wanglab/gogpt-training-data huggingface dataset:
Protein: Chaperonin-like RbcX protein 2, chloroplastic (AtRBCX2) (Q8L9X2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chaperone involved in RuBisCO assembly process.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:21922322}.
Interaction partners:
- Chaperonin-like RBCX protein 1, chloroplastic
- 2-oxoglutarate
- Casein kinase II subunit beta-2
- Appr-1-p processing enzyme family protein
- Ribulose bisphosphate carboxylase large chain
- Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic
Sequence:
MVSAWFVVGSPVMDSSSSPCLCLDAHTTGTIRRKKILGKARNLELGSSFTGSRIVFRLSPKRVSRIANRKSKKLLIVNEDVAGNYDDTFGDVQKQIVNYFTYKAVRTVLHQLYEMNPPQYTWFYNHIITNRPTDGKRFLRALGKESQELAERVMITRLHLYGKWIKKCDHGKIYQEISDENLALMRERLMETVIWPSDDTNSR
Protein: Fibroblast growth factor 2 (FGF-2) (Basic fibroblast growth factor) (bFGF) (Heparin-binding growth factor 2) (HBGF-2) (P13109)
Organism: Rattus norvegicus (Rat)
Function: Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Also acts as an integrin ligand which is required for FGF2 signaling (By similarity). Binds to integrin ITGAV:ITGB3 (By similarity). Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration (By similarity). Functions as a potent mitogen in vitro (By similarity). Can induce angiogenesis (By similarity). Mediates phosphorylation of ERK1/2 and thereby promotes retinal lens fiber differentiation (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P09038}. Nucleus {ECO:0000250|UniProtKB:P09038}. Note=Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism (By similarity). Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane (By similarity). Binding of exogenous FGF2 to FGFR facilitates endocytosis followed by translocation of FGF2 across endosomal membrane into the cytosol (By similarity). Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as CEP57 (By similarity). {ECO:0000250|UniProtKB:P09038}.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 4
- Vascular endothelial growth factor receptor 2
- Syndecan-1
- Syndecan-4
- Glypican-1
- Receptor protein-tyrosine kinase
- Platelet-derived growth factor receptor alpha
Sequence:
MAAGSITSLPALPEDGGGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHVKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTEECFFFERLESNNYNTYRSRKYSSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS
Protein: Putative defense protein Hdd11 (Hyphantria differentially displayed gene 11) (O96382)
Organism: Hyphantria cunea (Fall webworm moth) (Phalaena cunea)
Function: As this protein is expressed upon bacterial infection, it may have antimicrobial activity.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MWATYVFIAVSLACANGYSSGAPESVCQDMVPKHPVPPQSTPPPYTITTSTKTVKAGTPMEVVITGKKPTDKMRGLLLQAREGTKIVGKFTLAPNDPFAQLLNCGEPGNAITHKKHDEKNDKQTVAFTWTPPKDFVGEIKFRATIALNGAVFWVGVESGPVKVIS
Protein: Spindlin interactor and repressor of chromatin-binding protein (SPIN1-docking protein) (SPIN-DOC) (Q9BUA3)
Organism: Homo sapiens (Human)
Function: Negatively regulates the transcriptional activator activity of SPIN1 via inhibition of its histone methyl-binding ability. Represses the expression of a number of SPIN1-regulated genes and the SPIN1-mediated activation of the Wnt signaling pathway. Can also inhibit the histone methyl-binding abilities of SPIN2A, SPIN2B, SPIN3 and SPIN4. Positively regulates poly-ADP-ribosylation in response to DNA damage; acts by facilitating PARP1 ADP-ribosyltransferase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:29061846}. Chromosome {ECO:0000269|PubMed:34737271}. Note=Colocalizes with PARP1 to sites of DNA damage. {ECO:0000269|PubMed:34737271}.
Interaction partners:
- Spindlin-1
- Spindlin-2B
- Histone H3.3C
- Histone H3.1t
- Histone H3-7
- Histone H3.2
- Histone H3.1
- Histone H3.3
- Spindlin-3
Sequence:
MALKAEGAALDCFEVTLKCEEGEDEEEAMVVAVIPRPEPMLRVTQQEKTPPPRPSPLEAGSDGCEEPKQQVSWEQEFLVGSSPGGSGRALCMVCGAEIRAPSADTARSHILEQHPHTLDLSPSEKSNILEAWSEGVALLQDVRAEQPSPPNSDSGQDAHPDPDANPDAARMPAEIVVLLDSEDNPSLPKRSRPRGLRPLELPAVPATEPGNKKPRGQRWKEPPGEEPVRKKRGRPMTKNLDPDPEPPSPDSPTETFAAPAEVRHFTDGSFPAGFVLQLFSHTQLRGPDSKDSPKDREVAEGGLPRAESPSPAPPPGLRGTLDLQVIRVRMEEPPAVSLLQDWSRHPQGTKRVGAGDTSDWPTVLSESSTTVAGKPEKGNGV
Protein: Ribosome biogenesis protein BMS1 homolog (EC 3.6.5.-) (Ribosome assembly protein BMS1 homolog) (Q14692)
Organism: Homo sapiens (Human)
Function: May act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:27474224, ECO:0000269|PubMed:34516797}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 15 homolog
- WD repeat-containing protein 75
- HEAT repeat-containing protein 1
- U3 small nucleolar RNA-associated protein 4 homolog
- Nucleolar protein 56
- U3 small nucleolar RNA-associated protein 6 homolog
- KRR1 small subunit processome component homolog
- WD repeat-containing protein 46
- Bystin
- Nucleolar protein 58
Sequence:
MEAKDQKKHRKKNSGPKAAKKKKRLLQDLQLGDEEDARKRNPKAFAVQSAVRMARSFHRTQDLKTKKHHIPVVDRTPLEPPPIVVVVMGPPKVGKSTLIQCLIRNFTRQKLTEIRGPVTIVSGKKRRLTIIECGCDINMMIDLAKVADLVLMLIDASFGFEMETFEFLNICQVHGFPKIMGVLTHLDSFKHNKQLKKTKKRLKHRFWTEVYPGAKLFYLSGMVHGEYQNQEIHNLGRFITVMKFRPLTWQTSHPYILADRMEDLTNPEDIRTNIKCDRKVSLYGYLRGAHLKNKSQIHMPGVGDFAVSDISFLPDPCALPEQQKKRCLNEKEKLVYAPLSGVGGVLYDKDAVYVDLGGSHVFQDEVGPTHELVQSLISTHSTIDAKMASSRVTLFSDSKPLGSEDIDNQGLMMPKEEKQMDLNTGRMRRKAIFGDEDESGDSDDEEDDEMSEDDGLENGSSDEEAEEEENAEMTDQYMAVKGIKRRKLELEEDSEMDLPAFADSDDDLERSSAEEGEAEEADESSEEEDCTAGEKGISGSKAAGEGSKAGLSPANCQSDRVNLEKSLLMKKAALPTFDSGHCTAEEVFASEDESEESSSLSAEEEDSENEEAIRKKLSKPSQVSSGQKLGPQNFIDETSDIENLLKEEEDYKEENNDSKETSGALKWKEDLSRKAAEAFLRQQQAAPNLRKLIYGTVTEDNEEEDDDTLEELGGLFRVNQPDRECKHKADSLDCSRFLVEAPHDWDLEEVMNSIRDCFVTGKWEDDKDAAKVLAEDEELYGDFEDLETGDVHKGKSGPNTQNEDIEKEVKEEIDPDEEESAKKKHLDKKRKLKEMFDAEYDEGESTYFDDLKGEMQKQAQLNRAEFEDQDDEARVQYEGFRPGMYVRIEIENVPCEFVQNFDPHYPIILGGLGNSEGNVGYVQMRLKKHRWYKKILKSRDPIIFSVGWRRFQTIPLYYIEDHNGRQRLLKYTPQHMHCGAAFWGPITPQGTGFLAIQSVSGIMPDFRIAATGVVLDLDKSIKIVKKLKLTGFPYKIFKNTSFIKGMFNSALEVAKFEGAVIRTVSGIRGQIKKALRAPEGAFRASFEDKLLMSDIVFMRTWYPVSIPAFYNPVTSLLKPVGEKDTWSGMRTTGQLRLAHGVRLKANKDSLYKPILRQKKHFNSLHIPKALQKALPFKNKPKTQAKAGKVPKDRRRPAVIREPHERKILALLDALSTVHSQKMKKAKEQRHLHNKEHFRAKQKEEEEKLKRQKDLRKKLFRIQGQKERRNQKSSLKGAEGQLQ
Protein: threonine synthase (EC 4.2.3.1) (Q57X55)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Homoserine kinase, putative
Sequence:
MLTLRVCGTASVEVKERVVDGLLSVTGPQLFTYPRDGEKGEPSDVFRLCIDQTAAGLYMKRQSPGEEEEIYDCRFVWGEDSTVEEVITEVTSLVSHRQFSSTRGAVEPSVSFLSVIRDGLASDGGLFTLRKIPQVTASQLKYLCTAPNLSYVEAARSLLERLTDMSLKPHILSKHILEAYDPSRWNGLKDVCPLTPIHPRATSVADVPENHSDWHNMYLLELYHGPTGAFKDFALQLFPRYFDTAVAAVANQKGGDNNGCGGGEVVSSSTAAGKPLQYMILTATSGDTGVAAISGFVNAKSPCRVMVFYPLRGVSPVQKMHMISYDNGTTVRVIGVESDFDFCQQSVKKLFADEKLERELVNDAGVRLSSANSINWGRLIPQVVYYFWAYRKCIQQNGDKVTGALAFGDKVDFVVPSGNFGNILAAYVAKLMGLPVGKLIVASNTNDVLYEFVSTGCYDISHRHLVPTASPSIDILKASNVERFLFILSDGDSKYVSEQMGRLEFEKRFEVCGKVLQRMQETFWSSKCNESNCAAAIKKIFDATGKLLDPHTAVALHAATEYRREHPETRRPLVIASTAHWAKFPAAVLHAILGEDAVGAEGVESVTDPAESCKYLYEKVLALCPGEAVHPSLRAVLATVEARSGSLKPRVATRDVSLLRKEVTGFVVCTSEGSC
Protein: Nuclear protein 1 (Protein p8) (Q9WTK0)
Organism: Mus musculus (Mouse)
Function: Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses. Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (By similarity). Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation. Negatively regulates apoptosis through interaction with PTMA (By similarity). Inhibits autophagy-induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter. Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53. Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway (By similarity). Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (By similarity). Coactivator of PAX2 transcription factor activity, both by recruiting the EP300 cofactor to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (By similarity). Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (By similarity). Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion. Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities. Also required for LHB expression and ovarian maturation. Exacerbates CNS inflammation and demyelination upon cuprizone treatment.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O60356}. Cytoplasm {ECO:0000250|UniProtKB:O60356}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O60356}.
Interaction partners:
- Cellular tumor antigen p53
Sequence:
MATLPPTANPSQQPLNLEDEDGILDEYDQYSLAHPCVVGGGRKGRTKREAAANTNRPSPGGHERKLLTKFQNSERKKAWR
Protein: Cell division control protein 45 homolog (Q7JMR0)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Probable DNA replication complex GINS protein PSF2
- DNA replication complex GINS protein PSF3
- Probable DNA replication complex GINS protein PSF1
- DNA replication licensing factor mcm-4
- DNA replication licensing factor MCM2
- DNA replication licensing factor mcm-6
- DNA replication complex GINS protein SLD5
- Protein MCM10 homolog
- DNA replication licensing factor mcm-5
- DNA replication licensing factor MCM7
Sequence:
MIIEDNFRQEFYNKIKKGDKSVVLIVSVDTDALCTTMILTHLLRCDDIPFSILAVEGWSSVEKIFADSQEQKCHYILINCGATRSLTRLQIPPASIAFVIDSHRPFHIENVYENGQIHLLANPSEMSELQIPDLESVIREDSDDEEDSDEDEDQEYISYEQRMEKIRRKAIKREEMQIWERQRRTILWRYYESTWFSSPSCVTLLEMAAEMNRVSAETMWFTAVGLNSAMADKLISIEMYTQICVDRMRPFVHRFMPKNIVNQGKVDDLLHITFGRELPLALYSHWDLFSAMMVSEYFSIKTKNWTQKGDVNIRHLLAQLGITLHETKQKFEALPTEQRNLVVDVLEKEMDSSFATFFGTLGYCGKLSACDVARAVTLRLEMPKSETIMNRFRSGQSILRSSITGERQDRLNLNNTFTSICQRTLQVSWKTVAAAINQSEIIPNGPYYLFSCSRSIDEDMVDSRHFLYNTAGFMIRAFASMKKGRTTKPLIAMFPLTGESAGWLVVTGVMPIATIYEDSLLKTCIGRAFERVKKMTPPLRIVDDYFNSDIIRLKSEDRTRFIDFLQTVFEGTSN
Protein: Nuclear envelope phosphatase-regulatory subunit 1 (Transmembrane protein 188) (B8YCP3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus membrane {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004232}.
Interaction partners:
Sequence:
MNSLEQAEDLKAFERRLTEYIHCLQPATGRWRMLLIVVSVCTATGAWNWLIDPETQKVSFFTSLWNHPFFTISCITLIGLFFAGIHKRVVAPSIIAARCRTVLAEYNMSCDDTGKLILKPRPHVQ
Protein: NAD(P)H quinone oxidoreductase PST1 (EC 1.6.5.2) (Flavodoxin-like protein PST1) (FLP PST1) (A0A1D8PHR5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cell membrane {ECO:0000269|PubMed:26325183}; Peripheral membrane protein {ECO:0000269|PubMed:26325183}.
Interaction partners:
- Septicolysin
- D-xylose reductase [NAD
- Phm7p
Sequence:
MAQGKVAIIIYSLYHHVYDLALAEKAGIEAAGGVADIYQVAETLSDDVLAKMHAPAKPDIPIATHETLTQYDAFLFGIPTRFGNFPAQIKAFWDRTGGLWAKNALRGKYAGVFVWTGTPGGGQETTIINSLSTLAHHGIIYVPFGYGYPGMTDLEEVHGGSPWGAGTFASGNGSRKVTDLEKAIAKQQGEDFFKTVFK
Protein: Probable unidentified antibiotic-transport ATP-binding protein ABC transporter (O53149)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
Interaction partners:
- Probable unidentified antibiotic-transport integral membrane ABC transporter
- Probable unidentified antibiotic-transport integral membrane ABC transporter
- Alpha-
- Possible nitrogen fixation related protein
- Probable conserved ATP-binding protein ABC transporter
- Probable transcriptional regulatory protein
- Probable cysteine desulfurase
- Iron-sulfur cluster assembly SufBD family protein Rv1462
- Conserved protein
Sequence:
MNRAPDTPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVMLQGGGGYPAARAGEMLDLVASYAANPLDPHWLLDTLGLTEAARTTYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGAKDQLRFTAPPRLDLSLLASALPEGYQATELTPGEYLVEGPVDPQVLATVTAWCAQIDVLATDMRVEQRSLEDVFLDLTGRKLRQ
Protein: Voltage-dependent T-type calcium channel subunit alpha (E9PWL1)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
Interaction partners:
Sequence:
MDEEEDGAGAEESGQPRSFTQLNDLSGAGGRQGPGSTEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERVSMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLEPYYQTENEDESPFICSQPRENGMRSCRSVPTLRGEGGGGPPCGLDYEAYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIMYFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNASTLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAVGVRAGLLSSPVARGGQEPQPSGSCSRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRVPRASPEIQDRDANGSRWLMLPPPSTPTPSGGPPRGAESVHSFYHADCHLEPVRCQAPPPRSPSEASGRTVGSGKVYPTVHTSPPPEMLKDKALVEVAPSPGPPTLTSFNIPPGPFSSMHKLLETQSTGACHSSCKISSPCSKADSGACGPDSCPYCARTGAGEPESADHEMPDSDSEAVYEFTQDAQHSDLRDPHRRRRPSLGPDAEPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNIVFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMRVLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTLPDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLVAILVEGFQAEGDATKSESEPDFFSPSVDGDGDRKKRLALVALGEHSELRKSLLPPLIIHTAATPMSLPKSSSTGVGEALGSGSRRTSSSGSAEPGTAHHEMKSPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQDEEESSEEDRASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRSSASEHQDCNGKSASGRLARTLRADDPPLDGDDGDDEGNLSKGERLRAWVRARLPACCRERDSWSAYIFPPQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAVFLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVLRLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFVCQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVGVDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRLKRLEKKRRSKEKQMADLMLDDVIASGSSASAASEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGVIGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVLESVFKLVAFGFRRFFQDRWNQLDLAIVLLSIMGITLEEIEVNASLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLDTVMQALPQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVSTGDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKEAKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGVNSPDSPKPGAPHTTAHIGAASSGFSLEHPTMVPHTEEGPVPLGPDLLTVRKSGVSRTHSLPNDSYMCRNGSTAERSLGHRGWGLPKAQSGSILSVHSQPADTSCILQLPKDAHYLLQPHGAPTWGAIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLSEVSGPSCPLTRSSSFWGGSSIQVQQRSGSQSKVSKHIRLPAPCPGLEPSWAKDPQETRSSLELDTELSWISGDLLPSSQEEPLSPRDLKKCYSVEAQSCRRRPGSWLDEQRRHSIAVSCLDSGSQPRLCPSPSSLGGQPLGGPGSRPKKKLSPPSISIDPPESQGPRPPCSPGVCLRRRAPASDSKDPSASSPLDSTAASPSPKKDALSLSGLSSDPTDLDP
Protein: DNA polymerase III subunit psi (EC 2.7.7.7) (Accessory clamp loader complex subunit psi) (Replication clamp loader subunit HolD) (P28632)
Organism: Escherichia coli (strain K12)
Function: Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The exact function of the psi subunit is unknown.
Interaction partners:
- DNA polymerase III subunit delta'
- DNA polymerase III subunit chi
- DNA polymerase III subunit delta
- DNA polymerase III subunit alpha
- DNA polymerase III subunit tau
- DNA polymerase III subunit epsilon
- [Ribosomal protein bS18]-alanine N-acetyltransferase
- Beta sliding clamp
- DNA polymerase III subunit theta
- Single-stranded DNA-binding protein
Sequence:
MTSRRDWQLQQLGITQWSLRRPGALQGEIAIAIPAHVRLVMVANDLPALTDPLVSDVLRALTVSPDQVLQLTPEKIAMLPQGSHCNSWRLGTDEPLSLEGAQVASPALTDLRANPTARAALWQQICTYEHDFFPRND
Protein: Transketolase (TK) (EC 2.2.1.1) (P75611)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Interaction partners:
- Ribulose-phosphate 3-epimerase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Pyruvate kinase
- Enolase
- Probable ribose-5-phosphate isomerase B
- Ribose-phosphate pyrophosphokinase
- Glyceraldehyde-3-phosphate dehydrogenase
- L-lactate dehydrogenase
Sequence:
MKNLFACQHLALSAIQHAKGGHVGMALGASPILYTLWTKHIQFNPNCPKWINRDRLVMSAGHGSMALYPILHFAGLITKQEMLHHKYGQVNTSSHPEYAPNNFIDASTGPLGQGLGMAVGMALTQRVLAAEFKALSPKLFDHFTYVVVGDGDLQEGVSYEVAHLAGVYQLNKLIVLHDSNRVQMDSVVRDVSLENLQTRFTNMGWNYLETSDAVADIDAAIKQAKKSDKPTFIEVHTTIAKNTTLEDQPAGHWFIPTDKDFARFNSNTKTNFTPFEYPQTVYDFFHKQVIARQAKPVQAYKELLEKLKDKPLYTKFINWTENDYQALYLNQLDERKVAQANAATRNYLKDFLGQINNSNSNLYCLNADVARSCNIKLGDDNLHTNPHSRNIQVGIREFGMSTIMNGMALHGGVKVMGGTFLAFADYSKPAIRLGALMNLPTFYVYTHDSYQVGGDGPTHQPYDQLPMLRAIENVQVWRPCDEKETAAGVNYGLLSQDQTNVLILTRQALPSLEQSDSVQTLKGGYIISNRKQPDVIVAASGSEVQLALQLEQALNEQQLKTRVVSVPNINMLLSQPQSYLQQLFDPNSVLLTLEASASMEWYALAKYVKKHTHLGAFSFGESNDGQVVYEHKGFNVTNLLKLIKTLKS
Protein: Protein TIFY 10B (Jasmonate ZIM domain-containing protein 2) (Q9S7M2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Repressor of jasmonate responses. Jasmonoyl-isoleucine (JA-Ile) specifically promotes COI1-TIFY10B/JAZ2 interaction. Activated by MYC2, MYC3 and MYC4 transcription factors. Interacts with and suppresses RHD6 and RSL1 transcription factor activities to negatively regulate jasmonate-stimulated root hair development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- Transcription factor MYC2
- Coronatine-insensitive protein 1
- Transcription factor MYC3
- AFP homolog 2
- Protein TIFY 5A
- Protein TIFY 5B
- Transcription factor MYC4
- 12-oxophytodienoate reductase 3
- Transcription factor ABA-INDUCIBLE bHLH-TYPE
- Transcription factor bHLH13
Sequence:
MSSFSAECWDFSGRKPSFSQTCTRLSRYLKEKGSFGDLSLGMTCKPDVNGGSRQPTMMNLFPCEASGMDSSAGQEDIKPKTMFPRQSSFSSSSSSGTKEDVQMIKETTKSVKPESQSAPLTIFYGGRVMVFDDFSAEKAKEVIDLANKGSAKSFTCFTAEVNNNHSAYSQKEIASSPNPVCSPAKTAAQEPIQPNPASLACELPIARRASLHRFLEKRKDRITSKAPYQIDGSAEASSKPTNPAWLSSR
Protein: RabX4 (Q9VC31)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Rab GDP dissociation inhibitor
Sequence:
MALDFVATYKVLVLGDSNVGKTCIVHRYCDEKYYDTYISTIGIDFKQKLINLDGVPIKLQIWDTAGQERFRTLTTAYYRGAMGILLMYDVTNLESYNNLSYWLRNIQENASPDVVKVLAGNKCECSATQRMVDKERGEKIAENFDMPFFEVSCKSNINIEDAFLSLARKIREQRERRGDNFDNDESKDKKSPGSNGLGTFSLGSLSGENRCTC
Protein: Adenylate kinase 4 (AK 4) (EC 2.7.4.3) (ATP-AMP transphosphorylase 4) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase 4) (AMK4) (O82514)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P69441}.
Interaction partners:
- Adenylosuccinate lyase
- Adenylosuccinate lyase
- Adenosine kinase 2
- Adenosine kinase 1
- Thiamine pyrophosphokinase 2
- Thiamine pyrophosphokinase 1
- AMP deaminase
- At5g66005
- Alkaline-phosphatase-like family protein
- At1g72880
Sequence:
MATGGAAADLEDVQTVDLMSELLRRLKCSQKPDKRLIFIGPPGSGKGTQSPVVKDEYCLCHLSTGDMLRAAVASKTPLGVKAKEAMEKGELVSDDLVVGIIDEAMNKPKCQKGFILDGFPRTVTQAEKLDEMLKRRGTEIDKVLNFAIDDAILEERITGRWIHPSSGRSYHTKFAPPKTPGVDDITGEPLIQRKDDNADVLKSRLAAFHSQTQPVIDYYAKKAVLTNIQAEKAPQEVTSEVKKALS
Protein: Protocadherin 1 (Q8CFX3)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MGPLRPSPGPGGQRLLLPPLLLALLLLLAPSASHTTQVVYKVPEEQPPNTLIGSLAADYGLPDVGHLYKLEVGAPYLRVDGKTGDIFTTETSIDREGLRECQNQIPGNPCILEFEVSITDLVQNGSPRLLEGQIEVQDINDNTPNFASPVITLAIPENTNIGSLFPIPLATDRDAGPNGVASYELQAGPEAQELFGLQVAEDQEEKQPQLIVMGNLDRERWDSYDLTIKVQDGGNPPRASSALLRVTVLDTNDNAPKFERPTYEAELSENSPIGHSVIQVKANDSDQGANAEIDYTFHQAPEVVRRLLRLDRNTGLITVQGPVDREDLSTLRFSVLAKDRGATPKSARAQVVVTVKDMNDNAPTIEIRGIGLVTHQDGMANISEDVAEETAVALVQVSDRDEGENAAVTCVVAGDVPFQLRQASETGSDSKKKYFLQTTTPLDYEKVKDYTIEIVAVDSGNPPLSSTNSLKVQVVDVNDNAPVFTQSITEVAFPENNKPGEVVAEVTASDADSGSNAELVYSLEPEPAAQGLFTISPENGEIRVKTSLDREQRDSYELKVVAADRGSPSLQGTATVLVNVLDCNDNDPKFMLSGYNFSVMENMPALSPVGMVTVIDGDKGENARVQLSVEQDNGDFVIQNGTGTILSSLSFDREQQSTYTFQLKAVDGGVPPRSAYVGVTINVLDENDNAPFITAPSNTSHRLLTPQTRLGETVSQVTAEDIDSGINAELTYSIAGGNPYGLFQIGSHSGAITLEKEIERRHHGLHRLVVKVSDRGKPPRYGTALVHLYVNETLANRTLLETLLVHSLDTPLDIDIAGDPEYERSKQRGNILFGVVAGVVAVALLIALAVLVRYCRQREAKSGYQAGKKETKDLYAPKPSGKAAKGSKSKGKKSKSPKPVKPVEDEDDTGLQKSLKFNLMSDAPGDSPRIHLPLNYPPGSPDLGRHYRSNSPLPSIQLQPQSPSASKKHQVVQDLPPANTFVGTGDTTSTGSEQYSDYSYRTNPPKYPSKQVGQPFRLSTPQPPPHPYHGAIWTEVWE
Protein: Putative low affinity glucose transporter MstE (Q400D8)
Organism: Emericella nidulans (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGVDIKGLFKPKAEQQEHSQATTPSRTDSIAEKDNGIIDDSPVKYLTWRSFILGIVVSMGGFIFGYSTGQISGFTTMADFKKRFAERQANGEYVFSNVRNGLIVGLLCIGTMIGALVAAPIADRIGRKLSMSFWSIIHIVGIIIQIATDSNWVQIAMGRWVAGLGVGALSSVVPMYQSEAAPRQVRGAMISAFQLFVAFGIFISYIINYGTESIQSTASWRITMGIGFAWPLILGLGALFLPESPRYAYRLGRIDEARKVMTKLYGVEVNHRVVVQEMKDMKDKLEEERAAGVAPWHEVVTGPRMLYRTLLGIALQSLQQLSGANFIFYYGNSIFTSTGLNNSYVTQIILGAVNFGMTLPGLYIVEHFGRRASLMVGGAWMAICFYIWASVGNSVLDLDNPQNTPKAGAAMIVFTCFFIAGFATTWGPIVWSICSEMYPNRSRATSIGIATCANWTWNFLISFFTPFISGSIHFAYGYVFASCCVVGVLIVFFFVNETQGRTLEEVDTMYVLHVVPWKSASWVPDESIVRDLHPGSDANKTEGLGQAEHGEESRPEPVEIRE
Protein: Serine/threonine-protein phosphatase PP1-1 (EC 3.1.3.16) (P20604)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the dephosphorylation of the large subunit of RNA polymerase II. Is required in late G1 for normal G1 cyclin expression, bud initiation and expression of certain genes that are periodically expressed during late G1. Associates with the SAP proteins in a cell cycle-dependent manner.
Subcellular location: Cytoplasm.
Interaction partners:
- SIT4-associating protein SAP190
- SIT4-associating protein SAP155
- SIT4-associating protein SAP185
- Type 2A phosphatase-associated protein 42
- Protein phosphatase PP2A regulatory subunit B
- Protein phosphatase PP2A regulatory subunit A
- Serine/threonine-protein phosphatase 2A activator 1
- SIT4-associating protein SAP4
- Serine/threonine-protein phosphatase 2A activator 2
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
Sequence:
MVSRGPDEWLETIKKCQALTENEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFRTAGGFPDDINYIFLGDYVDRGYYSLETFTLLMCLKVKYPAKITLVRGNHESRQITQVYGFYEECLNKYGSTTVWKYCCQVFDFLTLAAIIDGKILCVHGGLSPEIRMLDQIRVLSRAQEVPHEGGFSDLLWSDPDNVEAWQVSPRGAGWLFGSKVAREFNHVNGLNLIARAHQLVMEGFKYHFPEKDVVTVWSAPNYCYRCGNVASVMKVDEDLEPTFKIFSAVPDDYIRESTANHNNQRAGYFL