wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-soluble NSF attachment protein (SNAP-alpha) (N-ethylmaleimide-sensitive factor attachment protein alpha) (P54921)
Organism: Rattus norvegicus (Rat)
Function: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. Together with GNA12 promotes CDH5 localization to plasma membrane.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P54920}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54920}.
Interaction partners:
- Vesicle-associated membrane protein 2
- Syntaxin-1A
- Syntaxin-5
- Synaptosomal-associated protein 23
- Multifunctional fusion protein
- Vesicle-associated membrane protein 3
- Vesicle-associated membrane protein 7
- Vesicle-associated membrane protein 8
- BET1 homolog
- Vesicle-fusing ATPase
Sequence:
MDTSGKQAEAMALLAEAERKVKNSQSFFSGLFGGSSKIEEACEIYARAANMFKMAKNWSAAGNAFCQAAQLHLQLQSKHDAATCFVDAGNAFKKADPQEAINCLMRAIEIYTDMGRFTIAAKHHISIAEIYETELVDVEKAIAHYEQSADYYKGEESNSSANKCLLKVAGYAAQLEQYQKAIDIYEQVGTSAMDSPLLKYSAKDYFFKAALCHFCIDMLNAKLAVQKYEELFPAFSDSRECKLMKKLLEAHEEQNVDSYTESVKEYDSISRLDQWLTTMLLRIKKTIQGDEEDLR
Protein: Advillin (Peripheral nervous system villin-like protein) (Pervin) (Q9WU06)
Organism: Rattus norvegicus (Rat)
Function: Ca(2+)-regulated actin-binding protein which plays an important role in actin bundling. May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis. In podocytes, controls lamellipodia formation through the regulation of EGF-induced diacylglycerol generation by PLCE1 and ARP2/3 complex assembly (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11849295}. Cell projection, neuron projection {ECO:0000269|PubMed:11849295}. Cell projection, axon {ECO:0000269|PubMed:11849295}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O75366}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:O75366}. Note=In podocytes, present in the F-actin-enriched cell periphery that generates lamellipodia and focal adhesions. {ECO:0000250|UniProtKB:O75366}.
Interaction partners:
Sequence:
MSLSSAFRTVTNDPGIITWRIEKMELVLVPLSAHGNFYEGDCYIILSTRRVGSLLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHREVQYHESDTFRGYFKRGIIYKKGGVASGMKHVETNTYDVKRLLHVKGKRNIRATEVEMSWDSFNQGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAASPELMTVLQNTLGRRSIIKPAVPDEVTDQQQKSTIMLYHVSDTTGQLSVTEVATRPLVQELLNHDDCYILDQSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTNVETVNDGAESAMFKQLFQKWSVKDQTTGLGKTFSIGKIAKIFQDKFDVTLLHTKPEVAAQERMVDDGNGKVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPCYILYIWQGRHASQDELAASAYQAVEVDQQFGGAPVQVRVSMGKEPRHFMAIFKGKLVIYEGGTSRKGNVEPDPPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLWTQAEHYLWYGKGSSGDERAMAKELAELLCDGDADTVAEGQEPPEFWDLLGGKAPYANDKRLQQETLDIQVRLFECSNKTGRFLVTEVTDFTQDDLSPGDVMLLDTWDQVFLWIGAEANATEKEGALSTAQEYLVTHPSGRDPDTPILIIKQGFEPPTFTGWFLAWDPHIWSEGKSYEQLKNELGDATAIVRITTDMKNATLSLNSSESGPKYYPVEVLLKSQDQELPEDVDPTKKENYLSERDFVSVFGITRGQFVSLPGWKQLQLKKEAGLF
Protein: Probable glutamine--tRNA ligase (EC 6.1.1.18) (Glutaminyl-tRNA synthetase) (Q9Y105)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Lysine--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- leucine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase
- AaRS-interacting multifunctional protein 1
- Glutamyl-tRNA
Sequence:
MAGDDLIAKFQALGMSEQKAKETLKNANVTKNLQLSLAAAGSATLSDGTGMLIYHMATKLKPQTADHLPLLVRYIVEHKLDNTQRVDAALEYLLKCGQSLNANIDLQALEKECGVGVVVTPEQIERTVQAKIKASYKEALLEQRYHFNSFKILQDVRGELKWADAKSVKAAIDVEIFDLLGPKTEADLKPQTKANDKPKAAKPKAEVTPAAQTAEAASDGATTISELMKTKVHFHAPGENFKADGYVVTEHTERLLKEHLARTGGKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKPFKITYSSDNFQQLYEWAVVLINKGLAYVCHQKAEELKGFNPKPSPWRERPIEESLRLFEDMKRGKIDEGAATLRMKVTLEEGKMDPVAYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIYCPVQWEYGRLNMNYALVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQIAVDPAMLEAAVRDVLNVTAPRRLVVLEPLKVTIKNFPHAAPVQLEVPDFPQNPQQGTHKITLDKVIYIEQGDFKLEPEKGYRRLAPKQSVGLRHAGLVISVDEIVKDPATGQVVELICTSQPAEQAEKPKAFVQWVSQPIQLEVRLYEQLFKHKNPEDPNEVPGGFLSDISEQSMSVVVAFADRALNQAKVYDKFQFERIGFFSVDPDTSANHLVFNRTVGLKEDAGKK
Protein: Unconventional myosin-If (Myosin-Ie) (O00160)
Organism: Homo sapiens (Human)
Function: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity).
Interaction partners:
- Unconventional myosin-Ic
- Unconventional myosin-XVIIIb
- Unconventional myosin-VI
- Unconventional myosin-IXa
- Actin nucleation-promoting factor WAS
- Myosin light polypeptide 6
- Myosin light chain 6B
- WAS/WASL-interacting protein family member 2
- Actin nucleation-promoting factor WASL
- Actin, cytoplasmic 2
Sequence:
MGSKERFHWQSHNVKQSGVDDMVLLPQITEDAIAANLRKRFMDDYIFTYIGSVLISVNPFKQMPYFTDREIDLYQGAAQYENPPHIYALTDNMYRNMLIDCENQCVIISGESGAGKTVAAKYIMGYISKVSGGGEKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSRGGEPDGGKISNFLLEKSRVVMQNENERNFHIYYQLLEGASQEQRQNLGLMTPDYYYYLNQSDTYQVDGTDDRSDFGETLSAMQVIGIPPSIQQLVLQLVAGILHLGNISFCEDGNYARVESVDLLAFPAYLLGIDSGRLQEKLTSRKMDSRWGGRSESINVTLNVEQAAYTRDALAKGLYARLFDFLVEAINRAMQKPQEEYSIGVLDIYGFEIFQKNGFEQFCINFVNEKLQQIFIELTLKAEQEEYVQEGIRWTPIQYFNNKVVCDLIENKLSPPGIMSVLDDVCATMHATGGGADQTLLQKLQAAVGTHEHFNSWSAGFVIHHYAGKVSYDVSGFCERNRDVLFSDLIELMQTSEQAFLRMLFPEKLDGDKKGRPSTAGSKIKKQANDLVATLMRCTPHYIRCIKPNETKRPRDWEENRVKHQVEYLGLKENIRVRRAGFAYRRQFAKFLQRYAILTPETWPRWRGDERQGVQHLLRAVNMEPDQYQMGSTKVFVKNPESLFLLEEVRERKFDGFARTIQKAWRRHVAVRKYEEMREEASNILLNKKERRRNSINRNFVGDYLGLEERPELRQFLGKRERVDFADSVTKYDRRFKPIKRDLILTPKCVYVIGREKVKKGPEKGQVCEVLKKKVDIQALRGVSLSTRQDDFFILQEDAADSFLESVFKTEFVSLLCKRFEEATRRPLPLTFSDTLQFRVKKEGWGGGGTRSVTFSRGFGDLAVLKVGGRTLTVSVGDGLPKSSKPTRKGMAKGKPRRSSQAPTRAAPAPPRGMDRNGVPPSARGGPLPLEIMSGGGTHRPPRGPPSTSLGASRRPRARPPSEHNTEFLNVPDQGMAGMQRKRSVGQRPVPGVGRPKPQPRTHGPRCRALYQYVGQDVDELSFNVNEVIEILMEDPSGWWKGRLHGQEGLFPGNYVEKI
Protein: Melanoma-derived growth regulatory protein (Melanoma inhibitory activity protein) (Q16674)
Organism: Homo sapiens (Human)
Function: Elicits growth inhibition on melanoma cells in vitro as well as some other neuroectodermal tumors, including gliomas.
Subcellular location: Secreted.
Interaction partners:
- Protein S100-B
- Fibronectin
Sequence:
MARSLVCLGVIILLSAFSGPGVRGGPMPKLADRKLCADQECSHPISMAVALQDYMAPDCRFLTIHRGQVVYVFSKLKGRGRLFWGGSVQGDYYGDLAARLGYFPSSIVREDQTLKPGKVDVKTDKWDFYCQ
Protein: Signal transduction histidine-protein kinase BarA (EC 2.7.13.3) (P0AEC5)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system UvrY/BarA involved in the regulation of carbon metabolism via the CsrA/CsrB regulatory system. Phosphorylates UvrY, probably via a four-step phosphorelay.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Response regulator UvrY
- RNase E specificity factor CsrD
- Aerobic respiration control sensor protein ArcB
- Sensor protein EvgS
- Oxygen sensor protein DosP
- Sensor protein TorS
- Carbon storage regulator
- Phosphotransferase RcsD
- Probable diguanylate cyclase DgcE
- Cyclic di-GMP phosphodiesterase PdeR
Sequence:
MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHSDIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYIALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNPNIIIEGPSTQCLAGKRLAYVEPNSAAAQCTLDILSETPLEVVYSPTFSALPPAHYDMMLLGIAVTFREPLTMQHERLAKAVSMTDFLMLALPCHAQVNAEKLKQDGIGACLLKPLTPTRLLPALTEFCHHKQNTLLPVTDESKLAMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKPGSGISSRVVTPEVNEIVVNPNATLDWQLALRQAAGKTDLARDMLQMLLDFLPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQLIEQQLRSGTKEEDLEPELLELLDEMDNVAREASKILG
Protein: Lipid/polyisoprenoid-binding YceI-like domain-containing protein (O07742)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable oxidoreductase
- Thiamine-phosphate synthase
- Mycoketide-CoA synthase
Sequence:
MAHKTRREGRAGRSSEYSRGVSDAVWTLDASDGELVLRTGVVGRAARLGHRLTIAMTRWQALVNWSGTDPVAGELVAEVDSFEVMRGEGGVKGLSEPEKALVRANALKTLNASRFPHIRFTTEAIAQTGNGYRLTGKLHIRGKSREHVIDLHTEDLGAAWRISADTTVRQSNYGVKPYSLLMGSIRVADEVSVAFTAVRAKDD
Protein: Serine protease 1 (EC 3.4.21.4) (Anionic trypsin I) (Anionic trypsin-I) (Beta-trypsin) (Cationic trypsinogen) (Pretrypsinogen I) (Trypsin I) (Trypsin-1) [Cleaved into: Alpha-trypsin chain 1; Alpha-trypsin chain 2] (P07477)
Organism: Homo sapiens (Human)
Function: Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Serine protease inhibitor Kazal-type 1
- Enteropeptidase
- Trypsin-3
- Chymotrypsinogen B
- Chymotrypsinogen B2
- Carboxypeptidase A1
- Cystic fibrosis transmembrane conductance regulator
- Plasminogen
- Proteinase-activated receptor 1
- Amyloid-beta precursor protein
Sequence:
MNPLLILTFVAAALAAPFDDDDKIVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS
Protein: Gamma-aminobutyric acid receptor subunit rho-1 (GABA(A) receptor subunit rho-1) (GABAAR subunit rho-1) (GABA(C) receptor) (P24046)
Organism: Homo sapiens (Human)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-1 GABA receptor could play a role in retinal neurotransmission.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P56475}; Multi-pass membrane protein {ECO:0000269|PubMed:37659407}. Cell membrane {ECO:0000269|PubMed:37659407}; Multi-pass membrane protein {ECO:0000269|PubMed:37659407}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit rho-2
- Gamma-aminobutyric acid receptor subunit rho-3
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit alpha-2
- Gamma-aminobutyric acid receptor subunit alpha-5
- Gamma-aminobutyric acid receptor subunit epsilon
- Gamma-aminobutyric acid receptor subunit alpha-1
Sequence:
MLAVPNMRFGIFLLWWGWVLATESRMHWPGREVHEMSKKGRPQRQRREVHEDAHKQVSPILRRSPDITKSPLTKSEQLLRIDDHDFSMRPGFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLSFPSTNNLSMTFDGRLVKKIWVPDMFFVHSKRSFIHDTTTDNVMLRVQPDGKVLYSLRVTVTAMCNMDFSRFPLDTQTCSLEIESYAYTEDDLMLYWKKGNDSLKTDERISLSQFLIQEFHTTTKLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVPLGITTVLTMSTIITGVNASMPRVSYIKAVDIYLWVSFVFVFLSVLEYAAVNYLTTVQERKEQKLREKLPCTSGLPPPRTAMLDGNYSDGEVNDLDNYMPENGEKPDRMMVQLTLASERSSPQRKSQRSSYVSMRIDTHAIDKYSRIIFPAAYILFNLIYWSIFS
Protein: Rifin (Q8I2C8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKDHYINILLFALPLNILVYNQRNYYITPRHTETNRSLCECELYSPTNYDSDPEMKRVMQQFEDRTTQRFHEYDEKMQSKRIQCKDRCDKEIQKIILKDKLDKELTEKFATLHTDIQNDAIPTCVCEKSLADKVEKTCLKCTQNLGGIVAPSSGVLGGIGEFELSVWKPAALAAAKEFAEKAGAAQGAIAGNAHGMKIVIYYLKDWGIQQCCPEIFNPFVAKNIYTEVANISGDIIAKYSAKCADTVTGGNSMCKAFCLKLGTNIAHGGRTLSVDHIVQLKIKGLVERADQAVAHVTKTTSETVTAAIKARETALIEGRFESSITSINASIIAIIVIVLILVIIYLILRYRRKKKMKKKLQYLKLLKE
Protein: Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1 (EC 2.4.3.3) (GalNAc alpha-2,6-sialyltransferase I) (ST6GalNAc I) (ST6GalNAc-I) (ST6GalNAcI) (hST6GalNAc-I) (Sialyltransferase 7A) (SIAT7-A) (Q9NSC7)
Organism: Homo sapiens (Human)
Function: Protein sialyltransferase specifically expressed in goblet cells that plays a key role in intestinal host-commensal homeostasis. Conjugates sialic acid with an alpha-2-6 linkage to N-acetylgalactosamine (GalNAc) glycan chains linked to serine or threonine in glycoproteins. Catalyzes the formation of the sialyl-Tn (S-Tn) antigen, an antigen found in intestinal goblet cells, as well as ulcerative colitis (UC) and various cancers. Protein sialylation in globlet cells is essential for mucus integrity and is required to protect the intestinal mucus against excessive bacterial proteolytic degradation.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16319059, ECO:0000269|PubMed:35303419}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Polypeptide N-acetylgalactosaminyltransferase 6
- Elongation factor 1-alpha 2
- Polypeptide N-acetylgalactosaminyltransferase 4
- Polypeptide N-acetylgalactosaminyltransferase 5
- Polypeptide N-acetylgalactosaminyltransferase 2
- Polypeptide N-acetylgalactosaminyltransferase 1
Sequence:
MRSCLWRCRHLSQGVQWSLLLAVLVFFLFALPSFIKEPQTKPSRHQRTENIKERSLQSLAKPKSQAPTRARRTTIYAEPVPENNALNTQTQPKAHTTGDRGKEANQAPPEEQDKVPHTAQRAAWKSPEKEKTMVNTLSPRGQDAGMASGRTEAQSWKSQDTKTTQGNGGQTRKLTASRTVSEKHQGKAATTAKTLIPKSQHRMLAPTGAVSTRTRQKGVTTAVIPPKEKKPQATPPPAPFQSPTTQRNQRLKAANFKSEPRWDFEEKYSFEIGGLQTTCPDSVKIKASKSLWLQKLFLPNLTLFLDSRHFNQSEWDRLEHFAPPFGFMELNYSLVQKVVTRFPPVPQQQLLLASLPAGSLRCITCAVVGNGGILNNSHMGQEIDSHDYVFRLSGALIKGYEQDVGTRTSFYGFTAFSLTQSLLILGNRGFKNVPLGKDVRYLHFLEGTRDYEWLEALLMNQTVMSKNLFWFRHRPQEAFREALHMDRYLLLHPDFLRYMKNRFLRSKTLDGAHWRIYRPTTGALLLLTALQLCDQVSAYGFITEGHERFSDHYYDTSWKRLIFYINHDFKLEREVWKRLHDEGIIRLYQRPGPGTAKAKN
Protein: Protoporphyrinogen oxidase (EC 1.3.3.4) (Q8IJC3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Ferrochelatase
- Uroporphyrinogen decarboxylase
- coproporphyrinogen oxidase
- Delta-aminolevulinic acid dehydratase
- hydroxymethylbilane synthase
- GDP-L-fucose synthase
Sequence:
MSEYKKYNVPSHEIYDVILIGGGLFNCCLYYYLKLKNSELSIIIVEKEENLGGYIKTYTYNIDDKKILVELGPNMFKLCNESYNLINKLNLLSSVRLLDDTLIRYIYIKNDKLYPLYLNIFSYLSFPLINISNKIKLLFKLIFKQYKNLNSYTNDISVENYMNDNFDSQHYNFLLLPFIYGSCAGNGKISAVSFFSRNLKLFHNKVNSLYIWNEKIKSEEKNRNIKCVNNNTFIYQHMNKKKKNFNLFTPCYNFFYISNKNMKMDVYLNVLYNYYSSNKKTEKKNVFNYICYRIPILLLHMKQFSINIFRHISIFLKCTYQFFYPFLMLPDLAKWTTSHFDDEKKKKKNLIGKTVTFKNGLYELIDKLQSHMNKEFIYTNHEVDFIEKAYNNLWMCNIKHENQNKTIYGKNIVLAVNSKICSNIMRNILPVNIRDILLNFSYSSIISISLYFKKSDINIPKNFFGFLSSDKCAHILGCFHINNMFKERCHDDNKVLLTLYMGGSNHPNDITLDEYEIKEIISNDLKNIFDIYNDAQPNILKIHKWKDAIPFYSYNYEKLLKKVMEELNKLSYKNLYLDSGWITGTSISDRIRSAQDLCEYIFSLTNLAS
Protein: Nuclear RNA export factor 1 (F1Q7H6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
- Aly/REF export factor.
- mRNA export factor
- NTF2-related export protein
- THO complex subunit 5 homolog
- Nuclear cap-binding protein subunit 2
- Nuclear pore complex protein Nup98-Nup96
- Regulator of nonsense transcripts 3B
- Regulator of nonsense transcripts 3A
- Nucleoporin 214.
- Polymerase
Sequence:
MATADDSRYYNEHDDRVGGPKHRNRKGRGPFRAPLYSDQMSRPRHRGGHSGGGGGGGGGGPGPRSRLHDDDGDVTMSDIPQDSSQRRYNPYGRQQNRRDDRNRKGGRGGGGNDDRGGNRFGGRGGGGGGGGGPSDGRSKNWFKMTIPYGKKYDKDWLLSSLQSVCPIPFHAIQYHLDGNRAQFYVEDSTTANAIFKVSRRITDKDGYKVAVIMNSCPPPTLIHSDLKPADLEHLKQCMAKRFDGSQQALDLNNIRVDPDLVSQNIEVTLNRKNSMCAVIKIIEENIPELVCLNLSNNRLFRLDDLVDIIHKVPNLKILNLSHNELKTERELDKLKGLKLVDLSLEGNPLCHHFKIHADYISAIRERFPKLLKLDGHDLPPPIGFDLDDGPSTLPPSKASYFCSEEIKNIILCFLQQFYNVYDSGNRQPLLDAYHDGATFSLSIPFVSLNPSKSTLGEYQKDSRNIKRMKDPTTRYRLIKHTRLNVVAFLNELPKTQHDIASFVVDVNTYTATLLAFTVCGVFKEMDGKSRETYRAFSRVFIAVPAGSTGLCIVNDELFVRNATTEEIRRAFVAPAPTPSSSPVPTLSAHQQEMLAAFSLKSGMNLEWSQKCLQDNDWDFERAAQIFTGLKAQGKIPDVAFVK
Protein: Transmembrane protein 235 (Claudin-27) (B1AQL3)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000305|PubMed:21689651}.
Interaction partners:
Sequence:
MALLATLLLSAALGALLSFALLAAAVASDYWYILEVADAGGLGGVQLFSHSGLWRTCEGQNSCVPLIDPFASAGLEVSPSVQHLLSLHRTVMVVLPLSLVLIVCGWVCGLLSSLSQSVPLLLATGCYFLLGGALTLAGLSIYISYSHLAFVEAARTYGVTHVQNVHISFGWSLALAWASCASEVLSGALLLAAARLLSLSQRPGVPHSVIL
Protein: SD02661p (Q95SW6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSGMDHSLKLWRLDKPDIKEAIELSSGFSPNKNTGPFPTIKEHFPDFSTRDIHRNYVDCVQWFGDFVFSKSCENSIVCWKPGKLSESWHEIKPQESATTVLHHFDYKMCEIWFVRFAFNAWQKILALGNQLGTTFVWELDCNDPNLTKCSQLVHPKSNSTIRQTSFSKDGSILVCVCDDSTVWRWDRVN
Protein: Gamma1a-synuclein (Synuclein, gamma b (Breast cancer-specific protein 1)) (Q502J6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDVLMKGFSMAKEGVVAAAEKTKAGVEEAALKTKEGVTYVGNKTKEGMVSGVNTVVQKTTDQANIVGETAVGGANVAGQNTVEGLENVAASTGMVNPGDFSHGGMEGGEGGEGY
Protein: Eukaryotic translation initiation factor 3 subunit M (eIF3m) (Q09722)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012, ECO:0000269|PubMed:15904532}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit C
- Probable eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit G
Sequence:
MEGSDFILVVDSSVEEQVEELAMYLDNLEANTDKNVLALCREYLASENVKEVLNLFLTRLPLLAQAPEKELEPILAVFINLIQESAAFEDHVSKFCQALEQIADQNNNLTPAILSVLSILFNTAVKERQHARLSILTSVVTLTTRYSLFSTLAPNLKYFPDWLKEAGVSVSDHRAFNIFVSKAIQSYDDEQSFAFLLEAVKMDNSTADEAVRELVQRAVNSPKYFFFDDIVTLPPVQQLEQSTLQLLGILSGGMTDDYVSWVAENHAHCQHQKFDEDAIARKMKLLTIASLATQAPNNTLSYGDVAKSLKIDENEVELWIIDVIRAGLVEGRMSQLTKTLSIHRSSYRVFGKHEWVALHEKLAKWGSSLRYMLQVMEQPLSSFTIASSKKGNRDGSAVTASE
Protein: Elongator complex protein 4 (A0A1W2PPP6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAVATCGSVAASTGSAVATASKSNVTSFQRRGPRASVTNDSGPRLVSIAGTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPANILQELPAPLLDDKCKKEFDEDVYNHKTPESNIKMKIAWRYQLLPKMEIGPVSSSRFGHYYDASKRMPQELIEASNWHGFFLPEKISSTLKVEPCSLTPGYTKLLQFIQNIIYEEGFDGSNPQKKQRNILRIGIQNLGSPLWGDDICCAENGGNSHSLTKFLYVLRGLLRTSLSACIITMPTHLIQNKAIIARVTTLSDVVVGLESFIGSERETNPLYKDYHGLIHIRQIPRLNNLICDESDVKDLAFKLKRKLFTIECITKLRSYDLRRQRYFLSRHLQRKFSIKKNPYFKKPHTLKKIY
Protein: GREB1-like protein (B8JKP6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a major role in early metanephros development.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- A-type potassium channel modulatory protein DPP6
- Transmembrane protein 241.
Sequence:
MGNSYAGQLKSARFEEALHNSIEASLRSSGGDPQPVFTQLYLEPDQYSGHVEDIKPKMDLSLRSDPSTHVLVKCHSSNSVEDMDDEDDSDTSSPPLPYLQGPPPDGCCTVDGFCQAGKDLRLVSMATESIEVPAGFELVGAKSPSIPEHILVCAVDKRFLPDENGKNALLGFSGNCVGCGEKGFRYFTEFSNHINLKLSTQPKKQKHLKYYLVKNSQGALCKGALICWKDCKTRPFSNSASSSKPSSSSSLSSKENGDTNGHSPSPFPLSDSPPARMQSGSSSGIFGPQELGFLKPLNTPTHGTKTLPIVPTALRVNGLTNGLSMDGRSTLLSPPRTNPLSTPSHGYRTTETGDSPASTAMSTGPPKKRHRSWHPTTLVPIPATAVPVPAIRPLTCSSGPLLSLSNQQPASVSGVIQPQPITAGETVIIPDNLLNSYGVRPVLLIGQGTLPYFFGNVGDLVVSPLLVSCYKGRELNEKTLASLGMSANQLLTTETMILLTLQYLARLGTEQIPLREEFEQIMLKAMLCGPTGPPVSPAQLPWLARMEASVSGGSVQVLVTHGSLGEGISESLRSLSETSPQQQQCLPNYVLIICTSKSGANEFCVLVLGKYQSRALAESMLSTNEFLKEISYELITGKVSVLASHFQSTSLGDNMDKQLVRYQRKRKDRVVQPFQGHLTEYIHSQEAATMIPESGPDLLSDDFQIHPPQLSVARSLLSQVCAIADSGSQSLDLGRFCKVDFLILVPPSHVLVHQTVQRIRQSGVLIDLGIEDVSLAMQKSDKYVVRLDTEVHTKMEAFMRKVKQNPYTLFVLIHDNSHVDLTSALSGSVCHGELQGLADRVVNCPEVLEAINLLVLQVSCFPFTLQSRQSRISTQNEVHWPDTENQQGEASPKDLIYFGLKDYSKSLQWGVASPILRCDDAFERMVKTLLERHPHLHSMVIRSYLLIQQYTEALMALTAAPSLRDHVTPQTLAMVEDLLSVPGRSKHGCGHMLLVRVPSLQLARLAQERLEEARDKLGLQYRFAVLLGSPAAEISLPVHFCARLRAWRGCKNEEWVPHTYEDLEGLPCIVILTGKDPLGETFPRSLKYCDLRLIDSSYLTRTALEQEVGLACSYVTRRVIPKTKTATSREERPREGERSSGETAEHDDLPMELERPPSNASAATRTSGSTTENGVSSSSILDKPSSQSDPCGSRTMMDSCSSPVRFKQECDSQAPSSSSTSSFSSASSSSSSSSSPAAQRPSQSTQAPRECNRTQVFPRTAVLSRAAYTLLAPETLGHPSSASLLPHADVSWSSPLRPPVPHGLGGAEQSLYYRQWTTARQHHADYEGPVPHPHPRRLLLSGPPQVGKTGAYLQFLRILFRMLIRLLEVDVYDEEELEEDVQDKSKVPPSSGPQWPDVEDVRKLRFDLCPHDCKFKYSSPVYANRMPKTQSGVKTERLDTEADPPKRNTVSVRLSLFAAHNAFHHCEQCHHYSEPIPAAQLSDCTFHAFTFCSSMLGEEVQLHFIIPKSKESHFVFSQQGSHLESMRLPLLSDKESGMMKSPIFTPTTGRQEHGLLNIYHAMEGAEHLHILVVKQYEMPLYRKYWPNHILLVLPAMFNNSGVGAARFMIKELSYHNLELERNRQEEQGVKRQDVWPFIVMMDDSCVLWNAQQPGPDGKTEVMNVSLKSVLQHMEATPKISQYAVCGLRKWSSSLSSQAPTSPFSRCHLHDLILLNVDLTQNVQYDLNRFTCEEVDFNLRANSSGLLLCRFNQFSIMKKHIPIGGHKDFLIKPKLMRIETPVRVCASQYVCAPDSEQTLLAAPAQFLLEKFLQSCSHRLFPLALSNSANPVLSIDSYLNLGPEVQVCYVSSRPHSVNVDHQGVIFSGLLLYLCDSFVVSSLLKKFNFLKGATLCVICQDRSSLRQTIVRLELEDEWQFRLRDEFQTANCSEDRPLYFLTGRHI
Protein: Aromatic-L-amino-acid decarboxylase (AADC) (EC 4.1.1.28) (DOPA decarboxylase) (DDC) (P05031)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (L-DOPA) to dopamine and L-5-hydroxytryptophan (5-HTP) to serotonin. Catalyzes the formation of serotonin more efficiently than dopamine. Displays no activity to tyrosine. Variation in the synthesis of bioamines may be a factor contributing to natural variation in life span.
Interaction partners:
- Tyrosine 3-monooxygenase
- Tryptophan 5-hydroxylase 2
- Arylalkylamine N-acetyltransferase 1
- Tyramine beta-hydroxylase
- Protein henna
- monoamine oxidase
- Kynurenine formamidase
- tyrosinase
- Tyrosine aminotransferase
- Aspartate aminotransferase
Sequence:
MSHIPISNTIPTKQTDGNGKANISPDKLDPKVSIDMEAPEFKDFAKTMVDFIAEYLENIRERRVLPEVKPGYLKPLIPDAAPEKPEKWQDVMQDIERVIMPGVTHWHSPKFHAYFPTANSYPAIVADMLSGAIACIGFTWIASPACTELEVVMMDWLGKMLELPAEFLACSGGKGGGVIQGTASESTLVALLGAKAKKLKEVKELHPEWDEHTILGKLVGYCSDQAHSSVERAGLLGGVKLRSVQSENHRMRGAALEKAIEQDVAEGLIPFYAVVTLGTTNSCAFDYLDECGPVGNKHNLWIHVDAAYAGSAFICPEYRHLMKGIESADSFNFNPHKWMLVNFDCSAMWLKDPSWVVNAFNVDPLYLKHDMQGSAPDYRHWQIPLGRRFRALKLWFVLRLYGVENLQAHIRRHCNFAKQFGDLCVADSRFELAAEINMGLVCFRLKGSNERNEALLKRINGRGHIHLVPAKIKDVYFLRMAICSRFTQSEDMEYSWKEVSAAADEMEQEQ
Protein: DNA-directed RNA polymerase subunit Rpo1C (EC 2.7.7.6) (DNA-directed RNA polymerase subunit A'') (B8YB54)
Organism: Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12) (Sulfolobus shibatae)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00411, ECO:0000269|PubMed:22848102}.
Interaction partners:
Sequence:
MIDEKDKSYLEEKVKQASNILPQKIVEDLKNLISNKEVLVTRDEIDKIFDLAIKEYSEGLIAPGEAIGIVAAQSVGEPGTQMTLRTFHFAGIRELNVTLGLPRLIEIVDAKKVPSTPMMTIYLTDEYKHDKEKALEVARKLEYTKIENVVSSTSIDIASMSIILQLDNEMLKDKGVTVDDVKKAINRLKLGEFVIDESEGNTLNISFANIDSIAALFKLRDKILNTKIKGIKGIKRAIVQKKGDEYIILTDGSNLSGVLSVKGVDIAKVETNNIREIEEVFGIEAAREIIIREISKVLAEQGLDVDMRHILLVADVMTRTGVVRQIGRHGVTGEKNSVLARAAFEVTVKHLLDAAARGDVEEFKGVVENIIIGHPIKLGTGMVELTMRPILR