wanglab/gogpt-training-data huggingface dataset:
Protein: Putative cyclic nucleotide-gated ion channel 8 (Cyclic nucleotide- and calmodulin-regulated ion channel 8) (Q9FXH6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative cyclic nucleotide-gated ion channel.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Calmodulin-2
- Cyclic nucleotide-gated ion channel 18
- Glutamate receptor 1.4
- Putative respiratory burst oxidase homolog protein J
Sequence:
MYKSQYISGHREKFVRLDDTDSRVSMSSNATGMKKRSCFGLFNVTSRGGGKTKNTSKSFREGVKIGSEGLKTIGKSFTSGVTRAVFPEDLRVSEKKIFDPQDKTLLLWNRMFVISCILAVSVDPLFFYLPIVDNSKNCIGIDSKLAVTTTTLRTIIDVFYLTRMALQFRTAYIAPSSRVFGRGELVIDPAKIAERYLTRYFIVDFLAVLPLPQIAVWKFLHGSKGTDVLPTKQALLHIVITQYIPRFVRFIPLTSELKKTAGAFAEGAWAGAAYYLLWYMLASHITGAFWYMLSVERNDTCLRSACKVQPDPKVCVQILYCGSKLMSSRETDWIKSVPDLFKNNCSAKSDESKFNYGIYSQAVSSGIVSSTTFFSKFCYCLWWGLQNLSTLGQGLQTSTYPGEVLFSIAIAVAGLLLFALLIGNMQTYLQSLTVRLEEMRIKRRDSEQWMHHRSLPQNLRERVRRYDQYKWLETRGVDEENIVQSLPKDLRRDIKRHLCLNLVRRVPLFANMDERLLDAICERLKPSLYTESTYIVREGDPVNEMLFIIRGRLESVTTDGGRSGFFNRGLLKEGDFCGEELLTWALDPKAGSNLPSSTRTVKALTEVEAFALEAEELKFVASQFRRLHSRQVQQTFRFYSQQWRTWAACFIQAAWRRHLRRKIAELRRKEEEEEEMDYEDDEYYDDNMGGMVTRSDSSVGSSSTLRSTVFASRFAANALKGHKLRVTESSKSLMNLTKPSEPDFEALDTDDLN
Protein: Claudin-4 (B5XFB8)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MASAGFQMLGTALGIIGWIGAIVVCALPQWKVTVFIGENIITAQTTWQGIWMNCVVQSTGQMQCKVYDSMLALPQDLQAARALIIISIMMGLVGILLSVAGGKCTNCVEYERTKSRIGVGSGVVFIIAGVLCLIPVCWSANTIIRDFYNPMLNSSQKMELGAALYIGWGAAALMIIGGGFLCANCPPKEDNYPTKYSAARSTAPRDYV
Protein: Probable cyclic di-GMP phosphodiesterase PdeC (EC 3.1.4.52) (P32701)
Organism: Escherichia coli (strain K12)
Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG (By similarity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Overexpression reduces biofilm formation.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Diguanylate cyclase DgcP
- Diguanylate cyclase DgcM
- Probable diguanylate cyclase DgcC
- Probable diguanylate cyclase DgcT
- Diguanylate cyclase DgcN
- Diguanylate cyclase DosC
- Probable diguanylate cyclase CdgI
- Diguanylate cyclase DgcZ
- Probable diguanylate cyclase DgcJ
- Probable diguanylate cyclase DgcF
Sequence:
MSHRARHQLLALPGIIFLVLFPIILSLWIAFLWAKSEVNNQLRTFAQLALDKSELVIRQADLVSDAAERYQGQVCTPAHQKRMLNIIRGYLYINELIYARDNHFLCSSLIAPVNGYTIAPADYKREPNVSIYYYRDTPFFSGYKMTYMQRGNYVAVINPLFWSEVMSDDPTLQWGVYDTVTKTFFSLSKEASAATFSPLIHLKDLTVQRNGYLYATVYSTKRPIAAIVATSYQRLITHFYNHLIFALPAGILGSLVLLLLWLRIRQNYLSPKRKLQRALEKHQLCLYYQPIIDIKTEKCIGAEALLRWPGEQGQIMNPAEFIPLAEKEGMIEQITDYVIDNVFRDLGDYLATHADRYVSINLSASDFHTSRLIARINQKTEQYAVRPQQIKFEVTEHAFLDVDKMTPIILAFRQAGYEVAIDDFGIGYSNLHNLKSLNVDILKIDKSFVETLTTHKTSHLIAEHIIELAHSLGLKTIAEGVETEEQVNWLRKRGVRYCQGWFFAKAMPPQVFMQWMEQLPARELTRGQ
Protein: LY86 protein (Lymphocyte antigen 86) (A4IFT3)
Organism: Bos taurus (Bovine)
Interaction partners:
Sequence:
MKGFAAALLIWTLLSPRRAGGEAWPTHTACRNGNLQVLYQSCDPLQDFGFSVDQCARQLKPNINIRFGMVLREDIEQLFLDVALFSKGLSILNFSYPVCEVDLPKFSFCGRRKGEQIYYAGPINNPGFEIPEGDYQVLLELYNQDHATVACANATVLYS
Protein: Phospholipase A and acyltransferase 5 (Ca(2+)-independent N-acyltransferase) (iNAT) (EC 2.3.1.-, EC 3.1.1.32, EC 3.1.1.4) (H-rev107-like protein 5) (HRAS-like suppressor 5) (HRSL5) (Q9CPX5)
Organism: Mus musculus (Mouse)
Function: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (By similarity). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q4KLN5}.
Interaction partners:
- NF-kappa-B inhibitor zeta
Sequence:
MGLSPAASGEFGIRLSRVPWPRPTQISKTSSTESSDTQSATGQSTVPHSDSASSQALLVQFLPKQLKQDRRLEQARSFQQGEKPETSLELTPSKKRTELIPTSNSEIESTQKNQAVEGNPRPRPGDLIEIFRIGYEHWAIYVEDDCVVHLAPPSEFEAGSITSIFSNRAVVKYSRLEDVLHGCSWKINNKLDGTYLPLPVDKIMQRTKNMINKIVQYSLIEGNCEHFVNDLRYGVPRSQQVEHALVEGAKAAGAVLSAVVDSIRPKPITA
Protein: Protein ECM25 (Extracellular matrix protein 25) (P32525)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in cell wall organization and biogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Actin cytoskeleton-regulatory complex protein SLA1
- Cell division control protein 42
- GTP-binding protein RHO1
- RHO GTPase-activating protein RGD1
Sequence:
MIDINVNNIFFRSYSVDPNSGHAIYVFDSTYLPASDEIGDKQVYDLLINALMDRLVMKLPQAPYSLVIFSSGFSQRKISWVYGIKMFAKLPKETKFYLQKIFIVHESFFVRSVYQVISNAMNFNFLDSKDSQHDFPSLVHVLDLTSLSELIDITRLRISLNVYLYDYQIREHINVPEEYYNRLTPLAIRQYRQLVFDKIFKKLQNDALLCELIFQKPGNYKKVNIFLDIIKRNNYIDLSQWDIYSLASVWLNYFIKNKAKPLIPIELIPLPIVDDLKFTSETFRKIIKFNQYQDLFMVIIPFFNRIIAHGESTKHDSRTLSKALTPALCKEKLSMMTNDRLAIGSRYIKNLLDFFPEIAKEISSPPSSVSSSSTIPVLPKPRKSSPTRYSELGCLTLPRSRSPSPQRSVTSPTYTPVALQNTPVLKPKSSSRNVSSPSFNAKPPLPIKAVTRPQLSLTSNSNTDLALASSSTDTLSSPTKTPSADSLPLSNSSTDLTISDNIKEMVKDEPAKDKNSVETDIFVQQFESLTLVQNAKIKKFDKELQEKKKKNETTSKTADKFSQKGYSDIKASNKVSRLAALYEERLQGLQVMNEMKQRW
Protein: Beta-1,4 N-acetylgalactosaminyltransferase 1 (EC 2.4.1.92) ((N-acetylneuraminyl)-galactosylglucosylceramide) (GA2 synthase) (EC 2.4.1.-) (GD2 synthase) (EC 2.4.1.-) (GM2 synthase) (EC 2.4.1.92) (GalNAc-T) (Q10468)
Organism: Rattus norvegicus (Rat)
Function: Involved in the biosynthesis of gangliosides GM2, GD2, GT2 and GA2 from GM3, GD3, GT3 and GA3, respectively.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:1606358, ECO:0000269|PubMed:3140234}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- Lactosylceramide alpha-2,3-sialyltransferase
- Beta-1,3-galactosyltransferase 4
- Beta-hexosaminidase subunit alpha
- Acetyl-coenzyme A transporter 1
- Beta-galactosidase
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
Sequence:
MRLDRRALYALVLLLACASLGLLYASTRDAPGLPNPLALWSPPQGPPRLDLLDLATEPRYAHIPVRIKEQVVGLLAQNNCSCESSGGRFALPFLRQVRAIDFTKAFDAEELRAVSISREQEYQAFLARSRSLADQLLIAPANSPLQYPLQGVEVQPLRSILVPGLSLQEASVQEIYQVNLIASLGTWDVAGEVTGVTLTGEGQSDLTLASPILDKLNRQLQLVTYSSRSYQANTADTVRFSTKGHEVAFTILIRHPPNPRLYPPSSLPQGAQYNISALVTVATKTFLRYDRLRALIASIRRFYPTVTIVIADDSDKPERISDPHVEHYFMPFGKGWFAGRNLAVSQVTTKYVLWVDDDFVFTARTRLEKLVDVLERTPLDLVGGAVREISGYATTYRQLLSVEPGAPGFGNCLRQKQGFHHELAGFPNCVVTDGVVNFFLARTDKVRQVGFDPRLNRVAHLEFFLDGLGSLRVGSCSDVVVDHASKVKLPWTSKDPGAELYARYRYPGSLDQSQVAKHRLLFFKHRLQCMTAE
Protein: Ral guanine nucleotide dissociation stimulator-like 3 (RalGDS-like 3) (Q3MIN7)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF) for Ral-A. Potential effector of GTPase HRas and Ras-related protein M-Ras. Negatively regulates Elk-1-dependent gene induction downstream of HRas and MEKK1 (By similarity).
Interaction partners:
- GTPase KRas
- GTPase NRas
- GTPase HRas
- Ras-related protein Ral-A
- Ras-related protein Ral-B
- GTP-binding protein Rit1
Sequence:
MERTAGKELALAPLQDWGEETEDGAVYSVSLRRQRSQRRSPAEGPGGSQAPSPIANTFLHYRTSKVRVLRAARLERLVGELVFGDREQDPSFMPAFLATYRTFVPTACLLGFLLPPMPPPPPPGVEIKKTAVQDLSFNKNLRAVVSVLGSWLQDHPQDFRDHPAHSDLGSVRTFLGWAAPGSAEAQKAEKLLEDFLEEAEREQEEEPPQVWTGPPRVAQTSDPDSSEACAEEEEGLMPQGPQLLDFSVDEVAEQLTLIDLELFSKVRLYECLGSVWSQRDRPGAAGASPTVRATVAQFNTVTGCVLGSVLGAPGLAAPQRAQRLEKWIRIAQRCRELRNFSSLRAILSALQSNPIYRLKRSWGAVSREPLSTFRKLSQIFSDENNHLSSREILFQEEATEGSQEEDNTPGSLPSKPPPGPVPYLGTFLTDLVMLDTALPDMLEGDLINFEKRRKEWEILARIQQLQRRCQSYTLSPHPPILAALHAQNQLTEEQSYRLSRVIEPPAASCPSSPRIRRRISLTKRLSAKLAREKSSSPSGSPGDPSSPTSSVSPGSPPSSPRSRDAPAGSPPASPGPQGPSTKLPLSLDLPSPRPFALPLGSPRIPLPAQQSSEARVIRVSIDNDHGNLYRSILLTSQDKAPSVVRRALQKHNVPQPWACDYQLFQVLPGDRVLLIPDNANVFYAMSPVAPRDFMLRRKEGTRNTLSVSPS
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit (GPI-GlcNAc transferase complex subunit GPI2) (GPI-GnT subunit GPI2) (EC 2.4.1.198) (P46961)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit
- GPI mannosyltransferase 1
- GPI mannosyltransferase 2
- GPI ethanolamine phosphate transferase 3
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
Sequence:
MTRSPWKRLLWLKQEYPDNYTDPSFIELRARQKAESNQKSDRKLSEAARAQIRLDFISFYQTILNTSFIYITFTYIYYYGFDPIPPTIFLSFITLIISRTKVDPLLSSFMDVKSSLIITFAMLTLSPVLKSLSKTTASDSIWTLSFWLTLWYIFVISSTKSKDKPSNLSTNILVALVAVLSSRLSTTIDVFCFLLICIQLNIILPTYLSVTNKVVPIISNIIVYSFLNVALGWIYMLLIFFASVFYITVLPKWFIYWKINYHKRDNDLLSTWDARTPILD
Protein: Prospero homeobox 1 (D3ZU00)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Extracellular link domain-containing 1
Sequence:
MPDHDSTALLSRQTKRRRVDIGVKRTVGTASAFFAKARATFFSAMNPQGSEQDVEYSVVQHADGEKSNVLRKLLKRANSYEDAMMPFPGATIISQLLKNNMNKNGGTEPSFQASGLSSTGSEVHQEDICSNSSRDSPPECLSPFGRPTMSQFDVDRLCDEHLRAKRARVENIIRGMSHSPSVALRGNENEREMAPQSVSPRESYRENKRKQKLPQQQQQSFQQLVSARKEQKREERRQLKQQLEDMQKQLRQLQEKFYQVYDSTDSENDEDGDLSEDSMRSEILDARAQDSVGRSDNEMCELDPGQFIDRARALIREQEMAENKPKREGSNKERDHGPNSLQPEGKHLAETLKQELNTAMSQVVDTVVKVFSAKPSRQVPQVFPPLQIPQARFAVNGENHNFHTANQRLQCFGDVIIPNPLDTFGNVQMPSSTDQTEALPLVVRKNSSEQSASGPATGGHHQPLHQSPLSATAGFTTPSFRHPFPLPLMAYPFQSPLGAPSGSFSGKDRASPESLDLTRDTTSLRTKMSSHHLSHHPCSPAHPPSTAEGLSLSLIKSECGDLQDMSDISPYSGSAMQEGLSPNHLKKAKLMFFYTRYPSSNMLKTYFSDVKFNRCITSQLIKWFSNFREFYYIQMEKYARQAINDGVTSTEELSITRDCELYRALNMHYNKANDFEVPERFLEVAQITLREFFNAIIAGKDVDPSWKKAIYKVICKLDSEVPEIFKSPNCLQELLHE
Protein: Xaa-Pro aminopeptidase 1 (EC 3.4.11.9) (Aminoacylproline aminopeptidase) (Cytosolic aminopeptidase P) (Soluble aminopeptidase P) (sAmp) (X-Pro aminopeptidase 1) (X-prolyl aminopeptidase 1, soluble) (O54975)
Organism: Rattus norvegicus (Rat)
Function: Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10095056}.
Interaction partners:
- Cytosol aminopeptidase
Sequence:
MAPKVTSELLRQLRQAMRNSECVAEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDNNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLVPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKEKVADLRLKMAERSIVWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLERIMLFIDGDRIDAPGVKQHLLLDLGLEAEYKIQVLPYKSILSELKTLCADLSPREKVWVSDKASYAVSEAIPKDHRCCMPYTPICIAKAVKNSAESAGMRRAHIKDAVALCELFNWLEQEVPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPIPETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKTKYNFNNRGSLTFEPLTLVPIQTKMIDVDALTDKECDWLNSYHQTCRDVIGKELQTQGRQEALEWLLRETEPISRQH
Protein: Potassium voltage-gated channel subfamily H member 1 (A0A0S1TJ81)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTIEKVRQTFENYEMNSFEILMYKKNRKGDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEERMKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNVLTEHASANHSLVKASVVTVRESPATPVSFQAASTSGVPDHAKLQAPGSECLGPKGGGGDCAKRKSWARFKDACGKSEDWNKVSKAESMETLPERTKASGEATLKKTDSCDSGITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQATVLEVRHELKEDIKALNAKMTNIEKQLSEILRILTSRRSSQSPQELFEISRPQSPESERDIFGAS
Protein: Autophagy-related protein 18h (AtATG18h) (Q8H1Q5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Required for autophagy (By similarity).
Subcellular location: Preautophagosomal structure membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Peripheral membrane protein of pre-autophagosomal structure (PAS) and vacuole. {ECO:0000250}.
Interaction partners:
- Autophagy-related protein 8d
- Ethylene-responsive transcription factor 5
- Autophagy-related protein 18a
- Autophagy-related protein 18e
- Autophagy-related protein 18c
- Autophagy-related protein 9
- Autophagy-related protein 18d
- Ubiquitin-like-conjugating enzyme ATG10
- DNA topoisomerase
- Cysteine/Histidine-rich C1 domain family protein
Sequence:
MKSNSKVNINNNGDNHNQTKNNGTNGFLPNSLKFISTCIRTASSGVRSASASVAASLSSDSHELKDQVLWSSFDRLHTSESSFKNVLLLGYTNGFQVLDIDDSNDVTEFVSRRDDPVTFLQMQPLPAKCDGVEGFRSSHPILLAVADEAKGSGPIVTSRDGSVRNGYEDPLALSPTVVRFYSLRSHNYVHVLRFRSTVYMVRCSPRIVAVGLGSQIYCFDALTLENKFSVLSYPVPQLGNQGISGVNVGYGPMAVGARWLAYASNSPLSSSIGRLSPQNVTPPGVSPSTSPNNGNLVARYAMESSKHLAAGLLNLGDKGYKTISKYCQDLKHDGPGPSLSSSPGRKVGRVGSHSAESDVVGTVIVKDFESRAIIAQFRAHTSPISALCFDPSGTLLVTASIHGNNINVFRIMPTPTKNGPGAQSYDWSSSHVPLYKLHRGMTSAVIQDICFSSYSQWIAIVSSKSTCHIYVLSPFGGENVLEIRNSQFDGPTLAPTLSLPWWSSPSFMTTHFSYPPPASVTLSVVSRIKCNNFFHAASSVVGKPTFPSGCLAAVFHQSVPQESQSSSPALDYLLVYTPSGHVVQYKLIPSLGGDQAESNTRNGATSGLTSEEELRVKVEPVQCWDVCRRADWPEREENICGLTYGGRKNAELTVDTSDSEDQTKPLEKHHVYLANAEVLINSGRKPIWQNSEISFYPMYPPDSDGKNLNSHQGGGETEIGKVSANEVDIRRKDLLPVYDNFHSVYTSMRNRGFSGERDSDSSSSSDPGQVKEMHPFNGMVYPEDEERRGSAHFALTPNQNPHTGIVTFKQPVVSISSAVKDTDYIDDDAHVLPKNASLPAETKIENSSGISGDSNVSSNRSDMSMNAADEGEGPIDGSPNFEQFFEEVVSNETVTETEHKDAPSDGKLDDDEDDDMLGGVFAFSEEG
Protein: Protein S100-A6 (Calcyclin) (S100 calcium-binding protein A6) (Q98953)
Organism: Gallus gallus (Chicken)
Function: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity).
Interaction partners:
- Calcyclin binding protein.
- Protein S100-A10
- Annexin A2
- Annexin A1
- Annexin
- S100 calcium binding protein A13
Sequence:
MAAPLDQAIGLLVATFHKYSGKEGDKNSLSKGELKELIQKELTIGPKLKDAEIAGLMEDLDRNKDQEVNFQEYVTFLGALAMIYNEALLQYK
Protein: tRNA (guanine(26)-N(2))-dimethyltransferase (EC 2.1.1.216) (Q386C5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- U3 small nucleolar RNA-associated protein 13 C-terminal domain-containing protein
- Ribosome production factor 2 homolog
- tRNA
Sequence:
MCRPLADCTKRKKSTLPPRTAFFRLLDCLLLLTEVEVLVPCISFSRFPPFFFHHFTVLQHELSLPGFSRGSVVAHHPAMRSGLFGTEGLRKETPRGYTVVVEGTTAVLFPPAAGSSTQIGRGFSDIDKEEVGKQRKDDSCAPNCSLNSKEDNTCGEEDEECGQAVFYNPAQVVNRDLSVCVIACFSQLRKEEPKNKGGTRRGITILEALSATGLRAIRYYKEIPDVRFIIANDIDCDAVECIRRNCEFNEVPCVAPTFQENFPSSCIRVDETTGTVESGGAIFANLDDANDLMFRLATNPTVNPGHRLCLAATQNGSCKDGVDTESGEARGIRPLIQQELVDVVDLDPYGSASPFLEGAVRCIREGGLLLVTSTDSAILCGNYPDTCHAKYNTVPTKNAACHEMAVRILLAAVERVANKHRKYIVPLLSLHIDFYVRCFVRVYTQPAEVKLSPCKLGYLIQCNHCPAFWVRQIAVSRMRVKKRSRKLGNAGEDVTAGSQGNVAKSEEHRLSDSGNARGTNEGGEAHKADEWGWERFPAAPSRRENPKIVSPSLQQIFPSSLRGHCCCVCGASVSLSGPIYAAPTQSAPFLGQLLVEIERRASANHITAVARISGLVRVAMEELADTPLFYQLPDVASFVRVRCPPAPLFIGALGRKGYRCSQVHCAPSGIKTDCPPEIVVGVMMQWKKYEEENNERVVEGGKEEDAVLDIHSDRVTSPPAMIEGGGCGSGDGKSNERGTRKKGRVDQRVPLVKPLSDVDFSYDKQFDFRGAVTGVAKFIPNAPNWGPKRKHQGAMHSAVDAP
Protein: adenylate cyclase (EC 4.6.1.1) (Q7KLG6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MYTKYLTDRGQRLAFIETHKAMEHKKESEKELQRTQKLLDSILPNIVNNQIRSEMYKGTDPTVETQFNKLYVYPMDNVSILFADIKGFTELASKTSAQQLVKILNDLFARFDRIAEDNHCLRVKLLGDCYYCVSQFESDNWKTRPDHAVCSVETGLHMIKAIKDVRLHTHVDLNMRIGIHSGSVMCGVLGNKKWHFDVWSNDVIIANHMESGGIPGRVHISEATLKCLNDAYEVEPGNGGCRDNHLKMLNVKTYLIKRTEPLRPKRRFGTRSSAHLAGSVATAAPPCATPTALPKSISASGSGSIGGVTATGNDGASIDGRSLEYAATIAVPAQQPTQLLQQQQKKNISLNSLPNVVEGVAMDSRRIRNGCGVMGGAGGTGGGGTGPCGMSTVSSPTAMMSAPLEVQLRPRNGACSIQNLAEAIDGKGLIIEDESTTDWIPEIPFKNLNSPEDGLNRADSILVDTKEDHRVSVAVLDEEIDEFIEQNIQINSNKEIRREYLNPWTLKFKDKSQEQKFCQLREDMFRSNMLCVFVIWIFMVLCQVIIIPRCTRLIICLSVGTVILTFCCVLVMAEEFPGLPRCLKTNSAKLVHQRQRRTLFICGVIVSMCMLSAIGLVLCPSSTYIGTADEHSRFLRMVSPYSNTSMTEKEFKLNVYLSATIHHNITISTPASGGPTPLVDITSSGPSDEFVRSTLNALTLNLTPPLPQSHRPYTLTTNGHSVSLSNLSYSDASVMQSSSDVEGQCAHPEYLVFTWVLCLVSLATALKLYYLVKALMALAMVAFYTTLIMMKFGSGDSFSLVELSRLGMPLGVQMLILLISFLVMVCYHARLVEVTSRLDFIWKEQAERELTNMKSNRALNDTLIKNILPDHVATYYLSDEHTDELYSKMHNLCGVMFASIPNFQDFYSEDIDNGKACIRILNEIICDFDELLEEPRFASVEKIKTVGATYMAAAGLNHEHLRLRGETSEDSVCDLVEFAFAMKQKLEEINGDAFNNFQLRVGICSGPLVSGVIGARKPVYDIWGNTVNVASRMDSTGENWRVQVPENTAELLCSRGYTCVKRGEIAVKGKGMMTTFYVHPKGISESQLISPVRMPAGIPLAQTPNLQRQTSHHGSFSAVVFGMLQASKRSTAIAGTPTGTPSPQIRRGHRGSTFSSVRLSQKSTTVNPVRRNTTRVRGRSYRQKKSSSNNSIVTQASSSYMPSFRRIDQIETTISKSHNDAL
Protein: E3 ubiquitin-protein transferase MAEA (EC 2.3.2.27) (Macrophage erythroblast attacher) (B4DQT1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus matrix {ECO:0000256|ARBA:ARBA00004109}.
Interaction partners:
Sequence:
MVVAELEKTLSGCPAVDSVVSLLDGVVEKLSVLKRKAVESIQAEDESAKLCKRRIEHLKEHSSDQPAAASVWKRKRMDRMMVEHLLRCGYYNTAVKLARQSGIEDLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKMKSCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQLDEVRQAMGMLAFPPDTHISPYKDLLDPARWRMLIQQFRYDNYRLHQLGNNSVFTLTLQAGLSAIKTPQCYKEDGSSKSPDCPVCSRSLNKLAQPLPMAHCANSRLVCKISGDVMNENNPPMMLPNGYVYGYNSLLSIRQDDKVVCPRTKEVFHFSQAEKVYIM
Protein: Zinc finger BED domain-containing protein DAYSLEEPER (Transposase-like protein DAYSLEEPER) (Q9M2N5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transposase-like protein that is essential for plant growth and development. Binds the promoter region of the DNA helicase KU70 and genes involved in chromatin remodeling. May regulate global gene expression by recruiting other cellular factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:23067104}.
Interaction partners:
- Terpenoid synthase 1
- Thioredoxin Y1, chloroplastic
- HAT transposon superfamily
- Protein FAR-RED ELONGATED HYPOCOTYL 3
- HAT transposon superfamily
- F10A16.15 protein
- HAT transposon superfamily
- ATP-dependent DNA helicase 2 subunit KU70
- Toll/interleukin-1 receptor-like protein
Sequence:
MEVYNDDTEMRSPETQPIKETALEVYNDTAEIRSPETQPIEETALEVYNDTEMVSPETQPIKRRKKKSMVWEHFTIEAVEPNCRRAFCKGCNQSFAYSNGNKVAGTSHLKRHIFKGTCPALIHTHDNDNNPLMSTPYTPKTDTPRRRYRSQNNASPYVAFNQDKCRQEIAKMIIMHDYPLHMVQHPGFVSFVQSIQPHFDAVSFNNVQGDCVATYLAEKQNVMKSLEGIPGRFCLTLDFWTSKLTLGYVFITAHYIDSDWKIQKKLLNVLMESYPEADEALSLAVANCVSEWGLEGKLFNVTFNHPASNSAVENIRPQLCIKNPGILDGQLVIGNCVARTFGSLAKDVLEKGKDVIKNIRDSVKHVKTSESHEERFTELKEQLQVPSEKVLSLDDQTQWNTTYMMLVAASELKEVFSCLDTADPDYKKPPSAEDWRHVEALCTFLKPLFEAVSTLQSTGNPSAVTFFHEVWKTQSDLSRAIAGEDPFVTGIAKTMQEKVDKYWRDCSLVLAMAVVMDPRFKMKLVEFSFSKIFGEDAGKNIKTVDDGIHELFTEYMALPSPQNTTSEGGKADGLSDFDTYIMETTGQNLKSELDQYLDETLLPRVQEFDVLDWWKQNKLKYPTLSKMARDILSIPVSAAAFDYVFDMEPREMDEYKTSLRPETVEALICAREWLLESNASSSAAAQNASATIKSEA
Protein: Cysteine--tRNA ligase, cytoplasmic (EC 6.1.1.16) (Cysteinyl-tRNA synthetase) (Q7KN90)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Valine--tRNA ligase
- Tyrosine--tRNA ligase
- leucine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Alanine--tRNA ligase, cytoplasmic
- serine--tRNA ligase
- Glycine--tRNA ligase
- Asparagine--tRNA ligase, cytoplasmic
Sequence:
MSKRGQPAWQAPEAVDRPKLKLFNSLTRQKEDFVPLDGNNVTWYSCGPTVYDASHMGHARSYISFDILRRILSDYFGYNIHYVMNITDIDDKIIRRARQNHLFDEYAAEAQKLPLDELLGQQKEVLQRFQDTCAKNTDPDKKIMLDKTLQRMNDAVEALTKAVGKGDEREISEKRLLYLNEAKDPISDWLDSLKGAQINDNAVFEALPRYWEDQFHNDMKSLNILPPDVLTRVSEYVPQIVTFIQKIIDNGLAYAANNSVYFDVNGFDKREKHHYAKLVPEAYGDTKSLQEGEGDLSIAEDRLSEKRSANDFALWKASKAGEPWWDSPWGKGRPGWHIECSAMASDIFGPTFDIHTGGVDLKFPHHDNELAQSEAAFNESEWVKYFLHTGHLTIAGCKMSKSLKNFVTIQEALKKHSATQLRLAFLLHSWKDTLDYSENTMEMATQYEKFLNEFFLNVKDLTRHVLSEEPRRQFDAWTEVEAALQKKFSNAQVQVHASLCDNIDTRSALDAIRELVSVSNVYIRDNKTRLNSLLLRNVATYITDLLHVFGAISGPRGGIGFPVSGGSGAQAAGADLETTVLPYVQSLAEFRYLVREQAKTLKAFDILKLCDDLRDNVLPNLGVRLEDKDIGKYAVKLVDRDSLLREREAKLAAEAEKAAEKERKKQAAAEAAAAKEAQRRVNPKEMFLAETEKYSAFDENGLPTHDKEGKEVSKGQIKKLQKLQQQQEQRYNEYLASIEKA
Protein: Agglutinin-like protein 1 (Adhesin 1) (Q5A8T4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Major cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Acts as a downstream effector of the EFG1 regulatory pathway. Required for rapamycin-induced aggregation of C.albicans. Binds glycans and mediates adherence to endothelial and epithelial cells, thereby playing an important role in the pathogenesis of C.albicans infections.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15302828, ECO:0000305|PubMed:12845604}. Secreted, cell wall {ECO:0000269|PubMed:18712765, ECO:0000269|PubMed:20705663, ECO:0000269|PubMed:20864472, ECO:0000269|PubMed:22106872}. Note=Identified as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer (Probable) (PubMed:15302828). Covers the germ tube as well as the cell surface with the exception of bud scars (PubMed:22106872). {ECO:0000269|PubMed:15302828, ECO:0000269|PubMed:22106872, ECO:0000305|PubMed:12845604}.
Interaction partners:
- Enhanced filamentous growth protein 1
- Hyphal wall protein 1
- Biofilm and cell wall regulator 1
- Extent of cell elongation protein 1
- Cell wall adhesin EAP1
- Transcription activator TEC1
- Transcriptional regulator NRG1
- Hyphally regulated cell wall protein 1
- Secreted aspartic protease 5
- Cell wall protein RBT1
Sequence:
MLQQFTLLFLYLSIASAKTITGVFDSFNSLTWSNAANYAFKGPGYPTWNAVLGWSLDGTSANPGDTFTLNMPCVFKYTTSQTSVDLTADGVKYATCQFYSGEEFTTFSTLTCTVNDALKSSIKAFGTVTLPIAFNVGGTGSSTDLEDSKCFTAGTNTVTFNDGDKDISIDVEFEKSTVDPSGYLYASRVMPSLNKVTTLFVAPQCENGYTSGTMGFSSSNGDVAIDCSNIHIGITKGLNDWNYPVSSESFSYTKTCTSNGIQIKYQNVPAGYRPFIDAYISATDVNQYTLAYTNDYTCAGSRSQSKPFTLRWTGYKNSDAGSNGIVIVATTRTVTDSTTAVTTLPFNPSVDKTKTIEILQPIPTTTITTSYVGVTTSYSTKTAPIGETATVIVDVPYHTTTTVTSEWTGTITTTTTRTNPTDSIDTVVVQVPSPNPTVSTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNHTVTTTEYWSQSFATTTTVTAPPGETDTVIIREPPNHTVTTTEYWSQSYATTTTVTAPPGGTDTVLIREPPNHTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTITAPPGETDTVIIREPPNHTVTTTEYWSQSYATTTTVTAPPGGTDTVLIREPPNHTVTTTEYWSQSYATTTTVTAPPGGTDTVLIREPPNHTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNHTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSFATTTTVTAPPGGTDTVIIYESMSSSKISTSSNDITSIIPSFSRPHYVNSTTSDLSTFESSSMNTPTSISSDGMLLSSTTLVTESETTTESICSDGKECSRLSSSSGIVTNPDSNESSIVTSTVPTASTMSDSLSSTDGISATSSDNVSKSGVSVTTETSVTTIQTTPNPLSSSVTSLTQLSSIPSVSESESKVTFTSNGDNQSGTHDSQSTSTEIEIVTTSSTKVLPPVVSSNTDLTSEPTNTREQPTTLSTTSNSITEDITTSQPTGDNGDNTSSTNPVPTVATSTLASASEEDNKSGSHESASTSLKPSMGENSGLTTSTEIEATTTSPTEAPSPAVSSGTDVTTEPTDTREQPTTLSTTSKTNSESVATTQATNENGGKSPSTDLTSSLTTGTSASTSANSELVTSGSVTGGAVASASNDQSHSTSVTNSNSIVSNTPQTTLSQQVTSSSPSTNTFIASTYDGSGSIIQHSTWLYGLITLLSLFI