wanglab/gogpt-training-data huggingface dataset:
Protein: BTB/POZ and TAZ domain-containing protein 5 (BTB and TAZ domain protein 5) (Q6EJ98)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19054356}.
Interaction partners:
- At1g25400
- Adenine nucleotide transporter BT1, chloroplastic/mitochondrial
- Expressed protein)
- Uncharacterized protein F12A4.5
- O-fucosyltransferase 20
- Germin-like protein subfamily 1 member 19
- Poly polymerase
- F21O3.6 protein)
- E3 ubiquitin-protein ligase RZFP34
Sequence:
MENMDDFSPENVLAPPPPPPPMKKSTDLFMQRSNSFVSKATRDSWDRMFDEAHGADVLIHTDDNGLIYAHSNVIGMASDVIRGMMKQHKRKSHRKSISILGVPHHALRVFIRFLYSSCYEKQDMEDFAIHLLVLSHVYVVPHLKRVCESEFESSLLNKENVIDVFQLALLCDAPRLGLLCHRMILNNFEEVSTSEGWQAMKESHPRLQKELLRSVAYELNSLKQRNRKQKEIQTYTQLYEAMEAFVHICRDGCREIGPTKTETPHMSCGFQACNGLEQLLKHLAGCKLRSIPGGCSRCKRMWQLLELHSRICVDSEQCKVPLCSSLKERMKTQSRKDEKRWKLLVRNVLSTKRIGGSPFFLQAIDVTL
Protein: Thiosulfate sulfurtransferase 18 (EC 2.8.1.1) (Sulfurtransferase 18) (AtStr18) (Q9FKW8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is thiosulfate > 3-mercaptopyruvate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15181206}.
Interaction partners:
- Thiosulfate/3-mercaptopyruvate sulfurtransferase 2
- Thiosulfate/3-mercaptopyruvate sulfurtransferase 1, mitochondrial
- Small ribosomal subunit protein mS29
- Adenylyltransferase and sulfurtransferase MOCS3
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL24c
- Molybdopterin synthase catalytic subunit
- Cysteine desulfurase 1, chloroplastic
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein uL29m
Sequence:
MSQSISSSTKAEEVVSVDVSQAKTLLQSGHQYLDVRTQDEFRRGHCEAAKIVNIPYMLNTPQGRVKNQEFLEQVSSLLNPADDILVGCQSGARSLKATTELVAAGYKKVRNVGGGYLAWVDHSFPINTEEEEPSAN
Protein: Testis-expressed protein 13B (Q9BXU2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALRPEDPSSGFRHGNVVAFIIEKMARHTKGPEFYFENISLSWEEVEDKLRAILEDSEVPSEVKEACTWGSLALGVRFAHRQGQLQNRRVQWLQGFAKLHRSAALVLASNLTELKEQQEMECNEATFQLQLTETSLAEVQRERDMLRWKLFHAELAPPQGQGQATVFPGLATAGGDWTEGAGEQEKEAVAAAGAAGGKGEERYAEAGPAPAEVLQGLGGGFRQPLGAIVAGKLHLCGAEGERSQVSTNSHVCLLWAWVHSLTGASSCPAPYLIHILIPMPFVRLLSHTQYTPFTSKGHRTGSNSDAFQLGGL
Protein: histidine kinase (EC 2.7.13.3) (Q1CXR8)
Organism: Myxococcus xanthus (strain DK1622)
Interaction partners:
- histidine kinase
- histidine kinase
- histidine kinase
Sequence:
MGSDDIVAALRQVPLFARLTGEQLRWMADHGRQLHFPAGTRIAEQGAAADGLSVIMEGHTQWSRRTGTESVPTFTLEAGDLFGELILFLNAPYPHSGDAVTDVRLFRLEPATFWELLRLAPGLSRGLMELASQRSQQQAQDVRPQSEVLPVGRMAAELGAELGSPAAAARRSAARLGELMATVSARAMALGDHGLSLPQRSVLLALPREAAERGRTSPPLEPLARAEREEALGSWLEARGVADAWEAAPALVASGLDVAWLESVATRVGGALLGDVLAWLVVAVSCDVLMAEVARGTARVSALVEGVKAYAFMDPVPREDVDVHDGLEHALAALGHRLRGEHLTVEREYDPHLPRLKAEGVALDELWTQLVLNALEALGERGGRVRLRTWKDAAHVVVEVSDDGPGIPKDLLPRIFEPFFSTKPHAAGMGLDVCRRIVERHGGDLCVRAEQSGTRIQVRLPA
Protein: Probable LRR receptor-like serine/threonine-protein kinase At5g16900 (EC 2.7.11.1) (C0LGT5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- At5g55620
- RNA-binding motif protein 25
- Kinesin-like protein KIN-UC
- Cytochrome P450 71B5
Sequence:
MEDRHRYLFFIFAIIHYVQAQQGFISLDCGLPSNEPPYIEPVTGLVFSSDADHIPSGISGRIQKNLEAVHIKPYLFLRYFPDGLRNCYTLDVLQNRRYMIKAVFVYGNYDGYNDYPSFDLYLGPNKWVRVDLEGKVNGSVEEIIHIPSSNSLQICLVKTGNSLPFISALELRLLRNDTYVVQDVSLKHLFRRYYRQSDRLIRYPDDVYDRVWSPFFLPEWTQITTSLDVNNSNNYEPPKAALTSAATPGDNGTRLTIIWTLDNPDEQIHLYVHFAELEPVGENTDEALRTLFTRTFYFVVNGKISYDESITPLDLAVSTVETVVNKCDGGNCSLQLVRSEASPGVRVPLVNAMEAFTAIKFPHSETNPDDVISIKVIQATYELSRVDWQGDPCLPQQFLWTGLNCSYMNMSTSPRIISLDLSSHKLTGKIVPDIQNLTQLQKLDLSNNKLTGGVPEFLANMKSLLFINLSNNNLVGSIPQALLDRKNLKLEFEGNPKLCATGPCNSSSGNKETTVIAPVAAAIAIFIAVLVLIIVFIKKRPSSIRALHPSRANLSLENKKRRITYSEILLMTNNFERVIGEGGFGVVYHGYLNDSEQVAVKVLSPSSSQGYKEFKAEVELLLRVHHINLVSLVGYCDEQAHLALIYEYMANGDLKSHLSGKHGDCVLKWENRLSIAVETALGLEYLHSGCKPLMVHRDVKSMNILLDEHFQAKLADFGLSRSFSVGEESHVSTGVVGTPGYLDPEYYRTYRLTEKSDVYSFGIVLLEIITNQPVLEQANENRHIAERVRTMLTRSDISTIVDPNLIGEYDSGSVRKALKLAMSCVDPSPVARPDMSHVVQELKQCIKSENLRLRTGLNQVIDSKSS
Protein: Interferon-induced protein with tetratricopeptide repeats 5 (IFIT-5) (Interferon-induced 58 kDa protein) (Retinoic acid- and interferon-inducible 58 kDa protein) (P58) (Q13325)
Organism: Homo sapiens (Human)
Function: Interferon-induced RNA-binding protein involved in the human innate immune response. Has a broad and adaptable RNA structure recognition important for RNA recognition specificity in antiviral defense. Binds precursor and processed tRNAs as well as poly-U-tailed tRNA fragments. Specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and selectively binds AT-rich dsDNA. Additionally, as a mediator in innate immunity, regulates positively IKK-NFKB signaling by sinergizing the recruitment of IKK to MAP3K7.
Subcellular location: Cell projection, ruffle membrane {ECO:0000269|PubMed:23317505}. Note=Colocalized with RIGI at cell surface ruffles. Localizes to actin-rich protrusions from the apical cell surface.
Interaction partners:
- Antiviral innate immune response receptor RIG-I
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon-induced protein 44
- Interferon-induced helicase C domain-containing protein 1
- Interferon-induced GTP-binding protein Mx1
- 2'-5'-oligoadenylate synthase 3
- Ubl carboxyl-terminal hydrolase 18
- Interferon regulatory factor 7
- 2'-5'-oligoadenylate synthase-like protein
- Interferon-induced protein with tetratricopeptide repeats 3
Sequence:
MSEIRKDTLKAILLELECHFTWNLLKEDIDLFEVEDTIGQQLEFLTTKSRLALYNLLAYVKHLKGQNKDALECLEQAEEIIQQEHSDKEEVRSLVTWGNYAWVYYHMDQLEEAQKYTGKIGNVCKKLSSPSNYKLECPETDCEKGWALLKFGGKYYQKAKAAFEKALEVEPDNPEFNIGYAITVYRLDDSDREGSVKSFSLGPLRKAVTLNPDNSYIKVFLALKLQDVHAEAEGEKYIEEILDQISSQPYVLRYAAKFYRRKNSWNKALELLKKALEVTPTSSFLHHQMGLCYRAQMIQIKKATHNRPKGKDKLKVDELISSAIFHFKAAMERDSMFAFAYTDLANMYAEGGQYSNAEDIFRKALRLENITDDHKHQIHYHYGRFQEFHRKSENTAIHHYLEALKVKDRSPLRTKLTSALKKLSTKRLCHNALDVQSLSALGFVYKLEGEKRQAAEYYEKAQKIDPENAEFLTALCELRLSI
Protein: Glucosylceramidase (EC 3.2.1.45) (Endoglycoceramidase-related protein 1) (EGCrP1) (Glucocerebrosidase) (I1BTD7)
Organism: Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Function: Specifically hydrolyzes the glucosidic linkage in glucosylceramide. May prevent accumulation of aberrent glucosylceramide containing immature ceramide (By similarity).
Subcellular location: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTHPDRSAHDLNVPIQHSGRWFQDNLGRTLLLRGINVCGSSKLPTRPYPGSTHLYDDILFWDHRNVSFVNRPFPLEDAHEHFSRLSAWGLTLIRLLVPWESIEHEGPGCYDEEYIDYLRQLIEMMPRYGIKCIIDPHQDTWSRFSGGSGAPGWTFEVAGLNIKHFKETGAAYVHNTNAVPGDPLPMVWPTNYTKLASCTMFTLFFAGDTFAPHRTYQSQSIQQFLNHHFIEAYRHLAERLSDLEAVLAFEFMNEPHPGYIGLDHLDSFDPIMNLLFGDSPTPLQSFALGDGIPQTVDVYIKSWPFPTKKSHDRVINASQTSAWFSGCVWKEHGVWTVDDQGVPRLVNTHYFSKHPKTGEKISFYEDFYKPLVNRYVAAIQSVKKEYYCLVEPLANEKPPVYNEHDHHHNVIFSPHWYDLDSVFYKKFNARMTHDVQCLQRGGNVFSATYFGKRGAKKNYRGQIKNIKEDGLLNMGEKPCIMGEVGIPMDLNNKMAFEDDNYENHVHFMDAIIYALETNLISFTLWNYDVFNDHEYGDHWNGENFSIYSVKKSEEDYMRHDDGNSKLSKKHLYDGGRVLEAVLRPYAAKVAGTPVSAEFNIDTLQYTFSFIPDCKGSTTTEIFVPYFHYGNKTIKTDVSFGRCSYIEEFQTLYHQYELNDPLPKLVTITMGILTTESANSCSVM
Protein: Pentraxin-related protein PTX3 (Pentaxin-related protein PTX3) (Tumor necrosis factor-inducible gene 14 protein) (TSG-14) (P48759)
Organism: Mus musculus (Mouse)
Function: Plays a role in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility.
Subcellular location: Secreted.
Interaction partners:
- Tumor necrosis factor-inducible gene 6 protein
- Mannose-binding protein C
- Mannose-binding protein A
- Fibroblast growth factor 2
- P-selectin
- Interleukin-6
- Ficolin-2
- Ficolin-1
- Fibroblast growth factor 10
- Hyaluronan synthase 2
Sequence:
MHLPAILLCALWSAVVAETSDDYELMYVNLDNEIDNGLHPTEDPTPCDCRQEHSEWDKLFIMLENSQMREGMLLQATDDVLRGELQRLRAELGRLAGGMARPCAAGGPADARLVRALEPLLQESRDASLRLARLEDAEARRPEATVPGLGAVLEELRRTRADLSAVQSWVARHWLPAGCETAIFFPMRSKKIFGSVHPVRPMKLESFSTCIWVKATDVLNKTILFSYGTKWNPYEIQLYLSSQSLVLVVGGKENKLAADTVVSLGRWSHLCGTWSSEQGSMSLWANGELVATTVEMAKSHSVPEGGLLQIGQEKNGCCVGGGFDESLAFSGRITGFNIWDRVLSEEEIRASGGVESCHIRGNVVGWGVTEIQAHGGAQYVS
Protein: Glutaminyl-tRNA synthetase 1 (A0A0U1RQL2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
TLGSTIDKATGILLYGLASRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMEVGGVLFFAFLQLLVPMLLGEARAVLKWADGKMIKNEVDMQVLHLLGPKLEADLEKKFKVAKARLEETDRRTAKDVVENGETA
Protein: Tegument protein UL51 homolog (F5HEA3)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Plays several roles during the time course of infection, including egress of virus particles from the perinuclear space and secondary envelopment of cytoplasmic capsids that bud into specific trans-Golgi network (TGN)-derived membranes.
Subcellular location: Virion tegument {ECO:0000250|UniProtKB:P10235}. Host cytoplasm {ECO:0000250|UniProtKB:P10235}. Host Golgi apparatus {ECO:0000250|UniProtKB:P10235}.
Interaction partners:
Sequence:
MQLAQRLCELLMCRRKAAPVADYVLLQPSEDVELRELQAFLDENFKQLEITPADLRTFSRDTDVVNHLLKLLPLYRQCQSKCAFLKGYLSEGCLPHTRPAAEVECKKSQRILEALDILILKLVVGEFAMSEADSLEMLLDKFSTDQASLVEVQRVMGLVDMDCEKSAYMLEAGAAATVAPPTPPAVVQGESGVREDGETVAAVSAFACSSVSDSLIPEETGVTRPMMSLAHINTVSCPTVMRFDQRLLEEGDEEDEVTVMSPSPEPVQQQPPVEPVQQQPQGRGSHRRRYKESAPQETLPTNHEREILDLMRHSPDVPREAVMSPTMVTIPPPQIPFVGSARELRGVKKKKPTAAALLSSA
Protein: Nascent polypeptide-associated complex subunit alpha-like protein 3 (NAC-alpha-like protein 3) (Alpha-NAC-like protein 3) (Q6ICZ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May promote appropriate targeting of ribosome-nascent polypeptide complexes.
Interaction partners:
- Nascent polypeptide-associated complex subunit beta
- Basic transcription factor 3
- Large ribosomal subunit protein uL22y
- Large ribosomal subunit protein uL18y
- Probable elongation factor 1-gamma 2
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein uL23y
- Uncharacterized protein T9C5.90
- Large ribosomal subunit protein uL4y
Sequence:
MTAEQKVELAAKLEEQKIDLDKPEVEDDDDNDEDDSEDDDEAEGHDGEAGGRSKQSRSEKKSRKAMLKLGMKPITGVSRVTVKKSKNILFVISKPDVFKSPASDTYVIFGEAKIEDLSSQLQSQAAEQFKAPNLSNVISQGETSSAATAAAVQDDDDEEVDEEGVEPKDIELVMTQAGVSKPRAVKALKLANGDIVSAIMELTT
Protein: Rho-related protein rac1A (P34144)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Overexpression promotes the formation of filopodia and membrane ruffles.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase pakB
- Uncharacterized protein
- Ras GTPase-activating-like protein rgaA
- Rac guanine nucleotide exchange factor B
- Putative rho GDP-dissociation inhibitor 2
- Putative rho GDP-dissociation inhibitor 1
- Ras guanine nucleotide exchange factor S
- Serine/threonine-protein kinase pakC
- Probable serine/threonine-protein kinase glkA
- Ras GTPase-activating-like protein gapA
Sequence:
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPINLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSIISPSSFENVNGKWHPEICHHAPNVPIILVGTKLDMREDKETQDRLKEKKLYPISYEQGLAKMKEINAVKYLECSALTQKGLKTVFDEAIRAVINPPLSKKKKSSGGCNIL
Protein: Probable calcium-binding protein CML16 (Calmodulin-like protein 16) (Q9LI84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Potential calcium sensor.
Interaction partners:
- Probable calcium-binding protein CML47
- Probable calcium-binding protein CML46
- Probable calcium-binding protein CML49
- Probable calcium-binding protein CML48
- GSH-induced LITAF domain protein
- F3I6.9 protein
- At5g57910
- Probable calcium-binding protein CML21
- Probable LRR receptor-like serine/threonine-protein kinase At4g37250
- Probable calcium-binding protein CML45
Sequence:
MASTKPTDQIKQLKDIFARFDMDKDGSLTQLELAALLRSLGIKPRGDQISLLLNQIDRNGNGSVEFDELVVAILPDINEEVLINQEQLMEVFRSFDRDGNGSITAAELAGSMAKMGHPLTYRELTEMMTEADSNGDGVISFNEFSHIMAKSAADFLGLTAS
Protein: Low affinity immunoglobulin epsilon Fc receptor (BLAST-2) (C-type lectin domain family 4 member J) (Fc-epsilon-RII) (Immunoglobulin E-binding factor) (Lymphocyte IgE receptor) (CD antigen CD23) [Cleaved into: Low affinity immunoglobulin epsilon Fc receptor membrane-bound form; Low affinity immunoglobulin epsilon Fc receptor soluble form] (P06734)
Organism: Homo sapiens (Human)
Function: Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B-cells (it is a B-cell-specific antigen).
Subcellular location: Cell membrane; Single-pass type II membrane protein. Cell membrane; Lipid-anchor. Secreted {ECO:0000269|PubMed:37453717}. Note=Also exists as a soluble excreted form, sCD23.
Interaction partners:
- Complement receptor type 2
- Neurogenic locus notch homolog protein 2
- Signal transducer and activator of transcription 6
- B-lymphocyte antigen CD19
Sequence:
MEEGQYSEIEELPRRRCCRRGTQIVLLGLVTAALWAGLLTLLLLWHWDTTQSLKQLEERAARNVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKSQELNERNEASDLLERLREEVTKLRMELQVSSGFVCNTCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVCDRLATCTPPASEGSAESMGPDSRPDPDGRLPTPSAPLHS
Protein: Tyrosine recombinase XerS (Q97QP2)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01816}.
Interaction partners:
Sequence:
MKREILLERIDKLKQLMPWYVLEYYQSKLAVPYSFTTLYEYLKEYDRFFSWVLESGISNADKISDIPLSVLENMSKKDMESFILYLRERPLLNANTTKQGVSQTTINRTLSALSSLYKYLTEEVENDQGEPYFYRNVMKKVSTKKKKETLAARAENIKQKLFLGDETEGFLTYIDQEHPQQLSNRALSSFNKNKERDLAIIALLLASGVRLSEAVNLDLRDLNLKMMVIDVTRKGCKRDSVNVAAFAKPYLENYLAIRNQRYKTEKTDTALFLTLYRGVPNRIDASSVEKMVAKYSEDFKVRVTPHKLRHTLATRLYDATKSQVLVSHQLGHASTQVTDLYTHIVSDEQKNALDSL
Protein: Nuclear egress protein 1 (P0CK47)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network.
Subcellular location: Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
Interaction partners:
Sequence:
MAPVTPDAVNARQQRPADPALRRLMHPHHRNYTASKASAHSVKSVSRCGKSRSELGRMERVGSVARSICSRHTRHGVDRSHFSLRDFFRGISANFELGKDFLREMNTPIHVSEAVFLPLSLCTLSPGRCLRLSPFGHSLTLGSHCEICINRSQVHVPQEFSSTQLSFFNNVHKIIPNKTFYVSLLSSSPSAVKAGLSQPSLLYAYLVTGHFCGTICPIFSTNGKGRLIMHLLLQGTSLHIPETCLKLLCENIGPTYELAVDLVGDAFCIKVSPRDTVYEKAVNVDEDAIYEAIKDLECGDELRLQIINYTQLILENKQ
Protein: Thymocyte selection-associated high mobility group box protein TOX (Thymus high mobility group box protein TOX) (Q66JW3)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator with a major role in neural stem cell commitment and corticogenesis as well as in lymphoid cell development and lymphoid tissue organogenesis. Binds to GC-rich DNA sequences in the proximity of transcription start sites and may alter chromatin structure, modifying access of transcription factors to DNA. During cortical development, controls the neural stem cell pool by inhibiting the switch from proliferative to differentiating progenitors. Beyond progenitor cells, promotes neurite outgrowth in newborn neurons migrating to reach the cortical plate. May activate or repress critical genes for neural stem cell fate such as SOX2, EOMES and ROBO2. Plays an essential role in the development of lymphoid tissue-inducer (LTi) cells, a subset necessary for the formation of secondary lymphoid organs: peripheral lymph nodes and Peyer's patches. Acts as a developmental checkpoint and regulates thymocyte positive selection toward T cell lineage commitment. Required for the development of various T cell subsets, including CD4-positive helper T cells, CD8-positive cytotoxic T cells, regulatory T cells and CD1D-dependent natural killer T (NKT) cells. Required for the differentiation of common lymphoid progenitors (CMP) to innate lymphoid cells (ILC). May regulate the NOTCH-mediated gene program, promoting differentiation of the ILC lineage. Required at the progenitor phase of NK cell development in the bone marrow to specify NK cell lineage commitment. Upon chronic antigen stimulation, diverts T cell development by promoting the generation of exhaustive T cells, while suppressing effector and memory T cell programming. May regulate the expression of genes encoding inhibitory receptors such as PDCD1 and induce the exhaustion program, to prevent the overstimulation of T cells and activation-induced cell death.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:11850626}.
Interaction partners:
Sequence:
MDVRFYPPPAQPAAAPAAPCLGPSPCLDPYYCNKFDGENMYMSMTEPSQDYVPASQSYPGPSLESEDFNIPPITPPSLPDHSLVHLNEVESGYHSLCHPMNHNGLLPFHPQTMDLPEITVSNMLGQDGALLSNSISVMQEIGNAEGAQYSSHPQMAAMRPRGQPTDIRQQASMMQPGQLTTINQSQLSAQLGLNMGGTNVAHNSPSPPGSKSATPSPSSSVHEDECEDASKINGGEKRPASDMGKKPKTPKKKKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDGLGEEQKQVYKKKTEAAKKEYLKQLAAYRASLVSKSYTDPVDVKTSQPPQLVNSKPSVFHGPSQAHSALYLSSHYHQQPGMTPQLTAMHPSLPRNIAPKPNNQMPVTVSIANMAVSPPPPLQISPPLHQHLSMQQHQSLAMQQPLGSQLPMQVQTALHSPTMQQGFTLQPDYQTIINPTSTAAQVVTQAMEYVRSGCRNPPPQPVDWSTDYCSSGGMQRDKALYLT
Protein: Antitoxin VapB2 (O07227)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin VapC2. The C-terminal helix of the antitoxin may obstruct the toxin's RNA-binding groove, blocking access to the active sites. Additionally, the C-terminal arginine of the antitoxin may remove Mg(2+) ions from the toxin active sites.
Interaction partners:
- Ribonuclease VapC2
- Ribonuclease VapC5
- Antitoxin VapB30
- Putative antitoxin VapB5
- Ribonuclease VapC30
- Ribonuclease VapC15
- Antitoxin VapB15
- Toxin Rv0299
Sequence:
MSDVLIRDIPDDVLASLDAIAARLGLSRTEYIRRRLAQDAQTARVTVTAADLRRLRGAVAGLGDPELMRQAWR
Protein: Acyl-CoA ligase easD (EC 6.2.1.-) (Emericellamide biosynthesis protein B) (Q5BA81)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of emericellamides, secondary metabolites acting as antibiotics. The biosynthesis of emericellamides initiates from the highly reducing polyketide synthase easB which catalyzes the formation of the linear polyketide chain. EasB produces several polyketides that can be further processed by the downstream enzymes. The polyketides are released from easB as linear polyketide carboxylic acids, which are converted to CoA thioesters by the acyl-CoA ligase easD. The substrates are then loaded onto the acyltransferase easC, which shuttles them to the first thiolation (T) domain of the nonribosomal peptide synthetase easA. EasA then performs condensation of the polyketides with one glycine, two alanine, one valine and one leucine residues. A last step of cyclization leads to the production of emericellamides.
Interaction partners:
- Nonribosomal peptide synthetase easA
- Acyltransferase easC
- Nucleoporin NSP1
- Highly reducing polyketide synthase easB
Sequence:
MVFSSPSWVPRIPCEIPDSIPVGQFALEGNTSLPPQCGGRPPFVCAITGKSYSTKVLVDRVEFLSRSLAQELGWSPNEGEPEDKVVGIYSWNTLDFFALCWAVHRLNGICLPLHPFSIVPEVVAHMKRAKCRVIFTCQSLVANTLEAARELSIPGDKIYTTALPEAYLQNPEPIDQFKSVDQLIAEGEKLQRLPPLQWEKGRAKIQVAYYCATSGTSGKQKLAKITHYNFIANVMQVCMHESYAKNGRNEIAFGAIPLTHGYGLNIGHIMVYRGDTYVICPRFDMQLMLKTIERFRVERLYVVPPILAALAANPFLLDLHDLSSVQATVTGAAALDRSIAAKLNKLRPTWKINHAYGLTETGVVATLTSPHDVWHGSSGSLLPSFEIRLVKPDGTDAEGLDEPGEVHFNSPSCFLGYVGDDESNKNTFDEKGWLKSGDIGVFRKSPNGHAHLFILERIKDMIKVKGEQVLPRDIESVLLSHPAVIDAAVIGVPDELSGERAKAYIVRSKTVMEDLDEDDLADEIDEFVQGKLHESHWLHDRIVFLEKLPKSESGKVLKKDLKAMN
Protein: Anoctamin (A0A8I5ZNW7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU280814}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU280814}.
Interaction partners:
Sequence:
MQDTQDSDISLEGLTREGAPADRECQRGPETIVHEAQDAGTPNSGDATGAVDGEREATMRVPEKYSTLPAEDRSVHIVNICAIEDLGYLPSEGTLLNSLSVDPDAECKYGLYFRDGKRKVDYILVYHHKRASGSRTLARRGLQNDMVLGTRSVRQDQPLPGKGSPVDVGSPEAPMDYHEDDKRFRREEYEGNLLEAGLELERDEDTKIHGVGFVKIHAPWHVLCREAEFLKLKMPTKKVYHISETRGLLKTINSVLQKITDPIQPKVAEHRPQTTKRLSYPFSREKQHLFDLTDRDSFFDSKTRSTIVYEILKRTTCTKAKYSMGITSLLANGVYSAAYPLHDGDYEGDNVEFNDRKLLYEEWASYGVFYKYQPIDLVRKYFGEKVGLYFAWLGAYTQMLIPASIVGVIVFLYGCATVDENIPSMEMCDQRHNITMCPLCDKTCSYWKMSSACATARASHLFDNPATVFFSVFMALWAATFMEHWKRKQMRLNYRWDLTGFEEEEDHPRAEYEARVLEKSLRKESRNKEKRRNVPEEPTNKWKQRVRTAMAGVKLTDKVKLTWRDRFPAYFTNLVSIIFMIAVTFAIVLGVIIYRISTAAALAMNSSPSVRSNIRVTVTATAVIINLVVIILLDEVYGCIARWLTKIEVPKTEKSFEERLTFKAFLLKFVNSYTPIFYVAFFKGRFVGRPGDYVYIFRSFRMEECAPGGCLMELCIQLSIIMLGKQLIQNNLFEIGIPKMKKFIRYLKLRRQSPSDREEYIKRKQRYEVDFNLEPFAGLTPEYMEMIIQFGFVTLFVASFPLAPLFALLNNIIEIRLDAKKFVTELRRPVAIRAKDIGIWYNILRGVGKLAVIINAFVISFTSDFIPRLVYLYMYSQNGTMHGFVNHTLSSFNVSDFQNGTAPNDPLDLGYEVQICRYKDYREPPWSEHKYDISKDFWAVLAARLAFVIVFQNLVMFMSDFVDWVIPDIPKDISQQIHKEKVLMVELFMREEQGKQQLLDTWMEKEKPRDVPCNNHSPTAHPEAGDSSPVPSYEYHGGAL
Protein: Trafficking kinesin protein 1 (D4ACC5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Ras homolog gene family member T1
- Mitochondrial Rho GTPase 2
- Kinesin-1 heavy chain
- Mitofusin-2
- Kinesin heavy chain isoform 5A
- Nuclear distribution protein nudE homolog 1
- Unconventional myosin-XIX
- Trafficking kinesin-binding protein 2
- Disrupted in schizophrenia 1 homolog
- Syntaphilin
Sequence:
MTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRRYHSLGLFPMDSLAAEIEGTMRKELQLEEPESPDITHQKRVFETVRNVNQVVKQRSLTPSPMNIPGSNQSSAMNSLLSSCVSTPRSSFYGSDVSHVVLDNKTNSILLETEAADLGNEEHNKKPGTPGTPGSHDLETALRRLSLRRENYLSERRFFEEEQERKLRELAEKGELHSGSLTPTESIMSLGTHSRFSEFTGFSGMSFSSRSYLPEKLQIVKPLEGSATLHHWQQLAQPHLGGILDPRPGVVTKGFRTLDVDLDEVYCLNDFEEDDTGDHISLAGLATSTTIQHMETSGREAQLRPGSPW
Protein: Stevor (Q8I3D1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNTYYLKILLFSFLINILVLPQYENCEKGHYNGSLVLNNTQRTTINSRLLAQTQNHNPHYHNDPELKEIIDKLNNEAIKKYQQTHDPYEQLREVVEKNGTKIRGEHAAEPMSTLEKDLLDTYEEIFHEESHMLKSGRYPNDDDKTNEKSSSCECTDINNTKLTKTKGKDKYLKHLKHRCSRGICTCSVGSLFLTLIGLAAAKKAALAYFSGTTKTCVSSIPIFNMFNCSSVATSLQAGGATCATGISDIAGTVSTAATTTIFPFSIAIYVLIAITVILIILYIWLYRRRKNSWKHECKKHLCK