wanglab/gogpt-training-data huggingface dataset:
Protein: Dahlein-5.1 (P84267)
Organism: Ranoidea dahlii (Dahl's aquatic frog) (Litoria dahlii)
Function: Has no antimicrobial activity. Strongly inhibits the formation of NO by neuronal nitric oxide synthase at micromolar concentrations. Acts by a non-competitive mechanism, probably by binding to calcium/calmodulin and as a consequence blocking calmodulin attachment to nNOS (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:11555873}.
Interaction partners:
Sequence:
GLLGSIGNAIGAFIANKLKP
Protein: Caffeine resistance protein 5 (O94528)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Brefeldin A resistance protein
- AP-1-like transcription factor
- Thioredoxin reductase
- Leptomycin B resistance protein pmd1
- Uncharacterized transcriptional regulatory protein C530.05
Sequence:
MGFLRETVFGELVEYVSHNSNDNDLEKLRVWKDISKVDSNDSCSSESGDLKIHEVNSEGHIIVRWDDANDPENPLNWPLWAKLVVTFDICFLTFAVYVGSAIFTPGISEMQETMHVGTVPVVLGLTLFVLGYAIGPLILSPLSEIPQVGRQKIYVLSLLVFVCLQIPTALGSSLGVLLPMRFLAGFFGSPALATGGATLADIWQPWLLPYFMCFWAIGAIGGPVLGPLLGGAMVVAESWRWQFWLLMMISGFALIVIFFFMPETSEWHILYKRAKRFRKITGNENYRTEAELASSHLSVAQLAKETIIRPIILSISEPIVLSLNIYIGLIYSILYLWFEAFPILFTSVYHFTIIENGLVYLGILVGALITLACYFVFLYKVMIPAFMASGGDFAPEGVLVISFPATFFIPICLFWFGWSGRESVHWIVPIVSTLFYASGAFLMFQSMFQYLAASYPKYVASVFAGNDLFRSAMAASFPLFARAMFNNTGPSYAPVAWGSTILGIVACLMIPIPFVLHKWGLKLRSRSKYAS
Protein: Aminoaldehyde dehydrogenase 1b (ZmAMADH1b) (EC 1.2.1.-) (4-trimethylammoniobutyraldehyde dehydrogenase AMADH1b) (EC 1.2.1.47) (Aminobutyraldehyde dehydrogenase AMADH1b) (EC 1.2.1.19) (Betaine aldehyde dehydrogenase AMADH1b) (EC 1.2.1.8) (Gamma-guanidinobutyraldehyde dehydrogenase AMADH1b) (EC 1.2.1.54) (G5DDC2)
Organism: Zea mays (Maize)
Function: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes. Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively. Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively. Catalyzes the oxidation of betaine aldehyde to glycine betaine.
Interaction partners:
Sequence:
MMASQAMVPLRQLFVDGEWRPPAQGRRLPVVNPTTEAHIGEIPAGTAEDVDAAVAAARAALKRNRGRDWARAPGAVRAKYLRAIAAKVIERKQELAKLEALDCGKPYDEAAWDMDDVAGCFEYFADQAEALDKRQNSPVSLPMETFKCHLRREPIGVVGLITPWNYPLLMATWKVAPALAAGCAAVLKPSELASVTCLELADICKEVGLPPGVLNIVTGLGPDAGAPLSAHPDVDKVAFTGSFETGKKIMAAAAPMVKPVTLELGGKSPIVVFDDVDIDKAVEWTLFGCFWTNGQICSATSRLLVHTKIAKEFNEKMVAWAKNIKVSDPLEEGCRLGPVVSEGQYEKIKKFILNAKSEGATILTGGVRPAHLEKGFFIEPTIITDITTSMEIWREEVFGPVLCVKEFSTEDEAIELANDTQYGLAGAVISGDRERCQRLSEEIDAGIIWVNCSQPCFCQAPWGGNKRSGFGRELGEGGIDNYLSVKQVTEYISDEPWGWYRSPSKL
Protein: Abelson interacting protein, isoform D (A0A0B4K774)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- FI14118p
- Wiskott-Aldrich syndrome protein family member
- Cytoplasmic FMR1-interacting protein
- Membrane-associated protein Hem
- Tyrosine-protein kinase Abl
- RE12101p
- Insulin receptor substrate 53 kDa, isoform A
- Wiskott-Aldrich syndrome protein family member
- LD06925p
- Cdc42 homolog
Sequence:
MLTETPMASENIMDELASLIRTEIPDGRQSLRDSYTNLERVADYCEDTYYRADNKKAALEATKNYTTQSLASVAYQINTLAYSYMQLLELQAQQLGEMESQMNHIAQTVHIHKEKVARREIGVLTANKVSSRQFKIVAPINPEKPIKYVRKPIDYSMLDEIGHGINSAQHSQVRQKHRGSSHGSVQSLLPPSVGPPPTTKPPTPPQMSRAGNTGTLGKSVSNTGTLGKSSREYRTPPVVNPPQVPSHYAPNYPIGHPKRMSTASSTMTTTTTGGGAAGNERAAGYSALPMPPSQQIATHVNLPSAGMMQSLPPPPPTTYDDRSSMPPAPPSPLTVSQHEMTEQSHIGMHTLGRNINRNPNRNHFSLNFARPGSQSPPLPPPPPPEDEHQDFGRPRTSTGPQLAPIVPEDQNLPGWVPKNFIEKVVAIYDYYADKDDELSFQESSVLYVLKKNDDGWWEGVMDGVTGLFPGNYVEPCV
Protein: Uncharacterized protein Rv2240c (P9WLG7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein Rv2239c
- Alkyl hydroperoxide reductase E
- Anti-sigma-F factor antagonist RsfB
- GTPase Obg
- Uncharacterized SURF1-like protein Rv2235
- Conserved protein
- Pyruvate dehydrogenase E1 component
- Anti-sigma-F factor antagonist RsfA
Sequence:
MLIGWRAVPRRHGGELPRRGALALGCIALLLMGIVGCTTVTDGTAMPDTNVAPAYRSSVSASVSASAATSSIRESQRQQSLTTKAIRTSCDALAATSKDAIDKVNAYVAAFNQGRNTGPTEGPAIDALNNSASTVSGSLSAALSAQLGDALNAYVDAARAVANAIGAHASTAEFNRRVDRLNDTKTKALTMCVAAF
Protein: Cell wall mannoprotein CIS3 (Covalently-linked cell wall protein 5/11) (Protein with internal repeats 4) (Soluble cell wall protein 8) (P47001)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the outer cell wall layer. Required for stability of the cell wall and for optimal growth. Required for resistance against several antifungal and cell wall-perturbing agents.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:10438739, ECO:0000269|PubMed:12898712, ECO:0000269|PubMed:15781460, ECO:0000269|PubMed:9301021, ECO:0000269|PubMed:9748433}. Note=Covalently attached to the cell wall. Localizes predominantly on the surface of growing buds.
Interaction partners:
- Probable family 17 glucosidase SCW4
- Probable family 17 glucosidase SCW10
- Cell wall mannoprotein PIR3
Sequence:
MQFKNVALAASVAALSATASAEGYTPGEPWSTLTPTGSISCGAAEYTTTFGIAVQAITSSKAKRDVISQIGDGQVQATSAATAQATDSQAQATTTATPTSSEKISSSASKTSTNATSSSCATPSLKDSSCKNSGTLELTLKDGVLTDAKGRIGSIVANRQFQFDGPPPQAGAIYAAGWSITEDGYLALGDSDVFYQCLSGNFYNLYDQNVAEQCSAIHLEAVSLVDC
Protein: Pulmonary surfactant-associated protein B (SP-B) (18 kDa pulmonary-surfactant protein) (6 kDa protein) (Pulmonary surfactant-associated proteolipid SPL(Phe)) (P07988)
Organism: Homo sapiens (Human)
Function: Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter.
Subcellular location: Secreted, extracellular space, surface film.
Interaction partners:
- Surfactant protein C
- Pulmonary surfactant-associated protein A1
- Pulmonary surfactant-associated protein D
- Surfactant protein A2
- Phospholipid-transporting ATPase ABCA3
- Homeobox protein Nkx-2.1
- Uteroglobin
- Granulocyte-macrophage colony-stimulating factor receptor subunit alpha
- Thyroid transcription factor 1-associated protein 26
- Advanced glycosylation end product-specific receptor
Sequence:
MAESHLLQWLLLLLPTLCGPGTAAWTTSSLACAQGPEFWCQSLEQALQCRALGHCLQEVWGHVGADDLCQECEDIVHILNKMAKEAIFQDTMRKFLEQECNVLPLKLLMPQCNQVLDDYFPLVIDYFQNQTDSNGICMHLGLCKSRQPEPEQEPGMSDPLPKPLRDPLPDPLLDKLVLPVLPGALQARPGPHTQDLSEQQFPIPLPYCWLCRALIKRIQAMIPKGALAVAVAQVCRVVPLVAGGICQCLAERYSVILLDTLLGRMLPQLVCRLVLRCSMDDSAGPRSPTGEWLPRDSECHLCMSVTTQAGNSSEQAIPQAMLQACVGSWLDREKCKQFVEQHTPQLLTLVPRGWDAHTTCQALGVCGTMSSPLQCIHSPDL
Protein: CD81 antigen (26 kDa cell surface protein TAPA-1) (Target of the antiproliferative antibody 1) (CD antigen CD81) (P35762)
Organism: Mus musculus (Mouse)
Function: Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling. Essential for trafficking and compartmentalization of CD19 receptor on the cell surface of activated B cells. Upon initial encounter with a microbial pathogen, enables the assembly of CD19-CR2 and B cell receptor complexes at signaling TERMs, lowering the threshold dose of antigen required to trigger B cell clonal expansion and humoral immune response (By similarity). In T cells, associates with CD4 or CD8 coreceptors and defines the maturation state of antigen-induced synapses with B cells (By similarity). Facilitates localization of CD3 in these immune synapses, required for costimulation and sustained activation of T cells, preferentially triggering T helper type 2 immune response. Can act both as positive and negative regulator of homotypic or heterotypic cell-cell fusion processes. In myoblasts, associates with another tetraspanin CD9 in complex with PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD9 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Positively regulates sperm-egg fusion and may be involved in the acrosome reaction. Regulates protein trafficking in intracellular compartments. In T cells, associates with dNTPase SAMHD1 and defines its subcellular location, enabling its degradation by the proteasome and thereby controlling intracellular dNTP levels (By similarity). Also regulates integrin-dependent migration of macrophages, particularly relevant for inflammatory response in the lung.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23213457}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P60033}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with CLDN1 and the CLDN1-CD81 complex localizes to the basolateral cell membrane. {ECO:0000250|UniProtKB:P60033}.
Interaction partners:
- B-lymphocyte antigen CD19
- Complement receptor type 2
- Claudin-1
- Prostaglandin F2 receptor negative regulator
- Interferon-induced transmembrane protein 3
- CD9 antigen
- Tumor susceptibility gene 101 protein
- Immunoglobulin superfamily member 8
- CD63 antigen
- Integrin beta-1
Sequence:
MGVEGCTKCIKYLLFVFNFVFWLAGGVILGVALWLRHDPQTTSLLYLELGNKPAPNTFYVGIYILIAVGAVMMFVGFLGCYGAIQESQCLLGTFFTCLVILFACEVAAGIWGFVNKDQIAKDVKQFYDQALQQAVMDDDANNAKAVVKTFHETLNCCGSNALTTLTTTILRNSLCPSGGNILTPLLQQDCHQKIDELFSGKLYLIGIAAIVVAVIMIFEMILSMVLCCGIRNSSVY
Protein: Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 90 kDa subunit homolog) (eIF3 p90) (Translation initiation factor eIF3 p90 subunit homolog) (spPrt1) (Q10425)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:15904532}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit H
- Probable eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit A
Sequence:
MSEILIEEIKDQIVVKDEEIDVSELEVKLNVTKPVGYDTVVVIEGAPVVEEAKQQDFFRFLSSKVLAKIGKVKENGFYMPFEEKNGKKMSLGLVFADFENVDGADLCVQELDGKQILKNHTFVVRKLNQLEKAFSTPDEFSFEEREFKEREHLRSWLTDYYGRDQFISYYGNRVSVNWNRKSDVPEQIVDRENWTETYVQWSPMGTYLVSLHLRGIQLWGGESWGMCARFLHPYVKFVDFSPNEKYLVSWSYEPVRLPPIGHPARETMPFTDDDEGKHCFVWDIASGRILRSFKIPPQPEGSKDGKKVIWPIFKWSADDKYLARVTVGQSISVYETPSLALVDKKTIKIDGVQNFEWCPVSDALGRDSKEQLLAYWTPEITNQPARVALISIPSKSTIRTKNLFNVSDCKLYWQSNGDYLCVKVDRHTKTKKSTFSNLEIFRIREKNIPVEVVDLKDVVLNFAWEPKSDRFAIISANDQVLNSTNVKTNLSFYGFEQKKNTPSTFRHIITFDKKTCNSLFMAPKGRFMVAATLGSSTQYDLEFYDLDFDTEKKEPDALANVQQIGSAEHFGMTELEWDPSGRYVTTSSTIWRHKLENGYRLCDFRGTLLREEMIGEFKQFIWRPRPPSPLTKEDMKKIRKKLKDYNRLFDEEDIAEQSSANRELAARRRQLISEWQKYRDEVIARVAEERAITGQPAITVPAEEEEIIQETVEEVISEEIEPVED
Protein: Myosin IB heavy chain (P34092)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Myosin IB may have a role in chemotaxis and aggregation; it could serve to stabilize and even retract cortical structures, such as pseudopods and lamellopods. Involved in the whole cell motility of aggregation-stages cells. Overexpression results in significant decrease in the rate of cellular translocation and fluid-phase pinocytosis and abnormalities in the normal rearrangement of the actin cytoskeleton.
Subcellular location: Cell projection, pseudopodium. Cytoplasm, cell cortex. Note=Highest concentration just beneath the plasma membrane in the anterior pseudopod at the leading edge of the cell and at sites of cell-cell contact in both stationary and aggregation stage cells. Also found in macropinocytic structures.
Interaction partners:
- Myosin-IB light chain
- Myosin ID heavy chain
- Protein CARMIL
Sequence:
MSKKVQAKQGTDDLVMLPKVSEDEICENLKKRYMNDFIYTNIGPVLISVNPFRNLNNSGPDFIEAYRGKHAQEVPPHVYQLAESAYRAMKNDQENQCVIISGESGAGKTEAAKLIMGYVSAISGSTEKVEYVKHVILESNPLLEAFGNAKTLRNNNSSRFGKYFEIQFDKAGDPVGGKIYNYLLEKSRVVYQNPGERNFHIFYQLLAGASAQEKRDYVLSSPESYYYLNQSQCYTVDGINDVSDYAEVRQAMDTIGLTAQEQSDIIRIVACVLHIGNIYFIEDDKGNAAIYDPNALELAASMLCIDSATLQNAILFRVINTGGAGGAGNRRSTYNVPQNVEQANGTRDALARTIYDRMFSWLVERVNQSLSYYKSPYQNVIGILDIFGFEIFEKNGFEQFCINFVNEKLQQFFIELTLKAEQEEYVREGIKWEPIKYFNNQIVCDLIEGKSPPGIFSLLDDICSTLHAQSTGTDQKFLEKMAGIYDGHLHWRGMTGAFAIKHYAGEVTYEAEGFSDKNKDTLFFDLIEAIQCSKMPFLASLFNEDTGSLQKKRPTTAGFKIKTSAGELMKALSQCTPHYIRCIKPNETKKAKDWENSRVKHQVQYLGLLENVRVRRAGFAYRNTFDKVLKRYKKLSSKTWGIWGEWKGDAIEGCKTIFQDMNLEAGQWQLGKTKVFIRHPETVFLLEEALDKKDFDCTAKIQKAFRNWKAKKHSLEQRAQIAHMFKDKKERQRNSIDRKFTSDYIDFENQFGLQEAMQNAHKKERVVFADTVIKIDRRAKQKNYEMVLTDQALYFVEKSIKKKVLVHTLIRRVGLREIKGVSISTLSDNVIVFHLPEHDQVIENDKKTEIIIVLVEYFKAIGGGSLNVQFSDRINYTLKKGEQKEISFQKSEQCPTLVVKKGGKGLIGTIASGLPSSTDSTPKNYNPNSMSQASSRPAPQQSAGRGRGMPQGAGQPQPQQPQQQQRPMPQPQQGGGARPMPQPQQGGGARPMGAPQQGGAPQQGAGRQLPQPTQQGGAPGGRGAPMGRGAPGGGPAGAGGRPLPTVAKPAPQPSRPTAKALYDYDASSTDELSFKEGDIIFIVQKDNGGWTQGELKSGQKGWAPTNYLQYN
Protein: RRM domain-containing protein (Q4Q2S5)
Organism: Leishmania major
Interaction partners:
- Putative elongation initiation factor 2 alpha subunit
- Translation initiation factor-like protein
- Eukaryotic translation initiation factor 3 subunit E
- CSN8/PSMD8/EIF3K domain-containing protein
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit 7-like protein
- Putative eukaryotic translation initiation factor 5
- Putative translation initiation factor
- Putative eukaryotic translation initiation factor 3 subunit 8
- Uncharacterized protein
Sequence:
MSNWADAAQDEEQYQAAYGSDDNDSYSEHEEPKPSWDTAKTEITFEVDADGNRFEVMRKVRSYHVDRPITMADIRAKLAHFGKGKGDQSTLVSAEPPLALEMGSVDQFERESRAEVKRMIHEASGIDVAVKDEHLRVVREMEEKAKKDPRVVRSGAGSTWGAIASKSTDNREQSTTGIRIRNLSDDITQENLSRIFEGRGWITKNVRIPRGDNNQTRGFAFVIFEEAWMADAAIKEGKFHFKNVVLDVSRAETRT
Protein: Fatty acyl CoA synthetase, putative (EC 6.2.1.3) (Q38BS1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Monoglyceride lipase, putative
- Monoglyceride lipase, putative
- Long-chain-fatty acid-CoA ligase protein, putative
- Fungal lipase-type domain-containing protein
- Lipase-like protein, putative
Sequence:
MGGCVASLIESRNTKSLVDNDDILQYNKLPCQIRVVAGTEREDASPVYRKFDVTDEDFEKMSHDAYHGEPLIQLIREICGLRGEKVAMAYRNMQRVERNVVKDASGKSKTMDMYVFSPGRRNISYKQLWETVENFSKGLCEIGLQERQCLALFEETRWEWYASLLSAWCHNMIVATVYANLGEDALRYALREAQCGCIICNGKNVPVLLDKVKLKEMGNPVVIYLDDLPTNVDIMDLRVYKWSTVVEMGAKSEKAQLNIPTCENCDDTALIMYTSGTTGDPKGVVHTHGSLASGVYALSIRLSEVFGDPRDDETYCSYLPLAHIMELAVLSILMLRGCLIGFGSPRTITNTFSKPHGDLVEYRPFVLSAVPRVFDTIKKNVEAMLPSPGSIKRTVFERGYQARLKALRDGKETPYLNEKVFNKVRQATGGNVRLYFSGGAPLSPATQEFINVVLGTVIQGWGLTETVCCGGTQFPGSLESESIGRMIDTVELRLLDTPEYRHTDKPEPRGEILLRGPFLFKEYYKQKALTEEVIDSEGWFHTGDVGCVSKNGTLRIIGRVKALVKNSNGEYLALESLEATYGQNKLCTPNGVCVLVHPQRSYIAALALTTEQLIMPFAKEHKIRGTYPEILENVELRKKVCESFQETGRAAGKKSFEIVRDVRLLSDEWTPENGVLTAAAKLKRRIIDERYKELIEEIFRNDV
Protein: M94 protein (H2A1E8)
Organism: Murid herpesvirus 1 (MuHV-1) (Mouse cytomegalovirus)
Interaction partners:
Sequence:
MATSRLSVKSLRSISRFVQWECCWILVNKSARYREFRAVTSQSPGLGKVSSTDDGRCLAASMMLFRRDGNFVLCLVVNKEPVGQFGCSGMRREKMVIDGLQEPVYVMRLLAPLIPVKLGFSPYMLPPKSIGGSGGLDPSVIYQNASVVTPEEAATVTMQGSGIVTVGLSGVGSWVQIKDGGNMKLFVFALCFDVFTACCDRLAFPSLAKIYSETVSCEADKCGFCRDSGRHVDPTGRFVGCVPDSGVCLCYSPCRGTDAAVSVRSWLPYLELEDGANTHSLFVRRYDGRKGLPATISDYLGARNNEGEEIPLRTEPWQLLKIEPTLSAMIIMACPLLKKIVLEHM
Protein: Profilin (Q26734)
Organism: Trypanosoma brucei brucei
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
Sequence:
MSWQSYVDDSLVGSGFMHSAAIVGLADGSYWAYGGTYVPQPEEVTHILKCLENFSLVQSSGVTICGVKFFGLQSGSEGQMKYIFFKKGAAGGCIYTSKQTAIIAVYGNPGDASALQQDLQKTEATYVAVNPADCNTTVKRIAEYLISLDY
Protein: Mitochondrial antiviral-signaling protein (Mitochondrial antiviral-signaling protein isoform X1) (F1REK4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSLTREQFYNKGIRPYMGRFATDIKVREILPYLQCLTISDREEIEAKKEQYGNYNAVQTLLDNLRRRENWIDEFITALRKCELGSLANEMSDIYDRIRGITSGPKPTDTLAPSLTGATATVTTATVHTVPPTTLPLLMPPAGDAPVHSTAPCKQATQEPSPDSVLQVAETQQVEQVSPPAPAPTPEPVPQTEITPQVIAPSQAAPDMSSPINLKVLTHTGEAVTITPVSRALDSLGFTITSSAGESPISTSCTQASISNTSQIQLTRPCSTTQSSGNIQVPKKEVKDLDTSEKFPVQDTNLPLRQERTFQGPEETSDPIANEVVQRHNGVGLPVSNAEIISNRTTQATTSTPTEVVAHAPHSVIPEQEYFSKPGFLQIPEPQQNRAGTLPVLQEDPCSLVSGDLEISRETASSTESRQVASLADQASTSSTSTLPLNNPSYTSALLTNNQPEEDHYESVSENQTLRHVFHVAEEPPAENLNGQPPSMLLRSRVNSEEPPTLNRVGIENVAHICVPSVDIAEASDHKSTTVIAREQECNAATAATIQQPEQREEGRPELFRINNVHVVTAAGIALSAVFLAWKLNH
Protein: Cap binding complex dependent translation initiation factor (K7EK08)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MENSSAASASSEAGSSRSQEIEELERFIDSYVLEYQVQGLLADKTEGDGESERTQSHISQWTADCSEPLDSSCSFSRGRAPPQQNGSKDNSLDMLGTDIWAANTFDSFSGATWDLQPEKLDFTQFHRKVRHTPKQPLPHIDREGCGKGKLEDGDGINLNDIEKVLPAWQGYHPMPHEVEIAHTKKLFRRRRNDR
Protein: Probable sucrose-phosphate synthase 2 (EC 2.4.1.14) (Protein KAONASHI 2) (Sucrose-phosphate synthase 2F) (AtSPS2F) (Sucrose-phosphate synthase 5.2) (AtSPS5.2) (UDP-glucose-fructose-phosphate glucosyltransferase) (Q9FY54)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in photosynthetic sucrose synthesis by catalyzing the rate-limiting step of sucrose biosynthesis from UDP-glucose and fructose- 6-phosphate. Involved in the regulation of carbon partitioning in the leaves of plants. May regulate the synthesis of sucrose and therefore play a major role as a limiting factor in the export of photoassimilates out of the leaf. Plays a role for sucrose availability that is essential for plant growth and fiber elongation. Required for nectar secretion.
Interaction partners:
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Probable sucrose-phosphatase 1
- Probable sucrose-phosphatase 3a
- Probable sucrose-phosphatase 3b
- Probable sucrose-phosphatase 2
- UTP--glucose-1-phosphate uridylyltransferase 1
- UTP--glucose-1-phosphate uridylyltransferase 2
- Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 2, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic
Sequence:
MVGNDWVNSYLEAILAAEPGIANSKPPGTGDSKSSLLLRERGHFSPTRYFVEEVITGFDETDLHRSWVQAAATRSPQERNTRLENLCWRIWNLARQKKQVEGKNAKREAKREREREKARREVTAEMSEDFSEGEKADLPGEIPTPSDNNTKGRMSRISSVDVFENWFAQHKEKKLYIVLISLHGLIRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVTAPDVDSSYSEPSEMLNPIDTDIEQENGESSGAYIIRIPFGPKDKYVPKELLWPHIPEFVDRALSHIMQISKVLGEQIGGGQQVWPVSIHGHYADAGDSTALLSGALNVPMVFTGHSLGRDKLEQLLKQGRPKEEINSNYKIWRRIEAEELCLDASEIVITSTRQEVDEQWRLYDGFDPVLERKLRARMKRGVSCLGRFMPRMVVIPPGMEFHHIVPHDVDADGDDENPQTADPPIWSEIMRFFSNPRKPMILALARPDPKKNLVTLVKAFGECRPLRELANLTLIMGNRNDIDELSSTNSSVLLSILKLIDKYDLYGQVAMPKHHQQSDVPEIYRLAAKTKGVFINPAFIEPFGLTLIEAGAHGLPTVATINGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVSDRQLWGRCRQNGLNNIHLFSWPEHCKTYLARIASCKQRHPKWQRVEFENSDSDSPSDSLRDINDISLNLKLSLDGEKSGSNNGVDTNLDAEDRAAERKAEVEKAVSTLAQKSKPTEKFDSKMPTLKRRKNIFVISVDCSATSDLLAVVKTVIDAAGRGSSTGFILSTSMTISETHTALLSGGLKPQDFDAVICSSGSELYFTSSGSEDKTALPYTLDADYHSHIEFRWGGESLRKTLIRWISSVEEKKKTKKGEILVEDESSSTNYCLSFKVKDPALMPPMKELRKLMRNQALRCNAVYCQNGARLNVIPVLASRSQALRYLLVRWGIDLSNMVVFVGDSGDTDYEGLLGGIHKTVILKGLASDLREQPGNRSYPMEDVTPLNSPNITEAKECGRDAIKVALEKLGISLLKP
Protein: V(D)J recombination-activating protein 2 (RAG-2) (O13034)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. DNA cleavage by the RAG complex occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. In the RAG complex, rag2 is not the catalytic component but is required for all known catalytic activities mediated by RAG1. It probably acts as a sensor of chromatin state that recruits the RAG complex to H3K4me3 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- V
- Tyrosine-protein kinase
- CD4-1 molecule
- DNA-dependent protein kinase catalytic subunit
- Transmembrane protein 232
- Fumarylacetoacetase.
- Cytochrome b
- Immunoglobulin heavy constant zeta.
- Runt-related transcription factor
- Transcriptional regulator Myc-A
Sequence:
MSLQPLTAVNCGSLVQPGFSLLDLEGDVYLFGQKGWPKRSCPTGIFGVRIKKGELKLRAISFSNNSSYLPPLRCPAIAHFEAQDGKPECYLIHGGRTPNNELSSSLYMLSVDSRGCNRKVTLRCEEKELVGDVPSARYGHTLSVINSRGKTACVLFGGRSYMPPTERTTQNWNSVGDCPPQVYLIDLEFGCCTAHTLPELTDGQSFHVALARQDCVYFLGGHILSSDCRPSRLIRLHVELLLGSPVLTCTILHEGLTITSAIASPIGYHEYIIFGGYQSETQKRMECTYVGLDDVGVHMESREPPQWTSEISHSRTWFGGSLGKGTALVAIPSEGNPTPPEAYHFYQVSFQKEQDGEATAQGCSQESTDFEDSAPLEDSEELYFGREPHELEYSSDVEGDTYNEEDEEDESQTGYWIKCCLSCQVDPNIWEPYYSTELTRPAMIFCSRGEGGHWVHAQCMELPESLLLQLSQDNSKYFCLDHGGLPKQEMTPPKQMLPVKRVPMKMTHRKAPVSLKMTPAKKTFLRRLFD
Protein: Small nuclear ribonucleoprotein SmD3b (SmD3-b) (snRNP core protein D3-b) (Q9LM92)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity). May play a major role in the splicing of cellular pre-mRNAs. Required for normal plant development.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62318}. Nucleus {ECO:0000250|UniProtKB:P62318}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000250|UniProtKB:P62318}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D2
- Probable small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein E
- Probable small nuclear ribonucleoprotein F
- Sm protein F
- Small nuclear ribonucleoprotein SmD1b
- Small nuclear ribonucleoprotein SmD1a
- Sm-like protein LSM3A
Sequence:
MSRSLGIPVKLLHEASGHIVTVELKSGELYRGSMIECEDNWNCQLEDITYTAKDGKVSQLEHVFIRGSKVRFMVIPDILKHAPMFKRLDARIKGKSSSLGVGRGRGAMRGKPAAGPGRGTGGRGAVPPVRR
Protein: 14-3-3a protein (B6REZ8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MEREQQVYLARLAEQAERYDEMVEAMKNVAKLDVELTVEERNLLSVGYKNVIGARRASWRILSSIEQKEEAKGNEQNVKRIKEYRQRVEDELAKICDDILSVIDKHLIPSSSTGESTVFYYKMKGDYFRYLAEFKAGEDRKEAADQSLKAYEAATTTANSDLPPTHPIRLGLALNFSVFYYEILNSAERACHLAKQAFDEAIAELDSLNEESYKDSTLIMQLLRDNLTLWTSDLPEEGGEQSKGDEPQAES