wanglab/gogpt-training-data huggingface dataset:
Protein: Queuine tRNA-ribosyltransferase accessory subunit 2 (Queuine tRNA-ribosyltransferase domain-containing protein 1) (Q9H974)
Organism: Homo sapiens (Human)
Function: Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03043}. Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03043}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03043}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03043}. Note=May associate with the mitochondrion outer membrane. {ECO:0000255|HAMAP-Rule:MF_03043}.
Interaction partners:
- Queuine tRNA-ribosyltransferase catalytic subunit 1
Sequence:
MKLSLTKVVNGCRLGKIKNLGKTGDHTMDIPGCLLYTKTGSAPHLTHHTLHNIHGVPAMAQLTLSSLAEHHEVLTEYKEGVGKFIGMPESLLYCSLHDPVSPCPAGYVTNKSVSVWSVAGRVEMTVSKFMAIQKALQPDWFQCLSDGEVSCKEATSIKRVRKSVDRSLLFLDNCLRLQEESEVLQKSVIIGVIEGGDVMEERLRSARETAKRPVGGFLLDGFQGNPTTLEARLRLLSSVTAELPEDKPRLISGVSRPDEVLECIERGVDLFESFFPYQVTERGCALTFSFDYQPNPEETLLQQNGTQEEIKCMDQIKKIETTGCNQEITSFEINLKEKKYQEDFNPLVRGCSCYCCKNHTRAYIHHLLVTNELLAGVLLMMHNFEHYFGFFHYIREALKSDKLAQLKELIHRQAS
Protein: Esculentin-1ISb (F1T150)
Organism: Odorrana ishikawae (Ishikawa's frog) (Rana ishikawae)
Function: Has antimicrobial activity against Gram-negative bacterium E.coli ATCC 8739 (MIC=3.1 ug), against Gram positive bacteria S.aureus ATCC 6538 (MIC=3.1 ug), methicillin-resistant S.aureus ATCC 43300 (MIC=12.5 ug), B.subtilis ATCC 6633 (MIC=12.5 ug) and against fungus C.albicans ATCC 90028 (MIC=50 ug).
Subcellular location: Secreted {ECO:0000305|PubMed:21193000}.
Interaction partners:
Sequence:
MFTLKKPLLLIVLLGIISLSLCEQERAADEDEGTKIKRRIFSKIGGKAIKNLILKGIKNIGKEVGMDVIRTGIDVAGCKIKGEC
Protein: Potassium voltage-gated channel subfamily E member 1 (Delayed rectifier potassium channel subunit IsK) (mISK) (IKs producing slow voltage-gated potassium channel subunit beta Mink) (Minimal potassium channel) (MinK) (P23299)
Organism: Mus musculus (Mouse)
Function: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. Assembled with KCNQ1/KVLQT1 is proposed to form the slowly activating delayed rectifier cardiac potassium (IKs) channel. The outward current reaches its steady state only after 50 seconds. Assembled with KCNH2/HERG may modulate the rapidly activating component of the delayed rectifying potassium current in heart (IKr).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P15382, ECO:0000250|UniProtKB:P15383}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P15382}. Apical cell membrane {ECO:0000250|UniProtKB:P15383}. Membrane raft {ECO:0000250|UniProtKB:P15382}. Note=Colocalizes with KCNB1 at the plasma membrane (By similarity). Targets to the membrane raft when associated with KCNQ1 (By similarity). {ECO:0000250|UniProtKB:P15382, ECO:0000250|UniProtKB:P15383}.
Interaction partners:
- Potassium voltage-gated channel subfamily KQT member 1
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Potassium voltage-gated channel subfamily E member 3
- Voltage-gated inwardly rectifying potassium channel KCNH2
- Sodium channel protein type 5 subunit alpha
- A-type voltage-gated potassium channel KCND2
- Potassium voltage-gated channel subfamily E regulatory beta subunit 5
- Potassium voltage-gated channel subfamily E member 4
- Potassium voltage-gated channel subfamily KQT member 4
Sequence:
MSLPNSTTVLPFLARLWQETAEQGGNVSGLARKSQLRDDSKLEALYILMVLGFFGFFTLGIMLSYIRSKKLEHSHDPFNVYIESDAWQEKGKAVFQARVLESFRACYVIENQAAVEQPATHLPELKPLS
Protein: Testis-expressed protein 264 homolog (E9Q137)
Organism: Mus musculus (Mouse)
Function: Major reticulophagy (also called ER-phagy) receptor that acts independently of other candidate reticulophagy receptors to remodel subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. The ATG8-containing isolation membrane (IM) cradles a tubular segment of TEX264-positive ER near a three-way junction, allowing the formation of a synapse of 2 juxtaposed membranes with trans interaction between the TEX264 and ATG8 proteins. Expansion of the IM would extend the capture of ER, possibly through a 'zipper-like' process involving continued trans TEX264-ATG8 interactions, until poorly understood mechanisms lead to the fission of relevant membranes and, ultimately, autophagosomal membrane closure. Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: acts by bridging VCP/p97 to covalent DNA-protein cross-links (DPCs) and initiating resolution of DPCs by SPRTN.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y6I9}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:Q9Y6I9}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9Y6I9}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y6I9}. Nucleus {ECO:0000250|UniProtKB:Q9Y6I9}. Chromosome {ECO:0000250|UniProtKB:Q9Y6I9}. Note=Is trafficked from tubular ER to growing autophagosomes via its cytosolic LIR motif. Also found in the cytosol, nucleus and chromatin. In response to formation of covalent DNA-protein cross-links (DPCs), localizes to the nuclear periphery, and associates with DNA replication forks. {ECO:0000250|UniProtKB:Q9Y6I9}.
Interaction partners:
- Cell cycle progression protein 1
- Atlastin-3
- Translocation protein SEC62
- Reticulophagy regulator 1
- Reticulon-3
- Gamma-aminobutyric acid receptor-associated protein
Sequence:
MPDLLLLGLIGALTLLLLLTLLAFAGYSGLLTGVTVSAGSPPIRNITVAYKFHVGSYGDTGHLFTESCSISPKLRSIAVYYDNPHTVPPEKCRCAVGSILSEGEESPSPELIHLYQKFGFKIFSFPAPSHVVIATFPYTTPISIWLAARRVHPALDTYIKERKLCAHPRLEIYHQDKIHFMCPLARQGDFYVPEVKETERKCRELAEATDTQTDGTGADTSDASSVSLDVRPGSRETSATTLSPGAGNRGWDDGDNRSEHSYSESGASGSSFEELDLEGEGPLGEPRLNPEAKLLGPPRELSTPERGEE
Protein: Protein shisa-like-2A (Q6UWV7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSGACTSYVSAEQEVVRGFSCPRPGGEAAAVFCCGFRDHKYCCDDPHSFFPYEHSYMWWLSIGALIGLSVAAVVLLAFIVTACVLCYLFISSKPHTKLDLGLSLQTAGPEEVSPDCQGVNTGMAAEVPKVSPLQQSYSCLNPQLESNEGQAVNSKRLLHHCFMATVTTSDIPGSPEEASVPNPDLCGPVP
Protein: 3-(3-hydroxydecanoyloxy)decanoate synthase (EC 2.3.1.-) (Q51559)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Required for rhamnolipid surfactant production. Supplies the acyl moieties for rhamnolipid biosynthesis by competing with the enzymes of the type II fatty acid synthase (FASII) cycle for the beta-hydroxyacyl-acyl carrier protein (ACP) pathway intermediates. Catalyzes the formation of one molecule of beta-hydroxydecanoyl-beta-hydroxydecanoate from two molecules of beta-hydroxydecanoyl-ACP. Is the only enzyme required to generate the lipid component of rhamnolipid. In vitro results establish that RhlA is highly selective for 10-carbon acyl-ACP intermediates and thus functions as the molecular ruler that controls the acyl chain composition of rhamnolipids. Cannot use beta-hydroxydecanoyl-CoA as substrate. Rhamnolipid production plays an important role in swarming motility.
Interaction partners:
- Rhamnosyltransferase chain B
- HTH-type quorum-sensing regulator RhlR
- Acyl-homoserine-lactone synthase
- Rhamnosyltransferase 2
- Protease LasA
- Elastase
- Phenazine biosynthesis protein PhzA1
- Anthranilate--CoA ligase
- ATP-dependent RNA helicase RhlB
- Acyl-homoserine-lactone synthase
Sequence:
MRRESLLVSVCKGLRVHVERVGQDPGRSTVMLVNGAMATTASFARTCKCLAEHFNVVLFDLPFAGQSRQHNPQRGLITKDDEVEILLALIERFEVNHLVSASWGGISTLLALSRNPRGIRSSVVMAFAPGLNQAMLDYVGRAQALIELDDKSAIGHLLNETVGKYLPQRLKASNHQHMASLATGEYEQARFHIDQVLALNDRGYLACLERIQSHVHFINGSWDEYTTAEDARQFRDYLPHCSFSRVEGTGHFLDLESKLAAVRVHRALLEHLLKQPEPQRAERAAGFHEMAIGYA
Protein: Carene synthase, chloroplastic (PaJF67) (PaTPS-3car) (EC 4.2.3.107) ((+)-car-3-ene synthase) (3-carene cyclase) (Q84SM8)
Organism: Picea abies (Norway spruce) (Picea excelsa)
Function: Terpene synthase (TPS) involved in defensive oleoresin formation in conifers in response to insect attack or other injury.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
MSVISILPLASKSCLYKSLMSSTHELKALCRPIATLGMCRRGKSVMASKSTSLTTAVSDDGVQRRIGDHHSNLWDDNFIQSLSSPYGASSYGERAERLIGEVKEIFNSLSRTDGELVSHVDDLLQHLSMVDNVERLGIDRHFQTEIKVSLDYVYSYWSEKGIGSGRDIVCTDLNTTALGFRILRLHGYTVFPDVFEHFKDQMGRIACSDNHTERQISSILNLFRASLIAFPGEKVMEEAEIFSATYLKEALQTIPVSSLSQEIQYVLQYRWHSNLPRLEARTYIDILQENTKNQMLDVNTKKVLELAKLEFNIFHSLQQNELKSVSRWWKESGFPDLNFIRHRHVEFYTLVSGIDMEPKHCTFRLSFVKMCHLITVLDDMYDTFGTIDELRLFTAAVKRWDPSTTECLPEYMKGVYTVLYETVNEMAQEAQKSQGRDTLSYVRQALEAYIGAYHKEAEWISSGYLPTFDEYFENGKVSSGHRIATLQPTFMLDIPFPHHVLQEIDFPSKFNDFACSILRLRGDTRCYQADRARGEEASCISCYMKDNPGSTQEDALNHINNMIEETIKKLNWELLKPDNNVPISSKKHAFDINRGLHHFYNYRDGYTVASNETKNLVIKTVLEPVPM
Protein: Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag] (P03348)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
Function: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi).
Subcellular location: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000250|UniProtKB:P12493}.
Interaction partners:
Sequence:
MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGHIARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSYKGRPGNFLQSRPEPTAPPFLQSRPEPTAPPEESFRSGVETTTPSQKQEPIDKELYPLTSLRSLFGNDPSSQ
Protein: Enoyl-CoA hydratase, mitochondrial (mECH) (mECH1) (EC 4.2.1.17) (EC 5.3.3.8) (Enoyl-CoA hydratase 1) (ECHS1) (Short-chain enoyl-CoA hydratase) (SCEH) (Q8BH95)
Organism: Mus musculus (Mouse)
Function: Converts unsaturated trans-2-enoyl-CoA species ((2E)-enoyl-CoA) to the corresponding (3S)-3-hydroxyacyl-CoA species through addition of a water molecule to the double bond. Catalyzes the hydration of medium- and short-chained fatty enoyl-CoA thioesters from 4 carbons long (C4) up to C16 (By similarity). Has high substrate specificity for crotonyl-CoA ((2E)-butenoyl-CoA) and moderate specificity for acryloyl-CoA, 3-methylcrotonyl-CoA (3-methyl-(2E)-butenoyl-CoA) and methacrylyl-CoA ((2E)-2-methylpropenoyl-CoA). Can bind tiglyl-CoA (2-methylcrotonoyl-CoA), but hydrates only a small amount of this substrate (By similarity). Plays a key role in the beta-oxidation spiral of short- and medium-chain fatty acid oxidation. At a lower rate than the hydratase reaction, catalyzes the isomerase reaction of trans-3-enoyl-CoA species (such as (3E)-hexenoyl-CoA) to trans-2-enoyl-CoA species (such as (2E)-hexenoyl-CoA), which are subsequently hydrated to 3(S)-3-hydroxyacyl-CoA species (such as (3S)-hydroxyhexanoyl-CoA) (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P14604}.
Interaction partners:
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- 3-hydroxyacyl-CoA dehydrogenase type-2
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Peroxisomal acyl-coenzyme A oxidase 3
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MAALRALLPRACSSLLSSVRCPELRRFASGANFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEQDPAVGAIVLTGGDKAFAAGADIKEMQNRTFQDCYSSKFLSHWDHITRVKKPVIAAVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKIFPVEKLVEEAIQCAEKIASNSKIVVAMAKESVNAAFEMTLTEGNKLEKRLFYSTFATDDRREGMTAFVEKRKANFKDH
Protein: Nucleoporin NIC96 (96 kDa nucleoporin-interacting component) (Nuclear pore protein NIC96) (P34077)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NIC96, which is localized to the core of the NPC and the distal ring of the nuclear basket, is required for de novo assembly of NPCs. It is involved in nuclear GSP1 import.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
Interaction partners:
- Nucleoporin NUP192
- Nucleoporin NUP157
- Nucleoporin NUP53
- Nucleoporin NUP133
- Nucleoporin NUP170
- Nucleoporin NUP85
- Nucleoporin NUP57
- Nucleoporin NUP2
- Nucleoporin NUP188
- Nucleoporin NUP84
Sequence:
MLETLRGNKLHSGTSKGANKKLNELLESSDNLPSASSELGSIQVSINELRRRVFQLRSKNKASKDYTKAHYLLANSGLSFEDVDAFIKDLQTNQFLEPNPPKIIESEELEFYIRTKKEENILMSIEQLLNGATKDFDNFINHNLNLDWAQHKNEVMKNFGILIQDKKTVDHKKSISSLDPKLPSWGNKGNNILNSNESRLNVNENNILREKFENYARIVFQFNNSRQANGNFDIANEFISILSSANGTRNAQLLESWKILESMKSKDINIVEVGKQYLEQQFLQYTDNLYKKNMNEGLATNVNKIKSFIDTKLKKADKSWKISNLTVINGVPIWALIFYLLRAGLIKEALQVLVENKANIKKVEQSFLTYFKAYASSKDHGLPVEYSTKLHTEYNQHIKSSLDGDPYRLAVYKLIGRCDLSRKNIPAVTLSIEDWLWMHLMLIKEKDAENDPVYERYSLEDFQNIIISYGPSRFSNYYLQTLLLSGLYGLAIDYTYTFSEMDAVHLAIGLASLKLFKIDSSTRLTKKPKRDIRFANILANYTKSFRYSDPRVAVEYLVLITLNEGPTDVELCHEALRELVLETKEFTVLLGKIGRDGARIPGVIEERQPLLHVRDEKEFLHTITEQAARRADEDGRIYDSILLYQLAEEYDIVITLVNSLLSDTLSASDLDQPLVGPDDNSETNPVLLARRMASIYFDNAGISRQIHVKNKEICMLLLNISSIRELYFNKQWQETLSQMELLDLLPFSDELSARKKAQDFSNLDDNIVKNIPNLLIITLSCISNMIHILNESKYQSSTKGQQIDSLKNVARQCMIYAGMIQYRMPRETYSTLINIDVSL
Protein: Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (Q7YZX3)
Organism: Onchocerca volvulus
Interaction partners:
Sequence:
MPITRVHARPIYDSRGNPTVEVDLTTEKGIFRAAVPSGASTGIHEALELRDNDEAVNHGKGVLQAVGNVNEQIGPALVAKNFCPTQQREIDLFMLQLDGTENKAKLGANAILGVSLAVCKAGAVHKGMPLYKYIAELAGTRQIVLPVPAMNVINGGSHAGNKLAMQEFMIMPVGASSFSEAMRMGSEIYHYLKAEIEKRYGLDATAVGDEGGFAPNIQDNKEGLDLLNTAIATAGYTGKVSIAMDCAASEYSKEADKLYDLKFKNPNSGKTQWKTGDQMMNFQSFIKEYPVVSIEDWFHEDDWHNWPKGLAKTNIQIVGDDLTVPNPKRIALAAEKKACNCLLLKVNQIGSVTESIDAANLARKNGWGVMVSHRSGETEDTFIADLVVGLAAGQIKTGAPCRSERLAKYNQILRIEEELGSAAVYAGQKFRNPQA
Protein: Spexin (NPQ) (Neuropeptide Q) (Spexin hormone) [Cleaved into: Spexin-1; Spexin-2] (D3Z752)
Organism: Mus musculus (Mouse)
Function: Plays a role as a central modulator of cardiovascular and renal function and nociception. Also plays a role in energy metabolism and storage. Inhibits adrenocortical cell proliferation with minor stimulation on corticosteroid release (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:24550067}. Secreted, extracellular space {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Note=Secreted via the classical ER/Golgi-dependent pathway into the extracellular medium largely as a full-length protein without the signal peptide, and not as a hydrolyzed and amidated peptide. Localized extracellularly surrounding the villous trophoblastic cells (By similarity). Detected in the serum. {ECO:0000250}.
Interaction partners:
- Galanin receptor type 2
- Galanin receptor type 3
- Galanin peptides
- Galectin-2
- ATP-dependent clpX-like chaperone, mitochondrial
Sequence:
MKGPSVLAVTAVVLLLVLSALENSSGAPQRLSEKRNWTPQAMLYLKGAQGRRFLSDQSRRKELADRPPPERRNPDLELLTLPEAAALFLASLEKSQKDEGGNFDKSELLEDRLFNW
Protein: Core binding factor beta subunit isoform 1 (Core binding factor beta subunit isoform 8) (Core-binding factor subunit beta) (A0A0B4P4A4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPRVVPDQRSKFENEEFFRKLSRECEIKYTGFRDRPHEERQARFQNACRDGRSEIAFVATGTNLSLQFFPANLHGDQRQAPTREYVDFERETGKVYLKAPMILNGVCVIWRGWLDLHRLDGMGCLEYDDERAQHEDALAQAAFEEARRRTRDFEDRDRSHREDLEQMPMAQLNHLITQEDPVASKIWD
Protein: Metal transporter Nramp1 (AtNramp1) (Q9SAH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High affinity manganese (Mn) transporter involved in Mn acquisition from the soil. Required for Mn uptake into the root in conditions of low Mn availability. Can transport iron (Fe), cadmium (Cd) and cobalt (Co).
Subcellular location: Cell membrane {ECO:0000269|PubMed:20228245}; Multi-pass membrane protein {ECO:0000269|PubMed:20228245}.
Interaction partners:
- Fe
- Putative cadmium/zinc-transporting ATPase HMA4
- Ferric reduction oxidase 2
- Metal tolerance protein 11
- Solute carrier family 40 member 1
- Putative metal tolerance protein C3
- Vacuolar iron transporter 1
- Metal tolerance protein 1
- Protein DETOXIFICATION 43
- Probable ferric reduction oxidase 1
Sequence:
MAATGSGRSQFISSSGGNRSFSNSPLIENSDSNQIIVSEKKSWKNFFAYLGPGFLVSIAYIDPGNFETDLQAGAHYKYELLWIILVASCAALVIQSLAANLGVVTGKHLAEQCRAEYSKVPNFMLWVVAEIAVVACDIPEVIGTAFALNMLFSIPVWIGVLLTGLSTLILLALQKYGVRKLEFLIAFLVFTIAICFFVELHYSKPDPGEVLHGLFVPQLKGNGATGLAISLLGAMVMPHNLFLHSALVLSRKIPRSASGIKEACRFYLIESGLALMVAFLINVSVISVSGAVCNAPNLSPEDRANCEDLDLNKASFLLRNVVGKWSSKLFAIALLASGQSSTITGTYAGQYVMQGFLDLRLEPWLRNLLTRCLAIIPSLIVALIGGSAGAGKLIIIASMILSFELPFALVPLLKFTSCKTKMGSHVNPMAITALTWVIGGLIMGINIYYLVSSFIKLLIHSHMKLILVVFCGILGFAGIALYLAAIAYLVFRKNRVATSLLISRDSQNVETLPRQDIVNMQLPCRVSTSDVD
Protein: GTP cyclohydrolase MptA (EC 3.5.4.39) (GTP cyclohydrolase I) (GCYH-I) (GTP cyclohydrolase IV) (D4GWJ7)
Organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Function: Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin (By similarity). Involved in archaeosine (G(+)) and folate biosynthesis.
Interaction partners:
- Probable GTP 3',8-cyclase
- Pyruvate kinase
- 6-carboxy-5,6,7,8-tetrahydropterin synthase
- CobW domain protein
- Nucleoside diphosphate kinase
- Adenylate cyclase domain protein
- PtpS family protein
Sequence:
MSHQLPDVQASQPDVTVGLSQVGVTGVEKLVKIARDGKRPLVLMAEFEVFVDLPGGRKGIDMSRNMQVIDEVLEAAVSEPAYRVEDMCGDAAERLLAKHEYTTTAEVSMTAELVVREDTPASGLSTQSTAEIIASATATDEGTREEIGAEVVGMTVCPCSQGMSASRARDVLQDLAVDDDTIEEFLDKVPQPGHSQRGHATLTVETQGSPEVDLMDLIDIARDSMSARIYNLAKRPDEDHMTYHAHANAKFVEDCVRSMAELSLEALDHLGDDAVVHMKQSNDESIHQHNAHAEREVTLGQLRDELDA
Protein: Troponin I, cardiac muscle (Cardiac troponin I) (P02646)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
Sequence:
ADESRDAAGEARPAPAPVRRRSSANYRAYATEPHAKSKKKISASRKLQLKTLMLQIAKQELEREAEERRGEKGRALSTRCQPLELAGLGFAELQDLCRQLHARVDKVDEERYDVEAKVTKNITEIADLTQKIFDLRGKFKRPTLRLRVRISADAMMQALLGTRAKETLDLRAHLKQVKKEDTEKENREVGDWRKNIDLLSGMEGRKKKFEG
Protein: Cytosolic sulfotransferase 12 (AtSOT12) (EC 2.8.2.-) (Sulfotransferase 1) (AtST1) (P52839)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the stereospecific sulfate conjugation of 24-epibrassinosteroids. Preferred substrates are 24-epicathasterone and 6-deoxo-24-epicathasterone. Low activity with 22-deoxy-24-epiteasterone. No activity with 24-epimers catasterone and brassinolide. Sulfonates salicylic acid. May be involved in detoxification. Enhances plant response to pathogen infection and contributes to long distance signaling in systemic acquired resistance (SAR).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Ubiquinol oxidase 1a, mitochondrial
- Sulfotransferase
- Calcium-binding site protein
- NAC domain-containing protein 13
- RNA-binding KH domain-containing protein RCF3
- RNA polymerase II C-terminal domain phosphatase-like 1
- NAC domain-containing protein 17
- Protein DETOXIFICATION 6
- Cystatin/monellin superfamily protein
Sequence:
MSSSSSVPAYLGDEDLTQETRALISSLPKEKGWLVSEIYEFQGLWHTQAILQGILICQKRFEAKDSDIILVTNPKSGTTWLKALVFALLNRHKFPVSSSGNHPLLVTNPHLLVPFLEGVYYESPDFDFSSLPSPRLMNTHISHLSLPESVKSSSCKIVYCCRNPKDMFVSLWHFGKKLAPEETADYPIEKAVEAFCEGKFIGGPFWDHILEYWYASRENPNKVLFVTYEELKKQTEVEMKRIAEFLECGFIEEEEVREIVKLCSFESLSNLEVNKEGKLPNGIETKTFFRKGEIGGWRDTLSESLAEEIDRTIEEKFKGSGLKFSS
Protein: RNA helicase (EC 3.6.4.13) (A0A0G2K7X6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRHSTAFLGWVFCLLFPFVLTQMNSLQIKEEKVKADTNGVIKTSTTAEKTEEEEKEDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPADRHPQCLCLSPTYELALQTGKVIEQMGKFHPELKLAYAVRGNKLERGQKVGEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDGNPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNILNRIQEHFNKKIERLDTDDLDEIEKIAN
Protein: Leukocyte antigen CD37 (CD antigen CD37) (Q61470)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P11049}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P11049}.
Interaction partners:
- B-lymphocyte antigen CD19
- CD63 antigen
- CD82 antigen
- Tetraspanin-32
- Leukocyte surface antigen CD53
- B-cell receptor CD22
Sequence:
MSAQESCLSLIKYFLFVFNLFFFVLGGLIFCFGTWILIDKTSFVSFVGLSFVPLQTWSKVLAVSGVLTMALALLGCVGALKELRCLLGLYFGMLLLLFATQITLGILISTQRVRLERRVQELVLRTIQSYRTNPDETAAEESWDYAQFQLRCCGWQSPRDWNKAQMLKANESEEPFVPCSCYNSTATNDSTVFDKLFFSQLSRLGPRAKLRQTADICALPAKAHIYREGCAQSLQKWLHNNIISIVGICLGVGLLELGFMTLSIFLCRNLDHVYDRLARYR
Protein: Fibril biogenesis regulator DifC (Q1CXR2)
Organism: Myxococcus xanthus (strain DK1622)
Interaction partners:
- Methyl-accepting chemotaxis protein DifA
- Chemotaxis protein CheA
- histidine kinase
- Chemotaxis protein CheW
- Chemotaxis protein CheW
- Fibril biogenesis regulator DifD
- histidine kinase
- Fibril biogenesis regulator DifG
- Chemotaxis protein CheW
- Chemotaxis coupling protein CheW
Sequence:
MRHVIFRVEKERYGLPLSAVREVVVPPERFTRVPRAPLAITGVMNLRGRVVTVVELRQLLSLPEGPTPPGRVVLLDRGRRDLGLLVTDVDGIEAVERVSTAPGKMTPAIRGVARLGGLGVTVLDPEGLDAAVVALFTHSK