFTNPYCIISLNSVQVARTHPREGQNPVFTEEFIFDDLSCDINRFEISLSNKSKKSKESDILFMRCQLSKLQRGQMIDEWFPLSSYVPLKGIEPGSLRVRVRYSMEKIMPEEEYSEFKELILQRDYHVIYALAHVCGQDRTLLASILLRILRHERAEALLLRTLNDREINMEDEATTLFRATTLASTLMEQYMKATATPFVHHALKDTILKIMESKQSCELNPSKLEKNEDVNLNLAHLLNILSELVEKIFMAAEILPPTLRYIYGCLQKSVQQKWPTNTTMRTRVVSGFVFLRLICPAILNPRMFNIIADPPSSTAGRTLTLVAKSVQNLANLVEFGAKEPYMEGVNPFIKNNKQRMIMFLDELGNVPDLPESTEHFRTDLSRDLAALHEICATHSDELRTLSNERGAQQHALKKLLAITELLQQKQVQYAMSNSSRTECTFMAVATTIQIL