wanglab/gogpt-training-data huggingface dataset:
Protein: Glycerol-3-phosphate acyltransferase 4, isoform E (EC 2.3.1.15) (A0A0B4LHH1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MIAVLLDIFWIPIGGFLSFLIFISAINKSIGVRKAYVNLLLRIFEYGRVSIETASKENQHIQNPKTDDKQGVQLVDDADSKEGTNGATLITRDAVLLPQPQEPAPEKPVSSTKDEINFDFEKCLDYVKSGVEAIIEDDVTSRFEAEELKSWNMLTRTNRHYEFISWKITSIWVFGFFIRYVILMPLRVLVCFVGIGQRHGGFLGVLQRALARASPHIWFERGEAKDRHLVAERLKQHVSDPNNPPILIFPEGTCINNTSVMQFKKGSFEVGGVIYPVAIKYDPRFGDAFWNSAKYSMMQYLYMMMTSWAIVCDVWYLPPMYRQEGESAIDFANRVKSVIAKQGGLIDLVWDGQLKRMKPKKEWREIQQVEFANRLKSDST
Protein: V(D)J recombination-activating protein 2 (RAG-2) (P21784)
Organism: Mus musculus (Mouse)
Function: Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T-lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. DNA cleavage by the RAG complex occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. The chromatin structure plays an essential role in the V(D)J recombination reactions and the presence of histone H3 trimethylated at 'Lys-4' (H3K4me3) stimulates both the nicking and haipinning steps. The RAG complex also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. The introduction of DNA breaks by the RAG complex on one immunoglobulin allele induces ATM-dependent repositioning of the other allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. In the RAG complex, RAG2 is not the catalytic component but is required for all known catalytic activities mediated by RAG1. It probably acts as a sensor of chromatin state that recruits the RAG complex to H3K4me3.
Subcellular location: Nucleus.
Interaction partners:
- V
- Histone H3.1
- Histone H3.3
- Histone H3.2
- Cytokine receptor common subunit gamma
- T-cell surface glycoprotein CD4
- High mobility group protein B1
- DNA-dependent protein kinase catalytic subunit
- Fumarylacetoacetase
- Immunoglobulin lambda-like polypeptide 1
Sequence:
MSLQMVTVGHNIALIQPGFSLMNFDGQVFFFGQKGWPKRSCPTGVFHFDIKQNHLKLKPAIFSKDSCYLPPLRYPATCSYKGSIDSDKHQYIIHGGKTPNNELSDKIYIMSVACKNNKKVTFRCTEKDLVGDVPEPRYGHSIDVVYSRGKSMGVLFGGRSYMPSTQRTTEKWNSVADCLPHVFLIDFEFGCATSYILPELQDGLSFHVSIARNDTVYILGGHSLASNIRPANLYRIRVDLPLGTPAVNCTVLPGGISVSSAILTQTNNDEFVIVGGYQLENQKRMVCSLVSLGDNTIEISEMETPDWTSDIKHSKIWFGSNMGNGTIFLGIPGDNKQAMSEAFYFYTLRCSEEDLSEDQKIVSNSQTSTEDPGDSTPFEDSEEFCFSAEATSFDGDDEFDTYNEDDEDDESVTGYWITCCPTCDVDINTWVPFYSTELNKPAMIYCSHGDGHWVHAQCMDLEERTLIHLSEGSNKYYCNEHVQIARALQTPKRNPPLQKPPMKSLHKKGSGKVLTPAKKSFLRRLFD
Protein: Interferon-gamma receptor 1 (B6RLL0)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MAWVRMVHISLILVLSQQVDSYVPPPVNVSVICHNFHNVVYWNYSEPSLQPQFNVEMTRKYSGAALVCSNTSLYHCDVSSFTKVIEEGYRFILTAVGQNTNSSEISFTYDDTVYPDLVDVQCSLDFPPVNISAVSDQIIKVQFIHPFHIYKYAIIKNERPDHKEFDYMVVTEDHLKQHSFACSYKQHHVCEAEIPVDGKMDRHCIKMKGKMNNVHVSAHQNICIEGKHGDSGPSYTALYIVIPIAAMVVIAFIVWLIYSKLTSGSFPQPKILASILSHIGSVRSLMLPERAILSEVQTGGSPLLQTPTESLPDETLTVFSTPQEEVLRLPIGLKEGSGGEVMLPNEGSGSSLQVTRELGLKVKSNFAELSNYDCSHRLVIEEMSPARSA
Protein: Ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14) (CTP:phosphoethanolamine cytidylyltransferase) (Phosphorylethanolamine transferase) (P33412)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ethanolamine-phosphate cytidylyltransferase which catalyzes the second step of phosphatidylethanolamine biosynthesis. Involved in the maintenance of plasma membrane and required for proper sporulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Choline/ethanolaminephosphotransferase 1
- Ethanolamine kinase
- Cholinephosphotransferase 1
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Choline kinase
- Phosphatidylserine decarboxylase proenzyme 2
Sequence:
MTVNLDPDKVWIDGCFDFTHHGHAGAILQARRTVSKENGKLFCGVHTDEDIQHNKGTPVMNSSERYEHTRSNRWCSEVVEAAPYVTDPNWMDKYQCQYVVHGDDITIDANGEDCYKLVKEMGRFKVVKRTYGVSTTEIIHRILTKKSLPPTHPDYYPTTQELSFYSVAQDAVSKHCYVFQRDLDNVLVNGGYKFDAEDCVYVDGDFDLFHMGDIDQLRKLKMDLHPDKKLIVGITTSDYSSTIMTMKERVLSVLSCKYVDAVIIDADATSMSQYNCEKYHIGTAVLTAAGKFSEYLTKELIVKRVESQREVYIARNQKKGMSI
Protein: Ubiquitin carboxyl-terminal hydrolase isozyme L5 (UCH-L5) (EC 3.4.19.12) (Ubiquitin C-terminal hydrolase UCH37) (Ubiquitin thioesterase L5) (Q9XSJ0)
Organism: Bos taurus (Bovine)
Function: Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associates with the proteasome 19S subunit in the cytoplasm. Associates with the INO80 complex in the nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Proteasomal ubiquitin receptor ADRM1
- Ubiquitin carboxyl-terminal hydrolase 14
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory subunit 8
- Proteasome subunit alpha type-3
- 26S proteasome non-ATPase regulatory subunit 8
- Proteasome subunit alpha type-1
Sequence:
MTGNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLDTIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDAKTAAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQRQLAEEPMDTDQGSNMLSAIQSEVAKNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLKTLAEHQQLIPLVEKAKEKQNAKKAQETK
Protein: Lipoxygenase (EC 1.13.11.-) (A1XCI6)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
MIQMNMKQPLVLPAHRGNVIGSRLASSPSPVAAAAAAASRRRGVVSSPRSRLQRHMRLPRISCSATEEASGAVSAVTVEKMLTVTASVQAAPAIGQMYFQRALDDAGDFFGKTLLMELVSSEVDAKTGLEKPRVTAFAHKTLREGHYEAEFKVPASFGPVGAVLLENEHHKEIFIREIKLVTGSDSSTAVTFGCNSWVHSKFDNPEKRIFFTLKSYLPSDTPKGLEDLRKKDLQALRGDGHGERKASERVYDYDVYNDLGDPDKNPAHQRPVLGGSKRYPYPRRCRTGRPRTRKDPEAEVRHGHNYVPRDEQFSEVKQLTFGATTLRSGLHALLPAIRPMLIKRELRFPHFPAIDDLYSDGIPLPAQTGLGAIRSIVPRVVKLVEDTTEHVLRFELPDMIERDRFSWFKDEEFARQTIAGLNPLCIQLLTEFPIRSKLDREVYGPAESAITKEILEKHMSGGAAMTVEQALAAKRLFILDYHDVFLPYVHRVRELPDTTLYGSRTVFFLTDLGTLMPLAIELVRPKSPTQPQWKRVFTHGPDATDAWLWKLAKAHVVTHDTGYHQLVSHWLRTHCCVEPYIIAANRQLSRLHPVYRLLHPHFRYTMEINALAREALINADGIIEESFWPGRYAVELSSAAYGATWQFDTEALPNDLVKRGLAVRRDDGELELTIKDYPYAHDGLMVWNTIRQWAADYVNVYYKSDEAVAADPELKAFWDEVRNVGHGDKKDEPWWPVLDTRDSLAETLTTIMWVTSGHHSAVNFGQYHFGGYFPNRPTTIRKSMPVEEEAGRDEEMKKFLKQPETTLLDMLPTQMQAIRVMTTLDILSSHSPDEEYMGELAEPSWLEEPMVKAAFEKFGGRMKEIEGFIDECNNNPELRNRCGAGIVPYELLKPFSKPGVTGRGIPNSISI
Protein: Ferric reduction oxidase 4 (AtFRO4) (EC 1.16.1.7) (Ferric-chelate reductase 4) (Q8W110)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ferric chelate reductase. May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates. May function as root surface cupric chelate reductase and participate in the reduction of Cu(2+), for Cu(+) acquisition via Cu(+) transporters in response to copper deficiency.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Squamosa promoter-binding-like protein 7
- Copper transporter 2
- Copper transporter 1
- Metal-nicotianamine transporter YSL2
- Fe
- Acetyl-CoA:benzylalcohol acetyltranferase-like protein
- Metal transporter Nramp3
- Vacuolar iron transporter 1
- Nicotianamine synthase 1
- Copper transporter 6
Sequence:
MGNMRSLVKTLMVVLFLGWILVWIMISTNLFKSKWTPKLSKYLNTTYFGPQGTNLVLLTVPMMFIAVLSCVYLHIQKKPTQPQREWKLKRIMGRVIMVMNPLGIVTATELTFSLLFVALLAWSLYNYLYLSYHVHLHNDDNAKIWQAKFRAFGLRIGYVGNICWAFLFFPVTRASTILPLVGLTSESSIKYHIWLGHVSNFCFLVHTVVFLIYWAMINKLMETFAWNPTYVPNLAGTIAMVIGIAMWVTSLPSFRRKKFEIFFYTHHLYGLYIVFYVIHVGDSWFCMILPNIFLFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKIQWHPFTITSSSNLEKDTLSVVIRRQGSWTQKLYTHLSSSIDSLEVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELISQSQNKSTKLPDVLLVCSFKHYHDLAFLDLIFPLDMSASDISRLNLRIEAYITREDKKPETTDDHRLLQTKWFKPQPLDSPISPVLGPNNFLWLGVVILSSFVMFLLLIGIVTRYYIYPVDHNTGSIYNFSYRGLWDMFLGSACIFISSSVVFLWRKKQNKEGDKEFKNQVQSVEFQTPTSSPGSWFHGHERELESVPYQSIVQATSVHFGSKPNLKKILLEAEGSEDVGVMVCGPRKMRHEVAKICSSGLAKNLHFEAISFNW
Protein: Dual specificity protein phosphatase (EC 3.1.3.16) (EC 3.1.3.48) (Q7T2L8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- Sprouty homolog 4
- Interleukin-17 receptor D
- Fibroblast growth factor 8
- Protein sprouty homolog 2
- Mitogen-activated protein kinase
- Fibroblast growth factor receptor 1-A
- ETS translocation variant 4
Sequence:
MLDKFKPVQIDSVMAISKTVEWLKEQLETRRDCLLVMDCRAQELYESSHVETAINVAIPSLMLRRLKKGNLPIKSLLSNGEDRERFARRCKTDTIVLYDEYSREWNENIDGGSVLGLLLRRMKDEGYKAFYLEGGFSKFQTDFPAMCETNLDGSSSSSSPTSQVLGLGGLRISSDSSDIESDIDRDPSSATDSDGSPLSNPQPSFPVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTLGLKSPCDNRVPAPTQPLYFTTPTNHNVFQLDPLEST
Protein: Transcriptional regulator SarA (Staphylococcal accessory regulator A) (Q5HI51)
Organism: Staphylococcus aureus (strain COL)
Function: Global regulator with both positive and negative effects that controls the expression of several virulence factors and the biofilm formation process in a cell density-dependent manner.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MAITKINDCFELLSMVTYADKLKSLIKKEFSISFEEFAVLTYISENKEKEYYLKDIINHLNYKQPQVVKAVKILSQEDYFDKKRNEHDERTVLILVNAQQRKKIESLLSRVNKRITEANNEIEL
Protein: Uncharacterized protein (Q383L0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKRQRTASRGLLASARKTLYRQRWLVAAAAAFLLVGYLLHETQENSPFGPLIDAVADDAAFLSEALDAAKVDQKEENLAHFSRGMIQIGSTLEKVVGVAARNKAEPAVIMEPYINRAVAIYRSAVDFALQMLDPLLKREEQKQRENQPMWGVKGAVSYATTVVLPEYYFAIDDTTSHSATLVRGMQLLLQISNTLPIAETPSPPTNTTPKTLVDCRRHGTDLEWLQFCVSSFKNRTTLAIRRAAVLEELIALHPEYAPLRLHYAAAIALDRDVIQAHTVVTFITGEMEKSSKRAYPDPLHAAMLRLLKAFVLPFDSSPTPPSPSDLDSAAREALKGVDEIGNCSNLIRPFGAESNSSWNRRFRGVKRPDVMDKWQAKQLLKAMRMLKQRLQAGSEGSDILPAGFAECS
Protein: Neuropeptide Y receptor type 2 (NPY-Y2 receptor) (Q9ERC0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Peptide YY
- Pro-neuropeptide Y
- Pancreatic polypeptide prohormone
- Somatotropin
- Amelogenin, X isoform
Sequence:
MGPLGAEADENQTVEVKVELYGSGPTTPRGELPPDPEPELIDSTKLVEVQVVLILAYCSIILLGVVGNSLVIHVVIKFKSMRTVTNFFIANLAVADLLVNTLCLPFTLTYTLMGEWKMGPVLCHLVPYAQGLAVQVSTITLTVIALDRHRCIVYHLESKISKQISFLIIGLAWGVSALLASPLAIFREYSLIEIIPDFEIVACTEKWPGEEKSVYGTVYSLSTLLILYVLPLGIISFSYTRIWSKLKNHVSPGAASDHYHQRRHKTTKMLVCVVVVFAVSWLPLHAFQLAVDIDSHVLDLKEYKLIFTVFHIIAMCSTFANPLLYGWMNSNYRKAFLSAFRCEQRLDAIHSEVSMTFKAKKNLEVKKNNGLTDSFSEATNV
Protein: Exportin-1 (Exp1) (Chromosome region maintenance 1 protein homolog) (Q6P5F9)
Organism: Mus musculus (Mouse)
Function: Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase Ran in its active GTP-bound form. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm (By similarity). {ECO:0000250}.
Interaction partners:
- Snurportin-1
- Nuclear pore complex protein Nup214
- GTP-binding nuclear protein Ran
- Ran-specific GTPase-activating protein
- Nuclear pore complex protein Nup88
- Exportin-2
- E3 SUMO-protein ligase RanBP2
- 60S ribosomal export protein NMD3
- GTP-binding nuclear protein Ran
- GTP-binding nuclear protein Ran, testis-specific isoform
Sequence:
MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFDFSSGQITQVKAKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFETLFTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHGQLLEKRLNLREALMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDIPPRRQLYLTVLSKVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTEIIMTKKLQNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPAQFKLVLDSIIWAFKHTMRNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKISTPLNPGNPVNNQMFIQDYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLVQIKEFAGEDTSDLFLEERETALRQAQEEKHKLQMSVPGILNPHEIPEEMCD
Protein: Kelch repeat and BTB domain-containing protein 8 (A0A1B8YAB1)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification. The BCR(KBTBD8) complex acts by mediating monoubiquitination of target proteins (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NFY9}. Golgi apparatus {ECO:0000250|UniProtKB:Q8NFY9}. Note=Translocates to the spindle apparatus during mitosis. {ECO:0000250|UniProtKB:Q8NFY9}.
Interaction partners:
- Cullin-3
- Kelch-like protein 25
- Speckle-type POZ protein
- Kelch-like protein 40
- Kelch-like protein 22
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2
- Protein kinase, DNA-activated, catalytic subunit
Sequence:
MAQTPSSTASTEVAKYVQTQNGIPPSNPVSSAMDPYHACSILQQLKAMYDEGKLTDIVVQVDHGKHFSCHRNVLAAISPYFRSMFTSGLTESTQKEVRLVGIEAESMQLVLNYAYTSRVQLTEANVQALFTAASIFQIPSLQDQCAQYMISRLEPQNCIGVFSFADHYGHQELKEKAQDYIRKKFLYVTKEQEFLHLRKDQLISILNSDDLDVEKEEHVYDSIISWYEHEQETREMHLPEIFAKCIRMPLMEETFVEQIPPIFAQAMPINRVQKGKISANCCTRRLGMTASEMIICFEAANKHSGKKQTVPCLDTLTGKVYKLCKPPGDLREVGILVTPDNELYIAGGYRPSNNDVCIDHKAESDFWLYDHSSNRWLPKAPLLRARIGCKLVHCCGKLYAIGGRVYEGDGRNPLKSVECYDTRDNCWTAVSLMPVAMEFHSAVEYKDKIYILQGEVFLCYDPPRDYWCYLTPMTAPRVQGMAAVYKDSIYYVAGIRGNHRVLTVEAYDVEQNRWTRKKDLPCEQSSNPYIKLVVFKSKLHLFVRATQVSVEEFVFRTSRKNSLYQYDEIADSWKKVYETPERLWDLGRHFECAVAKLYPQCLQKVL
Protein: Actin-binding protein WASF1 (Protein WAVE-1) (Wiskott-Aldrich syndrome protein family member 1) (WASP family protein member 1) (Q0IIJ3)
Organism: Bos taurus (Bovine)
Function: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). Also involved in the regulation of mitochondrial dynamics (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q92558}. Synapse {ECO:0000250|UniProtKB:Q8R5H6}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q92558}. Note=Dot-like pattern in the cytoplasm. Concentrated in Rac-regulated membrane-ruffling areas. Partial translocation to focal adhesion sites might be mediated by interaction with SORBS2 (By similarity). In neurons, colocalizes with activated NTRK2 after BDNF addition in endocytic sites through the association with TMEM108 (By similarity). {ECO:0000250|UniProtKB:Q8R5H6, ECO:0000250|UniProtKB:Q92558}.
Interaction partners:
- Cytoplasmic FMR1-interacting protein
- NCK associated protein 1.
- Protein BRICK1
- Cytoplasmic FMR1-interacting protein
- NCK associated protein 1 like
- BAR/IMD domain-containing adapter protein 2
- Abl interactor 1
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 5
- Actin-binding protein WASF2
Sequence:
MPLVKRNIDPRHLCHTALPRGIKNELECVTNISLANIIRQLSSLSKYAEDIFGELFNEAHSFSFRVNSLQERVDRLSVSVTQLDPKEEELSLQDITMRKAFRSSTIQDQQLFDRKTLPIPLQETYDVCEQPPPLNILTPYRDDGKEGLKFYTNPSYFFDLWKEKMLQDTEDKRKEKRKQKQKNLDRPHEPEKVPRAPHDRRREWQKLAQGPELAEDDANLLHKHIEVANGPASHFETRPQTYVDHMDGSYSLSALPFSQMSELLTRAEERVLVRPHEPPPPPPMHGAGDAKPIPTCISSATGLIENRPQSPATGRTPVFVSPTPPPPPPPLPSALSTSSLRASMTSTPPPPVPPPPPPPTTALQAPAVPPPPAPLQIAPGVLHPAPPPIAPPLVQPSPPVARAAPVCETVPVHPLPQGEVQGLPPPPPPPPLPPPGIRPSSPVTVAALAHPPSGLHPTPSTAPGPHVPLMPPSPPSQVTPASEPKRHPSTLPVISDARSVLLEAIRKGIQLRKVEEQREQEAKHERIENDVATILSRRIAVEYSDSEDDSEFDEVDWLE
Protein: DhaL domain-containing protein (P95121)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MNGARGNSGVILSQILRGIAEVTATAAAASGAVLRAVDANALGAALWRGVELVVASMGGVEVPGTIVSVLRAAAGAVDQCAHEGLAGAVTAAGDAAVIALEKTPEQLDVLADAGAVDAGGRGLLVLLDALRSTICGQAPARAVYEPSPRALPTDTATQRPAPQFEVMYLLAVCDAAAADQLRDRLKELGESVAIAAAPPDSYSVHVHTDDAGAAVEAGLAVGRVSRIVISALGSGTSGLPAGGWTRGRAVLAVVDGDGAAELFAGEGACVLRPGPDAVTPAADISAHQLVRAVVDTGAAHVMVLPNGYVAAEELVAGCTAAIGWGVDVVPVPTGSMVQGLAALAVHDAARQAVDDGYSMARAAGASRHGSVRIATQKALTWAGTCKPGDGLGIAGDEVLIVADDVAAAAIGLVDLLLASGGDLVTVLIGAGVTEDVAVVLERHVHDHHPGTELVSYRTGHRGDALLIGVE
Protein: Peptidyl-alpha-hydroxyglycine alpha-amidating lyase 2 (EC 4.3.2.5) (Peptidylamidoglycolate lyase 2) (dPAL2) (Q9W1L5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Peptidyl-alpha-hydroxylglycine alpha-amidating lyase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Mediates the dismutation of the unstable peptidyl(2-hydroxyglycine) intermediate to glyoxylate and the corresponding desglycine peptide amide. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
Subcellular location: Secreted {ECO:0000305|PubMed:15198673}.
Interaction partners:
- Peptidylglycine alpha-hydroxylating monooxygenase
- Neuroendocrine protein 7B2
Sequence:
MSRLLFVALLAISLGYVASSSSNHLPAGLAMDLGPGVNLNERFFDQVRALIKRRLQEKGLAKPEQPELAMPLTDDDAVALQNQRSYDNVPLPAASVPTPVLVENWPTEQHSFGQVTAVAVDPQGSPVVFHRAERYWDVNTFNESNIYYLIEYGPIKENTIYVLDAKTGAIKSGWGSNMFYMPHGLTIDLHGNYWITDVAMHQAFKFKPFSNKPLLTIGKRFRPGSSVKHLCKPTSIAVATTGEFFIADGYCNSRILKFNAAGKLLRTIPQPPEFLSLQVPHAITLLEHLDLLCIADRENMRVVCPKAGLISSHGEGEPAATIQEPDLGRVFGVASFGDIVFAVNGPTSMLPVRGFTIDPRSETIIGHWGEFKNPHSMAVSVNGSALYVTEIGTNHQTNRVWKYVLA
Protein: Uncharacterized protein (Q54YD3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSTTNTNTANSSNNNNNNNNNQKQKQQQKPKNNDKGCCDPSVNQPKSKQKPIDNSKAKLNTPKVVDMAEDAKYVDSHVHVDQLLIRLNKSLTDFPQFKQDNFPKQFEKLIQVCCDPVSIEYADFLIENNECIYGAYGVHPHNAKEYNDQIEQKLIDRMKSNPKVVAWGEMGLDYFYNKSSNDEQINAFSRQLKQAVKLGKPLVIHSREAEEDTLRLLKELVPVDYKIHIHCFTSNSDFAKQLLDHFPNLCIGFTGCITFRNSQSIRDSVEAVPIERILLETDGPYMTPEPFRGQIAHSGHIPMVANAISQIKNIPLDQVLKQCRENTTKIYGI
Protein: Tagatose-6-phosphate ketose/aldose isomerase, putative (Mog1/PsbP/DUF1795-like photosystem II reaction center PsbP family protein) (F4K4A6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAILLHSLSLHPPNPKPQNPYKPKILSSSATFRRDVVLRTASLCFVSFIFQNQIPESLADPLKSTKPLRLGIANTKSWFQYFGSGFAIRVPPDFEDVNEPEDYSAGLSLYGDKAKPQTFAARFQTPDGSEVLSVVIRPSNQLKITFLEAKDISDLGSLKAAARLFVPGAATIYSARTIKVKEEEGLRNYYFYEFGRDEERIALVASVNRGKVYIAGAAAPESKWKDDELKLRSAAISFTIL
Protein: Guanylate-binding protein 1 (EC 3.6.1.-) (EC 3.6.5.-) (GTP-binding protein 1) (GBP-1) (mGBP-1) (mGBP1) (Guanine nucleotide-binding protein 1) (Interferon-gamma-inducible protein MAG-1) (Interferon-induced guanylate-binding protein 1) (Q01514)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions. Confers protection to several pathogens, including the bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma gondii. Promotes IFN-gamma-mediated host defense against bacterial infections by regulating bacteriolytic peptide generation through its interaction with ubiquitin-binding protein SQSTM1, which delivers monoubiquitylated proteins to autolysosomes for the generation of bacteriolytic peptides. Exhibits antiviral activity against influenza virus (By similarity).
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:18025219, ECO:0000269|PubMed:21551061}; Lipid-anchor {ECO:0000250|UniProtKB:P32455}; Cytoplasmic side {ECO:0000250|UniProtKB:P32455}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P32455}; Lipid-anchor {ECO:0000250|UniProtKB:P32455}; Cytoplasmic side {ECO:0000250|UniProtKB:P32455}. Cell membrane {ECO:0000250|UniProtKB:P32455}; Lipid-anchor {ECO:0000250|UniProtKB:P32455}; Cytoplasmic side {ECO:0000250|UniProtKB:P32455}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P32455}. Secreted {ECO:0000250|UniProtKB:P32455}. Note=Localizes to pathogen-containing vacuoles or to the cell surface of bacteria that escaped vacuoles. Secreted from endothelial cells in the cerebrospinal fluid, upon bacterial challenge and independently of IFNG induction. Golgi membrane localization requires isoprenylation and the presence of another IFNG-induced factor. Sequestered in the cytosol following phosphorylation by PIM1 and subsequent interaction with 14-3-3 protein sigma (SFN). {ECO:0000250|UniProtKB:P32455}.
Interaction partners:
- Guanylate-binding protein 2
- Guanylate-binding protein 5
- Sequestosome-1
- Signal transducer and activator of transcription 1
- Interferon-induced protein with tetratricopeptide repeats 2
- Antiviral innate immune response effector IFIT1
- Interferon-stimulated gene 20 kDa protein
- Interferon-induced protein with tetratricopeptide repeats 3
- 2'-5'-oligoadenylate synthase 2
- Interferon regulatory factor 1
Sequence:
MASEIHMSEPMCLIENTEAQLVINQEALRILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKRTGFSLGSTVQSHTKGIWMWCVPHPKKAGQTLVLLDTEGLEDVEKGDNQNDCWIFALAVLLSSTFIYNSIGTINQQAMDQLHYVTELTDLIKSKSSPDQSDVDNSANFVGFFPIFVWTLRDFSLDLEFDGESITPDEYLETSLALRKGTDENTKKFNMPRLCIRKFFPKRKCFIFDRPGDRKQLSKLEWIQEDQLNKEFVEQVAEFTSYIFSYSGVKTLSGGITVNGPRLKSLVQTYVSAICSGELPCMENAVLTLAQIENSAAVQKAITYYEEQMNQKIHMPTETLQELLDLHRTCEREAIEVFMKNSFKDVDQKFQEELGAQLEAKRDAFVKKNMDMSSAHCSDLLEGLFAHLEEEVKQGTFYKPGGYYLFLQRKQELEKKYIQTPGKGLQAEVMLRKYFESKEDLADTLLKMDQSLTEKEKQIEMERIKAEAAEAANRALAEMQKKHEMLMEQKEQSYQEHMKQLTEKMEQERKELMAEQQRIISLKLQEQERLLKQGFQNESLQLRQEIEKIKNMPPPRSCTIL