wanglab/gogpt-training-data huggingface dataset:
Protein: Histone deacetylase 8 (HD8) (EC 3.5.1.98) (Protein deacetylase HDAC8) (EC 3.5.1.-) (Protein decrotonylase HDAC8) (EC 3.5.1.-) (Q9BY41)
Organism: Homo sapiens (Human)
Function: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones.
Subcellular location: Nucleus {ECO:0000269|PubMed:10748112, ECO:0000269|PubMed:14701748}. Chromosome {ECO:0000269|PubMed:10748112}. Cytoplasm {ECO:0000269|PubMed:15772115, ECO:0000269|PubMed:16538051}. Note=Excluded from the nucleoli (PubMed:10748112). Found in the cytoplasm of cells showing smooth muscle differentiation (PubMed:15772115, PubMed:16538051). {ECO:0000269|PubMed:10748112, ECO:0000269|PubMed:15772115, ECO:0000269|PubMed:16538051}.
Interaction partners:
- Histone-binding protein RBBP4
- Paired amphipathic helix protein Sin3a
- Mortality factor 4-like protein 1
- Histone H4
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 1A
- NAD-dependent protein deacetylase sirtuin-1
- NAD-dependent protein deacetylase sirtuin-2
- Sin3 histone deacetylase corepressor complex component SDS3
- Nuclear receptor corepressor 2
Sequence:
MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV
Protein: Protocadherin 1 (F7BJK1)
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:
NDNTPNFASPVITLAIPENTNIGSLFPIPLATDRDAGPNGVASYELQAGPEAQELFGLQVAEDQEEKQPQLIVMGNLDRERWDSYDLTIKVQDGGNPPRASSALLRVTVLDTNDNAPKFERPTYEAELSENSPIGHSVIQVKANDSDQGANAEIDYTFHQAPEVVRRLLRLDRNTGLITVQGPVDREDLSTLRFSVLAKDRGATPKSARAQVVVTVKDMNDNAPTIEIRGIGLVTHQDGMANISEDVAEETAVALVQVSDRDEGENAAVTCVVAGDVPFQLRQASETGSDSKKKYFLQTTTPLDYEKVKDYTIEIVAVDSGNPPLSSTNSLKVQVVDVNDNAPVFTQSITEVAFPENNKPGEVVAEVTASDADSGSNAELVYSLEPEPAAQGLFTISPENGEIRVKTSLDREQRDSYELKVVAADRGSPSLQGTATVLVNVLDCNDNDPKFMLSGYNFSVMENMPALSPVGMVTVIDGDKGENARVQLSVEQDNGDFVIQNGTGTILSSLSFDREQQSTYTFQLKAVDGGVPPRSAYVGVTINVLDENDNAPFITAPSNTSHRLLTPQTRLGETVSQVTAEDIDSGINAELTYSIAGGNPYGLFQIGSHSGAITLEKEIERRHHGLHRLVVKVSDRGKPPRYGTALVHLYVNETLANRTLLETLLVHSLDTPLDIDIAGDPEYERSKQRGNILFGVVAGVVAVALLIALAVLVRYCRQREAKSGYQAGKKETKDLYAPKPSGKAAKGSKSKGKKSKSPKPVKPVEDEDDTGLQKSLKFNLMSDAPGDSPRIHLPLNYPPGSPDLGRHYRSNSPLPSIQLQPQSPSASKKHQVVQDLPPANTFVGTGDTTSTGSEQYSDYSYRTNPPKYPSKQLPHRRVTFSATSQAQELQDPSQHSYYDSGLEESETPSSKSSSGPRLGPLALPEDHYERTTPDGSIGEMEHPENDLRPLPDVAMTGTCTRECSEFGHSDTCWMPGQSSPSRRTKSSALKLSTFVPYQDRGGQEPAGAGSPSPPEDRNTKTAPVRLLPSYSAFSHSSHDSCKDSATLEEIPLTQTSDFPPTATPASAQTAAKREIYL
Protein: Mitotic spindle assembly checkpoint protein MAD1 (Mitotic arrest deficient 1-like protein 1) (MAD1-like protein 1) (Q9WTX8)
Organism: Mus musculus (Mouse)
Function: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate (By similarity). Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y6D9}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9Y6D9}. Nucleus envelope {ECO:0000250|UniProtKB:Q9Y6D9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9Y6D9}. Note=Detected at the nucleus envelope during interphase. From the beginning to the end of mitosis, it is seen to move from a diffusely nuclear distribution to the centrosome, to the spindle midzone and finally to the midbody. Detected at kinetochores during prometaphase. Colocalizes with NEK2 at the kinetochore. Colocalizes with IK at spindle poles during metaphase and anaphase. {ECO:0000250|UniProtKB:Q9Y6D9}.
Interaction partners:
- Mitotic spindle assembly checkpoint protein MAD2A
- Cell division cycle protein 20 homolog
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Dual specificity protein kinase TTK
- Mitotic checkpoint protein BUB3
- Fizzy-related protein homolog
- Origin recognition complex subunit 2
- Mitotic spindle assembly checkpoint protein MAD2B
- Nucleoprotein TPR
Sequence:
MEDLGENTTVLSSLRSLNNFISQRMEGTSGLDVSTSASGSLQKQYEYHMQLEERAEQIRSKSYLIQVEREKMQMELSHKRARVELERAASTNARNYEREVDRNQELLARIRQLQECEATAEEKMREQLERHRLCKQNLDAVSQQLREQEDSLASAREMISSLKGRVSELQLSAMDQKVQVKRLESEKQELKEQLELQQRKWQEANQKIQELQASQDERAEHEQKIKDLEQKLCLQEQDAAVVKSMKSELMRMPRMERELKRLHEENTHLREMKETNGLLTEELEGLQRKLSRQEKMQEALVDLELEKEKLLAKLQSWENLDQTMGLNLRTPEDLSRFVVELQQRELTLKEKNNSITSSARGLEKVQQQLQDEVRQANAQLLEERKKRETHEALARRLQKRNALLTKERDGMRAILGSYDSELTQTEYSTQLTQRLWEAEDMVQKVHAHSSEMEAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKLTLQGDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERGGPIPADLEAASSLPSSKEVAELRKQVESAELKNQRLKEVFQTKIQEFRKVCYTLTGYQIDVTTESQYRLTSRYAEHQTDCLIFKATGPSGSKMQLLETEFSRSVPELIELHLLQQDSIPAFLSALTIELFSRQTSI
Protein: Transcription factor COE3 (Early B-cell factor 3) (EBF-3) (Olf-1/EBF-like 2) (O/E-2) (OE-2) (O08791)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator. Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3' (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H4W6}.
Interaction partners:
Sequence:
MFGIQENIPRGGTTMKEEPLGSGMNPVRSWMHTAGVVDANTAAQSGVGLARAHFEKQPPSNLRKSNFFHFVLALYDRQGQPVEIERTAFVDFVEKEKEPNNEKTNNGIHYKLQLLYSNGVRTEQDLYVRLIDSMTKQAIVYEGQDKNPEMCRVLLTHEIMCSRCCDKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKNAGNPRDMRRFQVVVSTTVNVDGHVLAVSDNMFVHNNSKHGRRARRLDPSEGTAPSYLENATPCIKAISPSEGWTTGGATVIIIGDNFFDGLQVVFGTMLVWSELITPHAIRVQTPPRHIPGVVEVTLSYKSKQFCKGAPGRFVYTALNEPTIDYGFQRLQKVIPRHPGDPERLPKEVLLKRAADLVEALYGMPHNNQEIILKRAADIAEALYSVPRNHNQIPTLGNTPAHTGMMGVNSFSSQLAVNVSETSQANDQVGYSRNTSSVSPRGYVPSSTPQQSNYNTVSTSMNGYGSGAMANLGVPGSPGFLNGSSANSPYGIVPSSPTMAASSVTLPSNCSSTHGIFSFSPANVISAVKQKSAFAPVVRPQASPPPSCTSANGNGLQAMSGLVVPPM
Protein: DNA (cytosine-5)-methyltransferase 1 (EC 2.1.1.37) (DNA methyltransferase 01) (DNA methyltransferase 2) (DNA methyltransferase AthI) (DNA Metase AthI) (M.AthI) (DNA methyltransferase DDM2) (Protein DECREASED DNA METHYLATION 2) (P34881)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Maintains chromatin CpG methylation that plays a role in genomic imprinting, regulation of embryogenesis and seed viability. Required for proper patterns of CG DNA methylation in dividing cells. Required for MEA promoter methylation in seeds.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Adenosylhomocysteinase 1
- ATP-dependent DNA helicase DDM1
- DNA
- Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH4
- Histone deacetylase 6
- Transcriptional activator DEMETER
- Adenosylhomocysteinase 2
- DNA glycosylase/AP lyase ROS1
- DEMETER-like protein 2
- DEMETER-like protein 3
Sequence:
MVENGAKAAKRKKRPLPEIQEVEDVPRTRRPRRAAACTSFKEKSIRVCEKSATIEVKKQQIVEEEFLALRLTALETDVEDRPTRRLNDFVLFDSDGVPQPLEMLEIHDIFVSGAILPSDVCTDKEKEKGVRCTSFGRVEHWSISGYEDGSPVIWISTELADYDCRKPAASYRKVYDYFYEKARASVAVYKKLSKSSGGDPDIGLEELLAAVVRSMSSGSKYFSSGAAIIDFVISQGDFIYNQLAGLDETAKKHESSYVEIPVLVALREKSSKIDKPLQRERNPSNGVRIKEVSQVAESEALTSDQLVDGTDDDRRYAILLQDEENRKSMQQPRKNSSSGSASNMFYIKINEDEIANDYPLPSYYKTSEEETDELILYDASYEVQSEHLPHRMLHNWALYNSDLRFISLELLPMKQCDDIDVNIFGSGVVTDDNGSWISLNDPDSGSQSHDPDGMCIFLSQIKEWMIEFGSDDIISISIRTDVAWYRLGKPSKLYAPWWKPVLKTARVGISILTFLRVESRVARLSFADVTKRLSGLQANDKAYISSDPLAVERYLVVHGQIILQLFAVYPDDNVKRCPFVVGLASKLEDRHHTKWIIKKKKISLKELNLNPRAGMAPVASKRKAMQATTTRLVNRIWGEFYSNYSPEDPLQATAAENGEDEVEEEGGNGEEEVEEEGENGLTEDTVPEPVEVQKPHTPKKIRGSSGKREIKWDGESLGKTSAGEPLYQQALVGGEMVAVGGAVTLEVDDPDEMPAIYFVEYMFESTDHCKMLHGRFLQRGSMTVLGNAANERELFLTNECMTTQLKDIKGVASFEIRSRPWGHQYRKKNITADKLDWARALERKVKDLPTEYYCKSLYSPERGGFFSLPLSDIGRSSGFCTSCKIREDEEKRSTIKLNVSKTGFFINGIEYSVEDFVYVNPDSIGGLKEGSKTSFKSGRNIGLRAYVVCQLLEIVPKESRKADLGSFDVKVRRFYRPEDVSAEKAYASDIQELYFSQDTVVLPPGALEGKCEVRKKSDMPLSREYPISDHIFFCDLFFDTSKGSLKQLPANMKPKFSTIKDDTLLRKKKGKGVESEIESEIVKPVEPPKEIRLATLDIFAGCGGLSHGLKKAGVSDAKWAIEYEEPAGQAFKQNHPESTVFVDNCNVILRAIMEKGGDQDDCVSTTEANELAAKLTEEQKSTLPLPGQVDFINGGPPCQGFSGMNRFNQSSWSKVQCEMILAFLSFADYFRPRYFLLENVRTFVSFNKGQTFQLTLASLLEMGYQVRFGILEAGAYGVSQSRKRAFIWAAAPEEVLPEWPEPMHVFGVPKLKISLSQGLHYAAVRSTALGAPFRPITVRDTIGDLPSVENGDSRTNKEYKEVAVSWFQKEIRGNTIALTDHICKAMNELNLIRCKLIPTRPGADWHDLPKRKVTLSDGRVEEMIPFCLPNTAERHNGWKGLYGRLDWQGNFPTSVTDPQPMGKVGMCFHPEQHRILTVRECARSQGFPDSYEFAGNINHKHRQIGNAVPPPLAFALGRKLKEALHLKKSPQHQP
Protein: Small ribosomal subunit protein eS32B (60S ribosomal protein L41-B) (L47) (Large ribosomal subunit protein eL41B) (YL41) (P0CX87)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
Sequence:
MRAKWRKKRTRRLKRKRRKVRARSK
Protein: Putative mediator of RNA polymerase II transcription subunit 28 (Putative mediator complex subunit 28) (Q54DD4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDTNNTNNINSLENPIDLENDPNILFTELNVKLESLITFLTKNDKDNQIFVDEIIDNKVTDLLIASKELENYFISQQSKYSAEKNKIQLKQEIYKVKKEIENKDRLIERYKNKVKEWKYHFEPLYQSQNHILHSTAQGLSGIENQFSPVFTPMPNTPSILQNLSQAKPSPSLGLGSTIL
Protein: Catabolite control protein A (Q9CF33)
Organism: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Interaction partners:
Sequence:
MVESTTTIYDVARVAGVSMATVSRVVNGNANVKEKTRQKVLEAIAELDYRPNAVARGLASKRTTTVGVILPTITSTYFAAITRGVDDIDSMYKYNMILANSDNDVEKEEKVLETFLSKQVDGIVYMGSSLDEKIRTSLKNSRTPVVLVGTIDGDKEIPSVNIDYHLAAYQSTKKLIDSGNKKIAYIMGSLKDVENTERMVGYQEALLEANIEFDENLVFEGNYSYEQGKALAERLLERGATSAVVSHDTVAVGLLSAMMDKGVKVPEDFEIISGANSPITQYTYPTLTSVNQPLYDLGAVAMRLLTKLMLKEDVEQNQLVLDHEIFSRRSTK
Protein: sn-1-specific diacylglycerol lipase (EC 3.1.1.116) (H0Z867)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MPGIVVFRRRWSVGSDDLVLPAVFLFLLHTTWFVILSVVLFGLVYNPNETCSLNLVDHGRGYLGILLSCMIAELAIIWLSMRGSILYTEPRDSMQYVLYVRLAILVIEFVYAIVGIVWLTQYYTSCNDITAKSVTLGMVVCNWVVILSVCITVLCVFDPTGRTFVKLRATKRRQRNLRTYNLRHRLEEGQASSWTRRLKVFLCCTRTKDSQSDAYSEIAYLFAEFFRDLDIVPSDIIAGLVLLRQRQRAKRNAVLDEANNDILAFLSGMPVTRNTKYLDLKNAQEMQRYREVCYYMLFALAAYGWPIYLMRKPTCGLCRLARSCSCCCLCPSRPRYAPGVTIEEDNCCGCNAIAIRRHFLDENMTSVDIVYTSCHDAVYETPFYVAVDHDKKKVVISIRGTLSPKDALTDLTGDAERLPVEGHHGTWLGHKGMVLSAEYIKKKLEQEMVLSQAFGRDLGRGTKHYGLIVVGHSLGAGTAAILSFLLRPQYPSLKCFAYSPPGGLLSEDAMEYSKEFVTAVVLGKDLVPRIGLSQLEGFRRQLLDVLQRSTKPKWRIIVGATKCIPKSELPEEPEENSVTSNRLWTHPSDLTIALSASTPLYPPGRIIHVVHNHPAEQCCCCEQEDPTYFAIWGDNKAFNEVIISPAMLHEHLPYVVMEGLNKVLENYNKGKTALLSAAKVMVSPTEVDLTPELIFQSQPLPSCPSVQIGTGAIPADRRNSSTKSKSHSEISLEGFYETKPLSPVQKDPVELLLLDTKERLSVELQDRRAPLATMESLSDNESIYSFDSRRSSGFRSIRGSPSLHAVMEKDETHCFYIDPVIPEENPSLSSRTELLAADSLSKHSQETQPPENVLNSGGTTPQRRCSAEGTGSDGERASSSPREEPPLHNGRLADVPSPQVLEFAEFIDSLFNLDSKSSSFQDIYCMMVSDSSSDFAEMPKSVSDQEILLRAQYEPNLVPKPPRLFAGSTDPSSGISVSPSFPLSSSGELMDITPTGVSSQECLATDKIRTSTPSGHVTSPAKQDDLMISAL
Protein: Cytochrome P450 3A1 (EC 1.14.14.1) (CYPIIIA1) (Cytochrome P450-PCN1) (P04800)
Organism: Rattus norvegicus (Rat)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- UDP-glucuronosyltransferase
- Cytochrome P450 1A2
- Cytochrome P450 1A1
- Cytochrome P450 2E1
- Cytochrome P450 4A10
- Aldehyde oxidase 1
- Cytochrome P450, family 2, subfamily j, polypeptide 4
- Estrogen sulfotransferase Ste2
- Cytochrome P450 4A2
- Aromatase
Sequence:
MDLLSALTLETWVLLAVVLVLLYGFGTRTHGLFKKQGIPGPKPLPFFGTVLNYYMGLWKFDVECHKKYGKIWGLFDGQMPLFAITDTEMIKNVLVKECFSVFTNRRDFGPVGIMGKAVSVAKDEEWKRYRALLSPTFTSGRLKEMFPIIEQYGDILVKYLKQEAETGKPVTMKKVFGAYSMDVITSTSFGVNVDSLNNPKDPFVEKTKKLLRFDFFDPLFLSVVLFPFLTPIYEMLNICMFPKDSIEFFKKFVYRMKETRLDSVQKHRVDFLQLMMNAHNDSKDKESHTALSDMEITAQSIIFIFAGYEPTSSTLSFVLHSLATHPDTQKKLQEEIDRALPNKAPPTYDTVMEMEYLDMVLNETLRLYPIGNRLERVCKKDVEINGVFMPKGSVVMIPSYALHRDPQHWPEPEEFRPERFSKENKGSIDPYVYLPFGNGPRNCIGMRFALMNMKLALTKVLQNFSFQPCKETQIPLKLSRQGLLQPTKPIILKVVPRDEIITGS
Protein: Shewanella-like protein phosphatase 1 (AtSLP1) (EC 3.1.-.-) (Q8L774)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Shows phosphatase activity, hydrolyzing the artificial substrate para-nitrophenylphosphate (pNPP) in vitro.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21976480}.
Interaction partners:
- Tyrosine-protein phosphatase RLPH2
- acid phosphatase
- Serine/threonine-protein phosphatase 4 regulatory subunit-like protein
- Probable protein phosphatase 2C 10
- Tyrosine-protein phosphatase At3g09960
- Phosphatidylglycerophosphate phosphatase PTPMT2
- Metal ion-binding protein
- Mitochondrial carrier protein MTM1
Sequence:
MASLYLNSLLPLPPSHPQKLLEPSSSSLLSTSNGNELALKPIVINGDPPTFVSAPARRIVAVGDLHGDLGKARDALQLAGVLSSDGRDQWVGQDTVLVQVGDILDRGDDEIAILSLLRSLDDQAKANGGAVFQVNGNHETMNVEGDFRYVDARAFDECTDFLDYLEDYAQDWDKAFRNWIFESRQWKEDRRSSQTYWDQWNVVKRQKGVIARSVLLRPGGRLACELSRHGVILRVNNWLFCHGGLLPHHVAYGIERINREVSTWMRSPTNYEDSPQMPFIATRGYDSVVWSRLYSRETSELEDYQIEQVNKILHDTLEAVGAKAMVVGHTPQLSGVNCEYGCGIWRVDVGMSSGVLDSRPEVLEIRGDKARVIRSNRDRLHELQVADYI
Protein: Poly(A)-specific ribonuclease PARN (EC 3.1.13.4) (Polyadenylate-specific ribonuclease) (A0A494BZW7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPADLSEFKEMTTCVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSFLSPPKIHVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIGIQAML
Protein: Frizzled-8 associated multidomain protein (Q6EHH9)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHVSLAEALEVRGGPLEEEELWAVLNQSAESLQELLRRADPAALGFIISPWSLLLLPSGSVSFTDENISNQDLRVFTAPEVLQTKSLSSLSAIEKMHIYSLGMTLYWGADYEVPETQPIQLGERLNSILLDMCDDQFYTRLSSRNSLGWLQCPYQKQQLCPSYYYIKQLVKLVLGSLSRVDQLGLKTEEPDRSQAIRDRLRGKGLPTGRTSTVDSFDAQTAISQQAFFNRGLSKSMGFLAFKDQSEEEDSCHFTSSDYNSGYENEVNSHHSHHQLMPSELDRKNYDSGQRKKNWVSSFDLLSLKDQSTEKDFSTNHHRPPRYPXTETIQISNLPKIKDRQLDGSSSTDVLGPFRLDQARHGLEVPTAVAISSAWTGSRKETKIQVLRAAMTLEEPARLHRTSHSDACSSSSESQSIVSSDPEFRQGLKRKDSTSVVAGLEDTDRLQLPGLRSNQHYENPPDGANIRQEMRKRQEEDMIEMQARMAIRQSRLNLYSGDVPRTSMLDLNRDPLREIAMENSLAQRNLRSFLGPEFVKMTTEPCVTLDLPPSILAKKGKTDEIRRKLNIILLTGQRIELICDTKSTCKDVFDIVVAHVGLVEHHLFGFAILKDQEFYFIDLELKLSKVSPDGWKEDTKKKGKSAINFNLYFRVKFFVDDISFLQHSLTCHQYYLQQRKDILDGKLYCDDEAAMLLASLALQAEYGDYQPEVHSMSYFRMEHFLPARVTEKLELTYLKEELPRLHSTYAGASVKEAELEFLRVCQKLPEYGVHFHRVQPEKKSQTGILLGVCPKGVLIFEVHNGTRTPVLRFPWRETKKVSFSKKKISLQNTSDSIKHVFQTDSNKTCQYLLQLCSSQHKFQLQMRARQSSQETKEIEITSMRSLNLQAESVRGFNMGRAISTSSLASSTLNKTAVRPMSIQPDLLKRLSCSDLSALQTHLSNGTRDRKTKNPWEERPRIISKSYHDLSQVAYSPQQMMLNTRMDNPPYSIEGLLSQASLNQMAMSDAESVTGNGRLNKSFSSVHRSLDLQKPESDSSSMDDSGHAYVVGVSMHSVANTSSPVVFKGNKNPNNCVTPTSTSDREITLVKLKKDPKYDFGFQIVGGDTCGKVELGIFISSITPGRPADLDGRLKPGDRLISINSVSLEGVSHQSALDILQGCPEDVSILVSQPKEKFLKDNQSTHSSSHSQRVFPLQDIEADSSSEEQSKLRGHQRLISGSSFGMSVGKCEGSLSSQDSRTESASLSNSQMKSPNNSAKEHPAKQSARTAKYPSLDSTKAGDRKRTQGDGGKGKRSGLTESVDSDRGDSDMDEETIQVARSKGQPRRNPLLRGQHRNELHKASPTPLKPGDAFFVVLEKNDDSLGISVTGGVNTSVKHGGIYVKAVIPKGAAEADGRIQKGDRVLSVNGTSLEGATHKQAVEMLRNTGQVVTLQLEKGQLPVTKVHAPVTPQGTLPIQHDQVVLQGMDRKKTLDYSFVTDENLFEVKLIKNSSGLGFSFSREENNFPGQAGSSIVRVKKLFPGQPASESGKIDIGDVIFKVNGVALKGLSQQEVVSVLRGTSSEVTLLMCRPPAGVLPEISPSMLTPLKSPLPSKSNDGQCNTKGTGNSSDEDEEANEKSMRRLKNPSRRDSYSDSSGTGEEDIISVTDEIATWNATIYQTPSSAIAPNHSQFNTPGIREDTIHTNFYTPQESPCKPELEDSSNPPSPMPYDLTPNQSAVIPQIVLPDAFLSESFSEEQLSIKSLGLKDLEEFEPEVELHVTLTKSEKGSLGFTVTKASDCIGCYIHDIIQDPAKSDGRLRPGDRLIKVNDVDVANMSHTEAVNLLRAAPKTVRLVLGRVLEFPRPQFPSHLLPDIVLTCHKGNIGLQLSSGPDSVSQNIYIQNIKAGSVADCDGSLKPQDILHYINGESTVGMTIEEAEQALESSLPTVALKATRDGTPVVPTSRKTVSQSPKTTKMNGFSSDEGIICIQAAPDVFTPEAGIVQILLEKPASGELGFSLIGGEYGIFVKSISPGGVADTEGSLQVGDRLLQVNGENMIGATHGKAVASIRKTKGTLQISVAREAMPSDTTILNCNGNIDSMTHIEDNRYNEDEDNDVIQSLLDVVHEQTQNFVELNLQNALLSEHFSVEQIEDGLEEKAEDTDCDGSSLPDDSPEQTKVNGVGYYRNKERTQRSAVDDDITWPSTGGQYKLFYKNFSVTKEDLSSLSLVKVQPSSRYTGFSLKAVIQSIHGKLEENTPSREFELLQDLKPTDGCLIGQTKENKKKNRYKNILPYDATRVSLGAENDYINASFIKMPVGNEEFVYIACQGPLPSTVSDFWQMVWEQNSSVISMMTQEIEGGKIKCQRYWPEEPGRPLMISNQLQLTLVMTQHLESFVLRVLELHDIQSEEVRQIAHLNYTAWPDHDTPSDPYQLLTFISFMRHIYKSGPIITHCSAGIGRSGTLICIDVMLALISKDLEFDISNMVHTMRLQRHGMIQTEEQYIFCYQVILYILKRLLAEEKTVK
Protein: AT4g30010/F6G3_40 (ATP-dependent RNA helicase) (Q9SZV4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- ATP synthase subunit beta-2, mitochondrial
- ATP synthase subunit beta-3, mitochondrial
- ATP synthase subunit beta-1, mitochondrial
- Probable inactive purple acid phosphatase 2
- Cytochrome c1 2, heme protein, mitochondrial
- Gamma carbonic anhydrase-like 2, mitochondrial
- ATP synthase subunit epsilon, mitochondrial
- Cytochrome c oxidase subunit 5b-1, mitochondrial
- Serine/threonine-protein kinase STY17
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
Sequence:
MALRRVYSEIRGKKVTELPGYIKSTFSMETVKTSVKRGLDNYNEKYIQTSSVDPILHICFYGMAFSYLVALPNERRHLEHQQHAKEHGGH
Protein: Programmed cell death activator egl-1 (Egg-laying defective protein 1) (O61667)
Organism: Caenorhabditis elegans
Function: Plays a major role in programmed cell death (PCD or apoptosis) by negatively regulating ced-9. Binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to activate the cell-killing caspase ced-3. Required to activate programmed cell death in the sister cells of the serotonergic neurosecretory motor (NSM) neurons during embryogenesis. Required to activate programmed cell death in the sister cells of the M4 motor neuron and I1 pharyngeal neuron during embryogenesis. During larval development, required for the elimination of transient presynaptic components upstream of ced-9, ced-4 and ced-3 apoptotic pathway. Together with ain-1, a component of the miRNA-induced-silencing complex (miRISC), and probably upstream of ced-3 and ced-4, regulates temporal cell fate patterning during larval development.
Subcellular location: Synapse {ECO:0000269|PubMed:26074078}. Note=Localizes to RMED/V synaptic regions in L1 larvae. {ECO:0000269|PubMed:26074078}.
Interaction partners:
- Apoptosis regulator ced-9
- Cell death protein 3
- Secreted protein
- Cell death protein 4
- Checkpoint protein
- Transcription factor cep-1
- Cell death abnormality protein 1
- Homeobox protein ceh-30
Sequence:
MLMLTFASTSSDLLPMSNVFDVQSSVFYNEKNMFYSSSQDFSSCEDSSQFADDSGFFDDSEISSIGYEIGSKLAAMCDDFDAQMMSYSAHASDRSLFHRLLDFFAF
Protein: MTRF1L release factor glutamine methyltransferase (EC 2.1.1.297) (HemK methyltransferase family member 1) (M.HsaHemKP) (Q9Y5R4)
Organism: Homo sapiens (Human)
Function: N5-glutamine methyltransferase responsible for the methylation of the glutamine residue in the universally conserved GGQ motif of the mitochondrial translation release factor MTRF1L.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18541145}.
Interaction partners:
- Peptide chain release factor 1-like, mitochondrial
- Peptide chain release factor 1, mitochondrial
- Multifunctional methyltransferase subunit TRM112-like protein
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- Ferrochelatase, mitochondrial
- Mitochondrial translation release factor in rescue
- Methyltransferase HEMK2
- Nicotinamide phosphoribosyltransferase
- F-box only protein 5
Sequence:
MELWGRMLWALLSGPGRRGSTRGWAFSSWQPQPPLAGLSSAIELVSHWTGVFEKRGIPEARESSEYIVAHVLGAKTFQSLRPALWTQPLTSQQLQCIRELSSRRLQRMPVQYILGEWDFQGLSLRMVPPVFIPRPETEELVEWVLEEVAQRSHAVGSPGSPLILEVGCGSGAISLSLLSQLPQSRVIAVDKREAAISLTHENAQRLRLQDRIWIIHLDMTSERSWTHLPWGPMDLIVSNPPYVFHQDMEQLAPEIRSYEDPAALDGGEEGMDIITHILALAPRLLKDSGSIFLEVDPRHPELVSSWLQSRPDLYLNLVAVRRDFCGRPRFLHIRRSGP
Protein: GTPase-interacting component 2 (Q06648)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for cell size and shape control, bud site selection, bud emergence, actin cytoskeletal organization, mitotic spindle orientation/positioning, and mating projection formation in response to mating pheromone.
Subcellular location: Bud neck {ECO:0000250}. Bud tip {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Cell division control protein 42
- Serine/threonine-protein kinase CLA4
- Protein BNI1
- Rho-type GTPase-activating protein 1
- Cell division control protein 24
- Cell division control protein 12
- Ras-related protein RSR1
- Bud emergence protein 1
- GTPase-interacting component 1
- GTPase-GDP dissociation stimulator BEM4
Sequence:
MTSASITNTGNETMNLPQMRSIWLDEDEEAEKLYGLQAQQFMGSDDEENLGITFINSDKPVLSNKKNIELPPLSPNSHPSCHHRRSNSNSAKSKESSSSSSSANKTNHKKVFLKLNLLKKKLLGAQPDIRGKGISTPFDFQHISHADTRNGFQDEQLQEPSSLSTEIKDDYTSSSSKRDSKSLNKAFVTERIPANRESKLISRSHENKTSRLSVARSISVTSSNYSKNTQGNNHSINGRVVSTSTMATSIFEYSPNASPKQFKNKSHALGHRYTNSTDSSESSLDFLKNYNFPTLLEDKPILDFLPRSQRSSAYRSLLETPNSNKDSAKAFFPSRQSPLPKRRNSIATPSPQSKFSYSDSPVNHRKSFDDVLYSFNQLEPLQT