wanglab/gogpt-training-data huggingface dataset:
Protein: Differentially expressed in FDCP 6 (DEF-6) (IRF4-binding protein) (SWAP-70-like adapter of T-cells) (Q8C2K1)
Organism: Mus musculus (Mouse)
Function: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which plays a role in the activation of Rho GTPases RAC1, RhoA and CDC42. Can regulate cell morphology in cooperation with activated RAC1. Involved in immune homeostasis by ensuring proper trafficking and availability of T-cell regulator CTLA-4 at T-cell surface (By similarity). Plays a role in Th2 (T helper cells) development and/or activation, perhaps by interfering with ZAP70 signaling. Required for optimal T-cell effector function, lymphocyte homeostasis and the prevention of systemic autoimmunity (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12648457}. Cell membrane {ECO:0000269|PubMed:12648457}. Nucleus {ECO:0000250|UniProtKB:Q9H4E7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9H4E7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H4E7}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9H4E7}. Note=Recruited to the plasma membrane upon binding phosphatidylinositol 3,4,5-trisphosphate. Binds to actin filaments. {ECO:0000250|UniProtKB:Q9H4E7}.
Interaction partners:
Sequence:
MALRKELLKSIWYAFTALDVEKSGKVSKSQLKVLSHNLYTVLNIPHDPVALEEHFRDDDDGPVSSQGYMPYLNKYILDKVEEGAFVKEHFDELCWTLTAKKNYRADGIGSSPLSNQDAFRLWCLFNFLSEDKYPLIMVPDEVEYLLKKLLGSLSLEMGLGELEELLAQDAQSAQTAVGLSVWQFLELFNSGRCLRGVGRDSLSMAIQEVYQELIQDVLKQGYLWKRGHLRRNWAERWFQLQPSSLCYFGSEECKEKRGTIPLDAHCCVEVLPDREGKRCMFCVKTASRTYEMSASDTRQRQEWTAAIQTAIRLQAEGKTSLHKDLKQKRREQREQRERRRAAKEEELLRLQQLQEEKERKLQELELLQEAQRQAERLLQEEEERRRSQHKELQQALEGQLREAEQARASMQAEMELKKEEAARQRQRIAELEEMQERLQEALQLEVKARRDEEAVRLAQTRLLEEEEEKLKQLMHLKEEQERYIERAQQEKQELQQEMALQSRSLQHAQQQLEEVRQNRQRADEDVEAAQRKLRQASTNVKHWNVQMNRLMHPIEPGDKRPTTSSSFTGFQPPPLARRDSSLKRLTRWGSQGNRTLSVNSSEQKSLNGGDETPILALASQEEKLDPAPGN
Protein: Gcr3p (A0A1D8PEB4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nuclear cap-binding protein subunit 2
- Sm protein B
- Nucleoporin
- Pre-mRNA-processing factor 17
- Sm protein F
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein G
- Nucleoporin NSP1
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein E
Sequence:
MEFSNKRSRDDFEQDEGQFHDGPSHDSFDHKRHHIDPAQELINNICKDIRRLGEAGDIENLIADTNYISNPIVAEFEKIDNLRNSILSTIYALITEQPHKISAIANLILICNAKNFVIAKYVIEYLHSKMQTMLDSQEGSVFNDIKNILKFLSTLTPIIEDNGIIQIFKQFLNFAIELQEQTEVRNGLAQEIYYNVLIAIPYVLSNDNSDDLKKSINELIELARNFKIVAESATVLLPFDTRMGNFELPYIPKQMVDLILPALIKLQNDDWNFRLFLDFKTHLDPVIQSALENNSISSELVKHKLPQLSFPSVENASFKSTSIDKLWNDNPRYLFQVYNNTTEYETVPPIETYLGLFFKDIAFDILTNLSFNKNETAIELSILDMFFDNKLFAPPGTSIDQLNAIYEDNKSGTNDPSLSTWKIEDVAVESILTMIFQLPNPLEVEIYYYTVLISCCRESPESIAPVFGRAIRYFYNHLETLDYELKIRFLDWMSIQLSNFEFSWKWEEWVSDSKKLKDLKYHPKKNFIKNLIAKEIRLSNKKRIKDSFIDIVDGEVVNLDEFYQYLDISMVPDVKSYIISYDTELYGESSRDTLIQLYEQKQEQLNSKSNIGAQNEIFFNFTNSELPFHETASKVYDFILTHWKSNTDFNELYKSVLESITAPNNERFAINLIIQTYAYIGSRSIYSVVSILSRDINKLKFLSGAPIDYVGDEARFEDLHFTEEEKQNRQNWIIEAVFRIWIHQPQVVFLILEYLIEFGIIDPKYILVKALESNLIIDNVSCMESINRILSKAESKELIIQLFTAIIDNLNKLELDKEKRVEIEEVTESNATEVDKQWLFYEYLGLLKSYYRKYIIGDVECHDKVKEIVGQLENASAKDEILKWFG
Protein: Chaperone protein DNAJ, putative (Q38AB7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGIDYYKVLGVSRDASPSDIKKAYHQLALKYHPDKASGNREEAERLFKEVAEAYDVLSDEKKKKIYDSYGEEGLKGGVPDGSSGGPGGAGFHGFSSGGGTYNFSNRDAFKVFESFFGSNDPFAGGDMFGGGPGLHRVFRGFGGPHGFMSGFGSPEMSPAHEVPPLEYTFSCTLEEIYSGCTKKFNVLRPLPTGEEKKLFEVAVLPGYKKGTKVRFVGEGGIVQGYPPNVMADLVFVLDEKPHPRFKRDGADVLTTVQINLKQALLGTTISVLCLDGTTQSLPLTGVSKNGRKLRVSGKGLPNRKTKQNGDMYVTIEVVMPTSLNEATKRLVEKCEF
Protein: Protein zwilch (Q9VA00)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin, Mad2 complexes and spindly/CG15415 onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the RZZ complex. Failure to assemble the complex due to the absence of any one of its components, results in the incorrect redistribution of the remaining components to diverse membrane compartments.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22685323}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12686595, ECO:0000269|PubMed:22685323}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:22685323}. Note=Dynamic pattern of localization during the cell cycle (PubMed:22685323). In most cells at interphase, present diffusely in the cytoplasm (PubMed:22685323). At metaphase, detected at the kinetochores and kinetochore microtubules, and in late anaphase and telophase accumulates at the spindle envelope midzone (PubMed:12686595, PubMed:22685323). {ECO:0000269|PubMed:12686595, ECO:0000269|PubMed:22685323}.
Interaction partners:
- Rough deal
- Centromere/kinetochore protein zw10
- Bub1-related kinase
- Spindly
- CENP-meta, isoform C
- Bub1 kinase, isoform A
- Kinetochore protein NDC80
- RINT1-like protein
- Monopolar spindle 1, isoform B
- Mitotic checkpoint protein BUB3
Sequence:
MSASANLANVYAELMRRCGESYTITYGAPPTYLVSMVGAAEAGKKIVLVFKEDRNGAVARLRTTPTRAAPKKEGSADLDLTGSPLKDDCLVDAIADLSIDLQLDHSNPWKLEEEYQRGIPVDKARSIVCSEFLQLAEGLGSVWFLCDGSDLGQTQLLQYEFNPTHFSRGILSYQGVRPAYLVTSQALVRHHGKTPDETLIENSYQVNPHMRLRCSWTSSAALPLLVNLNDCDVALNHTFRVGDCGPLTQDFMNQLRILVYIREDIVSYHTDVKQGVSRDPTYRCGSGIDMDELRESINQTMTDVSGLIGRYSISNAEFDIEDVVQRAKVRQLTDLTDKLWELLKCCHSYKDLKIAFSMLFQCAARCNIVNTPTNKNRLAKIITELANRRLAMPCLSGAEPLELLLEIGLEKLYKDYEFIYTESKMCSTNLLKDDSSGASMDDGSPQNLPQLRKSLHNAVRGDPTPGAGMRKTLLHHHGAVNSRSTKYAGSDDDAGFKNSHFDEHESTERISKLFQIHCTLEHLLMMHIHLNLANVYNDVCSELLKKPPKLVESIDDQLSDVMDIRLSAHYVRDHLDGKDPYSRHITMRSHNKFRELKTTFYFNSENICPPNLAQCFQCDDKEMVKERTYHSWIYHKIRSLK
Protein: Plastin-1 (Fimbrin) (P19179)
Organism: Gallus gallus (Chicken)
Function: Actin-bundling protein. In the inner ear, it is required for stereocilia formation. Mediates liquid packing of actin filaments that is necessary for stereocilia to grow to their proper dimensions.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q3V0K9}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q3V0K9}.
Interaction partners:
- Actin, cytoplasmic 1
- Fascin
- Calponin
- Calponin
- Fascin
- Actin, cytoplasmic 2
- Scinderin
- WH2 domain-containing protein.
- Cofilin-2
- Gelsolin
Sequence:
MENNVTTISREELEELREAFNKIDIDNSGYVSDYELQDLFKEASLPLPGYKVREIIEKIFAVTDSNKDGKINFEEFVSLIQELKSKDVSKSYRKSINKKLGITALGGTSSISTEGTQHSYSEEEKVAFVNWINKALQDDPDCKHILPMNPSDASLFKSLADGILLCKMINFSQPDTIDERAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKVGLFADIEISRNEALIALLNEGEELDQLMKLSPEELLLRWVNYHLANAGWQKISNFSQDIRDSRAYYHLLNQIAPKGDDFDEIHVEIDFSGFNDKNDLRRAECMLQQADKLGCRQFVTPADVVAGNPKLNLAFVANLFNTYPALHKPDNSSYDLTLLEGESNEERTFRNWMNSLGVSPYVNHLYSDLSDALIIFQLYEMTRVPVDWTHVNKRPYPLLGGNMKKIENCNYAVELGKTKAKFSLVGIAGHDLNEGNPTLTLALIWQLMRRYTLNVLSDLGEGEKVNDEIIIKWVNQTLANANKKTSITSFKDKSISTSLPVLDLIDAIAPKAVRQEMVKREDLSYQDKLNNAKYAISVARKIGARIYALPDDLVEVKPKMVMTVFACLMGRGLNKIK
Protein: Probable serine/threonine-protein kinase roco11 (EC 2.7.11.1) (Ras of complex proteins and C-terminal of roc 11) (Q6XHA5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Uncharacterized protein
- SAP DNA-binding domain-containing protein
- Latrophilin receptor-like protein A
- Probable serine/threonine-protein kinase roco6
- Tubulin beta chain
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase qkgA
- Uncharacterized protein
- Tubulin alpha chain
Sequence:
METSQIRNGFNKVEVDVVGPLKDLLVRVMKNINTPFKILNETFKINYCDQQETKTKSSFYIQTLDANDKSSLELTKSAIKNIQMQQQQQQQQQQQQQQQQHHDIFQFTQPSSSHNHSNHHHHHHQQQLQQQQQQQLQQQMKTPKLLFFIVMSVGVGKSYIKNIKEEAGTIPILEWFTNYIRSWEEVFKLTSNQVTSHIKRQLLTKACTTGNINLLDEILLSGISKEQIKETQTIGHGIILKSLIVNNLDSIVVSGSMSLLGAVIDNDNDKKGSSLILSKLNLNLFPKSIITACFNLAELDLSYNNIKEIPKEICQLKHLKILNMNNNQLDDLPLELANLTNLKYLAVQDNPLNKFPHHIIEQGTKRTLVFLKNIIEGKKSETWNKVKLMFVGQEGVGKSSLCKALMGSRRRSSSSFAAELQKSGDTISTEGVKIQSIKGKKIDFYAWDFGGQQVFYPTHQFFLTNQALYLLVFKLTDPNFAERVNYWTLQIKANSGLSVPMIFLVGTHCDACTPEQLSSAEQILKENFVKYSRIRQNAISFVSCTNGTGIKELKKILTNEAEKSNLIKSNIPGSYLILEQRLTDRGANSSRILINQNNINQNNNNNNNNNNHNNCNNNENCTTTAATAGTTTMTSTTTTTTNYSNENILNTSSNSLIALFTRSNSNSNLSNNYQKPLVNQKYIDYNDFERECKLSHLAQEEIQGATEFLHNMGIILHYDTPILRSLVVLDPQWLADVMSSLITFSHNWIKNGILNHSELVSIWSGKYDQSIWPSLLKLLEKFEVSYELPNEFPSRSLIPSLLPEEPIDRIQEIKEKLWIPLPEAIESKRVQIFGCQYNFDFMPLGFFPRLLLRILLIKGIDIKTYWANGILLDILTTEDIKIQKLNHKKHSILPNNSSSTSSSTSSSTSSSTSSSSSSSTSSSSTSTTTTTVQIQSSPFGNSTTIVNKLTNIDNNNNNNNNNNNNNNNNNNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNIKNIINNFENQNNLNNIITNNFGGKFEIIKKNDFESPLSSKKPKHQVLVTFKNQKSFESKDKDTYKLNVEIRSFNVSNNNDKDFLASLFFQQLLSTIDTLLSGSYGGLKVTRLIPCIHCIEKDPHSEPHLFDINSCISQLLLGKSQLVCGKDSTTPVRIDYIAPDLSIKKIPILLEDQVVCEEQIGVGGFGLVHKGKLILQDKSLVVAIKSYIVGNSSASDIIRKFQEFHHEMYIMSSLNHLNIVKLFGSMQNPPRMVMEFAPHGDLYHFLEKKKNIKWSFKVRLMLDIAKGIEYLQNQNPPIVHRDLRSPNIFLFSLDENAPVCAKVADFGLSQQSLYSVSGLLGNFQWMAPETIGAEESYTEKIDTYSFSMILFTILTGECPFDEFTSFGKMEFIRKIREEDLRPTIPSDCPPTISNLIELCWSGDPKKRPHFSYIVKELTNFYYNLNLSPIPEQKSINDKSPHPDLISNGVPKLQIAK
Protein: Uncharacterized protein (Q383X9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVSANKSTMPLSQGCAAAAGIPLEYFETRDHINHLISLGMPRVTPHTVPPKERVATLPVPPQQDHTELMLTISSGGSPQKSYFSTTESHLLTCGTLTPKTARKRPEIDSFDMEGAFAALVKRLESRVDEEDNKDMAS
Protein: Leucine-rich repeat-containing protein (Q553C7)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Latrophilin receptor-like protein A
- Small nuclear ribonucleoprotein E
- C2H2-type zinc finger-containing protein
- Small nuclear ribonucleoprotein Sm D3
- Probable small nuclear ribonucleoprotein Sm D2
- Probable small nuclear ribonucleoprotein G
- Pre-mRNA-splicing factor SYF1
- RNA-binding region RNP-1 domain-containing protein
- Protein BUD31 homolog
- Small nuclear ribonucleoprotein F
Sequence:
MSSATKLTPDNISFKIGKKIDINSIEELELSSLGFIDATSSFSRLKCLKKLDLSSNRFQLIRNIKGLFDLPVIEDLNLTGNPVTKQNNYRLIVIQNLPTLLILDEKKITATERNQAREFDSNQVAKDPLKKNVDSEEEEEEQEQKEQKEEKVEKVIEKKQQTVKHDESVEEVSKKLDEDLLFGTKSNQKKKLIFEDDEEISLDSVDLSKLEKKPVEKPTKKSILFQSDDEDDDLFKSTDNKTKTKKPINLDDDDLFGDNSGKDSKLSSDFDISSYINSQKSRAKSSLFDD
Protein: Aspartyl aminopeptidase (EC 3.4.11.21) (Q19087)
Organism: Caenorhabditis elegans
Function: Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Plays a role in membrane trafficking and is specifically involved in the recycling and degradation of endocytic cargo.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23427264}. Note=Diffuse expression in the cytosol. {ECO:0000269|PubMed:23427264}.
Interaction partners:
- Autophagy-related protein 9
- CDC50 family protein chat-1
Sequence:
MAAALKPSAPEIRKAAQEFINYLNKAVTPFHATQEVKDRLLQAGFTELPESGHWDIQPTSKYFVTKNRSAILAFAVGGSYKPGSGFSIVVGHTDSPCLRVKPISHQKSDKFLQVGVSTYGGGIWRTWFDRDLSVAGLVIVKNGEKLQHKLIDVKKPVLFIPNLAIHLETDRTTFKPNTETELRPILETFAAAGINAPQKPESTGFADPRNITNNHHPQFLGLIAKEAGCQPEDIVDLDLYLYDTNKAAIVGMEDEFISGARLDNQVGTYTAISGLLESLTGESFKNDPQIRIAACFDNEEVGSDSAMGASSSFTEFVLRRLSAGGSTTAFEEAIGKSMLISADQAHATHPNYSAKHEENHRPAFHGGVVVKVNVNQRYATTSTTHAALKQVAFEAQVPLQVVVVRNDSPCGSTVGPILATKLGLQTVDVGCPQLAMHSIREFADTSSIYQATTLYSTFYERLSTVLSNMQ
Protein: Farnesyl pyrophosphate synthetase, putative (EC 2.5.1.-) (Q38EX7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- squalene synthase
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Farnesyl pyrophosphate synthase
- Cis-prenyltransferase-like protein
Sequence:
MHRANIILRTAVTAANANAVLTGEGRPFSMVTREVKAMQNHISSLVANKENEVLDYAGKYVLSSGGKLLRPTLVAMMAHALVPPHMSQQFQASDIGSLDDIPSGTIRPFLRLGEVTELIHTAALVHDDVIDDSEMRRGKPALHCVHDVKRAVLAGDFLLARASLWIASLCVPRIVVLMTTALEDLTRGEMMQMEGCFDLERYEEKTYCKTGSLIANSLAATAVLADPSNSAHEVAAGEYGRRLGIAFQIVDDCLDITGDEKNLGKRTMVDMKAGIATLPTLLAARQDSKVDAAVRRRFKEPGDAEICVEAIERHGCVMEALQHADQHCRRGIAALRTLHESPARERLEAAMNLLLTREL
Protein: T-lymphocyte surface antigen Ly-9 (Cell surface molecule Ly-9) (Lymphocyte antigen 9) (SLAM family member 3) (SLAMF3) (Signaling lymphocytic activation molecule 3) (CD antigen CD229) (Q01965)
Organism: Mus musculus (Mouse)
Function: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. May participate in adhesion reactions between T lymphocytes and accessory cells by homophilic interaction. Promotes T-cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A. Promotes recruitment of RORC to the IL-17 promoter (By similarity). May be involved in the maintenance of peripheral cell tolerance by serving as a negative regulator of the immune response. May disable autoantibody responses and inhibit IFN-gamma secretion by CD4(+) T-cells. May negatively regulate the size of thymic innate CD8(+) T-cells and the development of invariant natural killer T (iNKT) cells. Can promote natural killer (NK) cell activation.
Subcellular location: Membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000305}.
Interaction partners:
- SH2 domain-containing protein 1A
- SH2 domain-containing protein 1B
- CD48 antigen
- Natural killer cell receptor 2B4
Sequence:
MADLKRYWCDWALGPLSENPRMSQQQIFSPILWIPLLFLLMGLGASGKETPPTVISGMLGGSVTFSLNISKDAEIEHIIWNCPPKALALVFYKKDITILDKGYNGRLKVSEDGYSLYMSNLTKSDSGSYHAQINQKNVILTTNKEFTLHIYEKLQKPQIIVESVTPSDTDSCTFTLICTVKGTKDSVQYSWTREDTHLNTYDGSHTLRVSQSVCDPDLPYTCKAWNPVSQNSSQPVRIWQFCTGASRRKTAAGKTVVGILGEPVTLPLEFRATRATKNVVWVFNTSVISQERRGAATADSRRKPKGSEERRVRTSDQDQSLKISQLKMEDAGPYHAYVCSEASRDPSVRHFTLLVYKRLEKPSVTKSPVHMMNGICEVVLTCSVDGGGNNVTYTWMPLQNKAVMSQGKSHLNVSWESGEHLPNFTCTAHNPVSNSSSQFSSGTICSGPERNKRFWLLLLLVLLLLMLIGGYFILRKKKQCSSLATRYRQAEVPAEIPETPTGHGQFSVLSQRYEKLDMSAKTTRHQPTPTSDTSSESSATTEEDDEKTRMHSTANSRNQVYDLVTHQDIAHALAYEGQVEYEAITPYDKVDGSMDEEDMAYIQVSLNVQGETPLPQKKEDSNTIYCSVQKPKKTAQTPQQDAESPETPTYENFT
Protein: Large ribosomal subunit protein eL19 (60S ribosomal protein L19) (Q6P5L3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P84098}.
Interaction partners:
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein eL24
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein uS9
- Ribosomal protein L15
- Large ribosomal subunit protein P1
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MSMLRLQKRLASSVLRCGKKKVWLDPNETNEIANANSRQQIRKLVKDGLIIKKPVTVHSRARCRKNTLARRKGRHMGVGKRKGTANARMPEKLCWMRRMRILRRLLRRYREAKKIDRHMYHSLYLRAKGNVFKNKRILMEHIHKLKADKARKKLLADQAEARRTKTREARKRREERQQAKKEEIIKTLSKEDETKK
Protein: Glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase) (N-myristoyltransferase) (Q8ILW6)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Myristoylates adenylate kinase AK2 (By similarity). During the asexual blood stage, may myristoylate proteins such as ARO, CDPK1 and GAP45. Probably by mediating protein myristoylation, plays a role in the assembly of the inner membrane complex during the early stages of schizogony and in the formation of rhoptries in the late stages and thus merozoite egress.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P30419}.
Interaction partners:
- ADP-ribosylation factor 1
Sequence:
MNDDKKDFVGRDLYQLIRNAKDKIKIDYKFWYTQPVPKINDEFDENVNEPFISDNKVEDVRKEEYKLPSGYAWCVCDITKENDRSDIYNLLTDNYVEDDDNVFRFNYSSEFLLWALSSPNYVKNWHIGVKYESTNKLVGFISAIPIDMCVNKNIIKMAEVNFLCVHKSLRSKRLAPVLIKEITRRINLESIWQAIYTAGVYLPKPISTARYFHRSINVKKLIEIGFSCLNTRLTMSRAIKLYRIDDTLNIKNLRLMKKKDIDGLQKLLNEHLKQYNLHAIFSKEDVAHWFTPIDQVIYTYVNEENGEIKDLISFYSLPSKVLGNNKYNILNAAFSFYNITTTTTFKNLIQDAICLAKRNNFDVFNALEVMDNYSVFQDLKFGEGDGSLKYYLYNWKCASCHPSKIGIVLL
Protein: Cystatin E/M (A0A494BAF5)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MERPHFPLAMGLGLLAFCLLTLSPDARAELRSRRTGERQNLSPTDPRVQKAAQAAVASYNMGSDSLYYFRDTKVIDAKYQSSRRQELSSFLPSLGLCSHTEVPASTPAGGWHQVLPDFGHRKHRVPKDQSLWRTHG
Protein: histidine kinase (EC 2.7.13.3) (Q93IG6)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- DUF742 domain-containing protein
- Serine protease inhibitor Rv3364c
- Probable ATP/GTP-binding protein
- Pentapeptide repeat protein MfpA
- Multifunctional 2-oxoglutarate metabolism enzyme
- 3-methyl-2-oxobutanoate dehydrogenase subunit beta
- Uncharacterized protein Rv1734c
- Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Ribose-phosphate pyrophosphokinase
Sequence:
MTMFARPTIPVAAAASDISAPAQPARGKPQQRPPSWSPRNWPVRWKVFTIALLPLVVAMVLAGLRVEAAMASTSGLRLVAARAEMIPAITKYMSALDVAVLASSTGHDVEGAQKNFTARKYELQTRLADTDVIADVRSGVNTLLNGGQALLDKVLADSIGLRDRVTAYAPLLLTAQNVIDASVRVDSEQIRTQVQGLSRAVGARGQMTMQEILVTRGADLAEPQLRSAMVTLAGTEPSTLFGMSAALGAGSPDTKNLQQQMVTRMAIMSDPAVALVNNPELLHSIQITRDIAEQVITDTTEAVTKSVQSQATDRRDAAIRDAVLVLAAIATAIVVVLVVARTLVGPMRVLRDGALKVAHTDLDGEIAAVRAGDEPIPEPLAVYTTEEIGQVAHAVDELHTRALLLAGEETRLRLLVNEMFETMSRRSRSLVDQQLSVIDQLERNEEDPARLDSLFRLDHLAARLRRNSANLLVLAGAQITRDHREPVPLSTVISAAVSEVEDYRRVDIARVPDCAVVGAAAGGVIHLLAELIDNALRYSSPTTPVRVAAAIGSEGSVLLRISDSGLGMTDADRRMANMRLRAGGEVTPDSARHMGLFVVGRLAGRHGIRVGLRGPVTGEQGTGTTAEVYLPLAVLEGTAPAQPPKPRVFAIKPPCPEPAAADPTDVPAAIGPLPPVTLLPRRTPGSSGIADVPAQPMQQRRRELKTPWWEDRFQQEPKQPPAPEPRPAPPPAKPAPPAGPVDDDVIYRRMLSEMVGDPHELAHSPDLDWKSVWDHGWSAAAEAADKPVQSRTDYGLPVREPGARLVPGAAVPEGPDREHPGAALASNGGLHPGRAPRHAAAVRDPDAVRASISSHFGGVRTGRSHARESSQGPNQQ
Protein: SD06708p (Q8MQW7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
NDHPEKYDQLVFMSIIHLIETVSDLKYQHFLSVLDVYINESFSFTLAYTKLMDVLQKNISEAISPKEKSADGNDLEESPEVRRLYKTTRYLHYVMKFVIRSRVLYAEMNCNTDYMDFATRLQELLRMFIDMIGCPSNLLKSEGALLKNLHIIATDLMQVFEHVRLSISIVEILEKFPPRRLTQSKMGCIKDFVETKLFTLPKCRAILLPVFCKHIKDHLESKEEIAECINIMNNILKLLFRSDVGSTHNDIRDIMIILFRTVMKAAHALDRDTGLVGKFFAIMLGILQRMDAQHYEYFVKDLHQSGELKHFVIEILLVFEELVSPHQKAVFPRDWMDMIMHQNTVILGALKHLTVVITDYFLCPFEKQIWSNFFQCSIAFLVQSPLQLNDFNDNKRQIVFARYRDIRKDTAMEIRKMWFQLGQHKPKFVPQLVEPILEMSMIPEKELRQETIPIFFDMMQCEYYSSRLEHESYGDTKFNNAHHKGNFSDFKTAMIEKLDILIGAGKGDAEYKHLFETIMLERCAAHNTLNVDGTAFVQMVTRLMDKLLEYRFIIQDESKENRMACTFSLLQFYSEVDLKEMYIRYVNKLCALHMEFENYTEAAFTLKLHTELLRWTDTELSHQLRSYRHNNCRTHRQLKEALYFEIMEYFDKGKQWECAIDMCRVLARQYEEEIFDYLKLAELLNRMALFYEKIIKELRHNSEYFRVCFYGRGFPRFLQNRVYIFRGKEYERHSDFCARMLVQHPQAELMQTLEAPGDDITNSDGQYIQVNKVEPIMGQAFNKFNDKIINNEIVKYFTANNVQKFQFSRPFRDSTNGGDRDDVRNLWLERTELRISYPLPGILRWFPVVETNTFKISPLERAVEIMKDTNRDIRQLVILHKSDETLHINPLSMKLNGIVDPAVMGGFAKYEEAFLTDDYLEQNPDDKELVEELKELIANQIPLLDLAIQLHRLRAPDSLKALQEHLERCFADMQQHVEQRYGRKSCDLKIERDSVVMRRPNSFLPSLFDGSNNRHSETSMGSSDSGLSKSTFLPRPQTNSIKNPFSGLSFNTRPSLGHSPSIKSNKSKDKTPSKRRTKDGKVKEREAHSLSSSQWYTPPLSTITSTPEKEINTSIASLASTSNSSLSGPKTPDPHVLTEELTPKRPLRSEMEKERRLSRPASIATPTASIKNFPDTRSLSESSNRNSVETTDSTSEEDIRPPPLPAKARDSTDFTSLSQNMDWTPNGYAMLSTISNTSSMSTTSTLTKTSITNTTYEYLETTNFSLVGAIDGNKPRPPTPPPKPSRHSKHIP
Protein: Cysteine desulfurase CsdA (EC 2.8.1.7) (Cysteine sulfinate desulfinase) (CSD) (EC 3.13.1.-) (Selenocysteine lyase) (EC 4.4.1.16) (Q46925)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine, and transiently retains the released sulfur atom on a cysteine residue, in the form of a persulfide. Can also desulfinate L-cysteine sulfinate (3-sulfino-L-alanine), which is the best substrate of the enzyme. Functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. Seems to participate in Fe/S biogenesis by recruiting the SufBCD-SufE proteins. Transfers sulfur to CsdE that increases the cysteine desulfurase activity of CsdA. Can also transfer sulfur directly to TcdA/CsdL in vitro. Appears to support the function of TcdA in the generation of cyclic threonylcarbamoyladenosine at position 37 (ct(6)A37) in tRNAs that read codons beginning with adenine.
Interaction partners:
- Sulfur acceptor protein CsdE
- Cysteine desulfuration protein SufE
- Iron-sulfur cluster assembly scaffold protein IscU
- Probable ATP-dependent transporter SufC
- Iron-sulfur cluster assembly protein SufB
- Iron-sulfur cluster assembly protein SufD
- tRNA threonylcarbamoyladenosine dehydratase
- Sulfur carrier protein TusA
Sequence:
MNVFNPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTIVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWLGGGKMVHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQDSSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALELLVD
Protein: Krml2.2 protein (V-maf avian musculoaponeurotic fibrosarcoma oncogene homolog Bb) (Q6P5N3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Protein c-Fos
Sequence:
MSAEQHGLLDLAKNQLNLDYGDFDMRFDVKKEAAALGPERSFIQQCGVHVPGSVSSTPMSTPCSSVPSSPSFSPSGQRTEDLYWTLSSTGAYPQHADPHCLELTHDDVREALSSNLMHAHPPQLHQAEMEGYRSIGQFAPPGMQQYHHHQQQQQYTDLHNPEFAHGKSVEQLMQQLDCSPQGAAHLKPLQQTHHRRSERAESRFSDQQLVSMSVRELNRHLRGMSKDDIIRLKQKRRTLKNRGYAQSCRHKRVQQKHLLEHEKTSLATQVEQLKHELGRLVRERDAYKLKCERLVVGMSCQSNNGPSCENPSSPEYLR
Protein: Uncharacterized protein C11E3.10 (O13689)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MMLPSYLHFAIRKKVLAIFIVLLIISAYLGFAPALPVPINDKVCHFFVFFLLTLVFYWVFDLSRRRATQLTILVCGVFGGLGSEFVQSFLTYRTFDLFDIVANLLGCSLALLLNILYHKRRLEKIRLQRYGHVPTIADDLEMQASAAEEEEEGEEDVSKSTP
Protein: Large ribosomal subunit protein uL23m (39S ribosomal protein L23, mitochondrial) (L23mt) (MRP-L23) (L23 mitochondrial-related protein) (Ribosomal protein L23-like) (Q16540)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL41
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein mL44
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL9m
Sequence:
MARNVVYPLYRLGGPQLRVFRTNFFIQLVRPGVAQPEDTVQFRIPMEMTRVDLRNYLEGIYNVPVAAVRTRVQHGSNKRRDHRNVRIKKPDYKVAYVQLAHGQTFTFPDLFPEKDESPEGSAADDLYSMLEEERQQRQSSDPRRGGVPSWFGL
Protein: Synaptotagmin A (F4IFM6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGFFSTILGFCGFGVGISLGLVIGYVLFVYLLPNDVKDPEIRSIADQDPKAMLRMLPEIPLWVKNPDFDRVDWINRFLEYMWPYLDKAICKTAKNIAKPIIEEQIPKYKIDSVEFETLTLGSLPPTFQGMKVYLTDEKELIMEPCLKWAANPNILVAIKAFGLKATVQVVDLQVFAQPRITLKPLVPSFPCFANIYVSLMEKPHVDFGLKLGGADLMSIPGLYRFVQVDIFLLHTSFKSLTCMSKNFFMRERADETVTFRLANTYEQIKDQVANMYLWPKTLVVPILDPAKAFRRPVGIVHVKVVRAVGLRKKDLMGGADPFVKIKLSEDKIPSKKTTVKHKNLNPEWNEEFKFSVRDPQTQVLEFSVYDWEQVGNPEKMGMNVLALKEMVPDEHKAFTLELRKTLDGGEDGQPPDKYRGKLEVELLYKPFTEEEMPKGFEETQAVQKAPEGTPAAGGMLVVIVHSAEDVEGKHHTNPYVRIYFKGEERKTKHVKKNRDPRWNEEFTFMLEEPPVREKLHVEVLSTSSRIGLLHPKETLGYVDIPVVDVVNNKRMNQKFHLIDSKNGKIQIELEWRTAS