wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein Eos (Ikaros family zinc finger protein 4) (Q9H2S9)
Organism: Homo sapiens (Human)
Function: DNA-binding protein that binds to the 5'GGGAATRCC-3' Ikaros-binding sequence. Transcriptional repressor. Interacts with SPI1 and MITF to repress transcription of the CTSK and ACP5 promoters via recruitment of corepressors SIN3A and CTBP2. May be involved in the development of central and peripheral nervous systems. Essential for the inhibitory function of regulatory T-cells (Treg). Mediates FOXP3-mediated gene silencing in regulatory T-cells (Treg) via recruitment of corepressor CTBP1 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12444977}.
Interaction partners:
- Forkhead box protein P3
- Zinc finger protein Aiolos
- DNA-binding protein Ikaros
- Zinc finger protein Pegasus
Sequence:
MHTPPALPRRFQGGGRVRTPGSHRQGKDNLERDPSGGCVPDFLPQAQDSNHFIMESLFCESSGDSSLEKEFLGAPVGPSVSTPNSQHSSPSRSLSANSIKVEMYSDEESSRLLGPDERLLEKDDSVIVEDSLSEPLGYCDGSGPEPHSPGGIRLPNGKLKCDVCGMVCIGPNVLMVHKRSHTGERPFHCNQCGASFTQKGNLLRHIKLHSGEKPFKCPFCNYACRRRDALTGHLRTHSVSSPTVGKPYKCNYCGRSYKQQSTLEEHKERCHNYLQSLSTEAQALAGQPGDEIRDLEMVPDSMLHSSSERPTFIDRLANSLTKRKRSTPQKFVGEKQMRFSLSDLPYDVNSGGYEKDVELVAHHSLEPGFGSSLAFVGAEHLRPLRLPPTNCISELTPVISSVYTQMQPLPGRLELPGSREAGEGPEDLADGGPLLYRPRGPLTDPGASPSNGCQDSTDTESNHEDRVAGVVSLPQGPPPQPPPTIVVGRHSPAYAKEDPKPQEGLLRGTPGPSKEVLRVVGESGEPVKAFKCEHCRILFLDHVMFTIHMGCHGFRDPFECNICGYHSQDRYEFSSHIVRGEHKVG
Protein: Interferon alpha-inducible protein 27-like protein 1 (Interferon-stimulated gene 12c protein) (ISG12(c)) (ISG12C) (Q96BM0)
Organism: Homo sapiens (Human)
Function: Plays a role in the apoptotic process and has a pro-apoptotic activity.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGKESGWDSGRAAVAAVVGGVVAVGTVLVALSAMGFTSVGIAASSIAAKMMSTAAIANGGGVAAGSLVAILQSVGAAGLSVTSKVIGGFAGTALGAWLGSPPSS
Protein: Tape measure protein pb2 precursor (TMP-pb2) (Pore-forming protein pb2) (Tail protein pb2) [Cleaved into: Tape measure protein pb2; Exolysin (EC 4.2.2.n1)] (Q6QGE7)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Fills the tail tube with its long coiled-coil domain and has pore-forming properties for host membrane penetration. Probable exolysin involved in host peptidoglycan digestion necessary for viral DNA entry into the host cell. Also functions as a tape measure protein that serves as a base for tail tube protein polymerization and acts as a template for tail length determination.
Subcellular location: [Tape measure protein pb2]: Virion {ECO:0000269|PubMed:18348984, ECO:0000269|PubMed:24198424, ECO:0000269|PubMed:36961893}. Note=Component of the tail (PubMed:18348984, PubMed:24198424, PubMed:36961893). Located in the lumen of the tail tube (PubMed:36961893). The C-terminus is located in the lumen of the baseplate, interacting with the base of the pb3 closed ring (PubMed:36961893). {ECO:0000269|PubMed:18348984, ECO:0000269|PubMed:24198424, ECO:0000269|PubMed:36961893}.; SUBCELLULAR LOCATION: [Exolysin]: Virion {ECO:0000269|PubMed:36961893}. Note=Component of the tail (PubMed:36961893). Located in the lumen of the tail tube (PubMed:36961893). The C-terminus is located in the lumen of the baseplate, interacting with the base of the pb3 closed ring (PubMed:36961893). {ECO:0000269|PubMed:36961893}.
Interaction partners:
Sequence:
MTDKLIRELLIDVKQKGATRTAKSIENVSDALENAAAASELTNEQLGKMPRTLYSIERAADRAAKSLTKMQASRGMAGITKSIDGIGDKLDYLAIQLIEVTDKLEIGFDGVSRSVKAMGNDVAAATEKVQDRLYDTNRALGGTSKGFNDTAGAAGRASRALGNTSGSARGATRDFAAMAKIGGRLPIMYAALASNVFVLQTAFESLKVGDQLNRLEQFGTIVGTMTGTPVQTLALSLQNATNGAISFEEAMRQASSASAYGFDSEQLEQFGLVARRAAAVLGVDMTDALNRVIKGVSKQEIELLDELGVTIRLNDAYENYVKQLNATSTGIKYTVDSLTTYQKQQAYANEVIAESTRRFGYLDDALKATSWEQFAANANSALRSLQQSAATYLNPVMDTLNTFLYQTKSSQMRVSAMARSASAKTTPAENVTALIENAVGAREDLDTYLKESEERVKKAQELKQQLDDLKAKQAATAPIANALTAGGIGGDESNKLVVQLTNELARQNKEIEERTKTEKVLRQAVQDTGEALLRNGKLAEQLGAKMKYADTAVPGDKGVFEVDPNNLKAVSEIQKNFDFLKKSSSDTANNIRMAASSITNAKKASSDLNSVVKAVEDTSKVTGQSADTLVKNLNLGFSSLDQMKAAQKGLSEYVTAMDKSEQNALEVAKRKDEVYNQTKDKAKAEAAAREVLLRQQQEQLTAAKALLAINPNDPEALKQVAKIETEILNTKAQGFENAKKTKDYTDKILGVDREIALLNDRTMTSTQYRLAQLRLELQLEQEKTELYSKQADGQAKVEQSRRAQAQISREIWEAEKQGTASHVSALMDALEVSQTQRNVTGQSQILTERLSILQQQLELSKGNTEEELKYRNEIYKTSAALEQLKKQRESQMQQQVGSSVGATYTPTTGLIGEDKDFADMQNRMASYDQAISKLSELNSEATAVAQSMGNLTNAMIQFSQGSLDTTSMIASGMQTVASMIQYSTSQQVSAIDQAIAAEQKRDGKSEASKAKLKKLEAEKLKIQQDAAKKQIIIQTAVAVMQAATAVPYPFSIPLMVAAGLAGALALAQASSASGMSSIADSGADTTQYLTLGERQKNVDVSMQASSGELSYLRGDKGIGNANSFVPRAEGGMMYPGVSYQMGEHGTEVVTPMVPMKATPNDQLSDGSKTTSGRPIILNISTMDAASFRDFASNNSTAFRDAVELALNENGTTLKSLGNS
Protein: Vacuolar proton translocating ATPase 100 kDa subunit (Clathrin-coated vesicle/synaptic vesicle proton pump 100 kDa subunit) (Vacuolar ATPase transmembrane subunit) (Q54E04)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase. Required in both the contractile vacuole system and the endosomal/lysosomal system. Also required for cytosolic pH regulation.
Subcellular location: Cytoplasmic vesicle membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Note=Found in membrane of contractile vacuole complex, an osmoregulatory organelle.
Interaction partners:
- V-type proton ATPase subunit d
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit E
- V-type proton ATPase subunit F
- V-ATPase proteolipid subunit C-like domain-containing protein
- V-type proton ATPase subunit B
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C
- V-type proton ATPase subunit H
- V-type proton ATPase catalytic subunit A
Sequence:
MSFLRPSIWRSSPMQMVQLFVQIEAAHDTVDELGKLGLIQFLDDNEHVNLFQRNFVNEVKRCDDMEKKLKFFEDQVKKEPKLQKLLPDNMLSVVDDDSQMDELEGRFDELESELKQVNANQETLQRNYNELIQLRHVLTKDSVFFQENPNLIEGEGHEHSARSPLLAEDQHVSEVAKQGVKLGFITGVMNTDKMPQFQRSLWRTTRGNNYVKDARIEEEIIDPQTGEETAKTVFIVFFQGERLQQKIKKICESFGANIYDCPDNSFERSNLLQKVTVRITDLYEVLQRSKDHKRQTLAGIVPRLYSWKKKVLLEKSIYHTMNLFDYDVGRKCLIAKGWTPKDKIEEIQLALRTATTRSGALVPSVLSIIKTEGSPPTHFETNKYTSSFQEIVNAYGIAHYREVNPAVLTIVTFPFLFGVMFGDVGHGALLLLSALGLISLEKKLAGKKLNELIQMPFDGRYVLFLMSLFSIYVGFIYNECFSIPMNIFGSQYNLNSTTGLYTYQHTDRVYPVGVDPLWKGAPNELVYYNSFKMKLSIIFGVVQMSVGICFSLLNYLNQKGPIKIVNILTQFVPQMIFLWSIFGYMSVLIILKWVVPYRSFEVDKVDPPFILPTIIAMFLSPGGTPDVVFFSGQGAVQTALLFLALISIPVMLVIKPLFMKRFHFQEVERKKLGHHEEEHDDEALYTGHHGEEFEMGEVFVHQVIHTIEFVLGAVSNTASYLRLWALSLAHSELSSVFWERILIGQVERGNPFLAFVGFGAWLGASVAVLLLMESLSAFLHALRLHWVEFQNKFYIGDGVRFIPYSATRILSEDDE
Protein: NADP-dependent mannitol dehydrogenase (MtDH) (EC 1.1.1.138) (Mannitol 2-dehydrogenase [NADP(+)]) (O93868)
Organism: Agaricus bisporus (White button mushroom)
Interaction partners:
Sequence:
MAPGFTISFVNKTIIVTGGNRGIGLAFTRAVAAAGANVAVIYRSAKDAVEVTEKVGKEFGVKTKAYQCDVSNTDIVTKTIQQIDADLGAISGLIANAGVSVVKPATELTHEDFKFVYDVNVFGVFNTCRAVAKLWLQKQQKGSIVVTSSMSSQIINQSSLNGSLTQVFYNSSKAACSNLVKGLAAEWASAGIRVNALSPGYVNTDQTAHMDKKIRDHQASNIPLNRFAQPEEMTGQAILLLSDHATYMTGGEYFIDGGQLIW
Protein: Eukaryotic translation initiation factor 2-alpha kinase gcn-2 (EC 2.7.11.1) (General control nonderepressible kinase 2) (D0Z5N4)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase which phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (eIF2alpha), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis (By similarity). Involved in the unfolded protein response (UPR) triggered by several stresses including mitochondrial, osmotic and oxidative stresses, amino acid deprivation and UV irradiation, probably by phosphorylating and inhibiting eIF2alpha. In addition, leads to the selective translation/transcription of some mRNA including atf-5, pha-4 and gpdh-1 which are part of the UPR. Required for maintaining lifespan during amino acid starvation. Involved in hypoxia-mediated adaptive protective response.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 1
- TOG domain-containing protein
- Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein
- Eukaryotic translation initiation factor 2-alpha kinase pek-1
- Transcription factor atf-4 homolog
- Protein skinhead-1
- Eukaryotic translation initiation factor 5
- Histidine--tRNA ligase
- Eukaryotic translation initiation factor 2 subunit 2
- BZIP domain-containing protein.
Sequence:
MTKENQIVLDERVKENQHLQEEEKLALDAVYLNQITYIKAHWHVWVPTNCHILLKALDSCFLNGDPLGKSKLSVILHVKCSEDYPQRKPAVDLLDPQGLSKEDVQNLLTILRQMADTWEGCVVIAELAHRVREFLTDHTPRPAGSFHDDMLANKVRTEAEKQRKRLDTEQKELELLEEEMRQRNAIEMEKTLNGTRQENETRIIGGRRIVVLSNMPNTQLLISEWTFRFSSNRNPAEGKRKDFAPFLQKLDAVYNEIQKLCEIKGLDQNLVEYAFVHLQKISVSPDQILIQLNVAQKIFSSEENMQDTYELIVQKSNLLRLLAAQAICGLRYLHEASMTHKHLTLGSVWTRNSTGDCVFRFSDFGSMGPLLDLVKMFGDICSGKYVARDEDKEKEYDRRRKDLFQLGTLLDGLILATRGSTYSRVPTPVEGNQNTGTNLLGNFIAKCQEAKNIDQLVEDPFLKEECQSESENIFTPFGGAMSPDGRMLADNVIIRVLGRGGFGDVVLVRNKMDSTDYAIKRIPLNAKSDKLNRKIAKEAKFFAKLNHPNMVRYYYAWAEDLIPIVEETSDDDSSLGAVPIPGKEKIGKKGKLKTGKSLEDKENKANLGGGDSLMPMNLRGLVKDHSIGVDAKEWSTPFGKPEGPKCASRMRQSKRSTPSGGLKHLSECSSDDEDDDDSSEIDWDAESEEVEDEESDDSDEEDEDDGERLVQLNTETSTGADSVFERSTADEDVVFTAESEDLNAKRRESIELMEINTTTTSKSKLAIDVVPVRKPRILCIQMEYCDRATLRQYIDENHCFNAPTEVWRIFSEVLCGLKYMHDMAMIHRDIKPLNIFLTSQNGVKIGDFGLATLEAMSSKGKIVGGAAEKSTSIEAMLSPNGVKSKGSDVHQTRDIGTQLYMAPELFVDELVHKAPYTSKIDIYSAGVVLFEMFYRPLPPSMDRVSTLNNLRDDIKIPSDFGAGLAAPMAGLARRTVEKMLQRNPDERPTADDLLNDEDLPMHTKEDATFRNLCEKVIKKRDGRMNAWLLDKQFKEEVPTSLNYCYDVDICLERAKYNNREVLVETLRAEFCKILKIHSFEKLHTHTLMPVSTALAAASVRTKPVEVLDRSGVPVALPMDLRQNFVRFCVRNSVQRMKRFNFGRVYSQTSANGHPHERWECCVDCIGPQCSSPSLEAELLLVACEMMIGSLPGMKFTLKIGHAQLIEAQIRHLKLSDDVRAELLDALHLISVSDRPHSHKEKMDMLTPKIGAKAANIITKLLIPVEDNFGAFKEKVACFRKKLKVDAARVLVDKAIRDLEEIVGTFKFCRTEAIEQISIVYDSQTCYRPRTFGDGLLFQIQVEKPSTIANNKRGRRQNVLAGGRYDSALLRERHPRDFVYEIPLCISGFGVAMDVVSQIRDSINKSANIPKTPQNHCKVLICSMVQPDGSNLITQKFELAKKLWSMGIEADVFHIPVDDLESLTEHRNRASITHILAVYNTLNEVICKTETSSETMDVDSAISSVWRGVQALDGQSIHMTPCGGGPISSISTPGEAHHHDDHHPGTPVIASKCFRSSVSTTVATTSIRPISATVANLNVILVTSADRFHKVMKEKKRVESQVRNHLTEFVAHFTSKTRIEVLVCDIPADVIKKIVSELTKTSSEAEIDKLFDQLIQKHGKVDLSPLRRQFHITLNGISTGSAQVAILFYRQSDNFYRYLV
Protein: UDP-glycosyltransferase 100 (UGTPg100) (EC 2.4.1.367) (A0A0K0PVW1)
Organism: Panax ginseng (Korean ginseng)
Function: Component of the dammarane-type triterpene saponins (e.g. PPT-type ginsenosides or panaxosides) biosynthetic pathway. Glycosyltransferase that catalyzes the biosynthesis of ginsenoside Rh1 from protopanaxatriol (PPT) and the conversion of ginsenoside F1 to ginsenoside Rg1.
Interaction partners:
Sequence:
MKSELIFLPVPAFGHLVGMVEMAKLFISRHENLSVTVLISKFFIDTGIDNYNKSLLAKPTPRLTIINLPEIDPQKYLLKPRCAIFPSLIENQKTHVRDVMSRMTQSESTRVVGLLADILFVDIFDIADEFNVPTYVYSPAGAGFLGLAFHLQTLNDDKKQDVTEFRNSDTELLVPSFANPVPAEFLPSIFLEKDGRHDVLLSLYWRCREAKGIIVNTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGEGQNSDEAAVILGWLDDQPPSSVVFLCFGSFGSFPENQVKEIAMGLERSGHRFLWSLRPCISEGETTLQLKYSNLELPAGFLDRTSCVGKVIGWAPQMAILAHEAVGGFVSHCGWNSVLESVWYGMPVATWPMYGEQQLNAFEMVKELGLAVEIEVDYRNEYNKSDFIVKADEIETKIKKLMMDGKNSKIRKKVKEMKEKSRVAMSENGSSYTSLAKLFEEIM
Protein: Ankyrin repeat domain-containing protein 7 (Q9D504)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKKFFPFRGKRKTDDSHSHSSEVPISLAKTAPPSLSIGGGYHLRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNGFTMYHHITANNENKKKTEQTAY
Protein: Ellipsoid body open, isoform C (X2J9Y4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Exportin-2
- Alsin homolog
- Nuclear pore complex protein Nup214
Sequence:
MHAASLTTVEGLLQEFYQPSTSNARKREIETNLLAFKSQPEAWQLCLRVATSSDTTENQFLWFFSTSTLEHTITRRWTQLTSTDKTLLRETLWNSYAQLVATPNVAKRHRDTLAQLIALLGKREFPEQDPNYMQHCMELTKTRFQLGINLLKITSEEVVSNRGDLTTEWKQYFYSCISMCVPDVLDLVTKYLLIAVCHINGKDIQTTIPNTLMDFSLTSALPNDNQLSSSILDLLGCVQHLVSWIRTELISEYFLMSILDLSQWRPAHEPISLAALSVLNELLYLQKPLPFPGPLMGGVTSLLEQHNNNRRQSEMYSDKFRELLRLYTTKYAAKLMQEPDLLETFLNLLYSCTTELHGALDFTEKLEIWTPIIKGIAQHPAKITRYNNVLTQLVDEIMRRTQFEANKPELEVLDNELMEDDTSATEWQQFLDQCFESLALLANTRGAHIVFAQVYNHWSRPQMYLLSLEHALDHGSARSYEAARKLKGANVGEILRDFATVCQAVVRLAPLMDSSTAAPGVADEMECQLQMLSDSLLQTLQLLASNRLYSGGSEMDKATFQTDLDNLYAQVLLAMRSIFPLTKAMSGEELLHRLFAILGSIFACNGSLTAASPIVQQAASELLLFISTVIRPKCLLDIPQIQSLLQAGSRLGAQLPRQVCINVHISLVSYMVLPWKSVPEQQQEYPRRLWMLREYVQGLAQNFLDLDLGQANESKVAATTLSLLGTFTALIEYFKATGGNAKDMLASTFKPILTKALMIFNNFGQSSIAMAITVAEFSLSMLRTLPTHLGAQFIKEMITLFISVSSREQLTLSRLAVMEKILQMFKLIVEQPGSASLGLLPSILDFSTQQILPLLQQQNAATDNSEITSLLYALFDSVLTCKWQFFYKNQLSNGHSGGGSGNFNCSDNLHPAHFMAILNAYGQMLVSGTDPSNVRSVLFSMQNVNERSRLYQRALFKEQLLASFQRALLNLLLSGEGSLHFDMIAQALYAMGQVDRRQLLESFVHASLPVAQTSLEEICQTNVLPFIVQDIPTFTQKLTQLMQDAHCVHLNETA
Protein: DNA-directed RNA polymerase II subunit RPB2 (RNA polymerase II subunit 2) (RNA polymerase II subunit B2) (EC 2.7.7.6) (DNA-directed RNA polymerase II 140 kDa polypeptide) (RNA polymerase II subunit B) (P08266)
Organism: Drosophila melanogaster (Fruit fly)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- Apoptosis inhibitor 5 homolog
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase II subunit RPB7
Sequence:
MMYDNEEELYEEENAEEISHELWQEACWIVINAYFDEKGLVRQQLDSFDEFIQMSVQRIVEDSPAIELQAEAQHTSGEVETPPRFSLKFEQIYLSKPTHWEKDGSPSPMMPNEARLRNLTYSAPLYVDITKTKNVEGLDPVETQHQKTFIGKIPIMLRSTYCLLSQLTDRDLTELNECPLDPGGYFIINGSEKVLIAQEKMATNTVYVFSMKDGKYAFKTEIRSCLEHSSRPTSTLWVNMMARGSQNIKKSAIGQRIIAILPYIKQEIPIMIVFRALGFVADRDILEHIIYDFDDPEMMEMVKPSLDEAFVVQEQNVALNFIGARGARPGVTKDKRIKYAKEILQKEMLPHVGVSDFCETKKAYFLGYMVHRLLLASLGRRELDDRDHYGNKRLDLAGPLLAFLFRGLFKNLMKEVRMYTQKFIDRGKDFNLELAIKTNIITDGLRYSLATGNWGDQKKAHQARAGVSQVLNRLTFASTLSHLRRVNSPIGRDGKLAKPRQLHNTLWGMLCPAETPEGAAVGLVKNLALMAYISVGSQPSPILEFLEEWSMENLEEIAPSAIADATKIFVNGCWVGIHRDPEQLMATLRKLRRQMDIIVSEVSMIRDIRDREIRIYTDAGRICRPLLIVENGSLLLKKTHVEMLKERDYNNYSWQVLVASGVVEYIDTLEEETVMIAMSPYDLKQDKDYAYCTTYTHCEIHPAMILGVCASIIPFPDHNQSPRNTYQSAMGKQAMGVYITNFHVRMDTLAHVLYYPMKPLVTTRSMEYLRFRELPAGINSIVAILCYTGYNQEDSVILNASAVERGFFRSVFYRSYKDSENKRVGDQEENFEKPHRGTCQGMRNAHYDKLDDDGIIAPGIRVSGDDVVIGKTITLPENDDELDSNTKRFSKRDASTFLRNSETGIVDQVMLTLNSEGYKFCKIRVRSVRIPQIGDKFASRHGQKGTCGIQYRQEDMAFTCEGLAPDIIINPHAIPSRMTIGHLIECLQGKLGSNKGEIGDATPFNDAVNVQKISTFLQEYGYHLRGNEVMYNGHTGRKINAQVFLGPTYYQRLKHMVDDKIHSRARGPVQILVRQPMEGRARDGGLRFGEMERDCQISHGAAQFLRERLFEVSDPYRVHICNFCGLIAIANLRNNTFECKGCKNKTQISQVRLPYAAKLLFQELMSMNIAPRLMVT
Protein: CDC42 small effector protein 1 (Q6TEL3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
Interaction partners:
- Rho guanine nucleotide exchange factor
- Homeobox protein engrailed-2a
Sequence:
MSAFWHKIGCCVVAKPPPKKKRRRIDRSMIGEPTNFVHLTHIGSGEMADGMQPSGPIKEQMRSKVPHANGRNSLL
Protein: Ceramide synthase BarA (Eurofung) (Q5B548)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Sphingolipid delta
- DAGKc domain-containing protein
- Sphinganine hydroxylase BasA
- Neutral ceramidase
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
- Alkaline phytoceramidase
- Cytochrome P450, putative
- Ceramide synthase LagA
Sequence:
MAKDTTLPAQSVTELNACVTTSSHRPVKDTTFREWVVSNQIGISLTTLSMLLAVHHLYPSLSPYTTPFFQLSYYQPSQGVYIQGWDDIYFVISSVFAFTAIRAIAMEWVFWPLARWSGLKRKASIRLAEQGWMWLYYAVFWTVGMYIWSQSDYWMDFKAIWAHWPARGVSGLMKWYLLAQLAFWVQQIFVINIEERRKDHYQMLTHHFITSCLLTSAYVYGFYNVSNVVLNLMDIVDLLLPTAKILKYLKFEMSCNIAFGVFMVVWAISRHIMYPLLCWSIFKDVPAVMPWGCYSGATGELISTNGYPDRVMHLFSPFLNIDGPICMNRTIKWIFLSSLLALQVLSIIWFSMVIRVAIGVLRTGNAEDTRSDSEEKDEEEVDPKSAANGNAIAAEVSSAEWRRNGPSSTRSRRSDRKALLGRIGCDTRT
Protein: F-box only protein 32 (Atrogin-1) (Muscle atrophy F-box protein) (MAFbx) (Q91Z62)
Organism: Rattus norvegicus (Rat)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins during skeletal muscle atrophy. Recognizes TERF1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q969P5}. Nucleus {ECO:0000250|UniProtKB:Q969P5}. Note=Shuttles between cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q969P5}.
Interaction partners:
- Cullin-1
- S-phase kinase-associated protein 1
- E3 ubiquitin-protein ligase TRIM63
- Myoblast determination protein 1
- Growth/differentiation factor 8
- Myogenin
- Forkhead box O3
- Eukaryotic translation initiation factor 3 subunit F
- Forkhead box protein O1
- Myosin-4
Sequence:
MPFLGQDWRSPGQSWVKTADGWKRFLDEKSGTFVSDLSSYCNKENLFNSLNYDVAAKKRKKDIQNSKTKTQYFHQEKWIYVHKGSTKERHGYCTLGEAFNRLDFSTAILDSRRFNYVVRLLELIAKSQLTSLSGIAQKNFMNILEKVVLKVLEDQQNIRLIRELLQTLYTSLCTLVQRVGKSVLVGNINMWVYRMETTLHWQQQLNSIQISRPAFKGLTITDLPVCLQLNIMQRLSDGRDLVSLGQAAPDLHVLSEDRLLWKRLCQYHFSERQIRKRLILSDKGQLDWKKMYFKLVRCYPRREQYGVTLQLCKHCHILSWKGTDHPCTANNPESCSVSLSPQDFINLFKF
Protein: Precursor of CEP13 (PCEP13) [Cleaved into: C-terminally encoded peptide 13 (CEP13)] (Q9FZ54)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signaling peptide that may regulate primary root growth rate and systemic nitrogen (N)-demand signaling.
Subcellular location: [C-terminally encoded peptide 13]: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:O80460}. Note=Accumulates in xylem sap. {ECO:0000250|UniProtKB:O80460}.
Interaction partners:
- Precursor of CEP15
- Precursor of CEP8
- Precursor of CEP4
- Precursor of CEP14
- Precursor of CEP7
- Precursor of CEP6
- Protein IDA-LIKE 5
- Precursor of CEP11
- AAA-type ATPase family protein
- Precursor of CEP9
Sequence:
MARPRISISMICLLILIVGFVLQSSQARKVLVPYGTSKGLFLSALPKGNVPPSGPSDKGHTSPPDDTDQRMVPENSPEIYRRLESVPSPGVGH
Protein: Leucine-rich repeat protein kinase family protein (F4I065)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MEKYFHGVLCVFIITVAFIHVVQAQDPNGFITLDCGLLPDGSPYTNPSTGLTFTSDSSFIESGKNGRVSKDSERNFEKAFVTLRYFPDGERNCYNLNVTQGTNYLIRAAFLYGNYDGLNTVPNFDLFIGPNKVTTVNFNATGGGVFVEIIHMSRSTPLDICLVKTGTTTPMISTLELRPLRSDTYISAIGSSLLLYFRGYLNDSGVVLRYPDDVNDRRWFPFSYKEWKIVTTTLNVNTSNGFDLPQGAMASAATRVNDNGTWEFPWSLEDSTTRFHIYLHFAELQTLLANETREFNVLLNGKVYYGPYSPKMLSIDTMSPQPDSTLTCKGGSCLLQLVKTTKSTLPPLINAIELFTVVEFPQSETNQDEVIAIKKIQLTYGLSRINWQGDPCVPEQFLWAGLKCSNINSSTPPTITFLNLSSSGLTGIISPSIQNLTHLQELDLSNNDLTGDVPEFLADIKSLLIINLSGNNFSGQLPQKLIDKKRLKLNVEGNPKLLCTKGPCGNKPGEGGHPKKSIIVPVVSSVALIAILIAALVLFLVLRKKNPSRSKENGRTSRSSEPPRITKKKKFTYVEVTEMTNNFRSVLGKGGFGMVYHGYVNGREQVAVKVLSHASKHGHKQFKAEVELLLRVHHKNLVSLVGYCEKGKELALVYEYMANGDLKEFFSGKRGDDVLRWETRLQIAVEAAQGLEYLHKGCRPPIVHRDVKTANILLDEHFQAKLADFGLSRSFLNEGESHVSTVVAGTIGYLDPEYYRTNWLTEKSDVYSFGVVLLEIITNQRVIERTREKPHIAEWVNLMITKGDIRKIVDPNLKGDYHSDSVWKFVELAMTCVNDSSATRPTMTQVVTELTECVTLENSRGGKSQNMGSTSSSEVTMTFDTEVNPVAR
Protein: Ubiquitin carboxyl-terminal hydrolase 19 (EC 3.4.19.12) (Deubiquitinating enzyme 19) (Ubiquitin thioesterase 19) (Ubiquitin-specific-processing protease 19) (Q3UJD6)
Organism: Mus musculus (Mouse)
Function: Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates (By similarity). Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing thier ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Exhibits a preference towards 'Lys-63'-linked ubiquitin chains (By similarity). Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase RNF123
- Baculoviral IAP repeat-containing protein 3
- E3 ubiquitin-protein ligase SIAH1A
- Baculoviral IAP repeat-containing protein 2
- E3 ubiquitin-protein ligase SIAH1B
- Hypoxia-inducible factor 1-alpha
- Ubiquitin carboxyl-terminal hydrolase 13
- Ubiquitin carboxyl-terminal hydrolase 7
- Ubiquitin carboxyl-terminal hydrolase 14
- Zinc finger-containing ubiquitin peptidase 1
Sequence:
MSAGASATGPRRGPPGLEEATSKKKQKDRANLESKDGDARRVSLPRKEPTKDELLLDWRQSADEVIVKLRVGTGPVRLEDVDAAFTDTDCVVRLPDGRQWGGVFFAEIQSSCTKVQARKGGLLQLVLPKKVPLLTWPSLLKPLGTQELVPGLQCQENGQELSPIALEPGSEPRRAKQEARNQKRAQGRGEVGSGAGPGTQAGPSAKRAVHLRRGPEGEGSMDGPGPQGDAPSFLSDSATQVEAEEKLCAPPMNTQTSLLSSEKSLALLTVEKTVSPRNDPVAPVMVQDRDPEPEQEDQVKEEMALGADPTALVEEPESMVNLAFVKNDSYEKGPDSVVVHVYVKEIRRDSSRVLFREQDFTLIFQTRDGNFLRLHPGCGPHTIFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEAPATRGAVGGAKVAVPTGPTPLDSTPPGGGPHPLTGQEEARAVEKEKPKARSEDSGLDGVVARTPLEHVAPKPDPHLASPKPTCMVPPMPHSPVSGDSVEEDEEEEKKVCLPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHQAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEVVAEEAWQRHKMRNDSFIVDLFQGQYKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKVLPIFYFAREPHSKPIKFLVSVSKENSSASEVLDSLSQSVHVKPENLRLAEVIKNRFHRVFLPSHSLDAVSPTDVLLCFELLSPELAKERVVVLEVQQRPQVPSIPISKCAACQRKQQSEEEKLKRCTRCYRVGYCNQFCQKTHWPDHKGLCRPENIGYPFLVSVPASRLTYARLAQLLEGYARYSVSVFQPPFQPGRMALESQSPGCTTLLSTSSLEAGDSEREPIQPSELQLVTPVAEGDTGAHRVWPPADRGPVPSTSGLSSEMLASGPIEGCPLLAGERVSRPEAAVPGYQHSSESVNTHTPQFFIYKIDASNREQRLEDKGETPLELGDDCSLALVWRNNERLQEFVLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRNLDLSKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSSQRSDVGWRLFDDSTVTTVDESQVVTRYAYVLFYRRRNSPVERPPRASHSEHHPDLGPAAEAAASQASRIWQELEAEEEMVPEGPGPLGPWGPQDWVGPPPRGPTTPDEGCLRYFVLGTVAALVALVLNVFYPLVSQSRWR