wanglab/gogpt-training-data huggingface dataset:
Protein: RapF inhibitor (Signaling peptide PhrF) (P71001)
Organism: Bacillus subtilis (strain 168)
Function: Signaling molecule involved in the regulation of genetic competence development. Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (By similarity). Stimulates expression of the genes controlled by ComA, a transcriptional factor that regulates the development of genetic competence. Acts by inhibiting RapF, which regulates the activity of ComA.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P94416}. Cytoplasm {ECO:0000250|UniProtKB:P94416}. Note=Produced through an export-import maturation process. {ECO:0000250|UniProtKB:P94416}.
Interaction partners:
- Regulatory protein RapF
- Regulatory protein RapC
- Competence and sporulation stimulating factor
- RapK inhibitor
- Response regulator aspartate phosphatase I
- Response regulator aspartate phosphatase J
- Phosphatase RapE inhibitor
- Response regulator aspartate phosphatase H
- RapG inhibitor
- Phosphatase RapH inhibitor
Sequence:
MKLKSKLLLSCLALSTVFVATTIANAPTHQIEVAQRGMI
Protein: UDP-glycosyltransferase 71B5 (EC 2.4.1.-) (O23382)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses low quercetin 3-O-glucosyltransferase activity in vitro.
Interaction partners:
Sequence:
MKIELVFIPLPGIGHLRPTVKLAKQLIGSENRLSITIIIIPSRFDAGDASACIASLTTLSQDDRLHYESISVAKQPPTSDPDPVPAQVYIEKQKTKVRDAVAARIVDPTRKLAGFVVDMFCSSMIDVANEFGVPCYMVYTSNATFLGTMLHVQQMYDQKKYDVSELENSVTELEFPSLTRPYPVKCLPHILTSKEWLPLSLAQARCFRKMKGILVNTVAELEPHALKMFNINGDDLPQVYPVGPVLHLENGNDDDEKQSEILRWLDEQPSKSVVFLCFGSLGGFTEEQTRETAVALDRSGQRFLWCLRHASPNIKTDRPRDYTNLEEVLPEGFLERTLDRGKVIGWAPQVAVLEKPAIGGFVTHCGWNSILESLWFGVPMVTWPLYAEQKVNAFEMVEELGLAVEIRKYLKGDLFAGEMETVTAEDIERAIRRVMEQDSDVRNNVKEMAEKCHFALMDGGSSKAALEKFIQDVIENMD
Protein: Protein Ku (Gp206) (Omega-Ku) (Q853W0)
Organism: Mycobacterium phage Omega (Mycobacteriophage Omega)
Function: Required for replication of viruses with short cos ends (4 bases). Stimulates dsDNA end-joining by host LigD; in conjunction with M.smegmatis or M.tuberculosis LigD can reconstitute NHEJ in S.cerevisiae. Binds dsDNA with either blunt, 5'- or 3-overhangs, protecting it from host exonuclease degradation.
Interaction partners:
Sequence:
MRAVWTGAVNFGLVNVPVKMYAATEEHDLKGHLAHVQDGGRIRYHKVCETCGEQVHTADLGKVFEVDGQTALLTDEDLAELPSENNKVIDVVEFVPAGEVDPILLDKPYYLNAEGSVRPYALLARTLSDADKVAIVRVTLRSKEHLAVLRVTGKNEVLTLQTLRWPDEVREPDFPKLDNKPELSEAELKVAAMLVDELSAPFNPDKHQDTYKVELRALVESKLEPVEVPEDVSGLLAKLEASVKPKQAKPDIRTWAKAQGFKISARGRIPKDIVDKYEGAMA
Protein: Uncharacterized protein (Q4GYM8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MASFLPSQVTARNSNGLAGVKSDAVSSTMSTHFTPLNHSNTNTNTNATIPQPGCLSTQCSGTGTVNNDVQVVTAASGCNATNNPFDIFSSYVASSALNSVAISNNVVNSHVEASKEDVSVSRLSNNSATLAPTADFNPALPGCVAEMQKFMSDRSIRPEEKEAVSIIEFALGRYAVARMQVKQRLEEGEAILRRWDELQKAIECAAASFQATSAASLTDSFLFTSPQQPLQHMVPNGPVGSVKGQRGRSRVDVDLSECKGILSHVGTFAQSFKKLREEQDQVCAALGDIQTKSPSHNNGQSLGFPFVVPPQREQLSLGGHPVDDLQVTVHVCGLRLRQQWEEVVGASCGDLLRGLKENVTANRALVALQGLCNDARERLNDMRTRIARLGSNRVEEAGRLDERLAAMDSYDPTMEEYEARRRQIDTELSTVKGWLEAIVQVQASADQLHETLRSWSAGIDIGTVLSPHQHQQQQEGPASANDRASSCWAVSTPSATTAAASIAECRLSSIRSSCQTGGAPDCRATYPQVNAAPSPVMRMIGTTVLPLTRYDSTRVGDDTTTATTAPTTTTFVAANGVTGVMANQNVSMPPQHVENICISVPTSGNEGSAVVCSDKKLPSSSDIQTANAPKELGNGALVVQLKDECAAVAVRDGTVADAAVVVEANKRKVRPSNETNNGEGNAAVCRDENDDDVDDVDDDDDDDADSRTSLFHPSAFSGGDRKKRRRREREPKRNGCMNTFASFFRAVINRATDAGESDGGSRTDGEEYEGSDASDDEDTEQLHKKTRVRLW
Protein: 7-dehydrocholesterol reductase (7-DHC) (Delta-14-SR) (EC 1.3.1.21) (EC 1.3.1.70) (3-beta-hydroxysterol Delta (14)-reductase) (C-14 sterol reductase) (Delta(14)-sterol reductase TM7SF2) (Sterol C14-reductase) (Sterol Delta(7)-reductase) (Transmembrane 7 superfamily member 2) (H0YE57)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU369120}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369120}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
INLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYIFRVANHQKDLFRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFWGVARHFNYVGDLMGSLAYCLACGGGHLLPYFYIIYMAILLTHRCLRDEHRCASKEFRVSSTAVLPAQTDFL
Protein: DnaJ heat shock protein family (Hsp40) member B6 (C9J2C4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFGSGFSSFDTGFTSFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKMVNGRKITTKRIVENGQERVEVEEDGQLKSLT
Protein: Uncharacterized protein C1840.07c (O74480)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Type 1 phosphatases regulator ypi1
Sequence:
MSSLGKLLKLTLLGILLSFSCKFVFGYFNVNQLFDHEFIKVFPNFKGNVEAKIKYPTVVYAIGDIHGDFPNALDVLSAAGVVSPVFPHEWTAGNATLVQTGDVVDRGPDTRKLFRWFNDLHKQAEKHGGRVVRLLGNHEFMNAKGDWRYVHPGDKASYPEPSEENRIIDWGHSGEIGNLLLSEYNVTYKDNTTGSHFMHAGLSPEWAYREETVNELGKELLSHFMSREKIPEYLEDFWAIEGPMWYRGLAQLSEEEACEVALNVTKTLNVNRLVMGHTPQFHGIVSRCEGRILLIDTGLCSAYAGERAVLRISQNDTDSIVEAVYRGKIVKL
Protein: FYVE-type domain-containing protein (Q57UA1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPSDHQLSKSTMAGAKHMGQHRRVSIKVCRQPNTRLGSSKGIGTPHERPRPSRGQSQRLRCSCCLQDLPSQVDGNLSDNTCWRCGYMTCTSCRSNLSPSAHRWVCTTCSKKISFTWLFQKTVHGADLLLRVLEFCEPRVQPLLKCVFATEDTQKTSQCEKTPTNGRGAVSQVTSCQKPKHVAVTSKGEETEEDAKLLVKGATQRRSAAKATPRKGKISSKYVTKAQSPEMQVRSPPPSPSRTPFKFLSNSPSGNKTPLKRIEKNTNLSSNGASPTAKPGIAHTTIPSDGGTSTIGKNVGAGTMVGVSGSRGGGHRQDELGTEVKNGNQFLRCDGMHPDPKCLVFSYSNDTHASSQLSFAISGADSPPPRFPNFSKFLDDQEGLRREFDEPQNRRLQHLFAEKDEPQKNYSDLVTVETSEGVSPLKVVECAEADNNFPIPPKLALNFCKLGLVSNHVTDAEQEPSAVHSSNNKLICKPTARVSINAESATQRGPKKNSCGSGGPHGSEHACTSRLVRSNTINGDCIDAVFKRIQPCLTTVVHDSNGAYTGGPQNGNTADAGTGTGTKLGASNKTHSRAPTIKPPSKTRTTSSSRTFKTPRALFSDSRLCGKDADSNSPHTRRGSARYLLAIEKDGVHSPRPAPVLAGVKPRGRTPLTARPPSSRCSGECGALARGSSILTRQGVSVPRQRTCEGQGSRHARVNTPLQRIHSSRLVPAEDSQGRYLPSHGNADAVKPRLSINSGQSVQLVPPAPLTVNPSRGRAVGTLNGKGATSTGGNSQTNLSRGGANGASTSRFIAQRTWNLL
Protein: 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34) (P00347)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:6546784}; Multi-pass membrane protein {ECO:0000269|PubMed:1374417}. Peroxisome membrane {ECO:0000250|UniProtKB:P04035}; Multi-pass membrane protein {ECO:0000269|PubMed:1374417}.
Interaction partners:
Sequence:
MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASALAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTTEHSKVSLGLDEDVSKRIEPSVSLWQFYLSKMISMDIEQVVTLSLAFLLAVKYIFFEQAETESTLSLKNPITSPVVTPKKAPDNCCRREPLLVRRSEKLSSVEEEPGVSQDRKVEVIKPLVVETESASRATFVLGASGTSPPVAARTQELEIELPSEPRPNEECLQILESAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSTKLPEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDGKEYQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETPEGFAVIKDAFDSTSRFARLQKLHVTMAGRNLYIRFQSKTGDAMGMNMISKGTEKALLKLQEFFPEMQILAVSGNYCTDKKPAAINWIEGRGKTVVCEAVIPAKVVREVLKTTTEAMIDVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVRSHMVHNRSKINLQDLQGTCTKKSA
Protein: CBL-interacting serine/threonine-protein kinase 22 (EC 2.7.11.1) (SNF1-related kinase 3.19) (SOS2-like protein kinase PKS14) (O80902)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity).
Interaction partners:
- Leucine-rich repeat
Sequence:
MAEDSNSSESIIVNVTGDDNKSALFGKYDLGKLLGSGAFAKVYQAEDLQNGGESVAIKVVQKKRLKDGLTAHVKREISVMRRLRHPHIVLLSEVLATKTKIYFVMELAKGGELFSRVTSNRFTESLSRKYFRQLISAVRYCHARGVFHRDLKPENLLLDENRDLKVSDFGLSAMKEQIHPDGMLHTLCGTPAYVAPELLLKKGYDGSKADIWSCGVVLFLLNAGYLPFRDPNIMGLYRKIHKAQYKLPDWTSSDLRKLLRRLLEPNPELRITVEEILKDPWFNHGVDPSEIIGIQADDYDLEENGKILNAFDLISSASSSNLSGLFGNFVTPDHCDQFVSDESTAVIMRKVEEVAKQLNLRIAKKKERAIKLEGPHGVANVVVKVRRLTNELVMVEMKNKQRDVGLVWADALRQKLRRLINQPVYKVPDKP
Protein: F16F4.11 protein (Sequence-specific DNA binding transcription factor) (Q9LMN5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein YIP
- Protein YIP
- Protein YIP
Sequence:
MDGNFPQGGVVRSGASSYGGFDLQGSMRVHHQDSMNQQHRHNPNSRPLHEGLPFTMVTGQTCDHHQNQNMSMSEQQKAEREKNSVSDDDEPSFTEEGGDGVHNEANRSTKGSPWQRVKWTDKMVKLLITAVSYIGDDSSIDSSSRRKFAVLQKKGKWKSVSKVMAERGYHVSPQQCEDKFNDLNKRYKKLNDMLGRGTSCQVVENPALLDSIGYLNDKEKDDVRKIMSSKHLFYEEMCSYHNGNRLHLPHDLALQRSLQLALRSRDDHDNDDSRKHQMEDLDDEDHDGDGDEHDEYEEQHYAYGDCRVNHYGGGGGPLKKIRPSLSHEDGDHPSHVNSLECNKVSLPQIPFSQADVNQGGAESGRAGSVQKQWMESRTLQLEEQKLQIQVELLELEKQRFRWQRFSKKRDQELERMRMENERMKLENDRMGLELKQRELGVEL
Protein: Probable nicotinate phosphoribosyltransferase (NAPRTase) (EC 6.3.4.21) (Q9UTK3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis.
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase
- Nicotinamide riboside kinase
- NAD-capped RNA hydrolase
- Putative purine nucleoside phosphorylase
- Uncharacterized protein C24B11.05
- IMP-specific 5'-nucleotidase 1
- Putative nicotinamide mononucleotide adenylyltransferase
- Nicotinamidase
- Putative glutamine-dependent NAD
Sequence:
MSEPAVVSILDTDLYKLTMLQAVLEHYPDAQVSYKYTNRSPKMALNQEAYNWLREQIRGLRNLHLLPEEEQWLRKNCPYLKESFYEFMHEFEFDPENSISLNYDSETKDLSIFIHGLWKNTIFYEIPLLALVSESYFKFVDKDWSPEGQFEKAYEKGKRLIRAGCAFTDFGTRRRRDPHTQEIVLQGLMKAQEDFKGPGSFLGTSNVYFAAKYNLNVSGTVAHEWYMGIAAITQNYKQANRIASLKWVQTFGTSLLIALTDTFSTDVFLKSFTANSADDLANVFHGVRQDSGCAEEYIEKVVKHYKSIGVDPSTKVIVHSDALNVDRCIELYKYCEKCGIKSAFGIGTNLTSDFQKVSNPSEVSKPMNIVIKLFSAEGTKAVKISDDIMKNTGDRDAVIQAKHQLCLPIA
Protein: Costars domain-containing protein (O62234)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSIACARIDKTIFKFKEMEQNVATQSKDDVYSKDFTQKKMDKSSSEYGRPKPGTLTEQRAKKAAAHVHREMLTLCEVVEDYGKQEKEGDPIRITFGRLFTIYVNISDKVVGTLLRARKHKMIDFEGEMLFQKRDDHVIITLLLSGAQLKEAIRAHAAANPKE
Protein: Cell fusion protein dni1 (Delayed minus-nitrogen induction protein 1) (O14107)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Cell membrane protein which plays a relevant role in coordinating membrane organization and cell wall remodeling during mating.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19627505}; Multi-pass membrane protein {ECO:0000269|PubMed:19627505}. Cell tip {ECO:0000269|PubMed:19627505}. Note=Localizes to the tip of shmoos which requires fus1, actin and lipid rafts.
Interaction partners:
- Plasma membrane fusion protein prm1
- Cell fusion protein fus1
Sequence:
MLFLHSVVQGTGTLCTLAAWILLALVMTGCQSSTTSKFQLFSLATNVAQINVGYFNMCVLSANATLICKPQFTGCPGLTSISLTDVRSKFLINEVHPWMIVFSFCVCGVSFLMGVVSSLPLIGRLEFLRNIRISLSFFSFFSILVTALFAHVAVSSFVMAVGNGTQNRVTASLGKKAMIFLWCSMGLVTLTGITDSIILLVTSRTKKIRKTILEKSKVLTPSSSFSSKSSTTKY
Protein: RING-box protein 2 (Rbx2) (EC 2.3.2.27) (EC 2.3.2.32) (RING finger protein 7) (Sensitive to apoptosis gene protein) (Q9WTZ1)
Organism: Mus musculus (Mouse)
Function: Probable component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription (By similarity). CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets (By similarity). Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the substrate. Promotes the neddylation of CUL5 via its interaction with UBE2F. May play a role in protecting cells from apoptosis induced by redox agents (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9UBF6}. Nucleus {ECO:0000250|UniProtKB:Q9UBF6}.
Interaction partners:
- Cullin-5
- Elongin-B
- Elongin-C
- Cullin-2
- Cullin-1
- Cullin-4A
- Core-binding factor subunit beta
- NEDD8-conjugating enzyme UBE2F
- S-phase kinase-associated protein 1
- Ubiquitin-like protein NEDD8
Sequence:
MADVEDGEEPCVLSSHSGSAGSKSGGDKMFSLKKWNAVAMWSWDVECDTCAICRVQVMDACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVVQRIGK
Protein: At3g04210/T6K12_17 (Disease resistance protein (TIR-NBS class)) (Q8H1N6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Receptor-like protein 34
- Receptor-like protein 31
- At3g04640
- Probable disease resistance protein At5g45490
- Probable disease resistance protein At5g45510
- Receptor-like protein 32
- RPW8-like protein 3
- Probable disease resistance protein At5g66900
- Receptor-like protein 33
- Probable disease resistance protein RDL6
Sequence:
MDSYFFLGTVVVVALAIYTLLGTISFMVYRKFRLHQEKNNISSCFSFSSCFSFSSSSSTSSPGRKHQVFPSFHGADVRKSFLSHIMKEFKSKGIDIFIDKDIKRGKSIGPELTEAIRGSRVAIVFLSRKYASSSWCLNELALIMKCRKELGLTVMTLFYDLDPTDVRKQTGDFGMAFKETCKGKTKDEIGRWRHALEEVAKIAGYHSSIWDNEADMIGIVTTDISNTLNISTPSSDFSDLVGMEDHMKKLERMLYLDLNDVRMIGIWGPPGIGKTSIARVLFRKHSDSFDLSVFMETVKGYTRPGCSDEHGLKLHLQQQFLSQIFNQKDVEVPHLGVVQDRLRDKRVLVVLDDVDQSAQLEAMAKENKWFGPGSRIIITTQDRRLLKAHGIKDVYKVDLPPPDDAFQIFCMYAFGKTSPKHGFEELAWEATYLSGIHPSGIKSMGSYFRKMSKPEWVNALQRLRTSKLDSESPRTHRKLINRLRNVKQKMLSNTLSRIRKHQIASAAAKAASVYETSIKEEVDSSAESLNH
Protein: Epstein-Barr nuclear antigen 1 (EBNA-1) (EBV nuclear antigen 1) (EC 3.1.21.-) (Q3KSS4)
Organism: Epstein-Barr virus (strain GD1) (HHV-4) (Human gammaherpesvirus 4)
Function: Plays an essential role in replication and partitioning of viral genomic DNA during latent viral infection. During this phase, the circular double-stranded viral DNA undergoes replication once per cell cycle and is efficiently partitioned to the daughter cells. EBNA1 activates the initiation of viral DNA replication through binding to specific sites in the viral latent origin of replication, oriP. Additionally, it governs the segregation of viral episomes by mediating their attachment to host cell metaphase chromosomes. Also activates the transcription of several viral latency genes. Finally, it can counteract the stabilization of host p53/TP53 by host USP7, thereby decreasing apoptosis and increasing host cell survival.
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:P03211}.
Interaction partners:
Sequence:
MSDEGPGTGPGNGLGQKEDSSGPEGSGGSGPQRRGGDNHGRGRGRGRGRGGGRPGAPGGSGSGPRHRDGVRRPQKRPSCIGCKGAHGGTGSGAGAGGAGAGGAGAGGGAGAGGGAGGAGGAGGAGAGGGAGAGGGAGGAGGAGAGGGAGAGGGAGGAGAGGGAGGAGGAGAGGGAGAGGGAGGAGAGGGAGGAGGAGAGGGAGAGGAGGAGGAGAGGAGAGGGAGGAGGAGAGGAGAGGAGAGGAGAGGAGGAGAGGAGGAGAGGAGGAGAGEEAGGAGAGGGAGGAGAGGAGGAGAGGAGGAGAGGAGGAGAGGGAGAGGAGAGGGGRGRGGSGGRGRGGSGGRGRGGSGGRRGRGRERARGRSRERARGRGRGRGEKRPRSPSSQSSSSGSPPRRPPPGRRPFFHPVGDADYFEYLQEGGPDGEPDVPPGAIEQGPTDDPGEGPSTGPRGQGDGGRRKKGGWFGKHRGQGGSNPKFENIAEGLRVLLARSHVERTTEEGNWVAGVFVYGGSKTSLYNLRRGIALAVPQCRITPLSRLPFGMAPGPGPQPGPLRESIVCYFMVFLQTHIFAEVLKDAIKDLVMTKPAPTCNIKVTVCSFDDGVDLPPWFPPMVEGAAAEGDDGDDGDEGGDGDEGEEGQE
Protein: Smad6a protein (A2VCX3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
RLCGPVKDDTPPPPYSHLSPLPEHKPLNSSLPMLPYIETEATRSAGGLSQDYSDASMSPSSLAQNHWCNVAYWELRTRVGRLYPVHDASLSIFYDLPQGTGLCLGLLPLSPRSTSVQRTRGKIGHGILLSKEPDGVWAYNRSQHPIFVNSPTLEHHPYLSLTVRRVMPGYSIKVFDYEKSCQMQPASHPVHPEGPYDPNSVRISFAKGWGPCYSRQFITSCPCWLEILLNNHR
Protein: FI01140p1 (FI14607p1) (Mind the gap, isoform G) (Mind the gap, isoform H) (Q0KIA5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTEARPLPLGVPAFRPIPQKQLAATQPSAPSSTPAERRVAVDTPEPRVSVNNKLVSSIDQPHSNRTFHVANPVVSQPVAVPVFQAMPQSIARIANVGKEHRTVSSHPNYLQFEEPKFDLKDVTVEELAAAANVTVDTIKHAIYVREQQLKAEHRAQLAAKLREEFMRTSTVRTTTTTTTTTTTTPRPQKSLAEHKVSKVMNAPKEYYPVGYDKNFDDNFKSKVDLPPTSFSCAKQKHFPGLYADTDLGCMVFHVCALTDDGMVRKSFLCPENTLFDQTILKCNWWFYVDCSSSTSVYDSNIPISKSYQLMKSLTYFSKYAGGQRHEQGGDKDENALDIDSLRESMEGVARRQEQAKKAELRVEEQRSMPKEDHEHVVPAEAEQQLSN
Protein: Cyclin T1 (A0A8I6G622)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEGERKNNNKRWYFTREQLENSPSRRFGVDSDKELSYRQQAANLLQDMGQRLNVSQLTINTAIVYMHRFYMIQSFTQFHRYSMAPAALFLAAKVEEQPKKLEHVIKVAHTCLHPQESLPDTRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRDCTMSQTGKGTESQLL
Protein: Protein HIRA (Histone regulator protein) (Q9LXN4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone chaperone involved in maintining knox genes silencing throughout leaf development. Involved in heterochromatic and euchromatic gene silencing, especially upon salt stress. Involved in gene expression reprogramming during dedifferentiation probably by modifying histone H3.3 recruitment at the nucleolus. Contributes to maintenance of silencing of pericentromeric repeats and certain transposons.
Subcellular location: Nucleus {ECO:0000269|PubMed:25086063}. Nucleus, nucleolus {ECO:0000269|PubMed:25086063}. Note=Localized at rDNA loci in the nucleolus. {ECO:0000269|PubMed:25086063}.
Interaction partners:
- Probable histone chaperone ASF1A
- Histone chaperone ASF1B
- Histone H4
- Transcription factor AS1
- Protein RIK
- Transcription factor bHLH145
- Histone H3.3
- Protein CHROMATIN REMODELING 20
Sequence:
MIAEKPFWVKHEGLQIFSIDVQPNGERFATGGGDHKVRIWNMKSVDKDLQNIDTKERLLATLRDHFGSVNCVRWAKNSRYVASGSDDQVIQIHERKPGSGTTEFGSGEAPDVENWKAVMTLRGHTADVVDLNWSPDDSMLASGSLDNTVHIWNMRTGMCTTVLRGHLSLVKGVTWDPIGSFIASQSDDKTVIIWRTSDWGMAHRTDGHWAKSLGSTFFRRLGWSPCGHFLTTTHGFQKPKHSAPVLERGEWSVAYDFLGHSAPIIVVRFNHSMFKRIPSSTHETKQVGWSNGTSKSGEKDLQSYNVIAMGSQDRTITVWTTGSARPLFVAKHFFGQSVVDLSWSPDGYSLFACSLDGTVAMIHFDPKELGVRLTDTELDELKKSRYGDVRGRQANLVESPAQLLLETASTKQAGSKRAASDVQQNQVTTKPSVSVESTAKRRKSQVDDRNKAAESTGQTLNKASTLNRVSSPVNQKVYRRPDGRKRIIPEAVGVPQQENNIMINGESHNFLPASAAAPAKGDSGDFPVEISNRDLSGKEIVCRNPDLKERSRITARATITESLVIEKVPGTSGRDGVLNVEQSVGIKESSSTDLLIRVFDWKDGEAAPPVCLEACPREHALDTVGAVSTSMVKETEISCKKSGETLWSDRIMGRVTVLAGNPNFWAAGCEDGSLQVYTKCGRRAMPTMMMGSAATFIDCDDSWKLLLVTRKGSLYVWDLFNRKCVLHDSLSSLVSSDVNLSSTVKGTIKVISVKLSKSGSPLVVLATRHAFLFDTSLMCWLRVADDCFPASNFSSSWNLGSAPCGELAGLQVDVRKYMARKPGWNRITDDGTQTRAHLESQLASSLALESPNEYRQCLLAYVRFLAREADESRLREVCESFLGPPTGMAEAASSDTNLSWDPYVLGVKKHKLLRNDILPAMASNRKVQRLLNEFIDLLSEYEDVETADPAPKGSTPTMNCGGVPSSLDQIGSDPPAMTATTPMTIDNDKPVSLENPAALDIGVCEKTGSEDRDKQDQNSRDSGS
Protein: Putative uncharacterized protein YKR047W (P36140)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MRFNIYFSLHTYMYIHIYIYICMYTYVYKYMNTVMTTLAKCVGIMTACIQEPVPACQQNRLALRQIPRRHPPSRDHHLLLRLRPRPLLLRPPRTRIPRLRR
Protein: Peroxidase 5 (Atperox P5) (EC 1.11.1.7) (Q9M9Q9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- MLP-like protein 31
- Transcription factor MYB51
- Probable WRKY transcription factor 11
Sequence:
MERFSLRFVLMMVSIILTSSICQAQLSPTFYDQSCRNALSKIRSSVRTAIARERRMAASLIRMHFHDCFVHGCDASILLEGTSTIESERDALPNFKSVRGFEVIDKAKSEVEKVCPGIVSCADIIAVAARDASEYVGGPKWAVKVGRRDSTAAFKALANSGELPGFKDTLDQLSGLFSKKGLNTRDLVALSGAHTIGQSQCFLFRDRLYENSSDIDAGFASTRKRRCPTVGGDGNLAALDLVTPNSFDNNYYKNLMQKKGLLVTDQVLFGSGASTDGIVSEYSKNRSKFAADFATAMIKMGNIEPLTGSNGEIRKICSFVN
Protein: Beta-glucosidase 18 (Os4bglu18) (EC 3.2.1.21) (Q7XSK0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Hydrolyzes glycosides and monolignol glucosides. Can hydrolyze para-nitrophenyl beta-D-glucopyranoside (pNPGlc) in vitro. Hydrolyzes para-nitrophenyl beta-D-fucopyranoside, para-nitrophenyl beta-D-galactopyranoside and para-nitrophenyl beta-D-xylopyranoside in vitro. Hydrolyzes the monolignol glucosides coniferin and syringin with high catalytic efficiencies.
Interaction partners:
- Beta-glucosidase 6
- Beta-fructofuranosidase, insoluble isoenzyme 3
- Beta-glucosidase 24
- Endoglucanase 8
- Beta-glucosidase 25
- beta-fructofuranosidase
- glucan endo-1,3-beta-D-glucosidase
- glucan endo-1,3-beta-D-glucosidase
- beta-fructofuranosidase
- Endoglucanase 11
Sequence:
MAGGSKTRIHASLVSTLLLLLPLASAIHRSDFPASFLFGTATSSYQIEGAYLEGNKSLSNWDVFTHLPGNIKDGSNGDIADDHYHRYEEDVELMNSLGVNAYRFSISWSRILPKGRFGGVNPAGIDFYNKLIDSILLKGIQPFVTLTHYDIPQELEDRYGAWLNAEIQSDFGHFADVCFGAFGDRVKYWTTFNEPNVAVRHGYMLGTYPPSRCSPPFGHCARGGDSHAEPYVAAHNVILSHATAIEIYKRKYQSKQRGMIGMVLYSTWYEPLRDVPEDRLATERALAFETPWFLDPLVYGDYPPEMRQILGGRLPSFSPEDRRKLRYKLDFIGVNHYTTLYARDCMFSDCPQGQETQHALAAVTGESNGLPIGTPTAMPTFYVVPDGIEKMVKYFMRRYNNLPMFITENGYAQGGDSYTDAEDWIDDEDRIEYLEGYLTKLAKVIRDGADVRGYFAWSVVDNFEWLFGYTLRFGLYYIDYRTQERSPKLSALWYKEFLQNLHENQ
Protein: Protein YobF (P64508)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Cold shock-like protein CspC
- Cell division topological specificity factor
- Ribosome-associated inhibitor A
- DNA topoisomerase 4 subunit A
- Uncharacterized protein YaeQ
- Elongation factor Tu 1
- Elongation factor Tu 2
- Protease 7
- Ribonuclease E
- HTH-type transcriptional regulator RcdA
Sequence:
MCGIFSKEVLSKHVDVEYRFSAEPYIGASCSNVSVLSMLCLRAKKTI
Protein: Dynein light chain roadblock-type 1 (Dynein light chain 2A, cytoplasmic) (P62627)
Organism: Mus musculus (Mouse)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9NP97}.
Interaction partners:
- Cytoplasmic dynein 1 heavy chain 1
- Cytoplasmic dynein 1 intermediate chain 2
- Cytoplasmic dynein 1 light intermediate chain 2
- Dynein light chain 2, cytoplasmic
- Cytoplasmic dynein 1 intermediate chain 1
- Cytoplasmic dynein 2 intermediate chain 2
- Cytoplasmic dynein 1 light intermediate chain 1
- Dynein light chain 1, cytoplasmic
- Cytoplasmic dynein 2 intermediate chain 1
- Cytoplasmic dynein 2 light intermediate chain 1
Sequence:
MAEVEETLKRLQSQKGVQGIIVVNTEGIPIKSTMDNPTTTQYANLMHNFILKARSTVREIDPQNDLTFLRIRSKKNEIMVAPDKDYFLIVIQNPTE
Protein: Phospholipase C (EC 3.1.4.3) (Phosphatidylcholine cholinephosphohydrolase) (W8EFP8)
Organism: Clostridium perfringens
Interaction partners:
Sequence:
MKRKICKALICAALATSLWAGASTKVYAWDGKIDGTGTHAMIVTQGVSILENDLSRNEPESVRKNLEILKENMHELQLGSTYPDYDKNAYDLYQDHFWDPDTDNNFSKDNSWYLAYSIPDTGESQIRKFSALARYEWQRGNYKQATFYLGEAMHYFGDIDTPYHPANVTAVDSAGHVKFETFAEERKEQYKINTAGCKTNEDFYADILKNKDFNAWSKEYARGFAKTGKSIYYSHASMSHSWDDWDYSAKVTLANSQKGTAGYIYRFLHDVSEGNDPSVGKNVKELVAYISTSGEKDAGTDDYMYFGIKTKDGKTQEWEMDNPGNDF