wanglab/gogpt-training-data huggingface dataset:
Protein: Interferon-induced GTP-binding protein Mx3 (RBTMx3) (Q91197)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Does not inhibit strain RB-1 of the fish pathogen, infectious hematopoietic necrosis virus (IHNV).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9188599}. Note=Displays diffuse uniform expression throughout the cytoplasm. {ECO:0000269|PubMed:9188599}.
Interaction partners:
Sequence:
MNNTLNQHYEEKVRPCIDLIDSLRSLGVEKDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLELKMKRKREGEEWHGKISYQDHEEEIEDPSDVEKKIREAQDEMAGVGVGISDDLISLEIGSPDVPDLTLIDLPGIARVAVKGQPENIGEQIKRLIRKFIMKQETINLVVVPCNVDIATTEALQMAQEVDPEGERTLGILTKPDLVDKGTEETVVDIVHNEVIHLTKGYMIVKCRGQKEIMERVSLTEATEREKAFFKEHAHLSTLYDEGHATIPKLAEKLTLELVHHIEKSLPRLEEQIEAKLSETHAELERYGTGPPEDSAERIYFLIDKVTAFTQDAINLSTGEELKSGVRLNVFSTLRQEFGKWKLHLDRSGENFNQRIEGEVSNYEKTYRGRELPGFINYKTFEVMVKDQIKQLEEPAVKKLKEISDAVRKVFLLLAQSSFTGFPNLLKSAKTKIEAIKQVNESTAESMLRTQFKMEMIVYTQDSTYSHSLSERKREEEDDRPLPTPKIRSTIFSTDNHATLQEMMLHLKSYYRISSQRLADQIPMVIRYLVLQEFASQLQREMLQTLQEKDNIEQLLKEDFDIGSKRAALQNKLKRLMKARSYLVEF
Protein: Muscleblind like splicing regulator 1 (H7C4T5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATNASAAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPDTHNICRTSD
Protein: Geranylgeranyl transferase type-1 subunit beta (EC 2.5.1.59) (Geranylgeranyl transferase type I subunit beta) (A0A1D8PSW8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Sequence:
MNQLLINKHEKFFNRCLIGLPSTAQSEDSNKLAIIYFCLHGLQLIQKFQFTNQELIYYRNFIINQFMIENNQIISFRSTYYFQKTNQKYDCPNLSSTLFALYNLLILKSPYHTIINRKKIMNFLCKCQVKDGINKGGFVPTLYYNEENGDYKQYGEPDLRVCYMALLIRHLMKYDDNNNNNNREDSNETDIDLISLQQFILDRININGGFSSTIMDESHLGFTFCAIASLKLLNYPLEKLKSTKEWLIHRQVDYPENLYPKDGNGDNYEYYRNIDIGGFNGRENKLSDTCYSWWCTGSLYNIDVNFIKLVDLNKAEDYLLNKTQNQLFGGFGRDPDSTPDPMHSYLALASLSLWNHEKFALQEINPILTITKESYQFFKEKIKY
Protein: Modulator of apoptosis 1 (MAP-1) (MAP1) (Paraneoplastic antigen Ma4) (Q96BY2)
Organism: Homo sapiens (Human)
Function: Retrotransposon-derived protein that forms virion-like capsids (By similarity). Acts as an effector of BAX during apoptosis: enriched at outer mitochondria membrane and associates with BAX upon induction of apoptosis, facilitating BAX-dependent mitochondrial outer membrane permeabilization and apoptosis. Required for death receptor-dependent apoptosis. When associated with RASSF1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation. Also promotes autophagy: promotes phagophore closure via association with ATG8 proteins. Acts as an inhibitor of the NFE2L2/NRF2 pathway via interaction with SQSTM1: interaction promotes dissociation of SQSTM1 inclusion bodies that sequester KEAP1, relieving inactivation of the BCR(KEAP1) complex.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19100260}. Mitochondrion outer membrane {ECO:0000269|PubMed:16199525}. Extracellular vesicle membrane {ECO:0000250|UniProtKB:Q9ERH6}. Note=Forms virion-like extracellular vesicles that are released from cells. {ECO:0000250|UniProtKB:Q9ERH6}.
Interaction partners:
- Ras association domain-containing protein 1
- Ras association domain-containing protein 6
- Ras association domain-containing protein 5
- E3 ubiquitin-protein ligase TRIM39
- Paraneoplastic antigen Ma1
- THO complex subunit 1
Sequence:
MTLRLLEDWCRGMDMNPRKALLIAGISQSCSVAEIEEALQAGLAPLGEYRLLGRMFRRDENRKVALVGLTAETSHALVPKEIPGKGGIWRVIFKPPDPDNTFLSRLNEFLAGEGMTVGELSRALGHENGSLDPEQGMIPEMWAPMLAQALEALQPALQCLKYKKLRVFSGRESPEPGEEEFGRWMFHTTQMIKAWQVPDVEKRRRLLESLRGPALDVIRVLKINNPLITVDECLQALEEVFGVTDNPRELQVKYLTTYQKDEEKLSAYVLRLEPLLQKLVQRGAIERDAVNQARLDQVIAGAVHKTIRRELNLPEDGPAPGFLQLLVLIKDYEAAEEEEALLQAILEGNFT
Protein: Calnexin (O02393)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
Sequence:
MAWKMGGNRAATLALLFASSLLLLSSANAADLDTESDDFEDGYVEDVQEEPAVIGGDEKLAYESPVIDAKKFHFADHFDDVEESRKRWVLSQAKKDDIAEEISKYDGIWNWESPQRIVWANDLGLVLKSKAKHAAIAAPLRKPFEFKSDKPLVVQYEVTLQEGQECGGSYLKLLSAGKDTEQLKAFNDKTPYTIMFGPDKCGNDVKMHFIFRHVNPINGTITEKHCNKPKNRLEEPFKDKLPHLYQLVVRPDNSFEIRVDHKIINEGSLLTDFKPPVNPPAEIDDPNDHKPESWDEREKIPDPTAHKPEDWDEDAPPQLPDTDAVMPNGWLEDEPDMIFDPTATKPEDWDAEIDGEWEAPLVDNPVCEKAPGCGKWKAPLIPNPNYKGKWRAPMIENPNYQGKWAPRKIPNPDFFEDLKPFQMTPISAVGLELWSMSSDILFDNLIITDDVEVARDFAANSFDIKRRYIDRESDSFVNKVVELAKANPSIWGIGLVAIVALVALTIYCRFGTAKSQDSAAKKAAAEAKKSDDPQPDDEPEAEEESDERAAGDTSKESTPLSASPKKNQKSDLDDNEEESKAAESREPAQTEESNTKTRKRQARKE
Protein: Endonuclease or glycosyl hydrolase (Q9M1Q4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSTNSASDGDFGTNSVPAEMAEAQYVRAKTSVWWDIENCQVPNGLDAHGIAQNITSALQKMNYCGPVSISAYGDTNRIPLTIQHALNSTGIALNHVPAGVKDASDKKILVDMLFWALDNPAPANFMLISGDRDFSNALHGLRMRRYNVLLAQPLKASVPLVHAAKTVWLWTSLSAGGIPLTRAESLQLVANQTTPKPGSEIPSSQPLDSNSDSRRVFDNKSKVKYVPKPSNHQPNNNYRQQQQNTQGKQFKKAPHEFFGTSEPSVSTSRPPPPNLPSSNVNTFPGNVMTNPQNQNQYTYPPRPGPFPPRQPYPNTDPSWNNGNSIPNHAQNYYPNAARPGAATMRPPYGNVFRPYRPENLNPPVGNGFRPMQHPRNDGPRFPSPPLLTPLDISNLSVSQYPSQTQNRPNFNPQVRQEFRPKMESSYTHNGPNKSYIPRCSSAPVTQSTTTTAHTYPSSPGVPPSQPPMVTGSGSSNDRWGTQECPPPSEYVQGLIGVILHALHILKTEKVMPTEPNISDCIQYGDPKHHGTDVKKALESALEHHMIMMTNVGKLKLYIGKNEALWNCVNPLGANAKQYPKETWDRIQQFLTSSSGRVEFTATTCRYEAAQVLKKECLKEFTLGDILQILNITATTKKWITHHQTGWKPITISLAAETTNETATEADPGIQTVA
Protein: Vacuolar protein sorting-associated protein VTA1 homolog (Dopamine-responsive gene 1 protein) (DRG-1) (LYST-interacting protein 5) (LIP5) (SKD1-binding protein 1) (SBP1) (Q9NP79)
Organism: Homo sapiens (Human)
Function: Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR (By similarity). Involved in HIV-1 budding.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15644320}. Endosome membrane {ECO:0000305|PubMed:15644320}; Peripheral membrane protein {ECO:0000305|PubMed:15644320}.
Interaction partners:
- Vacuolar protein sorting-associated protein 4B
- Charged multivesicular body protein 5
- Vacuolar protein sorting-associated protein 4A
- Charged multivesicular body protein 1b
- Charged multivesicular body protein 1a
- IST1 homolog
- Charged multivesicular body protein 2a
- Pre-mRNA-splicing factor SPF27
- GTP cyclohydrolase 1
- Lysosomal-trafficking regulator
Sequence:
MAALAPLPPLPAQFKSIQHHLRTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKTPECRKFLSKLMDQLEALKKQLGDNEAITQEIVGCAHLENYALKMFLYADNEDRAGRFHKNMIKSFYTASLLIDVITVFGELTDENVKHRKYARWKATYIHNCLKNGETPQAGPVGIEEDNDIEENEDAGAASLPTQPTQPSSSSTYDPSNMPSGNYTGIQIPPGAHAPANTPAEVPHSTGVASNTIQPTPQTIPAIDPALFNTISQGDVRLTPEDFARAQKYCKYAGSALQYEDVSTAVQNLQKALKLLTTGRE
Protein: Baseplate protein X (Gene X protein) (GpX) (P51772)
Organism: Escherichia phage P2 (Bacteriophage P2)
Function: Might be involved in the peptidoglycan digestion during virus entry into the host cell.
Subcellular location: Virion {ECO:0000305}. Note=Localizes to the baseplate at the junction of the tail tube. {ECO:0000269|PubMed:24097944}.
Interaction partners:
Sequence:
MKTFALQGDTLDAICVRYYGRTEGVVETVLAANPGLAELGAVLPHGTAVELPDVQTAPVAETVNLWE
Protein: 3-hydroxyisobutyryl-CoA hydrolase-like protein 3, mitochondrial (EC 3.1.2.-) (Q9T0K7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- Probable enoyl-CoA hydratase 1, peroxisomal
- Emb|CAB68146.1
- Probable 3-hydroxyisobutyrate dehydrogenase-like 3, mitochondrial
- Probable 3-hydroxyisobutyrate dehydrogenase-like 2, mitochondrial
- Probable 3-hydroxyisobutyrate dehydrogenase-like 1, mitochondrial
- Acetyl-CoA acetyltransferase 1
- Acetyl-CoA acetyltransferase 2
- Ketose-bisphosphate aldolase class-II family protein
- 2-oxoisovalerate dehydrogenase subunit beta 1, mitochondrial
Sequence:
MIIIKTLSHRIFFPKFSQTFSSQFHQTLRFSISDRRKFSAMAGAGVDDFVKGNVFPNGVALITLDRTKALNAMNLDMDIKYKSFLDEWESDPRVKCVIVEGSTSRAFCAGMDIKGVAAEIQKDKNTPLVQKVFTAEYTLICAIAAYKKPYISLMDGITMGFGLGLSGHGRYRVITERTVLAMPENGIGLFPDVGFSYIAAHSPGGGSVGAYLGLTGKRISAPSDALFVGLGTHYVPSEKLASLKEAILSANLSEDPNQDIQATLSKYSSNPESEAHLKSLLPHIESAFSSNKSIKETIEELKKYQQSTESSVVEWANEALKGLEKGAPFSLYLTQKYFSNVACAKSKPENELATLNGVMKTEYRIALRSALRGDFAEGVRAVLIDKDQNPKWNPTSIEEVDENEVEALFKPLSPEVEELKV
Protein: Carbohydrate sulfotransferase 6 (Corneal N-acetylglucosamine-6-O-sulfotransferase) (C-GlcNAc6ST) (hCGn6ST) (EC 2.8.2.21) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4-beta) (GST4-beta) (N-acetylglucosamine 6-O-sulfotransferase 5) (GlcNAc6ST-5) (Gn6st-5) (Q9GZX3)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues of keratan. Cooperates with B4GALT4 galactosyltransferase and B3GNT7 N-acetylglucosaminyltransferase to construct and elongate the sulfated disaccharide unit [->3Galbeta1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate polymer. Involved in biosynthesis of keratan sulfate in cornea, with an impact on proteoglycan fibril organization and corneal transparency. Involved in sulfation of endothelial mucins such as GLYCAM1.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Lumican
- Sulfotransferase 1C3
- Sulfotransferase 1B1
- Sulfotransferase 1C4
- Keratocan
Sequence:
MWLPRVSSTAVTALLLAQTFLLLFLVSRPGPSSPAGGEARVHVLVLSSWRSGSSFVGQLFNQHPDVFYLMEPAWHVWTTLSQGSAATLHMAVRDLVRSVFLCDMDVFDAYLPWRRNLSDLFQWAVSRALCSPPACSAFPRGAISSEAVCKPLCARQSFTLAREACRSYSHVVLKEVRFFNLQVLYPLLSDPALNLRIVHLVRDPRAVLRSREQTAKALARDNGIVLGTNGTWVEADPGLRVVREVCRSHVRIAEAATLKPPPFLRGRYRLVRFEDLAREPLAEIRALYAFTGLSLTPQLEAWIHNITHGSGPGARREAFKTSSRNALNVSQAWRHALPFAKIRRVQELCAGALQLLGYRPVYSEDEQRNLALDLVLPRGLNGFTWASSTASHPRN
Protein: Protein crumbs homolog 3 (Q9BUF7)
Organism: Homo sapiens (Human)
Function: Involved in the establishment of cell polarity in mammalian epithelial cells. Regulates the morphogenesis of tight junctions. Involved in promoting phosphorylation and cytoplasmic retention of transcriptional coactivators YAP1 and WWTR1/TAZ which leads to suppression of TGFB1-dependent transcription of target genes such as CCN2/CTGF, SERPINE1/PAI1, SNAI1/SNAIL1 and SMAD7 (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:12527193, ECO:0000269|PubMed:12771187, ECO:0000269|PubMed:14718572}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000269|PubMed:12527193}. Note=Localizes primarily to the apical membrane with a small fraction in the upper part of tight junctions of epithelial cells. {ECO:0000269|PubMed:14718572}.
Interaction partners:
- InaD-like protein
- Protein PALS1
- Partitioning defective 6 homolog beta
- Partitioning defective 6 homolog alpha
- Protein crumbs homolog 2
- Partitioning defective 6 homolog gamma
- Ubiquitin-protein ligase E3A
- Band 4.1-like protein 5
- Protein lin-7 homolog C
- LLGL scribble cell polarity complex component 2
Sequence:
MANPGLGLLLALGLPFLLARWGRAWGQIQTTSANENSTVLPSSTSSSSDGNLRPEAITAIIVVFSLLAALLLAVGLALLVRKLREKRQTEGTYRPSSEEQVGARVPPTPNLKLPPEERLI
Protein: Phospholipase B-like protein A (EC 3.1.1.-) (Q550U9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Phospholipase that removes both fatty-acid chains from phosphatidylcholine and produces the water-soluble glycerophosphorylcholine. In addition to phosphatidylcholine deacylation, it also hydrolyzes phosphatidylinositol and phosphatidylethanolamine.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRVIRSLLLLTIAIIGSVLSQSSIDDGYTVFYSQPDNYYVKPGTFSNGVAQAIFSNEMMTTGWSFMSISSSEGLYPNDIIAAGAGYLEGYISQEMIYQNWMNMYNNEYHNVIGSDVENWIQENLQYLQTMIDSAPSNDLYWQNVETVLTQITYMQRGYNQSVIDNGVDASQSLGITEFFLMNMDGDMIDLGPALNLTNGKQVTSPATATSPKQAFKEFMRRTGHCSALIKMTDDLSDLFSGHTTWSSYYEMVRMFKVYNLKYLFNGQPPASKVTMFSGYPGTLSSIDDFYLLDTKIVVIETTNGLMNNNLYHLITSESVLSWIRVIVANRLATGGESWCQTFSLYNSGTYNNQWIIVDYNKFIKGYGALDGTLYILEQVPDYVEYGDQTAILRTGYWPSFNIPFYENIYGLTGFNETYAQFGNWFSYQASPRSMIFKRDANNIHSLTQFQAMLRYNNWQNDPFSQGNAGNQISSRFDLVTADDPNNQYLDPDAFGGIDSKVVSADMVAALLVNAQSGPSHDNETPFTWNSQWNQKYTYAGQPTTWNFDWMTMSLQSMKPASPSSDSSSDSTTFN
Protein: Thiol:disulfide interchange protein DsbC (P0AEG6)
Organism: Escherichia coli (strain K12)
Function: Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD.
Subcellular location: Periplasm {ECO:0000269|PubMed:8168498}.
Interaction partners:
- Thiol:disulfide interchange protein DsbD
- Thiol:disulfide interchange protein DsbA
- Disulfide bond formation protein B
- Thiol:disulfide interchange protein DsbE
- FKBP-type peptidyl-prolyl cis-trans isomerase FkpA
- Thioredoxin reductase
- Tryptophan biosynthesis protein TrpCF
- Glutathione reductase
- Divalent-cation tolerance protein CutA
- Chaperone SurA
Sequence:
MKKGFMLFTLLAAFSGFAQADDAAIQQTLAKMGIKSSDIQPAPVAGMKTVLTNSGVLYITDDGKHIIQGPMYDVSGTAPVNVTNKMLLKQLNALEKEMIVYKAPQEKHVITVFTDITCGYCHKLHEQMADYNALGITVRYLAFPRQGLDSDAEKEMKAIWCAKDKNKAFDDVMAGKSVAPASCDVDIADHYALGVQLGVSGTPAVVLSNGTLVPGYQPPKEMKEFLDEHQKMTSGK
Protein: Leucine-rich repeat protein kinase family protein (Receptor-like protein kinase) (Q9M2R4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MQFLRLLTLLVSSYFFFFINFSSSLNPDGLSLLALKSAILRDPTRVMTSWSESDPTPCHWPGIICTHGRVTSLVLSGRRLSGYIPSKLGLLDSLIKLDLARNNFSKPVPTRLFNAVNLRYIDLSHNSISGPIPAQIQSLKNLTHIDFSSNLLNGSLPQSLTQLGSLVGTLNLSYNSFSGEIPPSYGRFPVFVSLDLGHNNLTGKIPQIGSLLNQGPTAFAGNSELCGFPLQKLCKDEGTNPKLVAPKPEGSQILPKKPNPSFIDKDGRKNKPITGSVTVSLISGVSIVIGAVSISVWLIRRKLSSTVSTPEKNNTAAPLDDAADEEEKEGKFVVMDEGFELELEDLLRASAYVVGKSRSGIVYRVVAGMGSGTVAATFTSSTVVAVRRLSDGDATWRRKDFENEVEAISRVQHPNIVRLRAYYYAEDERLLITDYIRNGSLYSALHGGPSNTLPSLSWPERLLIAQGTARGLMYIHEYSPRKYVHGNLKSTKILLDDELLPRISGFGLTRLVSGYSKLIGSLSATRQSLDQTYLTSATTVTRITAPTVAYLAPEARASSGCKLSQKCDVYSFGVVLMELLTGRLPNASSKNNGEELVRVVRNWVKEEKPLSEILDPEILNKGHADKQVIAAIHVALNCTEMDPEVRPRMRSVSESLGRIKSD
Protein: Protein NrfD (P32709)
Organism: Escherichia coli (strain K12)
Function: Probably involved in the transfer of electrons from the quinone pool to the type-c cytochromes.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Protein NrfC
- Cytochrome c-552
- Cytochrome c-type protein NrfB
- Formate-dependent nitrite reductase complex subunit NrfG
- Probable cytochrome c-type biogenesis protein NrfE
- Formate-dependent nitrite reductase complex subunit NrfF
- Ferredoxin-type protein NapH
Sequence:
MTQTSAFHFESLVWDWPIAIYLFLIGISAGLVTLAVLLRRFYPQAGGADSTLLRTTLIVGPGAVILGLLILVFHLTRPWTFWKLMFHYSFTSVMSMGVMLFQLYMVVLVLWLAKIFEHDLLALQQRWLPKLGIVQKVLSLLTPVHRGLETLMLVLAVLLGAYTGFLLSALKSYPFLNNPILPVLFLFSGISSGAAVALIAMAIRQRSNPHSTEAQFVHRMEIPVVWGEIFLLVAFFVGLALGDDGKVRALVAALGGGFWTWWFWLGVAGLGLIVPMLLKPWVNRSSGIPAVLAACGASLVGVLMLRFFILYAGQLTVA
Protein: V-type proton ATPase proteolipid subunit (F4HZ57)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Vacuole membrane {ECO:0000256|ARBA:ARBA00004128, ECO:0000256|RuleBase:RU363060}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128, ECO:0000256|RuleBase:RU363060}.
Interaction partners:
Sequence:
MASSGFSGDETAPFFGFLGAAAALVFSCMGAAYGTAKSGVGVASMGVMRPELVMKSIVPVVMAGVLGIYGLIIAVIISTGINPKAKSYYLFDGYAHLSSGLACGLAGLSAGMAIGIVGDAGVRVVDCNPDSKIKIYSFTTSFLSNLSQKELFIDLLSANAQQPKLFVGMILILIFAEALALYGLIVGIILSSRAGQSRAE
Protein: Chromosome transmission fidelity protein 18 homolog (Q8BIW9)
Organism: Mus musculus (Mouse)
Function: Chromosome cohesion factor involved in sister chromatid cohesion and fidelity of chromosome transmission. Component of one of the cell nuclear antigen loader complexes, CTF18-replication factor C (CTF18-RFC), which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. The CTF18-RFC complex binds to single-stranded and primed DNAs and has weak ATPase activity that is stimulated by the presence of primed DNA, replication protein A (RPA) and by proliferating cell nuclear antigen (PCNA). The CTF18-RFC complex catalyzes the ATP-dependent loading of PCNA onto primed and gapped DNA. Interacts with and stimulates DNA polymerase POLH. During DNA repair synthesis, involved in loading DNA polymerase POLE at the sites of local damage.
Subcellular location: Nucleus. Note=Associates with chromatin during S phase. {ECO:0000250}.
Interaction partners:
- Sister chromatid cohesion protein DCC1
- Chromosome transmission fidelity protein 8 homolog
- Replication factor C subunit 2
- Replication factor C subunit 5
- Replication factor C subunit 4
- DNA polymerase epsilon catalytic subunit A
- Replication factor C subunit 3
- ATP-dependent DNA helicase DDX11
- DNA polymerase alpha catalytic subunit
- DNA polymerase delta catalytic subunit
Sequence:
MEDYEEDLYGVEDDFQNQFAAELEVLAELEGTRDQAPPGTLQTPASRPPLTFEEAIAGGDTVPRPCPAGSPGNVNRNTRKNVRRDQPAPSSPMVKRPRLDVVKKLNFEPDMEELLYPDSPPGDITPPPSPEVFPEMLDAGYSDANADKDLMQTLPSPRNRNPVLRRPPILEDYINVTSTSGERAFLVLRADLIGPGVQNPLLDVHWRGCGQLDLLGVPFASLKEQVDSKRRQQLLEDAQQLSDTLHSLRSEGEEAVLEGPPAEEPAPGQNTAQHCLWVDEFAPQHYTELLSDDFTNRCLLKWLKLWDLVVFGRERPARKPRPGVETTRVGKEATAPGKWKSHEQALEEMLEAELDPSQRPRQKVALLCGPPGLGKTTLAHVVARHAGYCVVEMNASDDRSPEAFRTRIEAATQMESVLGVGGRPNCLVIDEIDGAPTAAINVLLGILNRKGPQEADQGGTAVAAGGRRRRAEGGLLTRPIICICNDQFTPSLRQLKQQALLLHVPPTLPSRLVQRLQEISLQHGMRSDPGALVALCEKTDNDIRACINTLQFLYGRGRRELSVKAVQTTHVGLKDQRKGLFSVWQEVFQLPRTQRRIVGQDLMLPAHALLLSNGDKGSLTLASQRFYHILRVTTSAGEHEKVVQGLFDNFLRLRLRDSSLSTVCCALDWLAFDDLLEQAAHRGQSFQLLCYLPFVPAAFHVLFASSHVPRITFPSSQQEAQTRMSQTRNHIQTLVSGMAPTTRSRATPQALVLDTLCLLLDVLAPKLRPVSTQLYSAHEKQQLSCLVGTMLAYSLTYHQERTPDGQYLYKLEPNVEEVCRFPELPARKPLTYQAKQLIAREIEMEKMRRAEALAWARSGPQVDQGSSGPASLWTDSGEKGTRQPAPRNHEQRLEHIMKRATVQEQPERDFFGRVVIRKVAVPSREVEAPQKDADEWRMGVAVGRSEVWFRFNEGVSNAVRRSLYIRDLL
Protein: Actin (A6MUT3)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
VMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDVKEKLSYIACYEQELETSKTSSSVEKSYELPDGQVITIGAERFRCPEVLFQPSLIGMEAAGIHETTYNSTMKCDVDIRKDLYGNIVLSGG
Protein: 4-carboxy-4-hydroxy-2-oxoadipic acid aldolase (CHA aldolase) (EC 4.1.3.17) (Gallate degradation protein C) (Q88JX9)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Function: Catalyzes the conversion of 4-carboxy-4-hydroxy-2-oxoadipic acid (CHA) to pyruvate and oxaloacetate, the last step of gallate degradation pathway.
Interaction partners:
- 4-oxalmesaconate hydratase
- 4-oxalomesaconate tautomerase
- 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
- Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase
- Acetolactate synthase
- Acetolactate synthase
- Acetolactate synthase, large subunit
- Acetolactate synthase small subunit
- HTH-type transcriptional regulator GalR
- Ribonuclease E
Sequence:
MSGLIGKTGIVVRNIPRVEPHMIDALGRLGVATVHEAQGRKGLLNTAVRPIQQGVAVAGSAVTVLVAPGDNWMFHVAVEQCRPGDVLVVAPSSPCSDGYFGDLLATSLQARGVLGLVIDAGVRDSQTLRDMGFAVWSRAINAQGTVKEVLGSVNLPLLCAGQLVNAGDIVVADDDGVVVVRHGEAQAVLEAATQRADLEERKRLRLAAGELGLDIYEMRPRLAAKGLRYVDHLTDLEG
Protein: RIKEN cDNA 2200002D01 gene (Q9D809)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEFDLAAALGPGSKKPEGAGHVGDPKHCPLKAPGGPEAGAAHKPRRVSGSSSDSSSSSSSSDSEAEGKEYAAGCKKHERSSDKAKKPKVKKEKMEKKEKKEKKEKEKKEKKAPH
Protein: At5g46870 (RNA-binding (RRM/RBD/RNP motifs) family protein) (Q6NM69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DEAD-box ATP-dependent RNA helicase 31
- DEAD-box ATP-dependent RNA helicase 26
- Nuclear transport factor 2
- non-specific serine/threonine protein kinase
- Peptidyl-prolyl cis-trans isomerase CYP63
Sequence:
MSMVTVKVSNVSLEATERDLKEFFSFSGDIAYLETQSENDGSKLAYVTFKDLQGAETAVLLTGSTIVDSSVTVTMSPDYQLPPDALASIESLKESNKSSSPTREDVSVFRKAEDVVSGMISKGFVLGKDAIAKAKSLDEKHQLTSTASARVTSFDKRIGFTEKINTGTTVVSEKVKEVDQKFQVTEKTKSAIAAAEQTVSNAGSAIMKNRYVLTGATWVTGAFNRVSKAAEEVGQKAKEKVGLAEEEEEEKKKVVDEVAIVHLTESPKALDQSEQDSKLPESKSQPHKELNASVV
Protein: Cellulose synthase A catalytic subunit 7 [UDP-forming] (AtCesA7) (EC 2.4.1.12) (Protein FRAGILE FIBER 5) (Protein IRREGULAR XYLEM 3) (AtIRX3) (Q9SWW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the secondary cell wall formation. Required for the xylem cell wall thickening.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27387950}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cellulose synthase A catalytic subunit 4
- Cellulose synthase A catalytic subunit 8
- Probable galacturonosyltransferase 12
- COBRA-like protein 4
- Beta-1,4-xylosyltransferase IRX9
- Transcription factor MYB46
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
- Protein CELLULOSE SYNTHASE INTERACTIVE 1
- Cellulose synthase A catalytic subunit 6
- NAC domain-containing protein 12
Sequence:
MEASAGLVAGSHNRNELVVIHNHEEPKPLKNLDGQFCEICGDQIGLTVEGDLFVACNECGFPACRPCYEYERREGTQNCPQCKTRYKRLRGSPRVEGDEDEEDIDDIEYEFNIEHEQDKHKHSAEAMLYGKMSYGRGPEDDENGRFPPVIAGGHSGEFPVGGGYGNGEHGLHKRVHPYPSSEAGSEGGWRERMDDWKLQHGNLGPEPDDDPEMGLIDEARQPLSRKVPIASSKINPYRMVIVARLVILAVFLRYRLLNPVHDALGLWLTSVICEIWFAVSWILDQFPKWFPIERETYLDRLSLRYEREGEPNMLAPVDVFVSTVDPLKEPPLVTSNTVLSILAMDYPVEKISCYVSDDGASMLTFESLSETAEFARKWVPFCKKFSIEPRAPEMYFTLKVDYLQDKVHPTFVKERRAMKREYEEFKVRINAQVAKASKVPLEGWIMQDGTPWPGNNTKDHPGMIQVFLGHSGGFDVEGHELPRLVYVSREKRPGFQHHKKAGAMNALVRVAGVLTNAPFMLNLDCDHYVNNSKAVREAMCFLMDPQIGKKVCYVQFPQRFDGIDTNDRYANRNTVFFDINMKGLDGIQGPVYVGTGCVFKRQALYGYEPPKGPKRPKMISCGCCPCFGRRRKNKKFSKNDMNGDVAALGGAEGDKEHLMSEMNFEKTFGQSSIFVTSTLMEEGGVPPSSSPAVLLKEAIHVISCGYEDKTEWGTELGWIYGSITEDILTGFKMHCRGWRSIYCMPKRPAFKGSAPINLSDRLNQVLRWALGSVEIFFSRHSPLWYGYKGGKLKWLERFAYANTTIYPFTSIPLLAYCILPAICLLTDKFIMPPISTFASLFFISLFMSIIVTGILELRWSGVSIEEWWRNEQFWVIGGISAHLFAVVQGLLKILAGIDTNFTVTSKATDDDDFGELYAFKWTTLLIPPTTVLIINIVGVVAGISDAINNGYQSWGPLFGKLFFSFWVIVHLYPFLKGLMGRQNRTPTIVVIWSVLLASIFSLLWVRIDPFVLKTKGPDTSKCGINC
Protein: CID domain-containing protein (A5Z2V1)
Organism: Caenorhabditis elegans
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB2
- RNA polymerase II subunit A C-terminal domain phosphatase ssup-72
- CID domain-containing protein 1
- Suppressor of forked domain-containing protein
- Polyadenylation and cleavage factor homolog 11
- 5'-3' exoribonuclease 2 homolog
- Putative RNA polymerase II subunit B1 CTD phosphatase rpap-2
- DNA-directed RNA polymerase II subunit RPB7
- C3H1-type domain-containing protein
- pre-mRNA 3' end processing protein pfs-2
Sequence:
MVVLTSDVVYSRLQDFQVKNPTQEAIETMSMWIMHYKDNASIDLIVDGWLNCFKTAGTDNKRIALFYVMNDVVQKAKMKHADTLIPAFQPAVLTAVGIGRKQDKVKAVMKRCIQIFKSRNVFSPASTTAMENLLASDADEGYEAEDQALEVDSDDLVKKITNFISARNVVADMMKCVNEGNFDYKEMCKHGMRDREEGGHILHEVHEAIDTMVQVRHSMEDQKKKMMALSETLELAKRVFLHQKREVLVVEEAYVNFRDGIKAVHTELLDMEAKKVYPGLLSPRNEDDRQTYGRSNNRSLSQQWGDNRNQIDMEMDEDERPQAPMMKPSLQALVGIASQPSLQSRIMQLGLKKIANGDEEMFQPTTTTTADTPLPSTFQPPPSKPAVINASKFSMPPPAITSAPLSDPRIRSDGEGPSQYAIALKQHGLPPPTGQQPVQNRMNAPPPAQPSPYQAIPQKPVEQTVYQGQFGGARDPRLANSVTPQSVAVAQQPPITGYQAQYEQIRDPRILQQAAPQQGYQATFEVQKPQLVSPQIQNNGYQARFEQSQLSPSIPQHQPVGQYHQQKNTYCQPPPQHHQYQQQSQQSHGYSSDYHSGDRRDDRGRDNYQNSRYDDRRGSSAPYNNQRGDRWRGSGSHHNDRNRNSGRDSWRGGNHRSGGGYHRY