wanglab/gogpt-training-data huggingface dataset:
Protein: Cytoplasmic linker associated protein 2 (E7ERI8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MEPRSMEYFCAQVQQKDVGGRLQVGQELLLYLGAPGAISDLEEDLGRLGKTVDALTGWVGSSNYRVSLMGLEILSAFVDRLSTRFKSYVAMVIVALIDRMGDAKDKVRDEAQTLILKLMDQVAPPMYIWEQLASGFKHKNFRSREGVCLCLIETLNIFGAQPLVISKLIPHLCILFGDSNSQVRDAAILAIVEIYRHVGEKVRMDLYKRGIPPARLEMIFAKFDEVQSSGGMILSVCKDKSFDDEESVDGNRPSSAASAFKVPAPKTSGNPANSARKPGSAGGPKVGGASKEGGAGAVDEDDFIKAFTDVPSIQIYSSRELEETLNKIREILSDDKHDWDQRANALKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVVREACITVAHLSTVLGNKFDHGAEAIVPTLFNLVPNSAKVMATSGCAAIRFIIRHTHVPRLIPLITSNCTSKSVPVRRRSFEFLDLLLQEWQTHSLERHAAVLVETIKKGIHDADAEARVEARKTYMGLRNHFPGEAETLYNSLEPSYQKSLQTYLKSSGSVASLPQSDRSSSSSQESLNRPFSSKWSTANPSTVAGRVSAGSSKASSLPGSLQRSRSDIDVNAAAGAKAHHAAGQSVRSGRLGAGALNAGSYASLEDTSDKLDGTASEDGRVRAKLSAPLAGMGNAKADSRGRSRTKMVSQSQPGSRSGSPGRVLTTTALSTVSSGVQRVLVNSASAQKRSKIPRSQGCSREASPSRLSVARSSRIPRPSVSQGCSREASRESSRDTSPVRSFQPLGPGYGISQSSRLSSSVSAMRVLNTGSDVEEAVADALLLGDIRTKKKPARRRYESYGMHSDDDANSDASSACSERSYSSRNGSIPTYMRQTEDVAEVLNRCASSNWSERKEGLLGLQNLLKNQRTLSRVELKRLCEIFTRMFADPHGKVFSMFLETLVDFIQVHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRESFPNDLQFNILMRFTVDQTQTPSLKVKVAILKYIETLAKQMDPGDFINSSETRLAVSRVITWTTEPKSSDVRKAAQSVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLRNTGNGTQSSMGSPLTRPTPRSPANWSSPLTSPTNTSQNTLSPSAFDYDTENMNSEDIYSSLRGVTEAIQNFSFRSQEDMNEPLKRDSKKDDGDSMCGGPGMSDPRAGGDATDSSQTALDNKASLLHSMPTHSSPRSRDYNPYNYSDSISPFNKSALKEAMFDDDADQFPDDLSLDHSDLVAELLKELSNHNERVEERKIALYELMKLTQEESFSVWDEHFKTILLLLLETLGDKEPTIRALALKVLREILRHQPARFKNYAELTVMKTLEAHKDPHKEVVRSAEEAASVLATSISPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERVSKETLNLLLPEIMPGLIQGYDNSESSVRKACVFCLVAVHAVIGDELKPHLSQLTGSKMKLLNLYIKRAQTGSGGADPTTDVSGQS
Protein: Subtilisin-like serine-protease S (SbtS) (Subtilase S) (EC 3.4.21.-) (A9JQS7)
Organism: Lotus japonicus (Lotus corniculatus var. japonicus)
Function: Required for arbuscular mycorrhiza (AM) development during AM symbiosis with AM fungi (e.g. Glomeromycota intraradices).
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:A9QY40}. Note=Accumulates in the intercellular spaces and the periarbuscular space (PAS) during arbuscular mycorrhizal (AM) symbiosis. {ECO:0000250|UniProtKB:A9QY40}.
Interaction partners:
Sequence:
MGSAKILSFTLLLFVGYTLVHGSTPKHYIVYMGDRSHPNSESVVRANHEILASVTGSLNDAKAAAIHHYSRSFQGFSAMITPEQAKKLADHNSVVSVFESKMNKLHTTHSWDFLGLDTVYKNNPSALDSASNVIVGVIDSGVWPESESFNDYGLGPVPEKFKGECVTGDNFTLANCNKKIIGARFYSKGLEAEIGPLENIVDSIFFRSPRDSDGHGTHTASTIAGSIVSNVSLFGMAKGTARGGAPSARLSIYKACWFGFCSDADVFAAMDDAIHDGVDILSLSLGPDPPQPLYFENAISVGAFHAFQKGILVSASAGNSVFPRTACNVAPWIFTVAASTVDREFRSDIYLGNSKVLKGLSLNPIKMEGSYGLIYGSAAAAAGDAALNASFCKEHTLDPTLIKGKIVICTVEKFTDNRREKAIIIKQGGGVGMILIDHNARDVGFQFVIPSTMIGQDAVEELQAYMKTEKNPTATIFPTLTLVGTKPAPESAAFSSVGPNIITPDIIKPDITGPGVNILAAWSPVATEATVEQKSVNYNIISGTSMSCPHISAISAIIKSHHPSWSPAAIMSAIMTSATVMDNTHSLIGRDPNGTQATPFDYGSGHVNPVASLNPGLVYDFSSQDVLNFLCSNGASPAQLKNLTGELTQCQKSPTASYNFNYPSIGVSNLNGSLSVYRTVTYYGQEPTEYFASVERPSGVIVRVTPAKLKFWKAGEKITFRIDFTPFKNSNGNFVFGALTWNNGKQRVRSPIGLNVLST
Protein: CCR4-NOT transcription complex subunit 7 (EC 3.1.13.4) (CCR4-associated factor 1) (CAF1) (Q17345)
Organism: Caenorhabditis elegans
Function: Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Within the complex, plays a role in miRNA-mediated deadenylation in embryos. Within the complex promotes germ cell development and fertility in hermaphrodites. Additional complex functions may be a consequence of its influence on mRNA expression.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- CCR4-NOT transcription complex subunit 9
- poly
- CCR4-NOT transcription complex subunit let-711
- Protein PAT1 homolog 1
- Not3 domain-containing protein
- NOT2/NOT3/NOT5 C-terminal domain-containing protein
- CCR4-NOT transcription complex subunit 4
- ATP-dependent RNA helicase cgh-1
- NOT2/NOT3/NOT5 C-terminal domain-containing protein
- m7GpppN-mRNA hydrolase dcap-2
Sequence:
MASSSSGGAGGAGGASGAPEVKIHNVYMSNVEEEFARIRGFVEDYPYVAMDTEFPGVVATPLGTFRSKEDFNYQQVFCNVNMLKLIQVGFAMVNDKGELPPTGDVWQFNFNFSFAEDMFSHESVEMLRQAGIDFTLLQNNGIPTAVFGELLTTSGLITDPRITWLTFSSGYDFGYLLKSITLGDLPKEESTFFMCHKTLFPTSFDIKILLRTPNCASAKLKGGLQEVADQLDVKRQGVRHQAGSDALLTAATFFKIKKQFFGDNWNQIAPLICGHMFGLGSSLSLFHSSGSTSRLGDETPQGLIGVPQQA
Protein: GTP-binding protein-like protein (F4J5A2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEKNIFKKISAVVPTELDFDRAIRFEYQIPNCTLIPDRVCHDDISDIRQKYAVKVMSAGTTLSNKLNDVLHEFPCVRHLDPVYASLLHQRYNMYHYDRAVRQVSVTQTLVNVMSFNYVDLLRKDDDCDSRDKCRSLGVTALARMLTFAKSCIPALNLLDQVREFMASVEDDAAATSLVNKYSDVLPPEKYPFPDIVWEDETADFVDPETLLLVEELDRRYELWLKGGSHI
Protein: Proteasome subunit beta (EC 3.4.25.1) (20S proteasome beta subunit) (Proteasome core protein PrcB) (P9WHT9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins. One function of the proteasome is to contribute to M.tuberculosis ability to resist killing by host macrophages, since the core proteasome is essential for persistence of the pathogen during the chronic phase of infection in mice. Likely functions to recycle amino acids under nutrient starvation, thereby enabling the cell to maintain basal metabolic activities (By similarity). The mechanism of protection against bactericidal chemistries of the host's immune response probably involves the degradation of proteins that are irreversibly oxidized, nitrated, or nitrosated. A proteolysis-independent activity of the proteasome core is required for optimal growth of M.tuberculosis in mouse lungs and for RNI resistance; in contrast, long-term survival of M.tuberculosis in stationary phase and during starvation in vitro and in the chronic phase of mouse infection required a proteolytically active proteasome.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}.
Interaction partners:
- Proteasome subunit alpha
- Prokaryotic ubiquitin-like protein Pup
- Proteasome-associated ATPase
- Pup deamidase/depupylase
- Bacterial proteasome activator
- Pup--protein ligase
- CysO-cysteine peptidase
- Glycerol kinase
- Conserved ATPase
- ESX-1 secretion system protein EccA1
Sequence:
MTWPLPDRLSINSLSGTPAVDLSSFTDFLRRQAPELLPASISGGAPLAGGDAQLPHGTTIVALKYPGGVVMAGDRRSTQGNMISGRDVRKVYITDDYTATGIAGTAAVAVEFARLYAVELEHYEKLEGVPLTFAGKINRLAIMVRGNLAAAMQGLLALPLLAGYDIHASDPQSAGRIVSFDAAGGWNIEEEGYQAVGSGSLFAKSSMKKLYSQVTDGDSGLRVAVEALYDAADDDSATGGPDLVRGIFPTAVIIDADGAVDVPESRIAELARAIIESRSGADTFGSDGGEK
Protein: Transcription factor SOX-10 (P56693)
Organism: Homo sapiens (Human)
Function: Transcription factor that plays a central role in developing and mature glia (By similarity). Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination (By similarity). Once induced, MYRF cooperates with SOX10 to implement the myelination program (By similarity). Transcriptional activator of MITF, acting synergistically with PAX3. Transcriptional activator of MBP, via binding to the gene promoter (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12138193}. Nucleus {ECO:0000269|PubMed:12138193}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q04888}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q04888}; Cytoplasmic side {ECO:0000250|UniProtKB:Q04888}.
Interaction partners:
- Paired box protein Pax-3
- E3 SUMO-protein ligase EGR2
- POU domain, class 3, transcription factor 2
- Microphthalmia-associated transcription factor
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- Myelin basic protein
- POU domain, class 3, transcription factor 1
- Nuclear factor of activated T-cells, cytoplasmic 4
- Histone deacetylase 2
- Periaxin
Sequence:
MAEEQDLSEVELSPVGSEEPRCLSPGSAPSLGPDGGGGGSGLRASPGPGELGKVKKEQQDGEADDDKFPVCIREAVSQVLSGYDWTLVPMPVRVNGASKSKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESDKRPFIEEAERLRMQHKKDHPDYKYQPRRRKNGKAAQGEAECPGGEAEQGGTAAIQAHYKSAHLDHRHPGEGSPMSDGNPEHPSGQSHGPPTPPTTPKTELQSGKADPKRDGRSMGEGGKPHIDFGNVDIGEISHEVMSNMETFDVAELDQYLPPNGHPGHVSSYSAAGYGLGSALAVASGHSAWISKPPGVALPTVSPPGVDAKAQVKTETAGPQGPPHYTDQPSTSQIAYTSLSLPHYGSAFPSISRPQFDYSDHQPSGPYYGHSGQASGLYSAFSYMGPSQRPLYTAISDPSPSGPQSHSPTHWEQPVYTTLSRP
Protein: Long-chain fatty acid transport protein 5 (FATP-5) (Fatty acid transport protein 5) (Bile acid-CoA ligase) (BA-CoA ligase) (BAL) (Bile acyl-CoA synthetase) (BACS) (EC 6.2.1.7) (Cholate--CoA ligase) (Fatty-acid-coenzyme A ligase, very long-chain 3) (Long-chain-fatty-acid--CoA ligase) (EC 6.2.1.3) (Solute carrier family 27 member 5) (Very long-chain acyl-CoA synthetase homolog 2) (VLCS-H2) (VLCSH2) (EC 6.2.1.-) (Very long-chain acyl-CoA synthetase-related protein) (VLACS-related) (VLACSR) (Q9Y2P5)
Organism: Homo sapiens (Human)
Function: May mediate the import of long-chain fatty acids (LCFA) by facilitating their transport across cell membranes. Also catalyzes the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates. Mainly functions as a bile acyl-CoA synthetase catalyzing the activation of bile acids via ATP-dependent formation of bile acid CoA thioesters which is necessary for their subsequent conjugation with glycine or taurine. Both primary bile acids (cholic acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid) are the principal substrates. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate ((25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate or THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Plays an important role in hepatic fatty acid uptake and bile acid reconjugation and recycling but not in de novo synthesis of bile acids (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10479480}; Multi-pass membrane protein {ECO:0000255}. Microsome {ECO:0000250|UniProtKB:Q9ES38}. Cell membrane {ECO:0000250|UniProtKB:Q4LDG0}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Bile acid-CoA:amino acid N-acyltransferase
- Sterol carrier protein 2
- Sterol 26-hydroxylase, mitochondrial
- Alpha-methylacyl-CoA racemase
- Acyl-coenzyme A thioesterase 8
- Bile salt export pump
- Long-chain-fatty-acid--CoA ligase 1
- Peroxisomal acyl-coenzyme A oxidase 2
Sequence:
MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWVPHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAFERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVLASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVDPLFVLDNRAQSFRPLTAEMYQAVCEGTWRL
Protein: Serine/arginine-rich splicing factor 12 (35 kDa SR repressor protein) (SRrp35) (Splicing factor, arginine/serine-rich 13B) (Splicing factor, arginine/serine-rich 19) (Q8WXF0)
Organism: Homo sapiens (Human)
Function: Splicing factor that seems to antagonize SR proteins in pre-mRNA splicing regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Serine/arginine-rich splicing factor 11
- RNA-binding protein FUS
- Serine/arginine-rich splicing factor 1
- Serine/arginine-rich splicing factor 9
- Transformer-2 protein homolog alpha
- Dual specificity protein kinase CLK2
- Dual specificity protein kinase CLK3
Sequence:
MSRYTRPPNTSLFIRNVADATRPEDLRREFGRYGPIVDVYIPLDFYTRRPRGFAYVQFEDVRDAEDALYNLNRKWVCGRQIEIQFAQGDRKTPGQMKSKERHPCSPSDHRRSRSPSQRRTRSRSSSWGRNRRRSDSLKESRHRRFSYSQSKSRSKSLPRRSTSARQSRTPRRNFGSRGRSRSKSLQKRSKSIGKSQSSSPQKQTSSGTKSRSHGRHSDSIARSPCKSPKGYTNSETKVQTAKHSHFRSHSRSRSYRHKNSW
Protein: Zinc uptake regulation protein (Zinc uptake regulator) (P9WN85)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Global transcriptional regulator involved in zinc homeostasis. Represses the transcription of at least 32 genes, including genes involved in zinc homeostasis, by binding to promoter sequences that contain a conserved 26 bp palindrome, in the presence of zinc.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase subunit alpha
- HTH-type transcriptional repressor SmtB
- Transcriptional regulator FurA
- Iron-dependent repressor IdeR
- RNA polymerase sigma factor SigA
- Probable transcriptional regulatory protein
- RNA polymerase sigma factor SigB
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit omega
- DNA-directed RNA polymerase subunit beta'
Sequence:
MSAAGVRSTRQRAAISTLLETLDDFRSAQELHDELRRRGENIGLTTVYRTLQSMASSGLVDTLHTDTGESVYRRCSEHHHHHLVCRSCGSTIEVGDHEVEAWAAEVATKHGFSDVSHTIEIFGTCSDCRS
Protein: AT4g27450/F27G19_50 (Aluminum induced protein with YGL and LRDR motifs) (Q93V62)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Serine/arginine-rich splicing factor SC35
- Cell division cycle 5-like protein
- Nuclear protein-like
- AT3G03270 protein
- Small nuclear ribonucleoprotein Sm D2
- At5g44730
- Anaerobic nitrite reductase AHB1
- U2 small nuclear ribonucleoprotein A'
- AT3G11930 protein
- Uncharacterized protein At3g23325
Sequence:
MLAIFHEAFAHPPEELNSPASEKCSKQPKLPEETLNDFLLRYPLNTFSMSFGQAAVLAYVRPSASFSIHQRLFCGFDDIYCLFFGSLNNLCQLNKQYGLTKTTNEAMFVIEAYRTLRDRGPYPADQVVKDLDGSFSFVVYDSKAGSVFTALGSDGGVKLYWGIAADGSVVISDDLDVIKEGCAKSFAPFPTGCMFHSEGGLMSFEHPMNKIKAMPRVDSEGVLCGANFKVDVYNRVNSIPRRGSEANWSL
Protein: Small ribosomal subunit protein eS12 (40S ribosomal protein S12) (P80455)
Organism: Drosophila melanogaster (Fruit fly)
Function: Subunit of the 40S ribosomal complex. In wing imaginal disks, might have a role in translation rate, growth and cell competition, probably through regulation of Xrp1 expression. Might have a role in development and longevity.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:P25398}.
Interaction partners:
- Small ribosomal subunit protein uS8A
- Large ribosomal subunit protein eL43
- 40S ribosomal protein S24
- Ubiquitin-ribosomal protein eL40 fusion protein
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein P2
- Small ribosomal subunit protein eS4
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein eS10B
Sequence:
MADVDVDVPSAAPVLDGAMDINTALQEVLKKSLIADGLVHGIHQACKALDKRQAVLCILAESFDEPNYKKLVTALCNEHQIPLIRVDSHKKLGEWSGLCKIDKEGKPRKVCGCSVVVIKDFGEETPALDVVKDHLRQNS
Protein: Inactive tyrosine-protein kinase PEAK1 (Pseudopodium-enriched atypical kinase 1) (Sugen kinase 269) (Tyrosine-protein kinase SgK269) (Q69Z38)
Organism: Mus musculus (Mouse)
Function: Probable catalytically inactive kinase. Scaffolding protein that regulates the cytoskeleton to control cell spreading and migration by modulating focal adhesion dynamics. Acts as a scaffold for mediating EGFR signaling.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20534451}. Cell junction, focal adhesion {ECO:0000269|PubMed:20534451, ECO:0000269|PubMed:35687021}. Note=Colocalizes with actin (PubMed:20534451).
Interaction partners:
- Eukaryotic translation initiation factor 5A-1
Sequence:
MSACNTFTEHVWKPGECKNCFKPKSLHQLPPDSEKTPITHGSGKTNANHSNNHRVRSTGNFRPPVAKKPTIAVKPTMMVADGQSVCGELSIQEHCENKPVILGWNQNKTSLSQKPLNNNSEGDAEGFGSDPQQCANNDSAQKISNNNNGLTEVLKEIAGLEATPPVRGNETNARETFLGRINDCYKRSLERKIPPSCMTGSMKDSQGKHVILSGSAEVISNEGGRFCYPEFSSGEESEEDVLFSNMEEEHESWDESDEELLAMEIRMRGQPRFANFRANTLSPVRFFVSKKWNTIPLRNKSLQRICAVDYDDSYDEILNGYEENSGVSYGQGSVQSTISSDCTSPGSSFTEESRSETASSLSQKVCNGGISPGNPGNSKDIAETESNFESPPGNNEEKDESLTSKSSVKVPETHKAVLALRLQEKDGKIAVHTEKPESKASTDIAGQAVTISLVPVEEQTKPYRVVNLEQPLCKPYTVVDVSAAMASEHLGRPKIKGSSSTPNSPVTSPALTPGQINAHLKKSSAIRYQEVWTSSTSPRQKIPKIELSTGGPGPNVPPRKNCHKSAPTSPTATNISSKTIPVKSPNLSEIKFNSYNNAGMPPFPIIIHDEPSYARSSKNAIKVPIVINPNAYDNLAIYKSFLGTSGELSVKEKTTSVISHTYEEIETESKVSDSTPSKLTDCPQAKGFSNSTERKRGSVAQKVQEFNNCLNRGQSSPQRSYSSTHSSPAKIQRPTQEPAGKTEGAQGSQVPGSSSNSTREKASAVLCQIVASIQPPQTPPEAPQSSPKACSVEELYAVPPDADTTKSIPKNPPVRPKSLFTSQSSGEGEAHQTTESPTAKIQKDPSTKPVTSPPSKLVTSAQSEPPPPFPPPRSTSSPYHASNLLQRHFTNWTKPTSPTRSTEAESILHSEGSRRAADAKPKRWISFKSFFRRRKTDEEEEKEKEREKGKLVGLDGTVIHMLPPPPVQRHHWFTEAKGEASEKPAIVFMYRCDPDQGHLSVDQSKAGAEKGRAEEVLLRNSEEKKSSYLPSQIPDKACSRVTHEVAGELSPRDPRTPAGKQDGTSVTPTLPPPDLEREEEKDDTLDPTDVSPCSATYSNLGQSRAAMIPPKHPRHPKGAVDDAIAFGEKTDQEGLNASQPTPPPLPKKMIRANTEPISKDLQKAMESSLCVMANPTYDIDPNWDASSAGSSISYELKGLDVESYESLERPLHKERPVPSAANSISSLATLSVKDRFSNSMESLSSRRGLSYRQTRSIQKPQRQALYRGLDNREEVVGKLRSLHTDALKRLAVKCEDLFMAGQKDQLRFGVDSWSDFRLTSDKPCCEAGDAVYYTASYAKDPLSNYAVKICKSKAKESQQYYHSLAVRQSLPVHFNIQQDCGHFLAEVPSRLLPWEDPDAPEKAEDGTEDSEEEGKAETLGGNPEPCSETEPSQKENQRVTNRKQRSHVVVITREVPHLTVADFVRDSLAHHGNSPDLYERQVCLLLLQLCSGLEHLKPYHVTHCDLRLENLLLVQHQPGGAAQGPSPADPCPTLACPTRLIVSNFSQAKQKSHLVDPQILRDQSRLAPEIITATQYKKCDEFQTGILIYEMLHLPNPFDENPELKEKEYTRTDLPRIPLRSPYSWGLQQLASCLLNPNPSERILISDAKGILQCLLWGPREDLFQIFTTSATLAQKNALLQNWLDIKRTLLMIKFAEKSLDREGGISLEDWLCAQYLAFATTDSLSYIVKILQYR
Protein: Global nitrogen regulator (P29283)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Required for full expression of proteins subject to ammonium repression. Transcriptional activator of genes subject to nitrogen control.
Interaction partners:
- PipX
- Nitrogen regulatory protein P-II
- Ferredoxin--nitrite reductase
- Ammonium transporter
- Acetylglutamate kinase
- DNA-directed RNA polymerase subunit gamma
- Ammonium transporter
- Cyclic nucleotide-binding domain
- Probable nitrogen assimilation transcriptional activator
- Ribulose bisphosphate carboxylase large chain
Sequence:
MLANENSLLTMFRELGSGKLPLQIEQFERGKTIFFPGDPAERVYLLVKGAVKLSRVYESGEEITVALLRENSVFGVLSLLTGQRSDRFYHAVAFTPVQLFSVPIEFMQKALIERPELANVMLQGLSSRILQTEMMIETLAHRDMGSRLVSFLLILCRDFGIPSPDGITIDLKLSHQAIAEAIGSTRVTVTRLLGDLRESKLIAIHKKRITVFNPVALSQQFS
Protein: Putative deoxyribonuclease TATDN2 (EC 3.1.21.-) (Q93075)
Organism: Homo sapiens (Human)
Function: Putative deoxyribonuclease.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- X-box-binding protein 1
Sequence:
MASERGKVKHNWSSTSEGCPRKRSCLREPCDVAPSSRPAQRSASRSGGPSSPKRLKAQKEDDVACSRRLSWGSSRRRNNSSSSFSPHFLGPGVGGAASKGCLIRNTRGFLSSGGSPLRPANASLEEMASLEEEACSLKVDSKDSSHNSTNSEFAAEAEGQNDTIEEPNKVQKRKRDRLRDQGSTMIYLKAIQGILGKSMPKRKGEAATRAKPSAAEHPSHGEGPARSEGPAKTAEGAARSVTVTAAQKEKDATPEVSMEEDKTVPERSSFYDRRVVIDPQEKPSEEPLGDRRTVIDKCSPPLEFLDDSDSHLEIQKHKDREVVMEHPSSGSDWSDVEEISTVRFSQEEPVSLKPSAVPEPSSFTTDYVMYPPHLYSSPWCDYASYWTSSPKPSSYPSTGSSSNDAAQVGKSSRSRMSDYSPNSTGSVQNTSRDMEASEEGWSQNSRSFRFSRSSEEREVKEKRTFQEEMPPRPCGGHASSSLPKSHLEPSLEEGFIDTHCHLDMLYSKLSFQGTFTKFRKIYSSSFPKEFQGCISDFCDPRTLTDCLWEELLKEDLVWGAFGCHPHFARYYSESQERNLLQALRHPKAVAFGEMGLDYSYKCTTPVPEQHKVFERQLQLAVSLKKPLVIHCREADEDLLEIMKKFVPPDYKIHRHCFTGSYPVIEPLLKYFPNMSVGFTAVLTYSSAWEAREALRQIPLERIIVETDAPYFLPRQVPKSLCQYAHPGLALHTVREIARVKDQPLSLTLAALRENTSRLYSL
Protein: Probable inositol polyphosphate 5-phosphatase C9G1.10c (EC 3.1.3.-) (O14306)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Barrier septum. Cell tip. {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-processing factor 19
- Polyphosphoinositide phosphatase
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase ptn1
- Uncharacterized protein C3C7.01c
- Uncharacterized protein C19F5.03
- Phosphatidylinositol 4-phosphate 5-kinase its3
- Phosphoinositide 3-phosphatase
- Cell division control protein 42 homolog
- Probable glycosidase C21B10.07
Sequence:
MASRQGFSNVNEDEPELPPSVLSLKSKFESLSTGDLTNLDEKTAKRRTVKGCKNGTSEPNVFKARPIPPPRQVSSTIGSSTGRKVSGSIQRLASNFKNPSNPHADVSKIDRLPSDSSESHVATPSSPTISNSFVSVSPLLKRPQQKGPEISFQSSVQSTKGNDLMKHDDTNNHQIPPPKPNFSSKAGSSSPISVSPLKNVKAYISQSPTHSEASSVLSSEEEEENVINSSKSVPSFDLHDPFSQTFGKECPISTAPPVLNIGDRSLETPPPIPSPRPPQPVAVEAIQQSRAVISQQLPLHVSPRKPPKPPLRKVSTQRSSSPIENLATKSDASLVTGLQSSPYTHIAPASEMSLIPEKPRLPPRPSHTLSELSSPALTSENLSSKPSPLFPPPPPRVKSLATNKPVSMPVSTEQSDPSVAASSSSSSQLDVVLKGSIPDTSSVRRNPPCFVNGVESINVDFEARIFDVSGDRLVLAGNGGLRVYDTVTGLCHWHMPLGDTKVTSLSFKSSPENYSDDGRFVWFGTRDGMLWEVDVQNHHIVTKKSVSNCPITYVMVYKNEMWTLDDMGKLYVWQEDEIMGLSIQSTPHSIRTIPHATHAMVLDNRLLWVVVGKSIYVYDPSTSENESASVLAKPMTPPGLIGDISCGTTISNFTDLVFYGHVDGKISIFSKTQYRFLELITSSSFYRICSLVGVGNTLWAAYTTGMIYVFDVSESPWRLLKSWHGHKASHNGATTILGIDVNSVWKAKRLQVVSMASSVVKFWDGLMMGDWLATEMRSRFPEYSNFTDVSILICSWNAGASKPSDLDSDTIGASMIPMMIRDNGYPDIVVFGFQELVDLENKRLTARSILSKSSSKGGSSNSANISSQYRLWREKLESEMMRVSSNDDYQVLVCENLVGLFSCVFVKNKLQSKIRMLQSTTVKTGLGGLHGNKGAIVVRFLVDDTSYCIVNCHLAAGQSNKAARNNDLATILDNASLFPENDETDQLNTFVGGGDGSLIMDHEVCVLHGDLNYRINTLRPKALDLIKKNDIKTLLQSDQLLVERKRNAGFRLRTFTEPEITFAPTYKYDVHSEQYDSSEKKRVPAWCDRICYRGSPDYISAENYTRYELKASDHRPVSALIHSKAKMVNAQSQGSTWDVVKRKWIEYADEFKRKAKITYVMNYTSVSYQTAEQYLSGNNWNVQNALKQVSS
Protein: Dolichyl-phosphate-mannose--protein mannosyltransferase 4 (EC 2.4.1.109) (O42933)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Required for normal cell wall and septum formation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:15809069, ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:15809069, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Dolichyl-phosphate-mannose--protein mannosyltransferase 1
- Dolichyl-phosphate-mannose--protein mannosyltransferase 2
- AdoMet-dependent rRNA methyltransferase spb1
- P cell-type agglutination protein map4
Sequence:
MASKSEKAVKKAQKLSKEPSVELTDTKSSDNVTPKQKSPNSTEEDVSLNLKTLKAKKFKLAFVLITVLSFITRFWNLNLPGEVVFDEVHFGKFASYYLQGKYFFDLHPPFAKLLLALVAKLAGYDGHYLFDNIGDNYKDNGVPYVTIRAWPALLSSLVPPVVFLIMKESGYDLLACIVSSSLVLFDNAHVTEGRLILLDATLLFSMVCAIYCYVRFFKLRHTPFSRPWWAWLFFTGFFLSCTISTKYVGFFTFLSIGLSVCLELWYLWDIKTGLTVERFFQHFLARFFCLIFFPFLFFLFWFYMHFNILTISGPGDSFMSLEFQETLSDNPITANSTILNYYDIVTIKHMGTNAFLHSHPEKYPIPYDDGRISSGGQQVTGYQFDDENNYWMILPADHYDPPIEAKLNVPVKNMDYIKLHHVGTNTDLMTHDVASPYHPTNEEFTTVSVDESAGKKHEYTLFQVVMSDNTDPQRPLYTKASSFKLIHKLTHVAMWSDPKPLPDWAFKQLEINGAKNIQTGSIFWTFDDIIGLKDSRLKKEKKIPKKLPFWKKYLELQLTMFRQNNMLTEFHPYSSNPSDWFTLHHGIAFWAKSEENKQIYLLGNPIGWWIIAGTVLSTTVVAAAEILLRQRGIRTLPETVRNHFYRSTMFFYMTYVFHYLPFFIMGRQLFLHHYLPAHLAGSLLVGAFIQLACRKSFRSPVSAGVPIPKDVDEKGHSKCHRKYGHVIELICTLLLIFVVIYCFTFFAPMTYGDKSLSVDEWTRRKWLDSWVFQYQKQN
Protein: Fetal brain protein 239 (Metallophosphoesterase MPPED2) (Metallophosphoesterase domain containing 2) (Metallophosphoesterase domain-containing 2b) (Mpped2 protein) (Q7ZUB6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- DnaJ
- tRNA methyltransferase 9B.
- Reticulocalbin 1, EF-hand calcium-binding domain
- Mitochondrial inner membrane protease subunit
- Elongator complex protein 4
Sequence:
MARRISSQGKVTISVDEYSSNPTQAFTHYNINQSRFQPPHVHMVEPLPYDAPKSVGHTRFVCVSDTHSRTDGIQMPFGDVLLHTGDFTELGLPSEVKKFNDWLGGLPYEYKVVIAGNHELTFDKDFMAELIKQDYYRFPSVSKLRSEDFDDVQSLLTNCVYLQDSEVTIKGFRIYGAPWTPWFNGWGFNLPRGQSLLDKWNQIPEDVDILMTHGPPLGFRDWVPKELQRVGCVELLNTVQKRVRPKLHAYGGIHEGYGIMTDGYTTFINSSTCTVSFQPTNPPIIFDLPNPGNS