wanglab/gogpt-training-data huggingface dataset:
Protein: Myosin-2 heavy chain (Myosin II heavy chain) (P08799)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.
Subcellular location: Cytoplasm, cell cortex. Note=Highest concentration in the posterior cell cortex.
Interaction partners:
- Myosin regulatory light chain
- Myosin, essential light chain
- SH3 and F-BAR domain-containing protein DDB_G0274695
- Cortexillin-1
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco11
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase qkgA
- Ras GTPase-activating-like protein gapA
Sequence:
MNPIHDRTSDYHKYLKVKQGDSDLFKLTVSDKRYIWYNPDPKERDSYECGEIVSETSDSFTFKTVDGQDRQVKKDDANQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGLDSQATIDLIDGRQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFRAGQLARIEEAREQRISEIIKAIQAATRGWIARKVYKQAREHTVAARIIQQNLRAYIDFKSWPWWKLFSKARPLLKRRNFEKEIKEKEREILELKSNLTDSTTQKDKLEKSLKDTESNVLDLQRQLKAEKETLKAMYDSKDALEAQKRELEIRVEDMESELDEKKLALENLQNQKRSVEEKVRDLEEELQEEQKLRNTLEKLKKKYEEELEEMKRVNDGQSDTISRLEKIKDELQKEVEELTESFSEESKDKGVLEKTRVRLQSELDDLTVRLDSETKDKSELLRQKKKLEEELKQVQEALAAETAAKLAQEAANKKLQGEYTELNEKFNSEVTARSNVEKSKKTLESQLVAVNNELDEEKKNRDALEKKKKALDAMLEEMKDQLESTGGEKKSLYDLKVKQESDMEALRNQISELQSTIAKLEKIKSTLEGEVARLQGELEAEQLAKSNVEKQKKKVELDLEDKSAQLAEETAAKQALDKLKKKLEQELSEVQTQLSEANNKNVNSDSTNKHLETSFNNLKLELEAEQKAKQALEKKRLGLESELKHVNEQLEEEKKQKESNEKRKVDLEKEVSELKDQIEEEVASKKAVTEAKNKKESELDEIKRQYADVVSSRDKSVEQLKTLQAKNEELRNTAEEAEGQLDRAERSKKKAEFDLEEAVKNLEEETAKKVKAEKAMKKAETDYRSTKSELDDAKNVSSEQYVQIKRLNEELSELRSVLEEADERCNSAIKAKKTAESALESLKDEIDAANNAKAKAERKSKELEVRVAELEESLEDKSGTVNVEFIRKKDAEIDDLRARLDRETESRIKSDEDKKNTRKQFADLEAKVEEAQREVVTIDRLKKKLESDIIDLSTQLDTETKSRIKIEKSKKKLEQTLAERRAAEEGSSKAADEEIRKQVWQEVDELRAQLDSERAALNASEKKIKSLVAEVDEVKEQLEDEILAKDKLVKAKRALEVELEEVRDQLEEEEDSRSELEDSKRRLTTEVEDIKKKYDAEVEQNTKLDEAKKKLTDDVDTLKKQLEDEKKKLNESERAKKRLESENEDFLAKLDAEVKNRSRAEKDRKKYEKDLKDTKYKLNDEAATKTQTEIGAAKLEDQIDELRSKLEQEQAKATQADKSKKTLEGEIDNLRAQIEDEGKIKMRLEKEKRALEGELEELRETVEEAEDSKSEAEQSKRLVELELEDARRNLQKEIDAKEIAEDAKSNLQREIVEAKGRLEEESIARTNSDRSRKRLEAEIDALTAQVDAEQKAKNQQIKENKKIETELKEYRKKFGESEKTKTKEFLVVEKLETDYKRAKKEAADEQQQRLTVENDLRKHLSEISLLKDAIDKLQRDHDKTKRELETETASKIEMQRKMADFFGGFKA
Protein: Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 1) (Benzoate--CoA ligase) (EC 6.2.1.25) (Butyrate--CoA ligase 1) (Butyryl-coenzyme A synthetase 1) (Lipoate-activating enzyme) (Middle-chain acyl-CoA synthetase 1) (XL-III) (Xenobiotic/medium-chain fatty acid:CoA ligase XL-3) (XM-ligase 3) (Q9BEA2)
Organism: Bos taurus (Bovine)
Function: Catalyzes the activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism. Capable of activating medium-chain fatty acids (e.g. butyric (C4) to decanoic (C10) acids), and certain carboxylate-containing xenobiotics, e.g. benzoate. Also catalyzes the activation of lipoate to lipoyl-nucleoside monophosphate. Activates lipoate with GTP at a 1000-fold higher rate than with ATP and activates both (R)- and (S)-lipoate to the respective lipoyl-GMP, with a preference for (R)-lipoate.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q91VA0}. Mitochondrion {ECO:0000269|PubMed:10561077, ECO:0000269|PubMed:11382754}.
Interaction partners:
- Lipoyl amidotransferase LIPT1, mitochondrial
- Hydroxysteroid dehydrogenase-like protein 2
- CACN subunit beta associated regulatory protein
Sequence:
MQRLMKFRVLWGIHMSCPGFHHAPQHLRCRSLSGAGTLRWNDYDRPEEFNFASDVLDHWTQMEKEGKRSPNPALWWVNDQGDEVKWSFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSDHSREGWLDFRSLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSHGFALRSYFPACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAHHLPQFDPKVIIETFFKYPITQCLAAPSVYRMILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSETGISCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKPTRPIGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKEFGQK
Protein: Serine protease inhibitor Cvsi-1 (Q30HU9)
Organism: Crassostrea virginica (Eastern oyster)
Function: Slow-binding inhibitor of serine proteases. The inhibitor rapidly binds to the protease forming a weak enzyme-inhibitor complex, and this is followed by a slow isomerization forming a tight-binding enzyme-inhibitor complex. Active against subtilisin A, perkinsin and trypsin with dissociation constants of 0.29 nM, 13.7 nM and 17.7 nM respectively. Not active against thermolysin, papain or pepsin. Has antiparasitic activity against the protozoan P.marinus.
Subcellular location: Secreted {ECO:0000269|PubMed:16872855}.
Interaction partners:
Sequence:
MDVVRTLILCVCLFGLTFAVPCIDGVCTSNELQCASGYVKGCHAGLCTCEHATTQSCTVVNNCLHLGTCSLHGRDGFWHCVDSVCKCFFF
Protein: Neuropilin (Q6T870)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MYWCLLCVTLTGLSVARALTDRPCGGKITITSAGYVTSPDYPTGYPVNKQCTWLIQAPDPQQKILINFNPHFDLESRECKYDFVQVFDGADENALSLGRFCGKIAPSPIISSGNSLLIKFTSDYESAGAGFSIRYEIHRTGTECSRNFTEPHGLIETPGFPDKYPNNLECIFIIFAPKMAEIILDFQSFDMEPDTTAPAGAVCRFDYLEIWDGYPTVGPHIGRYCGSRHPGRVISYTGILSLSIHTDNAITKEGFSANYSIRSSSDQLQPHQDECMYPLGMESGEITEDRIAASSQYNPSWSRLRSRLNYLENGWTPSEDSSREWIQVDLGFLRYVTAIGTQGAISKETKKAYFVRTYRISVSSNGEDWITLKDKTKQMVFQGNDNPTDEVRALLPKPTLTRYIRIRPLLWEQGICMRFEVYGCKIPDAPCSNMLGMVSGQISDSQISVWPSAERGWLPEQARLLTGRTGWVVAHPQGLVKNQSLELDLGAQRMVTGLVLQGGKYRDLNIFIKRFRVTYSVNGTDWNHILEENSNKVKVFIGNQNHDTPEVRTFDPVLMRFLRIYPERGSPDGMGLRLEVLGCDLQEPTTPLPLATTMETTAATVTSASMLLGNIPTTTTFPTTAENCDDDDGNCHSDALTDYDTTETAVSEPFLEMEEAPAYLWFACDFGWIDHPSYCGWSQDGGEGAEWHINNNSKHADHKLPSLDHTGMPNNFIYAAANTNTQTEMERTDEMETDEELERKGGRVARLASSQVTAPDSDLCMSFWYHFTEKHAGTLNIKQKVEHEQVDEEREILIRLLNGQTKSRWREGRVLLPSADTPYQVIIEAQVNPTHSGYISLDDIKILEVNPEDCKDPENTEDDEDEVEEIVNCEGTDNTXWSFGRGSMLKSLDPILITIIVMSAVGVLLGAVCGVLFYCACAHTTNRNLSALENYNFELVDGVKLKKEKLSAQKSYTEA
Protein: Phosphatidylcholine:ceramide cholinephosphotransferase 3 (EC 2.7.8.27) (Ethanolamine-phosphorylceramide synthase) (EPC synthase) (Sphingolipid synthase) (Sphingomyelin synthase) (SM synthase) (Q38E55)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target (By similarity).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- sphingolipid 4-desaturase
- Phosphatidic acid phosphatase, putative
- Phosphatidylinositol:ceramide inositolphosphotransferase
- Phosphatidylcholine:ceramide cholinephosphotransferase 4
- Phosphatidic acid phosphatase alpha, putative
- serine C-palmitoyltransferase
- Serine-palmitoyl-CoA transferase, putative
Sequence:
MAVPPVEMYSGSFWNRMRKPLPLRTQVIRFTVVFVIVSFILAVALQITHERMPDPKVTKPLPDLGFELLTKVPGMYVLADCCIGFLNILSVFTAFKLYLLHRHCVGSGEPELPCNIPGVSRFFLSVWLCKENCRIELRNVHTIAWIRFITSYALLLLFRSVVIVMTSFPAPDDLCQNPPKIENPVKNVILTVLTAGGGSIHCGDLMYSGHTVILTLHLMFHWIYGAMVHWSFRPVVTVVAIFSYYCIVASRFHYTDDVLVAIYLTIATFIAVGHNADGAPWQLQLFIRWWPCCGANSREMTEDSQPVMVAFKSEAAGQSSRKVVDERNH
Protein: Degenerin-like protein asic-1 (Acid-sensing/amiloride-sensitive ion channel protein 1) (O01635)
Organism: Caenorhabditis elegans
Function: Proton-gated cation channel; it is activated by a drop of the extracellular pH and then becomes rapidly desensitized (By similarity). Has high selectivity for sodium ions and can also transport lithium ions with high efficiency (By similarity). Can also transport potassium ions, but with lower efficiency (By similarity). It is nearly impermeable to the larger rubidium and cesium ions (By similarity). Promotes synaptic vesicle fusion to positively regulate the release of dopamine at dopaminergic neuron synapses.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q1XA76}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q1XA76}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q1XA76}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6NXK8}.
Interaction partners:
- Acid-sensing ion channel 1
- Acid-sensing ion channel 1-like
- Degenerin mec-10
- DEgenerin Like
Sequence:
MGKNSLKRALELDVVDFAEHTSAHGIPRAYVSTGWRRYMWLLCFLFCLSCFGHQAYLIVERFNRNDIIVGVEIKFEEIKFPAVTICNMNPYKNSAARELGAIRNAIEAFELAIDKSDGNAHSKRKKRSANSKMVPIDLLCKEEHGMFTAHDYGHVECTCVTFEDMSKVGDTDDDEIFWNCHQRKDWTHKICHLAEGSNQLKTCKCFEDTCVSDEVTKQLVWPLQLSKNGTKLCISPESSGPRYCASAQKFQVSTCSNCDWLGKCEESDDMDLEEEIDSKTCICHHGNCFQIKGNVKKRKRRTPERKVHERLLSRYEGLLAVYSHCNCTKQHGCVSTSVPDMDLENSNKTCLCFYNKKNEQIWPCYKEPEWEERKCSRCNTMGDCVYSDKPKKQTISCLCATPIKMCVRIDPPQTNDTSLDDRVVKFWDIQPSTTMSPIVKKKEERDKAYGYTGVKDRIALRAKAMENMIFAVDALTEEEKWKISYNKSDFIMKCSFNGRECNVKHDFVEYLDPTYGACFTYGQKLGNNTNERSGPAYGLRLEVFVNVTEYLPTTEAAGVRLTVHATDEQPFPDTLGFSAPTGFVSSFGIKLKSMVRLPAPYGDCVREGKTEDFIYTQKAYNTEGCQRSCIQKHLSKTCGCGDPRFPPYRESKNCPVDDPYKRECIKNEMHVATRDSKKLGCSCKQPCNQDVYSVSYSASRWPAIAGDLSGCPLGMAAHHCLNYKREQGSMIEVYFEQLNYESLLESEAYGWSNLLSDFGGQLGLWMGVSVITIGEVACFFFEVFISLISSNRTKRRPARKSFSSSLRCSTDYNLNKDGFNLDN
Protein: Probable LRR receptor-like serine/threonine-protein kinase At1g51820 (EC 2.7.11.1) (C0LGG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- AAA-ATPase At1g43910
- AAA-ATPase At3g28540
- Putative methylesterase 13, chloroplastic
Sequence:
MERHFVFIATYLLIFHLVQAQNQTGFISVDCGLSLLESPYDAPQTGLTYTSDADLVASGKTGRLAKEFEPLVDKPTLTLRYFPEGVRNCYNLNVTSDTNYLIKATFVYGNYDGLNVGPNFNLYLGPNLWTTVSSNDTIEEIILVTRSNSLQVCLVKTGISIPFINMLELRPMKKNMYVTQSGSLKYLFRGYISNSSTRIRFPDDVYDRKWYPLFDDSWTQVTTNLKVNTSITYELPQSVMAKAATPIKANDTLNITWTVEPPTTQFYSYVHIAEIQALRANETREFNVTLNGEYTFGPFSPIPLKTASIVDLSPGQCDGGRCILQVVKTLKSTLPPLLNAIEAFTVIDFPQMETNENDVAGIKNVQGTYGLSRISWQGDPCVPKQLLWDGLNCKNSDISTPPIITSLDLSSSGLTGIITQAIKNLTHLQILDLSDNNLTGEVPEFLADIKSLLVINLSGNNLSGSVPPSLLQKKGMKLNVEGNPHILCTTGSCVKKKEDGHKKKSVIVPVVASIASIAVLIGALVLFLILRKKRSPKVEGPPPSYMQASDGRLPRSSEPAIVTKNRRFSYSQVVIMTNNFQRILGKGGFGMVYHGFVNGTEQVAVKILSHSSSQGYKQFKAEVELLLRVHHKNLVGLVGYCDEGDNLALIYEYMANGDLKEHMSGTRNRFILNWGTRLKIVIESAQGLEYLHNGCKPPMVHRDVKTTNILLNEHFEAKLADFGLSRSFLIEGETHVSTVVAGTPGYLDPEYHRTNWLTEKSDVYSFGILLLEIITNRHVIDQSREKPHIGEWVGVMLTKGDIQSIMDPSLNEDYDSGSVWKAVELAMSCLNHSSARRPTMSQVVIELNECLASENARGGASRDMESKSSIEVSLTFGTEVSPNAR
Protein: Clockwork orange, isoform B (Clockwork orange, isoform C) (LD15411p) (Q8MRI9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNSCLADLSRLIPPQYQRKGRGRIEKTEIIEMAIRHLKHLQSECQQKESDYRSGYMDCMKEAAKFLYDVHMQDFCHRLLGRLQEHIDEMFKTDCYKSTRSCHMPDNVSASSGSPHQAYHPPLCHLRDMLATSASDVEHSQDHNDVKDLSFRNHLNQLQRSQQAAAAAAVAAAAVAVANGSSPASNAGVDSKVPLTNGGGTGGAPPAADNVPSNSTGSGSAAACAGGNSNSSGSNSSNAASSTICPPAGGSCPAKVTPLAAHQQPHQAPVITSTAPHHHHHHTDSSHHDFESSREPILHTDTSNMHSPPPRDLLLQQHPHLAHSHHTQDSLMSVRMRNYSESSHEIEHNNNYKYKNHIKERFVHELHDEETSSEHCPVAAHLQSDHSHLQALSEHSKDGTEPEIAPIMAKKRKLAEAAANGEIPLEVHTESSNAGASSANRLDKPSPSFNFSDIKDIKAELHNGNSNSSPLLAKLSAVAAAGGQLSTPSSTTAPLPPRHTFTVPIFALHGQGNYYVPLNVDYNALVPFLNGMDLLEKSYTSMPVVHPININVNFMPSSPSASLLAAAAAAAVAVGKQQQQQAVVAAGAGLPLSTNSAAAQAAAVAAAAVAKAKLEQAMNQSW
Protein: AP2-like ethylene-responsive transcription factor SNZ (Protein SCHNARCHZAPFEN) (Q6PV67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity). Repressor of flowering.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- 1-aminocyclopropane-1-carboxylate oxidase 4
- Squamosa promoter-binding-like protein 9
- Squamosa promoter-binding-like protein 15
- Squamosa promoter-binding-like protein 3
- MADS-box protein SOC1
- Squamosa promoter-binding-like protein 10
- Agamous-like MADS-box protein AGL8
- Squamosa promoter-binding-like protein 13A
- Squamosa promoter-binding-like protein 5
- Squamosa promoter-binding-like protein 13B
Sequence:
MLDLNLGILSTHNEDEDCKVPTSIFIQEEDSINPSNDNLSLITFGILKRNVEILPPPPPPPPPPPPSENELSGPGNEWLDLSSMQRNKQETLVMKKKSRRGPRSRSSHYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAYTAARAYDRAAIRFRGLQADINFIVDDYKQDIEKMKNLSKEEFVQSLRRASASLARGGSKYKNTHMRNDHIHLFQNRGLNAAAAKCNEIRKMEGDIKLGAHSKGNEHNDLELSLGISSSSKVRILEPADYYMGLNRSVTSLHGKPLPGYLPITEIKPLKTVVASSGFPFITMINPSSLSLSCFDP
Protein: L-xylulose/3-keto-L-gulonate kinase (L-xylulokinase) (EC 2.7.1.-) (EC 2.7.1.53) (3-dehydro-L-gulonate kinase) (P37677)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. Is involved in L-lyxose utilization via xylulose, and may also be involved in the utilization of 2,3-diketo-L-gulonate.
Interaction partners:
- Putative L-ribulose-5-phosphate 3-epimerase SgbU
- 3-keto-L-gulonate-6-phosphate decarboxylase SgbH
- 2,3-diketo-L-gulonate reductase
- L-ribulose-5-phosphate 3-epimerase UlaE
- L-ribulose-5-phosphate 4-epimerase SgbE
- 3-keto-L-gulonate-6-phosphate decarboxylase UlaD
- L-Rhamnulokinase
- 2,3-diketo-L-gulonate TRAP transporter small permease protein YiaM
- 2,3-diketo-L-gulonate-binding periplasmic protein YiaO
- Probable L-ascorbate-6-phosphate lactonase UlaG
Sequence:
MTQYWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQGKGLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHDYLRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEINHALPPVVGSAEICGEITAQTAALTGLKAGTPVVGGLFDVVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLRDGEAHPYVYGRYVNDGEFIVHEASPTSSGNLEWFTAQWGEISFDEINQAVASLPKAGGDLFFLPFLYGSNAGLEMTSGFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRERFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQRDLRHPVRTLLPDMTAHQLYQKKYQRYQHLIAALQGFHARIKEHTL
Protein: Ral guanine nucleotide dissociation stimulator-like 1 (RalGDS-like 1) (Q9NZL6)
Organism: Homo sapiens (Human)
Function: Probable guanine nucleotide exchange factor.
Interaction partners:
- GTPase KRas
- Ras-related protein Ral-A
- GTPase HRas
- Ras-related protein Ral-B
- GTPase NRas
- Ras-related protein R-Ras2
- Ras-related protein M-Ras
- Ras-related protein R-Ras
- Ras-related protein Rap-2a
Sequence:
MKLLWQAKMSSIQDWGEEVEEGAVYHVTLKRVQIQQAANKGARWLGVEGDQLPPGHTVSQYETCKIRTIKAGTLEKLVENLLTAFGDNDFTYISIFLSTYRGFASTKEVLELLLDRYGNLTSPNCEEDGSQSSSESKMVIRNAIASILRAWLDQCAEDFREPPHFPCLQKLLDYLTRMMPGSDPERRAQNLLEQFQKQEVETDNGLPNTISFSLEEEEELEGGESAEFTCFSEDLVAEQLTYMDAQLFKKVVPHHCLGCIWSRRDKKENKHLAPTIRATISQFNTLTKCVVSTILGGKELKTQQRAKIIEKWINIAHECRLLKNFSSLRAIVSALQSNSIYRLKKTWAAVPRDRMLMFEELSDIFSDHNNHLTSRELLMKEGTSKFANLDSSVKENQKRTQRRLQLQKDMGVMQGTVPYLGTFLTDLTMLDTALQDYIEGGLINFEKRRREFEVIAQIKLLQSACNSYCMTPDQKFIQWFQRQQLLTEEESYALSCEIEAAADASTTSPKPRKSMVKRLSLLFLGSDMITSPTPTKEQPKSTASGSSGESMDSVSVSSCESNHSEAEEGSITPMDTPDEPQKKLSESSSSCSSIHSMDTNSSGMSSLINPLSSPPSCNNNPKIHKRSVSVTSITSTVLPPVYNQQNEDTCIIRISVEDNNGNMYKSIMLTSQDKTPAVIQRAMLKHNLDSDPAEEYELVQVISEDKELVIPDSANVFYAMNSQVNFDFILRKKNSMEEQVKLRSRTSLTLPRTAKRGCWSNRHSKITL
Protein: C-type lectin domain family 11 member A (C-type lectin superfamily member 3) (Lymphocyte secreted C-type lectin) (Osteolectin) (Stem cell growth factor) (p47) (Q9Y240)
Organism: Homo sapiens (Human)
Function: Promotes osteogenesis by stimulating the differentiation of mesenchymal progenitors into mature osteoblasts. Important for repair and maintenance of adult bone (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11803813}. Secreted {ECO:0000269|PubMed:11803813, ECO:0000269|PubMed:9442024}.
Interaction partners:
- Mast/stem cell growth factor receptor Kit
- Kit ligand
- Macrophage colony-stimulating factor 1
Sequence:
MQAAWLLGALVVPQLLGFGHGARGAEREWEGGWGGAQEEEREREALMLKHLQEALGLPAGRGDENPAGTVEGKEDWEMEEDQGEEEEEEATPTPSSGPSPSPTPEDIVTYILGRLAGLDAGLHQLHVRLHALDTRVVELTQGLRQLRNAAGDTRDAVQALQEAQGRAEREHGRLEGCLKGLRLGHKCFLLSRDFEAQAAAQARCTARGGSLAQPADRQQMEALTRYLRAALAPYNWPVWLGVHDRRAEGLYLFENGQRVSFFAWHRSPRPELGAQPSASPHPLSPDQPNGGTLENCVAQASDDGSWWDHDCQRRLYYVCEFPF
Protein: MARCKS-related protein 1-A (MARCKS-like protein 1-A) (MARCKS-like protein 1-B) (Q6PD99)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in the control of cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P49006}. Cell membrane {ECO:0000250|UniProtKB:P49006}; Lipid-anchor {ECO:0000250|UniProtKB:P49006}. Note=Associates with the membrane via the insertion of the N-terminal N-myristoyl chain and the partial insertion of the effector domain. {ECO:0000250|UniProtKB:P49006}.
Interaction partners:
Sequence:
MGAQLTKGEATVEGKAVADKANGQENGHVKTNGDVSTKPDGEAVAADGNGTAEVAKDEAPKTEEGDGIEAAPATEAEASKSDGEAAKETKKKKKFSLKNSFKFKGISLKKNKKASEEAAEAVATPTTAEDKPEENGQAATETKEEEPAAETNETPAPEAEAEPKVEEAEPKAEEPAQQTETAPTEETTKSEESPAPVEETTPTESSDPEPAAE
Protein: Temporin-1Th (TH) (Temporin-H) (P79876)
Organism: Rana temporaria (European common frog)
Function: Antimicrobial peptide that renders both the outer and inner membrane of bacteria permeable to hydrophobic substances of low molecular mass.
Subcellular location: Secreted {ECO:0000269|PubMed:34235566, ECO:0000269|PubMed:9022710}.
Interaction partners:
Sequence:
MFTLKKSLLLLFFLGTINLSLCEEERNAEEERRDEPDERDVQVEKRLSPNLLKSLLGK
Protein: Probable histone H2AXb (HTA3) (Q9S9K7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H4
- ATP-dependent DNA helicase 2 subunit KU80
- Histone H3.1
- ATP-dependent DNA helicase 2 subunit KU70
- DNA repair protein RAD51 homolog 1
- Histone H3.3
- Histone H3-like 5
- Histone H3-like 3
- Histone H3-like 1
- Histone H3-like centromeric protein CENH3
Sequence:
MSSGAGSGTTKGGRGKPKATKSVSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKTRIVPRHIQLAVRNDEELSKLLGSVTIANGGVLPNIHQTLLPSKVGKNKGDIGSASQEF
Protein: SKP1-like protein 1A (SKP1-like 1) (UFO-binding protein 1) (Q39255)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1. SCF(UFO) is required for vegetative and floral organ development as well as for male gametogenesis. SCF(TIR1) is involved in auxin signaling pathway. SCF(COI1) regulates responses to jasmonates. SCF(EID1) and SCF(AFR) are implicated in phytochrome A light signaling. SCF(ADO1), SCF(ADO2), SCF(ADO3) are related to the circadian clock. SCF(ORE9) seems to be involved in senescence. SCF(EBF1/EBF2) may regulate ethylene signaling. Plays a role during embryogenesis and early postembryonic development, especially during cell elongation and division. Contributes to the correct chromosome segregation during tetrad formation.
Subcellular location: Nucleus {ECO:0000269|PubMed:11387208}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11387208}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:11387208}. Note=Associated to mitotic spindle and phragmoplasts during cell division.
Interaction partners:
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Cullin-1
- RING-box protein 1a
- Coronatine-insensitive protein 1
- Putative cullin-like protein 1
- Putative cullin-like protein 2
- Cullin-like protein 3
- Cullin-2
- Tubby-like F-box protein 9
- RING-box protein 1b
Sequence:
MSAKKIVLKSSDGESFEVEEAVALESQTIAHMVEDDCVDNGVPLPNVTSKILAKVIEYCKRHVEAAASKAEAVEGAATSDDDLKAWDADFMKIDQATLFELILAANYLNIKNLLDLTCQTVADMIKGKTPEEIRTTFNIKNDFTPEEEEEVRRENQWAFE
Protein: Juvenile hormone binding protein 5, isoform C (A0A126GUV0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH08336p
- Cuticle protein 16.5
Sequence:
MNQYFLTGLLLVLGVVLHIDWTTAKPPAKKADQLPSFLKVCHRNAPDLDTCVRESYEELRPRLMEGIPELYIPAMEPLVVPQVKMDQDSGAIYLHSVYRNVKVTGISKHTVNELRLEPSKLKFILSLTFPKLHMESDYSIKVSREGKIMMMPLLGDGHCKVDLVNITMRTELIGQEYKKNGANFLKINTVKVKYELSDVHIHLDNLFNGDKALGDRMNEFLNENWKALAEEVRPLMTKALVDILRASVDKLFASFSYDDLLPM