wanglab/gogpt-training-data huggingface dataset:
Protein: Ankyrin-repeat and fibronectin type III domain-containing 1 (A0A571BF63)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLCLEKLVAVLLKTQRTSDAYKKGPWKSQRYTVSGSRVAYKRLNCDDIWARKKSRRIPMVPGGTYSPMPESQPLEDSPKALPVLGEQSNSDNDINEPVFIWGISDKAAQRKSISAGEGSFRLQQEKQQPLVHRPGRGKGRLRLPHRLPFKDRHFTCSKIIGRRFACFAQRLSYRRKQSQCDLLNESTGHLPATCSSAASKSLSWNYCSKMTQQMQNLHLSQSKKHSAPSSPNAAKRLYRNLSEKLKGSHSSFDEAYFRTRTDRLSLRKTSVNFQGNEAMFEAVEQQDLDAVQLLLYQYTPEELDLNTPNSEGLTPLDIAIMTNNVPIARILLRTGARESPHFVSLESRAMHLNTLVQEAQDRVSELSAQVENEGFTLDNTEKEKQLKAWEWRYRLYRRMKTGFEHARAPEVPANACLMVSSSTSLTVSFQEPLSVNAAVVTRYKVEWSMSKDFSPLAGEIIMDNLQTLRCTITGLTTGQQYFVQVSAYNMKGWGPAQTTTPVCASPSNWKDYDDREPRHKGQSEVLESLLQQVRALHQHYSCRESSKLQTTGRKQSVSRSLKHLFHSSNKFVKTLKRGLYIATIFYYKDNMLVTNEDQIPIVEIDDSHTSSITQDFLWFMKLSCMWEDIRWLRQSVPISMSSSTVLQTRQKMLAATAQLQNLLGTHNLGRLYYEPIKDRHGNILIVTIREVEMLYSFFNGKWMQISKLQSQRKSLSTPEEPTALDILLITIQDILSYHKRSHQRLSPGLYLGYLKLCSSVDQIKVLVTQKLPNILCHVKIRENHNISKEEWEWIQKLSGSESMESVDHNADCPMQLFFYELQMAVAALLKQINIPRHQARNFRLYTQEVLEIGHNVSFLLLLPASDDVCTAPGQNNPYTPHSGFLNLPLQMFELVHFCSYREKFISLYCRLSAVVELDSLNTQQSLREAISDSEVAAAKQRHQQVLDFIQQIDEVWREMRWIMDALQYARYKQPVSGLPITKLIDSSSEQNLKKISSTSSHIDCLPSTSPSPEMHRRKAVSESQPCSDEEGCSEVFLPTDSDYDSSDALSPRDLDLVYLSSHDIAQQALSGLSGSAPDVLQVHDMKASMGPGQDPQGPGQGPDTDHSCVEFLHSLTLTGLAPKNHAKMVAGTRPPLGFLGKRKPGKHQHYGGFSRHHRWLRMHSETQSLSLSEGVYTQHLSQACGLAEDPGEAEGPGPVVDGPRGLPLAHAASLPEERRSCLQDPRRPLQRVYVEPYSDTLAGQDPKLWTSLSPTPAGRSSLPSSTSSEMSPDPTSPVSEILSSML
Protein: FagA protein (G3XD99)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Fumarate hydratase class II 2
- Superoxide dismutase
- Tetratricopeptide repeat protein
- ZIP family metal transporter
- Uncharacterized protein
- Regulatory protein PchR
- Heme-transport protein, PhuT
Sequence:
MSFEAHDPQALDHWYWLGTQIRCALDPDEPRLLDQYLGEARYLAGWEGVAAWPLFEKAYNLLLDTGRDPILPWHWRSLCLDYAYRPLCELQRLTTNGSQRRRLRQLSVRMARQDLAPSMSFDHPQQGNQDD
Protein: Protein kinase PINOID (EC 2.7.11.1) (Protein kinase ABRUPTUS) (O64682)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein kinase involved in the regulation of auxin signaling. Acts as a positive regulator of cellular auxin efflux and regulates organ development by enhancing polar auxin transport. Phosphorylates conserved serine residues in the PIN auxin efflux carriers. Phosphorylation of PIN proteins is required and sufficient for apical-basal PIN polarity that enables directional intercellular auxin fluxes, which mediate differential growth, tissue patterning and organogenesis. Acts in association with PIN1 to control the establishment of bilateral symmetry and promotion of cotyledon outgrowth. Regulates root gravitropism through modulation of PIN2-dependent basipetal auxin transport. Required for polarization of PIN3-dependent auxin transport for hypocotyl gravitropic response. The protein kinase activity of PID is essential for its auxin efflux regulatory function. PID kinase and PP2A phosphatase activities antagonistically regulate phosphorylation of PIN proteins, affecting PIN sorting.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16731587, ECO:0000269|PubMed:17889649, ECO:0000269|PubMed:20040538}. Cell membrane {ECO:0000269|PubMed:33705718}. Note=Targeted to the cell periphery.
Interaction partners:
- Auxin efflux carrier component 1
- Auxin efflux carrier component 2
Sequence:
MLRESDGEMSLGTTNSPISSGTESCSSFSRLSFDAPPSTIPEEESFLSLKPHRSSDFAYAEIRRRKKQGLTFRDFRLMRRIGAGDIGTVYLCRLAGDEEESRSSYFAMKVVDKEALALKKKMHRAEMEKTILKMLDHPFLPTLYAEFEASHFSCIVMEYCSGGDLHSLRHRQPHRRFSLSSARFYAAEVLVALEYLHMLGIIYRDLKPENILVRSDGHIMLSDFDLSLCSDSIAAVESSSSSPENQQLRSPRRFTRLARLFQRVLRSKKVQTLEPTRLFVAEPVTARSGSFVGTHEYVAPEVASGGSHGNAVDWWAFGVFLYEMIYGKTPFVAPTNDVILRNIVKRQLSFPTDSPATMFELHARNLISGLLNKDPTKRLGSRRGAAEVKVHPFFKGLNFALIRTLTPPEIPSSVVKKPMKSATFSGRSSNKPAAFDYF
Protein: Kinetochore protein NDC80 homolog (Kinetochore protein Hec1) (Kinetochore-associated protein 2) (xNdc80) (Q8AWF5)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules. May play a role in chromosome congression and may be essential for the end-on attachment of the kinetochores to spindle microtubules (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12514103}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12514103}. Note=Localizes to kinetochores from late prophase to anaphase. {ECO:0000269|PubMed:12514103}.
Interaction partners:
Sequence:
MRRSSVTNRQSLLPLRVQDANRMGLTTPQNKDRQGFGKLSMSKPHSGTSEKKTSFFGKRASNGTARTSQYGAFGGTEKIKDPRPLHDKAFIQQCIRQLCEFLNENGYSQALTVKSLQGPSTKDFLKIFAFIYTFICPNYENPESKFEEEIPRIFKELGYPFALSKSSMYTVGAPHTWPQIVAALVWLIDCVKLCCVLRSENPVFEDPPMGEQSENGIDFNQLFLDYTVRCYDQFMEGRDTFEEYDTDVCIRLKEAYHVDESNLEALQQESRRLMEEIERLEKEKENEPDRLASMRKLKASLQADIQKYQNYLTEIESHSTLLDQRVSSISEELEATELESRAIQQENLRLKNILDNQKYSVADIERIKYEETELQQTIAKLTKDLDEDKQQLWHEELKYAKMKESVETQLSEFHKIGRKVRLIPPTAEFANGYDFQIQCNLDSEQSSLMHYRNKINVPLVEILSQSEGHIASSTNKKMGVEDMVEQLNTLIGEKKNEVKVQKDEAQKLEEIYQQKVEESEEHEKRWISEIESLEKHRQLLESGVNKSLDEAMKDLQKEQQELQLVEHRTEEEMRQVENKLVRVVHAVANHVAVIEKHLEEKRLKVEREYEEFMKEDLLLDLRELLEKYKEKARVLDSL
Protein: Tehao (Q58SL2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FCLGLSPQCTCAAEGNVVRFHCPDEYAMLLEVSEPGASLYMSYYASTELQWLPRFNISSLVKIEFDAYIFWPEKFLSDLLKTLGVQTVKTIIFRDRTLETVVTRDVLNSGNGYMETSQPENITTWHFGSVPGLKKFKFFSHVPELQESIFHGFDTLRDLQLSVNVTTLPGNMLSTVNGTLKTLTIESPGIVSFGNPLLRELQQLRNLSLALIHPFHERDKQLQQHFFGSMTNLEEVRLASATSSVNRSMFKGTNKLQLIKMNGNDDLMELPGEIFLDQVNLKTLDLSCNAIVTLHEDVFKGLGNLTLLDLSKNRLTNLS
Protein: Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (EC 1.3.5.1) (Iron-sulfur subunit of complex II) (Ip) (P21801)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH1 and SDH2 form the catalytic dimer. Electrons flow from succinate to the FAD bound to SDH1, and sequentially through the iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4.
Subcellular location: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Interaction partners:
- Mitochondrial inner membrane protein SHH4
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Succinate dehydrogenase cytochrome b subunit
- Mitochondrial inner membrane protein SHH3
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Fumarate hydratase, mitochondrial
Sequence:
MLNVLLRRKAFCLVTKKGMATATTAAATHTPRLKTFKVYRWNPDEPSAKPHLQSYQVDLNDCGPMVLDALLKIKDEQDSTLTFRRSCREGICGSCAMNIGGRNTLACICKIDQNESKQLKIYPLPHMFIVKDLVPDLTNFYQQYKSIQPYLQRSSFPKDGTEVLQSIEDRKKLDGLYECILCACCSTSCPSYWWNQEQYLGPAVLMQAYRWLIDSRDQATKTRKAMLNNSMSLYRCHTIMNCTRTCPKGLNPGLAIAEIKKSLAFA
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (A0A140VJS9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MSDSEKLNLDSIIGRLLEGSRVLTPHCAPVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKNKGKYGQFSGLNPGGRPITPPRNSAKAKK
Protein: Verprolin (Q9P6R1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in cytoskeletal organization and cellular growth. May exert its effects on the cytoskeleton directly, or indirectly via proline-binding proteins such as profilin or proteins possessing SH3 domains. Plays a role in actin patch assembly by enhancing the ability of myo1 to stimulate actin polymerization by the Arp2/3 complex.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12939254, ECO:0000269|PubMed:16087707, ECO:0000269|PubMed:16823372}. Note=Localized to patches at the tips of growing interphase cells. These patches form prior to patches of myo1, but in cells lacking myo1, they are less intense and may be short lived. Detected in the medial region of mitotic cells, and this requires cdc15.
Interaction partners:
- Actin-binding protein wsp1
- Myosin-1
- Protein BZZ1
- Actin
- Endocytosis protein end4
- Actin-related protein 2
- Actin cytoskeleton-regulatory complex protein pan1
- Cofilin
- Inositol-1,4,5-trisphosphate 5-phosphatase 2
- Actin cytoskeleton-regulatory complex protein end3
Sequence:
MAPAPPPPPPAPAPAAAAPAPPLMTGDRSALLNSIQKGKKLKKATTNDRSAPVVGGGVVGERKSNTPKSFAAPPVPTGAPSLPTSSNNTQQAEERPSMPALGGLFAGGMPKLRHIGKSSASAAPPSAPAPPTPQSELRPPTSAPPRPSIPPPSPASAPPIPSKAPPIPSSLPPPAQPAAPVKSPPSAPSLPSAVPPMPPKVPPPPLSQAPVANTSSRPSSFAPPAGHAPNVTSESPKFPNRGPSIPSASVPPVPPSSYVLQQRPNRVDDHGRFHFKDDSYLPIPHPFLGVPKVYRGGSGTTVPLNLSSF
Protein: Uncharacterized protein, isoform B (Q5LJQ4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIKNEQRPLNFEKCPESDDELKKRLEIEKLINKNIDKNISFDVLVKLSLAPYGLVNDDFRRILWPQLAGVDINHLGQAPTLDKFQCHPEYNQVVLDVNRSLKRFPPGIPYEQRIALQDQLTVLILRVIQKYPNLRYYQGYHDVAVTFLLVVGEEIAFAIMEQLSTTHFSECMQETMEATQRRLMFIWPIIKFENPELYQFLQNSTVGTLFSLPWYLTWFGHSLTSYRTVVRLYDYFLASPIYTSIFVTAAILLYRSDEILKEDCDMASVHCLLSVVSYSLKY
Protein: A-kinase anchor protein 1, mitochondrial (A-kinase anchor protein 121 kDa) (AKAP 121) (Dual specificity A-kinase-anchoring protein 1) (D-AKAP-1) (Protein kinase A-anchoring protein 1) (PRKA1) (Spermatid A-kinase anchor protein 84) (S-AKAP84) (O88884)
Organism: Rattus norvegicus (Rat)
Function: Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane (By similarity). Involved in mitochondrial-mediated antiviral innate immunity (By similarity). Promotes translocation of NDUFS1 into mitochondria to regulate mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) activity (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:O08715}. Mitochondrion {ECO:0000250|UniProtKB:O08715}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- cAMP-dependent protein kinase type I-alpha regulatory subunit
- cAMP-dependent protein kinase type II-beta regulatory subunit
- Protein kinase cAMP-dependent type I regulatory subunit beta
- A-kinase anchor protein 6
- A-kinase anchor protein 13
- A-kinase anchor protein 10, mitochondrial
- 3',5'-cyclic-AMP phosphodiesterase 4D
Sequence:
MAIQFRSLFPLALPGMLALLGWWWFFSRKKDRLSSNGKQVGTLKVGPAIEDRLPTEEACPGVLSVTPSVTQPPGKEEQRSMDRPLSDPPALPRTRQVRRRSESSGNLPSIVDTRLQAGQCSDENSKVVLSLMGDEAKSIPLGRPLFPKDLSFPYEAVEGCKQESALGRTPGRGWLSQCAASGENARETGGAEGTGDAVLGESVLEEGLLPQECVSEVEKSEFPILAPGGGGGEKVRSGPPQVDELLKKEEYIVGKLPSSFVGPVHSELVKDEGALVPQVKGSQDRSLARELDKDKTLPEKDQIEQTAFQIISQVILEATEEIRATTVGKTVAQVHPTPGTQPQGQEESCVPASQETSLGQEIPDPASTRTGATASPSAGAPPPKTYVSCLSSPLSGPTKDQKPKNSAHHISLAPCPPPVTPQRQSLDGASNPRGDDTFVTCTSNNSQSVLSVTSLGLCSDPVSTSRLEDSCTETISSSGDKAVTPPLPDSTEPFSNGVLKEELSDLGTEDGWTMDTEADHSGGSDGNSMDSVDSCCGLTKPDSPQTVQAGSNPKKVDLIIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQNIQICHIEGSQHHVDKALNLIGKKFKELNLTNIYAPPLPSLALPSLPMTSWLMLPDGITVEVIVVNQVNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVVPLSDDDHFSPEADAAMSEMTGNTALLAQVTSYSATGLPLIQLWSVVGDEVVLINRSLVERGLAQWVDSCYASL
Protein: Sorting nexin-9 (Q91VH2)
Organism: Mus musculus (Mouse)
Function: Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3-phosphate (By similarity).
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Localized at sites of endocytosis at the cell membrane. Detected on newly formed macropinosomes. Transiently recruited to clathrin-coated pits at a late stage of clathrin-coated vesicle formation (By similarity). Colocalizes with the actin cytoskeleton at the cell membrane (By similarity). {ECO:0000250}.
Interaction partners:
- Sorting nexin-18
- Sorting nexin-33
- Dynamin-2
- Actin nucleation-promoting factor WASL
- Disintegrin and metalloproteinase domain-containing protein 15
- Dynamin-1
- Actin nucleation-promoting factor WAS
- Endophilin-A1
- Amphiphysin
- Myc box-dependent-interacting protein 1
Sequence:
MATKARVMYDFAAEPGNNELTVTEGEIITVTNPNVGGGWLEGKNNKGEQGLVPTDYVEILPNDGKDPFSCGNSVADQAFLDSLTASTAQTNSSSANSNNQVGGGNDPWTAWNAPKPGNWDSSDAWGSRTDGTSAQRNSSANNWDTGFGHPQAYQGPATGDDDEWDEDWDDPKSSSPYFKDSEPAEAGGIQRGNSRAGASSMKLPLNKFPGFAKPGMEQYLLAKQLAKPKEKIAIIVGDYGPMWVYPTSTFDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFGSAIPIPSLPDKQVTGRFEEEFIKMRMERLQAWMTRMCRHPVVSESEVFQQFLNFRDEKEWKTGKRKAEKDELVGVMIFSTMEPEAPDLDLIEIEQKCDAVGKFTKAMDDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLAAVFSSSGYQGETDLNDAITEAGKTYEEIASLVAEQPKKDLHFLMECNHEYKGFLGCFPDIIGAHKGAIEKVKESDKLVATSKITPQDKQTMVKRVGTMSYALQAEMNHFHSNRIYDYNSVIRLYLEQQVQFYETIAEKLRQALSRFPVM
Protein: Plasminogen (EC 3.4.21.7) [Cleaved into: Plasmin heavy chain A; Activation peptide; Plasmin heavy chain A, short form; Plasmin light chain B] (P06868)
Organism: Bos taurus (Bovine)
Function: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells (By similarity).
Subcellular location: Secreted {ECO:0000250}. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface (By similarity). {ECO:0000250}.
Interaction partners:
- Histidine-rich glycoprotein
- Alpha-2-antiplasmin
- Alpha-enolase
- Albumin
- Fibrinogen beta chain
- Annexin A2
- Coagulation factor XII
- Complement C3
- Tissue-type plasminogen activator
- Urokinase plasminogen activator surface receptor
Sequence:
MLPASPKMEHKAVVFLLLLFLKSGLGDLLDDYVNTQGASLLSLSRKNLAGRSVEDCAAKCEEETDFVCRAFQYHSKEQQCVVMAENSKNTPVFRMRDVILYEKRIYLLECKTGNGQTYRGTTAETKSGVTCQKWSATSPHVPKFSPEKFPLAGLEENYCRNPDNDENGPWCYTTDPDKRYDYCDIPECEDKCMHCSGENYEGKIAKTMSGRDCQAWDSQSPHAHGYIPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPQKRWEFCDIPRCTTPPPSSGPKYQCLKGTGKNYGGTVAVTESGHTCQRWSEQTPHKHNRTPENFPCKNLEENYCRNPNGEKAPWCYTTNSEVRWEYCTIPSCESSPLSTERMDVPVPPEQTPVPQDCYHGNGQSYRGTSSTTITGRKCQSWSSMTPHRHLKTPENYPNAGLTMNYCRNPDADKSPWCYTTDPRVRWEFCNLKKCSETPEQVPAAPQAPGVENPPEADCMIGTGKSYRGKKATTVAGVPCQEWAAQEPHQHSIFTPETNPQSGLERNYCRNPDGDVNGPWCYTMNPRKPFDYCDVPQCESSFDCGKPKVEPKKCSGRIVGGCVSKPHSWPWQVSLRRSSRHFCGGTLISPKWVLTAAHCLDNILALSFYKVILGAHNEKVREQSVQEIPVSRLFREPSQADIALLKLSRPAIITKEVIPACLPPPNYMVAARTECYITGWGETQGTFGEGLLKEAHLPVIENKVCNRNEYLDGRVKPTELCAGHLIGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSPYVPWIEETMRRN
Protein: Anoctamin transmembrane domain-containing protein (Q55GA1)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- DUF590 family protein
Sequence:
MEESSYDNFNINKFNINLNKVGDDDDNNNNNNIVNNNNIIYPINDINNENKGNTKTGGFLENIKITDQDNSLGEENYDLEINYEVVLVFDKSKKVVSDDPKLTWDIIIKKTMKILKELNLYSVLKVGTLDENHIFIIVGTTDELLRHYCIDNYIQIQKKIVTETTRISESMRLHLVETILINSNDLKYIYDDDFVIDKYPYANKNFETLKRECQKKWFFQSLDINVIKDYFGEEVTFYFLFLRFYNVGLGIVSLFGLAVAIVSYTRDSYKFASSSFSIALAVLSTLFFEIWKRYGSIYSWKWDQEDYIDDEEQLPSFKPGNFSEGVYHKGIFLKSKHFGKKVKYVQKNITTRPYLTSYQQKMKLLKTIGTFSVVVTLVLIVPIFTISIFTLRIALESIENKTVESGIGSVINALFILFFNFIYKNIAYFLTKFESHRVASSFNASYSTKLFLFQFVNSFSGLFYIAFLKNNVYLWGDIDLEDTCSTPNKIDGLWKGCTEDLQFQLFSILAVNFIASIFSELLGPWIQYYIKIIRQKPTGFREKIEPFEQQFYRDTFDTFQEFNQIIIQFSYISMFSAASPISPIISFFHNIFEERVDSYKLINSLRRPNYNGSNGLGSWFFIIVLVGMFSVLTNVLLIGFSFPTLLYFTDSPYNVLWIVFILEHLVILTKVVLAKAIPDETKKLKKKKASLDLITKSIMENDRELSKLLIEKIKSNEIPLTNDINPDSNQNNIIPTPFTSKTRQRALSISSKISKTMHSVINIKHDVDYEDENK
Protein: Immunoglobulin lambda variable 7-43 (Ig lambda chain V region 4A) (P04211)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MAWTPLFLFLLTCCPGSNSQTVVTQEPSLTVSPGGTVTLTCASSTGAVTSGYYPNWFQQKPGQAPRALIYSTSNKHSWTPARFSGSLLGGKAALTLSGVQPEDEAEYYCLLYYGGAQ
Protein: Uncharacterized protein (Q582J9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSSNDIASKIREANRRRAEEGSRIRQLQQERREEMLEREAEKAASKPSGFIPYIIISLIFLSFPLSEPIVDWVLVACFALLNGAWVLFFRSASWVNWGTLALCDFSLIRISHVIPHIPRLIKETPPHVLAAFIGGNLVAMVILYYAYVVRRLPWKTEVGSKKPKRVKRSDGEEVETLEEFARRRERANRIDNMFSGLIVANVVVLVLVGAIPFRTVFDAVRQIIGFFH
Protein: Ribonuclease H2 subunit B (Ribonuclease HI subunit B) (A0A2R8Y6Q6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGLSSCYCPEYLKDASKKMKNGLMFVKLVNPCSGEGAIYLFNMCLQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEKGNPEIDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVSSRVQSTAFFSGDQASTDKEEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKKIKLSDEPVEAKEDYTKFNTKDLKTEKKNSKMTAAQKALAKVDKSGMKSIDTFFGVKNKKKIGKV
Protein: MADS-box protein, GDEF2 (Q9ZS27)
Organism: Gerbera hybrida (Daisy)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MARGKIQIKKIENSTNRQVTYSKRRNGLFKKASELTVLCDAKVSIIMVSCTDKLHEYISPSITTKQFFDQYQKASGIDLWNSHYEKMQEELRQLKEVNRNLRRQIRQRLGDCLEDLGFEEFLDLEKESQEAVYIIRERKLKVIGNKLETSKKKVRSAQDVYKKLMHEFDIRGEDPQYGMIEDGVEYEALYGYPPHISAPRILTLRLQPNHPDNLHAAASDLTTYALLG
Protein: Transcriptional regulator of RNA polII, SAGA, subunit (Q58G10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQRSQDQRISLCELKEHIVKKTGVERSRRYFYYLGRFLSQKLTKSEFDKTCLRLLGRENLSLHNQLIRSILRNATVAKSPPPDHEAGHSTKANAFQSRGDGLEQSGTLIPNHSQHEPVWSNGVLPISPRKVRSGMQNRKSRDRPSPLGSNGKVEHMLHQPVCREDNRGSVGMENGDYQRSGRYVADEKDGEFLRPVEKPRIPNKEKIAAVSMRDDQNQEEQARVNLSMSPLIAPLGIPFCSASVGGSPRTIPVSTNAELISCYDSGGLPDIEMLRKRMENIAVAQGLEGVSMECAKTLNNMLDVYLKKLINSCFDLVGARSTNGDPGKQRIGKQQSQNKIVNGVWPTNSLKIQTPNGSSDIRQDHHSVSMLDFRTAMELNPRQLGEDWPTLRERISLRSFEEQDFEV
Protein: GM01778p (Q86NW6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MATLLLYYSTIPERSSCPFTTPATPGTTATINGHKSTEQQQQQQQQQHQQQQQQKQQPAQQTFTILIAIEKSQHLCVIDLICQSLRLLAKQIGNCEILAVCPDSSLLQLCNGQQQQKLQQQQQQNNNSDHPEPSSPSPVDLVKFISVDQVTTSVAPSQLPAGLLPSVPALSTLPGISQRHHDATKWREFFAQLEAFQRQCSTAGGRLVSALSEIRAADLQGLPTRRQLYGQHRALSRALMDSQLHSLRKMGAGQLARLQDLARAITSAPGSPRMTSQPQSSSSSSSGAFLNVDAACKLRKVTLLFNEVDRAAQRLEQLTEQRRERLRQLTRQRALEDEISEVTSWLGSDGAENLQKFSQLHWDNESQLRTQEQEFEKYYFIAMKHLAKGRDLHAAALKVSVLSESANNLKSALDQFAQKLELAHERYEAAGRLLHLLTQHQRENAAREELQRLAEQLGATSLLEKHWPVMRKTHTLPVASSTPAAAAGKRVSYRCSSASGSSFEGGPSSSNCSCWRESRNLEDMDQMEEEEEERDHDCDGGDGEEQQSKIADSGVGVCDNCERNPKLARICSCQSLNEKSHDELLEDECFDRPSKRYMDIMHSPMEANAHLQCHGSSLELPKLEELSCLDPKIQKTLLLIMREMIGTERDYVRSLYYVIENYIDELLREDIPQPLRGQRNVIFGNIEKIFEFHNSHFLGELERYERNPLKVGAAFLEMESKFYLYALYNKNKPKSDTLLSEYGSSFFKPKQMQLQDKLDLASYLLKPVQRMGKYALLLQQLVKACKGVEGAALQEIAADVEELQRAEEMVKFQLRHGNDLLAMDSLRDCDVNVKEQGRLLRQNEFLVWQGRGGKKTLRQVFLFEELVLFSKARRFPDHKNLDIYIYKNSIKTSDIGLTAHTGDSATKFEIWFRKRKPDDTWMLQCMSEDIKNAWTEEISKLLWKQAKRNREVRLAEMSSMGIGSKPCLDIRPSNNQISDRSIPLAQLNKTPKLRHSEPGKGSMRRPNSLISESSLSSGTSTTSGSSISGGSSSGHNDGGGRHSLHFGKLPGAHSASSTNCSATLELINETQALKLAKSPSGGGIKGADTAADGGNTSGNGNGNGNAFRSSKRNHKRSTTIVSQLSMESGIVSDMCVTPDQEQSAAESSRSSWSTSTTGASGASTTSASTVILRRYRSYAHAAESASPESGK
Protein: Nuclear cap-binding protein subunit 2 (20 kDa nuclear cap-binding protein) (Q585L4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364036}.
Interaction partners:
- RRM domain-containing protein
- Sm protein F
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D2
- Sm protein G
- Splicing factor 3A, putative
- Uncharacterized protein
- Spliceosome-associated protein, putative
- Small nuclear ribonucleoprotein SmD1
- Sm protein B
Sequence:
MAEYLIDLTPRMAYVDRHELLRSLLTEKEFIERRQEQLNKSTTVYVGNLSFYTTEDQIWEHFSRCGHIRDLVMGLSEVTRTPCGFCFVVFESQDGAMSAVIDLHGTLLDDRVITVSWDVGCDHTRRWGRGAHGGQVVDGVRQNLDSARGGLGVLRREELGVGAAVAEDQLVHYTWIPPRRVEKRGRS