wanglab/gogpt-training-data huggingface dataset:
Protein: Protein TsgA (P60778)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Protein AmpE
- p-hydroxybenzoic acid efflux pump subunit AaeB
Sequence:
MTNSNRIKLTWISFLSYALTGALVIVTGMVMGNIADYFNLPVSSMSNTFTFLNAGILISIFLNAWLMEIVPLKTQLRFGFLLMVLAVAGLMFSHSLALFSAAMFILGVVSGITMSIGTFLVTQMYEGRQRGSRLLFTDSFFSMAGMIFPMIAAFLLARSIEWYWVYACIGLVYVAIFILTFGCEFPALGKHAPKTDAPVEKEKWGIGVLFLSVAALCYILGQLGFISWVPEYAKGLGMSLNDAGTLVSNFWMSYMVGMWAFSFILRFFDLQRILTVLAGLAAILMYVFNTGTPAHMAWSILALGFFSSAIYTTIITLGSQQTKVPSPKLVNFVLTCGTIGTMLTFVVTGPIVEHSGPQAALLTANGLYAVVFVMCFLLGFVSRHRQHNTLTSH
Protein: Bacchus (Q9VQF7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Negatively regulates tyramine beta-hydroxylase tbh and thus the conversion of tyramine (TA) to octopamine (OA). In tyrosine decarboxylase 2 (Tdc2) neurons, acts in an amine-mediated signaling pathway to negatively regulate acute ethanol sensitivity probably via tbh-mediated depletion of TA.
Subcellular location: Nucleus {ECO:0000269|PubMed:23142736}.
Interaction partners:
- High mobility group protein Z
Sequence:
MSAATEQQNNGDVAVEKVAADDVSAVKDDLKAKAAAEDKAAAADAAGDAADNGTSKDGEDAADAAAAAPAKESVKGTKRPAEAKSAESKKAKKAAAADGDSDEEEALEEIIEGDSEIESDEYDIPYDGEEDDIECDDDDDDNDDGSGSDDQA
Protein: Binder of sperm protein homolog 1 (Bovine seminal plasma protein homolog 1) (Bovine seminal plasma protein-like 1) (Q3UW26)
Organism: Mus musculus (Mouse)
Function: Binds sperm in vitro and promotes sperm capacitation. Specifically promotes capacitation induced by high density lipoproteins (HDLs). Also binds heparin, phospholipid liposomes, and weakly to gelatin. Does not bind chondroitin sulfate B.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MAQPLDFLLVSICLFHSLFSFQVEDYYAPTIESLIRNPETEDGACVFPFLYRSEIFYDCVNFNLKHKWCSLNKTYQGYWKYCALSDYAPCAFPFWYRHMIYWDCTEDGEVFGKKWCSLTPNYNKDQVWKYCIE
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8UUX0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Forkhead box protein O1-A
- Forkhead box O3A
- E3 ubiquitin-protein ligase Mdm2
- 3-phosphoinositide-dependent protein kinase 1a.
- Forkhead box O3b.
- Tuberin
- 3-phosphoinositide-dependent protein kinase 1
- AKT1 substrate 1
- Serine/threonine-protein kinase TOR
- Forkhead box protein O1-B
Sequence:
MNEISVVREGWLHKRGEYIKTWRPRYFILKSDGSFIGYKEKPETSDANQPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSNSEREEWIRAIQAVANGLKSREEDEPMDINFGSPGDNSLEGMEAAITKSRTKVTMSDFDYLKLLGKGTFGKVILVREKATGMYYAMKILRKEVIIAKDEVAHTITESRVLQNTRHPFLTTLKYAFQTRDRLCFVMEYANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSKDVVYRDLKLENLMLDKDGHIKITDFGLCKEGITNEATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRNLSPEAKALLAGLLKKDPKQRLGGGPEDAKEVMTHKFFNNMNWQDVLQKKLVPPFKPQVTSETDTRYFDDEFTAQTITVTPPDQYDSLDAEDPDTRTHFSQFSYSASVRE
Protein: Small ribosomal subunit protein mS40 (28S ribosomal protein S18-2, mitochondrial) (MRP-S18-2) (28S ribosomal protein S18b, mitochondrial) (MRP-S18-b) (Mrps18-b) (S18mt-b) (Small ribosomal subunit protein bS18b) (Q9Y676)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25838379}.
Interaction partners:
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein mS22
- Large ribosomal subunit protein mL66
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein uS5m
Sequence:
MAASVLNTVLRRLPMLSLFRGSHRVQVPLQTLCTKAPSEEDSLSSVPISPYKDEPWKYLESEEYQERYGSRPVWADYRRNHKGGVPPQRTRKTCIRRNKVVGNPCPICRDHKLHVDFRNVKLLEQFVCAHTGIIFYAPYTGVCVKQHKRLTQAIQKARDHGLLIYHIPQVEPRDLDFSTSHGAVSATPPAPTLVSGDPWYPWYNWKQPPERELSRLRRLYQGHLQEESGPPPESMPKMPPRTPAEASSTGQTGPQSAL
Protein: Zymogen granule membrane protein 16 (Zymogen granule protein 16) (hZG16) (Secretory lectin ZG16) (O60844)
Organism: Homo sapiens (Human)
Function: May play a role in protein trafficking. May act as a linker molecule between the submembranous matrix on the luminal side of zymogen granule membrane (ZGM) and aggregated secretory proteins during granule formation in the TGN.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17307141}. Zymogen granule lumen {ECO:0000250|UniProtKB:Q8CJD3}. Golgi apparatus lumen {ECO:0000269|PubMed:17307141}.
Interaction partners:
- Calcium-activated chloride channel regulator 1
- Membrane-spanning 4-domains subfamily A member 12
- IgGFc-binding protein
- Colipase
- Syncollin
Sequence:
MLTVALLALLCASASGNAIQARSSSYSGEYGGGGGKRFSHSGNQLDGPITALRVRVNTYYIVGLQVRYGKVWSDYVGGRNGDLEEIFLHPGESVIQVSGKYKWYLKKLVFVTDKGRYLSFGKDSGTSFNAVPLHPNTVLRFISGRSGSLIDAIGLHWDVYPSSCSRC
Protein: Protein phosphatase 2A structural subunit (Q5ADN1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
- Protein phosphatase PP2A regulatory subunit B
- Serine/threonine-protein phosphatase
- Protein phosphatase methylesterase 1
- Serine/threonine-protein phosphatase 2A activator 2
- Serine/threonine-protein phosphatase 2A activator 1
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase SIT4
- Serine/threonine-protein phosphatase PP2A-like PPG1
Sequence:
MNNFSDDLYPLALLMDELKHDDVSNRVEAMQKLDTIAIALGPERTRKELLPFLNDVAQDDEEEVFAVLANKLGEFIPLIGGHQYSEPLISILTILASMEEPLVRDKAIDSLNKISLELSDEEINGIFLTLIQNLSQGNWFSKKIAACGLYQSVIIRVDATTRQNLLKLYFKLVTDDYPMVRRASATNLPRLIDLLTEFTEHNPNDVNKITNEDWEIISKMFQHLITDDQDSVKFLSVDVLISILEFFGKIHEYSFNADFLSSALKLIQDESWRVRYTAADRFSKIARNFTNNESDLFQLIDPFISLMKDHEGEVRKAIAKQLPVFCQLLVKFPSTKATVLNKIVPVANELSQDPQENVRASLASTITELSPILEKQATIDKLLPVFLIMLKDEFPDVRLNIISNLSVVNETIGINLLSTNLLPAITELAQDHKWRVRLAIIEYIPKLAKQLGESFFNEELLSLCMSWLWDPVYAIREAAVNNLKELTVIFGSEWAQVEIINRLLNQGDKIDNDDGNGDNNDNNDKVDYSNFIIRITCLFAITSLIPVIDYKVLIDKVLPFINGLINDSVPNIRFNVAKSYLILVESLINKKKSGQLSETNDQELKKFIDSQVLSNLQKLENDDDVDVRFYSIKSIKGINEILT
Protein: Eukaryotic translation initiation factor 1A (eIF-1A) (Eukaryotic translation initiation factor 4C) (eIF-4C) (P55877)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity).
Interaction partners:
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS14
- Eukaryotic translation initiation factor 5B
- Small ribosomal subunit protein uS5
- Eukaryotic translation initiation factor 2 subunit alpha
- Probable eukaryotic translation initiation factor 2 subunit beta
- Small ribosomal subunit protein uS15
- Protein translation factor sui1
- Eukaryotic translation initiation factor 2 subunit gamma
Sequence:
MPKNKGKGGKNRRRGKNENENEKRELTYAEEGQMYAQVTKMLGNGRIEAACFDGVKRLGHIRGKLRKKVWINQGDIILLSLREFQDEKGDVILKYTADEARTLKNQGELPETAKINETDTFGAEGEDDLDFEFDVDAI
Protein: Achaete scute target 1, isoform B (EH domain containing protein) (Q8T6I0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004159}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004159}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004159}.
Interaction partners:
Sequence:
MFSFLKREKNTQEVVENVIGELKKIYRSKLLPLEEHYQFHDFHSPKLEDPDFDAKPMILLVGQYSTGKTTFIRYLLERDFPGIRIGPEPTTDRFIAVMYDDKEGVIPGNALVVDPKKQFRPLSKYGNAFLNRFQCSSVASPVLNAISIVDTPGILSGEKQRIDRGYDFTGVLEWFAERVDRIILLFDAHKLDISDEFRRSIEALKGHDDKIRIILNKADMIDHQQLMRVYGALMWSLGKVLQTPEVARVYIGSFWDQPLRFDANRRLFEDEEQDLFRDLQSLPRNAALRKLNDLIKRARLAKVHAFIIAELRKDMPSVFGKDSKKKDLIKNLGQVYDRIQREHSISPGDFPDIKKMQEVLQHQDFTKFHSLKPHLLDIVDNMLAKDIARLMEMIPQEEMTMVADPIVKGGAFEGVIDDHVSPFGYMKGEGIDAGYGEHEWICNKDKPRTDGIFNGLGPVDGKISGATAKQELIKSKLPNSVLSKIWKLSDVDGDGFLDSDEFALALHLINVKLEGCELPTVLPEHLVPPSKRYD
Protein: Amino acid transporter heavy chain SLC3A1 (D2) (Neutral and basic amino acid transport protein) (NBAT) (Solute carrier family 3 member 1) (b(0,+)-type amino acid transporter-related heavy chain) (rBAT) (Q91WV7)
Organism: Mus musculus (Mouse)
Function: Involved in the high-affinity sodium-independent transport of cystine and neutral and dibasic amino acids (system B(0,+)-like activity). May function as an activator of SLC7A9 and be involved in the high-affinity reabsorption of cystine in the kidney proximal tubule.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12167606}; Single-pass type II membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:26739563}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- b
- Aromatic-preferring amino acid transporter, member 15)
- Solute carrier family 7 member 13
- Solute carrier family 7 member 12
- Y+L amino acid transporter 1
- Large neutral amino acids transporter small subunit 1
- Prolyl endopeptidase-like
- Y+L amino acid transporter 2
- Large neutral amino acids transporter small subunit 2
- Protein phosphatase 1B
Sequence:
MDEDKGKRDPIQMSLKGCRTNNGFVQNEDIPEQDPDPGSRDTPQPNAVSIPAPEEPHLKAVRPYAGMPKEVLFQFSGQARYRVPREILFWLTVVSVFLLIGATIAIIVISPKCLDWWQAGPIYQIYPRSFKDSDKDGNGDLKGIQEKLDYITALNIKTLWITSFYKSSLKDFRYAVEDFKEIDPIFGTMKDFENLVAAIHDKGLKLIIDFIPNHTSDKHPWFQSSRTRSGKYTDYYIWHNCTHVNGVTTPPNNWLSVYGNSSWHFDEVRKQCYFHQFLKEQPDLNFRNPAVQEEIKEIITFWLSKGVDGFSFDAVKFLLEAKDLRNEIQVNTSQIPDTVTHYSELYHDFTTTQVGMHDIVRDFRQTMNQYSREPGRYRFMGAEASAESIERTMMYYGLPFIQEADFPFNKYFTTIGTLSGHTVYEVITSWMENMPEGKWPNWMTGGPETPRLTSRVGSEYVNAMHMLLFTLPGTPITYYGEEIGMGDISVTNFNESYDSTTLVSKSPMQWDNSSNAGFTEANHTWLPTNSDYHTVNVDVQKTQPSSALRLYQDLSLLHATELVLSRGWFCLLRDDSHSVVYTRELDGIDNVFLVVLNFGESSTVLNLQGIISDLPPELRIRLSTNSASKGSAVDTRAISLEKGEGLVLEHSTKAPLHQQAAFRDRCFVSSRACYSSALDILYSSC
Protein: Disintegrin and metalloproteinase domain-containing protein 17 (ADAM 17) (EC 3.4.24.86) (TNF-alpha convertase) (TNF-alpha-converting enzyme) (CD antigen CD156b) (Q9Z1K9)
Organism: Rattus norvegicus (Rat)
Function: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). Plays a role in the proteolytic processing of ACE2 (By similarity). Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain (By similarity). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R, leading to the release of secreted form of IL6R (By similarity). Mediates the proteolytic cleavage and shedding of FCGR3A upon NK cell stimulation, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Neurogenic locus notch homolog protein 1
- Metalloproteinase inhibitor 3
- Disintegrin and metalloproteinase domain-containing protein 10
- Tumor necrosis factor
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 3
- Notch homolog 4, isoform CRA_b.
- Metalloproteinase inhibitor 1
- Transmembrane protease serine 2
- Tumor necrosis factor receptor superfamily member 16
Sequence:
MRQRLLFLTTLVPFVLAPRPPEEPGSGSHLRLEKLDSLLSDYDILSLSNIQQHSIRKRDLQSATHLETLLTFSALKRHFKLYLTSSTERFSQNLRVVVVDGKEESEYSVKWQDFFSGHVVGEPDSRVLAHIGDDDVTVRINTDGAEYNIEPLWRFVNDTKDKRMLVYKSEDIKDFSRLQSPKVCGYLNADSEELLPKGLIDREPSEEFVRRVKRRAEPNPLKNTCKLLVVADHRFYKYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGVQIEQIRILKSPQEVKPGERHFNMAKSFPNEEKDAWDVKMLLEQFSLDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYNPGVKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGLAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTIESKAQECFQERSNKVCGNSRVDEGEECDPGIMYLNNDTCCNSDCTLKPGVQCSDRNSPCCKNCQFETAQKKCQEAINATCKGVSYCTGNSSECPPPGDAEDDTVCLDLGKCKAGKCIPFCKREQELESCACADTDNSCKVCCRNLSGPCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCEKRVQDVIERFWDFIDQLSINTFGKFLADNIVGSVLVFSLIFWIPFSILVHCVDKKLDKQYESLSLFHHSNIEMLSSMDSASVRIIKPFPAPQTPGRLQALQPAAMMPPVSAAPKLDHQRMDTIQEDPSTDSHVDDDGFEKDPFPNSSAAAKSFEDLTDHPVTRSEKAASFKLQRQSRVDSKETEC
Protein: Nuclear nucleic acid-binding protein C1D (mC1D) (Small unique nuclear receptor corepressor) (Sun-CoR) (SunCoR) (O35473)
Organism: Mus musculus (Mouse)
Function: Plays a role in the recruitment of the RNA exosome complex to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA; this function may include MPHOSPH6. Can activate PRKDC not only in the presence of linear DNA but also in the presence of supercoiled DNA. Can induce apoptosis in a p53/TP53 dependent manner. May regulate the TRAX/TSN complex formation. Potentiates transcriptional repression by NR1D1 and THRB (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:9405624}. Cytoplasm {ECO:0000250|UniProtKB:Q13901}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q13901}. Note=EXOSC10 is required for nucleolar localization. Colocalizes with TSNAX in the nucleus. {ECO:0000250|UniProtKB:Q13901}.
Interaction partners:
- Exosome complex component 10
- Exosome complex component RRP46
- Exosome complex component CSL4
- Exosome complex component RRP45
- Exosome complex component RRP4
- Exosome complex component RRP43
- Exosome complex component RRP40
- Exosome complex exonuclease RRP42
- M-phase phosphoprotein 6
- Exosome complex component RRP41
Sequence:
MAGEEMNEDYPVEIHESLTALESSLGAVDDMLKTMMAVSRNELLQKLDPLEQAKVDLVSAYTLNSMFWVYLATQGVNPKEHPVKQELERIRVYMNRVKEITDKKKAAKLDRGAASRFVKNALWEPKAKSTPKVANKGKSKH
Protein: Fibroblast growth factor 18 (FGF-18) (O88182)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 3
- Fibroblast growth factor 23
- Vascular endothelial growth factor receptor 1
Sequence:
MYSAPSACTCLCLHFLLLCFQVQVLAAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQTELQKPFKYTTVTKRSRRIRPTHPG
Protein: Fatty acid amide hydrolase 1 (EC 3.5.1.99) (Anandamide amidohydrolase 1) (Q17449)
Organism: Caenorhabditis elegans
Function: Catalyzes the hydrolysis of endogenous amidated lipids like anandamide (AEA or N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine) and eicosapentaneoyl ethanolamide (EPEA or (5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl) ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules. EPEA promotes dauer formation and may constitute a signal of high nutrient availability. Breakdown of EPEA may promote lifespan extension when nutrient availability is high. Facilitates axon regeneration after injury by degradating inhibitory compounds such as AEA. FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity).
Interaction partners:
- Amidase domain-containing protein
- Glutamyl-tRNA
- Monoglyceride lipase faah-4
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D 1
- Serine aminopeptidase S33 domain-containing protein
- Lactamase_B domain-containing protein.
- Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein
- Glutamyl-tRNA
- Serine protease svh-1
- Transient receptor potential cation channel subfamily A member 1 homolog
Sequence:
MIFYLVLLVLGAIAFYVHFSNNRKKLIERLEIVAQRRRDDLSKNVEQARKAADKLDTQRRDWIGSLDFEQLRDELQRGHVTCVEAIRAYFHKAILAHEKTNAVTCFILDAERQAEELDEQAKLPYYVKPPLFGVPLSLKECLKVKGYDTTRGFVQDAYHPATEDSIQVEHYKKLGLIPFCQTNVPQSLLSYNCSNPLFGTTTNPYDSTRTCGGSSGGEGALIGAGGSLIGIGTDVGGSVRIPCHFTGTAGIKPSKMRFAHRGGGASVPGKPLIDANDGPMAKDVKTNVEFLRNVWGDIDFQSDRDPYCPPVHWNESVYSSEKKLRVGYYIDDGWFTPTPALQRAVLESKKHLEAAGHTVIPFYPPRLPSVMQLYFRAVCLDGGQYVLNKLLKDIIEPTIRFQVTLWMVPVWIQRILSYPVSLVFPRMGMLMQSLTRDTFELREAYADIEAYREEFVGLMMKDNLDVILCPASIMPAPQHDIPSKVVSGVSYTCLYNLLDFGAGVVPVTAVSKSDEEKLINEYPETDKWYQITKKATLGAVGMPIGVQVAAPPYREEAVLRTMREIEIAVTGK
Protein: ESX-4 secretion system protein EccC4 (ESX conserved component C4) (Type VII secretion system protein EccC4) (T7SS protein EccC4) (P9WNA7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ESX-4 secretion system protein eccD4
- Hypothetical alanine and valine rich protein
- Mycosin-4
- ESAT-6-like protein EsxU
- ESX-3 secretion system ATPase EccB3
- ESX-5 secretion system ATPase EccB5
- ESAT-6-like protein EsxT
- ESX-5 secretion system protein EccD5
- Possible exported protein
- ESX-3 secretion system protein EccD3
Sequence:
MNSGPACATADILVAPPPELRRSEPSSLLIRLLPVVMSVATVGVMVTVFLPGSPATRHPTFLAFPMMMLVSLVVTAVTGRGRRHVSGIHNDRVDYLGYLSVLRTSVTQTAAAQHVSLNWTHPDPATLWTLIGGPRMWERRPGAADFCRIRVGVGSAPLATRLVVGQLPPAQRADPVTRAALRCFLAAHATIADAPIAIPLRVGGPIAIDGDPTKVRGLLRAMICQLAVWHSPEELLIAGVVSDRNRAHWDWLKWLPHNQHPNACDALGPAPMVYSTLAEMQNALAATVLAHVVAIVDTAERGNGAITGVITIEVGARRDGAPPVVRCAGEVTALACPDQLEPQDALVCARRLAAHRVGHSGRTFIRGSGWAELVGIGDVAAFDPSTLWRNVNQHDRLRVPIGVTPDGTAVQLDIKEAAEQGMGPHGLCVGATGSGKSELLRTIALGMMARNSPEVLNLLLVDFKGGATFLDLAGAPHVAAVITNLAEEAPLVARMQDALAGEMSRRQQLLRMAGHLVSVTAYQRARQTGAQLPCLPILFIVVDEFSELLSQHPEFVDVFLAIGRVGRSLGMHLLLASQRLDEGRLRGLETHLSYRMCLKTWSASESRNVLGTQDAYQLPNTPGAGLLQTGTGELIRFQTAFVSGPLRRASPSAVHPVAPPSVRPFTTHAAAPVTAGPVGGTAEVPTPTVLHAVLDRLVGHGPAAHQVWLPPLDEPPMLGALLRDAEPAQAELAVPIGIVDRPFEQSRVPLTIDLSGAAGNVAVVGAPQTGKSTALRTLIMALAATHDAGRVQFYCLDFGGGALAQVDELPHVGAVAGRAQPQLASRMLAELESAVRFREAFFRDHGIDSVARYRQLRAKSAAESFADIFLVIDGWASLRQEFAALEESIVALAAQGLSFGVHVALSAARWAEIRPSLRDQIGSRIELRLADPADSELDRRQAQRVPVDRPGRGLSRDGMHMVIALPDLDGVALRRRSGDPVAPPIPLLPARVDYDSVVARAGDELGAHILLGLEERRGQPVAVDFGRHPHLLVLGDNECGKTAALRTLCREIVRTHTAARAQLLIVDFRHTLLDVIESEHMSGYVSSPAALGAKLSSLVDLLQARMPAPDVSQAQLRARSWWSGPDIYVVVDDYDLVAVSSGNPLMVLLEYLPHARDLGLHLVVARRSGGAARALFEPVLASLRDLGCRALLMSGRPDEGALFGSSRPMPLPPGRGILVTGAGDEQLVQVAWSPPP
Protein: Probable aquaporin PIP2-4 (Plasma membrane intrinsic protein 2.4) (AtPIP2;4) [Cleaved into: Probable aquaporin PIP2-4, N-terminally processed] (Q9FF53)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Probable aquaporin SIP1-2
- PAMP-induced secreted peptide 1
- Probable aquaporin SIP2-1
- NEP1-interacting protein 2
- Aquaporin SIP1-1
Sequence:
MAKDLDVNESGPPAARDYKDPPPAPFFDMEELRKWPLYRAVIAEFVATLLFLYVSILTVIGYKAQTDATAGGVDCGGVGILGIAWAFGGMIFVLVYCTAGISGGHINPAVTVGLFLARKVSLVRTVLYIVAQCLGAICGCGFVKAFQSSYYTRYGGGANELADGYNKGTGLGAEIIGTFVLVYTVFSATDPKRNARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIYNNEKAWDDQWIFWVGPMIGAAAAAFYHQFILRAAAIKALGSFGSFGSFRSFA
Protein: Ragulator complex protein LAMTOR4 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 4) [Cleaved into: Ragulator complex protein LAMTOR4, N-terminally processed] (Q0VGL1)
Organism: Homo sapiens (Human)
Function: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated.
Subcellular location: Lysosome {ECO:0000269|PubMed:22980980}.
Interaction partners:
- Ras-related GTP-binding protein B
- Ragulator complex protein LAMTOR3
- Ragulator complex protein LAMTOR2
- Neutral amino acid transporter 9
- Ragulator complex protein LAMTOR5
- Ras-related GTP-binding protein C
- Ragulator complex protein LAMTOR1
- Ras-related GTP-binding protein A
- Regulatory-associated protein of mTOR
- Ras-related GTP-binding protein D
Sequence:
MTSALTQGLERIPDQLGYLVLSEGAVLASSGDLENDEQAASAISELVSTACGFRLHRGMNVPFKRLSVVFGEHTLLVTVSGQRVFVVKRQNRGREPIDV
Protein: Alpha-mannosidase 2C1 (EC 3.2.1.24) (Alpha-D-mannoside mannohydrolase) (Mannosidase alpha class 2C member 1) (Neutral/cytosolic alpha-mannosidase) (Q91W89)
Organism: Mus musculus (Mouse)
Function: Cleaves alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues from glycoproteins. Involved in the degradation of free oligosaccharides in the cytoplasm.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16904268}.
Interaction partners:
- Lysosomal alpha-mannosidase
- Epididymis-specific alpha-mannosidase
- ER degradation-enhancing alpha-mannosidase-like protein 1
- Cytosolic endo-beta-N-acetylglucosaminidase
- Beta-mannosidase
- ER degradation-enhancing alpha-mannosidase-like protein 2
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Mannosyl-oligosaccharide glucosidase
Sequence:
MAAAPFLKHWRTTFERVEKFVSPIYFTDCNLRGRLFGDSCSVTLSSFLTPERLPYEKAVQQNFSPAQVGDSFGPTWWTCWFRVELVIPEVWVGQEVHLCWESDGESLVWRDGEPVQGLTKEGEKTSYVLSERLRASDPRSLTLYVEVACNGLLGAGKGSMIAAPDPEKMFQLSQAKLAVFHRDVHSLLVDLELLLGVAKGLGEDSQRSFQALHTANQMVNICDPAQPETYPAAKALASKFFGQHGGESQHTIHAMGHCHIDTAWLWPFKETVRKCARSWSTAVTLMEQNTDFIFACSQAQQLEWVKSQYPGLHARLQEFACRGQFVPVGGTWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMQGCGIKRFLTQKLSWNLVNSFPHHTFFWEGLDGSRVLVHFPPGDSYGMQGSVEEVLKTVTNNRDKGRTNHSGFLFGFGDGGGGPTQTMLDRLKRLSNTDGLPRVQLSSPGQLFTALERDSGQLCTWVGELFLELHNGTYTTHAQLKKGNRECEQILHDVEVLSSLALARSAQFLYPAAQLQHLWRLLLLNQFHDVVTGSCIQLVAEDAMNYYEDIRSHGNPLLSAAAAALCAGEPGPKGLLIINTLPWKRTEVLALPKPCGAHSLALVTVPSIGYAPAPTPTSLQPLLPQQPVFVMQETDGSVTLDNGIIRVRLDPTGCLTSLVLVASGREAIAEGALGNQFVLFDDVPLYWDAWDVMDYHLETRKPVLGQAGTLAVGTEGGLRGSAWFLLQISPNSRLSQEVVLDVGCPYVRFHTEVHWHEAHKFLKVEFPARIRSPQATYEIQFGHLQRPTHNNTSWDWARYEVWAHRWIDLSECDFGLALLNNCKYGASVRGNVLSLSLLRAPKAPDATADMGRHEFTYALMPHKGSFQEAGVIHAAYNLNFPLLALPAPGPAPDTTWSAFSVSSPAVVLETIKQAERCHQHRTLVLRLYEAHGSHVDCWLHTSLPVQEATLCDLLEQRDPTGHLSLQDNRLKLTFSPFQVRSLLLVLQSPPN
Protein: Fgr47p (A0A1D8PPN1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Endoplasmic reticulum chaperone BIP
Sequence:
MDHSKVPVFKRPTKLPTREELAAIFNPPKQRKLSSDSTPRIIEQSRVSLDLPSLTQTHQTQHSTTSSTKFISPPHLLPPNAAINNPILNSVPQNIIPIVHSPAIVSDFFSDITTDLTNEKLSNQINGILGKFPPPIPPENPTTTTTITTTTSNPQQTNTSEDFTLERGGMMVPFIYPPPPIINPNELPYSLASFKEKLDNLYYEQQQQLQQSQIKPSRGRPQGKKKLKTPDSSMTIKSPLSDITYNNTNDNQVYVEAPPLPFPPPNYMPYPLSSEKSTLTPSEVFGVFLEANSQLPRVDMVVASAAGSLFDMKSSAYKEGFNILDYELGKLNGNNNNNNNNNNNNMSGGNRGKLRQRTGLKGMDEEGTINDNETDDGQNREEQIIEEEEEREGEDEDSEEEEEEGEEGEEMGSEEGESEEEKQEIEQGEEIEDDETYFSKIDTKEYYDSYATINEDPTDTTTTTNKVEINMINPNFEKISSKLSNVKNKPTTIEQTDDKSSNEAIEDVYSYPEEAIGNLYRLDRNEFFPTNNNNNNKPNKEIAYISGLNHEKRRNELSKSIEVIEDFETRHLDDLFKVKKYHLLTRLKNLQSSKISFLNHTSSNMIKDDELLNIEQDLALERDLELLHLKLLENYELLKNSLNFYQNSHKIYNHLNYILINKLEKLKTFFEIQKNLFLEYIKKDDKDNDDDDDNGNSRNIFNINEKESNKLFIGISNHDYSNEIKDILKNLIVNDIQQSSNENNTPKNSDSNSNSNSNSIDSLELPELIKTPSSSNKLGGGGGGGGGERGGSLPPVLLHDFMPLITSQEFNLITGELNHKSLKNYVTTTNSTAASNPNHKKMLSNSIYEKMITSGSDTNLSDSGSNTTTTTTTTATSNIKGGKRRGGRRATTTTTSTNANTTTTTNPNDKSNNGISNGGGINGNVKENFDHKYSEATLLAKIMKQFSGPKMAKPDELNHDLELMGIKTKWPITK