wanglab/gogpt-training-data huggingface dataset:
Protein: DNA polymerase alpha subunit B (DNA polymerase alpha 73 kDa subunit) (Q9VB62)
Organism: Drosophila melanogaster (Fruit fly)
Function: Accessory subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit PolA1, an accessory subunit PolA2 and two primase subunits, the catalytic subunit Prim1 and the regulatory subunit Prim2) is recruited to DNA at the replicative forks (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:7592543}.
Interaction partners:
- DNA polymerase alpha catalytic subunit
- DNA primase large subunit
- DNA primase small subunit
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon catalytic subunit 1
- DNA polymerase epsilon subunit 2
- DNA polymerase delta subunit 2
- DNA polymerase zeta catalytic subunit
- Replication factor C subunit 3
- DNA replication licensing factor Mcm2
Sequence:
MEEELKQQFDEMGVEPADAVLGRCAELAITYNIHDATEFVEQWMAFSLSHLQGEDPAIENLGDFERKVLQLRKDKAGYKATGQKAKSYGSPSVQDTSSLATYGVMEDDPMLDDYVSESAVDSSALHTPKAKKQSDRTANLKGAALFSPASYTPQSAKRKAGLETPSNSVAGKPGDIVDTFGHPKLLAGSSWQSQMEHTVPVTQKLLHNDAPLTIANLGYMNDLLTDRCHNLRVRFNQTGPALVDKKLGQAGAAECIWYPQDRQVLQSAGGLHAVGMIHSEDDGPLDAHSAFMAVLDDDVEDEMDPTLTLNFSRVKSASIFPGQVVLAKGFIPRGKTFMVEEIHTERKLTPATPLQIDRELQFVVASGPFTDSTDLFYEPLHDLLKYLKDHRPDVLVLTGPFLDADHKMVGELAETFDTFFEKMIGGIMESIGSHTAVLVVTSQKDAMALSVYPTPPPALRRTYPNLYMLPDPSLVDLDGFTLGVTSTDVVDHLLSHEFAVNAGERMHRAINHLFHQGSFYPLYPPADEDMAYDSQLALKYAQLKQLPNVLILPSDQRHFIRLVNDCLVINPGRVADKKGGTFARFLVAPSVPGKAANMFNSVACQVQRI
Protein: Myosin 1 (F4JCF9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSQKVTPFMQSLKSLPADYRFDGSPVSDRLENSSGASVRLTNSNVPRKGGLRNGVSRTDTAAGDSEDSPYSGHGVFVEEQSLTDDVDSGAATMPLPQSDERRWSDTSAYARKKILQSWIQLPNGNWELGKILSTSGEESVISLPEGKVIKVISETLVPANPDILDGVDDLMQLSYLNEPSVLYNLNYRYNQDMIYTKAGPVLVAVNPFKEVPLYGNRYIEAYRKKSNESPHVYAIADTAIREMIRDEVNQSIIIRCICIHESMTYSISSSSGESGAGKTETAKIAMQYLAALGGGSGIEYEILKTNPILEAFGNAKTLRNDNSSRFGKLIEIHFSESGKISGAQIQTFLLEKSRVVQCAEGERSYHIFYQLCAGASPALREKLNLTSAHEYKYLGQSNCYSINGVDDAERFHTVKEALDIVHVSKEDQESVFAMLAAVLWLGNVSFTVIDNENHVEPVADESFLFHSLGSWCWKQECLLHNMCLSTVAKLIGCNINELTLTLSKRNMRVRNDTIVQKLTLPQAIDARDALAKSIYSCLFDWLVEQINKSLAVGKRRTGRSISILDIYGFESFDKNSFEQFCINYANERLQQHFNRHLFKLEQEEYIQDGIDWTRVDFEDNQNCLSLFEKKPLGLLSLLDEESTFPNGTDLTLANKLKQHLQSNSCFRGDKGKLFTVVHYAGEVTYETTGFLEKNRDLLHSDSIQLLSSCSCLLPQAFASSMLIQSEKPVVGPLYKAGGADSQRLSVATKFKSQLFQLMQRLGNTTPHFIRCIKPNNIQSPGVYEQGLVLQQLRCCGVLEVLCKGPYKRFFIIAILHQFNILPEMYQVGYTKLFFRTGQIGVLEDTRNRTLHGILRVQSSFRGYQARCLLKELKRGISILQSFVRGEKIRKEFAELRRRHKAAATIQSQVKSKIARIQYKGIADASVVIQSAIRGWLVRRCSGDIGWLKSGGAKTNELGEVLVKASVLSELQRRVLKAEAALREKEEENDILQQRLQQYENRWSEYETKMKSMEEIWQKQMRSLQSSLSIAKKSLAVEDSARNSDASVNASDATDWDSSSNQFRSQTSNGVGSRLQPMSAGLSVIGRLAEEFEQRAQVFGDDAKFLVEVKSGQVEANLDPDRELRRLKQMFETWKKDYGGRLRETKLILSKLGSEESSGSMEKVKRKWWGRRNSTRY
Protein: Pleckstrin homology domain-containing family G member 5 (PH domain-containing family G member 5) (Neuronal RhoA GEF protein) (Transcript highly enriched in cortex and hippocampus) (Q6RFZ7)
Organism: Rattus norvegicus (Rat)
Function: Functions as a guanine exchange factor (GEF) for RAB26 and thus regulates autophagy of synaptic vesicles in axon terminal of motoneurons (By similarity). Involved in the control of neuronal cell differentiation. Plays a role in angiogenesis through regulation of endothelial cells chemotaxis. Affects also the migration, adhesion, and matrix/bone degradation in macrophages and osteoclasts (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16467373}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16467373}. Cell membrane {ECO:0000269|PubMed:16467373}. Cell junction {ECO:0000250|UniProtKB:Q66T02}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q66T02}. Note=Predominantly cytoplasmic, however when endothelial cells are stimulated with lysophosphatidic acid, PLEKHG5 is found in perinuclear regions and at the cell membrane (PubMed:16467373). Localizes at cell-cell junctions in quiescent endothelial cells, and relocalizes to cytoplasmic vesicle and the leading edge of lamellipodia in migrating endothelial cells (By similarity). {ECO:0000250|UniProtKB:Q66T02, ECO:0000269|PubMed:16467373}.
Interaction partners:
- Rho-related GTP-binding protein RhoE
Sequence:
MDKGRAAKVCHHADCQQLHHRGPLNLCEICDSKFHNTTHYDGHVRFDLPPQGSVLARNVSTRSCPPRTSPAGDLEEEDEGYTNGKGDRKSAGLKISKKKARRRHTDDPSKECFTLKFDLNVDIETEIVPAMKKKSLGEVLLPVFERKGIALGKVDIYLDQSNTPLSLTFEAYRFGGHYLRVKAKPGDEGKVEQGVKDSKSLSLPALRPSGAGTPVLERVDPQSRRESSLDILAPGRRRKNMSEFLGDTSIPGQESPAPSSCSLPVGSSVGSSGSSESWKNRAASRFSGFFSSSPSTGAFGREVDKMEQLESKLHAYSLFGLPRMPRRLRFDHDSWEEEEDDEEEEDNSGLRLEDSWRELIDGHEKLTRRQCHQQEAVWELLHTEVSYIRKLRVITNLFLCCLLNLQESGLLCEVEAERLFSNIPELARLHRGLWSSVMVPVLEKARRTRALLQPSDFLKGFKMFGSLFKPYIRYCMEEEGCMEYMRSLLRDNDLFRAYVTWAEKHQQCQRLKLSDMLAKPHQRLTKYPLLLKSVLRKTDEPRAKEAIITMISSVERFIHHVNTCMRQRQERQRLAGVVSRIDAYEVVEGSNDEVDKFLKEFLHLDLTAPMPGTSPEETRQLLLEGSLRMKEGKDSKMDVYCFLFTDLLLVTKAVKKAERTKVIRPPLLVDKIVCRELRDPGSFLLIHLNEFHSAVGAYTFQASSQALCRSWVDTLYNAQNQLQQLRAQLLCAQEHPGTQHLQSLEEEEDEQEEEGEESGTSAASSPTILRKSSNSLDSEHCASDGSTETLAMVVVEPGETLSSPEFDRGPFSSQSDEASLSNTTSSITPTSELLPLGPVDGRSCSMDSAYGTLSPTSLQDFAAPHPVVEPVPVPQTLSPQPSPRLRRRTPVQLLPRLPHLLKSKSEASLLQLLSGTTTSVSPPAPSRSLSELCLITMAPGVRTQSSLQEGGPGWNCPGACGPCQGPPLSESENRPSHKAGGPADSARRKCREMPCGTVPRVQPEPSPGISAQHRKLTLAQLYRIRTTLLLNSTLTASEV
Protein: Glycerol-3-phosphate dehydrogenase, mitochondrial (GPD-M) (GPDH-M) (EC 1.1.5.3) (P32191)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
Interaction partners:
- Glycerol kinase
- Glycerol-3-phosphate dehydrogenase [NAD
- Dihydroxyacetone kinase 1
- External NADH-ubiquinone oxidoreductase 2, mitochondrial
- External NADH-ubiquinone oxidoreductase 1, mitochondrial
- Glycerol-3-phosphate dehydrogenase [NAD
- Dihydroxyacetone kinase 2
- L-lactate dehydrogenase
- Glycerol-3-phosphate O-acyltransferase 2
- Glycerol-3-phosphate O-acyltransferase 1
Sequence:
MFSVTRRRAAGAAAAMATATGTLYWMTSQGDRPLVHNDPSYMVQFPTAAPPQVSRRDLLDRLAKTHQFDVLIIGGGATGTGCALDAATRGLNVALVEKGDFASGTSSKSTKMIHGGVRYLEKAFWEFSKAQLDLVIEALNERKHLINTAPHLCTVLPILIPIYSTWQVPYIYMGCKFYDFFAGSQNLKKSYLLSKSATVEKAPMLTTDNLKASLVYHDGSFNDSRLNATLAITAVENGATVLNYVEVQKLIKDPTSGKVIGAEARDVETNELVRINAKCVVNATGPYSDAILQMDRNPSGLPDSPLNDNSKIKSTFNQIAVMDPKMVIPSIGVHIVLPSFYCPKDMGLLDVRTSDGRVMFFLPWQGKVLAGTTDIPLKQVPENPMPTEADIQDILKELQHYIEFPVKREDVLSAWAGVRPLVRDPRTIPADGKKGSATQGVVRSHFLFTSDNGLITIAGGKWTTYRQMAEETVDKVVEVGGFHNLKPCHTRDIKLAGAEEWTQNYVALLAQNYHLSSKMSNYLVQNYGTRSSIICEFFKESMENKLPLSLADKENNVIYSSEENNLVNFDTFRYPFTIGELKYSMQYEYCRTPLDFLLRRTRFAFLDAKEALNAVHATVKVMGDEFNWSEKKRQWELEKTVNFIKTFGV
Protein: RNA-binding signal recognition particle subunit (Q5A9A9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Signal recognition particle subunit SRP68
- Signal recognition particle subunit SRP72
- Signal recognition particle 54 kDa protein
- Signal recognition particle subunit
- Signal recognition particle subunit SRP14
- Signal recognition particle receptor subunit alpha homolog
- Large ribosomal subunit protein eL19
- Signal recognition particle receptor subunit beta
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS9
Sequence:
MSNNKRPVLEEVDDDDIDNMDMDIAEFDPSLTTPIAPKRPEPTVVRSQDSEPSLFPNIPLNQVQPPPKQASSRNGIMDPNSFTEEEKKQFDQFQIIYPCYFDINRSHKQGRRVSIDRAVENPLATTISDTCRRLGLPVFLELDKTHPQDFGNPGRVKVLFKAVFDNGKLINPKLQTKRVLFNVIAEYLSEHPTTLESIGPKSGVPRPPEFENEFQPEEIPKVKGFKMNTIVPIHSNLTLKHPMTKHIYDPEPETPAAGKPNVPKIPKKKVMKIRG
Protein: Proline utilization regulator (Q9I5F8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Gamma carbonic anhydrase family protein
- Probable transcriptional regulator
- Probable transcriptional regulator
- TonB-dependent receptor
- Transcriptional regulator XylS
- Probable transcriptional regulator
- Bifunctional protein PutA
- Probable transcriptional regulator
- 5'-nucleotidase
- DUF7380 domain-containing protein
Sequence:
MFDTRLIRLPDQSHTHAHEHHQLVMSLAGRAEFEVNGCGGEVCRMRACLVPGEAGHVFAGVGDNRMLIIDLGEDNPTPEDPDLLARLFEAPRYPTLDADFQNLLSYAGAELARYGSDPLLTRALGGVLIRALHLRLFGEQQPLAASGPLDLERLDAHIVRNLARRITVAELAQVACLSPSHFHAQFKDSVGLTPHQYLLKVRLDCAARLLRESRLPLVRIAEECGFSSQSALTTAMRRYLGLTPKSLRKG
Protein: Phosphatidylglycerol/phosphatidylinositol transfer protein (PG/PI-TP) (Q5B0Q1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol.
Subcellular location: Secreted {ECO:0000269|PubMed:25043916}.
Interaction partners:
- Translocon protein Sec61beta, putative
- Prefoldin subunit 1, putative
Sequence:
MKLLSPATALLFLAPLAVTATPASFFGYTQDVIAEGAPVRGDNPLEYCSEPSGDILEINSVDLAPNPPKAGTTLKIRAAGNLHERIEAGAYVVLEVKYGLITLLRDTADLCAQLTNVDLQCPLEEGPMVLTKEVDLPSQIPRGRYTVHADVYTKDNKRITCLDAKNIQF
Protein: Aspartyl protease UND (EC 3.4.23.-) (Protein UNDEAD) (Q9SV77)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable aspartic protease activated by the transcription factor MYB80. May participate in the regulation of the timing of tapetal programmed cell death (PCD) which is critical for pollen development.
Interaction partners:
- PHD finger protein MALE STERILITY 1
- Cysteine proteinases superfamily protein
- Transcription factor ABORTED MICROSPORES
- Probable cysteine protease RD19C
- KDEL-tailed cysteine endopeptidase CEP1
- Vacuolar-processing enzyme beta-isozyme
- Cysteine protease RD19A
- Cysteine proteinase RD21A
Sequence:
MKTTMNFVFLFFLPLLINAKPKRVTLHIPLVHNGANFYDSKVVSLPLSSPHSQRGLAFMAEIHFGSPQKKQFLHMDTGSSLTWTQCFPCSDCYAQKIYPKYRPAASITYRDAMCEDSHPKSNPHFAFDPLTRICTYQQHYLDETNIKGTLAQEMITVDTHDGGFKRVHGVYFGCNTLSDGSYFTGTGILGLGVGKYSIIGEFGSKFSFCLGEISEPKASHNLILGDGANVQGHPTVINITEGHTIFQLESIIVGEEITLDDPVQVFVDTGSTLSHLSTNLYYKFVDAFDDLIGSRPLSYEPTLCYKADTIERLEKMDVGFKFDVGAELSVNIHNIFIQQGPPEIRCLAIQNNKESFSHVIIGVIAMQGYNVGYDLSAKTAYINKQDCDM
Protein: Chaperone protein HtpG (Heat shock protein HtpG) (High temperature protein G) (Q728G0)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Molecular chaperone. Has ATPase activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
Interaction partners:
- Chaperone protein DnaK
- Chaperonin GroEL
- Chaperone protein DnaJ
- Co-chaperonin GroES
- Protein GrpE
- ATP-dependent protease subunit HslV
- Peptidyl-prolyl cis-trans isomerase
- Peptidyl-prolyl cis-trans isomerase
- ATP-dependent protease ATPase subunit HslU
- Histone deacetylase family protein
Sequence:
MATAPASHAFRTEVRKMLHIITHSLYTNREIFLRELVSNASDALDKLRFIRSRGDAVVAPDLAPGIDISVDKEARILTIADTGVGMTRQELMDNLGTIARSGSEQFVADLAAAENAKDADAASIIGRFGVGFYAVFMVADRVEVTSRSYIEGEAAHTWTSDGLGEFTVEEATGDIPQRGTVIKAHLREDAAEFLEKYRIEGILRKHSQFISFPIRVDGEQVNTTPALWREPKFSITDEQYADFYKHLTFDTEAPLRTLHVSVDAPVQFTGLVFVPPHGQEVFSMGRDRWGLDLYVRRVLIQRENKDLLPEYLGFLKGIVDTEDLPLNISRETLQENVVVRKIGQTLTKQVLADLARLAADDAEAYATFWRQHGKVFKLGYSDYANREKFAPLLRFNSSHHDDAQGLTSLDDYISRAREGQKEIWYIAAPGREAARLDPRVEVFRRKGLEVLYLLEPIDEFVLETLDSYSDFSFKAVEHADGEKLAQFEDTGPARDVTPLTEDEDAAFARLIERMKALLGDAVEDVRISHRLADSPACLVQPGGASTSSMDRLLRVLHKDESVPRKVFEVNRDHPILRNLLKVFTSDASDPLVEDTTRQLFATSLMLDGYLKDPHELAAMMHRLMEKSGDWYKAVRGL
Protein: OL-protocadherin isoform (Protocadherin 10) (Q925I8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MIVLLFFALLWMVDGVFSQLHYTVQEEQEHGTFVGNIAEDLGLDITKLSARRFQTVANSRTPYLDLNLETGVLYVNEKIDREQICKQSPSCVLHLEVFLENPLELFRVEIEVLDINDNPPSFPEPDLTVEISESATPGTRFPLESAFDPDVGTNSLRDYEITPNSYFSLDVQTQGDGNRFAELVLEKPLDREQQAVHRYVLTAVDGGGGGGGGEGGGGGGGAGLPPQQQRTGTALLTIRVLDSNDNVPAFDQPVYTVSLPENSPPGTLVIQLNATDPDEGQNGEVVYSFSSHISPRARELFGLSPRTGRLEVSGELDYEESPVYQVYVQAKDLGPNAVPAHCKVLVRVLDANDNAPEISFSTVKEAVSEGAAPGTVVALFSVTDRDSEENGQVQCELLGDVPFRLKSSFKNYYTIVTEAPLDREAGDSYTLTVVARDRGEPALSTSKSIQVQVSDVNDNAPRFSQPVYDVYVTENNVPGAYIYAVSATDRDEGANAKLTYSILECQIQGMSVFTYVSINSDNGYLYALRSFDYEQIKDFSFQVEARDAGSPQALAGNATVNILIVDQNDNAPAIVAPLPGRNGTPAREVLPRSAEPGYLLTRVAAVDADDGENARLTYSIVRGNEMNLFRLDWRTGELRTARRVPAKRDPQRPYELVIEVRDHGQPPLSSTATLVVQLVDGAVEPQGGGGDRGGGSGEHLRPSRSGGGETSLDLTLILIIALGSVSFIFLLAMIVLAVRCQKEKKLNIYTCLASDCCLCCCCCGNGSSTCCGRQARARKKKLSKSDIMLVQSANVPSNPAQVPVEESGGFGSHHHNQNYCYQVCLTPESAKTDLMFLKPCSPSRSTDAEHNPCGAIVTGYSDQQPDIISNGSILSNENKHQRAELSYLVDRPRRVNSSAFQEADIVSSKDSGHGDSEQGDSDHDVTNRGQSAGMDLFSNCTEECKALGHSDRCWMPSFVPSDGRQAADYRSNLHVPGMDSVPDTEVFEPPEVQPGAERSFSTFGKEKALHGTLERKELDGLLSNTRAPYKPPYLTRKRIC
Protein: Branched-chain-amino-acid aminotransferase (BCAT) (EC 2.6.1.42) (P9WQ75)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val.
Interaction partners:
- Dihydroxy-acid dehydratase
- 2-isopropylmalate synthase
- L-threonine dehydratase biosynthetic IlvA
- Cystathionine gamma-synthase
- Homoserine dehydrogenase
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Alanine aminotransferase
- Glutamate--cysteine ligase EgtA
- 4-aminobutyrate aminotransferase
- Ketol-acid reductoisomerase
Sequence:
MTSGSLQFTVLRAVNPATDAQRESMLREPGFGKYHTDHMVSIDYAEGRGWHNARVIPYGPIELDPSAIVLHYAQEVFEGLKAYRWADGSIVSFRADANAARLRSSARRLAIPELPDAVFIESLRQLIAVDKAWVPGAGGEEALYLRPFIFATEPGLGVRPATQYRYLLIASPAGAYFKGGIAPVSVWVSTEYVRACPGGTGAAKFGGNYAASLLAQAEAAENGCDQVVWLDAVERRYIEEMGGMNIFFVLGSGGSARLVTPELSGSLLPGITRDSLLQLAIDAGFAVEERRIDIDEWQKKAAAGEITEVFACGTAAVITPVARVRHGASEFRIADGQPGEVTMALRDTLTGIQRGTFADTHGWMARLG
Protein: PolyMG-specific alginate lyase (I6P4V6)
Organism: Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia)
Interaction partners:
Sequence:
MRSTRLSRHPTSLCLTTALAFCLTTLPATAASWLVHDAAEFDTAAASLQPGDEIVLADGTWTDTRLLLKGQGTAAAPIVLRAQTPGKVILSGQSDLRLAGSYLQVSNLVFRNGYTPGDAVVAFRESSKAVASHSQLSGLVIDNYSNPDPGDQDYWVSLYGSHNRLDHSQLRGKTNAGPTVVVVRDATQGLDNQHRIDHNWFGPRPALGVNGGETLRIGTSDTSLSASNNTVENNWFEGCDGETEIINSKSGGNTYRGNVFYRSAGALTLRHGNGNRVIDNVFLGDDKAGTGGVRIINGDQIVSNNYFERLAGSSNRSALAVMDGQADPPLSGYAPVVNATISRNTFVDVARISFGVGHDEAKGIVVAASNSRFSANLIVNRASRNPPNTASSLAGITFSGNVQSPAASSVFPAGVEGRSVSLQQAGSGLWVATPALPQVGADPALAMTAREATGVDWYPKVGEVALSRVSTGVDR
Protein: SD08128p (Q960B9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAANNNNSNIHNLGAGTEGLLSSVIASTGTPGMGSSPVPSRASSSSASSAAQSAWDQLTASASNNMSPSPTAGAPTVTGPILPDNLGVGAGSSPVASCSSPSTPTKTHAPSPLESMGHTPQGPPTLGPGGYGEELTAELVNQGWRKFWSKRENRPYYWNKVTGESLWEMPGTRPFDPLTDPLGICHAGGPTPIIPNMHQQQQHQHHHLKRRPSDDMHIHPNQHHMGGGPPMKKFVLAGPWDLEVCTNAVIVERPPTLLPQPHPEVEALRAAFTMKLLKTYEDLCMRRENIKAPRDSFNRWLMERKVIDTGCDPLLPSSCMPEISSSMYREIMSDIPIKIVKPKFTGDARKQLSRYAEAAKQIIESRSAPAESKKVVKWNVEDTFQWLRRTVGASYEDFQDRLAHLKRQCEPHLVETVKSSVETLCVKIYHLSADHARKIRERHSQLLKEHGIPEPTPPPPPPHLKKVWCYPIQFAVPSPRMPTIEYLQDRDHMIIKYTPATINQPDAQYINLTYLQKLEQLYRHNCFDDKKFDLFIGRVWCLLKRYQTFLGNALNSSQEAELTQAALPVPVFECLHRQFGVSFECFASPFNSYFRQYCSAFADTDAYFGSRGPFLDFKPVSGSFQVNPPHCEELIEASLLHIDKLLTDTMEPLSFIVFLPEWKSISKLDDSMYKRRSMVVLGMAHEYRHGYQHMLQKSDVLIKCMQGTQVVWLQNSAGYARWGPNEIRVEALREAFRPQRDRERERAAAAAAAAGVTSSQQSPSTPPSAASTAPTTNSCTISGVNSNSSSTATTTSTSSSPSLTTTSSSMSPLSPHTPTGNPPPQFPMTISNTSSSSNLVAASPTMSVQSDCSSPSSSTMSLSPAPASGGYPDGVTSATAAAVSITATTTTSAAGAGSAFGQANSISSSASTQAVINSAV
Protein: Leucine carboxyl methyltransferase 1 (EC 2.1.1.233) (Protein phosphatase methyltransferase 1) ([Phosphatase 2A protein]-leucine-carboxy methyltransferase 1) (O94257)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Interaction partners:
- Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Serine/threonine-protein phosphatase 2A activator 1
- Serine/threonine-protein phosphatase 2A activator 2
- Protein phosphatase methylesterase 1
- Protein phosphatase PP2A regulatory subunit A
- Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Protein phosphatase PP2A regulatory subunit B
- Uncharacterized protein C63.05
- Type 2A phosphatase activator tip41
Sequence:
MDITETDLDALKCRSSATKSGYIHDPFIKFFSPSRNSHKPPIINRGTYVRTWSIDHILQKFIESFDGKKQIISLGAGTDTRVFRYISEYGPENLKFIEFDFYPNCIRKIRTIEKHEALKQNIGDYVVDISGGSLVSGSLDIYSYDIREIVHKGFPGFVDFSLPTIVLSECCLCYLEPEEASSLCRWFQNMFATSGIVVYEPIQGMDNFGKMMKANLSARGVILKTLDCYETTEQQRMRFLDYGYSEVIAEDFLTIEETWIPIEEKKRTMSIEMLDELEEWQLLAKHYCLTFAATENLWNQIILQLPHLKT
Protein: Ecm25p (A0A1D8PFN0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Rga2p
- Actin cytoskeleton-regulatory complex protein SLA1
- Cell division control protein 42 homolog
- Rho family GTPase
Sequence:
MDRIFYKSDLRDPTTNYPIYIFDTSYLPSPDIINYNEFLITLMSYLPIKPYVLIMFSCGLNKISWIWGIKFIQKILNRRDLKNLIKVYTVHDSWFLKSMTSILQNFNSTRKNLEQLDQLLGAFTFVNDLSDTKNDRQTLVIHCQTLSELSYYLDITNLKISYNIFKHDLQISELKLSMRYQPIIHPLITLNVQKYSIFHHHLYQIFKIVENNGNKVELILYKPGNKFKCDILYQCILRNQLIWINDWDLYSIATVFKRILSELPFPLIDIELIKLPIGDNLQYTFKIFKRLINRLQRHQETQNYDQLLFQILDMCLKIVDNNDITKHTTTTISKGMSYCLSHELVSTNKTNIQIINRFLKNLLEYWSEIRKNFHIYTIDDVIDGKLQTESISTSHETSSYDLSHDITLDQESESSNSSNDDDDDEDIGFIETKDILRNLSLNNDNNNNNNNNNNNSADRTGASTSTSTSTNSFNKPNGFHQRTTSVTNKTIDQINIKKSHKKSLSDVSNLQIQYPPQKYKFTPTTITTTSGGTNSGTTSNTSRRDDNSKAQKKSNVENTSNGNELQSNGNTNSRSGIHSGITTFTPTPTLKKKPVIRGRKVSELAKLFEERSEGIEILRGMT
Protein: Uncharacterized protein (Q8I4Q4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MSRVLNFFKNLLLIYISNCLLYINNKHLLSIMHYEMYNTKLVSNLIIKRRLSETLMYNKRSQLKVSNINNYNDDHEENKNSLTEKKEMLKTSNRNENNRKSKKRRNYDVTKKKETLEDLLKEYDEEMKEIKKKKKKILF
Protein: Tumor necrosis factor ligand superfamily member 11 (Osteoclast differentiation factor) (ODF) (Osteoprotegerin ligand) (OPGL) (Receptor activator of nuclear factor kappa-B ligand) (RANKL) (TNF-related activation-induced cytokine) (TRANCE) (CD antigen CD254) [Cleaved into: Tumor necrosis factor ligand superfamily member 11, membrane form; Tumor necrosis factor ligand superfamily member 11, soluble form] (O14788)
Organism: Homo sapiens (Human)
Function: Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy. Induces osteoclastogenesis by activating multiple signaling pathways in osteoclast precursor cells, chief among which is induction of long lasting oscillations in the intracellular concentration of Ca (2+) resulting in the activation of NFATC1, which translocates to the nucleus and induces osteoclast-specific gene transcription to allow differentiation of osteoclasts. During osteoclast differentiation, in a TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and mitochondrial ROS generation necessary for proper osteoclast generation (By similarity).
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 11, soluble form]: Secreted {ECO:0000250}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 11B
- Tumor necrosis factor receptor superfamily member 11A
- Macrophage colony-stimulating factor 1 receptor
- TNF receptor-associated factor 6
- Tartrate-resistant acid phosphatase type 5
- Nuclear factor of activated T-cells, cytoplasmic 1
- Sclerostin
- Secreted frizzled-related protein 1
- Osteocalcin
- Macrophage colony-stimulating factor 1
Sequence:
MRRASRDYTKYLRGSEEMGGGPGAPHEGPLHAPPPPAPHQPPAASRSMFVALLGLGLGQVVCSVALFFYFRAQMDPNRISEDGTHCIYRILRLHENADFQDTTLESQDTKLIPDSCRRIKQAFQGAVQKELQHIVGSQHIRAEKAMVDGSWLDLAKRSKLEAQPFAHLTINATDIPSGSHKVSLSSWYHDRGWAKISNMTFSNGKLIVNQDGFYYLYANICFRHHETSGDLATEYLQLMVYVTKTSIKIPSSHTLMKGGSTKYWSGNSEFHFYSINVGGFFKLRSGEEISIEVSNPSLLDPDQDATYFGAFKVRDID
Protein: FI02989p (Lipid droplet subset dehydrogenase 1 (EC 1.1.1.-)) (Q9W3K9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Lipid droplet-associated hydrolase
Sequence:
MSKVTQSADNGSNANSNDIYNIVLLVVDIVMLIVKFWLAIAEAIVGLFRAPPLDDVNGKVVLITGTGHGMGKEMALQYAKLGATILCWDVNEQTNNQTVKEIKNNGGKAFGYVCNVTKREELIELAQKVRKEHGFIHVVVNNAGIMPCHPLLEHTENEIRLMYEINVLSHFWIIQAFLPDMIERNEGSIVALSSCAGLFGLINLVPYCGTKFAVRGYMAALVEELRQKNPQNNVKLTTIYPYMIDTGLCKNPRYRFPNLFKLIPADVAAGSIIEAQRQGLEEAAIPRHFVAAEKIGRLIPRKAMRLVNDFFDTGVDTDKS
Protein: Guanine nucleotide-binding protein subunit alpha-11 (G alpha-11) (G-protein subunit alpha-11) (G-protein subunit GL2 alpha) (P38409)
Organism: Bos taurus (Bovine)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C (By similarity). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (By similarity). Together with GNAQ, required for heart development (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P29992}; Lipid-anchor {ECO:0000250|UniProtKB:P29992}. Cytoplasm {ECO:0000250|UniProtKB:P29992}.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4
- Muscarinic acetylcholine receptor
- Muscarinic acetylcholine receptor
- Extracellular calcium-sensing receptor
- Cholecystokinin A receptor
- Growth hormone secretagogue receptor type 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Guanine nucleotide-binding protein G
- Endothelin-1 receptor
Sequence:
MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEKVTTFEHRYVSAIKTLWNDPGIQECYDRRREYQLSDSAKYYLTDVDRIATSGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIVTYPWFQNSSVILFLNKKDLLEDKILHSHLVDYFPEFDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
Protein: Terpene synthase 1 (CsTPS1) (Valencene synthase TPS1) (CsVS) (EC 4.2.3.73) (D0UZK2)
Organism: Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis)
Function: Sesquiterpene synthase involved in the biosynthesis of volatile compounds which contribute to fruit flavor and aroma. Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (+)-valencene. No activity detected with geranyl diphosphate (GPP).
Interaction partners:
Sequence:
MSSGETFRPTADFHPSLWRNHFLKGASDFKTVDHTATQERHEALKEEVRRMITDAEDKPVQKLRLIDEVQRLGVAYHFEKEIEDAIQKLCPIYIDSNRADLHTVSLHFRLLRQQGIKISCDVFEKFKDDEGRFKSSLINDVQGMLSLYEAAYMAVRGEHILDEAIAFTTTHLKSLVAQDHVTPKLAEQINHALYRPLRKTLPRLEARYFMSMINSTSDHLYNKTLLNFAKLDFNILLELHKEELNELTKWWKDLDFTTKLPYARDRLVELYFWDLGTYFEPQYAFGRKIMTQLNYILSIIDDTYDAYGTLEELSLFTEAVQRWNIEAVDMLPEYMKLIYRTLLDAFNEIEEDMAKQGRSHCVRYAKEENQKVIGAYSVQAKWFSEGYVPTIEEYMPIALTSCAYTFVITNSFLGMGDFATKEVFEWISNNPKVVKAASVICRLMDDMQGHEFEQKRGHVASAIECYTKQHGVSKEEAIKMFEEEVANAWKDINEELMMKPTVVARPLLGTILNLARAIDFIYKEDDGYTHSYLIKDQIASVLGDHVPF