wanglab/gogpt-training-data huggingface dataset:
Protein: CD302 antigen (C-type lectin BIMLEC) (C-type lectin domain family 13 member A) (DEC205-associated C-type lectin 1) (Type I transmembrane C-type lectin receptor DCL-1) (CD antigen CD302) (Q8IX05)
Organism: Homo sapiens (Human)
Function: Potential multifunctional C-type lectin receptor that may play roles in endocytosis and phagocytosis as well as in cell adhesion and migration.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, filopodium {ECO:0000269|PubMed:17947679}. Cytoplasm, cell cortex {ECO:0000269|PubMed:17947679}. Cell projection, microvillus {ECO:0000269|PubMed:17947679}. Note=Colocalizes with F-actin in filopodia, cellular cortex and microvilli of the apical cell surface.
Interaction partners:
- Protein argonaute-1
- Endoribonuclease Dicer
Sequence:
MLRAALPALLLPLLGLAAAAVADCPSSTWIQFQDSCYIFLQEAIKVESIEDVRNQCTDHGADMISIHNEEENAFILDTLKKQWKGPDDILLGMFYDTDDASFKWFDNSNMTFDKWTDQDDDEDLVDTCAFLHIKTGEWKKGNCEVSSVEGTLCKTAIPYKRKYLSDNHILISALVIASTVILTVLGAIIWFLYKKHSDSRFTTVFSTAPQSPYNEDCVLVVGEENEYPVQFD
Protein: At1g51080 (Golgin family A protein) (Q9C683)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSFSVVLFHSPHSAAVTTKTIFRISSSSSFRPRRNLSSSNGIFSTNQSKPLIKKLQIIETLAARDTIIDFGKHKGKMLGTLPSSYLKWVSKNLRAGVFEYWAKLADEVLEDDVYKDRTEWEFAEKILHGSDESMRALTSVRKSREEVNSVSMLLEISERFGWDNEDKIGWSKINFELLGTSKGGRIPRLRKANEEEEERGEMVRRREIKKKEEEEDENGWRRKQRRERMRQSLGRDDGKTVNRSEQKGVLGKLEDVEKQLEPKIQSPFPGRESLLKKVMNKRRSQ
Protein: Double-strand-specific pac1 ribonuclease (EC 3.1.26.3) (Protein hcs) (P22192)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Digests double-stranded RNA. Converts long double-stranded RNAs into short oligonucleotides, leaving 5'-phosphates on their cleavage products. Probably inhibits mating and meiosis by degrading a specific mRNA required for sexual development.
Interaction partners:
- Small ribosomal subunit protein uS9m
- Protein argonaute
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL32m
- Uncharacterized protein C328.01c
- Large ribosomal subunit protein bL33m
Sequence:
MGRFKRHHEGDSDSSSSASDSLSRGRRSLGHKRSSHIKNRQYYILEKKIRKLMFAMKALLEETKHSTKDDVNLVIPGSTWSHIEGVYEMLKSRHDRQNEPVIEEPSSHPKNQKNQENNEPTSEEFEEGEYPPPLPPLRSEKLKEQVFMHISRAYEIYPNQSNPNELLDIHNERLEFLGDSFFNLFTTRIIFSKFPQMDEGSLSKLRAKFVGNESADKFARLYGFDKTLVLSYSAEKDQLRKSQKVIADTFEAYLGALILDGQEETAFQWVSRLLQPKIANITVQRPIDKLAKSKLFHKYSTLGHIEYRWVDGAGGSAEGYVIACIFNGKEVARAWGANQKDAGSRAAMQALEVLAKDYSKFAR
Protein: Phosphatidylinositol mannoside acyltransferase (PIM acyltransferase) (EC 2.3.1.265) (P9WMB5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the transfer of a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to the 2-position of myo-inositol in phosphatidyl-myo-inositol monomannoside (PIM1) or dimannoside (PIM2). Essential for growth and survival in axenic cultures and during macrophage infection and in a mouse model of infection.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:12851411}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0QWG5}; Cytoplasmic side {ECO:0000250|UniProtKB:A0QWG5}. Note=Permanently associated with the membrane. {ECO:0000250|UniProtKB:A0QWG5}.
Interaction partners:
- Phosphatidyl-myo-inositol mannosyltransferase
- GDP-mannose-dependent alpha-
- Phosphatidylinositol phosphate synthase
- AP-4-A phosphorylase
- Probable conserved membrane protein
- GDP-mannose-dependent alpha-mannosyltransferase
- Threonine--tRNA ligase
Sequence:
MIAGLKGLKLPKDPRSSVTRTATDWAYAAGWMAVRALPEFAVRNAFDTGARYFARHGGPEQLRKNLARVLGVPPAAVPDPLMCASLESYGRYWREVFRLPTINHRKLARQLDRVIGGLDHLDAALAAGLGAVLALPHSGNWDMAGMWLVQRHGTFTTVAERLKPESLYQRFIDYRESLGFEVLPLSGGERPPFEVLSERLRNNRVVCLMAERDLTRTGVEVDFFGEPTRMPVGPAKLAVETGAALLPTHCWFEGRGWGFQVYPALDCTSGDVAAITQALADRFAQNIAAHPADWHMLQPQWLADLSESRRAQLRSR
Protein: Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (BubR1) (Mitotic checkpoint kinase MAD3L) (Q9Z1S0)
Organism: Mus musculus (Mouse)
Function: Essential component of the mitotic checkpoint. Required for normal mitosis progression and tumor suppression. The mitotic checkpoint delays anaphase until all chromosomes are properly attached to the mitotic spindle. One of its checkpoint functions is to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C, independently of its kinase activity. The other is to monitor kinetochore activities that depend on the kinetochore motor CENPE. Required for kinetochore localization of CENPE. Negatively regulates PLK1 activity in interphase cells and suppresses centrosome amplification. Also implicated in triggering apoptosis in polyploid cells that exit aberrantly from mitotic arrest. Essential for tumor suppression. May play a role in regulating aging and fertility (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12925705, ECO:0000269|PubMed:17925231}. Note=Cytoplasmic in interphase cells (By similarity). Associates with the kinetochores in early prophase. Kinetochore localization requires BUB1, PLK1 and KNL1 (By similarity). {ECO:0000250}.
Interaction partners:
- Mitotic spindle assembly checkpoint protein MAD2A
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Mitotic checkpoint protein BUB3
- Centromere-associated protein E
- Cell division cycle protein 20 homolog
- Cell division cycle protein 27 homolog
- Cell division cycle protein 23 homolog
- Serine/threonine-protein kinase Nek2
- Serine/threonine-protein kinase PLK1
- Anaphase-promoting complex subunit 4
Sequence:
MAEASEAMCLEGAEWELSKENIQPLRHGRVMSTLQGALAKQESAGHTALQQQKRAFESEIRFYSGDDPLDVWDRYINWTEQNYPQGGKESNMSALVERAIEALQGETRYYNDPRFLSLWIKLGHLCNEPLDMYSYLQSQGIGVSLAQFYISWAEEYEARENFKKADIIFQEGIERKAEPLDRLQSQHRQFQSRVSRQAFLALGNEEEEALEPSEPQRSSLAELKSRGKKMARAPISRVGGALKAPGQSRGFLNAVPQPVHGNRRITVFDENADTASRTELSKPVAQPWMAPPVPRAKENELQPGPWSTDRPAGRRPHDNPASVTSIPSVLPSFTPYVEESAQQTVMTPCKIEPSINHVLSTRKPGREEGDPLQRVQSHQQGCEEKKEKMMYCKEKIYAGVGEFSFEEIRAEVFRKKLKERREAELLTSAKKREEMQKQIEEMERRLKAMQAVQQEGAGGQQEEKMPTEDPARLQIASGPQEMSGVPLSCSICPLSSNPREISPAENILQEQPDSKGSSMPFSIFDESLSDKKDKSPATGGPQVLNAQRRPLSVLKTTEVGTTNEDVSPDICDELTELEPLSEDAIITGFRNVTLCPNPEDTCDFARAARLASTPFHEILSSKGIAADPEGLLQEEDLDGKAAEAHHTVHHQALIIKKLSPIIEESREATHSSGFSRSSSSAPSTSSIKGFQLLEKLELTNDGAEDAIQSPWCSQYRLQLLKSLLELSAFAEFSVEDRPMPVLEIGKEIELGPEDYVIKQEHLTCDDYRLFWVAPRSSAELTMIKASSQPIPWDFYINLKLKERLNEDYDQLCSCCQYQDGHVVWYQYINCSTLQNLLQHSEFVTHEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRNRIHDPYDYVNKDDHAVRIMDFSYSVDLRVQLDAFAYSGFRTAQILEGQKILANCSSPYHVDLLGIADLAHLLLFKEHLHVFWDGLLWKLSQSTSELKDSELWNKFFVRILNASDKSTVSVLGELAAEMGGAFDATFHSHLNRALWKLGKTISPEALLTQQDKQPGGSQSPA
Protein: BcDNA.GH02384 (Q9Y168)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Neuropathy target esterase sws
- Lysophosphatidylcholine acyltransferase
- LD22655p
- Lysophospholipid acyltransferase 5
- Uncharacterized protein, isoform A
- phospholipase A2
- FI23918p1
- BOS complex subunit TMEM147
Sequence:
MRLKSGVLSLLLLTTFLALGECFWPFSKWHGRNDNPSAPPEPKLSPVIFVPGDGGSQMDARLNKPNSPYLICQKTHDWYNLWLDLEQLVIPIVYCWIDNVKLYYDKVTRTTHNTPGVETRIPGWGNPEVVEWIDPTKNSAGAYFKDIANELVKLGYIRKQNIHGAPYDFRKAPNENQQFFIDLKQLVEDSYEANNQSAVTFISHSMGSLMTLVFLQEQTLQWKAKYVKRMISLAGVWAGSFKAVKVFAMGDDLDSFALSAKILKAEQITHPSTAWLLPSPLFWKPTEVLAMTPSRNYTMAQLEEFFKDLDYMTGWEMRKDTIRYNRNFDPPNVELHCLYGEGIDTVERLQYKKSDISGETPKLIMGLGDGTVNQRSLRACKYWAGYSKAPINTLALQNVDHLHILSNPDVLKYIRTVMQQP
Protein: Glycerol-3-phosphate acyltransferase 3 (GPAT-3) (EC 2.3.1.15) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10) (AGPAT 10) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9) (1-AGP acyltransferase 9) (1-AGPAT 9) (EC 2.3.1.51) (Acyl-CoA:glycerol-3-phosphate acyltransferase 3) (hGPAT3) (Lung cancer metastasis-associated protein 1) (Lysophosphatidic acid acyltransferase theta) (LPAAT-theta) (MAG-1) (Q53EU6)
Organism: Homo sapiens (Human)
Function: Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) by incorporating an acyl moiety at the sn-1 position of the glycerol backbone. Also converts LPA into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Protects cells against lipotoxicity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17002884, ECO:0000269|PubMed:19318427}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Glycerol-3-phosphate acyltransferase 2, mitochondrial
- Glycerol-3-phosphate dehydrogenase 1-like protein
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol kinase
- Glycerol kinase 2
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Acylglycerol kinase, mitochondrial
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Glycerol-3-phosphate acyltransferase 4
Sequence:
MEGAELAGKILSTWLTLVLGFILLPSVFGVSLGISEIYMKILVKTLEWATIRIEKGTPKESILKNSASVGIIQRDESPMEKGLSGLRGRDFELSDVFYFSKKGLEAIVEDEVTQRFSSEELVSWNLLTRTNVNFQYISLRLTMVWVLGVIVRYCVLLPLRVTLAFIGISLLVIGTTLVGQLPDSSLKNWLSELVHLTCCRICVRALSGTIHYHNKQYRPQKGGICVANHTSPIDVLILTTDGCYAMVGQVHGGLMGIIQRAMVKACPHVWFERSEMKDRHLVTKRLKEHIADKKKLPILIFPEGTCINNTSVMMFKKGSFEIGGTIHPVAIKYNPQFGDAFWNSSKYNMVSYLLRMMTSWAIVCDVWYMPPMTREEGEDAVQFANRVKSAIAIQGGLTELPWDGGLKRAKVKDIFKEEQQKNYSKMIVGNGSLS
Protein: Transcriptional repressor RcnR (P64530)
Organism: Escherichia coli (strain K12)
Function: Repressor of rcnA expression. Acts by binding specifically to the rcnA promoter in the absence of nickel and cobalt. In the presence of one of these metals, it has a weaker affinity for rcnA promoter.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Nickel/cobalt efflux system RcnA
- Nickel-responsive regulator
- HTH-type transcriptional regulator ZntR
- Nickel/cobalt homeostasis protein RcnB
- Arsenical resistance operon repressor
- HTH-type transcriptional regulator CueR
- Transcriptional regulator MntR
Sequence:
MSHTIRDKQKLKARASKIQGQVVALKKMLDEPHECAAVLQQIAAIRGAVNGLMREVIKGHLTEHIVHQGDELKREEDLDVVLKVLDSYIK
Protein: Probable inorganic phosphate transporter 1-3 (AtPht1;3) (H(+)/Pi cotransporter) (O48639)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High-affinity transporter for external inorganic phosphate.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Inorganic phosphate transporter 2-1, chloroplastic
- Phosphate transporter PHO1
- Mitochondrial phosphate carrier protein 1, mitochondrial
- Probable anion transporter 5
- SEC12-like protein 1
- Probable ubiquitin-conjugating enzyme E2 24
- Ammonium transporter 2
- Thiosulfate/3-mercaptopyruvate sulfurtransferase 2
- Protein PHOSPHATE STARVATION RESPONSE 1
- SPX domain-containing protein 1
Sequence:
MADQQLGVLKALDVAKTQLYHFTAIVIAGMGFFTDAYDLFCVSLVTKLLGRLYYFNPTSAKPGSLPPHVAAAVNGVALCGTLAGQLFFGWLGDKLGRKKVYGITLIMMILCSVASGLSLGNSAKGVMTTLCFFRFWLGFGIGGDYPLSATIMSEYANKKTRGAFIAAVFAMQGVGILAGGFVALAVSSIFDKKFPSPTYEQDRFLSTPPQADYIWRIIVMFGALPAALTYYWRMKMPETARYTALVAKNIKQATADMSKVLQTDLELEERVEDDVKDPKKNYGLFSKEFLRRHGLHLLGTTSTWFLLDIAFYSQNLFQKDIFSAIGWIPKAATMNAIHEVFKIARAQTLIALCSTVPGYWFTVAFIDIIGRFAIQLMGFFMMTVFMFAIAFPYNHWILPDNRIGFVVMYSLTFFFANFGPNATTFIVPAEIFPARLRSTCHGISAATGKAGAIVGAFGFLYAAQPQDKTKTDAGYPPGIGVKNSLIMLGVINFVGMLFTFLVPEPKGKSLEELSGEAEVDK
Protein: Monocyte differentiation antigen CD14 (Myeloid cell-specific leucine-rich glycoprotein) (CD antigen CD14) (P10810)
Organism: Mus musculus (Mouse)
Function: Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway (By similarity). Acts as an accessory receptor for M.tuberculosis lipoproteins LprA, LprG and LpqH, in conjunction with coreceptors TLR2 and TLR1. The lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen. Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-) (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:21821728, ECO:0000269|PubMed:8612135}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P08571}. Secreted {ECO:0000250|UniProtKB:P08571}. Membrane raft {ECO:0000250|UniProtKB:P08571}. Golgi apparatus {ECO:0000250|UniProtKB:P08571}. Note=Soluble, secreted forms seem to exist. They may arise by cleavage of the GPI anchor. {ECO:0000250|UniProtKB:P08571}.
Interaction partners:
- Toll-like receptor 4
- Lymphocyte antigen 96
- Toll-like receptor 2
- Lipopolysaccharide-binding protein
- Low affinity immunoglobulin gamma Fc region receptor III
- Transcription factor PU.1
- Myeloid differentiation primary response protein MyD88
- 60 kDa heat shock protein, mitochondrial
- Platelet glycoprotein 4
- Integrin alpha-M
Sequence:
MERVLGLLLLLLVHASPAPPEPCELDEESCSCNFSDPKPDWSSAFNCLGAADVELYGGGRSLEYLLKRVDTEADLGQFTDIIKSLSLKRLTVRAARIPSRILFGALRVLGISGLQELTLENLEVTGTAPPPLLEATGPDLNILNLRNVSWATRDAWLAELQQWLKPGLKVLSIAQAHSLNFSCEQVRVFPALSTLDLSDNPELGERGLISALCPLKFPTLQVLALRNAGMETPSGVCSALAAARVQLQGLDLSHNSLRDAAGAPSCDWPSQLNSLNLSFTGLKQVPKGLPAKLSVLDLSYNRLDRNPSPDELPQVGNLSLKGNPFLDSESHSEKFNSGVVTAGAPSSQAVALSGTLALLLGDRLFV
Protein: Myosin-2 (Myosin heavy chain 2) (Myosin heavy chain 2a) (Myosin heavy chain, skeletal muscle, adult 2) (A0A0G2K0F5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, myofibril {ECO:0000256|ARBA:ARBA00004657}.
Interaction partners:
Sequence:
MSSDSEMAVFGEAAPYLRKSEKERIEAQNRPFDAKTSVFVAEPKESFVKGTIQSKDAGKVTVKTEAGATLTVKEDQIFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQLITRTQAMCRGFLARVEYQKMVERRESIFCIQYNIRAFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE
Protein: ATPase GET3D, chloroplastic (AtGet3d) (EC 3.6.-.-) (Guided entry of tail-anchored proteins 3 homolog D) (Q6DYE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:37100288}. Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16461379}.
Interaction partners:
- Protein GET4
- acid phosphatase
Sequence:
MVSLVNSSLTCSSLTLNLLPILRTETPSLSRKRRAAYVAATSSRDVNDTAADSSQKLTKFVTFLGKGGSGKTTAAVFAAQHYALAGLSTCLVIHNQDPSAEFLLGSKIGTSPTLINDNLSVIRLETTKMLLEPLKQLKQADARLNMTQGVLEGVVGEELGVLPGMDSIFSMLELERLVGFFRQATRKNHKGKPFDVIIYDGISTEETLRMIGLSSKTRLYAKYLRSLAEKTDLGRLTSPSIMRFVDESMNINSNKSPFDGMTSPAMWDTLERFLETGASAWRDPERFRSFLVMDPNNPMSVKAALRYWGCTVQAGSHVSGAFAISSSHLTSQIPKADFVPLPFASASVPFTITGLDWDKILLDQANSSIRELLSETVSHGTSLTQTVMFDTAKKLVTLFMPGFEKSEIKLYQYRGGSELLIEAGDQRRVIHLPSQIQGKVGGAKFVDRSLIVTMR
Protein: Bardet-Biedl syndrome 4 (D4A8B1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Bardet-Biedl syndrome 9
- BBSome complex member BBS2
- Bardet-Biedl syndrome 5 protein homolog
- Bardet-Biedl syndrome 7 protein homolog
- BBSome complex member BBS1
- Tetratricopeptide repeat protein 8
- Pericentriolar material 1
- BBSome interacting protein 1
- Leucine zipper transcription factor-like protein 1
- Bardet-Biedl syndrome 10
Sequence:
MAEEKLGMKTQVPASIESQKPRPKKAPEFPIVEKLNWLIHLYYIRKDYEACKAVIKEQLQETQGLCEYAIYVQALIFRLEGNIQESLELFQTCAVLSPQCADNLKQVARSLFLLGKHKAATEVYNEAAKLNQKDWEICHNLGVCYTYLKQFSKAQDQLHSALQLNKHDLTYIMLGKIHLLQGDLDKAIEIYKKAVEFSPENTELLTTLGLLYLQLGVYQKAFEHLGNALTYDPANYKAILAAGSMMQTHGDFDVALTKYRVVACAIPESPPLWNNIGMCFFGKKKYVAAISCLKRANYLAPFDWKILYNLGLVHLTMQQYASAFHFLSAAINFQPKMGELYMLLAVALTNLEDIENAKRAYVEAVRLDKCNPLVNLNYAVLLYNQGEKKGALAQYQEMEKKVHFLKDNNPLEFDSEMVEMAQKLGAALQVGEALVWTKPVKDPKSKHRTNSGSKSATLQQPLGSFQALGQAMSSAAAHRKIPSGAVGAQLTKPPSLPLEPEPEPTVEASPTEASEQNKEK
Protein: Protein FAM3D (Q96BQ1)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRVSGVLRLLALIFAIVTTWMFIRSYMSFSMKTIRLPRWLAASPTKEIQVKKYKCGLIKPCPANYFAFKICSGAANVVGPTMCFEDRMIMSPVKNNVGRGLNIALVNGTTGAVLGQKAFDMYSGDVMHLVKFLKEIPGGALVLVASYDDPGTKMNDESRKLFSDLGSSYAKQLGFRDSWVFIGAKDLRGKSPFEQFLKNSPDTNKYEGWPELLEMEGCMPPKPF
Protein: Zinc finger protein ZFPM1 (Friend of GATA protein 1) (FOG-1) (Friend of GATA 1) (Zinc finger protein multitype 1) (P60622)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription regulator that modulates expression mediated by transcription factors of the GATA family. Cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- GATA-binding protein 1a.
- Endothelial transcription factor GATA-2a
- Rhombotin-2
- T-cell acute lymphocytic leukemia protein 1 homolog
- Histone-binding protein RBBP7
- GATA-binding protein 1b.
- Histone-binding protein RBBP4
- LIM domain-binding protein 1-A.
Sequence:
MSEMVHSRLKQGQGPAAAQQSFYPPGSPASVHKGATCFECDITFNNINNFYVHKRLYCSSRHQQGETGGLVKEGAVTAAAPPVSHAASPQARPVSRAASASPSCPDPAPGGTASEPKVVEVKIEDPGLKDATCSSSSEGEGPGGGQASEGSQSPSGSAEDQDDDPTRTFCQACNIRFSRHDNYIVHKRFYCASRHDPTNQRPHSGKAAFLPQPIRTRKRKKMYE
Protein: beta-glucosidase (EC 3.2.1.21) (Q2UIR4)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Probable glucan endo-1,3-beta-glucosidase eglC
- Rhamnogalacturonase A/B/Epimerase-like pectate lyase domain-containing protein
- beta-glucosidase
- Glucanase
- Probable 1,4-beta-D-glucan cellobiohydrolase A
- beta-glucosidase
- Probable beta-glucosidase H
- beta-glucosidase
- Probable glucan 1,3-beta-glucosidase D
- beta-glucosidase
Sequence:
MLTSPTARTSVRISRPATTERPNTVLTSGSLDIAMVQVVSRTLTPPTSNMKLSAALSTLAALQPAVGAAVQNRASDVADLEHYWSYGHSEPVYPTPETKGLGDWEEAFTKARSLVAQMTDKEKNNITYGYSSTANGCGGTSGGVPRLGFPGICLQDAGNGVRGTDMVNSYASGVHVGASWNRDLTYSRAQYMGAEFKRKGVNVALGPVAGPIGRIARGGRNWEGFSNDPYLSGALTGDTVRGLQESVIACVKHLIGNEQETHRSTPSMLANSRNQSSSSNLDDKTMHELYLWPFQDAVKAGAGSVMCSYNRINNSYGCQNSKAMNGLLKGELGFQGFVVSDWGAQHTGIASAAAGLDMAMPSSSYWENGTLALAVKNESLPSTRLDDMATRIVATWYKYAEIENPGHGLPYSLLAPHNLTDARDPKSKSTILQGAVEGHVLVKNTNNALPLKKPQFLSLFGYDAVAAARNTMDDLDWNMWSMGYDNSLTYPNGSAVDAMMLKYIFLSSANPSAFGPGVALNATTITGGGSGASTASYIDAPFNAFQRQAYDDDTFLAWDFASQNPLVNPASDACIVFINEQSSEGWDRPYLADPYSDTLVQNVASQCSNTMVVIHNAGVRLVDRWIENDNITAVIYAHLPGQDSGRALVEVMYGKQSPSGRLPYTVAKNESDYGSLLNPVIQSGTDDIYYPQDNFTEGVYIDYKAFVAANITPRYEFGYGLTYSTFDYSDLKVSTSSNVSTSYLAPGTTVAEGGLPSVWDIIATVTCTVSNTGSVAAAEVAQLYIGIPGGPAKVLRGFEKQLIEPGQQVQVTFDLTRRDLSTWDTEKQNWGLQAGSYALYVGKSVLDIQLTGSLSL
Protein: Chemotaxis protein CheY (P24072)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Chemotaxis protein CheW
- Flagellar motor switch protein FliM
- Flagellar motor switch phosphatase FliY
- Chemotaxis protein CheA
- Chemotaxis protein methyltransferase
- CheY-P phosphatase CheC
- Methyl-accepting chemotaxis protein McpB
- Methyl-accepting chemotaxis protein McpC
- Methyl-accepting chemotaxis protein McpA
- Chemoreceptor glutamine deamidase CheD
Sequence:
MAHRILIVDDAAFMRMMIKDILVKNGFEVVAEAENGAQAVEKYKEHSPDLVTMDITMPEMDGITALKEIKQIDAQARIIMCSAMGQQSMVIDAIQAGAKDFIVKPFQADRVLEAINKTLN
Protein: Endolysin (LysB4) (H9NAL3)
Organism: Bacillus phage B4
Interaction partners:
Sequence:
MAMALQTLIDKANRKLNVSGMRKDVADRTRAVITQMHAQGIYICVAQGFRSFAEQNALYAQGRTKPGSIVTNARGGQSNHNYGVAVDLCLYTQDGSDVIWTVEGNFRKVIAAMKAQGFKWGGDWVSFKDYPHFELYDVVGGQKPPADNGGAVDNGGGSGSTGGSGGGSTGGGSTGGGYDSSWFTKETGTFVTNTSIKLRTAPFTSADVIATLPAGSPVNYNGFGIEYDGYVWIRQPRSNGYGYLATGESKGGKRQNYWGTFK
Protein: Homeobox protein Hox-A1 (Homeobox protein Hox-1F) (P49639)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor (By similarity). Regulates multiple developmental processes including brainstem, inner and outer ear, abducens nerve and cardiovascular development and morphogenesis as well as cognition and behavior. Also part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. Seems to act in the maintenance and/or generation of hindbrain segments (By similarity). Activates transcription in the presence of PBX1A and PKNOX1 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P09022}.
Interaction partners:
- Homeobox protein Hox-B1
- Homeobox protein Hox-D1
- N-chimaerin
- Pre-B-cell leukemia transcription factor 1
- Sal-like protein 4
- Roundabout homolog 3
- Homeobox protein PKNOX1
Sequence:
MDNARMNSFLEYPILSSGDSGTCSARAYPSDHRITTFQSCAVSANSCGGDDRFLVGRGVQIGSPHHHHHHHHRHPQPATYQTSGNLGVSYSHSSCGPSYGSQNFSAPYSPYALNQEADVSGGYPQCAPAVYSGNLSSPMVQHHHHHQGYAGGAVGSPQYIHHSYGQEHQSLALATYNNSLSPLHASHQEACRSPASETSSPAQTFDWMKVKRNPPKTGKVGEYGYLGQPNAVRTNFTTKQLTELEKEFHFNKYLTRARRVEIAASLQLNETQVKIWFQNRRMKQKKREKEGLLPISPATPPGNDEKAEESSEKSSSSPCVPSPGSSTSDTLTTSH