wanglab/gogpt-training-data huggingface dataset:
Protein: AlgW protein (Q9HVX1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Sigma factor AlgU negative regulatory protein
- Sigma factor AlgU regulatory protein MucB
- RNA polymerase sigma-H factor
- GDP-mannose 6-dehydrogenase
- Alginate biosynthesis transcriptional regulatory protein AlgB
- Periplasmic tail-specific protease
- Positive regulator for alginate biosynthesis MucC
- Positive alginate biosynthesis regulatory protein
Sequence:
MPKALRFLGWPVLVGVLLALLIIQHNPELVGLPRQEVHVEQAPLLSRLQEGPVSYANAVSRAAPAVANLYTTKMVSKPSHPLFDDPMFRRFFGDNLPQQKRMESSLGSAVIMSAEGYLLTNNHVTAGADQIIVALRDGRETIAQLVGSDPETDLAVLKIDLKNLPAMTLGRSDGIRTGDVCLAIGNPFGVGQTVTMGIISATGRNQLGLNTYEDFIQTDAAINPGNSGGALVDAAGNLIGINTAIFSKSGGSQGIGFAIPTKLALEVMQSIIEHGQVIRGWLGVEVKALTPELAESLGLGETAGIVVAGVYRDGPAARGGLLPGDVILTIDKQEASDGRRSMNQVARTRPGQKISIVVLRNGQKVNLTAEVGLRPPPAPAPQQKQDGGE
Protein: Delta-guaiene synthase 3 (EC 4.2.3.87) (EC 4.2.3.93) (D0VMR8)
Organism: Aquilaria crassna (Eagle wood)
Function: Sesquiterpene synthase involved in the biosynthesis of delta-guaiene (78.2%) and alpha-guaiene (20.9%), two structures composed of five- and seven-membered rings. Produces also 0.9% of alpha-humulene.
Interaction partners:
Sequence:
MSSAKLGSASEDVSRRDANYHPTVWGDFFLTHSSDFLENNDSILEKHEELKQEVRNLLVVETSDLPSKIQLTDDIIRLGVGYHFETEIKAQLEKLHDHQLHLNFDLLTTSVWFRLLRGHGFSISSDVFKRFKNTKGEFETEDARTLWCLYEATHLRVDGEDILEEAIQFSRKKLEALLPELSFPLNECVRDALHIPYHRNVQRLAARQYIPQYDAEPTKIESLSLFAKIDFNMLQALHQRELREASRWWKEFDFPSKLPYARDRIAEGYYWMMGAHFEPKFSLSRKFLNRIIGITSLIDDTYDVYGTLEEVTLFTEAVERWDIEAVKDIPKYMQVIYIGMLGIFEDFKDNLINARGKDYCIDYAIEVFKEIVRSYQREAEYFHTGYVPSYDEYMENSIISGGYKMFIILMLIGRGEFELKETLDWASTIPEMVKASSLIARYIDDLQTYKAEEERGETVSAVRCYMREYDVSEEEACKKMREMIEIEWKRLNKTTLEADEVSSSVVIPSLNFTRVLEVMYDKGDGYSDSQGVTKDRIAALLRHAIEI
Protein: Uncharacterized protein (Q38CX4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPVRPPLQRCTVRPLRGVLVHRPRPKILPLEAAVMLGEPHAIAASFLLHAHISTARNVSIVRAKKASIRASNNMSDCLQRVLSCGLSRDVLLCACAAAATPPELLPPLVQRHVRAPRDGNVVVLSSAEWRAFFLSMLRAIHSTAAGRLEFSSLALLCATCLAPSVRLGDQLARAYCGFTGEIERNGAVCANSFGSTGSGRAADGVVAFAACCTMMNISEGMESRDTAWMRLWADVQPTLQSGCGDEATTMMPNESWIRCQELHLDCLLRTGRHEDIRKVLSPDSLVTKQFHRMSDDTLAQLFVQPSLCDTVRFRVLRALLDVSRAKSEALVALQRSPFSRNSHLPSVTRSARMVAALLRCLIVEARDQPSSSRNSCLFSDVEALCKMCNSYALAQSLLPYADGSNGSGADRTGVIALLMKATRDEYRSRCLAEFVAAISDAVAFARDFARRGDELASAMVHACAAVLTNLFTLCSPCRAKHDGHRANSSGKRRAKPAWRLRLERDEAVRSHKYELLPGELPHGALSHFIAMLLADGFVLDGGSLGANLAAADFLDLNFYSLQLLGSLYHATRAIGEGQELADVVGVVESLYRRRRQVFGEDGVALLCARCQITTLVRQKTGGNLGEGSSGDAAPSGVKVMRKRMSYLRPGAADLDFLRSRSVIAAGGAFAVDCSVGVWLRKATVQVEA
Protein: ATP-dependent DNA helicase II subunit 2 (EC 3.6.4.12) (ATP-dependent DNA helicase II subunit Ku80) (High affinity DNA-binding factor subunit 2) (Yeast Ku80) (Q04437)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.
Subcellular location: Nucleus {ECO:0000269|PubMed:9635192}. Chromosome, telomere {ECO:0000269|PubMed:9635192}.
Interaction partners:
- Regulatory protein SIR4
- DNA ligase 4
- ATP-dependent DNA helicase II subunit 1
- Telomere elongation protein EST1
- Cell division control protein 13
- Telomerase reverse transcriptase
- DNA repair and recombination protein RAD52
- Telomere replication protein EST3
- Protein STN1
- Non-homologous end-joining protein 1
Sequence:
MSSESTTFIVDVSPSMMKNNNVSKSMAYLEYTLLNKSKKSRKTDWISCYLANCPVSENSQEIPNVFQIQSFLAPVTTTATIGFIKRLKQYCDQHSHDSSNEGLQSMIQCLLVVSLDIKQQFQARKILKQIVVFTDNLDDLDITDEEIDLLTEELSTRIILIDCGKDTQEERKKSNWLKLVEAIPNSRIYNMNELLVEITSPATSVVKPVRVFSGELRLGADILSTQTSNPSGSMQDENCLCIKVEAFPATKAVSGLNRKTAVEVEDSQKKERYVGVKSIIEYEIHNEGNKKNVSEDDQSGSSYIPVTISKDSVTKAYRYGADYVVLPSVLVDQTVYESFPGLDLRGFLNREALPRYFLTSESSFITADTRLGCQSDLMAFSALVDVMLENRKIAVARYVSKKDSEVNMCALCPVLIEHSNINSEKKFVKSLTLCRLPFAEDERVTDFPKLLDRTTTSGVPLKKETDGHQIDELMEQFVDSMDTDELPEIPLGNYYQPIGEVTTDTTLPLPSLNKDQEENKKDPLRIPTVFVYRQQQVLLEWIHQLMINDSREFEIPELPDSLKNKISPYTHKKFDSTKLVEVLGIKKVDKLKLDSELKTELEREKIPDLETLLKRGEQHSRGSPNNSNN
Protein: Transcription factor CPH2 (Candida pseudohyphal regulator 2) (Q59RL7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor that positively controls filamentous growth, virulence, and invasiveness. Binds directly to the two SRE-1-like elements upstream of TEC1 and thus regulates positively expression of this important hyphal growth regulator. Functions independently of known signaling cascades involving EFG1. Regulates also gene expression during intestinal colonization but is not involved in host cell adhesion.
Subcellular location: Nucleus.
Interaction partners:
- Uncharacterized protein
- Transcription activator TEC1
- Enhanced filamentous growth protein 1
- Importin-95
- Transcription factor CPH1
- Biofilm and cell wall regulator 1
Sequence:
MLSQYDEQLAAGDNNGFNKQGNATLYSFDFVDADDFLDSISGALPNNGHNNVNPNTNDISFEDMNIMNPNIYSPVSAASGDDFTQSSGQPMISEGSNYTGQNFTDYLSDNSLEGYDKNTSRPLHEVDIGFSNKRSNSTSTGSLSHNEEITPISHYSVDSIVTSPEPPINKQGDFPPIKRTTTVSSTNSITNTTKKPAKVTKPKSKDKNSHNMIEKKYRTNINTKILALRDAVPALRIAAGCDDVSIADLEGLTPASKLNKASVLTKATEYIKHLESKNFILKQQNIELHRLIQHANMNPKSLPPPPQQMQAPPQPGFGFYPPQNQSFNVTPASQYPSPQQQVSPTQQQTVHHPPQPNRYLLGGMAAVMGTSLFGGSGENDFRSLSALPFSYLFPNAILNPSPLTIQLWTLTKVLLVVGSLASIFIPMYKQAQLKKEDKPNTIPETSLLDWILISIGFKTPAKLSVSKRDAIISNLQGGNDWSQLVSDYFYLAGCEINFENCFLSLVLGTIIRHRFPVVATILNHYLSMKEALLLNLDYKGFSKSLIRLNQLISKVDGVSIFESTNLTTRLTNVFTNNRINANIVDGQNHVKYIEFYQRNINDYYAIVFNWRLLEFIHELNVTYLEQLNDDQSQVLTDLKIIEAFFGEQDNKLFGYYQLFTSILNANYAPYLFESLKDKVESSLEKFRIAYEGIDLTDHEIHNTSSEDEYEQESPVVYKYEPTLKSQKSLISSLNLVNEEEFIILTCSLTIYYYKNKEYDRALKLLNYLRLDNDSKTLSLLTFTSLITLINELIPGKIEDNVNLDSAIRICRDWLENPDLTQYMDEDIKLELKKIVVTKGMIVNGIDVNESDEE
Protein: ornithine decarboxylase (EC 4.1.1.17) (Q9HVQ3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Polyamine aminopropyltransferase 1
- N-carbamoylputrescine amidohydrolase
- Polyamine aminopropyltransferase 2
- Ornithine cyclodeaminase
- Agmatine deiminase
- Spermidine acetyltransferase
- Putrescine--pyruvate aminotransferase
- Acireductone dioxygenase
- Enolase-phosphatase E1
- Biosynthetic arginine decarboxylase
Sequence:
MSIKVEDYFAPETFQRMKAFADKQETPFVVIDKQTIADAYDQLTDCFPFARIYYAVKANPATEITELLRDKGSNFDIASIYELDKVMKTGVGPERISYGNTIKKSKDIRYFYEKGVRLFATDSEADLRNIAKAAPGAKVYVRILTEGSTTADWPLSRKFGCQTDMAMDLLILARQLGLEPYGISFHVGSQQRDISVWDAAIAKVKVIFERLKEEDGIVLKMINMGGGFPANYITKTNDLETYAEEIIRFLKEDFGDDLPEIILEPGRSLIANAGILVSEVVLVARKSRTAVERWVYADVGKFSGLIETMDESIKFPIWTEKQGEMEEVVIAGPTCDSADIMYEHYKYGLPLNLASGDRLYWLSTGAYTTSYSAVEFNGFPPLKAFYL
Protein: Small ribosomal subunit protein eS1 (Q38BK6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03122}.
Interaction partners:
- 40S ribosomal protein S26
- 40S ribosomal protein S13, putative
- 40S ribosomal protein S15a, putative
- Ribosomal protein S19, putative
- 40S ribosomal protein S8
- 40S ribosomal protein S16, putative
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S4
- 40S ribosomal protein S5, putative
- 40S ribosomal protein S15, putative
Sequence:
MTLGKNKRISKGGKRGKKKAQEAMSRKEWYDVVAPKNFEVRQFAKTICNKTQGTKIAADFLRGRVYEGNLADLNKTQNEDDAYRKVKFTVQEVQGRNLLTQFHGMDMTSDRVYYLLRKWCTTIEATVEAKTADGYGLRLFLIAFTKKQENQLSKNCYAKTRLVKWVRMRATNIIRRRLAKLDINDAVSLLTRNILRDRLAKRCNPIIPLRDLRIRKVKVIRTPKFDAQALIAAHGEVPTSAEGEARVVEEAQEETA
Protein: Small ribosomal subunit protein mS23 (28S ribosomal protein S23, mitochondrial) (MRP-S23) (S23mt) (Q8VE22)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q2NL27}.
Interaction partners:
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein mS29
Sequence:
MAGSRLETVGSVFSRTRDLMRAGVLKEKPLWYDIYKAFPPLREPVFRRPRLRYGKAKADIQDIFYQEDQIRAKFFATYGSGQKAFDLFNPNFKSTCQRFVEKYTELQNLGETDEEKLFVETGKALLAEGIILRRVREARTVSVRLQASSEGHEPQEDDDLAQRGQVKQEPETAPSPP
Protein: Granule-bound starch synthase 1, chloroplastic/amyloplastic (EC 2.4.1.242) (Granule-bound starch synthase I) (GBSS-I) (allergen Ory s GBSS_I) (A2Y8X2)
Organism: Oryza sativa subsp. indica (Rice)
Function: Required for the synthesis of amylose in endosperm.
Subcellular location: Plastid, chloroplast. Plastid, amyloplast. Note=Amyloplast or chloroplast, granule-bound. {ECO:0000250}.
Interaction partners:
- Glucose-1-phosphate adenylyltransferase
- glucose-1-phosphate adenylyltransferase
- Glucose-1-phosphate adenylyltransferase
- Glucose-1-phosphate adenylyltransferase
- 1,4-alpha-glucan branching enzyme
- 1,4-alpha-glucan branching enzyme
- 1,4-alpha-glucan branching enzyme
- 4-alpha-glucanotransferase
- starch synthase
- Sucrose synthase
Sequence:
MSALTTSQLATSATGFGIADRSAPSSLLRHGFQGLKPRSPAGGDATSLSVTTSARATPKQQRSVQRGSRRFPSVVVYATGAGMNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYDQYKDAWDTSVVAEIKVADRYERVRFFHCYKRGVDRVFIDHPSFLEKVWGKTGEKIYGPDTGVDYKDNQMRFSLLCQAALEAPRILNLNNNPYFKGTYGEDVVFVCNDWHTGPLASYLKNNYQPNGIYRNAKVAFCIHNISYQGRFAFEDYPELNLSERFRSSFDFIDGYDTPVEGRKINWMKAGILEADRVLTVSPYYAEELISGIARGCELDNIMRLTGITGIVNGMDVSEWDPSKDKYITAKYDATTAIEAKALNKEALQAEAGLPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFHMGRLSVDCKVVEPSDVKKVAATLKRAIKVVGTPAYEEMVRNCMNQDLSWKGPAKNWENVLLGLGVAGSAPGIEGDEIAPLAKENVAAP
Protein: Kirre like nephrin family adhesion molecule 3, like precursor (Kirre-like nephrin family adhesion molecule 3, like) (A0A0R4IT86)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- NPHS1 adhesion molecule, nephrin.
Sequence:
MLAFYIALCLLGTVSQAAYFSQQPQDQVVVAGQSVTLPCVIVGYRGMVQWTKDGLALGGERDLPGWVRYSLMGDPLSGEHSLVIDSAELGDDAIYECQATQAGLRSHRAKLTVLVPPSDPIVEGGPVVRLKAHTPHNLTCRASGAKPAAEITWYRDGEIMQNAIYSKSLMEDGKRETAVSMLPMVPEDSDSGRTYTCRVLNPAAPAGRQTSVTINVQHPPSVTLSVQPQTVMEGAKVLFICSASANPEITGYRWSKGGVPISEANGDSLEVTADHSYFTDPVSCEVSNSVGSTNVSTLVDVQFGPRLLTEPKPQIVDIGMDAAFTCSWTGNPPLTLAWTKQGSNVVLSNSNTLQLKAVTQDDTGTYTCKAIVPRIGVAERDVTLTVNGPPIITAEATQQAIKHSKGKLECLVGSSPPPDKIVWTFGDMMLSSGSSGRFSVQTVNSDQGVLSSLILSETLAQDFQLRYNCTAWNRFGTGTALVTLEEQEALPLLIIIGASVGGGCVFIVCVITLVSICCRHNAKGKKGTRLSKSDIRVQIVHSDHNAARGNDDEEDVKEPMAPNSSESPGTSRTEHSDLLEEEDDERSDIKDPTNGYYNVRAHEDRHITRTGFSEYANNARPVYTPTQLPSPSPLYGQHSTQPRIYDFSQRYATTPANRTTYEQQQPQQPQQQPQTPTAYPQETVYSGSTYLPATYGRAFTSYVKPASYEKVDGYEHSDQASKVSSSSRFSYASSQVSSQQSDYGRPSQQRMQTHV
Protein: Puromycin-sensitive aminopeptidase (Q8VID2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
VSPINYSLCLKPDLLDFTFEGKLEAAAQVRQATNQIVMNCADIDIITASYAPEGDEEIHATGFNYQNEDEKVTLSFPSTLQTGTGTLKIDFVGELNDKMKGFYRSRYTTPAGEVRYAAVTQFEATDARRAFPCWDEPAIKATFDISLVVPKDRVALSNMNVIDRKPYPDDENLVEVKF
Protein: Battenin (Protein CLN3 homolog) (Q54F25)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Ceroid-lipofuscinosis neuronal protein 5 homolog
- Cathepsin D
- Cysteine proteinase 1
- Palmitoyl-protein thioesterase 1
- Cysteine protease
- Tripeptidyl-peptidase 1
- Counting factor associated protein D
Sequence:
MGKDYTFIRNWISFHFMGNINNFSYCVVNAASGNLSAYFHNSKNIGIILWANIAFGLVSRLVNTFLIENVNSKLKIVVNCLFMSIGLIGVALSVYVNFGFCIAAIAFVGIASSFGESVILSYMKKFPAELVNGWSSGTGIAGVCGSLFYIAMVAAGLSNSTIFYMMLPTVAVYFLLFFFGLKVPNHLEEDRTDNHNNSNNSSNNSKYTEKQSLVKKDQLIEDIDDGGGAEVAPPGETKKQRYIRCARLVWFNAVNLALVYFFEYVASVGGADLALKKDPNNDNFFIANAFAIFSFCYQLGVLISRSSLQFVKIKHIGVITILQGINMVFWIIQAKYKMVTSVWVLFILMVYCGLLGGASYVNVFYLILHQKNIPNEDRELCINYAALLVTVGITLAACFILVMDHTFLASEVPKTDSSSST
Protein: Fructose-bisphosphate aldolase 1 (EC 4.1.2.13) (Aldolase CE-1) (CE-1) (P54216)
Organism: Caenorhabditis elegans
Function: May be involved in the metabolism of fructose-bisphosphate (beta-D-fructose 1,6-bisphosphate) and of fructose 1-phosphate.
Interaction partners:
- Triosephosphate isomerase
- ATP-dependent 6-phosphofructokinase 2
- ATP-dependent 6-phosphofructokinase 1
- Fructose-1,6-bisphosphatase isozyme 2
- Glyceraldehyde-3-phosphate dehydrogenase 2
- transketolase
- Glyceraldehyde-3-phosphate dehydrogenase 3
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Glyceraldehyde-3-phosphate dehydrogenase 4
Sequence:
MASYSQFLTKAQEDELRSIANAIVTPGKGILAADESTGSMDKRLNSIGLENTEENRRKYRQLLFTAGADLNKYISGVIMFHETFYQKTDDGKPFTALLQEQGIIPGIKVDKGVVPMAGTIGEGTTQGLDDLNARCAQYKKDGAQFAKWRCVHKISSTTPSVTALKEIASNLGSRYASICQQNGLVPIVEPEILPDGEHCLARGQKITETVLSYVYHALNEHHVFLEGTLLKPNMVTSGQSFTGEKPSNADIGLATVTALQRGVPSAVPGVVFLSGGQSEEDATLNLNAINQVSGKKPWALTFSYGRALQASCLAKWAGKDENIAAAQEVLLHRAQVNSLASVGKYTGDASADAAASQSLFVANHSY
Protein: Peptide chain release factor RF3 (RF-3) (P0A7I4)
Organism: Escherichia coli (strain K12)
Function: Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.
Subcellular location: Cytoplasm.
Interaction partners:
- Peptide chain release factor RF2
- Peptide chain release factor RF1
- Ribosome-recycling factor
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein bL12
- Large ribosomal subunit protein bL9
- Large ribosomal subunit protein bL20
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein bL33
Sequence:
MTLSPYLQEVAKRRTFAIISHPDAGKTTITEKVLLFGQAIQTAGTVKGRGSNQHAKSDWMEMEKQRGISITTSVMQFPYHDCLVNLLDTPGHEDFSEDTYRTLTAVDCCLMVIDAAKGVEDRTRKLMEVTRLRDTPILTFMNKLDRDIRDPMELLDEVENELKIGCAPITWPIGCGKLFKGVYHLYKDETYLYQSGKGHTIQEVRIVKGLNNPDLDAAVGEDLAQQLRDELELVKGASNEFDKELFLAGEITPVFFGTALGNFGVDHMLDGLVEWAPAPMPRQTDTRTVEASEDKFTGFVFKIQANMDPKHRDRVAFMRVVSGKYEKGMKLRQVRTAKDVVISDALTFMAGDRSHVEEAYPGDILGLHNHGTIQIGDTFTQGEMMKFTGIPNFAPELFRRIRLKDPLKQKQLLKGLVQLSEEGAVQVFRPISNNDLIVGAVGVLQFDVVVARLKSEYNVEAVYESVNVATARWVECADAKKFEEFKRKNESQLALDGGDNLAYIATSMVNLRLAQERYPDVQFHQTREH
Protein: Transportin MOS14 (Importin beta MOS14) (Protein MODIFIER OF SNC1 14) (Transportin-SR) (TRN-SR) (Q8GUL2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as nuclear import receptor for serine-arginine rich (SR) proteins. Regulates nuclear import of SR proteins that are required for proper splicing of the two resistance (R) genes SNC1 and RPS4, a crucial step for their functions in plant immunity.
Subcellular location: Nucleus {ECO:0000269|PubMed:21738492}.
Interaction partners:
- Transportin
- Serine/arginine-rich splicing factor RS31
- GTP-binding nuclear protein Ran-1
- Importin subunit beta-1
- Serine/arginine-rich-splicing factor SR34
- Serine/arginine-rich splicing factor RSZ21
- Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1
- Importin subunit alpha-8
- Importin beta-like SAD2
- Cyclin-L1-1
Sequence:
MEHQNAVKEALNALYHHPDDTVRVHADRWLQNFQGTLDAWQVADNLLHDSSSNLETLIFCSQTLRSKVQRDFEELPPGAFQKLRQSLTTLLKKFHKGPPKVRTQISIAVAALAVHVPAADWGDGGIISWLRDEMHMHPEYVPGFLELLTVLPEETFNYKIAARPDRRRQFEKELTSQMEAALSILSACLKISELKEQVLEAFASWLRLRHGIPGTVLACHPLVHAALSSLNCDPLSEASVNVISELIHHTASPSSGGISAQTPLIQVIVPQILSLQAHLRDSSKDEEDVKAIGRLFADVGDSYVELIATGSDEPMVIVHALLEVTAHPEFDIASMTFNFWHSLQLMLTKRESYSSLGSEASIEVERNRRLHIFQPAYQSLVSLVGFRVQYPEDYQGLSYEDLKEFKQTRYAVADVLIDAALILGGDTTLKILYMKLLEANAQTGNNFQDWRPAEAILFCIWAISNYVSVVEAEVMPQVMALLQNLPQQAQLLQTACLLVGAYSKWLNAAPASVSILPSIIRILMSGMGTSEDCAAAAALAFRHTCDDCRKNLCGYFEDLFNIYCMAINGGGGYKVSAEDSLNLVEALGMVVTELPLDQAKGALEKLCFSAASPLEEAAKEDLEKKHARELTVHIDRFAFLFRYVNHPEAVAAEINKHWAIFRVIFDARPWDMRTMESLCRACKYAVRTSGRYIIDTIGEMLEKIQFHYQQHHQPCFLYLSSEVIKIFGSDPSCAVYLKNLIETLFAHTTCLMTSIKEVTARPDIADDCFLLASRCLRYCPHLFIPSPIFPALVNCAMIGITVQHREACHSILTFLTDIFDLEKSVNEEQFVRIRDNIIIPRGATITRILIASLAGALPSSRLDTVTYSLLALTRTYRLQAVSWAKESVSLIPRTALTETESTKFLQALSDIAYGADVNSLIGQVEELSDVCRRNRTVQELVQAALKPLELNLVTAPVS
Protein: Keratin, type I cuticular Ha2 (Hair keratin, type I Ha2) (Keratin-32) (K32) (Q14532)
Organism: Homo sapiens (Human)
Interaction partners:
- Keratin, type I cuticular Ha5
Sequence:
MTSSCCVTNNLQASLKSCPRPASVCSSGVNCRPELCLGYVCQPMACLPSVCLPTTFRPASCLSKTYLSSSCQAASGISGSMGPGSWYSEGAFNGNEKETMQFLNDRLASYLTRVRQLEQENAELESRIQEASHSQVLTMTPDYQSHFRTIEELQQKILCTKAENARMVVNIDNAKLAADDFRAKYEAELAMRQLVEADINGLRRILDDLTLCKADLEAQVESLKEELMCLKKNHEEEVGSLRCQLGDRLNIEVDAAPPVDLTRVLEEMRCQYEAMVEANRRDVEEWFNMQMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEARYSSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLEGEINTYRSLLENEDCKLPCNPCSTPSCTTCVPSPCVPRTVCVPRTVGMPCSPCPQGRY
Protein: Citrate synthase, mitochondrial (EC 2.3.3.1) (Citrate (Si)-synthase) (Q8VHF5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P00889}.
Interaction partners:
- Aconitate hydratase, mitochondrial
- Cytoplasmic aconitate hydratase
- Malate dehydrogenase, mitochondrial
- ATP-citrate synthase
- Malate dehydrogenase, cytoplasmic
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Fumarate hydratase, mitochondrial
- Pyruvate carboxylase, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Isocitrate dehydrogenase, mitochondrial
Sequence:
MALLTAAARLLGAKNSSCLVLAARHASASSTNLKDILSNLIPKEQARVKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAKGGEEPLPEGLFWLLVTGQMPTEEQVSWLSQEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGINRTKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGAIDSKLDWSHNFTNMLCYTEPQFTELMRLYLTIHSDHDGGNVSAHTSHLVGSALSDTYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLMKFVDSKSG
Protein: BPTI/Kunitz inhibitor domain-containing protein (Q9VCM5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRINLIYFTLLWAFFFSTEVFGKVKIRESDIRRITKMGSYKVRQEKCLFIPSYGRCKKHIAVYGYNIITNRCSEFTYSGCGGNPNRFMTDSQCRNTCYVVPARKTVSEPDYYADDGVTEPMQVDEEDDY
Protein: Single-stranded DNA-binding protein (SSB) (Gene product 5) (gp5) (Protein p5) (Q38504)
Organism: Bacillus phage phi29 (Bacteriophage phi-29)
Function: Single-stranded DNA binding protein required for the elongation during viral DNA replication by strand displacement. Displaced viral DNA strands are transiently coated with the ssDNA-binding protein and therefore protected against nucleases. The latter is then probably removed by the replisome that performs lagging strand synthesis or during the events that lead up to the recombination process. Stimulates in vitro DNA replication several fold. Has helix-destabilizing activity since it removes secondary structure from the ssDNA in replicative intermediates.
Interaction partners:
Sequence:
MENTNIVKATFDTETLEGQIKIFNAQTGGGQSFKNLPDGTIIEANAIAQYKQVSDTYGDAKEETVTTIFAADGSLYSAISKTVAEAASDLIDLVTRHKLETFKVKVVQGTSSKGNVFFSLQLSL
Protein: histone deacetylase (EC 3.5.1.98) (F4J8S1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVVETIERSCEGSKRRHVNGGDIAVPCSGEECSNGDINVAPGVSAKRARVSREMTFEDIYGADALLNDDDDEDDDCDWEPVQAPMEFVKWCCVNCTMSNPGDMVHCCICGEHKESGILRHGYLASPFFKDTGLIEVEEKYGGSSSATSSTAVGFDERMLLHSEFEVKAQPHPERPDRLRAIAASLATAGVFPGRCLPINAREITKQELQMVHTSEHVDAVDTTSQLLYSYFTSDTYANEYSARAARLAAGLCADLATDIFTGRVKNGFALVRPPGHHAGVRHAMGFCLHNNAAVAALVAQAAGAKKVLIVDWDVHHGNGTQEIFEQNKSVLYISLHRHEGGNFYPGTGAADEVGSNGGEGYCVNVPWSCGGVGDKDYIFAFQHVVLPIASAFSPDFVIISAGFDAARGDPLGCCDVTPAGYSRMTQMLGDLCGGKMLVILEGGYNLRSISASATAVIKVLLGENPENELPIATTPSVAGLQTVLDVLNIQLEFWPSLAISYSKLLSELEARLIENKSEKSDEKEGCSGSDMVEMGTKEAFVQLSLGSYDFKIKVILESILPNPS
Protein: Cell invasion protein SipA (Effector protein SipA) (P0CL52)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F-actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments.
Subcellular location: Secreted {ECO:0000269|PubMed:8522512}. Note=Secreted via the type III secretion system 1 (SPI-1 T3SS).
Interaction partners:
- Cell invasion protein SipD
- Inositol phosphate phosphatase SopB
- SPI-1 type 3 secretion system translocon protein SctB
- Surface presentation of antigens protein SpaK
- Chaperone protein SicA
- SPI-1 type 3 secretion system translocon protein SctE
- Guanine nucleotide exchange factor sopE2
- Secreted effector protein SptP
- SPI-1 type 3 secretion system secretin
- Protein PrgH
Sequence:
MVTSVRTQPPVIMPGMQTEIKTQATNLAANLSAVRESATATLSGEIKGPQLEDFPALIKQASLDALFKCGKDAEALKEVFTNSNNVAGKKAIMEFAGLFRSALNATSDSPEAKTLLMKVGAEYTAQIIKDGLKEKSAFGPWLPETKKAEAKLENLEKQLLDIIKNNTGGELSKLSTNLVMQEVMPYIASCIEHNFGCTLDPLTRSNLTHLVDKAAAKAVEALDMCHQKLTQEQGTSVGREARHLEMQTLIPLLLRNVFAQIPADKLPDPKIPEPAAGPVPDGGKKAEPTGINININIDSSNHSVDNSKHINNSRSHVDNSQRHIDNSNHDNSRKTIDNSRTFIDNSQRNGESHHSTNSSNVSHSHSRVDSTTHQTETAHSASTGAIDHGIAGKIDVTAHATAEAVTNASSESKDGKVVTSEKGTTGETTSFDEVDGVTSKSIIGKPVQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKTDTLQSDTTVITGNKAGTTDNDNSQTDKTGPFSGLKFKQNSFLSTVPSVTNMHSMHFDARETFLGVIRKALEPDTSTPFPVRRAFDGLRAEILPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQKEKLAEIALQFAREAGLTRLKGETDYVLSNVLDGLIGDGSWRAGPAYESYLNKPGVDRVITTVDGLHMQR