wanglab/gogpt-training-data huggingface dataset:
Protein: Sodium channel protein type 11 subunit alpha (NaN) (Sensory neuron sodium channel 2) (Sodium channel protein type XI subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.9) (O88457)
Organism: Rattus norvegicus (Rat)
Function: This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant sodium channel isoform. Also involved, with the contribution of the receptor tyrosine kinase NTRK2, in rapid BDNF-evoked neuronal depolarization (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10196578}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium channel regulatory subunit beta-1
- Sodium channel regulatory subunit beta-4
- Sodium channel protein type 1 subunit alpha
- Unc-79 homolog, NALCN channel complex subunit
- Sodium channel regulatory subunit beta-2
- Sodium channel protein type 9 subunit alpha
- Sodium channel regulatory subunit beta-3
- Sodium channel protein type 2 subunit alpha
- Sodium channel protein type 3 subunit alpha
Sequence:
MEERYYPVIFPDERNFRPFTSDSLAAIEKRIAIQKERKKSKDKAAAEPQPRPQLDLKASRKLPKLYGDIPPELVAKPLEDLDPFYKDHKTFMVLNKKRTIYRFSAKRALFILGPFNPLRSLMIRISVHSVFSMFIICTVIINCMFMANSMERSFDNDIPEYVFIGIYILEAVIKILARGFIVDEFSFLRDPWNWLDFIVIGTAIATCFPGSQVNLSALRTFRVFRALKAISVISGLKVIVGALLRSVKKLVDVMVLTLFCLSIFALVGQQLFMGILNQKCIKHNCGPNPASNKDCFEKEKDSEDFIMCGTWLGSRPCPNGSTCDKTTLNPDNNYTKFDNFGWSFLAMFRVMTQDSWERLYRQILRTSGIYFVFFFVVVIFLGSFYLLNLTLAVVTMAYEEQNRNVAAETEAKEKMFQEAQQLLREEKEALVAMGIDRSSLNSLQASSFSPKKRKFFGSKTRKSFFMRGSKTAQASASDSEDDASKNPQLLEQTKRLSQNLPVDLFDEHVDPLHRQRALSAVSILTITMQEQEKFQEPCFPCGKNLASKYLVWDCSPQWLCIKKVLRTIMTDPFTELAITICIIINTVFLAVEHHNMDDNLKTILKIGNWVFTGIFIAEMCLKIIALDPYHYFRHGWNVFDSIVALLSLADVLYNTLSDNNRSFLASLRVLRVFKLAKSWPTLNTLIKIIGHSVGALGNLTVVLTIVVFIFSVVGMRLFGTKFNKTAYATQERPRRRWHMDNFYHSFLVVFRILCGEWIENMWGCMQDMDGSPLCIIVFVLIMVIGKLVVLNLFIALLLNSFSNEEKDGSLEGETRKTKVQLALDRFRRAFSFMLHALQSFCCKKCRRKNSPKPKETTESFAGENKDSILPDARPWKEYDTDMALYTGQAGAPLAPLAEVEDDVEYCGEGGALPTSQHSAGVQAGDLPPETKQLTSPDDQGVEMEVFSEEDLHLSIQSPRKKSDAVSMLSECSTIDLNDIFRNLQKTVSPKKQPDRCFPKGLSCHFLCHKTDKRKSPWVLWWNIRKTCYQIVKHSWFESFIIFVILLSSGALIFEDVNLPSRPQVEKLLRCTDNIFTFIFLLEMILKWVAFGFRRYFTSAWCWLDFLIVVVSVLSLMNLPSLKSFRTLRALRPLRALSQFEGMKVVVYALISAIPAILNVLLVCLIFWLVFCILGVNLFSGKFGRCINGTDINMYLDFTEVPNRSQCNISNYSWKVPQVNFDNVGNAYLALLQVATYKGWLEIMNAAVDSREKDEQPDFEANLYAYLYFVVFIIFGSFFTLNLFIGVIIDNFNQQQKKLGGQDIFMTEEQKKYYNAMKKLGTKKPQKPIPRPLNKCQAFVFDLVTSQVFDVIILGLIVLNMIIMMAESADQPKDVKKTFDILNIAFVVIFTIECLIKVFALRQHYFTNGWNLFDCVVVVLSIISTLVSRLEDSDISFPPTLFRVVRLARIGRILRLVRAARGIRTLLFALMMSLPSLFNIGLLLFLVMFIYAIFGMSWFSKVKKGSGIDDIFNFETFTGSMLCLFQITTSAGWDTLLNPMLEAKEHCNSSSQDSCQQPQIAVVYFVSYIIISFLIVVNMYIAVILENFNTATEESEDPLGEDDFEIFYEVWEKFDPEASQFIQYSALSDFADALPEPLRVAKPNKFQFLVMDLPMVMGDRLHCMDVLFAFTTRVLGDSSGLDTMKTMMEEKFMEANPFKKLYEPIVTTTKRKEEEQGAAVIQRAYRKHMEKMVKLRLKDRSSSSHQVFCNGDLSSLDVAKVKVHND
Protein: Haze protective factor 1 (Q05164)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in cell wall organization and biosynthesis.
Subcellular location: Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP), enriched at bud sites and their neighborhood.
Interaction partners:
- SWIRM domain-containing protein YOR338W
- Protein NAM8
- Protein SCP160
- Nuclear segregation protein BFR1
- ATP-dependent RNA helicase DHH1
- Secreted protein CSS1
- Nuclear fusion protein BIK1
- Uncharacterized protein YOL118C
Sequence:
MFNRFNKLQAALALVLYSQSALGQYYTNSSSIASNSSTAVSSTSSGSVSISSSIELTSSTSDVSSSLTELTSSSTEVSSSIAPSTSSSEVSSSITSSGSSVSGSSSITSSGSSVSSSSSATESGSSASGSSSATESGSSVSGSSTSITSGSSSATESGSSVSGSTSATESGSSASGSSSATESGSSASGSSSATESGSSVSGSSSATESGSSVSGSSSATESGSASSVPSSSGSVTESGSSSSASESSITQSGTASGSSASSTSGSVTQSGSSVSGSSASSAPGISSSIPQSTSSASTASGSITSGTLSSITSSASSATATASNSLSSSDGTIYLPSTTISGDITLTGSVIATEAVEVAAGGKLTLLDGDKYVFSADFIIHGGVFVEKSKPTYPGTEFDISGENFDVSGTFNAEEPAASSASAYSFTPGSFDNSGDISLSLSESTKGEVTFSPYSNSGAFSFSNAILNGGSVSGLQRRAESGSVNNGEINLENGSTYVVVEPVSGSGTINIISGNLYLHYPDTFTGQTVVFKGEGVLAVDPTETNTTPIPVVGYTGENQIAITADVTALSYDSATGVLTATQGNSQFSFSIGTGFSSSGFNVSEGTFAGAYAYYLNYGGVVASSATPSSTSTTSGATNSTSGSTSFGASVTGSTASTSFGASVTGSTASTLISGSPSVYTTTLTYATTTSTVVVSCSETTDSNGNVYTITTTVPCSSTTATITSCDETGCHVTTSTGTVATETVSSKSYTTVTVTHCDNNGCNTKTVTSECPEETSATTTSPKSYTTVTVTHCDDNGCNTKTVTSEAPEATTTTVSPKTYTTATVTQCDDNGCSTKTVTSEAPKETSETSETSAAPKTYTTATVTQCDDNGCNVKIITSQIPEATSTVTATSASPKSYTTVTSEGSKATSLTTAISKASSAISTYSKSAAPIKTSTGIIVQSEGIAAGLNANTLNALVGIFVLAFFN
Protein: Apolipoprotein M (Apo-M) (ApoM) (Protein G3a) (O95445)
Organism: Homo sapiens (Human)
Function: Probably involved in lipid transport. Can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid.
Subcellular location: Secreted {ECO:0000269|PubMed:17525477, ECO:0000269|PubMed:18279674, ECO:0000269|PubMed:18460466}. Note=Present in high density lipoprotein (HDL) and to a lesser extent in triglyceride-rich lipoproteins (TGRLP) and low density lipoproteins (LDL).
Interaction partners:
- Beta-2-glycoprotein 1
- Apolipoprotein A-II
- Apolipoprotein A-I
- G patch domain and ankyrin repeat-containing protein 1
- Apolipoprotein C-III
- Apolipoprotein A-IV
- Apolipoprotein C-II
- Apolipoprotein A-V
- Apolipoprotein E
- Apolipoprotein C-I
Sequence:
MFHQIWAALLYFYGIILNSIYQCPEHSQLTTLGVDGKEFPEVHLGQWYFIAGAAPTKEELATFDPVDNIVFNMAAGSAPMQLHLRATIRMKDGLCVPRKWIYHLTEGSTDLRTEGRPDMKTELFSSSCPGGIMLNETGQGYQRFLLYNRSPHPPEKCVEEFKSLTSCLDSKAFLLTPRNQEACELSNN
Protein: Signal recognition particle subunit SRP72 (Q9VDK7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PIRNR:PIRNR038922}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- Signal recognition particle 9 kDa protein
- Signal recognition particle 19 kDa protein
- Signal recognition particle subunit SRP68
- Signal recognition particle 14 kDa protein
- Signal recognition particle 54 kDa protein
- Signal recognition particle receptor subunit beta
- Signal recognition particle receptor subunit alpha homolog
- FI01658p
- Large ribosomal subunit protein uL22
- Large ribosomal subunit protein eL39
Sequence:
MSKDANPKEALIKAAYADVNKFGNNQEFDKAVKAVNRILGVAPDDPTALHCKVVCLVQLSKFEEAYKFIEKNRLSSLFFEKAYCEYQLNKQQQALKTIDDAGLQPLPPNLKELRTQVLYRLERYDECLDSYRDIIKNTSDEYEEERRTNLSAVAANLAVDQTKEVPEVPEDTYEQYFNSACIQANRQKYAEAERKLRTSEKLCLEDECASEEEIIEEVDVIRVQLAYVLQLQGKTKEASSIYADCLRHKPKDAALVAVASNNLVVVNKDQNVFDSKKKIRAALADACESRLTSRQKQVIALNNCLLALYTNAGDQVQQLSQKLAQTYPQVEFEALLIRCTQLAKDRKHKEAIEQLQKFAAAHKSHEFVSKFAIIQLQLLQGNRKDAIETLLSLGEAKYKPGVVSALVSLYLGTDNKTAASALLKSAVDWYKKNEVSSGDLSDMWRQAAEFHLRGGASETAASSLEELLKLNPNDTKVLAQLVIAYAQFQPKRALELSRKLPKLETLTTASEIDALEAANWVMSAKAAKKTANTKVEPSPSTPLEKKKNRNRKRKGKLPKNYNAEVAPDPERWLPKYERTGFRKKRGGARGKDVIKGSQGMASGAADQYDMSSRVNLTKNSPATPVYQETAPGPRQQHRKGGHKKKKGGRF
Protein: AMP-binding enzyme, putative (AFU_orthologue AFUA_5G04270) (C8V3Q2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Fatty acid activator Faa4, putative
- Palmitoyl-protein thioesterase 1
- Uncharacterized protein
- Fatty acid synthase subunit alpha reductase
- Fatty acid synthase subunit alpha
- Fatty acid synthase subunit beta
- Fatty acid synthase alpha subunit pkiB reductase
- Fatty acid synthase beta subunit aflB dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Fatty acid synthase alpha subunit stcJ reductase]
- Fatty acid synthase beta subunit stcK dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase]
Sequence:
MFFTQERAHYARAAELTQEPPKGKPYSVAIPGTEKDGRSPIYRSWWTQKELVKTLDPKVTTAHEIFESTANDTPKADCLGWRPYDPVKKTWGQYQWISYGTVQKRRTDFGAGLVELHHKHNCARPGQYGIGLWCQNRPEWQITDLACMSQSLYSVSIYDVLASDATQYIINHAELSCVVASLPHIPTLIKLKPVLPNLKIIVSLDSLEAGEPAGHSKRALLESMAAGHDLTIYSMDQVEALGAASNRPLNPPKPSDIVTINYTSGTTGAPKGVVLTHENAVAATSGALVSVSQARGDTFPSYLPLAHIYERLTEHAALWSGARIGYFHGNILELVDDLKVLKPTGFVSVPRLYSRFGTAIRAATIEAPGFRGTLSKHIVAAKSANLKNPDPSKATVKHALYDRIWAKKVAAAVGLENAKQLISGSAPLDPSLHDFLRVAIGADFSQGYGLTETYAMACAQSPKDVTSGNCGRVAPCTEVCLLSLPDMEYSVDDKPFPRGELLVRGPNVFKEYLKNPEETSKAITEDGWFRTGDVAKIDDMGRIIIIDRRKNVLKLAQGEYISPERLEGIISSELGYLAQVYVHGDSMQTFLVAIFGVQAELFASFASKVLGRTIDPTDVAGIKAVLQDNKIKKAVLRDLERVAKKNKLAGYERVKNCALMVEPFSVENDLLTPTLKLKRPPVVKKYRQLLDQLYEEANNEQSAPKAKL
Protein: C-Jun-amino-terminal kinase-interacting protein 1 (JIP-1) (JNK-interacting protein 1) (Islet-brain-1) (IB-1) (JNK MAP kinase scaffold protein 1) (Mitogen-activated protein kinase 8-interacting protein 1) (Q9WVI9)
Organism: Mus musculus (Mouse)
Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and thus inhibiting the JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response (By similarity). Acts as a scaffold protein that coordinates with SH3RF1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the activation of MAPK8/JNK1 and differentiation of CD8(+) T-cells.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Mitochondrion membrane {ECO:0000250}. Note=Accumulates in cell surface projections. Under certain stress conditions, translocates to the perinuclear region of neurons. In insulin-secreting cells, detected in both the cytoplasm and nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Stress-activated protein kinase JNK
- Dual specificity mitogen-activated protein kinase kinase 7
- Mitogen-activated protein kinase 9
- C-Jun-amino-terminal kinase-interacting protein 2
- Mitogen-activated protein kinase 10
- Transcription factor Jun
- Kinesin light chain 1
- Mitogen-activated protein kinase kinase kinase 11
- Amyloid-beta precursor protein
- Mitogen-activated protein kinase kinase kinase kinase 1
Sequence:
MAERESGLGGGAASPPAASPFLGLHIASPPNFRLTHDISLEEFEDEDLSEITDECGISLQCKDTLSLRPPRAGLLSAGSSGSAGSRLQAEMLQMDLIDAAGDTPGAEDDEEEEDDELAAQRPGVGPPKAESNQDPAPRSQGQGPGTGSGDTYRPKRPTTLNLFPQVPRSQDTLNNNSLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQGSPVPTQDRGTSTDSPCRRSAATQMAPPSGPPATAPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDPAEPTSTFMPPTESRMSVSSDPDPAAYSVTAGRPHPSISEEDEGFDCLSSPERAEPPGGGWRGSLGEPPPPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCFGDYSDESDSATVYDNCASASSPYESAIGEEYEEAPQPRPPTCLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLFSCVINGEEHEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFPAYYAIEVTKEPEHMAALAKNSDWIDQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLTVHFNPPSSCVLEISVRGVKIGVKADDALEAKGNKCSHFFQLKNISFCGYHPKNNKYFGFITKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE
Protein: WD repeat domain 3, isoform CRA_b (cDNA FLJ77605, highly similar to Homo sapiens WD repeat domain 3 (WDR3), mRNA) (Q5TDG3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGLTKQYLRYVASAVFGVIGSQKGNIVFVTLRGEKGRYVAVPACEHVFIWDLRKGEKILILQGLKQEVTCLCPSPDGLHLAVGYEDGSIRIFSLLSGEGNVTFNGHKAAITTLKYDQLGGRLASGSKDTDIIVWDVINESGLYRLKGHKDAITQALFLREKNLLVTSGKDTMVKWWDLDTQHCFKTMVGHRTEVWGLVLLSEEKRLITGASDSELRVWDIAYLQEIEDPEEPDPKKIKGSSPGIQDTLEAEDGAFETDEAPEDRILSCRKAGSIMREGRDRVVNLAVDKTGRILACHGTDSVLELFCILSKKEIQKKMDKKMKKARKKAKLHSSKGEEEDPEVNVEMSLQDEIQRVTNIKTSAKIKSFDLIHSPHGELKAVFLLQNNLVELYSLNPSLPTPQPVRTSRITIGGHRSDVRTLSFSSDNIAVLSAAADSIKIWNRSTLQCIRTMTCEYALCSFFVPGDRQVVIGTKTGKLQLYDLASGNLLETIDAHDGALWSMSLSPDQRGFVTGGADKSVKFWDFELVKDENSTQKRLSVKQTRTLQLDEDVLCVSYSPNQKLLAVSLLDCTVKIFYVDTLKFFLSLYGHKLPVICMDISHDGALIATGSADRNVKIWGLDFGDCHKSLFAHDDSVMYLQFVPKSHLFFTAGKDHKIKQWDADKFEHIQTLEGHHQEIWCLAVSPSGDYVVSSSHDKSLRLWERTREPLILEEEREMEREAEYEESVAKEDQPAVPGETQGDSYFTGKKTIETVKAAERIMEAIELYREETAKMKEHKAICKAAGKEVPLPSNPILMAYGSISPSAYVLEIFKGIKSSELEESLLVLPFSYVPDILKLFNEFIQLGSDVELICRCLFFLLRIHFGQITSNQMLVPVIEKLRETTISKVSQVRDVIGFNMAGLDYLKRECEAKSEVMFFADATSHLEEKKRKRKKREKLILTLT
Protein: ASXL transcriptional regulator 2 (D3Z8N9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase BAP1
- Forkhead box protein K1
- Host cell factor 1
- ASXL transcriptional regulator 1
- Forkhead box K2
- ASXL transcriptional regulator 3
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Histone-lysine N-methyltransferase EZH2
- SUZ12 polycomb repressive complex 2 subunit
- Chromobox homolog 8
Sequence:
MFKEELYGISSKVSSRLSQPSSPQSSCPSPTIPASKVISPSQKHSKKALKQALKQQQQKKQQQQQQQQCRPSMSISNQHLSLKTVKTASDSVPAKPALWEGKQSDGQSSSPQNSNSSFSSSVKVESSLLGLGKKSLQRSDRLHTRQMKRTKCADIDVETPDSILVNTNLRALINKHTFSVLPGDCQQRLLLLLPEVDRQVGPDGLMKLNGSALNNEFFTSAAQGWKERLSEGEFTPEMQVRIRQEIEKEKKVELWKEQFFESYYGQSSGLSLEDSQKLTASPSDPKANKSPAEQPKSILPSEASPVSTIPVFPQSECKEEAVQIPSPFKKESQDEARPISQSPETVLALASNTNELITVKPIKSPKDEGLLEQKPVASAEQESEKENHVTTSSSNESENQEALAISASKPKNAGFEKPTTTKPAGASPLGPDMQVPPAPVSDHIPESLKRKAALTQEEATSSWEKRPRITENRQHQQPFQASPQPFLNRGDRAQVRKVPPLKIPVSRISPMLFSTSQVSPRARFPVSITSPYRTGARTLADIKAKAQLVKAQKAAAAAAAAAAAAASVGGTIPGPVPGGGRSPREGGERKTAGGGSAGSDPVSTNGKGPALELAGTGSRGGTRELLPCDPQPETNTPGQAQPPGVSGAQLQQTSSVPAGLAASGTCTSVPLPAHIEMSNREKPNPHRATATAASPCHSQEPRSCRLERALSPTGPPLISGASPVCFVADGTVEPKAGSNKNAPKPSALTKTTASAPLDMTSSPVTSLLTTASLEKLPAPQISGAATSTGSAPSSSTLPVASSLKTPGTSANMNGPVSRPSSSIPANNPLVTQLLQGKDVPLEQILPKPLTKIEMKTVPLHTKEERGGIGVFPGTSVVEGSREDVSGRQAHLAIQQLGKPLQSKQLSQAPRPVCPAKDRKDPCIDTHQYQEGLSKTTQGQLFQTLIQRAQRQSVLSFVPPTQFNFAHSGFHLEDISTSQKFMLGFAGRRTSKPAMAGHYLLNISTYGRGTDSVKRTHSVNPEERFCLSSPTEALRVGHADCKNTTGESSSSKEEESDEDSVGDEQESVSVKEEPWAPHSGEAPSTNDCLASKSGKTEVPVNEQTTLGKENYILSRGQTFDEKTLARDFIQATHKQMAHAVRGKTVCSSPELFNSTALSLPADSPTHQPLLLPPLQTPKLYGSPTQIGPSYRGMINVSTSSDMDHNSAIPGSQVSSNVGDVMSFSVTVTTIPASQAMNPSSHGQTIPVQTFPDENSIEDTPSKCYCRLKAMIMCKGCGAFCHDDCIGPSKLCVSCLVVR
Protein: Aldehyde-alcohol dehydrogenase (Q6Q3I0)
Organism: Listeria ivanovii
Interaction partners:
Sequence:
MAIKENAAQEVLEVQKVIDRLADNGQKALKAFENYDQEQVDNIVHAMALAGLDQHMPLAKLAVEETGRGLYEDKCIKNIFATEYIWNNIKNNKTVGVINEDVQTGVIEIAEPVGVVAGVTPVTNPTSTTLFKAIIAIKTRNPIIFAFHPSAQGCSSAAAKVVYDAAIAAGAPEHCIQWVEKPSLEATKQLMNHEKVALVLATGGAGMVKSAYSTGKPALGVGPGNVPAYIDKTAXIKRSVSDIILSKSFDQGMICASEQAVIVDKEVAKEVKAEMEANKCYFVKGAEFKKLESYVINPEKGTLNPDVVGKSPAWIANQAGFKIPEDTKILVAEIKGVGDKYPLSHEKLSPVLAFIEAANQTEAFDRCEEMLVYGGLGHSAVIHSTDKEVQKAFGIRMKACRIIVNAPSAQGGIGDIYNGFIPSLTLGCGSYGKNSVSQNVSATNLLNVKRIADRRNNMQWFKLPPKIFFEKYSTQYLQKMEGVERVFIVTDPGMVQFKYVDVVIEHLKKRGNDVSYQVFADVEPDPSDVTVYKGAELMKDFKPDTIIALGGGSAMDAAKGMWLFYEHPEASFFGLKQKFLDIRKRTFKYPKLGGKAKFVAIPTTSGTGSEVTPFAVITDKENNIKYPLADYELTPDVAIVDAQYVTTVPAHITADTGMDVLTHAIESYVSVMASDYTRGVSIRAIELVFENLRDSVLKGDPDAREKMHNASALAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVIRYNALKPRKHALFPRYESFRADEDYARISRIIGFPAATTEEGVKSLVDEIIKLGKDVGIDMSLKGQNVAKKDLDAVVDTLADRAFMDQCTTANPKQPLVSELKEIYLEAYKGV
Protein: AP-3 complex subunit beta (Adaptor protein complex AP-3 beta subunit) (Adaptor-related protein complex 3 subunit beta) (Beta-3-adaptin) (Clathrin assembly protein complex 3 beta large chain) (Q556J8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Part of the AP-3 complex, an adaptor-related complex which is essential for the compartmentalization of the endocytic pathway.
Subcellular location: Endosome membrane {ECO:0000250}.
Interaction partners:
- AP-3 complex subunit mu
- AP-3 complex subunit delta
- AP-3 complex subunit sigma
- AP-1 complex subunit gamma
- AP-2 complex subunit alpha-2
- Arpin
- AP-4 complex subunit epsilon
- AP-1 complex subunit beta
- AP-1 complex subunit mu
- AP-2 complex subunit mu
Sequence:
MDTVLNNINQSRYFNDSTANTKIEEIKKHLDSPSDADKLESMKKLIAMLSKGRDVSEAFPQVVKNVIVKNLEIKKLVYMYLVHYAESQNDSALLSINTIQKSLNDQSQVIRASALRVMSSIRVIDIIEVIILAIEKSVKDTSPFVRKAAAFAIAKVHKLDCDKQEPLIDLLEILLNDTSTMVLGAAIVAFNELCPQRFDLLHQHYRKICQLLADFDEWSQVIVLDILTKYARSQFRCPDSTMNDKNIKQFKKKSKSFYSDEEDQEDDEPENSLYKKKPLERDMFDSSEEIDMDHRLLLKSTLPLLQSRNNAVVMAVSSLYFYCAPSIEAQKVGKSLVRILRSGPEVQYITLTNISTMVTLRPSMFEPHLSEFFIHSSDPEYSIKLKLEILTRLATPENIGKILKEFKEYVKNEDKKFVAATIQAIGSCASTVPDVTESCIYGLMSLLSNQSTVVVAESVIVLKRLLQLNATNEKLEKLEKEKEKEKDVKENQSTISKHSSSNNSIKYDNIILHLSKLLDTLQVPSARASIVWVIGEYCYRVPLVAPDVFRKLVKSFSDEHESVKLETLNLGSKLYVQFTDNNSTTTTDNSIPNEFKNERTKEKITLMFQYVLNLAKFDQNYDIRDNSRMLKHFYFNTENTQSINSNIKQIVINQKPIPTETSISEDRQRFTLGSLSHIVNHTALGYTALPDFPDVAPDPSVREPIQRWIPNQQSQQQQHQQQQLNNIFVDTPFYSDEEEEDEEEYDEEEEEEEYEEQNEYEDFFGEEKKNKKKNRKQQNYDEDEYNQDIDDGEYDGEGEVQAEDEDDFDELFGITNDDNNQTANGIGGGGSGEEEMDKFDFENYINSTTKSVKKILLKPTISGGLSIDYCFIRIRDNEEFSCQPRYNIIQLNIKNQSDETFTDISIINKNLIDGADISEFDPIESIEPNQAIQKQIYVLFNSTSQSCKFEISFNKGNFPVTLTPIIGELLIPIVPIYESISQWKDEFEEVGEFKQVDDQFEFGDQCLDKLNNNNNNNNNNNNESGDENIGLMPILPIVLEGINLIPIASNKLKSKIQFASKTLLKDENIYVQIQLLKQQPPTVNCIIRSNDQVVSALLLKKLKDVLQK
Protein: Protein amnionless (Q9VPN2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required in the nephrocyte for normal uptake of proteins and elimination of toxins, and for maintenance of endocytic trafficking structures. May function together with Cubn.
Subcellular location: Cell membrane {ECO:0000305|PubMed:23264686}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Cubulin 2
- Cubilin homolog
- Sol1, isoform C
- GEO10215p1
Sequence:
MGLHWQWLIWALVGLHVALATKWYGGGMDFNDPTAWLDDHLPCAQDLVVFPEYYPALLPLPEDISIDGLVFPREGAILLAEESTITFGSDKQPSCESDENKAYLKPPKSSKWFDPGTWTDKSKEFSTFTPELERIPCDDEQVIIKGHGPLAFDLENVQYLRLGQLILAGSSISKTYLEQLISRDLGQFLFYNAEYVQVEYYRGELCGCHKDFERLLEPVCHNVQEQCETPHCLSPVRPLGSCCLICGAILSTPTTHCTEGSRKELVAQISNLISQESLKDQIGLHVEFVGSQKFGNCLQAVVTDRHKYSERSLEFLQQNEHNWNKTGTTLKVSGRPYNPNVSFSSIVLILFCMALVGLVSVVILAHFMPENPYLNRIPQWIHDPRLWRWRHLGLRLRRNLLFNRFDNGGAEGGSSEGGASGVDRLGIMAYDPESGEVRERAFDNPMFEQGGALEEAAKESQEQDEILSVPKMETGDLDARSVVDEQELTEINLETCEADTDEETI
Protein: Mitochondrial sodium/calcium exchanger protein (Sodium/calcium exchanger 9) (O16242)
Organism: Caenorhabditis elegans
Function: Mitochondrial sodium/calcium antiporter that mediates sodium-dependent calcium efflux from mitochondrion, thereby acting as a key regulator of mitochondrion calcium homeostasis (Probable). Required for patterning of neural circuits: functions in the same pathway as RAC-dependent effectors of the unc-6/netrin signaling pathway to set left/ right patterning of the VD/DD GABAergic circuit.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:28196860}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Calx-beta domain-containing protein
- Calx-beta domain-containing protein
- Calx-beta domain-containing protein
- Calcium homeostasis modulator protein
Sequence:
MCSSEECLIDKSWTSEEKCEYIKCNQDSCEGGGYLTWSHYVKCQYNIGVRVILIILGILYLIILFVIMSSIADDFFCPAISGIVSHLRMSESIAGVTFLAFGNGAPDVFSSISSVLTTPKPKADLALGDLFGTSIFVTTVVLAIIIFTKSFKVAIIPTLRDLIFYMTTLAFIVFCFLKFDKIEVWMPATFLGIYGVYVVTVIILGIYRTHRKKRNLKKKNKELEDFLSRPSSAASTTPIFGAMKLKEETISVSALFHFMIGYSQFIKNLTRANLKRTTNNNNNDNKNEKRGIVNLGFSEPYSIPSERKISTIFKQNTFETDLESLESLADLDGSDDEGREEKFGYAHHTVFTSHDQISLVASEIEEIEITTWRSWDWVWDLFNHLKSWPSRDEFSEMNIFIKIVTVIKVVPVFFFKLTVPSNEMSWCKPLFILHCFASIQFALFSIQIITLKPFDGSPGLWLYGLGFSAILAMVAMYFLPLSKEQKYYKEIYSYLGFLMSIAWIYATSNEIVSVVTMIGVVTGLSMELLGLTIMAWSNCIGDIVADIAVVKQGYPKMAMAAAIGGPLFNLLIGFGLPFTIAAAQGKEMELLINPVYRLLMLFLGISLVTTFVALFIQRFTVRRPHAVLLIFIFVVFLIFICLAEFHVLEWN
Protein: Ribosomal RNA small subunit methyltransferase NEP1 (EC 2.1.1.-) (18S rRNA (pseudouridine-N1)-methyltransferase) (Q9P8P7)
Organism: Candida albicans (Yeast)
Function: S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates the pseudouridine corresponding to position 1189 (Psi1189) in S.cerevisiae 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-ribosomes.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11935223}.
Interaction partners:
Sequence:
MSELKNGTTEPKKNETTQSDSKSKSTSTNKSSVPPASLVPVQPTALTSRDKTTQRLIVVLSQACLETYKMNSGGPGGDRFALLNCDDHQGLLRKMGRDIAEARPDITHQCLLTLLDSPINKAGRLQVYIQTARGVLIEVNPSVRIPRTFKRFSGLMVQLLHKLSIRSENSKEVLLKVIKNPITDHLPTKCRKVTLSFDAELKRVQDYVTTLDENESICVFVGAMARGKDNFADEFVDEKIGLSDYPLSASVACSKFCHGCEDVWGIY
Protein: Biogenesis of lysosome-related organelles complex 1 subunit 2 (BLOC-1 subunit 2) (Q9CWG9)
Organism: Mus musculus (Mouse)
Function: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes (By similarity). In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6QNY1}. Lysosome membrane {ECO:0000250|UniProtKB:Q6QNY1}. Note=Localizes to the centrosomes in a microtubule-dependent manner. {ECO:0000250|UniProtKB:Q6QNY1}.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- Biogenesis of lysosome-related organelles complex 1 subunit 3
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- SNARE-associated protein Snapin
- BLOC-1-related complex subunit 8
- Dysbindin
- KxDL motif-containing protein 1
- Biogenesis of lysosome-related organelles complex 1 subunit 4
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- BLOC-1-related complex subunit 7
Sequence:
MAAAAEGVPATRREEQPPRDDAAVETAEEAKEPAEADINELCRDMFSKMATYLTGELTATSEDYKLLENMNKLTSLKYLEMKDIAINISRNLKDLNQKYAELQPYLDQINMIEEQVAALEQAAYKLDAYSKKLEAKYKKLEKR
Protein: Apoptosis inhibitor 5-like protein API5 (Protein APOPTOSIS INHIBITOR 5) (Q6Z6S1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Putative anti-apoptotic factor involved in the regulation of tapetal programmed cell death (PCD) and degeneration during anther development. Interacts directly with the DEAD-box ATP-dependent RNA helicases AIP1 and AIP2 that form dimers and bind the promoter region of the cysteine protease CP1 involved in tapetum PCD.
Subcellular location: Nucleus {ECO:0000269|PubMed:21467577}.
Interaction partners:
- DNA-directed RNA polymerase
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit beta''
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase
- DNA-directed RNA polymerase subunit beta
Sequence:
MAASDADAAEVERLYELGERLSSAKDKSQHAADYEAIISAVKGQSVKAKQLAAQLIPRFFRSFPALAPRAMEAMFDLVDMEELATRIQAIRGFPLLAKDAEFVSKIADILGQLLASEENVERDAVHKALMSLIRQDVKSSLQPLFKHVESGSEIREKVICFLKDKVFPVKAELLKPQAEMERYITDLIKKSVLDVTGLEFKLFMDFLRSLSIFGDSAPRESFQELIEIIQAQADLDAQFNVSDIDHIERWTSCMYMALPIFMRGGSSSKFLNYFVKQIVPVFDKIPEEKKLDLLKTVAASSPYATAQDARQLLPPVVQLLKKYMPGKKVEDINHNYVECLMYIFHHLAHKTPNTTNSLCGYKIVTGQPSDRLGEDFSEHYKDFTERLTGTEETVRAVSKRLTQGMADFNKAISSAKTEEEKTKIKSDQQKSTMTMRAYNNILAMAQPLRAKSPLFIGDKKITLSWMEQPKKPAPTTTGGKRSQPATNGNTPASKKGRGEGAARNQLVNRAFEGLSRGGRGSGRGRGRGGRGRGWGYR