wanglab/gogpt-training-data huggingface dataset:
Protein: Cytosolic phospholipase A2 (cPLA2) (Phospholipase A2 group IVA) [Includes: Phospholipase A2 (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase); Lysophospholipase (EC 3.1.1.5)] (P47713)
Organism: Mus musculus (Mouse)
Function: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response. Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production. Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
Interaction partners:
- Polyunsaturated fatty acid 5-lipoxygenase
- Prostaglandin G/H synthase 2
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Mitogen-activated protein kinase 3
- Phospholipase A and acyltransferase 3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Arachidonate 12-lipoxygenase, 12R-type
- Protein kinase C alpha type
- Polyunsaturated fatty acid lipoxygenase ALOX8
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
Sequence:
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRQQRKENIKENMKKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYIAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIQNRMSMTLSSLKEKVNAARCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQNKGSTMEEELENITAKHIVSNDSSDSDDEAQGPKGTENEEAEKEYQSDNQASWVHRMLMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLSPLRDFSSQDSFDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHFVLANINFRKYKAPGVLRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKDAIVESIEYRRQNPSRCSVSLSNVEARKFFNKEFLSKPTV
Protein: Thrombopoietin receptor (TPO-R) (Myeloproliferative leukemia protein) (Proto-oncogene c-Mpl) (CD antigen CD110) (P40238)
Organism: Homo sapiens (Human)
Function: Receptor for thrombopoietin that acts as a primary regulator of megakaryopoiesis and platelet production. May represent a regulatory molecule specific for TPO-R-dependent immune responses.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15899890, ECO:0000269|PubMed:25538044, ECO:0000269|PubMed:32029621}; Single-pass type I membrane protein. Golgi apparatus {ECO:0000269|PubMed:25538044}. Cell surface {ECO:0000269|PubMed:25538044}.
Interaction partners:
- Thrombopoietin
- Tyrosine-protein kinase JAK2
- Erythropoietin
- Interleukin-3
- Calreticulin
- Integrin alpha-IIb
- Granulocyte colony-stimulating factor
- Kit ligand
- Non-receptor tyrosine-protein kinase TYK2
- Platelet glycoprotein IX
Sequence:
MPSWALFMVTSCLLLAPQNLAQVSSQDVSLLASDSEPLKCFSRTFEDLTCFWDEEEAAPSGTYQLLYAYPREKPRACPLSSQSMPHFGTRYVCQFPDQEEVRLFFPLHLWVKNVFLNQTRTQRVLFVDSVGLPAPPSIIKAMGGSQPGELQISWEEPAPEISDFLRYELRYGPRDPKNSTGPTVIQLIATETCCPALQRPHSASALDQSPCAQPTMPWQDGPKQTSPSREASALTAEGGSCLISGLQPGNSYWLQLRSEPDGISLGGSWGSWSLPVTVDLPGDAVALGLQCFTLDLKNVTCQWQQQDHASSQGFFYHSRARCCPRDRYPIWENCEEEEKTNPGLQTPQFSRCHFKSRNDSIIHILVEVTTAPGTVHSYLGSPFWIHQAVRLPTPNLHWREISSGHLELEWQHPSSWAAQETCYQLRYTGEGHQDWKVLEPPLGARGGTLELRPRSRYRLQLRARLNGPTYQGPWSSWSDPTRVETATETAWISLVTALHLVLGLSAVLGLLLLRWQFPAHYRRLRHALWPSLPDLHRVLGQYLRDTAALSPPKATVSDTCEEVEPSLLEILPKSSERTPLPLCSSQAQMDYRRLQPSCLGTMPLSVCPPMAESGSCCTTHIANHSYLPLSYWQQP
Protein: Photosystem II reaction center protein T (PSII-T) (P69674)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Seems to play a role in the dimerization of PSII.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00808}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00808}.
Interaction partners:
- Photosystem II reaction center protein L
- Photosystem II reaction center protein J
- Photosystem II CP47 reaction center protein
- Photosystem II reaction center protein H
- Cytochrome b559 subunit beta
- Photosystem II reaction center protein K
- Photosystem II CP43 reaction center protein
- Photosystem II D2 protein
- Photosystem II reaction center protein I
- Cytochrome b559 subunit alpha
Sequence:
MEALVYTFLLVSTLGIIFFAIFFREPPKVPTKKVK
Protein: HDC03337 (Q6IH48)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGPRLYPAAILILHCLLLLFLQVDSRGNQNHTQMERQRHLRAHNLHRPPYDGYDWHKHFNRDAEPKATVAKEKEEKTFKHRSGHLKKMKQTARDISNWSRARSAYQKETAELEEWGRKKNITDNELKLFFDGEISTKDKYRLFGDIQTVVQILKEVIKKGAVTEKEKAMITPELKPLILRFGRMFEREFAKNTNALEALQILVHEVQKSNSRNMRHKSAKRSH
Protein: Ferric uptake regulation protein (Ferric uptake regulator) (P0A0S8)
Organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)
Function: Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes. Regulates the expression of the fbp protein.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Leucyl/phenylalanyl-tRNA--protein transferase
Sequence:
MEKFNNIAQLKDSGLKVTGPRLKILDLFETHAEEHLSAEDVYRILLEEGVEIGVATIYRVLTQFEQAGILQRHHFETGKAVYELDKGDHHDHIVCVKCGEVTEFHNPEIEALQDKIAEENGYRIVDHALYMYGVCSDCQAKGKR
Protein: Vitamin K-dependent protein S (P53813)
Organism: Rattus norvegicus (Rat)
Function: Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis.
Subcellular location: Secreted.
Interaction partners:
- Tyrosine-protein kinase Mer
- Tyrosine-protein kinase receptor TYRO3
- Vitamin K-dependent gamma-carboxylase
- Tyrosine-protein kinase receptor UFO
- Coagulation factor V.
- Coagulation factor VIII
- Matrix Gla protein
- Growth arrest-specific protein 6
- Furin
- Vitamin K-dependent protein C
Sequence:
MRVLSVRFRVLLACLALVLPNSETNFLSKERASQVLVRKRRANTLLEETKKGNLERECIEELCNKEEAREVFENNPETDYFYPKYLGCLGAFRVGAFSAARQSANAYPDLRSCVNAIPDQCDPMPCNEDGYLSCKDGQGAFTCICKPGWQGDKCQFDINECKDPSNINGGCSQTCDNTPGSYHCSCKIGFAMLTNKKDCKDVDECSLKPSVCGTAVCKNIPGDFECECPNGYRYDPSSKSCKDVDECSENTCAQLCVNYPGGYSCYCDGKKGFKLAQDQRSCEGIPVCLSLDLDKNYELLYLAEQFAGVVLYLKFRLPDITRFSAEFDFRTYDSEGIILYAESLDHSNWLLIALREGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVEELDDSVSIKIAKEAVMNINKLGSLFKPTDGFLDTKIYFAGLPRKVESALIKPINPRLDGCIRGWNLMKQGALGAKEIVEGKQNKHCFLTVEKGSYYPGSGIAQFSIDYNNVTNAEGWQINVTLNIRPSTGTGVMLALVSGDTVPFALSLVDSGSGTSQDILVFVENSVAAHLEAITLCSEQPSQLKCNINRNGLELWTPVRKDVIYSKDLQRQLAILDKTMKGTVATYLGGVPDISFSATPVNAFYSGCMEVNINGVQLDLDEAISKHNDIRAHSCPSVRKIQKNF
Protein: Leucine-rich PPR-motif containing (Mitochondrial leucine-rich PPR motif-containing protein) (E5KNY5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAALLRSARWLLRAGAAPRLPLSLRLLPGGPGRLHAASYLPAARAGPVAGGLLSPARLYAIAAKEKDIQEESTFSSRKISNQFDWALMRLDLSVRRTGRIPKKLLQKVFNDTCRSGGLGGSHALLLLRSCGSLLPELKLEERTEFAHRIWDTLQKLGAVYDVSHYNALLKVYLQNEYKFSPTDFLAKMEEANIQPNRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAGIEPGPDTYLALLNAYAEKGDIDHVKQTLEKVEKSELHLMDRDLLQIIFSFSKAGYPQYVSEILEKVTCERRYIPDAMNLILLLVTEKLEDVALQILLACPVSKEDGPSVFGSFFLQHCVTMNTPVEKLTDYCKKLKEVQMHSFPLQFTLHCALLANKTDLAKALMKAVKEEGFPIRPHYFWPLLVGRRKEKNVQGIIEILKGMQELGVHPDQETYTDYVIPCFDSVNSARAILQENGCLSDSDMFSQAGLRSEAANGNLDFVLSFLKSNTLPISLQSIRSSLLLGFRRSMNINLWSEITELLYKDGRYCQEPRGPTEAVGYFLYNLIDSMSDSEVQAKEEHLRQYFHQLEKMNVKIPENIYRGIRNLLESYHVPELIKDAHLLVESKNLDFQKTVQLTSSELESTLETLKAENQPIRDVLKQLILVLCSEENMQKALELKAKYESDMVTGGYAALINLCCRHDKVEDALNLKEEFDRLDSSAVLDTGKYVGLVRVLAKHGKLQDAINILKEMKEKDVLIKDTTALSFFHMLNGAALRGEIETVKQLHEAIVTLGLAEPSTNISFPLVTVHLEKGDLSTALEVAIDCYEKYKVLPRIHDVLCKLVEKGETDLIQKAMDFVSQEQGEMVMLYDLFFAFLQTGNYKEAKKIIETPGIRARSARLQWFCDRCVANNQVETLEKLVELTQKLFECDRDQMYYNLLKLYKINGDWQRADAVWNKIQEENVIPREKTLRLLAEILREGNQEVPFDVPELWYEDEKHSLNSSSASTTEPDFQKDILIACRLNQKKGAYDIFLNAKEQNIVFNAETYSNLIKLLMSEDYFTQAMEVKAFAETHIKGFTLNDAANSRLIITQVRRDYLKEAVTTLKTVLDQQQTPSRLAVTRVIQALAMKGDVENIEVVQKMLNGLEDSIGLSKMVFINNIALAQIKNNNIDAAIENIENMLTSENKVIEPQYFGLAYLFRKVIEEQLEPAVEKISIMAERLANQFAIYKPVTDFFLQLVDAGKVDDARALLQRCGAIAEQTPILLLFLLRNSRKQGKASTVKSVLELIPELNEKEEAYNSLMKSYVSEKDVTSAKALYEHLTAKNTKLDDLFLKRYASLLKYAGEPVPFIEPPESFEFYAQQLRKLRENSS
Protein: Cation-efflux pump FieF (Ferrous-iron efflux pump FieF) (P69380)
Organism: Escherichia coli (strain K12)
Function: Divalent metal cation transporter which exports Zn(2+), Cd(2+) and possibly Fe(2+). May be involved in zinc and iron detoxification by efflux. In vitro, can also bind, but probably not transport, Hg(2+), Co(2+), Ni(2+), Mn(2+), Ca(2+) and Mg(2+).
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01425, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16049012, ECO:0000269|PubMed:19749753}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01425, ECO:0000269|PubMed:16049012, ECO:0000269|PubMed:19749753}.
Interaction partners:
- Zinc/cadmium/lead-transporting P-type ATPase
- Zinc transporter ZupT
- Zinc transport protein ZntB
- PTS system fructose-like EIIA component
- Malate dehydrogenase
- tRNA-specific adenosine deaminase
- HTH-type transcriptional regulator ZntR
- Putative multidrug resistance protein MdtD
Sequence:
MNQSYGRLVSRAAIAATAMASLLLLIKIFAWWYTGSVSILAALVDSLVDIGASLTNLLVVRYSLQPADDNHSFGHGKAESLAALAQSMFISGSALFLFLTGIQHLISPTPMTDPGVGVIVTIVALICTIILVSFQRWVVRRTQSQAVRADMLHYQSDVMMNGAILLALGLSWYGWHRADALFALGIGIYILYSALRMGYEAVQSLLDRALPDEERQEIIDIVTSWPGVSGAHDLRTRQSGPTRFIQIHLEMEDSLPLVQAHMVADQVEQAILRRFPGSDVIIHQDPCSVVPREGKRSMLS
Protein: ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase) (P52034)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
Interaction partners:
- Glucose-6-phosphate isomerase
- Enolase
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase
- Fructose-1,6-bisphosphatase isozyme 2
- Pyruvate kinase
- Glycogen phosphorylase
- Probable transaldolase
- transketolase
- 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase long form)
Sequence:
MNSEINQRFLARGSQKDKGLAVFTSGGDSQGMNAAVRACVRMAIYLGCKVYFIREGYQGMVDGGDCIQEANWASVSSIIHRGGTIIGSARCQDFRERQGRLKAANNLIQRGITNLVVIGGDGSLTGANLFRQEWSSLLDELVKNKTITTEQQEKFNVLHIVGLVGSIDNDFCGTDMTIGTDTALHRIIEAIDAISSTAYSHQRTFIMEVMGRHCGYLALVGGLACEADFIFIPEMPPKVDWPDRLCSQLAQERSAGQRLNIVIVAEGAMDREGHPITAEDVKKVIDERLKHDARITVLGHVQRGGNPSAFDRILACRMGAEATLALMEATKDSVPVVISLDGNQAVRVPLMECVERTQAVAKAMAEKRWADAVKLRGRSFERNLETYKMLTRLKPPKENFDADGKGIEGYRLAVMHIGAPACGMNAAVRSFVRNAIYRGDVVYGINDGVEGLIAGNVRELGWSDVSGWVGQGGAYLGTKRTLPEGKFKEIAARLKEFKIQGLLIIGGFESYHAAGQIADQRDNYPQFCIPIVVIPSTISNNVPGTEFSLGCDTGLNEITEICDRIRQSAQGTKRRVFVIETMGGYCGYLATLAGLAGGADAAYIYEEKFSIKDLQQDVYHMASKMAEGVSRGLILRNEKASENYSTDFIYRLYSEEGKGLFTCRMNILGHMQQGGSPTPFDRNMGTKMAAKCVDWLAAQIKANIDANGVVNCKSPDTATLLGIVSRQYRFSPLVDLIAETNFDQRIPKKQWWLRLRPLLRILAKHDSAYEEEGMYITVEEECDTDAVA
Protein: Hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) (A0A8I6ANS1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MCTGIWKMLVAAVCLALLGCLQAQEFRGHVSIILLGATGDLAKKYLWQGLFQLYLDEAGKGHSFSFHGAALTAPQQGQKLMDKALESLSCPKDLVPSRCDELKAQFLQLSQYRQLKTVEDYQTLNKDIETQVQQDGLWEAGRVFYFSVPPFAYADIARNINSSCRPHPGAWLRVVFEKPFGHDHLSAQQLASELGSFFQEEEMYRVDHYLGKQAVAQILPFRDQNRKALDGLWNRHHVERVEIILKETVDAGGRASFYEEYGVIRDTLQNHLTEILTLVAMELPPNISSSAAVLQHKLQAFQALRGLQKSNAILGQYQAYSGQVRQELQKPDGFQSLTPTFAGVLVHIDNLRWEGVPFILMSGKALDERVGYVRILFKNRAYCTQGERHWVPERSRCLPQQIVFYIGHGELGHPAILVSKNLFKPSLPAQSWKGVQDQPGLHLFGRPLSDYYAYRPVREQDAYSTLLSHIFHCRKESFITTENLLASWVFWTPLLDSLSFEVPRLYPGGAENDHLLDFEFSGGQLTFSQQQLEVLMPELGSVPKPSDFQVLRAQYRKSPLITAWPEELISKLANDIEAAAVQAVRRFGKFHLALSGGSSPIALFQQLATGHYSFPWAYTHLWLVDERCVPLSDPDSNFQGLQAHLLQHVRVPYYNIHPMPVHLHQRLCAEEDQGAQTYASEISALVANSSFDLVLLGMGTDGHTASLFPQSPRGLDGDQLVVLTESPFRPHQRMSLSLPLINRAKKVAVLVMGRTKREITTLVSRVGHEPKKWPISGVVPLSGQLVWYMDYEAFLG
Protein: Calnexin (D6RFL1)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
Sequence:
MKESKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGIYEEKHAKRPDADLKTYFTDKKTHLYT
Protein: E3 ubiquitin-protein ligase RLIM (EC 2.3.2.27) (LIM domain-interacting RING finger protein) (RING finger LIM domain-binding protein) (R-LIM) (RING finger protein 12) (RING-type E3 ubiquitin transferase RLIM) (Q9WTV7)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex-related dosage differences of X-encoded genes in somatic cells of female placental mammals.
Subcellular location: Nucleus {ECO:0000269|PubMed:19945382}.
Interaction partners:
- Axin-2
- Neurite extension and migration factor
- Ubiquitin-ribosomal protein eS31 fusion protein
- Cysteine-rich hydrophobic domain-containing protein 1
Sequence:
MENSDSNDKGSDQSAAQRRSQMDRLDREEAFYQFVNNLSEEDYRLMRDNNLLGTPGESTEEELLRRLQQIKEGPPPQSPDENRAGESSDDVTNSDSIIDWLNSVRQTGNTTRSGQRGNQSWRAVSRTNPNSGDFRFSLEINVNRNNGSQTSENESEPSTRRLSVENMESSSQRQMENSASESASARPSRAERNSAEAVTEVPTTRAQRRARSRSPEHRRTRARAERSRSPLQPTSEIPRRAPTLEQSSENEPEGSSRTRHHVTLRQQISGPELLGRGLFAASGSRNPSQGTSSSDTGSNSESSGSGQRPPTIVLDLQVRRVRPGEYRQRDSIASRTRSRSQAPNNTVTYESERGGFRRTFSRSERAGVRTYVSTIRIPIRRILNTGLSETTSVAIQTMLRQIMTGFGELSYFMYSDSDSEPSASVSSRNVERVESRNGRGSSGGGNSSGSSSSSSPSPSSSGESSESSSEMFEGSSEGGSSGPSRRDGRHRAPVTFDESGSLPFLSLAQFFLLNEDDEDQPRGLTKEQIDNLAMRSFGENDALKTCSVCITEYTEGNKLRKLPCSHEYHVHCIDRWLSENSTCPICRRAVLSSGNRESVV
Protein: Myosin regulatory light chain cdc4 (Q09196)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in cytokinesis. Required for the formation and function of the contractile ring.
Subcellular location: Cytoplasm.
Interaction partners:
- Myosin type-2 heavy chain 1
- Ras GTPase-activating-like protein rng2
- Myosin type-2 heavy chain 2
- Cell division control protein 15
- Anillin-related medial ring protein mid1
- Myosin regulatory light chain 1
- Cell division control protein 12
- Actin
- Myosin-51
- Myosin-1
Sequence:
MSTDDSPYKQAFSLFDRHGTGRIPKTSIGDLLRACGQNPTLAEITEIESTLPAEVDMEQFLQVLNRPNGFDMPGDPEEFVKGFQVFDKDATGMIGVGELRYVLTSLGEKLSNEEMDELLKGVPVKDGMVNYHDFVQMILAN
Protein: At1g55915 (Zinc ion binding protein) (Q0WPG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSSANLEDLNKVWEIKALKRKPREDEARKILEKVANQVQPIMTRRKWRVKLLSEFCPTNPRLLGVNVNRGVQVKLRLRRVNHDLDFLSYHEILDTMLHELCHNAHGPHNASFYKLWDELRKECEELMSKGITGTGQGFDMPGKRLGGLSRQPSLSFLRATAATAAEKRVRAGTLLPSGPQRLGGDSSIMSDLSPIQAAAMAAERRLLDDIWCGSQSTDALEDEENDSDTYKEPVSIRETCTSVNGKSVKRCNSWSNAHSCPPSSSHQQGSDVIDLTEESFEIRCTKRNRSPGDQGPSCAKDVPNAGVMKSSIPLPSTSYNANQSREESTMWECAECTLLNPSLAPICELCTAAKPKEREMKHKVWSCKFCTLENEVKLEKCEACGQWRYSYGAPLSTGAPNVGT
Protein: Sestrin homolog (Q54WU6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May function as a negative feedback regulator of TOR function.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y6P5}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6P5}.
Interaction partners:
- DEP domain-containing protein DDB_G0279099
- UPF0171 family protein
- GATOR2 complex protein WDR24
- NPR2 family protein
- Peroxiredoxin-4
- GATOR2 complex protein MIOS
- Eukaryotic translation initiation factor 4E
Sequence:
MISMGMTSKGQNVDGAPAGNSSSEWIISSSSSPFQANKRYSLDPPFGSDYSPPASPQNELDPLSSYFLNLQSEDNDVRKTAIEYIINTLSNPDNEKLIKNHLPMIVVLSTESPFDDISEAFTNFLKPIQEKYHIPKQRTTVFTSESQLPPLNTDDELTRKLFQDVFLQHGRVNHLTRILGWHPQYLEKFLLAYNTIMRDPGPLPLHWRNYIGILAAARYKCSYIIALQEHEFLMNNGDARWLQGIDHIPAKLKNLLKVIELLAHQPWLLPKLDIEYLVKGTDAWSIAELVHAMVLICTFLSLSGFVFCCGISPECGLSESNNLSSSFSLNDSDCEIEDTAATENTAKVMELLKNRRSQQQDDDDDDQLHDRQQDFHNAGDDSQSSNNNTTTTTTTTTTTTTTTNTNTTSNSAGGGDSSSSTLSQSSDRMSDFSRYIGNNTMTHTDFDVSSKLYNIFSAQEYSWREHGYELVSRYFPDAAPLLDEEFSFVYTMTYYKFNNNTDIDTLPFRRAVWYYVQRVKGMLHDDYNYQEVNMFLSRSLKNFVKKAVCFPETIKRDDYSKLGYSLKPDEKCHLSLLAVCSHKQASLLYGLYSVMNYQNRR
Protein: Eukaryotic elongation factor 2 kinase (EC 2.7.11.20) (E7F318)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAEEELMFSMEEVGSARDGSRNRCVKNRVCFQNSNASDDDDEEDEDDLRICPITDDIISPTKGFCEFPKNLAHNQQLSNSLPKNSFTYKNKNDNIEDVRFGSLTEKGRATWKHAIEKAKAMPDPWAEFHLEEMETERCTRYRYSAITGEWAKDEIFIKVSSQTFGKGAMRECFRAKKLSNFSHSHNWKSASNYVAKRYMETVDRSVYFEDVRLQMEAKLWGEEFNRHRPPKQVDIMQMCVVEMTTRPGSPLFHLEHYIEGKYTKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTSKGTDFGDGNLGVRGMALFFHSHLCNKICRSMGLTRFDLSPAEIAQLDCTNKLLQSAKTVLRGFEEQCGSPRVRTTSLGHMPVLLSRLSETSSVDESSDTDSIPCSPLSMGVSVGRSPMGWSFMNEMNETHRSQNTEQQDSENGGDSGYPSEKRSEGDPVEHHGQGRPIYNRHYSESDEDSVRRLTEEKWSFYHSSRSHIHRPSCVAVEVERLNALLLEKKIGKSILGKVHLAMVRYHEAGRFCEKDEPWDQISAMYHLETAAMCGELEAIVALGQCYLQLPHHILPEIELEPSEENSQKGFRFLLQAAEAGDRPSMILVARAFDTGLKLPSDRAMDWTEAVHWYDSALKMTDYDEGGEFDGMQDEPRYLLLARLAEMYQEGGNNLDADPQRAGDLFTEAADAAMEAMKGRLANQYYMKAEEAWAMMEE
Protein: Anthranilate 1,2-dioxygenase ferredoxin subunit (Q84BZ1)
Organism: Burkholderia cepacia (Pseudomonas cepacia)
Function: Part of the multicomponent anthranilate dioxygenase, that converts anthranilate to catechol. This protein seems to be a 2Fe-2S ferredoxin.
Interaction partners:
- Anthranilate 1,2-dioxygenase small subunit
- Anthranilate 1,2-dioxygenase system ferredoxin--NAD
- Anthranilate 1,2-dioxygenase large subunit
- CDP-6-deoxy-delta-3,4-glucoseen reductase
- Pyridine nucleotide-disulfide oxidoreductase
Sequence:
MTEATLAEWHPLGAIDEFTEDEPAARVAGQKPIAVFRIGDELFAMHDLCSHGHARLSEGYVEDGCVECPLHQGLIDIRTGAPKCAPITEPVRVYPIRIVDGQVEVNVG
Protein: Candida glabrata strain CBS138 chromosome L complete sequence (Q6FL30)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Negative regulator of the PHO system
- Cyclin-dependent kinase 1
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome E complete sequence
- Adenylate cyclase
- Serine/threonine-protein phosphatase
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
Sequence:
MKFGKYLEARQVELAEYNTHFIDYKALKKLMKQLATVPMINDDDLNASKNLINVDIDFNEASVYRSLQANKASFFFKLERELEKVNLYYVDKESELKVKLDVIVSKMNDYRSSGRLNSKQAVVYKNISAVIKKFLKDVRNLEQYVELNRTGFAKVLKKWDKRSHSNEKEFYLATVVSVQPIFTRTEVARLSDEALNLLVDLNDLVEYSVGNGVNSPSTALGPGSSSNAVAISMDGGKNNSNNTKARRSSSSTGSEKGFFKVLGFSSTDLDLEIEYWIQDIINISTLKDDQRRLATISNFVPTKVLPRLEELLQNNEQKEQIEKECITKLFSLLIDSNLVDECLSVVYLACEQYIDFNHIDEDAEIFSNVNLFHEACACSTAPRSFLLYEALKFKNITSADLKNLMNMKDIHGRIPLHHAAEQGKTEFVELILESNLVDMLDIPDQDRKTPLILALESNDIKAVKLLLQHGSNAYPNAQDKVLDPLSVACKKGNFEAVKLILDFLGDKIEGPSLDKMELLHIVSKNSNSSALAELLISKGANVNYGDKFLGRTPLFYAVMNGKDNIVSLLLRCNASIDVMDDEGYTPLFYTIWESDVKVLNAMLPSIKSIKQKKIHSDLLQPKKLTLPNNDLLDLDSSSINDLTDSFENIPAFSLPPPIIPLRKYGHNFLEDKIYVKVIFKAGTESITLENDNDSLINAPGRIMLSSGSSDIIPRNVLFPVGGTSVTAVDDDLDEEGEIIFYPDTLENFSIQFDVFPTTGNRLIARTVTPPSFLLSSSMNGTNSLKIPLVDLKLSVIGTLSVEYQVIQPFSGTSLKVTECEPYWKSTNEEKEPQNSEPSKIDNGYITETSLCGSFETIKIYYLNDGRLVASKEMFVTVNGAKILLMDLTTEQLQAILQSSLFIDNEMINTSNDLKILLCKGVFDFKTLLDLIPSSIKLNIQICFPTAEEIVSIPVRPSPLIAVDKLINNLLEMIFSNERYLKSTTNHSRSLVFSSCCWEVCATLNWKQPIFPVFLKFDNLVSYVDPESSTECYKYDTAHHILDLVQNQEEYKKLIKKIDIFGMVKFAIKSHLLGLILPEKLLHICDTVVDSIRKKGLLVISFSDSPINEAEKELNANGVSDEDEIIFLKSGDDKNLML
Protein: Chromaffin granule amine transporter (Solute carrier family 18 member 1) (Vesicular amine transporter 1) (VAT1) (Q01818)
Organism: Rattus norvegicus (Rat)
Function: Electrogenic antiporter that exchanges one cationic monoamine with two intravesicular protons across the membrane of secretory and synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to accumulate high concentrations of monoamines inside the vesicles prior to their release via exocytosis. Transports catecholamines and indolamines with higher affinity for serotonin. Regulates the transvesicular monoaminergic gradient that determines the quantal size. Mediates presynaptic monoaminergic vesicle transport in the amygdala and prefrontal brain regions related with emotion processing in response to environmental stimuli (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P54219}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q8R090}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Vesicular inhibitory amino acid transporter
- Vesicular glutamate transporter 1
- Vesicular glutamate transporter 2
- Vesicular glutamate transporter 3
- Vesicular acetylcholine transporter
- Alpha-synuclein
- Synaptic vesicular amine transporter
Sequence:
MLQVVLGAPQRLLKEGRQSRKLVLVVVFVALLLDNMLLTVVVPIVPTFLYATEFKDSNSSLHRGPSVSSQQALTSPAFSTIFSFFDNTTTTVEEHVPFRVTWTNGTIPPPVTEASSVPKNNCLQGIEFLEEENVRIGILFASKALMQLLVNPFVGPLTNRIGYHIPMFVGFMIMFLSTLMFAFSGTYALLFVARTLQGIGSSFSSVAGLGMLASVYTDNYERGRAMGIALGGLALGLLVGAPFGSVMYEFVGKSSPFLILAFLALLDGALQLCILWPSKVSPESAMGTSLLTLLKDPYILVAAGSICLANMGVAILEPTLPIWMMQTMCSPEWQLGLAFLPASVAYLIGTNLFGVLANKMGRWLCSLVGMVAVGISLLCVPLAHNIFGLIGPNAGLGFAIGMVDSSLMPIMGYLVDLRHTSVYGSVYAIADVAFCVGFAIGPSTGGVIVQVIGFPWLMVIIGTINIIYAPLCCFLQNPPAKEEKRAILSQECPTETQMYTFQKPTKAFPLGENSDDPSSGE
Protein: Aldehyde dehydrogenase (P96824)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Acetyl-coenzyme A synthetase
- NADP-dependent alcohol dehydrogenase C
- 4-aminobutyrate aminotransferase
- methylmalonate-semialdehyde dehydrogenase
- Probable fatty oxidation protein FadB
- Acetate kinase
- Probable zinc-type alcohol dehydrogenase
- Alcohol dehydrogenase B
- Probable alcohol dehydrogenase adh
- Glutamate decarboxylase
Sequence:
MSDRVKAVAPPDGRTMMTTESVARKTQKSETEAPREPAPVSDEKQTDVAKTVARLRKTFASGRTRSVEWRKQQLRALQKLMDENEDAIAAALAEDLDRNPFEAYLADIATTSAEAKYAAKRVRRWMRRRYLLLEVPQLPGRGWVEYEPYGTVLIIGAWNYPFYLTLGPAVGAIAAGNAVVLKPSEIAAASAHLMTELVYRYLDTEAIAVVQGDGAVSQELIAQGFDRVMFTGGTEIGRKVYEGAAPHLTPVTLELGGKSPVIVAADADVDVAAKRIAWIKLLNAGQTCVAPDYVLADATVRDELVSKITAALTKFRSGAPQGMRIVNQRQFDRLSGYLAAAKTDAAADGGGVVVGGDCDASNLRIQPTVVVDPDPDGPLMSNEIFGPILPVVTVKSLDDAIRFVNSRPKPLSAYLFTKSRAVRERVIREVPAGGMMVNHLAFQVSTAKLPFGGVGASGMGAYHGRWGFEEFSHRKSVLTKPTRPDLSSFIYPPYTERAIKVARRLF