wanglab/gogpt-training-data huggingface dataset:
Protein: Neurite extension and migration factor (KIAA2022 protein associated with intellectual disability, language impairment and autistic behavior homolog) (KIDLIA) (XLMR protein related to neurite extension) (Xpn) (D3ZGX1)
Organism: Rattus norvegicus (Rat)
Function: Involved in neurite outgrowth by regulating cell-cell adhesion via the N-cadherin signaling pathway. May act by regulating expression of protein-coding genes, such as N-cadherins and integrin beta-1 (ITGB1).
Subcellular location: Nucleus {ECO:0000269|PubMed:24071057, ECO:0000269|PubMed:27822498}. Cytoplasm {ECO:0000250|UniProtKB:Q5DTT1}.
Interaction partners:
Sequence:
MDNQQDKVIAASANGENNLINGVKENDSEEQDVAMKSFAALEASTPIQPIPVVQKESPMFPRGLLPLPSKKPCMQSPPSPLGLIEAPDHSATGASVNAISLTSGVAKGLNTWSLPNECEKAPFAIMEPAGISALNGDCLMQPSRTCLGCFMESKEAVDPEPGISLKVGDLNRDYETCAVSDIGIQCINAGENLKYGEQLLSDQLLGFPLHKSRAGDRRESEKPDIDLEDPTQKSYYEALLLDKCNTEEALLANSNQDWGYFETFISESKIELLDLCSKNELSVNLFSEEDVENYMFDDDESTLGSDVCSLKIRYESFQDNVRDKTTLLMQEDAQFNFFPSVFTTCPKRESKSGVLKQSSDLSQFKVPDVSIIWGDEDKNLDKKKGKEEVHEDKSIEKKDEKDNGEKPALNNKPCSGLEVEQFKNLKPDHLTNSLETSGNFSDDSSFIEVSYDAMGEIKDCSRYMARDTNSGSSSSQQNYGLRAKRKVRYSEDYLYDVDSLEGEKVNERKEWPPGGSKEEDDDEWCPKKRRKVTRKEPPVIIKYIIINRFKGEKNMLVKLGKVDASETTVNLSESQLSKYAKLSPLKGFWQKKKKQKNGNTDSVKTPFCQKQSFEPGSFEVSFLPPARKRKSKLGNRHRIQRIQSMEASASSKQVSFGSDQKQASNRKEEGGLKGTPKSALLAAPSSANGSHLRGLIGPDSAKVKAQDTEFKGPERKVLNKIKFKSEARLKSKKIKTGQENKPVVQMSPVSEDPSSKANLKNEVTPGTSNSSHMSEFHETKVVKNSTFLPTTCSSEMPLSSANVATNIPVIPGGYLQTLLDASDLSNNTSISYFTNHSAEQNEASLSQTEKAFAPLQSAQDCVLSSSSDSQLQQSSQNFKMEASNYGSLWPDKDTSGSQEFMTEVSGEIATSQSSEFEATQVVSMENNLTAITYSPVCLNSGGSGCNKVLYASVQDSHLAPDDSYQLCHFNNGEICFPFQQGPISTEDDGQLFSFDSMTPLSVSSSSYCPLSLKSCEKDGDDDINDDFLAHCSPKLVIQQSIDEIAPLKESTDLLDISNFTPDKFRHSSLSEMSPPDTPSLSPQSTRCESIKTLGTMKGFQEGVPGSLSSMEKIKWDCSTLSQQVQADDGFTLNNHQFQFHMFNDEDSVGLLQKNPCLSTFDEPAGQISANNKVSKSRKKTSPGKSGAVSQSSSQKNTRKKSPKASNKGVEKPPSKTSRQVPKSAKKGKYVAAVNGEKMQIGIGHSGGQPNSTSSNGKTLTECIQHGGPVAPMKIPSQKGLSGDWALGKESRPGWNDMSVVTNTNNLLDDDQREFQEPSYILSNIASGMADVQRFMMASMEPLWEPMEHQGESNTFYSPDSNSLKLKTLKILAGTPQESKKKINNGSSGATKNHRSIKAVSKSSGKAAVGDPGHADVSGSSEDSRSAFFDKKYSNMNTLGNNGPTHKKLYRHKSSSKTLRDEKYKGKRVEREQIHKDEAGTTCFEKLRGSSYNLLKAETAFGVLPVFEEETHIFQKDI
Protein: Lipid droplet-associated triacylglycerol lipase (TAG lipase) (EC 3.1.1.3) (Q06522)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Shows both triacylglycerol (TAG) lipase and ester hydrolase activities. May play a role in TAG homeostasis.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:24868093}. Membrane {ECO:0000255}; Peripheral membrane protein {ECO:0000255}.
Interaction partners:
- Lipid droplet phospholipase 1
- Lipid droplet hydrolase 1
Sequence:
MTVKEYTKSKLPCSILNIKPTVTKSGEDAPLLVWIPGNPGLLYYYQEMLHHLHLKHPDWEILGISHAGMTLNAHSNTPIFSLQDQVDHQVEVINNFSCKNRKIIIMGHSVGAYIVQKVCLSNKLVGSVQKVGLVTPTVMDIHTSEMGIKMTAALRYIPPLAHVVSLFSYIFFYWILSEGFSRFIIDKFMGCGSTGYQAVLSTRIFLTHRQFVRQSLGLAAQEMEEITTNWEFQDRFINYCEENGISIWFLFSSNDHWVSGKTRSHLSDYYKDKVKQERLKIDVTDKIPHSFVVKHAEYAINAFF
Protein: Major intrinsically disordered Notch2-binding receptor 1 (Membrane integral NOTCH2-associated receptor 1) (Ubiquitination and mTOR signaling protein) (Q9UPX6)
Organism: Homo sapiens (Human)
Function: Intrinsically disordered protein which may negatively regulate mTOR signaling pathway by stabilizing the mTOR complex component DEPTOR. Negatively regulates angiogenesis. Negatively regulates cell growth. Negatively regulates neurite outgrowth in hippocampal neurons (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:29329397, ECO:0000269|PubMed:30080879}; Single-pass type IV membrane protein {ECO:0000269|PubMed:30080879}.
Interaction partners:
Sequence:
METSQETSLFLVKILEELDSKQNTVSYQDLCKSLCARFDLSQLAKLRSVLFYTACLDPNFPATLFKDKMKCTVNNQQSKKIMVAADIVTIFNLIQMNGGAAKEKLPTGRQKVRKKEASFESCRSDTEICNAAECEPLNCELSERSFSRGYPIRQSSKCRKMDCKDCPQFVPASEPNFLLGVSKEVKNRAASLDRLQALAPYSVTSPQPCEMQRTYFPMNIENESISDQDSLPINQSIKETFISNEEPFVVQSCVQKRNIFKEDFHNLMAVSPSLVGPISKAENEHREPQSRKEPHKPPFFNHSFEMPYNSQYLNPVYSPVPDKRRAKHESLDDLQASTYFGPTPVMGTQEARRCLGKPNKQTPWPAKSWSLNTEEVPDFERSFFNRNPSEEKLHYPNASSQTPNFPAPERRPTYLVPKDQQPILPIAYAAKQNGLKSKEISSPVDLEKHEPVKKFKDKSINCTSGQLSSDTSSVGTQTEHVLEPKKCRDLCTSGQGKYSDRHTMKHSDDDSEIVSDDISDIFRFLDDMSISGSTGVIQSSCYNSTGSLSQLHKSDCDSSPEHNLTKIANGVPNSKGDKGNRPENTHHSEEELKTSVCKLVLRIGEIERKLESLSGVRDEISQVLGKLNKLDQKMQQPEKVSVQIDLNSLTSEGPSDDSASPRMFHAHSGSHGPKLENNPDWCCSDASGSNSESLRVKALKKSLFTRPSSRSLTEENSATESKIASISNSPRDWRTITYTNRVGLNEEEIKDTGPGDNKDWHRKSKEADRQYDIPPQHRLPKQPKDGFLVEQVFSPHPYPASLKAHMKSNPLYTDMRLTELAEVKRGQPSWTIEEYARNAGDKGKLTALDLQTQESLNPNNLEYWMEDIYTPGYDSLLKRKEAEFRRAKVCKIAALIAAAACTVILVIVVPICTMKS
Protein: Calcium load-activated calcium channel (GEL complex subunit TMCO1) (Transmembrane and coiled-coil domain-containing protein 1) (J3QQY2)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MVRMKSMFAIGFCFTALMGMFNSIFDGRVVAKLPFTPLSYIQGLSHRNLLGDDTTDCSFIFLYILCTMSIRQNIQKILGLAPSRAATKQAGGFLGPPPPSGKFS
Protein: Transmembrane protein 41B (Protein stasimon) (Q8K1A5)
Organism: Mus musculus (Mouse)
Function: Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes. Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine. Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted by ATG2 (ATG2A or ATG2B) to mediate autophagosome assembly. In addition to autophagy, involved in other processes in which phospholipid scramblase activity is required (By similarity). Required for normal motor neuron development (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30352685}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q5BJD5}. Note=Localized to specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria. {ECO:0000269|PubMed:30352685}.
Interaction partners:
- Vacuole membrane protein 1
- WD repeat-containing protein 46
Sequence:
MAKGRVADRSPTEMLHSTPAGDRAVRTQGSAAPGSKDHLNEKPCAEAGSARTSLLILVSIFSCAAFVMFLVYKNFPQLSEEERVNMKVPRDMDDAKALGKVLSKYKDTFYVQVLVAYFATYIFLQTFAIPGSIFLSILSGFLYPFPLALFLVCLCSGLGASFCYMLSYLVGRPVVYKYLTEKAVKWSQQVERHREHLINYIIFLRITPFLPNWFINITSPVINVPLKVFFIGTFLGVAPPSFVAIKAGTTLHQLTTAGEAVSWSSVFILMVLALLSILPAIFQKQLKQKFE
Protein: Protein get1 (Guided entry of tail-anchored proteins 1) (Q9HGM2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Acts as a membrane receptor for soluble get3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03113, ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03113, ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATPase get3
- Golgi to ER traffic protein 4
- Small glutamine-rich tetratricopeptide repeat-containing protein 2
- Protein transport protein sec61 subunit beta
- ER lumen protein-retaining receptor
- Sad1-interacting factor 1
Sequence:
MMDLIISTILLSLFIHFFDKFAKKRTIDGAYRIYVSVSNNKDLKKNKEILEQLLTVKKELNATSSQDQFAKWARLNRKYEQLSQEWEKQSANVKIFQDTFKRVLSLFLWILTRGFRFYIQFKESKTPVFFLPAFLLPSWALWVLSLPRSIYGSVSLTVWNFAVQKTISGIF
Protein: CG14842 (Q2XYC2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
LSLCLAIYCGGGHGHGNVVLSLPPSLIATATKAALSHQRQQQQQQQHQKKDARVLFDSPADALRDMMHNGNGNGNGPMDSGKFSLSDVEQPAAQRSEDFNRNADDLGARQSAPQEIAMGMELGMGLGLGPNNYRTTPPHRYWGQRCQGRSGGSGTSKCPQEYYR
Protein: Carnitine palmitoyltransferase I (MIP15836p) (Withered, isoform C (EC 2.3.1.21)) (Withered, isoform D) (Q9V3K9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- long-chain-fatty-acid--CoA ligase
- Carnitine palmitoyltransferase 2
- Long-chain-fatty-acid--CoA ligase
- Long-chain-fatty-acid--CoA ligase heimdall
- Very long-chain-fatty-acid--CoA ligase bubblegum
- HL08109p)
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MAEAHAAVAFSFAITHEGFDINYDHEVLNLVWNSGVRSWKKRLARARNGVRNGVYPAHIQSLWLISAIALGLHFAGYQAPFNLTNRILVHLPSNTINWQVTACFLAALVVWLSICFTMRYTLKLLLMYKGWMYESRAPGSRVSLPTMLWVAVVRVLSSWNKPGLYSFQGSLPRLPLPSVKDTMTRYLRSVRPLLDDENYTRMERLAKEFEQTIGKKLQWYLILKSWWSTNYVSDWWEEYVYLRGRSPLCVNSNFYGTDAIFMNLTDKQAARAANVISLLLNFRRLIEHQELQPIMVQGMIPLCSWQYERTFNTARVPGLETDRIIHYRDSNHIVVLHKGCYYKMLIYYKGRILRPCELQVQIEEILKGKATPVEGEEHLAALTAWNRSKWAEARNTFFSWGVNQTSLRTIESAAFVLSLDDEPFEFDLARPELLDNFGKKLLHGNGYNRWFDKCFTVCVGTNGRVGFNAEHTWSDAAIASHMWENLIVDDLVSDGYDETGNTKGTPAFQPPTPTRLTWDLKPCLAQIEEATIDVTKLINEVNLRILVHQDYGKGFMKKCRISPDAYIQMALQLAYYRDAGRFSLTYEASMTRLFREGRTETVRPCTIESSAWVKAMQNPNTTNDERVKMMQAACDRHQLGYQDAMCGRGIDRHLFCLYVVSKYLEVDSPFLNEVLSEPWRLSTSQTPHGQTPKMDLKKHPNCISAGGGFGPVADDGYGVSYIIAGENLIFFHISAKTTCQQTDVHRFAQNISQALSDIRSMFEQHMKDHPKPAKSLTNGKST
Protein: Thyrotropin-releasing hormone receptor (TRH-R) (Thyroliberin receptor) (Q01717)
Organism: Rattus norvegicus (Rat)
Function: Receptor for thyrotropin-releasing hormone (TRH). Upon ligand binding, this G-protein-coupled receptor triggers activation of the phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P34981}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pro-thyrotropin-releasing hormone
- Thyrotropin-releasing hormone receptor 2
- Guanine nucleotide-binding protein G
- Thyrotropin receptor
- Thyrotropin subunit beta
- Beta-arrestin-1
- Guanine nucleotide-binding protein subunit alpha-11
Sequence:
MENETVSELNQTELPPQVAVALEYQVVTILLVVVICGLGIVGNIMVVLVVMRTKHMRTATNCYLVSLAVADLMVLVAAGLPNITDSIYGSWVYGYVGCLCITYLQYLGINASSCSITAFTIERYIAICHPIKAQFLCTFSRAKKIIIFVWAFTSIYCMLWFFLLDLNISTYKDAIVISCGYKISRNYYSPIYLMDFGVFYVMPMILATVLYGFIARILFLNPIPSDPKENSKTWKNDSTHQNKNMNLNTTNRCFNSTVSSRKQVTKMLAVVVILFALLWMPYRTLVVVNSFLSSPFQENWFLLFCRICIYLNSAINPVIYNLMSQKFRAAFRKLCNCKQKPTEKAANYSVALNYSVIKESDRFSTELDDITVTDTYVSTTKVSFDDTCLASEKNGPSSCTYGYSLTAKQEKI
Protein: SKI-like proto-oncogene (A0A8I6A1B8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MENLQSNFSLVQGSNKKLSGMEDDGSPPVKKMMTDIHANGKTLTQVLPGPLLIPSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQRLCNALLRPRTFPQNGSILPAKSSWAQLKETGSAFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYLGTPEEKKLKIILEEMKEKFSMRNGKRIQSKTDTPSGMELPPWYPVIKQEGDHGPQTHSFLHPSYYLYMCDKVVAPNVSLASAASQSKAVTKAETNSSVSNNSTSKKKCESTICDLVRDTDKQGSGASSPLVVRDVTCEDDKGKIVEDVMRTYVRQQEKLSSILQKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKLEQVMKQKCTCDSNVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVKSSKTAKE
Protein: EG:171E4.4 protein (O46063)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPIDTRELMEAIAIVADERNVRVAVKQSGKGAAICAACSFAGGMLLGPVGLAVGGARRNRRLQDDKRHIPSAGRSHPKRPDGRTARAAGAARNHGRGRHTSHRRGDAAAADCPERLHSAGCA
Protein: Facilitated glucose transporter protein 1 (O44827)
Organism: Caenorhabditis elegans
Function: Facilitative glucose transporter that plays a role in glucose metabolism and regulation of longevity. May also play a role in lipid metabolism. Glucose transport activity of isoform a is competitively inhibited by mannose, galactose and fructose, suggesting ability to transport also other hexose sugars.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23826391, ECO:0000269|PubMed:24024580}; Multi-pass membrane protein {ECO:0000269|PubMed:23826391, ECO:0000269|PubMed:24024580}.; SUBCELLULAR LOCATION: [Isoform a]: Basolateral cell membrane {ECO:0000269|PubMed:23826391}; Multi-pass membrane protein {ECO:0000269|PubMed:23826391, ECO:0000269|PubMed:24024580}. Note=Detected on the basolateral but not on the apicolateral membrane of intestinal cells. {ECO:0000269|PubMed:23826391}.
Interaction partners:
- Sodium-dependent high-affinity dicarboxylate transporter 2
Sequence:
MSEKSRSDTSATASLSDSSKSPSSYSTPGTTTQKIIFPDGKLTKCLAFSAFVITLASFQFGYHIGCVNAPGGLITEWIIGSHKDLFDKELSRENADLAWSVAVSVFAVGGMIGGLSSGWLADKVGRRGALFYNNLLALAAAALMGLAKSVGAYPMVILGRLIIGLNCGFSSALVPMFLTEISPNNLRGMLGSLHQLLVTIAILVSQIFGLPHLLGTGDRWPLIFAFTVVPAVLQLALLMLCPESPKYTMAVRGQRNEAESALKKLRDTEDVSTEIEAMQEEATAAGVQEKPKMGDMFKGALLWPMSIAIMMMLAQQLSGINVAMFYSTVIFRGAGLTGNEPFYATIGMGAVNVIMTLISVWLVDHPKFGRRSLLLAGLTGMFVSTLLLVGALTIQNSGGDKWASYSAIGFVLLFVISFATGPGAIPWFFVSEIFDSSARGNANSIAVMVNWAANLLVGLTFLPINNLMQQYSFFIFSGFLAFFIFYTWKFVPETKGKSIEQIQAEFEKRK
Protein: Candida glabrata strain CBS138 chromosome L complete sequence (Q6FLR3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome B complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
Sequence:
MFKYNRPFLVSCVGSLFALYLVLKFVNNVFDLAGVLAVWFSANYIPDFRSVPGVEFYDLNDYTGLPDGWQRNDRILFCVPLRDAAEHLPMFFDHLNAMTYPHHLIDLSFLVSDSSDNTMGVLMHHLQQAQKDKNKRFGNIEIFEKDFGQIIGQSFSDRHGFAAQGPRRKLMARARNWLGSVAIKPYHSWVYWRDVDVEVIPRSIMEDLMHHDKDVIVPNVWRPLPDWLGNIQPYDLNSWVESEGGLQLADTLSEDSVIVEGYPEYATWRTHLAYMRDPNGNPEDEMMLDGIGGVSILSKARVFRAGSHFPAFSFQKHAETEAFGKLSRRMGFDVVGLPHYVIWHIYEPSTDDLKYMAWMAEEEKRKLEEIQLREFYDRIWEIGYEDVRDDWAHEKDIIFKNMETQKDIVVDWSDDADVSSNGDQSLNNANANNAAQQDKPLDFDPNK
Protein: Apidaecin 2+ (C0HKX9)
Organism: Pimpla disparis (Parasitic wasp) (Coccygomimus disparis)
Function: Antimicrobial peptide active against many Gram-negative enterobacterial and plant-associated bacterial species. Not active against other bacterial species like H.pylori, P.mirabilis, B.pertussis or N.gonorrhoeae.
Subcellular location: Secreted {ECO:0000269|PubMed:7929322}.
Interaction partners:
Sequence:
GKPNKPRPAPIKPRPPHPRL
Protein: CASP-like protein 2B1 (AtCASPL2B1) (Q8L9B5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000269|PubMed:24920445}; Multi-pass membrane protein {ECO:0000269|PubMed:24920445}.
Interaction partners:
Sequence:
MKLIDRRMRLTELLLRCSISVFALLALILVVTDTEVKLIFTIKKTAKYTDMKAVVFLVVANGIAAVYSLLQSVRCVVGTMKGKVLFSKPLAWAFFSGDQAMAYLNVAAIAATAESGVIAREGEEDLQWMRVCTMYGKFCNQMAIGVSSALLASIAMVFVSCISAFSLFRLYGATKDRRTTPW
Protein: RPW8-like protein 2 (AtHR2) (Q9SCS8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable disease resistance (R) protein.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Exocyst complex component SEC8
- Exocyst complex component SEC6
- Exocyst complex component SEC5A
- Exocyst complex component SEC5B
- Exocyst complex component SEC3A
- Exocyst complex component SEC3B
- Exocyst complex component EXO84B
- Exocyst complex component EXO84C
- Exocyst complex component EXO84A
- Protein PHLOEM PROTEIN 2-LIKE A6
Sequence:
MPLTEIIAGAALGLALQILHEAIQRAKDRSLTTSCILDRLDSTILRITPLMAKVEKLNKESDESLRKVFEDLKHLLEKAVVLVEAYAELKRRNLLGKYRYKRRIKELEGSLKWMVDVDVKVNQWADIKDLMAKMSEMNTKLEKIMGQPIDCIISEDNTNMDIVERVDPSLEAKAGCSNSDSKPKIDIHLRWSKQSKDHGIRFVLN
Protein: Peroxygenase 1 (AtPXG1) (EC 1.11.2.3) (Caleosin-1) (Embryo-specific protein 1 (ATS1)) (O81270)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies. May be involved in the interaction between oil bodies and vacuoles during seed germination and in the oxylipin signaling pathways and plant defense responses. Can catalyze sulfoxidation of thiobenzamide, hydroxylation of aniline, epoxidation of oleic acid or intramolecular oxygen transfer.
Subcellular location: Microsome membrane {ECO:0000269|PubMed:11197322}. Lipid droplet {ECO:0000269|PubMed:11197322}.
Interaction partners:
- Cytochrome P450 704B1
- Cytochrome P450 86A1
- Protein HOTHEAD
- Vicilin-like seed storage protein At2g28490
- Oleosin 18.5 kDa
- Oleosin 21.2 kDa
- Very-long-chain enoyl-CoA reductase
- Acyl-CoA thioesterase family protein.
- Acyl-CoA hydrolase 2
- Oleosin 14.9 kDa
Sequence:
MGSKTEMMERDAMATVAPYAPVTYHRRARVDLDDRLPKPYMPRALQAPDREHPYGTPGHKNYGLSVLQQHVSFFDIDDNGIIYPWETYSGLRMLGFNIIGSLIIAAVINLTLSYATLPGWLPSPFFPIYIHNIHKSKHGSDSKTYDNEGRFMPVNLELIFSKYAKTLPDKLSLGELWEMTEGNRDAWDIFGWIAGKIEWGLLYLLARDEEGFLSKEAIRRCFDGSLFEYCAKIYAGISEDKTAYY
Protein: Uncharacterized protein (Q583E2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGVAPSRETLKRGLYIVPPPTSGNGNSSGGHKKLDIVLVPLTKEFFPSADCPLFVQFHKTRCDAGVNYYFRHPGNPGDLSRIPNASSSDGKTSYPSREVLYSGVVERTEEMLFDTDEEMRLAHERSLRDERSGGPSSLSGERDKTADVKEKRVLPIMCAVAFRYDPEKLGQLQQNQATTGGGRAPHLQTLMANGVRVGGSIVNIVGCFGFVPMEVEGMQSLTSAPHTPVCPGIARSGSGSALTGLPRGPHSLAGVRGATSCSSSLDNQYLSVSSLQHCSMISGLTFHDNPTSFPTVYMQPNQRTPVSRNGTSSRVSSLCTTPTYDPYARQWTALQPEALPRERGRAMRHRSVAPEENFNRFFSLPPPVAAPLAAIVFLTKSAGEQNLGRVTFVAASTYYNQLVEAGVLKRRGKNALASSEVEKCHLPPLETFSFSSLMTNVPIISFVYEMRCRWEQFGLLSRQNSAPHSRTDSLNFSSASTSGLKAGAPPESANMGVSHENLEMWLTDDSMFHGRIGKELAERLCLSMAERPDVTSSRAEPLPDDRNYWRFCGLVDRKNQPPTQLCEGDDVSVDPVNVYVMGAAVIDGFDEGDVLRYDRTSRSWVADRNIPLDAVVLAAMRPFCKAARTAPPDDIGWVTTEVEEEDEKEVEAQDHAETAGEEGVDADATMRRKVCDGTVERKKKRVHVREGNFYIYRFELNGKVYYHGTVPDFANPNKKKLAQNLAAPAAGAVSPAASTVPAHPATGEKEKEQKPVAEKVKVENSTNKESVSTISALFSFFAGCGEGSERSYMSYLPTRVRYGAVQAAAQLMGVLFHTAPQFQPLPDRSAVATTSITSQTAFPPSAGLSAQPARRPSTFVKVGPEAEVNETRQVPNNAATGPRTFAKRFIDETAFIWDWRKS
Protein: Alpha-adducin (Erythrocyte adducin subunit alpha) (Q63028)
Organism: Rattus norvegicus (Rat)
Function: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Beta-adducin
- Gamma-adducin
- Ankyrin 2
- Ankyrin-3
- Tropomodulin-1
- Tropomodulin 4
- RCG25684, isoform CRA_a.
- Tropomodulin-2
- Dematin actin binding protein
- Ankyrin 1
Sequence:
MNGDTRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTASVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDRGSTNLGVNQAGFTLHSAIYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSLGEVAYHDYHGILVDEEEKILIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGGPDNLVLLDPGKYKAKSRSPGTPAGEGSGSPPKWQIGEQEFEALMRMLDNLGYRTGYPYRYPALRERSKKYSDVEVPASVTGHSFASDGDSGTCSPLRHSFQKQQREKTRWLNSGRGDDASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVMMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFNTLTDRELEEYRREVERKQKGSEENLDETREQKEKSPPDQSAVPNTPPSTPVKLEGGLPQEPTSRDGSDATTSKPTPPDLSPDEPSEALAFPTVAEEAHASPDTTQPLAEADPEPASASAPGAEEVASPATEEGSPMDPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSDS
Protein: Ornithine decarboxylase (ODC) (EC 4.1.1.17) (P07805)
Organism: Trypanosoma brucei brucei
Function: Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
Interaction partners:
Sequence:
MDIVVNDDLSCRFLEGFNTRDALCKKISMNTCDEGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVKCNDDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIRYARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTDDSLARCRLSVKFGAKVEDCRFILEQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHILDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVASAFTLAVNVIAKKVTPGVQTDVGAHAESNAQSFMYYVNDGVYGSFNCILYDHAVVRPLPQREPIPNEKLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVVGTSSFNGFQSPTIYYVVSGLPDHVVRELKSQKS
Protein: Capsid protein VP1 (Coat protein) (Q2NNN5)
Organism: Feline calicivirus (FCV)
Subcellular location: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MCSTCANVLKYYDWDPHIRLVIDPNRFLSVSFCDKPLLCCYPDLLPEFGTVWDCNQSPLEIYLESILGDDEWSSTFEAIDPVVPPMHWDEAGKIFQPHPGVLMHHLINQVAKAWDPNLPLFRLEADDGSITSPEQGTMVGGVIAEPSAQMSTAADMATGKSVDSEWEAFFSFHTSVNWSTSETQGKILFKQSLGPLLNPYLEHLAKLYVAWSGSVDVRFSISGSGVFGGKLAAIVVPPGVNPVQSTSMLQYPHVLFDARQVEPVIFSIPDLRSTLYHLMSDTDTTSLVIMVYNDLINPYASDSNSSGCIVTVETKPGPDFKFHLLKPPGSMLTHGSVPSDLIPKSSSLWIGNRHWTDITDFVIRPFVFQANRHFDFNQETAGWSTPRFRPITITISEKDGSKLGIGVAMDSIVPGIPDGWPDTTIPEKLVPAGDYAIANGTGNDITTAKDYDSATVIQNNTNFKGMYICGSLQRAWGDKKISNTAFITTATRSDNTITPSNVIDPTKIAVYQDTHVGAEVQTSDDTLAILGYTGIGEEAIGADRDRVVRISVLPETGARGGNHPIFYKNSIKLGYVIRSIDVFNSQILHTSRQLSLNNYLLPPDSFAVYRITDSNGSWFDIGIDSDGFSFVGASNVGKLEFPLTASYMGIQLAKIRLASNIRSSMTKL
Protein: RNA-binding protein 10 (G patch domain-containing protein 9) (RNA-binding motif protein 10) (RNA-binding protein S1-1) (S1-1) (P98175)
Organism: Homo sapiens (Human)
Function: May be involved in post-transcriptional processing, most probably in mRNA splicing. Binds to RNA homopolymers, with a preference for poly(G) and poly(U) and little for poly(A) (By similarity). May bind to specific miRNA hairpins.
Subcellular location: Nucleus {ECO:0000269|PubMed:18315527}. Note=In the extranucleolar nucleoplasm constitutes hundreds of nuclear domains, which dynamically change their structures in a reversible manner. Upon globally reducing RNA polymerase II transcription, the nuclear bodies enlarge and decrease in number. They occur closely adjacent to nuclear speckles or IGCs (interchromatin granule clusters) but coincide with TIDRs (transcription-inactivation-dependent RNA domains).
Interaction partners:
- Splicing factor U2AF 65 kDa subunit
- ATP-dependent RNA helicase DHX15
- G-patch domain and KOW motifs-containing protein
- SURP and G-patch domain-containing protein 1
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- Polypyrimidine tract-binding protein 1
- Splicing factor 3A subunit 1
- Proline-rich protein PRCC
- RNA-binding protein 4
- Splicing factor U2AF 35 kDa subunit
Sequence:
MEYERRGGRGDRTGRYGATDRSQDDGGENRSRDHDYRDMDYRSYPREYGSQEGKHDYDDSSEEQSAEDSYEASPGSETQRRRRRRHRHSPTGPPGFPRDGDYRDQDYRTEQGEEEEEEEDEEEEEKASNIVMLRMLPQAATEDDIRGQLQSHGVQAREVRLMRNKSSGQSRGFAFVEFSHLQDATRWMEANQHSLNILGQKVSMHYSDPKPKINEDWLCNKCGVQNFKRREKCFKCGVPKSEAEQKLPLGTRLDQQTLPLGGRELSQGLLPLPQPYQAQGVLASQALSQGSEPSSENANDTIILRNLNPHSTMDSILGALAPYAVLSSSNVRVIKDKQTQLNRGFAFIQLSTIVEAAQLLQILQALHPPLTIDGKTINVEFAKGSKRDMASNEGSRISAASVASTAIAAAQWAISQASQGGEGTWATSEEPPVDYSYYQQDEGYGNSQGTESSLYAHGYLKGTKGPGITGTKGDPTGAGPEASLEPGADSVSMQAFSRAQPGAAPGIYQQSAEASSSQGTAANSQSYTIMSPAVLKSELQSPTHPSSALPPATSPTAQESYSQYPVPDVSTYQYDETSGYYYDPQTGLYYDPNSQYYYNAQSQQYLYWDGERRTYVPALEQSADGHKETGAPSKEGKEKKEKHKTKTAQQIAKDMERWARSLNKQKENFKNSFQPISSLRDDERRESATADAGYAILEKKGALAERQHTSMDLPKLASDDRPSPPRGLVAAYSGESDSEEEQERGGPEREEKLTDWQKLACLLCRRQFPSKEALIRHQQLSGLHKQNLEIHRRAHLSENELEALEKNDMEQMKYRDRAAERREKYGIPEPPEPKRRKYGGISTASVDFEQPTRDGLGSDNIGSRMLQAMGWKEGSGLGRKKQGIVTPIEAQTRVRGSGLGARGSSYGVTSTESYKETLHKTMVTRFNEAQ