wanglab/gogpt-training-data huggingface dataset:
Protein: Killer cell lectin-like receptor subfamily A member 16 (Q4Z8P4)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MSEQEVTFSTVRFQKTSGLQNRVRLEETLKPRKAGLRVCSVSWQFIVIALGILISLRLVIVAVLVTNIFQYGQQKHELQEFLNHHNNCSIMQSDIKLKNELLKKKSIECNLLESLNRDQNRLYNKTKTVLDFLQHTGRGDKVYWFCYGMKCYYFVMDRKPWSGCKQTCQSSGLSLLKIDDEDELKFLQLVVPSDVCWIGLSYDNKKKDWSWVDNGPSKLALNTRKYNIRDGGCMLLSKTRLDNGNCDQVFICICAKRLDKFPH
Protein: Non-specific lethal 1, isoform J (E1JIM1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAPALTAEPLSPKEKLTSTASPSARSSSESGGVGCAVGLVKKPATPTPATATTRITRSSAAAASVTASPHLQQQRSSLAINNKRKSGNAKASNEPMGLSTAPTPHSTTSPNPSTDTAAASTSAVEHNNNDSNSTSAGNSTSADNSSTPKDNSTAQLLADLTINFEETISAEICLRKTLPDVSLGKEPVPPASVLAVATSSTSAGSALSLSAVDEVTKIEIDNIEERLSQLDGNATGRPEEHVAPPSVPVPVQEAPNTPTRPQAPPSAHLESPQPARTQQQSIQQMTPQSTTSSNNFLKDGAAGAVLEDQDIEEVLKALKTFDGGHVNPDTICEFFDEVWEEAAPAAPLPPAPPENVVDVPGAKPSCSGILVSGSNISQPNVIIKQEQRPWQESHAELEQQQHVISRRIEFLLRRMRKLQARAMCRHASEEVVGIMEWSARSSHKAPVPARSSTLTEQEATVLSIVSGRPSSTFWEEQNKHPLPASQMSNVIRHIATAAKHQQICHSASGSSATLAPSSSWYNSCNSSALPMKRPRKNQLDASVATGATPTAPAPGAVTSRQAAGTTGSATGSNTPRADDIVPGYDTYVTNELTHVSGLLHTELREVQNAIDSDATESSSGGESADEMVTYNNNQQLSLPITRRAVWRYSRDRAAIALRWSWLCSQLTDLEMKIRQHSDLYMDLTQSKGEIQLESTAKTSPSLAQPANGIKEEPGSDYLCSRARPLVLSEFRKRKLFQTTNMHTISKKAARPSNIKCGCQWPQVPCTLCTGRTDPTAPRDLVETMMPQNRVALLDAGYHPVLSFASDVSQSVHLEAVARQPDWQYRVMRSQPKAIVKAMWKAERETIASGGVGGQGGSRRSGDAAKRRYIRRKERNNNSNKEAGSGAKAAAVAAGGAGGNGSSSVGGGDSGNGTGTATTSSSTTPTTTPLVANSKLL
Protein: CCCTC-binding factor (A0A2R8Y6C1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEGDAVEAIVEESETFIKGKERKTYQRRREGGQEEDACHLPQNQTDGGEVVQDVNSSVQMVMMEQLDPTLLQMKTEVMEGTVAPEAEAAVDDTQIITLQVVNMEEQPINIGELQLVQVPVPVTVPVATTSVEELQGAYENEVSKEGLAESEPMICHTLPLPEG
Protein: RNA transcription, translation and transport factor protein (G3V4C6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFRRKLTALDYHNPAGFNCKDETEFRNFIVWLEDQKIRHYKIEDRGNLRNIHSSDWPKFFEKYLRDVNCPFKIQDRQEAIDWLLGLAVRLEYGDNAEKYKDLVPDNSKTADNATKNAEPLINLDVNNPDFKAGVMALANLLQIQRHDDYLVMLKAIRILVQERLTQDAVAKANQTKEEMQFLMKLLKFCDCCT
Protein: Phospholipid/glycerol acyltransferase domain-containing protein (Q54X10)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MEKFSNWRDGPTGIHPLLPPKAKSVSVFGYIIKFVIGPIISIIRVPIILILTALLIIFNIIARSIPIGWLSRMICRFFDIIIGRIILLCMGFIQLDEFTETLSRSKVASGSIDQCTRKDIIICNHSSYVDIIYLCYKFSPTFAIPPNDEKNLNENIGKLIPLTLGRALENSIYSPIQLSSKSVDTNKLVESIQSSWNGPLVIFPEGTTSNGQGLLDISPIFPSQSQSQSQSQFNTFKEISANKLSIHVIGLSYHYGIYSPCYSSVGNVFLHLFLVCCQISNSIQIHYLSRSCMPPPPKQSQLSQYINNNGLSDENEWFDQLFKSLSSLINTRRTKITNNDKLSFISKWKGYKVDYSSKKSN
Protein: Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 subunit 9) (eIF-3-eta) (Q4G061)
Organism: Rattus norvegicus (Rat)
Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P55884}. Note=Localizes to stress granules following cellular stress. {ECO:0000250|UniProtKB:P55884}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit H
Sequence:
MQDAENVAAPEAAEERAEPARQQPVSESPPTDEAAGSGGSEVGRTEDAEEDAEARPEPEVRAKPAAQSEEETAASPAASPTPQSAQEPSAPGKAEAGGEQARHPSARAEEEGGSDGSAAEAEPRALENGEADEPSFSDPEDFVDDVSEEELLGDVLKDRPQEADGIDSVIVVDNVPQVGPDRLEKLKNVIHKIFSKFGKIINDYYPEEDGKTKGYIFLEYASPAHAVDAVKNADGYKLDKQHTFRVNLFTDFDKYMTISDEWDIPEKQPFKDLGNLRYWLEEAECRDQYSVIFESGDRTSIFWNDVKDPVSIEERARWTETYVRWSPKGTYLATFHQRGIALWGGDKFKQIQRFSHQGVQLIDFSPCERYLVTFSPLMDTQDDPQAIIIWDILTGHKKRGFHCESSAHWPIFKWSHDGKFFARMTLDTLSIYETPSMGLLDKKSLKISGIKDFSWSPGGNIIAFWVPEDKDIPARVTLMQLPTRQEIRVRNLFNVVDCKLHWQKNGDYLCVKVDRTPKGTQGVVTNFEIFRMREKQVPVDVVEMKETIIAFAWEPNGSKFAVLHGEAPRISVSFYHVKSNGKIELIKMFDKQQANTIFWSPQGQFVVLAGLRSMNGALAFVDTSDCTVMNIAEHYMASDVEWDPTGRYVVTSVSWWSHKVDNAYWLWTFQGRLLQKNNKDRFCQLLWRPRPPTLLSQDQIKQIKKDLKKYSKIFEQKDRLSQSKASKELVERRRTMMEDFRQYRKMAQELYMKQKNERLELRGGVDTDELDSNVDDWEEETIEFFVTEEVIPLGSQE
Protein: U-box domain-containing protein 1 (EC 2.3.2.27) (Plant U-box protein 1) (MtPUB1) (RING-type E3 ubiquitin transferase PUB1) (E4NKF8)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Exhibits U-box-dependent E3 ubiquitin ligase activity in vitro. Negatively modulates successive stages of infection and development of rhizobial (e.g. Sinorhizobium meliloti) and arbuscular mycorrhizal fungi (AM, e.g. Rhizophagus irregularis) symbioses, in an ubiquitin ligase activity-dependent manner. Negative regulator of the LYK3 signaling pathway leading to nitrogen-fixing symbiosis (eg. infection and nodulation) by rhizobia. May be involved in the discrimination of rhizobium strains producing variant Nod factors.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20971894}.
Interaction partners:
- LysM domain receptor-like kinase 3
- Protein VAPYRIN
Sequence:
MNDPRSKMMISPGLLPTESLLDSLILISNEVSSMQKFPLVQIKNVSSMIRRIKLLSSLFEEIQESDSPLPPSSILCFIEIFSVITRVKVLIQECTDGSSLWSLIQLDFISNQFFVLVKEMGRALDILPLNLLNVAQDIKEQVDLLHKQSKRVELELFIDPREVQRRENLFEVMSKNCLQNKKTNNNKGFIDFVKVEEIMCSIGLRTLSDYVEEISKLEVEAQNQAGTGGLIVVSNINNLMSLVSYTKSMVFRNDGESEECKPISMFLYNKSKIHDNDSSSSSSFSQSMMTVNIPDEFRCPISLDLMRDPVIVSSGHTYDRISIAEWINSGHHTCPKSGQRLIHTALIPNYALKSLVHQWCYENNVKMNEAITKNNNSSSKRHKNENAIDHISENKASKDAVKMTAEFLVGKLATGSTDIQRQSAYEIRLLAKTGMDNRRIIAEVGAIPFLVTLLVSKDSRIQEHVVTALFNLSIYDNNKILIMAAGAIDNIVEVLEFGKTMEARENAAAAIYSLSMIDDCKVQIGASSRAIPALVGLLKEGTIIGKRDAATALFNLAVYNPNKLSIVKSGAVTLLVELLMDDKAGITDDSLAVLAVLLGCSEGLEEIKNSKSLVPLLIDLLRFGSVKGKENSITLLLGLCKEEGELVAMRLLANPRSIPSLQSLAADGSLRARRKADALLRLLNRCCSQPHHSL
Protein: tRNA (cytosine(49)-C(5))-methyltransferase (EC 2.1.1.-) (Q9V106)
Organism: Pyrococcus abyssi (strain GE5 / Orsay)
Function: Catalyzes AdoMet-dependent formation of m5C in tRNA. In the presence of protein archease, specifically methylates the cytosine at position 49 (m5C49) of tRNA. In the absence of archease, catalyzes the formation of m5C at many locations in tRNAs or rRNAs.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Protein archease
- tRNA
- Protein involved in ribosomal biogenesis
Sequence:
MDYKEEFKKINKKLVERYSKLDDSEEFWAYLYKPLRPSIRINTLKGNLKEIKALLEEKFELEPIPWTKGEGFYIKSYDVNYGQLIEYSLGLIIPQEASSMIPPVVLDPKPSEVILDMAAAPGSKTTQMAQYMENEGCIIANDAKRDRANILIANLTRAGVLIAKVTVKDGAYFARYENTFDRVLLDAPCSSVGMIRKNFKFARTWSIGKVYYHSRLQKRLILAAYKSLKPGGVLVYSTCTVDPLENEEVVDFLLQKTDAKLEKVKLPLKTSEPVIEWEGRKYSDEVRKTIRIHPQDNDTEAFYIAKIRKPR
Protein: Axin-like protein pry-1 (Protein polyray) (O62090)
Organism: Caenorhabditis elegans
Function: Works in parallel with axl-1 in negatively regulating bar-1 signaling in vulval precursor cells and Q neuroblasts. Inhibits Wnt signaling, which affects tissue specific expression of Hox genes, egl-5, lin-39 and mab-5. This in turn affects QR (postembryonic neuroblast) cell migration, vulval cell fate specification, and the development of sensory structures by the seam cell lineage. Has a role in alae V cell patterning, ray formation in the male tail and axon guidance. Does not affect B cell polarity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:16077004}. Nucleus {ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:16077004}. Cytoplasm, cell cortex {ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:16077004}. Note=Subcellular location was measured using a GFP reporter gene. Location of the pry-1:GFP fusion protein ranges from plasma membrane and cytoplasmic dots to diffuse cytoplasmic and nuclear staining. This difference may be due to variations in expression levels of the fusion protein in different transgenic lines. {ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:16077004}.
Interaction partners:
- Beta-catenin/armadillo-related protein 1
- Armadillo repeat-containing protein wrm-1
- Glycogen synthase kinase-3
- Adenomatous polyposis coli protein-related protein 1
- DiSHevelled related
- DiSHevelled related
- Casein kinase I isoform alpha
- Beta-catenin-like protein hmp-2
- Putative serine/threonine-protein kinase gskl-1
- Protein kinase domain-containing protein
Sequence:
METHLGWARSLEAVLSDRSALDAFQEWLIEYSSPQYLDLFFAIRAYERMALEGKPEKSQLSKSIYSKFLSSRTGNCEAIPKHFRAPIGEKLRHGTELEDRVFSHCSNFVQEFLRRQHEEFVGSEEFIEAFNKMSSTTADQLPGGSAHHSSHQNTMRRSSGTTSRKSAAQIATQLTAEALLKSKHDRHSKLGETKLEKMYPPTRQPYVCNATTSHNDSAVSSTFSGDTPEAHRMHSNRLRHIRDEQARENHGTMTLPRVEKASVDGQQWDHSSESGRRNFAMEITRKLLRHIDKVKLNDEMEKRIDDIEECRYTTIDMVNGTEPNDDLGKIDEDEELDDYLKMKMTDDSQKGSTNRSPKGPAGEPNKSGEGSKNTTLSPTNRAPAQLHNTIRVPRRKDYPRDTSASLKSHRHHQIDTNRMMSQSMCAPSYSSASSSYSRDSFAPAPTTRVNFAPGSSKSSQFYDSSGIGSMAPSAFSATSSLDYKDRRQHRKAPTPKKHSKIGKNLSNLITISYLGTDKIPVVTHVPNDGPMTLAEFKRHFALPNGAHQLFFKTECEDGSAPFQLLLIKDEHHLLPVFEGRIAAELR
Protein: Adhesion G protein-coupled receptor B2 (A2A3C3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MTPACPLLLSVILSLRLATAFDPAPSACSALASGVLYGAFSLQDLFPTIASGCSWTLENPDPTKYSLYLRFNRQEQVCAHFAPRLLPLDHYLVNFTCLRPSPEEAVAQAESEVGRPEEEEAEAAAGLELCSGSGPFTFLHFDKNFVQLCLSAEPSEAPRLLAPAALAFRFVEVLLINNNNSSQFTCGVLCRWSEECGRAAGRACGFAQPGCSCPGEAGAGSTTTTSPGPPAAHTLSNALVPGGPAPPAEADLHSGSSNDLFTTEMRYGEEPEEEPKVKTQWPRSADEPGLYMAQTVHGVWEEWGSWSLCSRSCGRGSRSRMRTCVPPQHGGKACEGPELQTKLCSMAACPVEGQWLEWGPWGPCSTSCANGTQQRSRKCSVAGPAWATCTGALTDTRECSNLECPATDSKWGPWNAWSLCSKTCDTGWQRRFRMCQATGTQGYPCEGTGEEVKPCSEKRCPAFHEMCRDEYVMLMTWKKAAAGEIIYNKCPPNASGSASRRCLLSAQGVAYWGLPSFARCISHEYRYLYLSLREHLAKGQRMLAGEGMSQVVRSLQELLARRTYYSGDLLFSVDILRNVTDTFKRATYVPSADDVQRFFQVVSFMVDAENKEKWDDAQQVSPGSVHLLRVVEDFIHLVGDALKAFQSSLIVTDNLVISIQREPVSAVSSDITFPMRGRRGMKDWVRHSEDRLFLPKEVLSLSSPGKPATSGAAGSPGRGRGPGTVPPGPGHSHQRLLPADPDESSYFVIGAVLYRTLGLILPPPRPPLAVTSRVMTVTVRPPTQPPAEPLITVELSYIINGTTDPHCASWDYSRADASSGDWDTENCQTLETQAAHTRCQCQHLSTFAVLAQPPKDLTLELAGSPSVPLVIGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNMLIGIIVFNKLMARDGISDKSKKQRAGSERCPWASLLLPCSACGAVPSPLLSSASARNAMASLWSSCVVLPLLALTWMSAVLAMTDRRSVLFQALFAVFNSAQGFVITAVHCFLRREVQDVVKCQMGVCRADESEDSPDSCKNGQLQILSDFEKDVDLACQTVLFKEVNTCNPSTITGTLSRLSLDEDEEPKSCLVGPEGSLSFSPLPGNILVPMAASPGLGEPPPPQEANPVYMCGEGGLRQLDLTWLRPTEPGSEGDYMVLPRRTLSLQPGGGGGGGEDAPRARPEGTPRRAAKTVAHTEGYPSFLSVDHSGLGLGPAYGSLQNPYGMTFQPPPPTPSARQVPEPGERSRTMPRTVPGSTMKMGSLERKKLRYSDLDFEKVMHTRKRHSELYHELNQKFHTFDRYRSQSTAKDKPSPGERPSLSQHRRHQSWSTFKSMTLGSLPPKPRERLTLHRAAAWEPTEPPDGDFQTEV
Protein: Netrin receptor UNC5C (Protein unc-5 homolog 3) (Protein unc-5 homolog C) (O95185)
Organism: Homo sapiens (Human)
Function: Receptor for netrin required for axon guidance (By similarity). Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (By similarity). NTN1/Netrin-1 binding might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion. Axon repulsion in growth cones may also be caused by its association with DCC that may trigger signaling for repulsion (By similarity). Might also collaborate with DSCAM in NTN1-mediated axon repulsion independently of DCC (By similarity). Also involved in corticospinal tract axon guidance independently of DCC (By similarity). Involved in dorsal root ganglion axon projection towards the spinal cord. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:25419706}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000269|PubMed:25419706}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q761X5}. Cell projection, axon {ECO:0000250|UniProtKB:O08747}. Cell projection, dendrite {ECO:0000250|UniProtKB:O08747}. Cell projection, growth cone {ECO:0000250|UniProtKB:O08747}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O08747}. Cell projection, filopodium {ECO:0000250|UniProtKB:O08747}.
Interaction partners:
- Netrin-1
- Adhesion G protein-coupled receptor L3
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L2
- Netrin receptor DCC
- Proto-oncogene tyrosine-protein kinase Src
- Focal adhesion kinase 1
- Tyrosine-protein phosphatase non-receptor type 11
- Leucine-rich repeat transmembrane protein FLRT2
- Neogenin
Sequence:
MRKGLRATAARCGLGLGYLLQMLVLPALALLSASGTGSAAQDDDFFHELPETFPSDPPEPLPHFLIEPEEAYIVKNKPVNLYCKASPATQIYFKCNSEWVHQKDHIVDERVDETSGLIVREVSIEISRQQVEELFGPEDYWCQCVAWSSAGTTKSRKAYVRIAYLRKTFEQEPLGKEVSLEQEVLLQCRPPEGIPVAEVEWLKNEDIIDPVEDRNFYITIDHNLIIKQARLSDTANYTCVAKNIVAKRKSTTATVIVYVNGGWSTWTEWSVCNSRCGRGYQKRTRTCTNPAPLNGGAFCEGQSVQKIACTTLCPVDGRWTPWSKWSTCGTECTHWRRRECTAPAPKNGGKDCDGLVLQSKNCTDGLCMQTAPDSDDVALYVGIVIAVIVCLAISVVVALFVYRKNHRDFESDIIDSSALNGGFQPVNIKAARQDLLAVPPDLTSAAAMYRGPVYALHDVSDKIPMTNSPILDPLPNLKIKVYNTSGAVTPQDDLSEFTSKLSPQMTQSLLENEALSLKNQSLARQTDPSCTAFGSFNSLGGHLIVPNSGVSLLIPAGAIPQGRVYEMYVTVHRKETMRPPMDDSQTLLTPVVSCGPPGALLTRPVVLTMHHCADPNTEDWKILLKNQAAQGQWEDVVVVGEENFTTPCYIQLDAEACHILTENLSTYALVGHSTTKAAAKRLKLAIFGPLCCSSLEYSIRVYCLDDTQDALKEILHLERQMGGQLLEEPKALHFKGSTHNLRLSIHDIAHSLWKSKLLAKYQEIPFYHVWSGSQRNLHCTFTLERFSLNTVELVCKLCVRQVEGEGQIFQLNCTVSEEPTGIDLPLLDPANTITTVTGPSAFSIPLPIRQKLCSSLDAPQTRGHDWRMLAHKLNLDRYLNYFATKSSPTGVILDLWEAQNFPDGNLSMLAAVLEEMGRHETVVSLAAEGQY
Protein: Na(+)/H(+) antiporter NhaA (Na(+)/H(+) exchanger) (Na(+)/Li(+)/H(+) antiporter) (Sodium/proton antiporter NhaA) (P13738)
Organism: Escherichia coli (strain K12)
Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Plays an important role in the regulation of intracellular pH, cellular Na(+) content and cell volume. Catalyzes the exchange of 2 H(+) per Na(+). This stoichiometry applies at both neutral and alkaline pH values. In addition, can also transport lithium and is involved in lithium detoxification. Binding of the Li(+) and H(+) ligands to NhaA is coupled and antagonistic.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:15988517, ECO:0000269|PubMed:1645730, ECO:0000269|PubMed:19396973, ECO:0000269|PubMed:25422503}; Multi-pass membrane protein {ECO:0000269|PubMed:15988517, ECO:0000269|PubMed:19396973, ECO:0000269|PubMed:25422503}.
Interaction partners:
- Na
- Transcriptional activator protein NhaR
- Sodium-potassium/proton antiporter ChaA
- Glutathione-regulated potassium-efflux system protein KefB
- Glutathione-regulated potassium-efflux system protein KefC
- Lactose permease
Sequence:
MKHLHRFFSSDASGGIILIIAAILAMIMANSGATSGWYHDFLETPVQLRVGSLEINKNMLLWINDALMAVFFLLVGLEVKRELMQGSLASLRQAAFPVIAAIGGMIVPALLYLAFNYADPITREGWAIPAATDIAFALGVLALLGSRVPLALKIFLMALAIIDDLGAIIIIALFYTNDLSMASLGVAAVAIAVLAVLNLCGARRTGVYILVGVVLWTAVLKSGVHATLAGVIVGFFIPLKEKHGRSPAKRLEHVLHPWVAYLILPLFAFANAGVSLQGVTLDGLTSILPLGIIAGLLIGKPLGISLFCWLALRLKLAHLPEGTTYQQIMVVGILCGIGFTMSIFIASLAFGSVDPELINWAKLGILVGSISSAVIGYSWLRVRLRPSV
Protein: Rab3 interacting molecule, isoform V (A0A0B4K679)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MDEMPDLSHLTPHERMQIENVLMRQKQEEEKQNEIMRRKQDEVVTLEMQIRQRSEQQKKAGVELDATCHICLKTKFADGVGHICHYCNIRCCARCGGKVTLRSNKVIWVCILCRKKQELLSKTGQWINKTAAQQDGFIRRIEPDGSSDISQHPIVDPHDTTDKRPKLERTRSAAEKENLPMQRAGSMLRRQYSQQEQPTNRRLSASDSGMDPVMSPGQQMQHHQQQQRARMQPMNPQQAQQGYGMQQQQQPRSGGAYPDDDPRYYQGELDGLMRQHPHLAHPSQVQPQHTPQSHSQQQQSQHQQQHLMPQQHRPSPQQHSQQQQQQQQHSQQFAARQQQHQQQQHQQQVQQSYHAQIHQQPQQHPHPHSQQQQHHQQMQHQHGQSVPQMGGYQKPPPLTRNLTISGGHAMDSSAYSQQQQQQQRRALAGSQYASQQQRSFSSSEEEFQHQLLAAQGAVTVTAGSDYDGGRLQVRTSLDPWRQQRSLNERDLLSSGGGGGGGVGGADFRHLSHATQRLYASADQRDRYELQLQHRERLEQYPLTRTARLDVQQRNSLNRSNHERQFSGGGAGVGPGGAGGGGAAGAYRRAPPLAAAGGGGSSSSSTTSSSYYPQSKPQIVIGPGSGYDRGSGSMASMASAAAATAADAQGQAARNSQRGGLLGATRGGGGSSSVSSTEAAYWDEPATSSSSSAAQDSRRFTERRIKKTVRFDAHDEEASILASSSLPPVTAILPSTAVDVGAATILSSGKSLDAVGVGGADWSRWEAERQGSQDSATKDSGIDTSSTFTSSEDSNRGDGPKNPVNWQTSADNTRLIGHMILRKYYDGEDILGLKVNGGQPLATGGSVSGAGTGAAIGAGGPCGAIVEKVKRGSVADLEGRIRPGDEILEWNGRGLHNKSADEVYDIIDESRLDAQVELIVSRPIGSGGGSGGSSANVSPISGASGGSANSVPARRSSANFPHSGLASSMAGSAVVSSGGRYLQRKAPAVEAIEIHRDKPSVLITSPGSPDIHTSVSGPGSVSGSGLRQRGGVGQTQRLGPSHSTHSHSSSGSGSGSGSSTSSVHAPASAHGPVHASASASGSAPGGLHGTTTAGHHHHPHPHHYHPHQHPLPHPHQHQGPPAAHLQGHGVGGGIGMGSGSGTTTQPIPIEGRLQLKLGYDQNTLQLIVTLVCATGLSLRQSGAGRNPYAKVFLLPDRSHKSKRRTKTVGTTCEPRWGQTFVYSGLRRCDLNGRLLEVTLWDYVRYGANDFIGEVVIDLAHHILDDEAEWYQLQPHQDTSYLLRDEGSDVDGLILTPTDHLSPPSTMSRLSDSDTTSDCDIDGMTPGASISSMGSSASPPPLLELDLNERRSRRDMSPQGRKRVAGMVARDYRTVSGIGQSYHNQASATGYYRRGGGNGVGSAIGPGGMSLSQRSHSAAPSDGYHSSGVGGAASGGPAYGYRSTSPRRGSLSPPDDRYIDYPVLPVHGSSPNAPSVYQGPGGVSSAAASASQQQRFQSRSATATPTGSPKKRQLPQVPQTSRSAMLRDRLGQDFDERLASGGRFGRHRTRQPHHQATYRSTGMGGWERHYTGLSDSDLHSMDARMRPRHSLSPDKDFMGEFGDSDMESVVSVTSSAFSTQSERPRTSRGLSEYDKDKNGAEEAGGSKSAEGAGAEDKVDGSLSDTANDRKKGGGVDQERSPKGGSGMGKKSNSTSQLSATGRKRRMGFGKKGKNSFTVHRSEEVLPGDITRELRTGGGLGVSLGGAGGAAGGSGGAGGGGLSRGSSSEVDAIEQFFGDGAGGERFSPSLRNDGALNEFVDGLGPGQLVGRQVLGAPSLGDIQLSLCHQKGCLEVEVIRARGLQQKAQSKMLPAPYVKVYLVSGKRCVDKMKTSSARRTLDPLYQQQLVFKQSYTGCILQITVWGDYGRIEKKVFMGVAQIMLDDLNLSNIVIGWYKLFGTTSLVSCPTNIGLGSRRSSIASLDSLKL
Protein: N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) (Q9HT86)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- AmpG
- Beta-lactamase
- HTH-type transcriptional activator AmpR
- Beta-hexosaminidase
- Soluble lytic transglycosylase B
- UPF0056 inner membrane protein
- Lytic murein transglycosylase
- Probable zinc protease
- Insulinase family protein
Sequence:
MRSFVLLAFTLSLLAGCSSGPRLNTDYTSANQDSRVQFIVLHYTSTDLPHSLGILTHGGVSAHYLIGDDEPATVYRLVDENRRAWHAGVSEWQGRTWLNATSIGIEIVNQGYRDTPQGRVWYPFSEAQIQALIPLLKDIAKRHGITPDRIIGHSDIAPGRKVDPGPLFPWKRLADAGLVPWPKPGELARRLAELNGQLPDVRWFQQQLARHGYLVPQTGELEKDTRDVIGAFQMKYRPARFDGEPDLETAALLLAVPTS
Protein: Hypoxia-inducible factor 1-alpha (HIF-1-alpha) (HIF1-alpha) (ARNT-interacting protein) (Basic-helix-loop-helix-PAS protein MOP1) (Class E basic helix-loop-helix protein 78) (bHLHe78) (Member of PAS protein 1) (PAS domain-containing protein 8) (Q16665)
Organism: Homo sapiens (Human)
Function: Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300. Activity is enhanced by interaction with NCOA1 and/or NCOA2. Interaction with redox regulatory protein APEX1 seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9822602}. Nucleus {ECO:0000269|PubMed:22009797, ECO:0000269|PubMed:9822602}. Nucleus speckle {ECO:0000250|UniProtKB:Q61221}. Note=Colocalizes with HIF3A in the nucleus and speckles (By similarity). Cytoplasmic in normoxia, nuclear translocation in response to hypoxia (PubMed:9822602). {ECO:0000250|UniProtKB:Q61221, ECO:0000269|PubMed:9822602}.
Interaction partners:
- Prolyl hydroxylase EGLN3
- Aryl hydrocarbon receptor nuclear translocator
- Cullin-2
- CREB-binding protein
- Hypoxia-inducible factor 1-alpha inhibitor
- Aryl hydrocarbon receptor nuclear translocator 2
- Prolyl hydroxylase EGLN2
- Cellular tumor antigen p53
- Histone acetyltransferase p300
- Elongin-B
Sequence:
MEGAGGANDKKKISSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDDMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGLVKKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTECVLKPVESSDMKMTQLFTKVESEDTSSLFDKLKKEPDALTLLAPAAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN
Protein: Synaptophysin-like protein 2 (Q5VXT5)
Organism: Homo sapiens (Human)
Function: Involved in communication between the T-tubular and junctional sarcoplasmic reticulum (SR) membranes.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Triad junction, the junctional complex between the transverse tubule and the sarcoplasmic reticulum. {ECO:0000250}.
Interaction partners:
- Junctophilin-1
- Junctophilin-2
- Junctophilin-4
- Junctophilin-3
Sequence:
MSSTESAGRTADKSPRQQVDRLLVGLRWRRLEEPLGFIKVLQWLFAIFAFGSCGSYSGETGAMVRCNNEAKDVSSIIVAFGYPFRLHRIQYEMPLCDEESSSKTMHLMGDFSAPAEFFVTLGIFSFFYTMAALVIYLRFHNLYTENKRFPLVDFCVTVSFTFFWLVAAAAWGKGLTDVKGATRPSSLTAAMSVCHGEEAVCSAGATPSMGLANISVLFGFINFFLWAGNCWFVFKETPWHGQGQGQDQDQDQDQGQGPSQESAAEQGAVEKQ
Protein: Gamma-secretase subunit APH-1B (APH-1b) (Aph-1beta) (Presenilin-stabilization factor-like) (Q8WW43)
Organism: Homo sapiens (Human)
Function: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (amyloid-beta precursor protein). It probably represents a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex. Probably present in a minority of gamma-secretase complexes compared to APH1A.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nicastrin
- Gamma-secretase subunit PEN-2
- Presenilin-2
- Presenilin-1
- Gamma-secretase subunit APH-1A
- Amyloid-beta precursor protein
- Transmembrane emp24 domain-containing protein 10
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 2
Sequence:
MTAAVFFGCAFIAFGPALALYVFTIATEPLRIIFLIAGAFFWLVSLLISSLVWFMARVIIDNKDGPTQKYLLIFGAFVSVYIQEMFRFAYYKLLKKASEGLKSINPGETAPSMRLLAYVSGLGFGIMSGVFSFVNTLSDSLGPGTVGIHGDSPQFFLYSAFMTLVIILLHVFWGIVFFDGCEKKKWGILLIVLLTHLLVSAQTFISSYYGINLASAFIILVLMGTWAFLAAGGSCRSLKLCLLCQDKNFLLYNQRSR