wanglab/gogpt-training-data huggingface dataset:
Protein: Junctional adhesion molecule C (JAM-C) (Junctional adhesion molecule 3) (JAM-3) [Cleaved into: Soluble form of JAM-C (sJAM-C)] (Q68FQ2)
Organism: Rattus norvegicus (Rat)
Function: Junctional adhesion protein that mediates heterotypic cell-cell interactions with its cognate receptor JAM2 to regulate different cellular processes. Plays a role in homing and mobilization of hematopoietic stem and progenitor cells within the bone marrow. At the surface of bone marrow stromal cells, it contributes to the retention of the hematopoietic stem and progenitor cells expressing JAM3 (By similarity). Plays a central role in leukocytes extravasation by facilitating transmigration through the endothelium (By similarity). Plays a role in spermatogenesis where JAM2 and JAM3, which are respectively expressed by Sertoli and germ cells, mediate an interaction between both cell types and play an essential role in the anchorage of germ cells onto Sertoli cells and the assembly of cell polarity complexes during spermatid differentiation (By similarity). Also functions as a counter-receptor for ITGAM, mediating leukocyte-platelet interactions and is involved in the regulation of transepithelial migration of polymorphonuclear neutrophils (PMN). Plays a role in angiogenesis. Plays a role in the regulation of cell migration (By similarity). During myogenesis, it is involved in myocyte fusion (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9BX67}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BX67}. Cell junction {ECO:0000250|UniProtKB:Q9BX67}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q9BX67}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9BX67}. Note=Detected in the acrosome region in developing spermatids (By similarity). In epithelial cells, it is expressed at desmosomes but not at tight junctions (By similarity). Localizes at the cell surface of endothelial cells; treatment of endothelial cells with vascular endothelial growth factor stimulates recruitment of JAM3 to cell-cell contacts (By similarity). {ECO:0000250|UniProtKB:Q9BX67, ECO:0000250|UniProtKB:Q9D8B7}.; SUBCELLULAR LOCATION: [Soluble form of JAM-C]: Secreted {ECO:0000250|UniProtKB:Q9BX67}.
Interaction partners:
- Tight junction protein ZO-1
- Junctional adhesion molecule 2.
- Golgi reassembly-stacking protein 2
- Golgi reassembly stacking protein 2
- Integrin beta
- Junctional adhesion molecule A
- Partitioning defective 3 homolog
- Integrin alpha-D
- InaD-like protein
- Espin
Sequence:
MALSRRLRLRLCARLPDFFLLLLFRGCVIEAVNLKSSNRNPVVHEFESVELSCIITDSQTNDPRIEWKKIQDGQTTYVYFDNKIQGDLAGRTDVFGKTSLRIWNVTRSDSAIYRCEVVALNDRKEVDELTIELIVQVKPVAPVCRVPKAVPVGKAATLQCQESEGYPRPYYSWYRNDVPLPTDSRANPRFQNSSFHVNSETGTLVFSAVHKEDSGQYYCIASNDAGAARCEGQDMEVYDLNIAGIIGGVLVVLIVLAVITMGICCAYRRGCFISSKQDGESYKSPGKHEGVNYIRTSEEGDFRHKSSFVI
Protein: Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain] (P05156)
Organism: Homo sapiens (Human)
Function: Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha-chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins. Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces. The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired complement activation, while in apoptotic cells or microbes, the absence of such cofactors leads to C3b-mediated complement activation and subsequent opsonization.
Subcellular location: Secreted, extracellular space. Secreted {ECO:0000269|PubMed:6327681}.
Interaction partners:
- Complement factor H
- Complement C3
- Membrane cofactor protein
- Complement factor B
- Complement C4-B
- Complement C4-A
- Complement receptor type 1
- Group XIIA secretory phospholipase A2
- Complement factor H-related protein 3
- Thrombomodulin
Sequence:
MKLLHVFLLFLCFHLRFCKVTYTSQEDLVEKKCLAKKYTHLSCDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRSFPTYCQQKSLECLHPGTKFLNNGTCTAEGKFSVSLKHGNTDSEGIVEVKLVDQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSINSTECLHVHCRGLETSLAECTFTKRRTMGYQDFADVVCYTQKADSPMDDFFQCVNGKYISQMKACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGCAGFASVTQEETEILTADMDAERRRIKSLLPKLSCGVKNRMHIRRKRIVGGKRAQLGDLPWQVAIKDASGITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEYVDRIIFHENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISNCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVCMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHVGRPFISQYNV
Protein: Membrane-anchored lipid-binding protein LAM4 (Lipid transfer at contact site protein 3) (Lipid transfer protein anchored at membrane contact sites 1) (P38800)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in sterol transfer between intracellular membranes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26001273}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to puncta in the cell periphery representing cortical endoplasmic reticulum (cER)-plasma membrane (PM) membrane contact sites. {ECO:0000269|PubMed:26001273}.
Interaction partners:
- Membrane-anchored lipid-binding protein SIP3
- Membrane-anchored lipid-binding protein LAM1
- Calcium-channel protein CCH1
- 2-deoxy-glucose resistant protein 2
Sequence:
MTRDSKKKHHWGTAFLRTIGVKRKHKKDRNFLNNTTGENVSTTASAERFRRVGGNPDIPSLLKPETFTESPAKGSQKAAASSLAHSQGVFNIPIVIDPMETNRLEKTNTNLTAGSLKGRFQDGNSNSNSVPSLSVQALEKEKLQSGKREGSSNQAEEKTPDGHDEHTAFETFLSFAHNAVSHIPKINVQDADNGTISRNEPKDRKKNSSNISGALSENSTNNKNTSSTKESDGPFLKNLDNILAASKSSTPSNQQLNTTEAGSKSKPSSLSRLAFGNLKGHIHSNSHSSSNAISGDDTSLDDTRKMTDDMARKVVFEPIRHSHDKPTPGVGNLKLEHFDDSQATLEGLEAMSAESLPEADHLDSRGPVQQSNLERKTVPSKWSVVSSSTTDGVKPRRRAKSMISAMADKQNTSSDVLQDCKKRLSFNSSNGLTNNDPEYEDREPREMSKKFLNRRSFSPGSISMGMKVLPSTALKYSLNKVKNSTDIASTIIPRPSMSNGRPSSGLRRSSSKSFSSTPVNIIEPSEENGRQSSIRIKGVEYASEKKDAEFHAIFKDSGVSPNERLILDHSCALSRDILLQGRMYISDQHIGFYSNILGWVSTVFIPFKTIVQIEKRATAGIFPNGIVIDTLHTKYTFASFTSRDATYDLITEVWNQIILGKRFRSNSNNTNSSSNSISDDENDDYDDDYDDYGDDDDDLYDNSNNISDSTDMTSSVSIGKPEDLPMPLQTDTPYGTGIPPLGPKIHSPTETVYKPAPNEKLVNESTIHASLGRVVNILFGKDVSYIMAILKAQKNSDISPIPVLVDSPTVSEGKKRDYSYVKTTPGAIGPGKTKCMITETIQHFNLEEYVQVLQTTKTPDVPSGNSFYVRTVYLLSWANNNETKLKLYVSVEWTGKSLIKSPIEKGTFDGVTDATKILVEELGNILTRSATKRKRSSKENTVTVSTLPKMEPSSHAPTEPDIQKDKDDSIIRENENIPAPLGTVVQLLFGSNTEYMQKVITRDKNNVNVETIPKFTPSLVEGGSRHYEYTKKLNNSIGPKQTKCLLTESIEHMDINNYVLVTQTTKTPDVPSGSNFAVESKIFLFWGQHDTTNMTVITKINWTSKSFLKGAIEKGSVEGQKVSVDYMLSELRDIISRAKSKKPVKKVMKSHDKHRPFHSKVEQKSSESRKSDDNKDILTHILDFVQNNFSSEIFMNKLLSPQKLFLILGLTIMLFWSPRLHVFQEKNNLQIIKPGRLLIDGQEYNYVPSFGTLYNSYENAISSKKKRENVNYARDKSPIVGRESDIWDWISNRGSAISPRGRAMLRNDDEHKLQQLSESIKITEMQLNHMKTMLDNIERDANDLS
Protein: UPF0749 protein Rv1825 (P9WFG3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein Rv1824
- Uncharacterized protein Rv1829
- UPF0749 protein Rv1823
- Probable phosphatidylglycerophosphate synthase
- Glycine cleavage system H protein
- Phosphatidylinositol phosphate synthase
- Putative cardiolipin synthase
- Probable conserved membrane protein
- Protein translocase subunit SecA 2
Sequence:
MSENRPEPVAAETSAATTARHSQADAGAHDAVRRGRHELPADHPRSKVGPLRRTRLTEILRGGRSRLVFGTLAILLCLVLGVAIVTQVRQTDSGDSLETARPADLLVLLDSLRQREATLNAEVIDLQNTLNALQASGNTDQAALESAQARLAALSILVGAVGATGPGVMITIDDPGPGVAPEVMIDVINELRAAGAEAIQINDAHRSVRVGVDTWVVGVPGSLTVDTKVLSPPYSILAIGDPPTLAAAMNIPGGAQDGVKRVGGRMVVQQADRVDVTALRQPKQHQYAQPVK
Protein: Phytase PHO112 (EC 3.1.3.-) (EC 3.1.3.8) (Histidine acid phosphatase PHO112) (HAP) (Myo-inositol hexakisphosphate phosphohydrolase PHO112) (Myo-inositol-hexaphosphate 3-phosphohydrolase PHO112) (A0A1D8PS71)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Acid phosphatase
- Bifunctional hydroxyethylthiazole kinase/thiamine-phosphate diphosphorylase
- Thiamine pyrophosphokinase
- Alkaline phosphatase
- Trifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase/thiaminase
- Alkaline phosphatase
- FAD synthase
- Riboflavin synthase
- Riboflavin kinase
- Tyrosine protein phosphatase
Sequence:
MVSVSKLINNGLLLTSQSVFQDVATPQQASVQQYNILNFLGGSAPYIQRNGYGISTDIPAGCEIAQIQLYSRHGERYPSKSNGKSLEAIYAKFKNYNGTFKGDLSFLNDYTYFVKDQSNYAKETSPKNSEGTYAGTTNALRHGAAFRAKYGSLYKENSTLPIFTSNSNRVHETSKYFARGFLGDDYEEGKTVKFNIISEDADVGANSLTPRSACSKNKESSSSTAKKYNTTYLNAIAERLVKPNPGLNLTTSDVNNLFSWCAYEINVRGSSPFCDLFTNEEFIKNSYGNDLSKYYSNGAGNNYTRIIGSVILNSSLELLKDTENSNQVWLSFAHDTDLEIFHSALGLLEPAEDLPTSYIPFPNPYVHSSIVPQGARIYTEKLQCGNDAYVRYIINDAVVPIPKCATGPGFSCKLDDFENFVKERIGDVDFIKQCGVNSTYPSELTFYWDYKNVTYNAPLEL
Protein: mRNA-capping enzyme subunit beta (EC 3.6.1.74) (mRNA 5'-phosphatase) (mRNA 5'-triphosphate monophosphatase) (Q9P6Q6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- mRNA-capping enzyme subunit alpha
- Transcription elongation factor spt5
- Abhydrolase domain-containing protein C57A10.08c
- Uncharacterized mitochondrial carrier C19G12.05
- SAGA complex/transcription factor TFIID complex subunit Taf9
- SAGA complex/transcription factor TFIID complex subunit Taf12
- SAGA complex subunit Sgf73
- SAGA complex/transcription factor TFIID complex subunit Taf6
- m7GpppX diphosphatase
- SAGA complex/transcription factor TFIID complex subunit Taf10
Sequence:
MDLKGLLHEENELPSIEKRKIDENAVEHDKVERKRTKSVAVPKIEMNFLNKPIVPDTTKVISNFLTHYLITEPVEHVEIEAKLGTLIDLETQNRFEFPVMNETILNPEFNLRTRFESDMTASEHKYLNEFLNQAFRDSQKPGRLPFAYKHTKQVDLFYETEDNSRDKIRVSKNQSDNQVLACVKKRRVADLFLYCPNDAFDIRISISDELPVSMPSGNQQPSLTRLKDRVGYVHQEIKIDLTKTTQNDPVYDTTERHELEVEFGNIADLRDRAQKAKDGMEAPLFRRVQLFMDNVRILRREHS
Protein: Alpha-1,4-N-acetylglucosaminyltransferase (Alpha4GnT) (EC 2.4.1.-) (Q14BT6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of N-acetylglucosamine (GlcNAc) to core 2 branched O-glycans. Necessary for the synthesis of type III mucin which is specifically produced in the stomach, duodenum, and pancreatic duct. May protect against inflammation-associated gastric adenocarcinoma.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Mucin-6
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4
Sequence:
MLKEIYLSLSLVLVFACGLLYQLTMRSQCFFACLPPFSFPQGLDGLLRSGRSIMFIETSERVEPPPMVSCAVESAAKIYPEQPIIFFMKGLRDSVQLTSNTSYPAFSLLSAINNVFFVPLDMERLFKDTPLFSWYTKVNSSTEKHWLHVSSDAARLAIIWKYGGIYMDTDVISLQPIPEENFLAAQGSRHSSNGVFGFLPHHPFLWACMENFVEHYDSTIWGNQGPQLMTRMLRVWCRLKDFHGLGDLKCLNISFLHPQRFYPIPYPQWKRYYQVWDKEPSFNESYALHLWNYMNKEGKTVVRGSKTLVENLYQKHCPKTYRVLIQGAEGTVSKKPGTGSR
Protein: Synaptonemal complex protein 3 (O62238)
Organism: Caenorhabditis elegans
Subcellular location: Chromosome {ECO:0000269|PubMed:17565948}. Note=Upon entrance into pachytene, localizes continuously at the interface between paired and aligned homologous chromosomes (PubMed:17565948). As nuclei progress through late prophase, chromosomal association is progressively reduced (PubMed:17565948). {ECO:0000269|PubMed:17565948}.
Interaction partners:
- Synaptonemal complex protein 4
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- HORMA domain-containing protein
- HORMA domain-containing protein
- HORMA domain-containing protein
- Meiotic recombination protein spo-11
- HORMA domain-containing protein
- Cyclin N-terminal domain-containing protein
- PH domain-containing protein
- Zip homologous protein 3
Sequence:
MNFEKLVSQAVNGDRFKIFCGQLTEFTNSLAGEREAIEKGMRQIETQQLEAETSFTERIAEDRVKCAAQRESLERQLQDLTATDNKLSEQKRDWEERQEKAYDELMSYLENEDVDSAGTQFGDHFNSLIKSMNNLSHDSMNGQFNSLKNNLDELNIEKKQLEVAIADQSSTISEMIPSLRPTCGATYKERNTLRIIFHYQVAKLRSEYQKCRLQEEALKARLST
Protein: Transcription factor WRKY5 (OsWRKY5) (WRKY transcription factor 5) (Q75L34)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription factor that acts as positive regulator of leaf senescence. Is involved in both the onset and progression of leaf senescence. Upregulates the expression of genes controlling chlorophyll degradation and leaf senescence. Acts as positive regulator of the senescence-associated NAC genes NAC4 and NAC58. Acts as positive regulator of abscisic acid (ABA) biosynthesis during leaf senescence. Acts as negative regulator of drought tolerance by inhibiting ABA-induced stomatal closure during drought stress. Functions as a direct negative regulator of MYB2 transcription through binding to the repeated W-boxes of the MYB2 promoter region.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223, ECO:0000269|PubMed:31505875}.
Interaction partners:
Sequence:
MEMMVQKQRHEEGEEERGGLCAREIKELDFFSAAGAGAGRRDDDDVLRADGISSSHAGFMVSTALDLLTAVNDGDHHEEKKGQSNIHQSKQMDAAATTVEGELRQAGEENRRLRRRLEELTSSYGALYHQLVQAQQLHTKHQQQAPIAGVQLLDALAAASPASHRRRAAAAVDGDRTADSDGGEGDENVSPSLGSKRPAAAATLTRLTPESGSGGENNGGGEQAPAAEMAPCRKARVSVRARSEAPMISDGCQWRKYGQKMAKGNPCPRAYYRCTMASQCPVRKQVQRCAEDKSILITTYEGTHSHPLPPAAAAMAKTTSAAAAMLLSGPAVSRDALFAAHHHVVAPPPFFHHPYAGSTMATLSASAPFPTITLDLTQPPPTTTTTAAAAMLQLHRPYAFSSLPFSMYGAGGGSHRPPVVLPPPSSVVETMTAAITRDPNFTTAVAAALSSIMAGGGAQARTPPRGGSDAAGDINGGGGADHATAGARAAAAATQPCGTSPT
Protein: Candida glabrata strain CBS138 chromosome K complete sequence (Q6FM95)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcriptional activator HAP2
- Candida glabrata strain CBS138 chromosome J complete sequence
- DNA polymerase epsilon subunit D
- Candida glabrata strain CBS138 chromosome K complete sequence
Sequence:
MEKMEKTYGQEPGQEPGQEPGQEQEQALEQSREQEQGRGAGMKGEELDVQFDNGAHEDGLEFEEDEDVFRNVGLGLEGHYKEIMIEYWQQLINEIESTNEPGSEYQDDFKSHSLPFARIRRVMKTDEEVKMISAEAPIIFAKACEVFITELTMRAWCVAEKHKRRTLQKADIAEALQMSDMFDFLIDIVPRSTIGAQNNSS
Protein: 1,3-beta-glucanosyltransferase (EC 2.4.1.-) (Q4WLT3)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU361209}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU361209}.
Interaction partners:
Sequence:
MRFSSILAGAILLASRTSAVDVDPIVIKGSKFFYKSNDTQFYIRGVAYQQDYSGSQSSSNSFKDPLADADACKRDVPYLEKLGTNTIRVYAVDPTADHTMCMDLLSQAGIYVIADLSSPGESIIRNDPKWDSDLFNRYVTVVDALAKYTNVIGFFAGNEVSNTKQTTHASAFVKAAVRDMKAYIKAKNYRPMGVGYATNDDSSIREKMADYFNCDNAEESIDFWGYNIYSWCGDSSYEESGYSTRTDEFRDYSVPVFFAEYGCNAVEPRKFTEVSALYGSRMASVWSGGIVYMYFQEANNYGLVSIDGDKVRTRADYSYLSQQLASATPSGTKKSEYTPANSALQSCPPVNGDWLATASPLPPSPNGDLCSCMEESLSCVLKDTVSGDQIEKLFGTVCGYDVCEGVTTNATTGKYGAYSVCSPKQQLSYAMNLYYEQQSAKGKGQSACNFNGAASTRTSSSPSGTCSALLKEAGISGTGTVTSSPTGVAGAAVVDSSGSASASTSQGAAYMNAPGRVTAGIQQLGLYVVTAIAAGAGMVLL
Protein: phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) (B2RYG2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
SPPSLTPRLHWFLWPSRSASPGAMAAMYLPGLRLSWHRLRPWCRSPCRSIQTLRVLSGDLSQLPAGVRDFVERSAHLCQPAGIHICDGTEAENAATLALLEEQGLIRKLPKYENCWLARTDPKDVARVESKTVIVTSSQRDTVPLLAGGASGQLGNWMSPDEFQRAVDQRFPGCMQGRTMYVLPFSMGPLGSPLSRIGVQLTDSPYVVASMRIMTRLGTHVLQALGDGDFIKCLHSVGQPLTGHGDPVGRWPCNPEKTLIGHVPEQREIVSFGSGYGGNSLLGKKCFALRIASRLARDEGWLAEHMLILGITNPAGKKRYVAAAFPSACGKTNLAMMRPALPGWKVECVGDDIAWMRFDSEGQLRAINPENGFFGVAPGTSATTNPNAMATIQSNTVFTNVAETSDGGVYWEGIDQPLPPGVTVTSWLGKPWKPGDKEPCAHPNSRFCVPARQCPIMDPAWEAPEGVPIDAIIFGGRRPKGVPLVYEAFSWRHGVFVGSAMRSESTAAAEHKGKTIMHDPFAMRPFFGYNFGHYLEHWLSMEGRKGARLPRIFHVNWFRRDEAGRFLWPGFGENARVLDWICRRLGGEDSARETPIGLVPKEGALDLSGLRAIDTSQLFSIPKDFWEQEVRDIRSYLTEQVNQDLPKEVLAELEALEERVQKM
Protein: Signal transduction histidine-protein kinase/phosphatase UhpB (EC 2.7.13.3) (EC 3.1.3.-) (P09835)
Organism: Escherichia coli (strain K12)
Function: Part of the UhpABC signaling cascade that controls the expression of the hexose phosphate transporter UhpT. UhpB functions as a membrane-associated protein kinase that autophosphorylates in response to interaction with UhpC, and subsequently transfers its phosphate group to the response regulator UhpA. Can also dephosphorylate UhpA.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transcriptional regulatory protein UhpA
- Membrane sensor protein UhpC
- Hexose-6-phosphate:phosphate antiporter
- Nitrate/nitrite response regulator protein NarP
- Nitrate/nitrite response regulator protein NarL
- DNA-binding transcriptional activator EvgA
- Fimbriae Z protein
- Transcriptional regulatory protein RcsB
Sequence:
MKTLFSRLITVIACFFIFSAAWFCLWSISLHLVERPDMAVLLFPFGLRLGLMLQCPRGYWPVLLGAEWLLIYWLTQAVGLTHFPLLMIGSLLTLLPVALISRYRHQRDWRTLLLQGAALTAAALLQSLPWLWHGKESWNALLLTLTGGLTLAPICLVFWHYLANNTWLPLGPSLVSQPINWRGRHLVWYLLLFVISLWLQLGLPDELSRFTPFCLALPIIALAWHYGWQGALIATLMNAIALIASQTWRDHPVDLLLSLLVQSLTGLLLGAGIQRLRELNQSLQKELARNQHLAERLLETEESVRRDVARELHDDIGQTITAIRTQAGIVQRLAADNASVKQSGQLIEQLSLGVYDAVRRLLGRLRPRQLDDLTLEQAIRSLMREMELEGRGIVSHLEWRIDESALSENQRVTLFRVCQEGLNNIVKHADASAVTLQGWQQDERLMLVIEDDGSGLPPGSGQQGFGLTGMRERVTALGGTLHISCLHGTRVSVSLPQRYV
Protein: Putative RNA-binding protein involved in heterochromatin assembly (Asparagine-rich protein) (Protein ARP) (P32770)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in chromatin organization.
Subcellular location: Chromosome {ECO:0000250|UniProtKB:O13801}. Nucleus {ECO:0000250|UniProtKB:O13801}.
Interaction partners:
- 25S rRNA
- Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1
- Synchronized import protein 1
- Protein HGH1
- Uncharacterized protein YBL081W
- Protein-lysine N-methyltransferase EFM2
- U3 small nucleolar RNA-associated protein 4
Sequence:
MHYVVLELQVAHLPDTPKDQCRIANIAFQIVNAETLVCHYGTNSLPSIEVNGTTKSLESAMVQLDKDIHDVIGNDDFVLVSLYSTWHIRVTLPRQARDDGFILTSYLQHPKVFDLWKEFDRWCVNHPEILGQKKAISNNNCNTKSISINAAKNTKDLDEIVRILEVSIPTEEAGSVPEIYSLLKRTTDILIQLHKKCTSPEDMESVLTKPYDSHTDIRAFLQEKSKILYMNNLPPDTTQSELESWFTQYGVRPVGFWTVKNIVEDTSNVNNNWSLNNSPYVEDQDSISGFVVFQTHEEATEVLALNGRSILSNLANTKQPRVVEHVLELQPSSTGVLDKAQEILSPFPQSKNKPRPGDWNCPSCGFSNFQRRTACFRCSFPAPSNSQIHTANSNNNVNSSRNNLNNRVNSGSSSNISNTAANHPYGAPEFNMIANNTPAALTYNRAHFPAITPLSRQNSLNMAPSNSGSPIIIADHFSGNNNIAPNYRYNNNINNNNNNINNMTNNRYNINNNINGNGNGNGNNSNNNNNHNNNHNNNHHNGSINSNSNTNNNNNNNNGNNSNNCNSNIGMGGCGSNMPFRAGDWKCSTCTYHNFAKNVVCLRCGGPKSISGDASETNHYIDSSTFGPASRTPSNNNISVNTNGGSNAGRTDGNDNKGRDISLMEFMSPPLSMATKSMKEGDGNGSSFNEFKSDKANVNFSNVGDNSAFGNGFNSSIRW
Protein: S-adenosyl-L-methionine-dependent methyltransferases superfamily protein (Q8L601)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Putative tRNA
- 25S rRNA
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Pumilio homolog 24
- Putative rRNA 2'-O-methyltransferase fibrillarin 3
Sequence:
MGRGGRHRGRTQRKDFKESRENVWKRPKSDASVDGSDNAVPEQKPTWEPIVTVNPNFEEYYKKQGIVKAEEWDLFMEILRKPLPAAFRVNSNGQFCDEIISILENDFMKSLQAEAIEGGELEAIKPLPWYPKNLAWHSNFSRKEIRKNQTLERFHEFLKLENEVGNITRQEAVSMVPPLFLDVHPDHFVLDMCAAPGSKTFQLLEIIHEASEPGSLPNGLVVANDVDFKRSNLLIHQTKRMCTSNLIVTNHEGQQFPGCRLNKSRASEKGISENMPINQLAFDRVLCDVPCSGDGTLRKAPDIWRKWNSGMGNGLHSLQIILAMRGLSLLKVGGKMIYSTCSMNPVEDEAVVAEILRRCGDSVELLDVSDKLPELIRRPGLKAWKVRDKGGWFTSYKDVPQNRRGGVLVSMFPSGKYLKDSTETTEKNENGDVNGCEDGLKETDISVVDATPEEQAEEVSDLPLERCMRIIPHDQNTGAFFIAVLQKKSPLPEFQEKPNTKRNSTAKSTDSTEKSPSKESVVTVDAGVPDESAVEKVIEADSNIEKNDSLEPEKKITEGESITEDKEANSSNAGGKRKVPMQGKWKGFDPVVFVKDETVINGIKEFYGIKDESFPLHGHLVARNTDTSSVKRIYYVSKSVKEVLQLNFAVGQQLKIASVGLKMFERQSAKEGSSTLCPFRISSEGLPVILPYITKQVLYTPMADFKLLLQDKSIKFHDFVNPQLAQKATDLVMGSCVVILSDGEVPVKADASTIAISCWRGKASLAVMATVADCQELLERFAEKTPKTEGGSVNGSNGDSDGPLAMET
Protein: Enoyl-[acyl-carrier-protein] reductase, mitochondrial (EC 1.3.1.104) (2-enoyl thioester reductase) (Nuclear receptor-binding factor 1) (NRBF-1) (Q9DCS3)
Organism: Mus musculus (Mouse)
Function: Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Displays a preference for medium-chain over short- and long-chain substrates (By similarity). May provide the octanoyl chain used for lipoic acid biosynthesis, regulating protein lipoylation and mitochondrial respiratory activity particularly in Purkinje cells.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BV79}.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Fatty acid synthase
- Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Lipoyl amidotransferase LIPT1, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 3
Sequence:
MLVSQRVTGARARAPQLAGLLEAWYRHGRTTSSYSALSEPSRVRALVYGNHGDPAKVVQLKNLELTAVEGSDVHVRMLAAPINPSDINMIQGNYGLLPKLPAVGGNEGVGQVIAVGSSVSALKPGDWVIPANAGLGTWRTEAVFSEEALIGIPKDIPLQSAATLGVNPCTAYRMLVDFEQLQPGDSVIQNASNSGVGQAVIQIASALRLKTINVVRDRPDIKKLTDRLKDLGADYVLTEEELRMPETKTIFKDLPLPRLALNCVGGKSSTELLRHLAPGGTMVTYGGMAKQPVTASVSLLIFKDLKLRGFWLSQWKKNHSPDEFKELILTLCNLIRQGRLTAPSCSEVPLQGYQQALEASMKPFVSSKQILTM
Protein: WW domain-containing adapter protein with coiled-coil (Q9BTA9)
Organism: Homo sapiens (Human)
Function: Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1). Interacts with the RNA polymerase II transcriptional machinery via its WW domain and with RNF20-RNF40 via its coiled coil region, thereby linking and regulating H2BK120ub1 and gene transcription. Regulates the cell-cycle checkpoint activation in response to DNA damage. Positive regulator of amino acid starvation-induced autophagy. Also acts as a negative regulator of basal autophagy. Positively regulates MTOR activity by promoting, in an energy-dependent manner, the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex. This leads to the dimerization of the mTORC1 complex and its subsequent activation. May negatively regulate the ubiquitin proteasome pathway.
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:Q924H7}. Nucleus {ECO:0000269|PubMed:21329877}. Note=In distinct nuclear speckles. Colocalizes with pre-mRNA processing complexes. {ECO:0000250|UniProtKB:Q924H7}.
Interaction partners:
- E3 ubiquitin-protein ligase BRE1A
- E3 ubiquitin-protein ligase BRE1B
- Cell division cycle 5-like protein
- Ubiquitin-conjugating enzyme E2 A
- RNA-binding protein 25
Sequence:
MVMYARKQQRLSDGCHDRRGDSQPYQALKYSSKSHPSSGDHRHEKMRDAGDPSPPNKMLRRSDSPENKYSDSTGHSKAKNVHTHRVRERDGGTSYSPQENSHNHSALHSSNSHSSNPSNNPSKTSDAPYDSADDWSEHISSSGKKYYYNCRTEVSQWEKPKEWLEREQRQKEANKMAVNSFPKDRDYRREVMQATATSGFASGMEDKHSSDASSLLPQNILSQTSRHNDRDYRLPRAETHSSSTPVQHPIKPVVHPTATPSTVPSSPFTLQSDHQPKKSFDANGASTLSKLPTPTSSVPAQKTERKESTSGDKPVSHSCTTPSTSSASGLNPTSAPPTSASAVPVSPVPQSPIPPLLQDPNLLRQLLPALQATLQLNNSNVDISKINEVLTAAVTQASLQSIIHKFLTAGPSAFNITSLISQAAQLSTQAQPSNQSPMSLTSDASSPRSYVSPRISTPQTNTVPIKPLISTPPVSSQPKVSTPVVKQGPVSQSATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNASNATVVPQNSSARSTCSLTPALAAHFSENLIKHVQGWPADHAEKQASRLREEAHNMGTIHMSEICTELKNLRSLVRVCEIQATLREQRILFLRQQIKELEKLKNQNSFMV