wanglab/gogpt-training-data huggingface dataset:
Protein: 3-oxosteroid 1-dehydrogenase (EC 1.3.99.4) (Steroid 1:2-dehydrogenase) (Q04616)
Organism: Rhodococcus opacus (Nocardia opaca)
Function: Catalyzes the elimination of the C-1 and C-2 hydrogen atoms of the A-ring from the polycyclic ring structure of 3-ketosteroids.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MQDWTSECDLLVVGSGGGALTGAYTAAAQGLTTIVLEKTDRFGGTSAYSGASIWLPGTQVQERAGLPDSTENARSYLRALLGDAESERQDAYVETAPAVVALLEQNPNIEFEFRAFPDYYKAEGRMDTGRSINPLDLDPADIGDLAGRCVRNCTKTDRMDHAPGRMIGGRALIAVSAAVQSTARQNFAPESVLTSLIVEDGRVVGGLRSNPRYRQRIKANRGVLMHAGGGFEGNAEMREQAGTPGKAIWSMGPSGPTPATRSPPELAGRRRNSLARSGVVLPRGRAARRRRLHGRVRGGLVVDSPGSVPQRVASVRPVRTSHGCSPDDNGSAVPSFMIFDSREVTDCPPSASRTRPPPSTSKPEPGSVPTLSKNSLPRPDYRPERIAQHCRKVQRCRKLGVDEEFHRGEDPYDAFFCPPNGGANAALTAIENGPFYAARDRLSDLGTKGGLVTDVNGRVLRADGSAIDGLYAAGNTSASVAPFYPGPGVPLGTAMVFSYRAAQDMAK
Protein: Aminopeptidase P1 (AtAPP1) (EC 3.4.11.9) (F4JQH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (By similarity). Aminopeptidase that binds to the auxin transport inhibitor N-1-naphthylphthalamic acid (NPA). May play a negative role in the regulation of PIN auxin transport proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11891249}. Cell membrane {ECO:0000269|PubMed:11891249}; Peripheral membrane protein {ECO:0000303|PubMed:11891249}. Microsome membrane {ECO:0000269|PubMed:11891249}; Peripheral membrane protein {ECO:0000303|PubMed:11891249}.
Interaction partners:
- F18B13.13 protein
- Inosine triphosphate pyrophosphatase
- Pentatricopeptide repeat
- Transcription factor bHLH148
Sequence:
MSEILSSLRSLMASHSPPLDALVVPSEDYHQSEYVSARDKRREFVSGFSGSAGLALITKKEARLWTDGRYFLQALQQLSDEWTLMRMGEDPLVEVWMSDNLPEEANIGVDSWCVSVDTANRWGKSFAKKNQKLITTTTDLVDEVWKSRPPSEMSPVVVHPLEFAGRSVSHKFEDLRAKLKQEGARGLVIAALDEVAWLYNIRGTDVAYCPVVHAFAILTTDSAFLYVDKKKVSDEANSYFNGLGVEVREYTDVISDVALLASDRLISSFASKTVQHEAAKDMEIDSDQPDRLWVDPASCCYALYSKLDAEKVLLQPSPISLSKALKNPVELEGIKNAHVRDGAAVVQYLVWLDNQMQELYGASGYFLEAEASKKKPSETSKLTEVTVSDKLESLRASKEHFRGLSFPTISSVGSNAAVIHYSPEPEACAEMDPDKIYLCDSGAQYLDGTTDITRTVHFGKPSAHEKECYTAVFKGHVALGNARFPKGTNGYTLDILARAPLWKYGLDYRHGTGHGVGSYLCVHEGPHQVSFRPSARNVPLQATMTVTDEPGYYEDGNFGIRLENVLVVNDAETEFNFGDKGYLQFEHITWAPYQVKLIDLDELTREEIDWLNTYHSKCKDILAPFMNQTEMEWLKKATEPVSVSA
Protein: Large ribosomal subunit protein uL11 (60S ribosomal protein L12) (P30050)
Organism: Homo sapiens (Human)
Function: Binds directly to 26S ribosomal RNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680}.
Interaction partners:
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL21
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL20
- Elongation factor 2
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL28
- Small ribosomal subunit protein eS27
Sequence:
MPPKFDPNEIKVVYLRCTGGEVGATSALAPKIGPLGLSPKKVGDDIAKATGDWKGLRITVKLTIQNRQAQIEVVPSASALIIKALKEPPRDRKKQKNIKHSGNITFDEIVNIARQMRHRSLARELSGTIKEILGTAQSVGCNVDGRHPHDIIDDINSGAVECPAS
Protein: Large ribosomal subunit protein uL4 (50S ribosomal protein L4) (P60723)
Organism: Escherichia coli (strain K12)
Function: One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Interaction partners:
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein bL21
- Small ribosomal subunit protein uS13
- Elongation factor Tu 1
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein bS6
- Small ribosomal subunit protein uS17
Sequence:
MELVLKDAQSALTVSETTFGRDFNEALVHQVVVAYAAGARQGTRAQKTRAEVTGSGKKPWRQKGTGRARSGSIKSPIWRSGGVTFAARPQDHSQKVNKKMYRGALKSILSELVRQDRLIVVEKFSVEAPKTKLLAQKLKDMALEDVLIITGELDENLFLAARNLHKVDVRDATGIDPVSLIAFDKVVMTADAVKQVEEMLA
Protein: Actin cortical patch protein Sur7, putative (AFU_orthologue AFUA_2G02310) (C8V7S3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MPASRAVLGLLGLFFTAGALLLMWLVFLAGVRNTTPLDNIYFLQVDTSNIPGAPTLSRWTWWNLCAVEDGKSQCGSSHPDFPFDPPSHRNFGTEVNIPSAFIGTNHYFLTSRFSWPFEILALFFGVLSLFTGLLAMCTRIGSYISALMAWLALTFHIIVTCLVTAVFVQGRNKFNGNDQSARLGVKAFAFLWTSVACWMLACLMYCMGGTVGRKDRGYSGRKQRRRGFFTARQPSQERNKEIAP
Protein: 2-acylglycerol O-acyltransferase 2 (EC 2.3.1.20) (EC 2.3.1.22) (Acyl-CoA:monoacylglycerol acyltransferase 2) (MGAT2) (hMGAT2) (Diacylglycerol O-acyltransferase candidate 5) (hDC5) (Diacylglycerol acyltransferase 2-like protein 5) (Monoacylglycerol O-acyltransferase 2) (Q3SYC2)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of diacylglycerol from 2-monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity. Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12621063, ECO:0000269|PubMed:27184406}; Multi-pass membrane protein {ECO:0000269|PubMed:12621063}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27184406}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Phospholipid phosphatase 5
- Phospholipid phosphatase 4
- Monoglyceride lipase
- Lipoprotein lipase
- 2-acylglycerol O-acyltransferase 3
- Diacylglycerol O-acyltransferase 2
- 2-acylglycerol O-acyltransferase 1
- Acylglycerol kinase, mitochondrial
- Phosphatidate phosphatase LPIN2
Sequence:
MVEFAPLFMPWERRLQTLAVLQFVFSFLALAEICTVGFIALLFTRFWLLTVLYAAWWYLDRDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFANLCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNLLGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSGSWLRYIQNRLQKIMGISLPLFHGRGVFQYSFGLIPYRRPITTVVGKPIEVQKTLHPSEEEVNQLHQRYIKELCNLFEAHKLKFNIPADQHLEFC
Protein: Dwarfin sma-2 (MAD protein homolog 1) (Q02330)
Organism: Caenorhabditis elegans
Function: Involved in TGF-beta pathway. Plays a role in male tail tip morphogenesis.
Subcellular location: Cytoplasm. Nucleus {ECO:0000305}.
Interaction partners:
- Dwarfin sma-4
- Dwarfin sma.
- Serine/threonine-protein kinase receptor sma-6
- Mitogen-activated protein kinase mpk-1
- Dwarfin sma-3
- Protein dbl-1
- Smad-related protein daf-14
- TGF-beta family profile domain-containing protein
- Ubiquitin carboxyl-terminal hydrolase
- Ski protein homolog
Sequence:
MINFDGIKKITERLKWKQGDEDENWAKKAIDNLMKKLIKHNKQALENLEFALRCQGQQKTECVTIPRSLDGRLQISHRKALPHVIYCRVYRWPDLQSHHELKAIEDCRFCYESGQKDICINPYHYKRVHATGVLPPVLVPRYSEKPPQEVPPTLAKFQLMEMSGSRMPQNVNMANVNFTANQFHQYNPNGIEEMDTSQKFDIPPGVPTCLVPFDKVWEEQFWATVSYYELNTRVGEQVKVSSTTITIDGFTDPCINGSKISLGLFSNVNRNATIENTRRHIGNGVKLTYVRSNGSLFAQCESDSAIFVQSSNCNYINGFHSTTVVKIANKCSLKIFDMEIFRQLLEDCSRRGFDASFDLQKMTFIRMSFVKGWGAEYQRQDVTSTPCWIEIHLHAPLAWLDRVLSTMGPTPRPISSIS
Protein: F-BAR domain only protein 1 (O14526)
Organism: Homo sapiens (Human)
Function: Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. May regulate Bmp signaling by regulating clathrin-mediated endocytosis of Bmp receptors. Involved in the regulation of T-cell poliferation and activation. Affects TCR clustering upon receptor triggering and modulates its internalisation, playing a role in TCR-dependent T-cell activation.
Subcellular location: Membrane, clathrin-coated pit {ECO:0000305|PubMed:17617719, ECO:0000305|PubMed:20448150, ECO:0000305|PubMed:32098969}; Peripheral membrane protein {ECO:0000305|PubMed:17617719, ECO:0000305|PubMed:20448150}; Cytoplasmic side {ECO:0000305|PubMed:17617719, ECO:0000305|PubMed:20448150}. Note=Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2. According to PubMed:17617719 it may also dynamically associate with Golgi/TGN membranes.
Interaction partners:
- Intersectin-1
- Epidermal growth factor receptor substrate 15
- Intersectin-2
- Cdc42-interacting protein 4
- Epidermal growth factor receptor substrate 15-like 1
- Epsin-2
- Adaptin ear-binding coat-associated protein 1
- Clathrin coat assembly protein AP180
- Huntingtin-interacting protein 1-related protein
- F-BAR domain only protein 2
Sequence:
MSYFGEHFWGEKNHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMDKAETKTKKAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLLRKFAESKGTGREKPGPLDFEAYSAAALQEAMKRLRGAKAFRLPGLSRREREPEPPAAVDFLEPDSGTCPEVDEEGFTVRPDVTQNSTAEPSRFSSSDSDFDDEEPRKFYVHIKPAPARAPACSPEAAAAQLRATAGSLILPPGPGGTMKRHSSRDAAGKPQRPRSAPRTSSCAERLQSEEQVSKNLFGPPLESAFDHEDFTGSSSLGFTSSPSPFSSSSPENVEDSGLDSPSHAAPGPSPDSWVPRPGTPQSPPSCRAPPPEARGIRAPPLPDSPQPLASSPGPWGLEALAGGDLMPAPADPTAREGLAAPPRRLRSRKVSCPLTRSNGDLSRSLSPSPLGSSAASTALERPSFLSQTGHGVSRGPSPVVLGSQDALPIATAFTEYVHAYFRGHSPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDPETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPGATAVPTPLTNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEAGGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGVDLELVGSGYRMSLVKRRFATGMYLVSC
Protein: RuvB-like helicase (EC 3.6.4.12) (Q8ID85)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Zinc finger protein, putative
- Actin-related protein, putative
- Probable ATP-dependent helicase PF08_0048
- RuvB-like helicase
- RuvB-like helicase
- DNA methyltransferase 1-associated protein 1, putative
- SNF2 helicase, putative
- YL1 nuclear protein, putative
- Nucleolar protein 5, putative
- PIH1 domain-containing protein, putative
Sequence:
MKLEEVKDIQKIERIGAHSHIRGLGLNDCLDARYCSEGMIGQMSARKAAGIVLRMIKEGRISGRAILLAGQPGTGKTAIAMGIAKALGEDTPFTHISGSEVYSLEMSKTEALTQAFRRSIGVRVKEESEVIEGEVVEIEIEKFNERDINNKNKKLGKMILKTTEMETLYDLGSKMIEALQKENITAGDVICIDKGTGKITKIGKSFARSKDYDAMDPNTLFVQCPEGELQKRKEVVHTVTLHDIDAINSRTQGFLALFSGDTGEIKNEIREHIDMKINEWQEDEKAEIVPGVLFIDEVHMLDIECFSYLNRALESEQSPIVIMATNRGITHIRGTDYKAPHGIPLDLLDRTLIIPTYPYKHQDILKILEQRAEEEDVDIDEYAKELLCKIASESSLRYALHLITLANLVSKKRKATEVTVQDVRRVYNLFIDVKRSTQYLIEYQNEFMFSELPKEELSVKEEDSSEEKRELHEKNSENSSTSN
Protein: Succinate dehydrogenase assembly factor 4, mitochondrial (SDH assembly factor 4) (SDHAF4) (Starvation-upregulated protein) (Q9VLU6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Binds to the flavoprotein subunit SdhA in its FAD-bound form, blocking the generation of excess reactive oxigen species (ROS) and facilitating its assembly with the iron-sulfur protein subunit SdhB into the SDH catalytic dimer (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P38345}.
Interaction partners:
- Succinate dehydrogenase assembly factor 3, mitochondrial
Sequence:
MQSVTRQTARVLPQMGKQVSYLSTSGAWRATASGGDMVVEIKEPKTRTEKLMAFQKKLRAKTPLGKLDEFSRHPYQEKEPLKPWPNQTNPYTGEIGGPAGPEPTRYGDWERKGRVSDF
Protein: Ras-related protein Rab-34 (EC 3.6.5.2) (Ras-related homolog) (Ras-related protein Rab-39) (Ras-related protein Rah) (Q64008)
Organism: Mus musculus (Mouse)
Function: Transport protein involved in the redistribution of lysosomes to the peri-Golgi region. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis (By similarity). Plays a role in the fusion of phagosomes with lysosomes (By similarity). Acts also as a positive regulator of hedgehog signaling and regulates ciliary function.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12475955}. Golgi apparatus {ECO:0000269|PubMed:12475955, ECO:0000269|PubMed:33989524}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q9BZG1}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9BZG1}; Lipid-anchor {ECO:0000250|UniProtKB:Q9BZG1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9BZG1}. Cell projection, cilium {ECO:0000269|PubMed:29290584, ECO:0000269|PubMed:30301781, ECO:0000269|PubMed:33989524}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9BZG1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:33989524}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250|UniProtKB:Q9BZG1}.
Interaction partners:
- Rab-interacting lysosomal protein
Sequence:
MNILAPVRRDRVLAELPQCLKKEAALHVRKDFHPRVTCACQEHRTGTVGFKISKVIVVGDLSVGKTCLINRFCKDTFDKNYKATIGVDFEMERFEVLGVPFSLQLWDTAGQERFKCIASTYYRGAQAIIIVFNLNDVASLEHTKQWLTDALKENDPSNVLLFLVGSKKDLSTPAQYSLMEKDALKVAQEIKAEYWAVSSLTGENVREFFFRVAALTFEANVLADVEKSGARHIADVVRINSDDKNLYLTASKKKATCCP
Protein: Pseudin-1 (P83188)
Organism: Pseudis paradoxa (Paradoxical frog)
Function: Possesses antifungal activity against C.albicans and is also active against E.coli and S.aureus.
Subcellular location: Secreted {ECO:0000269|PubMed:11689009}.
Interaction partners:
Sequence:
GLNTLKKVFQGLHEAIKLINNHVQ
Protein: Fms related receptor tyrosine kinase 3 ligand (A0A8I6A9D9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
QCWRQPGAQILLHPASPRESWSPRSHGASKASAQAAVAPAATASHSGAAGSRLVPSLAKDKKEGGAPPWGAPPLPSLGCETCASLTQPGSSLEDTEAKPESSDRRFAQPGHRD
Protein: Uncharacterized protein (Q57V96)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLTSTAYGMELQARAIAPFYHSSNNSSSTHRFVAGTACFAGGNVIRLLTFQEESQLLECTATWSHEEEIFGLWSSPSVAGPSLLAVGASSYCRIFRVSDDVSGELEPVVNFNAAAAQVLWDLEGLQNEVKLISEDSLRIYSLTEGKMGEEIGRFRVDGCAELRCAALDPHHSSVCLAAGEGIGIAVIDTRRKGPIVMPNTTTLHGLGMIQSIDFSNAREGLFMTAGTDGVIMWHDFRMDGEKSVVERRGYLDAHDHCVQRSLFNPFHDELLISCGSDHTLKLWDTSKKGADGECAVCVSKLSDFAESVVACCWSNSNPWVFAGLSYNGRVLVDSVPEECKMQFIGKEG
Protein: Diphthine methyltransferase (EC 3.1.1.97) (Diphthamide biosynthesis protein 7) (WD repeat-containing protein 85) (Q9BTV6)
Organism: Homo sapiens (Human)
Function: Catalyzes the demethylation of diphthine methyl ester to form diphthine, an intermediate diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta).
Interaction partners:
- Elongation factor 2
- 2-
- 2-
- Diphthine methyl ester synthase
- Diphthine--ammonia ligase
- Diphthamide biosynthesis protein 3
- DnaJ homolog subfamily C member 24
Sequence:
MMGCFALQTVDTELTADSVEWCPLQGCRHLLACGTYQLRRPEDRPAGPQNKGGMEVKEPQVRLGRLFLYSFNDNNSIHPLVEVQRKDTSAILDMKWCHIPVAGHALLGLADASGSIQLLRLVESEKSHVLEPLSSLALEEQCLALSLDWSTGKTGRAGDQPLKIISSDSTGQLHLLMVNETRPRLQKVASWQAHQFEAWIAAFNYWHPEIVYSGGDDGLLRGWDTRVPGKFLFTSKRHTMGVCSIQSSPHREHILATGSYDEHILLWDTRNMKQPLADTPVQGGVWRIKWHPFHHHLLLAACMHSGFKILNCQKAMEERQEATVLTSHTLPDSLVYGADWSWLLFRSLQRAPSWSFPSNLGTKTADLKGASELPTPCHECREDNDGEGHARPQSGMKPLTEGMRKNGTWLQATAATTRDCGVNPEEADSAFSLLATCSFYDHALHLWEWEGN
Protein: NLR family, pyrin domain containing 4G (Q66JP4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MASFISDFGLMWYLKELNKKEFIKFKEFLIQEILKLKLKQISWTEVKKASREDLANLLLKCYEENQAWDMTFNILQKINRKDLTERATEEIADVVDSSPLGLTDSGNPKLYRDHLKKKLTHDCSKKFNVRIQDFIKEIFIQNDCDTFENLLISKGTEKKPHMVFLQGMAGIGKTMMLKNLMLAWSKGLVFQNKFSYTFYFCCRDVKQLKTASLAELISREWPSPSAPIEEILSQPEKLLFIIDSLEGMECDLTKQESELCDNCMEKQPVSILLSSLLTRKMLPESSFLLSTTPETFEKMEDRILCTDVKTATAFDERSIKIYFHRLFQDKIRAQEAFSLVRENEQLFTICQVPLLCWMVATCLKEEIEKGGDPVSVCRHITSLYTTHILNLFIPQSAQYPSKKSQDQLQGLCSLAAEGMWTDTFVFGEEALRRNGILDSDIPTLLDIGMLGKIREFENYYIFLHPSVQEVCAAIFYLLKSHVDHPSQDVKSIETVLFMFLKKVKTQWIFLGCFIFGLLQKSEQEKLVVFFGRRLSQKIQHKLYQCLETISGNAELQEQIDGMKLFCCLSEIEDEAFLVKVMNCMQQINFVAKNYSDLILAAYCLKHCSTLKKLSFSTQNVLNEKGNQRCMKKLIICWNDMCSVFVRSKDIQVLQIKDTSFNEPAIRILYEYLKYPSFTLNKLVANNVHFFGDNHAFFELIQNCSLQYLDLGCSFLTHSEVKLLCDVLNQAECNIEKLV
Protein: Beta-1,3-N-acetylglucosaminyltransferase radical fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase) (Q9R1U9)
Organism: Rattus norvegicus (Rat)
Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in enhancement of NOTCH1 activation by DLL1 and JAG1 (By similarity). Inhibits Notch signaling in postmitotic neurons of the brain. It may play a role in adult brain and in neurogenesis. It may play a role in limb development (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 1
- Notch homolog 4, isoform CRA_b.
- O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
- Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe
Sequence:
MSRVRRVLCRACLALAAVLAVLLLLPLPLPLPLPLPRAPAPDPGRVPTGSLTLEVSRLQPDDVFIAVKTTRKNHGPRLRLLLRTWISRAPRQTFIFTDGDDPELQLLAGSQMINTNCSAVRTRQALCCKMSVEYDKFIESGRKWFCHVDDDNYVNPKSLLHLLSTFSSNQDIYLGRPSLDHPIEATERVQGGGTSNTVKFWFATGGAGFCLSRGLALKMSPWASLGSFMSTAERVRLPDDCTVGYIVEGLLGARLLHSPLFHSHLENLQKLPSGAVLQQVTLSYGGPENPHNVVNVAGSFSIRQDPTRFQSVHCLLYPDTHWCPMKNRGKEAFQ
Protein: Homeobox protein Nkx-3.2 (Bagpipe homeobox protein homolog 1) (Homeobox protein NK-3 homolog B) (P78367)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor that acts as a negative regulator of chondrocyte maturation. PLays a role in distal stomach development; required for proper antral-pyloric morphogenesis and development of antral-type epithelium. In concert with GSC, defines the structural components of the middle ear; required for tympanic ring and gonium development and in the regulation of the width of the malleus (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Runt-related transcription factor 2
- Transcription factor 21
- Heart- and neural crest derivatives-expressed protein 2
- Mothers against decapentaplegic homolog 4
Sequence:
MAVRGANTLTSFSIQAILNKKEERGGLAAPEGRPAPGGTAASVAAAPAVCCWRLFGERDAGALGGAEDSLLASPAGTRTAAGRTAESPEGWDSDSALSEENESRRRCADARGASGAGLAGGSLSLGQPVCELAASKDLEEEAAGRSDSEMSASVSGDRSPRTEDDGVGPRGAHVSALCSGAGGGGGSGPAGVAEEEEEPAAPKPRKKRSRAAFSHAQVFELERRFNHQRYLSGPERADLAASLKLTETQVKIWFQNRRYKTKRRQMAADLLASAPAAKKVAVKVLVRDDQRQYLPGEVLRPPSLLPLQPSYYYPYYCLPGWALSTCAAAAGTQ
Protein: Activity-regulated cytoskeleton associated protein 2 (dArc2) (Q7JV70)
Organism: Drosophila melanogaster (Fruit fly)
Function: Self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer. Arc2 protein is released from cells in extracellular vesicles that mediate the transfer of mRNA into neighboring cells.
Subcellular location: Extracellular vesicle membrane {ECO:0000269|PubMed:29328915}. Note=Forms virion-like extracellular vesicles. {ECO:0000269|PubMed:29328915}.
Interaction partners:
- Activity-regulated cytoskeleton associated protein 1
Sequence:
MTQMSDEQFRIFIETIKSLGPIKEEPPSKGSFSNCTVRFSGQRDHDAVDEFINAVETYKEVEGISDKDALKGLPLLFKSIAVVWWKGVRRDAKTWSDALQLLRDHFSPTKPSYQIYMEIFETKQSYDEVIDSFICKQRALLAKLPEGRHDEETELDFIYGLMQPKYRESIPRHEVKTFRELLDRGRTVERTRH
Protein: E4-ORF1 (EC 3.6.1.23) (Early E4 14.0 kDa protein) (ORF1) (Probable dUTPase E4 ORF1) (P89079)
Organism: Human adenovirus D serotype 9 (HAdV-9) (Human adenovirus 9)
Function: Plays a key role in virus oncogenecity in animals. Binds and sequesters human MUPP1/MPDZ protein in the cytoplasm, preventing it from playing a role in cellular proliferation regulation. Induces cell transformation, probably by inactivating MPDZ protein.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:9151828}.
Interaction partners:
Sequence:
MAESLYAFIDSPGGIAPVQEGTSNRYTFFCPESFHIPPHGVVLLHLKVSVLVPTGYQGRFMALNDYHARDILTQSDVIFAGRRQELTVLLFNHTDRFLYVRKGHPVGTLLLERVIFPSVKIATLV
Protein: Insulin-like growth factor-binding protein 1 (A4K8J2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Insulin-like growth factor 2a.
- Insulin-like growth factor 2
- Insulin-like growth factor-binding protein 6
Sequence:
MRAVCVCVLLVCVLVCVLDASPVPAPEPIRCAPCSADQLSACPAVSPGCAEVVRDPGCGCCSSCALRSGDSCGVHTANCGAGLRCVPRAGDPRPLHSLTRGHAVCVEHHPTEEDTELTSEPGSLHHLLSLNRALDPRDTAEAQESIKSQLNAIRQKLIQQGPCHTELLASLDVITESQQALGEKFTSFYLPNCDKHGFYKAKQCVSSLVAQAPRCWCVSSWNGKRLAGTADVEADTPCPQELTH
Protein: Insulin-like growth factor-binding protein 3 (IBP-3) (IGF-binding protein 3) (IGFBP-3) (P47878)
Organism: Mus musculus (Mouse)
Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R. Promotes testicular germ cell apoptosis.
Subcellular location: Secreted.
Interaction partners:
- Insulin-like growth factor 1
- Insulin-like growth factor 2
- Insulin-like growth factor-binding protein complex acid labile subunit
- Epidermal growth factor receptor
- Insulin-2
- Insulin-1
- Insulin-like growth factor-binding protein 3 receptor
- Insulin-like growth factor-binding protein 5
- Fibronectin
- Insulin-like growth factor 1 receptor
Sequence:
MHPARPALWAAALTALTLLRGPPVARAGAGAVGAGPVVRCEPCDARALSQCAPPPTAPACTELVREPGCGCCLTCALREGDACGVYTERCGTGLRCQPRPAEQYPLRALLNGRGFCANASAAGSLSTYLPSQPAPGNISESEEEHNAGSVESQVVPSTHRVTDSKFHPLHAKMDVIKKGHARDSQRYKVDYESQSTDTQNFSSESKRETEYGPCRREMEDTLNHLKFLNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYDTKGKDDVHCLSVQSQ
Protein: Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.24) (F4J8C7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514, ECO:0000256|RuleBase:RU365032}.
Interaction partners:
Sequence:
MEMEEGASGVGEKIKIGVCVMEKKVKCGSEVFSAPMGEILDRLQSFGEFEILHFGDKVILEDPIESWPICDCLIAFHSSGYPLEKAQAYAALRKPFLVNELDPQYLLHDRRKVYEHLEMYGIPVPRYACVNRKVPNQDLHYFVEEEDFVEVHGERFWKPFVEKPVNGDDHSIMIYYPSSAGGGMKELFRKIGNRSSEFHPDVRRVRREGSYIYEEFMATGGTDVKVYTVGPEYAHAEARKSPVVDGVVMRNTDGKEVRYPVLLTPAEKQMAREVCIAFRQAVCGFDLLRSEGCSYVCDVNGWSFVKNSYKYYDDAACVLRKMCLDAKAPHLSSTLPPTLPWKVNEPVQSNEGLTRQGSGIIGTFGQSEELRCVIAVVRHGDRTPKQKVKLKVTEEKLLNLMLKYNGGKPRAETKLKSAVQLQDLLDATRMLVPRTRPGRESDSDAEDLEHAEKLRQVKAVLEEGGHFSGIYRKVQLKPLKWVKIPKSDGDGEEERPVEALMVLKYGGVLTHAGRKQAEELGRYFRNNMYPGEGTGLLRLHSTYRHDLKIYSSDEGRVQMSAAAFAKGLLDLEGQLTPILVSLVSKDSSMLDGLDNASIEMEAAKARLNEIVTSGTKMIDDDQVSSEDFPWMTDGAGLPPNAHELLRELVKLTKNVTEQVRLLAMDEDENLTEPYDIIPPYDQAKALGKTNIDSDRIASGLPCGSEGFLLMFARWIKLARDLYNERKDRFDITQIPDVYDSCKYDLLHNSHLDLKGLDELFKVAQLLADGVIPNEYGINPQQKLKIGSKIARRLMGKILIDLRNTREEALSVAELKESQEQVLSLSASQREDRNSQPKLFINSDELRRPGTGDKDEDDDKETKYRLDPKYANVKTPERHVRTRLYFTSESHIHSLMNVLRYCNLDESLLGEESLICQNALERLCKTKELDYMSYIVLRLFENTEVSLEDPKRFRIELTFSRGADLSPLRNNDDEAETLLREHTLPIMGPERLQEVGSCLSLETMEKMVRPFAMPAEDFPPASTPVGFSGYFSKSAAVLERLVNLFHNYKNSSSNGRS