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.-) (B1WC68)
Organism: Rattus norvegicus (Rat)
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:0000250|UniProtKB:Q9BY41}. Chromosome {ECO:0000250|UniProtKB:Q9BY41}. Cytoplasm {ECO:0000250|UniProtKB:Q9BY41}. Note=Excluded from the nucleoli. Found in the cytoplasm of cells showing smooth muscle differentiation. {ECO:0000250|UniProtKB:Q9BY41}.
Interaction partners:
- Nuclear receptor corepressor 2
- Structural maintenance of chromosomes protein 3
- Histone-lysine N-methyltransferase EZH2
- Structural maintenance of chromosomes protein 1A
- Paired amphipathic helix protein Sin3a
- F-box-like/WD repeat-containing protein TBL1XR1
- TBL1X/Y related 1
- NAD-dependent protein deacetylase sirtuin-1
- Histone H2A
- Histone H2A.Z
Sequence:
MEIPEEPANSGHSLPPVYIYSPEYVSICDSLVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIEYGLGYDCPATEGIFDYAAAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV
Protein: Transcription factor GTE4 (Bromodomain-containing protein GTE4) (Protein GLOBAL TRANSCRIPTION FACTOR GROUP E4) (Q9LNC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the activation and maintenance of cell division in the meristems and by this controls cell numbers in differentiated organs. Its action in cell cycle regulation may be directed through the RB-E2F pathway.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeobox-DDT domain protein RLT2
- At1g61215
- Protein ANTHESIS POMOTING FACTOR 1
- Transcription factor Pur-alpha 1
Sequence:
MASEPVNGGEGIDGAREKQIIKVYKRKGKGQRKQSSFFALEAAIEKPEGLLENENDNNDVSPAETLAPEFEDPIVVVKNSIEEAALGTNSHGDKNLTEAPSENLPGDDSDKVIDKPLVEAFSQAQPQDDASLAAMDKSEEVPSQIPKAQDDVNTVVVDENSIKEPPKSLAQEDVTTVIVDKNPIEAPSQTLSLEDGDTLVVDKNPIEVSSEEDVHVIDADNLIKEAHPENFVERDTTDAQQPAGLTSDSAHATAAGSMPMEEDADGRIRIHVASTTKQQKEEIRKKLEDQLNVVRGMVKKIEDKEGEIGAYNDSRVLINTGINNGGGRILSGFASAGLPREVIRAPRPVNQLSISVLENTQGVNEHVEKEKRTPKANQFYRNSEFLLGDKLPPAESNKKSKSSSKKQGGDVGHGFGAGTKVFKNCSALLERLMKHKHGWVFNAPVDVKGLGLLDYYTIIEHPMDLGTIKSALMKNLYKSPREFAEDVRLTFHNAMTYNPEGQDVHLMAVTLLQIFEERWAVIEADYNREMRFVTGYEMNLPTPTMRSRLGPTMPPPPINVRNTIDRADWSNRQPTTTPGRTPTSATPSGRTPALKKPKANEPNKRDMTYEEKQKLSGHLQNLPPDKLDAIVQIVNKRNTAVKLRDEEIEVDIDSVDPETLWELDRFVTNYKKGLSKKKRKAELAIQARAEAERNSQQQMAPAPAAHEFSREGGNTAKKTLPTPLPSQVEKQNNETSRSSSSSSSSSSSSSSDSDSDSSSSSGSDQT
Protein: Zipper protein (Q90712)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MAFTLGCNNPSFTLPWRTLLPYLMALHLLQPPSAQITVVAPSLRVTANVGQDVVLRCHLCPCKNAWSLDIRWIQLRSSGFVHHYRNGEDLEQMTEYKGRTELLRKGLSDGNLDLRITAVSTSDSGSYSCVVQDDDGYAEALVELEVSDPFSQIVHPWKVALAVIVTILVGSFVIIAFLYRKKATQSRELKRKDAMLGRKDAVLEELPAILDSSAANLKILASKLVKQTEKLDIRNSLMKKQYEMTEKQAAELEKHLINTDLSAADLNIAAAKLDKQTEELDKWKSALKIQYEKLGLRAANLKKQVTELAKQTEEVENHYEEMGLRAPNLKKNIVELEKQTEHVENRKSELKKQYENLASHASELKKQAAVLKEQAEQLEIQNSLSKIRNKHRERKNEMLEKQTVEQEQTEEWAESKKSVVETKELEQPSKEQD
Protein: CAP, isoform L (B7YZD9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPNNRNRNRNRNRNKRNRNQNQNQNPSQNQNENHQQQAEGAEDREEQQDFQTQIAVAQSSSFVDDNGNSGSVSNGPTENSEEVTNTLEKTEKKEEIFEQPATVIQKEADSDAEMGAKNSKHRKEKSDKQASNGKSEEQVRPPPTIIRRPPGSPRQAKVIVHRIVREEDTANGKAQSPEPPKAVESKEQHMEVEDSKKEKPEAQQEIETKEERENEPSPKELPESSHLSEDAQQKHVEVEENQQVYDEVDYSKDETTDNNPQQEQHDSKEPEQYVLQLEKAMEFVENAHQQHVAAVQSYQKQRDTEQNAQQQEQNEAQHLQESTKAHQQNIAVPQILVDPKKREEGLAQQLHHDVKEEPILNNAQQQNDDTAPKSPKEVTIKVQFQTEDPYSQQPPPQKPTSKVIIHQIHVETTDEEQNAKPTFEEVSSTTGSLAGTLSPPPRYLVESPKNVSSGQFSNFSRNVQIQEMELNSDFSSGEFNSLQSPLVCEVDSESEGSVVLGPERSPSDQQVPSSSRVEQHEQVRQKRAQYRNALESHFMPQLLNPRYLDSILEENEWRNSTASSGGSDQTGIRTPKLNETFPRSQLDFSRRHKRREEAPSPLKLETKLLEESTDLESCTRLQSALSPQSEDAELVYLSSSASSSVSDLMELELEQAAALAERALVDLDTDASRLIARPDDEMSSTSTTTADRSETEAETETETEREGEQSRESTPVNANPTLASSQSSLLSAATPTPTPTPTPADREQLAKDTNVSGGSTVSFGAASPLAATREEFVRNMDKVRELIEMTRREQEQGELPRSPSPPPVPPPPASVPPYSPESSSFHLASLQLKRQESNDSHCSDSTTHSQCTAINLASPPPPPTAQPPTPPLRQKPAPPPVPQPVSPPAPPTPQSEPELSVADSVANANADVDADADTDTEAIKKLRLLCTEQLASMPYGEQVLEELASVAQNISDQSQNKMPYPMPQLPHIKELQLNANESKSSSAWLGLPTQSDPKLLVCLSPGQRDLVNNQTQPDDLLDAHQKFVERRGYHELSKAQVLEQDHQQQQSEMLKTAAMMRELRKSLSPPAPPVPPPPVPVKSAETAAKATAHENAKRDDASEQKQKIAACESSSLENKPRRAADLGAQQSAEQRQSSSTTTSSHKATTETMSSDTAKFPTLDSMESELARMFPQHKGDIFEEQRKRFSNIEFPSHQPVSQTKRYSNIETSSYESKKRMENGQVVYDVSTSSHEKKEQGDPPKDQPVPPVPPPPIMSATKLNGNTFIDGDVAPKNSQPSRESGSGSGNGTYEEFRQRAKAAADAFGEQREQQNGLDQDRVFKDFDRLSQQMHAELQSTREKREKSASMYDLSGFTRPASGHPRLDELQQRRHAHMQELEREIERSAKSRQERMSSVPRQMEATPPRTHEIPIELEPRSRRAESLCNLNEPPPRPHTTVGHYNHPVVQDDWSRYANDLGYSENIARPFAREVEICYQRQNQRTPHCIRAPRLSASTNDLSSSSQYSYDTFNAYGGRRTHAPMLNQAQQQQRPHYGSCYSMIERDPNPRYISTTSRRGVSPAPPPVATPQQQQVPPPAYDRQQRRSSLPRELHEQQLKYILSKEEELKFEVERLQQERRRLMEEMQRAPVLPAPQRRESYRPAAKLPTLSEDEVFRQQMAEEWMNKVAEREERRQHKIIRISKIEDEHDHSAVDKATISDEFLDRVKERRHKLSMPADSDWESGAESQPQPAAQSQPESDVEAPPVRILEGQAEANLRQLPRHLREFAKFSTSEQLPDGAQMERHEEQERREEATDNAHSSATKKTSIVKTYKVSRLPPSVQARPSYKSNGYVSEPEPNYDSDYSTVRYRTQNPHRVQSVSSAVNVRNLNQDEKLYGTMPNPIKSAQNSYKNQPGRIENYTTGHSSVSEKEKKENLEQSKLSPLYTEGNLSRALAKESGYTSDSNLVFRKKEVPVSSPLSPVEQKQAYKSLQAGGEPPLLGFRKPAPEKPRDLDPNAPPIPPQPPVKGLSSYDFPYSTDTVDGSDVNIHFKTPIRHEQRQNLSEEELAIRQAEHMQKLYHEERRRKYLQELQDMNSRRHTDNFTPSQKSPIALNRYDDFPTDVTLKSLVGPKTVARALFNFQGQTSKELSFRKGDTIYIRRQIDANWYEGEHNAMIGLLPASYVEIVSRDGARTPSKRPSEGQARAKYNFQAQSGIELSLNKGELVTLTRRVDGNWFEGKIANRKGIFPCSYVEVLTDIGAEDIAARTTTVITSQSTTNLRPNLDVLRTNINNEFNTLTQNGAQPPNGILKETRTLHKTDALHVDTSSEPLAYRALYKYRPQNSDELELLEGDVVHVLEKCDDGWFVGTSQRTGCFGTFPGNYVERA
Protein: CUB and zona pellucida-like domain-containing protein 1 (CUB and ZP domain-containing protein 1) (Transmembrane protein UO-44) (Q86UP6)
Organism: Homo sapiens (Human)
Function: Localized to zymogen granules, where it functions in trypsinogen activation (By similarity). May indirectly regulate cell motility, cell-cell and cell/extracellular matrix interactions.
Subcellular location: Zymogen granule membrane {ECO:0000250|UniProtKB:P70412}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P70412}.
Interaction partners:
Sequence:
MELVRRLMPLTLLILSCLAELTMAEAEGNASCTVSLGGANMAETHKAMILQLNPSENCTWTIERPENKSIRIIFSYVQLDPDGSCESENIKVFDGTSSNGPLLGQVCSKNDYVPVFESSSSTLTFQIVTDSARIQRTVFVFYYFFSPNISIPNCGGYLDTLEGSFTSPNYPKPHPELAYCVWHIQVEKDYKIKLNFKEIFLEIDKQCKFDFLAIYDGPSTNSGLIGQVCGRVTPTFESSSNSLTVVLSTDYANSYRGFSASYTSIYAENINTTSLTCSSDRMRVIISKSYLEAFNSNGNNLQLKDPTCRPKLSNVVEFSVPLNGCGTIRKVEDQSITYTNIITFSASSTSEVITRQKQLQIIVKCEMGHNSTVEIIYITEDDVIQSQNALGKYNTSMALFESNSFEKTILESPYYVDLNQTLFVQVSLHTSDPNLVVFLDTCRASPTSDFASPTYDLIKSGCSRDETCKVYPLFGHYGRFQFNAFKFLRSMSSVYLQCKVLICDSSDHQSRCNQGCVSRSKRDISSYKWKTDSIIGPIRLKRDRSASGNSGFQHETHAEETPNQPFNSVHLFSFMVLALNVVTVATITVRHFVNQRADYKYQKLQNY
Protein: Protein phosphatase 2C 16 (AtPP2C16) (EC 3.1.3.16) (AtP2C-HA) (Protein HYPERSENSITIVE TO ABA 1) (Protein phosphatase 2C HAB1) (PP2C HAB1) (Q9CAJ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Key component and repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, seed germination and inhibition of vegetative growth. Confers enhanced sensitivity to drought.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19033529}. Nucleus {ECO:0000269|PubMed:19033529}. Note=Mainly cytoplasmic.
Interaction partners:
- Abscisic acid receptor PYR1
- Serine/threonine-protein kinase SRK2E
- Abscisic acid receptor PYL3
- Abscisic acid receptor PYL2
- Abscisic acid receptor PYL10
- Abscisic acid receptor PYL4
- Abscisic acid receptor PYL5
- Abscisic acid receptor PYL1
- Abscisic acid receptor PYL9
- Abscisic acid receptor PYL8
Sequence:
MEEMTPAVAMTLSLAANTMCESSPVEITQLKNVTDAADLLSDSENQSFCNGGTECTMEDVSELEEVGEQDLLKTLSDTRSGSSNVFDEDDVLSVVEDNSAVISEGLLVVDAGSELSLSNTAMEIDNGRVLATAIIVGESSIEQVPTAEVLIAGVNQDTNTSEVVIRLPDENSNHLVKGRSVYELDCIPLWGTVSIQGNRSEMEDAFAVSPHFLKLPIKMLMGDHEGMSPSLTHLTGHFFGVYDGHGGHKVADYCRDRLHFALAEEIERIKDELCKRNTGEGRQVQWDKVFTSCFLTVDGEIEGKIGRAVVGSSDKVLEAVASETVGSTAVVALVCSSHIVVSNCGDSRAVLFRGKEAMPLSVDHKPDREDEYARIENAGGKVIQWQGARVFGVLAMSRSIGDRYLKPYVIPEPEVTFMPRSREDECLILASDGLWDVMNNQEVCEIARRRILMWHKKNGAPPLAERGKGIDPACQAAADYLSMLALQKGSKDNISIIVIDLKAQRKFKTRT
Protein: Potassium voltage-gated channel subfamily H member 1 (Q108P3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTSEKVRLTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQEKVVLFLCTFSDITAFKQPIEDDSSKGWGKFARLTRALTSSRGVLQQLQPTVHKGENVHKHSRLAEVLQLGSDILPQYKQETPKTPPHIILHYCAFKTTWDWVILILTFYTAIMVPYNVSFKTKQNNVTWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEGISSLSSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWLACIWYSIGDYEVIDEDRNTVRTDSWLYMLAESIGTPYRFNASGTGRWEGGPTKDTVYITSLYFTMTSLTSIGFGNIAPTTDGEKIFAVAMMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIASTWSMSHGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTIHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGKGDVFGDVFWKEVTLAQACANVRALTYCDLHVIKRDALQKVLEFYTAFSNHFSRNLLLTYNLRKRLVFRKISDVKREEEERLRRKNEAPLNLPPDHPVRRLFQRFRQQKEARLAAVRPNSEDSDLEKGQIHNEVISQDVIATTSIVTVTESPATPIPSHLIKNRTLGPFDQAKLSAPAPNASRMSEPRARGWARFRESVAKPESWGNVPKAESMETLPERSSSAKTSEPSGLKKTDSCDSGITKSDLRLDEGGIRTPVDRSPVQPDGKSPPIPPIPTIPEHTLQASLLELRTELKEELSALGNRMVALEAQVAEVLRLLRNRKSPTSPMSLFQISRPTSPDTDKEDMFP
Protein: Checkpoint protein RAD24 (P32641)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Participates in checkpoint pathways arrest of the cell cycle, a mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Regulates the DNA damage checkpoint pathway throughout the cell cycle, when associated with RCF5. Component of the RFC-like RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA damage checkpoint control protein MEC3
- Replication factor C subunit 3
- Replication factor C subunit 5
- Replication factor C subunit 4
- DNA damage checkpoint protein 1
- Replication factor C subunit 2
- Telomere length regulation protein ELG1
- Serine/threonine-protein kinase MEC1
- DNA damage checkpoint control protein RAD17
- Chromosome transmission fidelity protein 18
Sequence:
MDSTNLNKRPLLQYSLSSLGSQITKWSSSRPTSPVRKARSTENDFLSKQDTSSILPSINDDGGEQWYEKFKPNCLEQVAIHKRKLKDVQEALDAMFLPNAKHRILLLSGPSGCSKSTVIKELSKILVPKYRQNSNGTSFRSTPNEHKVTEFRGDCIVNDLPQMESFSEFLKGARYLVMSNLSLILIEDLPNVFHIDTRRRFQQLILQWLYSSEPLLPPLVICITECEIPENDNNYRKFGIDYTFSAETIMNKEILMHPRLKRIKFNPINSTLLKKHLKFICVQNMKMLKEKNKWNKRQEVIDYIAQETGDIRSAITTLQFWATSSGSLPISTRESTISYFHAIGKVIHGSHSTNNDNEMINNLFENSNNLLSKEDFKLGILENYNTFNKGEFSISDASSIVDCLSECDNMNGLPESNEYGLREVRKTFRNISKQGHNHGTVYFPREWKVRKLQNSFKVQAEDWLNVSLYKYNAVHSFRNITLEFGYYAPLIRKCQSYKKKYILYYLKNLPSGSSGPKQTMDKFSDIMKVENGIDVVDRIGGPIEALSVEDGLAPLMDNDSNNCDHLEDQKKERDRRLRMLIDQYERNVMMANDDLEDEETSFNDDPIVDSDSDNSNNIGNETFGRSDEDESLCEILSQRQPRKAPVISESLSDSDLEIL
Protein: Leucine carboxyl methyltransferase 1 (EC 2.1.1.233) (Protein-leucine O-methyltransferase) ([Phosphatase 2A protein]-leucine-carboxy methyltransferase 1) (Q9UIC8)
Organism: Homo sapiens (Human)
Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Protein phosphatase methylesterase 1
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 2A activator
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- TIP41-like protein
Sequence:
MATRQRESSITSCCSTSSCDADDEGVRGTCEDASLCKRFAVSIGYWHDPYIQHFVRLSKERKAPEINRGYFARVHGVSQLIKAFLRKTECHCQIVNLGAGMDTTFWRLKDEDLLPSKYFEVDFPMIVTRKLHSIKCKPPLSSPILELHSEDTLQMDGHILDSKRYAVIGADLRDLSELEEKLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKWAANSFERAMFINYEQVNMGDRFGQIMIENLRRRQCDLAGVETCKSLESQKERLLSNGWETASAVDMMELYNRLPRAEVSRIESLEFLDEMELLEQLMRHYCLCWATKGGNELGLKEITY
Protein: Anaphase-promoting complex subunit 5 (Q08683)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Anaphase-promoting complex subunit CDC27
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit CDC23
- Anaphase-promoting complex subunit CDC26
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit CDC16
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit MND2
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 9
Sequence:
MSKYGPLGITNFITPYDLCILILIHAHCSQDNGISVPTAVFLRLISPTRPSLEWNPLLKDNSNLRSSSIVPPPVLPILDNIIRILLDDKDGNKIALTLMGYLEAINGLDSINRLMMDLEKNCLVNNYRSMKMRTTSTRRQMTRASFLGTFLSTCIRKYQIGDFEMRETIWINLQNFKTVFKHTPLWLRFKDNVHIQKVKNCLLANDEISVEDQQMVEFFQHFNNGNDADSKTMNEENYGTLISIQHLQSIVNRQIVNWLDNTEFNLMGQEETSSTYEEQSGLVFDLLDTLSLNDATKFPLIFILKYLEAIKENSYQTALDSLHNYFDYKSTGNSQNYFHISLLSLATFHSSFNECDAAINSFEEATRIARENKDMETLNLIMIWIINFIEVHPEYANRFYITVEQIIKYLKNSSDVEDANIFSNAYKFETLLSMVKESKTAEVSSSLLKFMAITLQNVPSQNFDLFQSLVSYEVKFWKELGYESISDVYEKFLSKTSSSSLRNYDSSIINQDIKVAFKALEEDDFLKVKQYLLKSESLELDYDQKINLKYLRVKYLVKIGDYDLSMRLINQYVKECCEEVADSNWRFKFEIESINVLLLSDVGIRSLPKIIKLIDEYKEIGNPLRCVILLLKLCEVLIQVGKSMEAECLISCNLSTILEFPFVRKKTDELLESLSVEEDRDVQMT
Protein: Virulence-associated membrane protein 1 (VMP1) (A0A0D1E6R6)
Organism: Mycosarcoma maydis (Corn smut fungus) (Ustilago maydis)
Function: During infection, may play a role in establishing and maintaining biotrophy; the formation of a tight interaction zone between the host and the pathogen.
Subcellular location: Membrane {ECO:0000305|PubMed:34093627}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRGILVALTAALIFCSLTPAQPVLHIQETNRAKNRANRKLVARQPEYKAVETLEKNVNIAIAVGTALVTLVSAGVGGMLLSDHLACKSVAKQEEIMQKSWDSMHPDGFTPAGDQMRPVSFDCSTQERGLKPLQSYTNGAEMY
Protein: Large ribosomal subunit protein uL15m (39S ribosomal protein L15, mitochondrial) (E5RIZ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
QERRPRGRRRGQTPFYIRIPKYGFNEGHSFRRQYKPLSLNRLQYLIDLGRVDPSQPIDLTQLVNGRGVTIQPLKRDYGVQLVEEGADTFTAKVNIEVQLASELAIAAIEKNGGVVTTAFYDPRSLDIVCKPVPFFLRGQPIPKRMLPPEELVPYYTDAKNRGYLADPAKFPEARLELARKYGYILPDITKDELFKMLCTRKDPRQIFFGLAPGWVVNMADKKILKPTDENLLKYYTS
Protein: Diacylglycerol kinase 1 (DAG kinase 1) (DGK 1) (Diglyceride kinase 1) (EC 2.7.1.107) (Q01583)
Organism: Drosophila melanogaster (Fruit fly)
Function: Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity (By similarity). May have a role in the development of the embryonic nervous system and the function of the adult nervous system and muscle; regulating signal transduction in neurons.
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Phosphatidate cytidylyltransferase, photoreceptor-specific
- 1-Acylglycerol-3-phosphate O-acyltransferase 3, isoform E
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- O-acyltransferase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase classes I and II
- FI05338p
- 1-Acylglycerol-3-phosphate O-acyltransferase 4, isoform A
- Phospholipase
Sequence:
MNIGIAAPKWDKLSPREFLQLQELASYSTRKLQDVLREFSSPSAASTPKCIPDGDIDFDGFRRFLDAFLDCEAPLDLAKHLFVSFLKPNVTQAQLHGRALNQMAAISSTAACAPVTSHTKGSIPNINSIAELMPQCSGGGGGIGGTGGVAGAEGHAQARSSFVDKIHGITDKLHHSLGGHLSHDPSKTGSVHPMLTVTPSPLASGPSMFQASNPARRSVDSSPSHSATNHSQMSRNSSKKSSNSVNCKIDADIKLLARKLSHFDPLTLKVPLKDVVCYLSLLEAGRPEDKLEFMFRLYDTDSNGVLDTAEMDAIVNQMMAVAEYLGWDVSELRPILQEMMVEIDYDADGTVSLDEWQRGGMTTIPLLVLLGVDSTTLKEDGIHVWRLKHFSKPAYCNLCLNMLVGLGKKGLCCVLCKYTVHERCVQHAPASCITTYVKSKKPKCGGDLLHHWVEGNCYGRCSKCRKRIKAYHGITGLTCRWCHMMLHNRCASSVKKECTLGEYSELIVPPTAICPAVLDRQRSVNQAHKKSQMHHHQATHFQITPPDELSCPLLVFVNPKSGGRQGDRILRKFQYMLNPRQVYDLSKGGPKEGLTLFKDLPRFRVICCGGDGTVGWVLEAMDSIELASQPAIGVIPLGTGNDLARCLRWGGGYEGENIPKLMDKFRRASTVMLDRWSIEVTNTPHSDDMRPKVTLHSNMQKVIELSQSVVVDKSLMERFEEIQRQSKQVATSMGTAASSTSIMMASKTETEMETMATMEFGSSTTTTNRTTTTKSISMSTFETQCLQQTLRTAMSSSSSNTSSGSPCNGNQDAETEVDSHAAAAADVREKSVPRRSGETEKQSLETLLLQHKQQMQQQQQQQQQGVTSLAVEEAATATPVGSNQSDNSSQRNKQNNILKQQITLSLDLSDHEDEPKDDGGGAGDGTKSNGNSIPATPATPITPTTPNAASSVLQQQQQQHLQFEQQQKPIKVQSDKDCTVPYNIINNYFSVGVDAAICVKFHLEREKNPHKFNSRMKNKLWYFEYATSETFAASCKNLHESIEIVCDGVALDLANGPHLQGVALLNIPYTHGGSNLWGEHLSQKRIRKSAGPFGKSKKLRAGDKEFSATSFNSVDLSVAIQDFGDRLIEVIGLENCLHMGQVRTGLRASGRRLAQCSEVIIKTKKTFPMQIDGEPWMQMPCTIKVTHKNQVPMLMAPRSEKGRGFFNLLCS
Protein: Eukaryotic translation initiation factor 5 (eIF-5) (P38431)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]). eIF-5 is essential for cell viability.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 2 subunit gamma
- Eukaryotic translation initiation factor 5B
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor eIF-1
- Eukaryotic translation initiation factor 2 subunit beta
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 1A
Sequence:
MSINICRDNHDPFYRYKMPPIQAKVEGRGNGIKTAVLNVADISHALNRPAPYIVKYFGFELGAQTSISVDKDRYLVNGVHEPAKLQDVLDGFINKFVLCGSCKNPETEIIITKDNDLVRDCKACGKRTPMDLRHKLSSFILKNPPDSVSGSKKKKKAATASANVRGGGLSISDIAQGKSQNAPSDGTGSSTPQHHDEDEDELSRQIKAAASTLEDIEVKDDEWAVDMSEEAIRARAKELEVNSELTQLDEYGEWILEQAGEDKENLPSDVELYKKAAELDVLNDPKIGCVLAQCLFDEDIVNEIAEHNAFFTKILVTPEYEKNFMGGIERFLGLEHKDLIPLLPKILVQLYNNDIISEEEIMRFGTKSSKKFVPKEVSKKVRRAAKPFITWLETAESDDDEEDDE
Protein: Cell wall protein DAN4 (Delayed anaerobic protein 4) (P47179)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cell wall.
Subcellular location: Secreted, cell wall {ECO:0000305|PubMed:9613572}. Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}.
Interaction partners:
Sequence:
MVNISIVAGIVALATSAAAITATTTLSPYDERVNLIELAVYVSDIRAHIFQYYSFRNHHKTETYPSEIAAAVFDYGDFTTRLTGISGDEVTRMITGVPWYSTRLKPAISSALSKDGIYTAIPTSTSTTTTKSSTSTTPTTTITSTTSTTSTTPTTSTTSTTPTTSTTSTTPTTSTTSTTPTTSTTSTTPTTSTTSTTPTTSTTSTTPTTSTTSTTPTTSTTSTTPTTSTTPTTSTTSTTSQTSTKSTTPTTSSTSTTPTTSTTPTTSTTSTAPTTSTTSTTSTTSTISTAPTTSTTSSTFSTSSASASSVISTTATTSTTFASLTTPATSTASTDHTTSSVSTTNAFTTSATTTTTSDTYISSSSPSQVTSSAEPTTVSEVTSSVEPTRSSQVTSSAEPTTVSEFTSSVEPTRSSQVTSSAEPTTVSEFTSSVEPTRSSQVTSSAEPTTVSEFTSSVEPTRSSQVTSSAEPTTVSEFTSSVEPTRSSQVTSSAEPTTVSEFTSSVEPIRSSQVTSSAEPTTVSEVTSSVEPIRSSQVTTTEPVSSFGSTFSEITSSAEPLSFSKATTSAESISSNQITISSELIVSSVITSSSEIPSSIEVLTSSGISSSVEPTSLVGPSSDESISSTESLSATSTFTSAVVSSSKAADFFTRSTVSAKSDVSGNSSTQSTTFFATPSTPLAVSSTVVTSSTDSVSPNIPFSEISSSPESSTAITSTSTSFIAERTSSLYLSSSNMSSFTLSTFTVSQSIVSSFSMEPTSSVASFASSSPLLVSSRSNCSDARSSNTISSGLFSTIENVRNATSTFTNLSTDEIVITSCKSSCTNEDSVLTKTQVSTVETTITSCSGGICTTLMSPVTTINAKANTLTTTETSTVETTITTCPGGVCSTLTVPVTTITSEATTTATISCEDNEEDITSTETELLTLETTITSCSGGICTTLMSPVTTINAKANTLTTTETSTVETTITTCSGGVCSTLTVPVTTITSEATTTATISCEDNEEDVASTKTELLTMETTITSCSGGICTTLMSPVSSFNSKATTSNNAESTIPKAIKVSCSAGACTTLTTVDAGISMFTRTGLSITQTTVTNCSGGTCTMLTAPIATATSKVISPIPKASSATSIAHSSASYTVSINTNGAYNFDKDNIFGTAIVAVVALLLL
Protein: Sorting nexin (A0A8I5ZS69)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MMEGLDDGPDFLSEEDRGLKSINVDLQSDAALQVDISDALSERDKVKFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPDFDASREKLQKLGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYNQDLSVRGKNKKEKLEDFFKNMVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDSTDICKFFLKVSELFDKTRVKARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETSQQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCLAVLNGDT