wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin-conjugating enzyme E2 10 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 10) (Ubiquitin carrier protein 10/12) (Ubiquitin-conjugating enzyme E2-17 kDa 10/12) (Ubiquitin-protein ligase 10/12) (P35133)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Mediates the selective degradation of short-lived and abnormal proteins.
Interaction partners:
- E3 ubiquitin-protein ligase UPL4
- E3 ubiquitin-protein ligase UPL3
- Ubiquitin-NEDD8-like protein RUB1
- Ubiquitin-activating enzyme E1 2
- RING-box protein 1a
- Ubiquitin-activating enzyme E1 1
- MND1-interacting protein 1
- E3 ubiquitin-protein ligase CHIP
- Ubiquitin-ribosomal protein eL40y fusion protein
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 1
Sequence:
MASKRILKELKDLQKDPPTSCSAGPVAEDMFHWQATIMGPSESPYAGGVFLVTIHFPPDYPFKPPKVAFRTKVFHPNINSNGSICLDILKEQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHMYKTDKNKYESTARSWTQKYAMG
Protein: Oxygen-dependent coproporphyrinogen-III oxidase (CPO) (Coprogen oxidase) (Coproporphyrinogenase) (EC 1.3.3.3) (P72848)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Involved in the heme and chlorophyll biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00333}.
Interaction partners:
- Uroporphyrinogen decarboxylase
- Oxygen-independent coproporphyrinogen III oxidase
- Protoporphyrinogen IX oxidase
- Ferrochelatase
- Heme chaperone HemW
- Heme oxygenase 1
- Porphobilinogen deaminase
- Glutamate-1-semialdehyde 2,1-aminomutase
- Glutamyl-tRNA reductase
- Delta-aminolevulinic acid dehydratase
Sequence:
MTVSPTTQPQTNHSLPPADAKQRVSQFMQTLQDEICQGLEALDGKGKFQEDSWQREEGGGGRSRVLADGDFLEQGGVNFSEVWGKSLPPSILKQRPEAEGHEFYATGTSMVLHPKNPYIPTVHLNYRYFEAGPVWWFGGGADLTPYYPFAEDAAHFHHTLKNACDQTHGEFYPVFKRWCDEYFYLKHRQEMRGIGGIFFDYQDGNAPLYRGPDPNGPAAQYSNQLAPIEPLGWEDLFSFAQRCGRAFLPAYSPIVEKRRNTEYGDRQRQFQLYRRGRYVEFNLVYDRGTIFGLQTNGRTESILMSLPPLVRWQYCYSPEAGSPEAELTEKFLVPQDWVNS
Protein: LD06392p (R2D2) (R2d2, isoform B) (R2d2, isoform C) (Q9VLW8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Endoribonuclease Dcr-2
- Ribonuclease 3
- Protein argonaute-1
- Endoribonuclease Dcr-1
- Protein argonaute-2
- Transcription initiation factor TFIID subunit 11
- Staphylococcal nuclease domain-containing protein 1
- LD23072p
- Protein Loquacious
- LD07162p
Sequence:
MDNKSAVSALQEFCARTQINLPTYSFIPGEDGGYVCKVELLEIEALGNGRSKRDAKHLAASNILRKIQLLPGIHGLMKDSTVGDLDEELTNLNRDMVKELRDYCVRREMPLPCIEVVQQSGTPSAPEFVACCSVASIVRYGKSDKKKDARQRAAIEMLALISSNSDNLRPDQMQVASTSKLKVVDMEESMEELEALRRKKFTTYWELKEAGSVDHTGMRLCDRHNYFKNFYPTLKKEAIEAINSDEYESSKDKAMDVMSSLKITPKISEVESSSLVPLLSVELNCAFDVVLMAKETDIYDHIIDYFRTMLI
Protein: Uncharacterized protein (Q57Y69)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Trypanosoma glutamic acid/alanine-rich protein domain-containing protein
Sequence:
MVFARGVTLYILVAGLCSIGGKSSSHWGRISRSEYCTTVAKSVRAINTRYANAWHTFEVALKRTSVVKGKCDEDVKKVSDDEITDVADSGKKRVVDEYYNAIMYVGTEIRNYERDLHKLTVYLKDRCGFWLSFMPVTISFKRSIEETTAEATGKVSKIETLSGDAASYAADAANDECSTVEDKRREKEAGAGEDTSGKQNEETSDGPVPESPESPTSMDEQREEKRSTDTAKGDTDSSQEGLGEKTADEEPAVVAEPAVGKEAQAEVD
Protein: Nuclear factor of activated T-cells, cytoplasmic 1 (NF-ATc1) (NFATc1) (NFAT transcription complex cytosolic component) (NF-ATc) (NFATc) (O95644)
Organism: Homo sapiens (Human)
Function: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 or IL-4 gene transcription. Also controls gene expression in embryonic cardiac cells. Could regulate not only the activation and proliferation but also the differentiation and programmed death of T-lymphocytes as well as lymphoid and non-lymphoid cells. Required for osteoclastogenesis and regulates many genes important for osteoclast differentiation and function (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16511445}. Nucleus {ECO:0000269|PubMed:16511445}. Note=Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin-mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. Translocation to the nucleus is increased in the presence of calcium in pre-osteoblasts (By similarity). The subcellular localization of NFATC plays a key role in the regulation of gene transcription (PubMed:16511445). Nuclear translocation of NFATC1 is enhanced in the presence of TNFSF11. Nuclear translocation is decreased in the presence of FBN1 which can bind and sequester TNFSF11 (By similarity). {ECO:0000250|UniProtKB:O88942, ECO:0000269|PubMed:16511445}.
Interaction partners:
- Protein phosphatase 3 catalytic subunit alpha
- Calcineurin subunit B type 1
- Nuclear factor of activated T-cells, cytoplasmic 2
- Transcription factor Jun
- Transcription factor GATA-4
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Transcription factor Sp7
- Tartrate-resistant acid phosphatase type 5
- Glycogen synthase kinase-3 beta
- Mitogen-activated protein kinase 8
Sequence:
MPSTSFPVPSKFPLGPAAAVFGRGETLGPAPRAGGTMKSAEEEHYGYASSNVSPALPLPTAHSTLPAPCHNLQTSTPGIIPPADHPSGYGAALDGGPAGYFLSSGHTRPDGAPALESPRIEITSCLGLYHNNNQFFHDVEVEDVLPSSKRSPSTATLSLPSLEAYRDPSCLSPASSLSSRSCNSEASSYESNYSYPYASPQTSPWQSPCVSPKTTDPEEGFPRGLGACTLLGSPRHSPSTSPRASVTEESWLGARSSRPASPCNKRKYSLNGRQPPYSPHHSPTPSPHGSPRVSVTDDSWLGNTTQYTSSAIVAAINALTTDSSLDLGDGVPVKSRKTTLEQPPSVALKVEPVGEDLGSPPPPADFAPEDYSSFQHIRKGGFCDQYLAVPQHPYQWAKPKPLSPTSYMSPTLPALDWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLMLQLFIGTADDRLLRPHAFYQVHRITGKTVSTTSHEAILSNTKVLEIPLLPENSMRAVIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQPSGRTLSLQVASNPIECSQRSAQELPLVEKQSTDSYPVVGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVHVSFYVCNGKRKRSQYQRFTYLPANVPIIKTEPTDDYEPAPTCGPVSQGLSPLPRPYYSQQLAMPPDPSSCLVAGFPPCPQRSTLMPAAPGVSPKLHDLSPAAYTKGVASPGHCHLGLPQPAGEAPAVQDVPRPVATHPGSPGQPPPALLPQQVSAPPSSSCPPGLEHSLCPSSPSPPLPPATQEPTCLQPCSPACPPATGRPQHLPSTVRRDESPTAGPRLLPEVHEDGSPNLAPIPVTVKREPEELDQLYLDDVNEIIRNDLSSTSTHS
Protein: Histone acetyltransferase (EC 2.3.1.48) (Q9NHW0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU361211}.
Interaction partners:
Sequence:
MALESGSSSSESGSSSTSGSTSSETGSSSDTDSSSATPEEKPSTNSSAKSQTQTQQQTNSGNAQRRKPVPAASEDKPKPSVAPSSKKVNNPPKSKLSSDDDEYEDSAPPAKKNSRAMGSSTVTAAAAASAAWRKPPASVNKPSNPANKPSNPTQRSANNNTNRSLENGEGKRPSLSSSSNSTDDSMKIVKNGRKVPLKMASTVRPKQIRGKLPPAKKNGGGPVISSDGSSGSESGSNSGDESSSGSESEGSDSSNSYSSQPVKGGAKGKRSGPTKIQNSDSEEERKDKANPMRKLTRSLSMRRTKQQPKQETDSESDGDLEDDKIMISKSPAKKPAPSNLNASKSKVKREPIGISSGVLSSIKSRPVSPITETEKKCPIEGCDSSGHLSGNLDKHFLPEACPIYHNMSASECKERANERKLRNEQRLKMPVNIVTAPGNQNTNLKTLSPEQREFLAKIRESRANFKPANNNFLDSKVKLEKDVTDEDREPNLAGLVPDYDLQLFREAQAQASERIEDELKDLPVGKGIKYISMGKYKMKVWYQSPYPDDAARLPKMYICEFCLRYQKSETGIKRHAEKCVWRHPPGDEIYRKGKLQVWQVDGKRYKQYCQHLCLLAKFFLDHKTLYYDVEPFLFYIMTLADVDGCHIVGYFSKHIPFLQEKNSFYNVSCILTLPPYQRKGYGRLLIDFSYLLTRVEGKIGSPEKPLSDLGLISYRSYWKDVLLDYLCNRSGNTIAIKDVSQETAIYSYDIVSTLQALGMMKYWKGKHIVLKKQDVLDEYEERVKRRGTFPKIDDSCLRWQPFINIQPSSSP
Protein: RNA-directed RNA polymerase catalytic subunit (EC 2.7.7.48) (Polymerase basic protein 1) (PB1) (RNA-directed RNA polymerase subunit P1) (P03431)
Organism: Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Function: RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04065, ECO:0000269|PubMed:19906916}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04065, ECO:0000269|PubMed:19906916}.
Interaction partners:
Sequence:
MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGRWTTNTETGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGIFENSCIETMEVVQQTRVDKLTQGRQTYDWTLNRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVMESMKKEEMGITTHFQRKRRVRDNMTKKMITQRTIGKKKQRLNKRSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVYFVETLARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSFTITGDNTKWNENQNPRMFLAMITYMTRNQPEWFRNVLSIAPIMFSNKMARLGKGYMFESKSMKLRTQIPAEMLASIDLKYFNDSTRKKIEKIRPLLIEGTASLSPGMMMGMFNMLSTVLGVSILNLGQKRYTKTTYWWDGLQSSDDFALIVNAPNHEGIQAGVDRFYRTCKLLGINMSKKKSYINRTGTFEFTSFFYRYGFVANFSMELPSFGVSGINESADMSIGVTVIKNNMINNDLGPATAQMALQLFIKDYRYTYRCHRGDTQIQTRRSFEIKKLWEQTRSKAGLLVSDGGPNLYNIRNLHIPEVCLKWELMDEDYQGRLCNPLNPFVSHKEIESMNNAVMMPAHGPAKNMEYDAVATTHSWIPKRNRSILNTSQRGVLEDEQMYQRCCNLFEKFFPSSSYRRPVGISSMVEAMVSRARIDARIDFESGRIKKEEFTEIMKICSTIEELRRQK
Protein: KEOPS complex subunit Cgi121 (Q9UZ62)
Organism: Pyrococcus abyssi (strain GE5 / Orsay)
Function: Component of the KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Cgi121 acts as an allosteric effector that regulates the t(6)A activity of the complex. Cgi121 is not required for tRNA modification.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- KEOPS complex subunit Bud32
- tRNA N6-adenosine threonylcarbamoyltransferase
- KEOPS complex subunit Pcc1
- Hexuronate transporter related protein
Sequence:
MTPKFKNFKHDNSGQVETYLFEVISKYTMLEIKTKFGKLCIAKVKLASESIERALNLCNDNCQIVSAKCHEEVIFATILAIKAFSSGRNTAKTIKGEILLRLAGVKQIKDAIKIIGARKGENLIIYFGVSDPCSSLKDFISSLGLREEPLKPCDEDEVKRGFERAAIIEAL
Protein: Beta-galactosidase A (EC 3.2.1.23) (Lactase A) (Q700S9)
Organism: Penicillium sp
Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. Has high in vitro transglycosylation activity with p-nitrophenyl-beta-D-galactopyranoside, methyl-beta-D-galactopyranoside or lactose as a donor and galactose as an acceptor.
Subcellular location: Secreted {ECO:0000269|PubMed:11053867}.
Interaction partners:
Sequence:
MKLLSSWVVAALAAQAAGAAISHKLDGFTIREHADPAKRALLQKYVTWDEHSIFVNGERLMIFSGEVHPYRLPVASLYIDIFEKVKALGFNCVSFYVDWALLEGNPGHYSAEGIFDLQPFFDAAKEAGIYLLARPGPYINAEVSGGGFPGWLQRVDGILRTSDEAYLKATDNYASNIAATIAKAQITNGGPIILYQPENEYSGACCGYNGFPDGSYMQYIEDHARDAGIVVPFISNDAWAAGHNAPGTGAGAVDIYGHDSYPLGFDCANPSTWPSGNLPTYFHTSHEQQSPSTPYSLVEFQGGAFDPWGGVGFAKCAALLNHEFERVFYKNDFSFGVAFLNLYMIFGGTNWGNLGHPGGYTSYDYGSAISESRNITREKYSELKLLGNFAKVSPGYLVANPGDLSTSTYTNTADLTVTPLLGSNSSASSFFVIRHSDYSSQASVEYKLTVPTSAGNLTIPQLGGSLTLSGRDSKIHVTDYDVAGTNILYSTAEVFTWKKFNNEKVLVLYGGPGEHHEFAVSGASSSSVVEGSSSGISSKKVGKALVVAWDVSTARRIVQVGSLKVFLLDRNSAYNYWVPQVPTKGTAPGYSNQETTASSIIVKAGYLVRSAYLDGNDLHIQADFNATTPIEVVGAPSGAKNLVINGKKTQTKVDKNGIWSASVAYTAPKVQLPSLKSLKWKSVDTLPEAKNTYDDSAWTSADHAYTNNSAHSLQTPTSLFASDYGYHTGALLFRGHFTANGKEKTFFVQTKGGTAYGHSIWINETYVGSWAGTSINDNNNATYTLPTLQSGKNYVITVVIDNMGLDEDWTIGSEDMKNPRGIIQYSLSGQEASAISWKLTGNLGGENYRDTVRGPLNEGGLYAERQGFHQPQPPTQKWDSSSPFTGLTKPGIRFYSTSFDLDLPSGYDIPLYFNFGNSTSTPAAYRVQLYVNGYQYGKYVNNIGPQTSFPVPEGILNYHGTNWLALSLWAQEDNGAKLDSFELINTTPVLTSLGEVKSVNQPKYQARKGAY
Protein: MAS-related G protein-coupled receptor, member X2-like (E9PTZ8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Protachykinin-1
Sequence:
MEERKISDSLQRVDSNILDWETNSTTVNESNHTGMSSCGIMSCTMIFLSLIIAIVVLVGNAIVIWLLGFQMCRNAFSIYILNLAGADFLFIGFQIGYCFYIIFDIYTIPIKLPLFFIVMLNFAYLCGLSILSAVSIERCLCVMRPFWYRCQLPRHTSAVICTMLWVLSLVLSLSEGKECGFLPGTNISDWCKTIDLIITSWLIVLFVVLLVSSLALVITIFCGLYRIPVTRLYVVIVFTVLFFLLFGLPYGIYLFLLVWAETFYYVFPCGFLPVTIFLSCINSCANPIIYFLVGSVRHHRFQRKSLKLLLQQARQDTPETEEYVEMGSLGRSRETVCKGLRAALTRHKF
Protein: Hepatocyte growth factor-regulated tyrosine kinase substrate (Q960X8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential role in endosome membrane invagination and formation of multivesicular bodies, MVBs. Required during gastrulation and appears to regulate early embryonic signaling pathways. Inhibits tyrosine kinase receptor signaling by promoting degradation of the tyrosine-phosphorylated, active receptor, potentially by sorting activated receptors into MVBs. The MVBs are then trafficked to the lysosome where their contents are degraded.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:11832215}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11832215}. Note=Locates to vesicles present in the perinuclear regions of muscle cells and in the periphery of Garland cells of third-instar larvae.
Interaction partners:
- Jak pathway signal transduction adaptor molecule
- Tumor suppressor protein 101
- Epidermal growth factor receptor pathway substrate clone 15, isoform A
- Ubiquitin carboxyl-terminal hydrolase
- Clathrin heavy chain
- Vacuolar protein sorting-associated protein 28 homolog
- Polyubiquitin
- RH72336p
- Ubiquitin-ribosomal protein eS31 fusion protein
- AP-1 complex subunit gamma
Sequence:
MFRSSFDKNLENATSHLRLEPDWPSILLICDEINQKDVTPKNAFAAIKKKMNSPNPHSSCYSLLVLESIVKNCGAPVHEEVFTKENCEMFSSFLESTPHENVRQKMLELVQTWAYAFRSSDKYQAIKDTMTILKAKGHTFPELREADAMFTADTAPNWADGRVCHRCRVEFTFTNRKHHCRNCGQVFCGQCTAKQCPLPKYGIEKEVRVCDGCFAALQRPTSGSGGAKSGPRPADSELPAEYLNSTLAQQVQTPARKTEQELKEEEELQLALALSQSEAEQQKPKLQSLPPAAYRMQQRSPSPEAPPEPKEYHQQPEEATNPELAKYLNRSYWEQRKISESSSMASPSAPSPMPPTPQPQQIMPLQVKSADEVQIDEFAANMRTQVEIFVNRMKSNSSRGRSISNDSSVQTLFMTLTSLHSQQLSYIKEMDDKRMWYEQLQDKLTQIKDSRAALDQLRQEHVEKLRRIAEEQERQRQMQMAQKLDIMRKKKQEYLQYQRQLALQRIQEQEREMQLRQEQQKAQYLMGQSAPPFPYMPPSAVPQHGSPSHQLNNVYNPYAAGVPGYLPQGPAPAPNGHGQFQAIPPGMYNPAIQQPMPPNLQPGGLMQQPAPPGNPQMMPPMPENQFANNPAAILQLPQQHSIAQPPQIPFQPQPQQIPGQQPQQIPGQQPQQIPGQQPQQIPGQQPQQIPVQQPQPQPQMGHVMLQQHQAPPAAQAPPVTEIANNQVQAVAAAPAPPQNEPGPAPVKAEEPATAELISFD
Protein: Plasmepsin I (EC 3.4.23.38) (Aspartic hemoglobinase I) (Plasmepsin 1) (Q7KQM4)
Organism: Plasmodium falciparum (isolate 3D7)
Function: During the asexual blood stage, catalyzes the initial cleavage of native host hemoglobin (Hb) resulting in Hb denaturation; specifically cleaves between Phe-33 and Leu-34 of Hb alpha-chain. Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P39898}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P39898}. Vacuole lumen {ECO:0000250|UniProtKB:P39898}. Vacuole membrane {ECO:0000250|UniProtKB:P39898}. Note=At the beginning of the asexual blood stage, the transmembrane zymogen is transported to the cytostome, an endocytic structure spanning the parasite cell membrane and the parasitophorous vacuole membrane where host proteins such as hemoglobin are endocytosed. Following endocytosis, localizes to the cytostome vacuole membrane to be then delivered to the digestive (or food) vacuole where it is cleaved into the soluble and active enzyme. In trophozoites, localizes to the digestive vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000250|UniProtKB:P39898}.
Interaction partners:
Sequence:
MALSIKEDFSSAFAKNESAVNSSTFNNNMKTWKIQKRFQILYVFFFLLITGALFYYLIDNVLFPKNKKINEIMNTSKHVIIGFSIENSHDRIMKTVKQHRLKNYIKESLKFFKTGLTQKPHLGNAGDSVTLNDVANVMYYGEAQIGDNKQKFAFIFDTGSANLWVPSAQCNTIGCKTKNLYDSNKSKTYEKDGTKVEMNYVSGTVSGFFSKDIVTIANLSFPYKFIEVTDTNGFEPAYTLGQFDGIVGLGWKDLSIGSVDPVVVELKNQNKIEQAVFTFYLPFDDKHKGYLTIGGIEDRFYEGQLTYEKLNHDLYWQVDLDLHFGNLTVEKATAIVDSGTSSITAPTEFLNKFFEGLDVVKIPFLPLYITTCNNPKLPTLEFRSATNVYTLEPEYYLQQIFDFGISLCMVSIIPVDLNKNTFILGDPFMRKYFTVFDYDNHTVGFALAKKKL
Protein: Uncharacterized oxidoreductase Rv2900c (EC 1.-.-.-) (P9WJP9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Sulfur carrier protein FdhD
- Cytochrome bc1 complex cytochrome c subunit
- Elongation factor Tu
- Probable conserved transmembrane protein
- Glutamate synthase large chain
Sequence:
MYVEAVRWQRSAASRDVLADYDEQAVTVAPRKREAAGVRAVMVSLQRGMQQMGALRTAAALARLNQRNGFDCPGCAWPEEPGGRKLAEFCENGAKAVAEEATKRTVTAEFFARHSVAELSAKPEYWLSQQGRLAHPMVLRPGDDHYRPISWDAAYQLIAEQLNGLDSPDRAVFYTSGRTSNEAAFCYQLLVRSFGTNNLPDCSNMCHESSGAALTDSIGIGKGSVTIGDVEHADLIVIAGQNPGTNHPRMLSVLGKAKANGAKIIAVNPLPEAGLIRFKDPQKVNGVVGHGIPIADEFVQIRLGGDMALFAGLGRLLLEAEERVPGSVVDRSFVDNHCAGFDGYRRRTLQVGLDTVMDATGIELAQLQRVAAMLMASQRTVICWAMGLTQHAHAVATIGEVTNVLLLRGMIGKPGAGVCPVRGHSNVQGDRTMGIWEKMPEQFLAALDREFGITSPRAHGFDTVAAIRAMRDGRVSVFMGMGGNFASATPDTAVTEAALRRCALTVQVSTKLNRSHLVHGATALILPTLGRTDRDTRNGRKQLVSVEDSMSMVHLSRGSLHPPSDQVRSEVQIICQLARALFGPGHPVPWERFADDYDTIRDAIAAVVPGCDDYNHKVRVPDGFQLPHPPRDAREFRTSTGKANFAVNPLQWVPVPPGRLVLQTLRSHDQYNTTIYGLDDRYRGVKGGRRVVFINPADIETFGLTAGDRVDLVSEWTDGQGGLQERRAKDFLVVAYSTPVGNAAAYYPETNPLVPLDHTAAQSNTPVSKAIIVRLEPTA
Protein: Plant UBX domain-containing protein 5 (PUX5) (Q7Y175)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cell division control protein 48 homolog A
- Plant UBX domain-containing protein 2
- F13M7.16 protein
- Plant UBX domain-containing protein 11
- Plant UBX domain-containing protein 3
- Cell division control protein 48 homolog E
- Cell division control protein 48 homolog D
- Plant UBX domain-containing protein 1
- Plant UBX domain-containing protein 4
- Plant UBX domain-containing protein 6
Sequence:
MATETNENLINSFIEITSSSREEANFFLESHTWNLDAAVSTFLDNDAAAAAEPNPTGPPPPSSTIAGAQSPSQSHSPDYTPSETSPSPSRSRSASPSSRAAPYGLRSRGGAGENKETENPSGIRSSRSRQHAGNIRTFADLNRSPADGEGSDSDEANEYYTGGQKSGMMVQDPKKVKDVDELFDQARQSAVDRPVEPSRSASTSFTGAARLLSGEAVSSSPQQQQQEQPQRIMHTITFWLNGFTVNDGPLRGFSDPENAAFMNSISRSECPSELEPADKKIPVHVDLVRRGENFTEPPKPKNPFQGVGRTLGASGSGSSSAPQASSAPMNVAPAPSRGLVVDPAAPTTSIQLRLADGTRLVSRFNNHHTVRDVRGFIDASRPGGSKEYQLLTMGFPPKQLTELDQTIEQAGIANAVVIQKF
Protein: LexA repressor (EC 3.4.21.88) (Q1D406)
Organism: Myxococcus xanthus (strain DK1622)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
- Protein RecA
- Protein RecA
- DNA repair protein RecN
- Methyltransferase
- DNA polymerase IV
Sequence:
MEELTERQREILSFIVKETETRGFPPTIREIGEHMDIRSTNGVNDHLKALERKGYLNRGEQQSRSLVATKRARLLLGLGARKDSGMVEIPLLGKVAAGAPLLAQENMEDSVKIDSFLLGGVNGREVFALRVKGQSMIDDGIHDGDYLFVKKTPSAQPGEIVVALIEDEATVKRYYPEGDRIRFQPANATMQPIYVSRAEFRSTMILGQVVGVYRKLQGGRTP
Protein: Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (PHK-gamma-M) (EC 2.7.11.19) (Phosphorylase kinase subunit gamma-1) (Serine/threonine-protein kinase PHKG1) (EC 2.7.11.1, EC 2.7.11.26) (Q16816)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 (By similarity).
Interaction partners:
- Phosphorylase b kinase regulatory subunit beta
- Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
- Phosphorylase b kinase regulatory subunit alpha, liver isoform
- Calmodulin-1
- Glycogen phosphorylase, muscle form
- Phosphorylase b kinase gamma catalytic chain, liver/testis isoform
Sequence:
MTRDEALPDSHSAQDFYENYEPKEILGRGVSSVVRRCIHKPTSQEYAVKVIDVTGGGSFSPEEVRELREATLKEVDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKRGELFDYLTEKVTLSEKETRKIMRALLEVICTLHKLNIVHRDLKPENILLDDNMNIKLTDFGFSCQLEPGERLREVCGTPSYLAPEIIECSMNEDHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDYSDTVKDLVSRFLVVQPQNRYTAEEALAHPFFQQYLVEEVRHFSPRGKFKVIALTVLASVRIYYQYRRVKPVTREIVIRDPYALRPLRRLIDAYAFRIYGHWVKKGQQQNRAALFENTPKAVLLSLAEEDY
Protein: Integrin subunit alpha 9 (A0A8I6GL49)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MGLSKTCAAWVLVGAPKADSKYSTSVKSPGAVFKCRVHTNPDRRCTELDMARERNRGESCGKTCRGDRDDEWMGVSLARQPKADGRVLACAHRWKNIYYETDHILPHGFCYLIPSNLQAKGRMLIPCYEEYKKKYGEEHGSCQAGIAGFFTEELVIMGAPGSFYWAGTLKVLNLTDNTYFKLNDDAIMNRRYTYLGYAVTAGHFSHPSVTDVVGGAPQDEGIGKVYIFRADRRSGTLIKIFQASGKKMGSYFGSSLCAVDLNMDGLSDLLVGAPMFSEIRDEGQVTVYLNQGHGVLEEQLTLTGDAAYNAHFGESIASLGDLDDDGFPDVAVGAPMEDDFAGTVYIYHGDAQGIVPQYSMKLSGRKINPILQMFGQSISGGIDMDGNGYPDVTVGAFLSDSVVLLRARPVITVDVSIFLPGSINITAPQCHDGQQPVNCLNVTVCFRFHGKNVPGEIGLNYNLTADVAQKEKGQLPRVYFVLLGETAGQVSERLQLTHMDEVCHHYVAHVKRRVQDVISPIVFEAAYSLGEHVIGEEDRELPDLTPVLRWKKGQRIAQKNQTVFERNCRSEDCAADLQLRGKLLLSSVDEKTTHLALGAVKNISLNISISNLGDDAYDANVSFNVSRELFFINMWQKEEMGISCELLESDFLKCSVGFPFMRSKSKYEFSVIFDTSHLSGEEEILSFIVTAQSGNMERSEALHDNTLTLTIPLVHEVDTSITGIVSPTSFVYGESVDASNFIQLDDQECHFQPVNITLQVYNMGPSTLPGSSVSISFPSRLSPGGAEMFQVQDMVVSQEKGNCSLQRNPTPCIIPQEQENIFHTIFAFFSKSGRKVLDCEKTGSFCLTLHCNLSALPKEESRAIDLYMLLNTEILKKDSSSVIQFMARAKVKVEPALRVVEIANGNPEETLVVFEALHNLEPRGYVVGWIIAISLLVGILIFLLLAVLLWKMGFFRRRYKEIIEAEKNRKENEEAWDWVQKNQ
Protein: Serine/threonine receptor-like kinase NFP (RLK NFP) (Nod factor perception protein) (EC 2.7.10.-) (Nod-factor receptor 5) (Q0GXS4)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: During nodulation, plays a central role in nodule organogenesis. Involved in the perception of Nod factors, the first step of recognition of rhizobia prior to nodulation. Necessary in epidermal cells to induce cortical cell divisions leading to nodule primordia formation. Required during root nodule symbiosis with Sinorhizobium meliloti by triggering infection threads and release of bacteria into the cytoplasm of cells in the infection zone of developing nodules, especially in cells derived from the meristem. Promotes plant fitness (e.g. fruit weight and leaf number).
Subcellular location: Cell membrane {ECO:0000269|PubMed:25351493}; Single-pass membrane protein {ECO:0000255}. Vacuole lumen {ECO:0000269|PubMed:25351493}. Note=Removed from the plasma membrane upon the release of rhizobia into the host cytoplasm. Vacuolar localization is observed in cells undergoing breakdown of the receptors. {ECO:0000269|PubMed:25351493}.
Interaction partners:
- Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase DMI-3
- Protein NODULATION SIGNALING PATHWAY 1
- Early nodulin-11
- Protein NODULATION SIGNALING PATHWAY 2
- LysM domain receptor-like kinase 3
- Protein VAPYRIN
- histidine kinase
- Myosin heavy chain-like protein, putative
- histidine kinase
Sequence:
MSAFFLPSSSHALFLVLMLFFLTNISAQPLYISETNFTCPVDSPPSCETYVAYRAQSPNFLSLSNISDIFNLSPLRIAKASNIEAEDKKLIPDQLLLVPVTCGCTKNHSFANITYSIKQGDNFFILSITSYQNLTNYLEFKNFNPNLSPTLLPLDTKVSVPLFCKCPSKNQLNKGIKYLITYVWQDNDNVTLVSSKFGASQVEMLAENNHNFTASTNRSVLIPVTSLPKLDQPSSNGRKSSSQNLALIIGISLGSAFFILVLTLSLVYVYCLKMKRLNRSTSSSETADKLLSGVSGYVSKPTMYEIDAIMEGTTNLSDNCKIGESVYKANIDGRVLAVKKIKKDASEELKILQKVNHGNLVKLMGVSSDNDGNCFLVYEYAENGSLEEWLFSESSKTSNSVVSLTWSQRITIAMDVAIGLQYMHEHTYPRIIHRDITTSNILLGSNFKAKIANFGMARTSTNSMMPKIDVFAFGVVLIELLTGKKAMTTKENGEVVILWKDFWKIFDLEGNREERLRKWMDPKLESFYPIDNALSLASLAVNCTADKSLSRPTIAEIVLCLSLLNQPSSEPMLERSLTSGLDAEATHVVTSVIAR