wanglab/gogpt-training-data huggingface dataset:
Protein: Potassium voltage-gated channel subfamily A member 6 (RCK2) (Voltage-gated potassium channel subunit Kv1.6) (Voltage-gated potassium channel subunit Kv2) (P17659)
Organism: Rattus norvegicus (Rat)
Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KNCA5, KCNA6, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (Probable). Homotetrameric channels display rapid activation and slow inactivation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1993474}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Potassium voltage-gated channel subfamily A member 1
- Voltage-gated potassium channel subunit beta-2
- Voltage-gated potassium channel subunit beta-1
- Potassium voltage-gated channel subfamily A member 2
- Voltage-gated potassium channel subunit beta-3
- FAU ubiquitin like and ribosomal protein S30 fusion like 2
- Ubiquitin-like protein FUBI
- Calcium-activated potassium channel subunit alpha-1
Sequence:
MRSEKSLTLAAPGEVRGPEGEQQDAGEFQEAEGGGGCCSSERLVINISGLRYETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFMEEIRFYQLGDEALAAFREDEGCLPEGGEDEKPLPSQPFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPQFRADGRGGSNEGSGTRMSPASRGSHEEEDEDEDSYAFPGSIPSGGLGTGGTSSFSTLGGSFFTDPFFLVETLCIVWFTFELLVRFSACPSKAAFFRNIMNIIDLVAIFPYFITLGTELVQRHEQQPVSGGSGQNRQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADDVDSLFPSIPDAFWWAVVTMTTVGYGDMYPMTVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEQEEQGQYTHVTCGQPTPDLKATDNGLGKPDFAEASRERRSSYLPTPHRAYAEKRMLTEV
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (D3ZZK3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Early endosome {ECO:0000256|ARBA:ARBA00004412}.
Interaction partners:
- Ephrin-B3
- Ephrin B2
- Ephrin-A4
- Ephrin-A1
- Ephrin-A3
- Ephrin A2
- Ephrin-A5
- Ephrin-B1
- Ephexin-1
- Tyrosine-protein kinase
Sequence:
MAGIFYFILFSFLFGICDAVTGSRVYPANEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEASQNNWLRTDWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRESQFGKIDTIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVEVRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGHEEQNGECQACKIGYYKALSTDATCAKCPPHSYSVWEGATSCTCDRGFFRADNDAASMPCTRPPSAPLNLISNVNETSVNLEWSSPQNTGGRQDISYNVVCKKCGAGDPSKCRPCGSGVHYTPQQNGLKTTRVSITDLLAHTNYTFEIWAVNGVSKYNPSPDQSVSVTVTTNQAAPSSIALVQAKEVTRYSVALAWLEPDRPNGVILEYEVKYYEKDQNERSYRIVRTAARNTDIKGLNPLTSYVFHVRARTAAGYGDFSEPLEVTTNTVPSRIIGDGANSTVLLVSVSGSVVLVVILIAAFVISRRRSKYSQAKQEADEEKHLNQGVRTYVDPFTYEDPNQAVREFAKEIDASCIKIEKVIGVGEFGEVCSGRLKVPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIHLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGMLRGIGSGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPIALHQLMLDCWQKERSDRPKFGQIVNMLDKLIRNPNSLKRTGPESSRPNTALLDPSSPEFSAVVSVGDWLQAIKMDRYKDNFTAAGYTTLEAVVHMSQE
Protein: ORF K10 (P88947)
Organism: Human herpesvirus 8 type M
Interaction partners:
Sequence:
MGSSGTRQVTQASSFTWRVPGDPPAPSTLTGPSDPHSSGAGLPGTAPPKPQHETRLAGTVSGVSGVAQTPGDTGQLAPPMRDGSRLPSTSPWIPACFPWGDLPVTGWWPQGASGLPEKVHPPTTGQFDPLSPRWTYTGIPSSQLNPAAPSWIPPHAQAGTFVGEFSQGAPLAPQGLLPQSGQCARAWLPRRETGAEGACGASTEGRAPQGAASERVYPFEPQPPSAPAPGYAKPSCYNWSPLAEPPATRPIRAPVWHPPVGHAVVPEVRTPLWIPWSSGGAPNQGLSHTQGGASATPSAGAPPTPEVAERQEPSSSGIPYVCQGDNMATGYRRVTTSSGALEVEIIDLTGDSDTPSTTVASTPLPVSGPRVFQPTVLYSAPEPAVNPEVSHLPTELERRECVCPGSGERPRVPLVSTYAGDRYAVGGYGPEQSLVPPPLGLPLTLSNLQGEDICTWEEGLGNILSELQEEPSSSTRQATDRRRPRSRSPHGRRTPVSHSGPEKPPSKMFFDPPDSQRVSFVVEIFVYGNLRGTLRREGDAGEAMLCSWPVGDTLGHLCQSFVPELLRIPRLTVPSPEQMEILNRVFEGLGHGFPIFCSMSGIYSRNATQVEGWWFGNPNSRYERILRSFSPRVPQQLFNTARYLATTAAIPQTPLSVNPVTCGTVFFGASPASTENFQNVPLTVKIFIGSIWDSLH
Protein: GIG10 (Migration-inducing gene 18 protein) (cDNA, FLJ93821, Homo sapiens SH3-domain kinase binding protein 1 (SH3KBP1), mRNA) (Q5JPT6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVEAIVEFDYQAQHDDELTISVGEIITNIRKEDGGWWEGQINGRRGLFPDNFVREIKKEMKKDPLTNKAPEKPLHEVPSGNSLLSSETILRTNKRGERRRRRCQVAFSYLPQNDDELELKVGDIIEVVGEVEEGWWEGVLNGKTGMFPSNFIKELSGESDELGISQDEQLSKSSLRETTGSESDGGDSSSTKSEGANGTVATAAIQPKKVKGVGFGDIFKDKPIKLRPRSIEVENDFLPVEKTIGKKLPATTATPDSSKTEMDSRTKSKDYCKVIFPYEAQNDDELTIKEGDIVTLINKDCIDVGWWEGELNGRRGVFPDNFVKLLPPDFEKEGNRPKKPPPPSAPVIKQGAGTTERKHEIKKIPPERPEMLPNRTEEKERPEREPKLDLQKPSVPAIPPKKPRPPKTNSLSRPGALPPRRPERPVGPLTHTRGDSPKIDLAGSSLSGILDKDLSDRSNDIDLEGFDSVVSSTEKLSHPTTSRPKATGRRPPSQSLTSSSLSSPDIFDSPSPEEDKEEHISLAHRGVDASKKTSKTVTISQVSDNKASLPPKPGTMAAGGGGPAPLSSAAPSPLSSSLGTAGHRANSPSLFGTEGKPKMEPAASSQAAVEELRTQVRELRSIIETMKDQQKREIKQLLSELDEEKKIRLRLQMEVNDIKKALQSK
Protein: Protein phosphatase 2C 37 (AtPP2C37) (EC 3.1.3.16) (Protein ABA-HYPERSENSITIVE GERMINATION 3) (Protein phosphatase 2C A) (PP2CA) (P49598)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Major negative regulator of abscisic acid (ABA) responses during seed germination and cold acclimation. Confers insensitivity to ABA. Modulates negatively the AKT2/3 activity, which mediates K(+) transport and membrane polarization during stress situations, probably by dephosphorylation. Prevents stomata closure by inactivating the S-type anion efflux channel SLAC1 and its activator SRK2E. Represses KIN10 activity by the specific dephosphorylation of its T-loop Thr-198, leading to a poststress inactivation of SnRK1 signaling.
Interaction partners:
- Abscisic acid receptor PYL13
- Serine/threonine-protein kinase SRK2D
- Abscisic acid receptor PYL4
- Abscisic acid receptor PYR1
- Serine/threonine-protein kinase SRK2E
- Abscisic acid receptor PYL8
- Abscisic acid receptor PYL10
- Abscisic acid receptor PYL5
- Abscisic acid receptor PYL12
- Serine/threonine-protein kinase SRK2I
Sequence:
MAGICCGVVGETEPAAPVDSTSRASLRRRLDLLPSIKIVADSAVAPPLENCRKRQKRETVVLSTLPGNLDLDSNVRSENKKARSAVTNSNSVTEAESFFSDVPKIGTTSVCGRRRDMEDAVSIHPSFLQRNSENHHFYGVFDGHGCSHVAEKCRERLHDIVKKEVEVMASDEWTETMVKSFQKMDKEVSQRECNLVVNGATRSMKNSCRCELQSPQCDAVGSTAVVSVVTPEKIIVSNCGDSRAVLCRNGVAIPLSVDHKPDRPDELIRIQQAGGRVIYWDGARVLGVLAMSRAIGDNYLKPYVIPDPEVTVTDRTDEDECLILASDGLWDVVPNETACGVARMCLRGAGAGDDSDAAHNACSDAALLLTKLALARQSSDNVSVVVVDLRKRRNNQASS
Protein: Malate dehydrogenase, mitochondrial (EC 1.1.1.37) (P17505)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:11502169}.
Interaction partners:
- Citrate synthase, mitochondrial
- Citrate synthase, peroxisomal
- Fumarate hydratase, mitochondrial
- Citrate synthase 3, mitochondrial
- Aspartate aminotransferase, mitochondrial
- Pyruvate carboxylase 2
- Malate synthase 1
- Pyruvate carboxylase 1
- NAD-dependent malic enzyme, mitochondrial
- Phosphoenolpyruvate carboxykinase
Sequence:
MLSRVAKRAFSSTVANPYKVTVLGAGGGIGQPLSLLLKLNHKVTDLRLYDLKGAKGVATDLSHIPTNSVVKGFTPEEPDGLNNALKDTDMVLIPAGVPRKPGMTRDDLFAINASIVRDLAAATAESAPNAAILVISNPVNSTVPIVAQVLKNKGVYNPKKLFGVTTLDSIRAARFISEVENTDPTQERVNVIGGHSGITIIPLISQTNHKLMSDDKRHELIHRIQFGGDEVVKAKNGAGSATLSMAHAGAKFANAVLSGFKGERDVIEPSFVDSPLFKSEGIEFFASPVTLGPDGIEKIHPIGELSSEEEEMLQKCKETLKKNIEKGVNFVASK
Protein: Sortase (Sortase A) (Q9S446)
Organism: Staphylococcus aureus
Interaction partners:
Sequence:
MKKWTNRLMTIAGVVLILVAAYLFAKPHIDNYLHDKDKDEKIEQYDKNVKEQASKDKKQQAKPQIPKDKSKVAGYIEIPDADIKEPVYPGPATPEQLNRGVSFAEENESLDDQNISIAGHTFIDRPNYQFTNLKAAKKGSMVYFKVGNETRKYKMTSIRDVKPTDVGVLDEQKGKDKQLTLITCDDYNEKTGVWEKRKIFVATEVK
Protein: Cytochrome P450 83B1 (EC 1.14.14.45) (Protein ALTERED TRYPTOPHAN REGULATION 4) (Protein RED ELONGATED 1) (Protein SUPERROOT 2) (O65782)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the metabolism of aromatic oximes. Catalyzes the oxime metabolizing step in indole glucosinolate biosynthesis by converting indole-3-acetaldoxime into indole-3-S-alkyl-thiohydroximate. Probably required for glucosinolate activation in response to pathogens. Functions in auxin homeostasis because indole-3-acetaldoxime also serves as a precursor for auxin biosynthesis. Specifically metabolizes (E)-p-hydroxyphenylacetaldoxime into an S-alkyl-thiohydroximate.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- S-alkyl-thiohydroximate lyase SUR1
- Cytosolic sulfotransferase 16
- Tryptophan N-monooxygenase 1
- Tryptophan N-monooxygenase 2
- UDP-glycosyltransferase 74B1
- Indoleacetaldoxime dehydratase
- Cytochrome P450 71A12
- Cytochrome P450 71A18
- Transcription factor HFR1
- Cytosolic sulfotransferase 17
Sequence:
MDLLLIIAGLVAAAAFFFLRSTTKKSLRLPPGPKGLPIIGNLHQMEKFNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMKRFIDILYETQALLGTLFFSDLFPYFGFLDNLTGLSARLKKAFKELDTYLQELLDETLDPNRPKQETESFIDLLMQIYKDQPFSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRSVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDNPNEFIPERFMNEHKGVDFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPKGIKPEDIKMDVMTGLAMHKKEHLVLAPTKHI
Protein: Starch synthase 2, chloroplastic/amyloplastic (AtSS2) (EC 2.4.1.21) (Soluble starch synthase II) (Q9MAC8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the synthesis of glycan chains within amylopectin in leaves. Is required to produce chains with a degree of polymerization of 12 to 25 (DP12-DP25).
Subcellular location: Plastid, chloroplast. Plastid, amyloplast {ECO:0000305}.
Interaction partners:
- 1,4-alpha-glucan-branching enzyme 2-2, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- 1,4-alpha-glucan-branching enzyme 3, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE2
- 1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 3, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 2, chloroplastic
- Probable glucose-1-phosphate adenylyltransferase large subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic
Sequence:
MASVAESSFPLLCQIKTQRRINSSTLRHSRVSYHDLPSGSLSFRSRSFVLGHRCKCVSRVEASGSDDDEPEDALQATIDKSKKVLAMQRNLLHQIAERRKLVSSIKESTPDLDDAKASSKQESASSVNANTDATKKEIMDGDANGSVSPSTYGKSSLSKEPEAKTFSPSTESLKNRKQSSASVISSSPVTSPQKPSDVATNGKPWSSVVASSVDPPYKPSSVMTSPEKTSDPVTSPGKPSKSRAGAFWSDPLPSYLTKAPQTSTMKTEKYVEKTPDVASSETNEPGKDEEKPPPLAGANVMNVILVAAECAPFSKTGGLGDVAGALPKSLARRGHRVMVVVPRYAEYAEAKDLGVRKRYKVAGQDMEVMYFHAFIDGVDFVFIDSPEFRHLSNNIYGGNRLDILKRMVLFCKAAVEVPWYVPCGGVCYGDGNLAFIANDWHTALLPVYLKAYYRDHGIMKYTRSVLVIHNIAHQGRGPVDDFSYVDLPSHYLDSFKLYDPVGGEHFNIFAAGLKAADRVLTVSHGYSWEVKTLEGGWGLHNIINENDWKFRGIVNGIDTQEWNPEFDTYLHSDDYTNYSLENLHIGKPQCKAALQKELGLPVRPDVPLIGFIGRLDHQKGVDLIAEAVPWMMSQDVQLVMLGTGRPDLEEVLRQMEHQYRDKARGWVGFSVKTAHRITAGADILLMPSRFEPCGLNQLYAMNYGTIPVVHAVGGLRDTVQQFDPYSETGLGWTFDSAEAGKLIHALGNCLLTYREYKESWEGLQRRGMTQDLSWDNAAEKYEEVLVAAKYHW
Protein: Elongation factor Tu (EF-Tu) (C2E605)
Organism: Lactobacillus johnsonii ATCC 33200
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
Interaction partners:
Sequence:
MAEKEHYERTKPHVNIGTIGHVDHGKTTLTAAITTVLAEDGLAQAEDYSQIDAAPEEKERGITINTAHVEYETKNRHYAHMDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVQYIVVFLNKVDLVDDPELIDLVEMEVRDLLSEYDYPGDDVPVIRGSALKALEGDPEQQDVIRKLMETVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVASGRIDRGTVKVGDEVEIVGLTDKIEKSTVTGLEMFHKTLDLGEAGDNVGVLLRGIDRDQVERGQVLAAPGSIQTHKNFKGQVYILNKDEGGRHTPFFSDYRPQFYFHTTDVTGKIELPEGTEMVMPGDNVEFTVELIKPVAIEKGTKFTIREGGKTVGAGQVTEILD
Protein: Ras GTPase-activating protein 1 (Q3TTA2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
ETPEQAEDWMKGLQAFCSLRKSSPGTSNKRLRQVSSLVLHIEEAHKLPVKHFTNPYCNIYLNSVQVAKTHAREGQNPVWSEEFVFDDLPPDINRFEITLSNKTKKSKDPDILFMRCQLSRLQKGHATDEWFLLSSHIPLKGIEPGSLRVRARYSMEKIMPEEEYSEFKELILQKELHVVYALSHVCGQDRTLLASILLKIFLHEKLESLLLCTLNDREISMEDEATTLFRATTLASTLMEQYMKATATQFVHHALKDSILKIMESKQSCELSPSKLEKNEDVNTNLAHLLSILSELVEKIFMASEILPPTLRYIYGCLQKSVQHKWPTNNTMRTRVVSGFVFLRLICPAILNPRMFNIISDSPSPIAARTLTLVAKSVQNLANLVEFGAKEPYMEGVNPFIKSNKHRMIMFLDELGNVPELPDTTEHSRTDLSRDLAALHEICVAHSDELRTLSNERGVQQHVLKKLLAITELLQQKQNQYTKTNDIR
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q961J4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPTPRYEAELNALHDIVRQAVLSLLTDSQPVVKQTLMESGICDLCAFFGKEKANDVILSHIMTFLNDEDKNLRGAFYDNIAGVAGYVGWQASDILVPLLQQGFTDREEFVIAKAIRAVTILIELGHIKKPAVTEIVQETACYLCHPNLWVRHEICGMIATTARNLSAIDVQCKIMPAIGAFLKAPLIQVEKPHILLDCVHPPVPRQIFDSVLRFQDIHHFIRALEARSRVRSQTRQGALPQYEEMGQTLRNLFRRLSSEGLTDLIEMQLLAMNPFLISMKHKALQDLDDTASGNGRIVVSRKQVACHEYPLADKASKMPLDNRSSEGPTLASPASDAAITPLGAGGLAGSPASGAVVLGVPTATVSAATSLGEYTMPERNCWLERSSECRKDLESLTAKIKSRYNVLAISQRCSYDKLVTPYPPGWRMTGTLVAHLHEHSESVIKLASLRPHGSLFASGSIDGTVRLWDCSKLNGNQGVNKSRQVYSANTPIYALAACDSGQSLAVGGKDGSMLMMRIDRNSAKMTLQQALNQNDHKDGPVVDMHAYDQATQSVIVYATLYGGIVAWDTRMQHSAWRLQNELRHGVITTICADPTGSWLATGTSGGKHICWDLRFRLPIAEIKHPADSWIRKVACHPTEPSYLISASQSNNEVSVWNIETGQRQTVLWASPVAALSSASPSDPATTCGILSGVVDGSPFILTGSSDQRIRYWDITNPKNSSLKVPAANDNLADVAFNYGARLIDGSQVIEEQIISMASTGDSQQLRSSTEENPRSGPDMPTASHHDAITDLLMCKDKGQIYIASASRNGVIKLWK
Protein: V-type proton ATPase subunit C (V-ATPase subunit C) (Vacuolar proton pump subunit C) (Q9V7N5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity). In enterocytes, acts as part of a pHCl-2 sensory pathway which mediates Tor-dependent larval growth and metabolism in response to zinc availability. Likely acts in maintaining enterocyte lysosomal acidification which consequently promotes Tor activation at the lysosome membrane.
Interaction partners:
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B
- V-type proton ATPase subunit E
- V-type proton ATPase subunit G
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit D 1
- V-type proton ATPase subunit F 1
- V-type proton ATPase catalytic subunit A isoform 2
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase catalytic subunit A isoform 1
Sequence:
MMSEYWIISAPGDKTCQQTYDTMNNLTSKQHNLCNNYKFHIPDLKVGTLDQLVGLSDDLGKLDTYVEQITRKVANYLGEVLEDQRDKLHENLMANNSPGPPDDSMPCRHHQRIKHLSLRHQRKHQHTHHQNKPQHYHHHHHHHQLPQDLKGKSAATCSPATPPAPASAPPHLPPACACDVLAPGSLTGGSLTNLSTSHEPEPEFDVCPCDECFACAPPSTSATASTLLADECYSQTASSMLSATRCALSTVAAIATGSGLGNGPSTSAAAAAAASNSSGGGGGGGPASCSTLCSSAYFSTSAPTTSSSVHSSMSRSNSKRLNNNTCSINNNKLSFRSGSHVSQLHLATQQPQHHHSHPHQQPHTNPLQSPVQKSMSEDEGDASNAHEDGETDEDPKSPHSVQSDLSDAFDWWFNKPKRNSKKSSAQQQHETAQLQHQQTTQQHATPLTPQNHNQYQNQHLSKAMTFWHQASTTPRSSYRSFFNSLADQIYSKRSTPSQLNINNGFNLTPTHRSSPVSSCCGSSSQGRSSPDTDPAEPPEFPLSPAELPQYLTRFQWDMAKYPIKQSLRNIADIISKQIGQIDGDLKTKSQAYNNLKGNLQNLEKKKTGSLLTRNLADLVKKEHFILDSEYLTTLLVIVPKVMANDWLTNYEKITDMIVPRSSQLIQEDADYCLFNVTLFKKVAEEFKLHARERKFIVRDFVYNEEELAAGKNEMTKLMTDKKKQFGPLVRWLKVNFSEAFCALIHVKALRVFVESVLRYGLPVNFQAILIEPNKKSVKRLRDVLNQLYGHLDGASAGGAVSSADNVDIPGLGFGQSEYFPYVFYKVNIDMVEQAKV
Protein: Protein twist (P10627)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the establishment and dorsoventral patterning of germ layers in the embryo.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:3416836}.
Interaction partners:
- Myocyte-specific enhancer factor 2
- Protein snail
- Transcription factor Zelda
- Segmentation protein even-skipped
- Muscle-specific homeobox protein tinman
- Protein daughterless
- Protein zerknuellt 1
- Segmentation protein fushi tarazu
- Zygotic gap protein knirps
- Embryonic polarity protein dorsal
Sequence:
MMSARSVSPKVLLDISYKPTLPNIMELQNNVIKLIQVEQQAYMQSGYQLQHQQQHLHSHQHHQQHHQQQHAQYAPLPSEYAAYGITELEDTDYNIPSNEVLSTSSNQSAQSTSLELNNNNTSSNTNSSGNNPSGFDGQASSGSSWNEHGKRARSSGDYDCQTGGSLVMQPEHKKLIHQQQQQQQQHQQQIYVDYLPTTVDEVASAQSCPGVQSTCTSPQSHFDFPDEELPEHKAQVFLPLYNNQQQQSQQLQQQQPHQQSHAQMHFQNAYRQSFEGYEPANSLNGSAYSSSDRDDMEYARHNALSSVSDLNGGVMSPACLADDGSAGSLLDGSDAGGKAFRKPRRRLKRKPSKTEETDEFSNQRVMANVRERQRTQSLNDAFKSLQQIIPTLPSDKLSKIQTLKLATRYIDFLCRMLSSSDISLLKALEAQGSPSAYGSASSLLSAAANGAEADLKCLRKANGAPIIPPEKLSYLFGVWRMEGDAQHQKA
Protein: Emopamil-binding protein-like (Emopamil-binding-related protein) (Q9BY08)
Organism: Homo sapiens (Human)
Function: Does not possess sterol isomerase activity and does not bind sigma ligands.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12760743}; Multi-pass membrane protein {ECO:0000269|PubMed:12760743}.
Interaction partners:
Sequence:
MGAEWELGAEAGGSLLLCAALLAAGCALGLRLGRGQGAADRGALIWLCYDALVHFALEGPFVYLSLVGNVANSDGLIASLWKEYGKADARWVYFDPTIVSVEILTVALDGSLALFLIYAIVKEKYYRHFLQITLCVCELYGCWMTFLPEWLTRSPNLNTSNWLYCWLYLFFFNGVWVLIPGLLLWQSWLELKKMHQKETSSVKKFQ
Protein: Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (Dihydrolipoamide S-acetyltransferase component 1 of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex component E2 1) (PDC-E2 1) (PDCE2 1) (Q0WQF7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta-2, chloroplastic
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Pyruvate dehydrogenase E1 component subunit beta-3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-3, chloroplastic
- Dihydrolipoyl dehydrogenase 2, mitochondrial
- Dihydrolipoyl dehydrogenase 1, chloroplastic
Sequence:
MVLPLFRRAAIARTSSLLRARLFAPASEFHSRFSNGLYHLDDKISSSNGVRSASIDLITRMDDSSPKPILRFGVQNFSSTGPISQTVLAMPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKDIPVNEPIAIMVEEEDDIKNVPATIEGGRDGKEETSAHQVMKPDESTQQKSSIQPDASDLPPHVVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKDVAVGKPIALIVEDAESIEAIKSSSAGSSEVDTVKEVPDSVVDKPTERKAGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKASKSSASTKKKQPSKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKELQENHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGNKVVEPVIGLDGIEKPSVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL
Protein: Alpha/beta-Hydrolases superfamily protein (Phospholipase-like protein) (Putative phospholipase) (Q8VZV6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
Sequence:
MGLHPISDANEHNPFGSLTADEFYAKHSVSHSSAFITNPRGLKLFTQWWSPLPPTKPIGIIAVVHGFTGESSWFLQLTSILFAKSGFITCAIDHQGHGFSDGLIAHIPDINPVVDDCISFFDDFRSRQTPSDLPCFLYSESLGGAIALYISLRQRGVWDGLILNGAMCGISDKFKPPWPLEHLLFVVANLIPTWRVIPTRGSIPDVSFKEPWKRKLAMASPRRTVAKPRAATAYELIRVCKDLQGRFEEVEVPLLIVHGGGDVVCDVACVEELHRRAISEDKTIKIYPELWHQMIGESEEKVDLVYGDMLSWLKSRAERKARAAVDGGAA
Protein: Nodulin-like domain-containing protein (Q582K8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSAPVDNVVVERLSTANQKPINEPRRFALLVLGTFCCICTSFMYAFNLISGAMQARYNLTQRDLSTITTVGIAVGYFLLPYSFIFDYLGPKPIFVIAMTVFCLGALLFALTFQEVIEGSVVRLSVYNGFLTLGCMLFDLGSVVTVLSVFPSNRGAVMAIVKTFTGLGSAIVGSIQLAFFSKSVANYFFFLMSFSLVVGTLAVVFMNLPPFHLTGYQKTHLDEEEKAQRLARKGVYLKQKAPMWRFVHGFAILVTLIVFLPLQGALVAYLKLGSNFKVGFAVTVIVLTVIFPFMAYPLTTFDGKRPHDDSEGETCCRREVAEEVSASDDTGVETDVDYIAPQFQETFIEGLKTARLWCLLWSIFCCVGVHYVIIYNARFIYTALAGEAPDDALNALLTVLNGVGSAVGRLCMSYFEVWSQKRRAEDRVPITFSMFVPSVCIITMLTLFLTLPKAALPLPYFIAALSNGFTAAIIALVTRTIFAKDPAKHYNFCFLGSVLSAIFLNRLLYGEWYTQQADKLGQDVCTERVCVVMPLAFMLGLAFPAFATSTYLHLQYRRLCMLALDERRRIREGERGPKEPSSCPKEPTRDAREAAPQ
Protein: Nectin-1 (Herpes virus entry mediator C) (Herpesvirus entry mediator C) (HveC) (Nectin cell adhesion molecule 1) (Poliovirus receptor-related protein 1) (CD antigen CD111) (Q9JKF6)
Organism: Mus musculus (Mouse)
Function: Involved in cell adhesion and synaptogegesis. Has some neurite outgrowth-promoting activity. Receptor for alphaherpesvirus (HSV-1, HSV-2 and pseudorabies virus) entry into cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11827984, ECO:0000269|PubMed:21798896}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, adherens junction {ECO:0000269|PubMed:15328010, ECO:0000269|PubMed:15728677}. Presynaptic cell membrane {ECO:0000269|PubMed:11827984}; Single-pass type I membrane protein {ECO:0000255}. Note=In the auditory epithelium, specificaly localizes to the apical side of the lateral membranes of hair cells. {ECO:0000269|PubMed:21798896}.
Interaction partners:
- Afadin
- Nectin-3
- Partitioning defective 3 homolog
- Nectin-2
- Cell adhesion molecule 3
- Nectin-4
- Cadherin-1
- Tumor necrosis factor receptor superfamily member 14
- T-cell immunoreceptor with Ig and ITIM domains
- Major prion protein
Sequence:
MARMGLAGAAGRWWGLALGLTAFFLPGTHTQVVQVNDSMYGFIGTDVVLHCSFANPLPSVKITQVTWQKASNGSKQNMAIYNPTMGVSVLPPYEKRVEFLRPSFIDGTIRLSGLELEDEGMYICEFATFPTGNRESQLNLTVMAKPTNWIEGTRAVLRARKGQDDKVLVATCTSANGKPPSAVSWETRLKGEAEYQEIRNPNGTVTVISRYRLVPSREAHRQSLACIVNYHLDRFRESLTLNVQYEPEVTIEGFDGNWYLQRTDVKLTCKADANPPATEYHWTTLNGSLPKGVEAQNRTLFFRGPITYSLAGTYICEATNPIGTRSGQVEVNITEFPYTPTPEHGRRAGQMPTAIIGGVAGSVLLVLIVVGGIIVALRRRRHTFKGDYSTKKHVYGNGYSKAGIPQHHPPMAQNLQYPDDSDDEKKAGPLGGSSYEEEEEEEGGGGGERKVGGPHPKYDEDAKRPYFTVDEAEARQDGYGDRTLGYQYDPEQLDLAENMVSQNDGSFISKKEWYV
Protein: Hepatoma-derived growth factor-related protein 3 (Zgc:92612) (Q5FVD1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MARPRPREYKAGDLVFAKMKGYPHWPARIDELPEGAVKPPANKYPIFFFGTHETAFLGPKDLLPYKDYKDKFGKSNKRKGFNEGLWEIENNPGVKFTGFQVMQQSSSETEGEGGNAADGSSDGDSAAEEDEAQMKSDKAGSKRKKSTSSKVSKQCRKGSGDEDLERDGKDEQKSGSEAGDHDNNIQNSSDKTSPGTLREDH