wanglab/gogpt-training-data huggingface dataset:
Protein: ShKT domain-containing protein (Q9XVB4)
Organism: Caenorhabditis elegans
Interaction partners:
- ShKT domain-containing protein
- Purple acid phosphatase
- DUF19 domain-containing protein
- C-type lectin domain-containing protein
- Putative serine protease F56F10.1
- EGF-like domain-containing protein
- Transmembrane 9 superfamily member
- DUF19 domain-containing protein
- EGF-like domain-containing protein
- Putative phospholipase B-like 2
Sequence:
MLLQSSILLLSVSLAACQISTAPCQDDPYTDCRDYAALCNNPMYKNFLDVFCPKTCGLCSDSTTLVPPTGSSNCVDTNVHCKSWVKQGYCTSCFVDCAERIQNCAKSCGFCNPGACINCQQREKFANNIFIN
Protein: Fcgbp protein (Q58E52)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
QCGCLYQGRYYVLGATFYPGPECERLCECGPDGQVTCQEGADCEPYEECRIENGVQACHPTGCGHCLANGGLHYVTLDGRVYDLHGSCSYVLASVCHPKPGDEEFSIVLEKNSAGDPQRVVVTVAGQVVGLARGPQVTVDGEVVTLPVATGHVSVTAEGRNIVLQTNKGMKVLFDGDAHILMSIPSSFRGRLCGLCGNFNGNWSDDFVLPSGAVAPNVEAFGTAWRAPGSSLGCGEGCGPQGCPVCLAEETQAYEKNDACGKIRDPHGPFAACHKVLSPLEYFRQCVYDMCAHKGDKAYLCRSLAAYTAACQAAGAAVKPWRTDSVCPLQCPAHSHYSICTRSCQGSCAALSGLTGCTTRCFEGCECDDHFLLSHGVCIPAQDCGCVHNGQYMPVNSSLMSSDCSERCFCSPNNGLTCHEAGCPSGHVCEIQAGVRECQAARGLCSISVGANLTTFDGAHNAISSPGVYELSSRCPGLQKNVPWYRVLADVQPCHNNDKIVSKVHIFFQDGLVTVIPSKGAWVNGLRVDLPATVLTSVSVRRMPDGSMLVHQKAGVTVWLGKDGLLDVMVGDDLAAMLCGACGNFDGDQTNDAYGSQGKTPIEKWRAQDFSPCSN
Protein: Alpha-hemolysin translocation ATP-binding protein HlyB (P08716)
Organism: Escherichia coli
Function: Part of the ABC transporter complex HlyBD involved in hemolysin export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDSCHKIDYGLYALEILAQYHNVSVNPEEIKHRFDTDGTGLGLTSWLLAAKSLELKVKQVKKTIDRLNFIFLPALVWREDGRHFILTKISKEVNRYLIFDLEQRNPRVLEQSEFEALYQGHIILITSRSSVTGKLAKFDFTWFIPAIIKYRRIFIETLVVSVFLQLFALITPLFFQVVMDKVLVHRGFSTLNVITVALSVVVVFEIILSGLRTYIFAHSTSRIDVELGAKLFRHLLALPISYFESRRVGDTVARVRELDQIRNFLTGQALTSVLDLLFSLIFFAVMWYYSPKLTLVILFSLPCYAAWSVFISPILRRRLDDKFSRNADNQSFLVESVTAINTIKAMAVSPQMTNIWDKQLAGYVAAGFKVTVLATIGQQGIQLIQKTVMIINLWLGAHLVISGDLSIGQLIAFNMLAGQIVAPVIRLAQIWQDFQQVGISVTRLGDVLNSPTESYHGKLTLPEINGDITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYLYQLQSD
Protein: Zinc finger protein 568 (E9PYI1)
Organism: Mus musculus (Mouse)
Function: Has transcriptional repression activity, partially through the recruitment of the corepressor TRIM28 but has also repression activity independently of this interaction. Essential during embryonic development, where it acts as direct repressor of IGF2-P0, placental-specific transcript of IGF2, in early development and regulates convergent extension movements required for axis elongation and tissue morphogenesis in all germ layers. Also important for normal morphogenesis of extraembryonic tissues including the yolk sac, extraembryonic mesoderm and placenta. May enhance proliferation or maintenance of neural stem cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:22110054, ECO:0000269|PubMed:23071813}.
Interaction partners:
Sequence:
MERLSQMAGRRAWCAEDSVPRQEEEDRTRPSKTVTFKDVAVDLTQEEWQQMKPAQRALYRDVMLETYSNLVTVGCQVTKPDVIFKLEQAEEPWVLEEEMFWRRSPEAARGRMKSFAFKDMAKDLRFEDVVIYFSLEEWECLRHSHRNLYRAVMLDNYSNLLSLSLADTKPRVVSLLEQGKEPWMVMRNETKIWHPDWVSRTEAKDSSKIKTLQEKMAKKHTCPTLEDSKTRGDREVTRELEGQQVHQEGHLRQAAVTSVERPDSVQCTAHREAHPGGKPCSSEKSQKTSLCQPPPIEREQLHSKAKASEHAQHGKVFNSCTSDTAVHPRPQESRKDSERKKSALAGGPDTSKPQSAQGSERPHKCKECGKAFHTPSQLSHHQKLHVGEKPYKCQECGKAFPSNAQLSLHHRVHTDEKCFECKECGKAFMRPSHLLRHQRIHTGEKPHKCKECGKAFRYDTQLSLHLLTHAGARRFECKDCDKVYSCASQLALHQMSHTGEKPHKCKECGKGFISDSHLLRHQSVHTGETPYKCKECGKGFRRGSELARHQRAHSGDKPYKCKECGKSFTCTTELFRHQKVHTGDRPHKCKECGKAFIRRSELTHHERSHSGEKPYECKECGKTFGRGSELSRHQKIHTGEKPYKCQQCGKAFIRGSHLTQHQRIHTGRRSE
Protein: Terminase DNA packaging enzyme small subunit (Q6U9F0)
Organism: Aeromonas phage 44RR2.8t
Interaction partners:
Sequence:
MNDVLDFTQLKDLNGIEGIHGEDVQVYAPLVLRDPVSNPNNRKIDQDDDYELVRRNMHYQSQMLLDMAKIALENAKNADSPRHVEVFAQLMGQMTTTNKEMLKMHKEMKDLAGAATVAIDGQVQKDADGEFIEFEGSPDELLDLELADEDIGDD
Protein: Dynein light chain Tctex-type 5 (Tctex1 domain-containing protein 1) (Q8N7M0)
Organism: Homo sapiens (Human)
Interaction partners:
- Dynein light chain Tctex-type 1
- Dynein light chain Tctex-type 3
- Dynein light chain roadblock-type 2
- Dynein light chain roadblock-type 1
- Cytoplasmic dynein 1 intermediate chain 1
- Cytoplasmic dynein 1 light intermediate chain 2
- Dynein light chain 2, cytoplasmic
- Cytoplasmic dynein 1 light intermediate chain 1
- Cytoplasmic dynein 2 light intermediate chain 1
- Cytoplasmic dynein 2 intermediate chain 1
Sequence:
MMMSDNAKGRAAHSWKKRGSISSLSNHEFWRKEIHGRIKDSMSTVSYMEEPSQRDDISRLTVQMENTYQLGPPKHFPVVTVNHILKDVVTSYLQVEEYEPELCRQMTKTISEVIKAQVKDLMIPRYKLIVIVHIGQLNRQSILIGSRCLWDPKSDTFSSYVFRNSSLFALANVYAVYLE
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q38CU3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MQGTMYWVVFLVAALQGIHLVLGQEEILNEQEFEALCRMINWAERGLKHINLARQVTEEALKIGVRYLEVAGEEEVTELTELQEKACMSNKKTSHEKNCGLYKTFWEESQEALKRTARSQAPHRGRNSLQYHTAEGIKIKVMEVADTYHEVKKEILKLRTDNMEEQLNQALYGVGHFTGEVKGGDSDRSRVCGQNLGNRDATGGWSLAVDLLCLCARHISWSSVKSVCCEECGTGENSNTWNPALDGALHWEFLKENCPGDNTNHHTEGEQLKSAKKNFMAKVSKIATIPYRTMYKLGDSKNIQTKQCGANIGTGQGICVYYGSDNGANLHWMQALERVENDVEVLLQDSKYKSTKLKRIKELSQEIQNLIEGGTPRGRQKRSVDTENSVPETPADPSDPTQSTTHTNEKKRIVRKPISTGNNASKSYGGDEVDSYDSKCDGENSACSDSPAKPTVKSSKSAINCPLGLILLLV
Protein: Glucocorticoid modulatory element-binding protein 2 (GMEB-2) (O88873)
Organism: Rattus norvegicus (Rat)
Function: Trans-acting factor that binds to glucocorticoid modulatory elements (GME) present in the TAT (tyrosine aminotransferase) promoter and increases sensitivity to low concentrations of glucocorticoids. Binds also to the transferrin receptor promoter (By similarity).
Subcellular location: Nucleus. Cytoplasm. Note=May be also cytoplasmic.
Interaction partners:
Sequence:
MATPDVSVHMEEVVVVTTPDTAVDGSGVEEVKTVLVTTNLAPHGGDLTEDNMETENAAAAACAFTASSQLKEAVLVKMAEEGENLEAEIVYPITCGDSRANLIWRKFVCPGINVKCVQYDEHVISPKEFVHLAGKSTLKDWKRAIRMNGIMLRKIMDSGELDFYQHDKVCSNTCRSTKIDLSGARVSLSSPTSTEYIPLTPAAADVNGSPATITIETCEDPGDWTTTIGDDTFAFWRGLKDAGLLDEVIQEFQQELEETMKGLQQRVQDPPLQLRDAVLLNNIVQNFGMLDLVKKVLASHKCQMDRSREQYARDLAALEQQCDEHRRRAKELKHKSQHLSNVLMTLTPVSLPSPMKRPRLARATSGPAAMASQVLTQSAQIALGPGMPMSQLTSVPLGKVVSTLPSTVLGKGSPQAAPASSPASPLLGGYTVLASSGSTFPSTVEIHPDTSSLTVLSTAAMQDGTTVLKVVSPLQLLTLPGLGPTLQNVAQASPAGSTIVTMPTAAATGPEEHTATIEVAAVAEDHEQK
Protein: Anillin (Actin-binding protein 8) (ABP8) (Protein scraps) (Q9V4P1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression and proper formation of the midbody. Required during cellularization of syncytial embryos for the proper formation and function of the furrow canals, the stable inward folds of the plasma membrane which separate the peripheral nuclei. Also required for the formation of the pole cells, the progenitors of the adult germline which are formed by cytokinesis of the cytoplasmic buds at the posterior pole of the syncytial embryo. Essential for embryonic viability.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Cell projection, cilium, flagellum {ECO:0000269|PubMed:20237161}. Note=Mainly found in the nucleus during interphase. Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contractile ring in anaphase. This pattern persists until telophase, when the protein becomes concentrated in the midbody. Accumulates in the nucleus of newly divided cells in a diffuse staining pattern, thereby restarting the cycle. Localizes to ring canal structures at the growing end of elongating spermatid cysts (PubMed:20237161). {ECO:0000269|PubMed:20237161}.
Interaction partners:
- Rac GTPase-activating protein 1
- Kinesin-like protein
- Ras-like GTP-binding protein Rho1
- Protein peanut
- Aurora kinase B
- Pebble, isoform B
- non-specific serine/threonine protein kinase
- Kinesin-like protein Klp61F
- Inner centromere protein, isoform A
- Protein diaphanous
Sequence:
MDPFTQHMLEKAEQRSRALGISNASKFPLVECSVPSSSATSASGGDAGVLAPRSRSPGGQSAASGGGKVVTLGKATLEASPAKPLRHYTAVNKENLDMGIEINITTDKPIGVQVEIQEQEVTDDEEQAEGGALNPLLEAEPVNQPLARLRDTSRSRLQRMGALYSNTDDLSSPIHRTEGQFHVTTGEEEDCGNRSSRQPKQRLGKLAALADTINQWEDDTSHHEVHRLLEAPPPKPHLSSRRAEKGPAPLPPKKDEVDEASRTKQLKWDPKVLSSLEAQGFQRRESSTIKHTYDYAKQEEAAPASKVEDAVLTAKPPVPQKSTTVSQVAKNFASSAPAPKPAPAPAVSVKSGLVSGRAALFENKGTGGQSQGLRNQKDPCELSLKERMKLFETGNNKAMLPMAPIGSAPSITQIRAEEVKQHLAAMHPVTAAAATTVVAATKPKQENKLRDKVAALVANAQSSAETRIKDIDRQRQEDMQIISNRFNKQKELFDNQPSDSSVAAQARPPAPAPSRVVRPMPPPPPPPIAALSPGLASSKRRSPGDAPTTDEDSKRARKSHSDRLYPALSDLDSSGDNCCAAETASATDDSHQQDEEETESCMDESDDQSQTEDSSAGMCNGSLGREIMSAVQRNEVEMQQQQTGKKTVRYADQDMYYDDSSLNSSQVSAGIDDYLDEALVEDYGSTQDDQSDSGDEQNASRLSLGSKGTTASNSFSFRKNPASICTPIEEHHEMEMDLQTPLLSGAQPVKSELSVNQDNDNLVTLVHTVSFYRRQQSANSSNSTPVRKICREQQVMRSALAGDCHAKHRLEYDSPQQSDYVAAATDIADQTDEDDEEMQNAREVNDASQAQDKIKKLLSEVCKQQQVIGQASQALNLCAATVEFSGSTESVEGERYLLLATHRRQACLDEVQRLRVENSIRPVGAPKEKGLLTVKDITIPLRQEYVRKMASNNINGHHLVCLLKYNEHVLATKTVPTMPGLLSVKFPDVLQLNNVYADFRITLEIYGMLAQRDQLPHELKYHINLNKKGGIKTPKKKGGENRLVMPPVQSPAGPHVVRTPQLVQYGFAIFSLREIQRTTWTLTQVLGVSPLEGVVHMKVNCELSVSVEYKGFLTMFEDISGFGAWHRRWCYLNGSVINYWKYPDDEKRKTPMGSIDLNSCTSQKVTTAPRDICARLNTMLLECERPALETDQESLIIVPNGRTTTVRHLLSADTKEEREEWCAYLNKALTLLRAWGTTH
Protein: Histone deacetylase 11 (HD11) (EC 3.5.1.98) (Q91WA3)
Organism: Mus musculus (Mouse)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein deacetylase HDAC6
- Nuclear receptor corepressor 2
- NAD-dependent protein deacetylase sirtuin-1
- Transcription initiation factor TFIID subunit 1
- NAD-dependent protein deacetylase sirtuin-7
- Nuclear receptor corepressor 1
- NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
- Histone H2A.Z
- Bromodomain-containing protein 2
- Core histone macro-H2A.2
Sequence:
MPHATQLYQHVPEKRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLKEEKLLSDGMLVEAREASEEDLLVVHTRRYLNELKWSFVVATITEIPPVIFLPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNRHIYPGDRFAKEAIRRKVELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDEVVFRVVRAHDIPILMVTSGGYQKRTARIIADSILNLHDLGLIGPEFPCVSAQNSGIPLLSCAVP
Protein: Delta-amaurobitoxin-Pl1d (Delta-AMATX-Pl1d) (Delta-palutoxin IT4) (Delta-paluIT4) (P83259)
Organism: Pireneitega luctuosa (Tangled nest spider) (Paracoelotes luctuosus)
Function: Binds at site 4 of sodium channels (Nav) and inhibits the fast inactivation of cockroach channels. This toxin is active only on insects (By similarity) Has a potent activity against S.litura larvae.
Subcellular location: Secreted.
Interaction partners:
Sequence:
ACATKNQRCASWAGPYCCDGFYCSCRSYPGCMCRPNS
Protein: Succinate dehydrogenase assembly factor 3, mitochondrial (SDH assembly factor 3) (SDHAF3) (Q9P7Y2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit sdh2 of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF1.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q04401}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Probable succinate dehydrogenase flavoprotein subunit, mitochondrial
Sequence:
MNNITKLMKQKNILTPPLPLYRRVLRAHRYHLGAEERALGDEYVKAEFRRHRNVTNPLHLVGFLSSWERYADALENESWKQEKYSNTDLLESLNDQQIGQLYELSKALQEQKKSE
Protein: Regulator of nonsense transcripts 1 homolog (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent helicase UPF1) (Q9FJR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons (premature termination codon PTC) by associating with the nuclear exon junction complex (EJC) and serving as link between the EJC core and NMD machinery. Eliminates the production of nonsense-containing RNAs (ncRNAs). Required for plant development and adaptation to environmental stresses, including plant defense and response to wounding.
Subcellular location: Cytoplasm. Cytoplasm, P-body. Note=Remobilize from the cytoplasm into processing bodies by SMG7.
Interaction partners:
- Regulator of nonsense transcripts UPF3
- Regulator of nonsense transcripts UPF2
- Nuclear cap-binding protein subunit 1
- Nonsense-mediated mRNA decay factor SMG7
- Nuclear cap-binding protein subunit 2
- mRNA-decapping enzyme subunit 2
- mRNA-decapping enzyme-like protein
- RNA-binding protein Y14
- Eukaryotic translation initiation factor 4G
- Eukaryotic initiation factor 4A-III homolog
Sequence:
MDSQQSDLFDTASQPDTVADEYTFLEFNTQGDSEFDYQDFGSPTAWPTPSDSISIADVADRGEGGAAADHHSEASSPSSLSAGAGNGAKVGRGGVGGSGGVSSSSQVDALAAGVGNLNFEETGDDDGFDYGKNDFTEHACKYCGISNPACVVRCNVASCRKWFCNSRGNTSGSHIVNHLVRAKHKEVCLHRDSPLGETILECYNCGCRNVFLLGFISAKTDSVVVLLCRDPCLNVNALKDMNWDLSQWCPLIDDRCFLPWLVKVPSEQEQLRARQISAQQINKIEELWKTNPDATLEDLEKPGVDDEPQPVQPKYEDAYQYQNVFAPLIKLEADYDKMMKESQSKENLTVRWDIGLNKKRVAYFVFPKEENELRLVPGDELRLRYSGDAVHPSWQSVGHVIKLTAQEEVALELRANQGVPIDVNHGFSVDFVWKSTSFDRMQGAMKNFAVDETSVSGYIYHQLLGHEVEAQMVRNTLPRRFGVPGLPELNASQVNAVKSVLQKPISLIQGPPGTGKTVTSAAIVYHMAKQGQGQVLVCAPSNVAVDQLAEKISATGLKVVRLCAKSREAVSSPVEYLTLHYQVRHLDTSEKSELHKLQQLKDEQGELSSSDEKKYKNLKRATEREITQSADVICCTCVGAADLRLSNFRFRQVLIDESTQATEPECLIPLVLGVKQVVLVGDHCQLGPVIMCKKAARAGLAQSLFERLVTLGIKPIRLQVQYRMHPALSEFPSNSFYEGTLQNGVTIIERQTTGIDFPWPVPNRPMFFYVQLGQEEISASGTSYLNRTEAANVEKLVTAFLKSGVVPSQIGVITPYEGQRAYIVNYMARNGSLRQQLYKEIEVASVDSFQGREKDYIILSCVRSNEHQGIGFLNDPRRLNVALTRARYGIVILGNPKVLSKQPLWNGLLTHYKEHECLVEGPLNNLKQSMVQFQKPRKIYNDRRLFYGGGAGMIGNDNFGSGNPNADRRGSRGRAGGSYLPSGPPNGARPGLHPAGYPIPRVPLSPFPGGPPSQPYAIPTRGPVGAVPHAPQPGNHGFGAGRGTSVGGHLPHQQATQHNVGTIGPSLNFPLDSPNSQPSPGGPLSQPGYGSQAFRDGFSMGGISQDFLADDIKSQGSHDPYNMADFATQASPGGFAVDYATQGAHGAFPGNFMNQNSQGGYSRFSGINDFMSQEYMAHGGQGLFTQAGFIDSSQDDGQQNPYGVNNPNLQSQGLPNSLYSQPFAHYNTQPLNLSGPQQSQPNQSSQNPKHPYNG
Protein: Dynein intermediate light chain dil1 (Q9P3W4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the cytoplasmic dynein which acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (By similarity). Promotes oscillatory nuclear movement and efficient pairing of homologous centromeres during meiotic prophase.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:20404563}. Note=Localized to the leading edge of the horsetail nucleus, where the spindle pole body (SPB) is expected, and to the leading microtubules. In cycling cells, forms foci which distributed asymmetrically during cell division.
Interaction partners:
- Dynein intermediate chain 1
- Dynein heavy chain, cytoplasmic
- Dynein light chain 1
- Twin horsetail protein 2
- Shugoshin-1
- Anaphase-promoting complex subunit hcn1
- Meiotic recombination protein rec24
- Mei4-dependent protein 2
Sequence:
MDELLEKLLNDLKKKEPKACSIICIGEDLDIIQCMNEHGCFSGGSYSELSNDCETVNFRGIAYKCFFTKDQVKVNFWQISHLTGGLFNFLVSQALNEHGLDLLWIIMVVAQTLSALVSFPEKLLNILRNMKTILINTEETVRNRFEESQNKKLVALLDKNSTTLDISSGILLNFTVVLKQLKHALGLHTSVDNSQEFILQFLRTTLLSVPTSSIVSISADPTSWNNLNVLMKYNFMFQKFKPRDFHAQTIQSETMFIPPCWDTISKIQSVNHEFNIALFKQTAKNFYDTLDISLLLGLFDKSISMLNCHSSKISDGDIPYKSHQVFLQELQNKYSEIKTYSSNKLNKSSIKSSLWKDLIQ
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FSU9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome A complete sequence
- Lysophospholipase 1
Sequence:
MKLSIPLLSLAATSVLAAPAVVTVTEVAHEHDVKTVRGVVYVQGGETKTSYTTLDDSTPTSVAEPVQENQVQNNAQAPAPSSSSSPTPAPAPAASPSSSSPAAASPSPSPSPAQDSNLSDFAKSMLNEHNIKRALHQDTNPLTWSDELAQYAQNYANNYDCSGNLVHSGGPYGENLAIGYSPVGSVDAWYDEIKDYNYANPGFSESTGHFTQVVWKSSTKVGCAVKSCGGVWGDYVICSYDPAGNFLGEFAQNVAPLK
Protein: Adenylyltransferase and sulfurtransferase MOCS3 (Molybdenum cofactor synthesis protein 3) (Ubiquitin activating enzyme 4) [Includes: Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (Adenylyltransferase MOCS3) (Sulfur carrier protein MOCS2A adenylyltransferase); Molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) (Sulfur carrier protein MOCS2A sulfurtransferase) (Sulfurtransferase MOCS3)] (Q9VLJ8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln) (By similarity). Also essential during biosynthesis of the molybdenum cofactor (By similarity). Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus (By similarity). The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A (By similarity). Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:29491838}.
Interaction partners:
- Ubiquitin-related modifier 1 homolog
- Molybdopterin synthase catalytic subunit
- Cysteine desulfurase, mitochondrial
- Sulfurtransferase
- Ubiquitin-like modifier-activating enzyme 5
- Cytoplasmic tRNA 2-thiolation protein 1
- Molybdopterin synthase sulfur carrier subunit
- Ubiquitin-fold modifier 1
- Molybdenum cofactor biosynthesis protein 1
- Small ubiquitin-related modifier
Sequence:
MMESEVDSERTMLKREIAELRAALNQKEQCLRELDSLFSFATRPEQEVVGNDLESPDVAVHTKLTNDDIARYSRQLILPDFGVQGQLKLKNSSVLIVGLGGLGCPAAQYLAAAGCGHLGLVDYDEVERSNFHRQILHSEDRCGMSKAESARIALLELNPHCEIQCHSRMLYPHNAMHIIRGYDVVLDCTDNVPTRYLLSDACVMLSKPLVSGSALKMDGQLTVYNYANGPCYRCIFPVPPPPEAVTNCGDGGVLGAVTGTIGAMQALEAIKVIVGMGDVLAGRLLIFDGGSGVFRNIRIRSKRPNCHMCSAQPLITELINYEMFCGMHATDKNNPMLLLSTDERLSVEDYQQKIQAQPHLLIDVRPTAEFEICQLPEAVNVPLVEILDDSYLKRLGKQLEDKELPIVLVCRRGNDSQIAVQHLRNRFPTHFVRDLIGGLHAWTNSVDPSFPIY
Protein: Uncharacterized protein (Q38FM0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSVFPPGRDSQNVVVRSNVGVPSGPDVTLVASAPLLLVSTAAVHSLSGSHSKLKTSHPGLAVRRMFEPQELCAIREDALREYLRMKMADELSDVERMEADARERLVEQALFFFEALATRNVEKCKKLARGRELLYFIERLKDREAIEDQRRYALEEALREEGRAEWRREVEEKAAYGEYLRAFEEWKREQENTVRAACAFVMGTEVRYRRGVVAEESDAWEELWRKEREEREEAERIAYENFYNSPEQVILREERERVEGKLRQKYERQMVRHLKEQEQIVKSCKHGRGNTSIFEGPKASKKCASCGVSFDKDLGYYVRSYGKTIPPPPPLPESMLDSAKPKFAASHMPGTQSGVQPTPVPPPTSEGKLPPIGKKR
Protein: Stromal cell-derived factor 1 (C-X-C motif chemokine 12) (Q6V9B5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Chemokine
- C-X-C chemokine receptor type 4b
- Atypical chemokine receptor 3b
- Atypical chemokine receptor 3a
- Chemokine
- Chemokine
- Stromal cell-derived factor 1
- C-C motif chemokine 21
- Chemokine
- C-X-C motif chemokine 19 precursor
Sequence:
MDSKVVALVALLMLAFWSPETDAKPISLVERCWCRSTLNTVPQRSIREIKFLHTPSCPFQVIAKLKNNREVCINPKTKWLQQYLKNALNKIKKKRSE
Protein: Pseudouridine-5'-phosphatase (EC 3.1.3.96) (Haloacid dehalogenase-like hydrolase domain-containing protein 1) (Haloacid dehalogenase-like hydrolase domain-containing protein 1A) (Protein GS1) (Pseudouridine-5'-monophosphatase) (5'-PsiMPase) (Q08623)
Organism: Homo sapiens (Human)
Function: Dephosphorylates pseudouridine 5'-phosphate, a potential intermediate in rRNA degradation. Pseudouridine is then excreted intact in urine.
Interaction partners:
- Protein-glucosylgalactosylhydroxylysine glucosidase
- Glucose-6-phosphate isomerase
- Alanine--glyoxylate aminotransferase
- Protein YIPF6
- Patatin-like phospholipase domain-containing protein 4
- Steryl-sulfatase
- Mannose-6-phosphate isomerase
- Threonylcarbamoyl-AMP synthase
- Phosphoacetylglucosamine mutase
- Hydroxyacid-oxoacid transhydrogenase, mitochondrial
Sequence:
MAAPPQPVTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEVFPTAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEVQHGKPDPDIFLACAKRFSPPPAMEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPELFGLPSYE
Protein: Melanophilin a (Melanophilin b) (Q05AI5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDKKLDLSRLSEEEAKHVWEVIQRDFVLRKKEEERLGELKTKIEKEEAKRELLGSQSNLSESHCIRCLQPFKFLVNSRRQCVDCKLFTCKTCSRYNKNEHGWVCDPCRMSRVLKIGTLGWYHDNVHSRFKRFGSAKVMRSLYKRLNEEGHRDDDTQSMPDVRNAYNGHDEEHMDASEAQRYKQMRKTKRLLSVHPMDLEIDDYAVHSRRQSVQYIHDDRGQRNDLEYNSEIYHQHQQRMNRRKSLDRFSRPDDGLYSENRMVRARSLSKINSSMAPRQIYLDTSEEEDMYRYPVYQLPPRRRSRASSQENIQQGAPPINELSKRMSAIESLLNRLEEKITVPSDQPALPPAGHMEEEKLRRKLDELMSDKGLSSDEEDPKRAPQYKRSTVRGDQTAMVLASQEPLSSSSDEMPTEAQKVYMTAGKSYEVAKKLQKIEHNAKNHYGGPLTDSELSELEDQVALAVAKVQGTESEVSDIESKLAALSAKGLSIDKAKKKVNRSNN
Protein: Inositol monophosphatase 1 (IMP 1) (IMPase 1) (EC 3.1.3.25) (D-galactose 1-phosphate phosphatase) (EC 3.1.3.94) (Inositol-1(or 4)-monophosphatase 1) (Lithium-sensitive myo-inositol monophosphatase A1) (P29218)
Organism: Homo sapiens (Human)
Function: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17068342}.
Interaction partners:
- Inositol-3-phosphate synthase 1
- Inositol monophosphatase 2
- Inositol polyphosphate 1-phosphatase
- Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol oxygenase
- Myotubularin
- Inositol polyphosphate-4-phosphatase type I A
- Inositol polyphosphate 4-phosphatase type II
- Transcription termination factor 2
Sequence:
MADPWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRTPETVRMVLSNMEKLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDLMSRRVIAANNRILAERIAKEIQVIPLQRDDED