wanglab/gogpt-training-data huggingface dataset:
Protein: Peroxisomal biogenesis factor 11 beta (F7FA09)
Organism: Rattus norvegicus (Rat)
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00046271}.
Interaction partners:
Sequence:
MDAWVRFSAQSQARERLCRCGGGRSAGGRAEAAQYACSLLGHALQRHGASPELQKQIRQLEGHLSLGRKLLRLGNSADALESAKRAVHLSDVVLRFCITVSHLNRALYFACDNVLWAGKSGLAPRVDQEKWAQRSFRYYLFSLIMNLSRDAYEIRLLMEQETSAHSRRMKISGVGVSGLETGGPGGPGTPGGCLPQLALKFRLRILLLARVLRDHPPLLLDVLRNACDLFIPLDKLGLWRCGPGIVGLCGLISSVLSILTLICPWLRLKP
Protein: Frataxin homolog, mitochondrial (EC 1.16.3.1) (O74831)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+). May be able to store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Iron sulfur cluster assembly protein 1, mitochondrial
- Protein isd11
- Probable cysteine desulfurase, mitochondrial
- Ferrochelatase, mitochondrial
- J-type co-chaperone jac1, mitochondrial
- NifU-like protein C1709.19c
- Iron-sulfur cluster assembly factor IBA57
- Iron-sulfur assembly protein 2
- Uncharacterized protein C11D3.10
- Uncharacterized aminotransferase C777.03c
Sequence:
MQSLRAAFRRRTPIFLKPYEFSTNVFGLRCRYYSQVRHNGALTDLEYHRVADDTLDVLNDTFEDLLEEVGKKDYDIQYANGVITLMLGEKGTYVINKQPPAHQIWLSSPVSGPKHYEYSLKSKTWCSTRDEGTLLGILSSEFSKWFSRPIEFKKSEDF
Protein: A-type potassium channel modulatory protein KCNIP2 (Kv channel-interacting protein 2) (KChIP2) (Potassium channel-interacting protein 2) (Q9JJ69)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and KCND3 trafficking to the cell surface. Essential for the expression of I(To) currents in the heart. Required for normal protein levels of KCND2 in the heart ventricle.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9JM59}; Lipid-anchor {ECO:0000250|UniProtKB:Q9JM59}. Note=Detected on lipid rafts (By similarity). {ECO:0000250|UniProtKB:Q9JM59}.
Interaction partners:
- A-type voltage-gated potassium channel KCND3
- A-type voltage-gated potassium channel KCND2
- Voltage-gated potassium channel KCNC1
- Potassium voltage-gated channel subfamily A member 4
- Potassium voltage-gated channel subfamily A member 5
- A-type voltage-gated potassium channel KCND1
- A-type potassium channel modulatory protein DPP6
- Sodium channel protein type 5 subunit alpha
- Potassium voltage-gated channel subfamily B member 1
Sequence:
MRGQGRKESLSDSRDLDGSYDQLTGHPPGPSKKALKQRFLKLLPCCGPQALPSVSETLAAPASLRPHRPRPLDPDSVEDEFELSTVCHRPEGLEQLQEQTKFTRRELQVLYRGFKNECPSGIVNEENFKQIYSQFFPQGDSSNYATFLFNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIYDMMGKYTYPALREEAPREHVESFFQKMDRNKDGVVTIEEFIESCQQDENIMRSMQLFDNVI
Protein: 8-amino-7-oxononanoate synthase 1 (AONS) (EC 2.3.1.47) (7-keto-8-amino-pelargonic acid synthase) (7-KAP synthase) (KAPA synthase) (8-amino-7-ketopelargonate synthase) (P9WQ87)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide (By similarity). Can also use pimeloyl-CoA instead of pimeloyl-ACP as substrate. To a lesser extent, can also utilize D-alanine instead of L-alanine as substrate.
Interaction partners:
- Dethiobiotin synthetase BioD
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- Biotin synthase
- Conserved protein
- Putative 8-amino-7-oxononanoate synthase 2
- Probable hypothetical membrane protein
Sequence:
MKAATQARIDDSPLAWLDAVQRQRHEAGLRRCLRPRPAVATELDLASNDYLGLSRHPAVIDGGVQALRIWGAGATGSRLVTGDTKLHQQFEAELAEFVGAAAGLLFSSGYTANLGAVVGLSGPGSLLVSDARSHASLVDACRLSRARVVVTPHRDVDAVDAALRSRDEQRAVVVTDSVFSADGSLAPVRELLEVCRRHGALLLVDEAHGLGVRGGGRGLLYELGLAGAPDVVMTTTLSKALGSQGGVVLGPTPVRAHLIDAARPFIFDTGLAPAAVGAARAALRVLQAEPWRPQAVLNHAGELARMCGVAAVPDSAMVSVILGEPESAVAAAAACLDAGVKVGCFRPPTVPAGTSRLRLTARASLNAGELELARRVLTDVLAVARR
Protein: Cinnamate reductase (EC 1.3.1.-) (G9F1Y9)
Organism: Clostridium sporogenes (strain ATCC 7955 / DSM 767 / NBRC 16411 / NCIMB 8053 / NCTC 8594 / PA 3679)
Function: Involved in the fermentation of L-phenylalanine via a Stickland reaction. Catalyzes the reduction of (E)-cinnamate to yield 3-phenylpropionate.
Interaction partners:
Sequence:
MKDQYKVLYDPIKIGKLEIKNRYVLAPMGPGGMCNADGSFNKRGIEFYVERAKGGTGLIMTGVTMVENNIEKCALPSMPCPTINPLNFITTGNEMTERVHAYGAKIFLQLSAGFGRVSIPSIVGKVAVAPSKIPHRFLPGVTCRELTTEEVKEYVKAFGESAEIAKKAGFDGVEIHAVHEGYLLDQFAISFFNHRTDEYGGSLENRLRFACEVVQEIKKRCGQDFPVSLRYSIKSFIKDWCKGGLPDEEFEEKGRDIPEGIEAAKILVAAGYDALNGDVGSYDSWYWSHPPMYQKKGLYLPYNEILKKVVDVPIITAGRMEDPELSSDAILSGKTDMIALGRPLLADAEIPNKIFEDKYDKVRPCLSCQEGCMGRLQNFATVSCAVNPACGREKEYGLKKAEQIKKVLIVGGGVAGMEAARVAAIRGHKVTLIEKNGYLGGNIVPGGVPDFKDDDRALVKWYEGILKDLGVEIKLNVAASKENIKEFGADEVLLATGSSPRTLTIEGADKVYSAEDVLMERKNVGEKVIIIGGGLVGCETALWLKQQGKEVTIVEMQNDILQVGGPLCHANHDMLIDLIKFNKIDVKASSYISKKTDEGFVLNTNGEESIINADSAVVAIGYLSEKDLYSEVRFDIPNARLIGDANKVQNIMYAIWSAYEVAKNI
Protein: rRNA N(6)-adenosine-methyltransferase METTL5 (EC 2.1.1.-) (Methyltransferase-like protein 5) (Q9NRN9)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of a heterodimer with TRMT112, which specifically methylates the 6th position of adenine in position 1832 of 18S rRNA. N6-methylation of adenine(1832) in 18S rRNA resides in the decoding center of 18S rRNA and is required for translation and embryonic stem cells (ESCs) pluripotency and differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:31564433}. Presynapse {ECO:0000269|PubMed:31564433}. Postsynapse {ECO:0000269|PubMed:31564433}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112-like protein
- rRNA N
- RNA N
- Zinc finger CCCH domain-containing protein 13
- Protein virilizer homolog
- N
- Pre-mRNA-splicing regulator WTAP
- 5'-deoxynucleotidase HDDC2
- RNA-binding protein 15
- N
Sequence:
MKKVRLKELESRLQQVDGFEKPKLLLEQYPTRPHIAACMLYTIHNTYDDIENKVVADLGCGCGVLSIGTAMLGAGLCVGFDIDEDALEIFNRNAEEFELTNIDMVQCDVCLLSNRMSKSFDTVIMNPPFGTKNNKGTDMAFLKTALEMARTAVYSLHKSSTREHVQKKAAEWKIKIDIIAELRYDLPASYKFHKKKSVDIEVDLIRFSF
Protein: Immunoglobulin superfamily DCC subclass member 3 (Putative neuronal cell adhesion molecule) (Q8BQC3)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAEPRTASPRRLPALRRPGFLPPLLPPPPPPLLLLLLLLPLPAPSLGLGHSAELAFSVEPNDDIANPGQPIVLGCKVEGTPPVQVSWRKNGAELPEGTHTTLLANGSLLIHHFRLEQGGSPSDEGDYECVAQNRFGLLVSRKARLQAATMSDFHVHPQAVTGEEGGVARFQCQIHGLPKPLITWEKNRVPIDTDDERYTLLPKGVLQITGLRAEDSGIFHCVASNIASVRVSHGARLTVSGSGSGTYKEPTILVGPENLTLTVHQTAVLECVATGNPRPIVSWSRLDGRPIGVEGIQVLGTGNLIISDVTVQHSGVYVCAANRPGTRVRRTAQGRLVVQAPAEFVQHPQSISRPAGTTAMFTCQAQGEPPPHVTWLKNGQVLGAGGHVRLKNNNSTLSISGVGPEDEAIYQCVAENIAGSSQASARLTVLWAEGLPGPPRNVRAVSVSSTEVRVSWSEPLAHTKEIIGYVLHIRKAADSPKLEYQEAVSKSTFQHLVRDLEPSTAYSFYIKAYTPRGASLASVPTLASTLGEAPVPPPLSVRLLGSSSLQLLWKPWPRLAQHNGGFKLFYRPVSATSFTGPILLPGTVSSYNLSQLDPSTVYEVKLLAYNQHGDGNATVRFVSLKGASERTALTPPCDCRKEDVTNHTSTTGIVIGIHIGVTCIIFCVLFLLFGQRGRVLLCKDVENQLSPPQGPRSQRDPGILALNGLSRGEGGQLSRDEKPVDAKELEQLFPTAGSAAQPGSTPTDPAAPAPCEETQLSMVQLQGFNLVAGRTTEATSPCAGPGPVPAPQDIGPVPLSEGQTQPPAVAAPQ
Protein: SNF1-related protein kinase regulatory subunit gamma-1-like (AKIN subunit gamma-1-like) (CBS domain-containing protein CBSCBS2) (Q9CAR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, which may play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants.
Interaction partners:
- Cytochrome P450, family 87, subfamily A, polypeptide 7
- Phosphoglucan phosphatase LSF1, chloroplastic
- Transcription initiation factor IIE subunit beta
- Cytochrome P450, family 87, subfamily A, polypeptide 6
- CBS domain-containing protein CBSCBSPB3
- Transcription initiation factor IIE subunit beta
- Thiamine phosphate phosphatase-like protein
- non-specific serine/threonine protein kinase
- Receptor homology region, transmembrane domain- and RING domain-containing protein 5
- Receptor homology region, transmembrane domain- and RING domain-containing protein 4
Sequence:
MAGSEAVEDKEIKSAVSSCEAYFEKVQSRKNLPKSLQETLNSAFAGIPVSSFPQVPGGRVIEIQAETPVSEAVKILSDSKILSAPVINTDHESSLDWRERYLGIIDYSSIILWVLESAELAAIALSATSATAAGVGAGAVGALGVAALGMTGPVAAAGLAAAAVGAAVAGGVAAERGIGKDAPTAADKLGKDFYEVILQEEPFKSTTVRTILKSFRWAPFLPVSTESSMLSVMLLLSKYRLRNVPVIKTGEPDIKNYVTQSAVVHGLEGCKGRDWFDHISALPISDLGLPFMSPNEVISIESEELILEAFKRMRDNNIGGLPVVEGLNKKIVGNISMRDIRYLLLQPEVFSNFRQLTVKSFATKIATAGEEYGLAIPAITCRPDSTLGSVINSLASRSVHRVYVAAGDENELYGVITLRDVISCFVSEPPNYFENCLGFSVKEMLNR
Protein: Furin (EC 3.4.21.75) (Dibasic-processing enzyme) (Paired basic amino acid residue-cleaving enzyme) (PACE) (P09958)
Organism: Homo sapiens (Human)
Function: Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. Converts through proteolytic cleavage the non-functional Brain natriuretic factor prohormone into its active hormone BNP(1-32). By mediating processing of accessory subunit ATP6AP1/Ac45 of the V-ATPase, regulates the acidification of dense-core secretory granules in islets of Langerhans cells (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11331585, ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:8846780, ECO:0000269|PubMed:9130696, ECO:0000269|PubMed:9412467}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:9130696, ECO:0000269|PubMed:9412467}; Single-pass type I membrane protein {ECO:0000305}. Secreted {ECO:0000305|PubMed:11799113}. Endosome membrane {ECO:0000269|PubMed:9412467}; Single-pass type I membrane protein {ECO:0000305}. Note=Shuttles between the trans-Golgi network and the cell surface (PubMed:11799113, PubMed:9412467). Propeptide cleavage is a prerequisite for exit of furin molecules out of the endoplasmic reticulum (ER). A second cleavage within the propeptide occurs in the trans Golgi network (TGN), followed by the release of the propeptide and the activation of furin (PubMed:11799113). {ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:9412467}.
Interaction partners:
- Phosphofurin acidic cluster sorting protein 1
- Disintegrin and metalloproteinase domain-containing protein 17
- Matrix metalloproteinase-14
- Angiotensin-converting enzyme 2
- Transmembrane protease serine 2
- Stromelysin-3
- Collagen alpha-1
- Transforming growth factor beta-1 proprotein
- Beta-secretase 1
- Collagen alpha-1
Sequence:
MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPEVVAGLSCAFIVLVFVTVFLVLQLRSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL
Protein: Nuclear factor 1 B-type (CCAAT-box-binding transcription factor) (Nuclear factor I/B) (TGGCA-binding protein) (Q9QY88)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
LLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALC
Protein: Calpain-1 catalytic subunit (EC 3.4.22.52) (Calcium-activated neutral proteinase 1) (CANP 1) (Calpain mu-type) (Calpain-1 large subunit) (Micromolar-calpain) (muCANP) (P35750)
Organism: Sus scrofa (Pig)
Function: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1. Cleaves and activates caspase-7 (CASP7).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P07384}. Cell membrane {ECO:0000250|UniProtKB:P07384}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250|UniProtKB:P07384}.
Interaction partners:
- Calpain small subunit 1
- Calpain-2 catalytic subunit
- Calpastatin
- Uncharacterized protein.
- BH3-interacting domain death agonist
- Cyclin-dependent kinase 5 activator.
- Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
- Interleukin-1 alpha
Sequence:
MAEEVITPVYCTGVSAQVQKLRAKELGLGRHENAIKYLGQDYEQLRAHCLQSGSLFRDEAFPPVPQSLGFKELGPNSSKTYGVKWKRPTELFSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPTKDGKLVFVHSAQGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYSIILKALERGSLLGCSIDISSVLDMEAVTFKKLVKGHAYSVTGAKQVNYQGQMVNLIRMRNPWGEVEWTGAWSDGSSEWNGVDPYQRDQLRVRMEDGEFWMSFRDFLREFTRLEICNLTPDALKSQRVRNWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLEETDDPEDDYGGRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPVHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKKAGTQELDDQVQAILPDEQVLSEEEIDENFKALFRQLAGEDMEISVRELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLFELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA
Protein: Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma (GMP-PDE gamma) (EC 3.1.4.35) (Q13956)
Organism: Homo sapiens (Human)
Function: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones.
Interaction partners:
- Potassium voltage-gated channel subfamily V member 2
- Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
- Guanylate kinase
- Hypoxanthine-guanine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- GMP synthase
- Adenine phosphoribosyltransferase
- GMP reductase 1
- Guanine nucleotide-binding protein G
- Cyclic nucleotide-gated channel beta-3
Sequence:
MSDNTTLPAPASNQGPTTPRKGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDITVICPWEAFSHLELHELAQFGII
Protein: Protein-tyrosine-phosphatase PTP1 (EC 3.1.3.48) (Protein tyrosine phosphatase 1) (AtPTP1) (O82656)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein-tyrosine-phosphatase that dephosphorylates and probably inhibits MPK6 in non-oxidative stress conditions. In association with MKP1, represses salicylic acid (SA) and camalexin biosynthesis, thus modulating defense response. May also repress MPK3. Dephosphorylates and inactivates MPK4 in vitro.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19789277}. Nucleus {ECO:0000269|PubMed:19789277}.
Interaction partners:
- Mitogen-activated protein kinase 6
- Mitogen-activated protein kinase 4
- Mitogen-activated protein kinase 3
- Protein-tyrosine-phosphatase MKP1
- F14O23.23 protein
- Dual specificity protein phosphatase 1B
- Dual specificity protein phosphatase 1
- Mitogen-activated protein kinase 2
- Mitogen-activated protein kinase 7
- Mitogen-activated protein kinase 12
Sequence:
MATGKTSSAANLFTGSTRFDLSSADSPPSKLSLSSDQLNHCHQALGVFRGKIQNPDSIAHEFTGLQANRMWPSELLLNSTVAMNSVNVEKNRYSDVVPFDKNRIVLNPCKDSSAKGYVNASLIKTSESESISQFIATQGPLPHTMEDFWEMVIQQHCPIIVMLTRLVDNNRTVKCGDYFQDEDGPREFGNISLTTKWIKTTDTSLMLRNLEVNYKETEDQPMSVLHIQYPEWPDHGVPKDTVAVREILKRLYQVPPSLGPIIVHCSAGIGRTGTYCAIHNTIQRILAGDMSALDLAKTVALFRKQRIGMVQTMDQYFFCYNAIVDELEDLTAGTNAGTSS
Protein: Interleukin-15 (IL-15) (P97604)
Organism: Rattus norvegicus (Rat)
Function: Cytokine that stimulates the proliferation of T-lymphocytes. Stimulation by IL15 requires interaction of IL15 with components of the IL2 receptor, including IL2RB and probably IL2RG but not IL2RA (By similarity). In neutrophils, stimulates phagocytosis probably by signaling through the IL15 receptor, composed of the subunits IL15RA, IL2RB and IL2RG, which results in kinase SYK activation (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Interleukin-2 receptor subunit beta
- Interleukin-15 receptor subunit alpha
- Interleukin 2 receptor, gamma, isoform CRA_a.
- Tyrosine-protein kinase JAK3
- Interleukin 9
- Interleukin-7 receptor subunit alpha
- Interleukin-2 receptor subunit alpha
- Interleukin-7
- Interleukin-2
- Interferon gamma
Sequence:
MKILKPYMRNTSILYYLCFLLNSHFLTEAGIHVFILGCVSVGLPKTEANWIDVRYDLEKIESLIQFIHIDTTLYTDSDFHPSCKVTAMNCFLLELQVILHEYSNMTLNETVRNVLYLANSTLSSNKNVIESGCKECEELEERNFTEFLQSFIHIVQMFINTS
Protein: Endopolygalacturonase AN8327 (EC 3.2.1.15) (Pectinase AN8327) (Polygalacturonase AN8327) (Q5ATQ3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Exopolygalacturonase X-2
- Exopolygalacturonase X-1
- Probable endopolygalacturonase D
- Probable exopolygalacturonase Bgalacturonohydrolase B)
- Endopolygalacturonase B
- Pectinesterase A
- NAD binding Rossmann fold oxidoreductase, putative
- Exo-1,4-beta-xylosidase bxlB
- Exo-1,4-beta-xylosidase xlnD
- Alpha-L-arabinofuranosidase B
Sequence:
MFYALGPLALFAFATEVMATPVAYPMTTASPTLAKRDSCTFSGSDGAASASRSQTDCATITLSDITVPSGTTLDLSDLEDDTTVIFEGTTSWEYEEWDGPLLQIKGNGITIKGADGAKLNPDGSRWWDGEGSNGGVTKPKFFYAHDLTDSTIQNLYIENTPVQAVSINGCDGLTITDMTIDNSAGDDAGGHNTDGFDIGESSNVVITGAKVYNQDDCVAVNSGTSITFSGGTCSGGHGLSIGSVGGRDDNTVDTVTFKDSTVSNSVNGIRIKAKSGETGEIKGVTYSGISLESISDYGILIEQNYDGGDLDGEVTSGIPITDLTIENISGSGAVDSDGYNIVIVCGDDACSNWTWSDVEVTGGEDYGSCENVPSVASCST
Protein: Dahlein-4.1 (P84264)
Organism: Ranoidea dahlii (Dahl's aquatic frog) (Litoria dahlii)
Function: Has no antimicrobial activity.
Subcellular location: Secreted {ECO:0000269|PubMed:11555873}.
Interaction partners:
Sequence:
GLWQLIKDKIKDAATGFVTGIQS
Protein: Cytotoxin-associated protein A (B5Z6S0)
Organism: Helicobacter pylori (strain G27)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTNETINQQPQTEAAFNPQQFINNLQVAFLKVDNAVASYDPDQKPIVDKNDRDNRQAFNGISQLREEYSNKAIKNPAKKNQYFSDFIDKSNNLINKDALIDVESSTKSFQKFGDQRYQIFTSWVSHQNDPSKINTRSIRNFMENIIQPPIPDDKEKAEFLKSAKQSFAGIIIGNQIRTDQKFMGVFDESLKERQEAEKNGGPTGGDWLDIFLSFIFDKKQSSDVKEAINQEPVPHVQPDIATTTTDIQGLPPEARDLLDERGNFSKFTLGDMEMLDVEGVADIDPNYKFNQLLIHNNALSSVLMGSHNGIEPEKVSLLYGGNGGPKAKHDWNATVGYKDQQGNNVATIINVHMKNGSGLVIAGGEKGINNPSFYLYKEDQLTGSQRALSQEEIRNKVDFMEFLAQNNAKLDNLSEKEEEKFRNEIKDFQKDSKAYLDALGNDRIAFVSKKDTKHSALITEFGNGDLSYTLKDYGKKADKALDREKNVTLQGNLKHDGVMFVDYSNFKYTNASKNPNKGVGVTNGVSHLEAGFSKVAVFNLPDLNNLAITSLVRRDLEDKLIAKGLSPQETNKLVKDFLSSNKELVGKALNFNKAVAEAKNTGNYDEVKQAQKDLEKSLKKRERLEKEVAKKLESKSGNKNKMEAKSQANSQKDEIFALINKEANREARAITYAQNLKGIKRELSDKLENVNKNLKDFSKSFDEFKNGKNKDFSKSEETLKALKGSVKDLGINPEWISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVIINQKVTDKVDNLNQAVSVAKATGDFSRVEQALADLKNFSKEQLAQQAQKNEDFNTGKNSALYQSVKNGVNGTLVGNGLSKAEATTLSKNFSDIKKELNAKLGNFNNNNNNGLKNSTEPIYAKVNKKKAGQAASPEEPIYAQVAKKVNAKIDRLNQIASGLGVVGQAVGFPLKRHDKVGDLSKVGQSVSPEPIYATIDDLGGPFPLKRHDKVGDLSKVGLSVSPEPIYATIDDLGGPFPLKRHDKVGDLSKVGLSREQQLKQKIDNLSQAVSEAKAGFFGNLEQTIDNLKDSAKNNPVSLWAEGAKKVPASLSAKLDNYATNSHTRINSNIQSGAINEKATGMLTQKNPEWLKLVNDKIVAHNVGSVPLLEYDKIGFNQKSMKDYSDSFKFSTELNNAVKDVKSGFTQFLANAFSTGYYRLAGENAEHGIKNVNTKGGSKNLKGLRNTKNAKTTPC
Protein: Monocarboxylate transporter 10 (MCT 10) (Aromatic amino acid transporter 1) (Solute carrier family 16 member 10) (T-type amino acid transporter 1) (Q8TF71)
Organism: Homo sapiens (Human)
Function: Sodium- and proton-independent thyroid hormones and aromatic acids transporter. Mediates both uptake and efflux of 3,5,3'-triiodothyronine (T3) and 3,5,3',5'-tetraiodothyronine (T4) with high affinity, suggesting a role in the homeostasis of thyroid hormone levels. Responsible for low affinity bidirectional transport of the aromatic amino acids, such as phenylalanine, tyrosine, tryptophan and L-3,4-dihydroxyphenylalanine (L-dopa). Plays an important role in homeostasis of aromatic amino acids (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11827462, ECO:0000269|PubMed:18337592, ECO:0000269|PubMed:28754537}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q91Y77}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Monocarboxylate transporter 8
- Solute carrier organic anion transporter family member 1C1
Sequence:
MVLSQEEPDSARGTSEAQPLGPAPTGAAPPPGPGPSDSPEAAVEKVEVELAGPATAEPHEPPEPPEGGWGWLVMLAAMWCNGSVFGIQNACGVLFVSMLETFGSKDDDKMVFKTAWVGSLSMGMIFFCCPIVSVFTDLFGCRKTAVVGAAVGFVGLMSSSFVSSIEPLYLTYGIIFACGCSFAYQPSLVILGHYFKKRLGLVNGIVTAGSSVFTILLPLLLRVLIDSVGLFYTLRVLCIFMFVLFLAGFTYRPLATSTKDKESGGSGSSLFSRKKFSPPKKIFNFAIFKVTAYAVWAVGIPLALFGYFVPYVHLMKHVNERFQDEKNKEVVLMCIGVTSGVGRLLFGRIADYVPGVKKVYLQVLSFFFIGLMSMMIPLCSIFGALIAVCLIMGLFDGCFISIMAPIAFELVGAQDVSQAIGFLLGFMSIPMTVGPPIAGLLRDKLGSYDVAFYLAGVPPLIGGAVLCFIPWIHSKKQREISKTTGKEKMEKMLENQNSLLSSSSGMFKKESDSII
Protein: Rubredoxin-2 (Rdxs) (Q9HTK8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase.
Subcellular location: Cytoplasm.
Interaction partners:
- Rubredoxin-NAD
- Alkane 1-monooxygenase 1
- Alkane 1-monooxygenase 2
- Luciferase-like domain-containing protein
Sequence:
MRKWQCVVCGFIYDEALGLPEEGIPAGTRWEDIPADWVCPDCGVGKIDFEMIEIA
Protein: ATP-dependent RNA helicase, putative (Q8TZH8)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Interaction partners:
- Replication factor A related protein
- DUF63 domain-containing protein
- Large ribosomal subunit protein uL1
- Fructose-1,6-bisphosphatase
- DNA topoisomerase 1
- Large ribosomal subunit protein eL40
- Elongation factor 2
Sequence:
MMLLRRDLIQPRIYQEVIYAKCKETNCLIVLPTGLGKTLIAMMIAEYRLTKYGGKVLMLAPTKPLVLQHAESFRRLFNLPPEKIVALTGEKSPEERSKAWARAKVIVATPQTIENDLLAGRISLEDVSLIVFDEAHRAVGNYAYVFIAREYKRQAKNPLVIGLTASPGSTPEKIMEVINNLGIEHIEYRSENSPDVRPYVKGIRFEWVRVDLPEIYKEVRKLLREMLRDALKPLAETGLLESSSPDIPKKEVLRAGQIINEEMAKGNHDLRGLLLYHAMALKLHHAIELLETQGLSALRAYIKKLYEEAKAGSTKASKEIFSDKRMKKAISLLVQAKEIGLDHPKMDKLKEIIREQLQRKQNSKIIVFTNYRETAKKIVNELVKDGIKAKRFVGQASKENDRGLSQREQKLILDEFARGEFNVLVATSVGEEGLDVPEVDLVVFYEPVPSAIRSIQRRGRTGRHMPGRVIILMAKGTRDEAYYWSSRQKEKIMQETIAKVSQAIKKQKQTSLVDFVREKESEKTSLDKWLKKEKEEATEKEEKKVKAQEGVKVVVDSRELRSEVVKRLKLLGVKLEVKTLDVGDYIISEDVAIERKSANDFIQSIIDGRLFDQVKRLKEAYSRPIMIVEGSLYGIRNVHPNAIRGAIAAVTVDFGVPIIFSSTPEETAQYIFLIAKREQEEREKPVRIRSEKKALTLAERQRLIVEGLPHVSATLARRLLKHFGSVERVFTASVAELMKVEGIGEKIAKEIRRVITAPYIEDEE
Protein: Clavesin-2 (Retinaldehyde-binding protein 1-like 2) (clathrin vesicle-associated Sec14 protein 2) (Q5SYC1)
Organism: Homo sapiens (Human)
Function: Required for normal morphology of late endosomes and/or lysosomes in neurons (By similarity). Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Early endosome membrane {ECO:0000269|PubMed:19651769}; Peripheral membrane protein {ECO:0000269|PubMed:19651769}.
Interaction partners:
Sequence:
MTHLQAGLSPETLEKARLELNENPDTLHQDIQEVRDMVITRPDIGFLRTDDAFILRFLRARKFHHFEAFRLLAQYFEYRQQNLDMFKSFKATDPGIKQALKDGFPGGLANLDHYGRKILVLFAANWDQSRYTLVDILRAILLSLEAMIEDPELQVNGFVLIIDWSNFTFKQASKLTPSMLRLAIEGLQDSFPARFGGIHFVNQPWYIHALYTVIRPFLKEKTRKRIFLHGNNLNSLHQLIHPEILPSEFGGMLPPYDMGTWARTLLDHEYDDDSEYNVDSYSMPVKEVEKELSPKSMKRSQSVVDPTVLKRMDKNEEENMQPLLSLD