wanglab/gogpt-training-data huggingface dataset:
Protein: RRM domain-containing protein (Q7JMB8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNASSAPQQQQQQQQPQQGQAPQQQQQGPPQHQYQQQRPFHGRVQNHMRGSGPFGNSNGYGRYTAPRGDQQHHDSTPLSSTNLYIRGLMPNTNDDLLREMCSKYGNIASTKAIMDKATNNCKGYGFVDFESPQAAAAAVDGLNTEGVQAQMAKLQQQEQDPTNLYIANLPLDFTEQMLETELNKFGMVISTRILRTPDNQSRGVGFARMDSKEKCEVIISALNGGRFDTMSKEGPALLIKQADTGRKSKHSMNNPEMLQRMQYPQVYQSYYGYHPAAVYQQHYDVNSLASQMGGMHVGGGNPQANGGGDMYGAHMYGQNAGGQGGQGVGQGGQGGNQQFYNPNNGRNKKYFQPMNPQ
Protein: Anti-sigma-B factor antagonist (Anti-anti-sigma-B factor) (Q9WVX8)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B (By similarity).
Interaction partners:
- Anti-sigma factor
- Anti-sigma factor
- Regulatory protein
- protein-serine/threonine phosphatase
- protein-serine/threonine phosphatase
- protein-serine/threonine phosphatase
- protein-serine/threonine phosphatase
- PPM-type phosphatase domain-containing protein
- protein-serine/threonine phosphatase
- SpoIIE family protein phosphatase
Sequence:
MDLSLSTRTVGDRTVVEVGGEIDVYTAPKLREQLVELVNDGSFHLVVDMEGVDFLDSTGLGVLVGGLKRVRAHEGSLRLVCNQERILKIFRITGLTKVFPIHTSVEEAVAATD
Protein: Phosphatidylinositol-3-phosphatase (PI3P phosphatase) (EC 3.1.3.64) (Acid phosphatase SapM) (EC 3.1.3.2) (Secreted acid phosphatase) (O53361)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Virulence factor that plays an important role in blocking phagosome-lysosome fusion and thus participates in the intracellular survival of the pathogen. Acts as a phosphatase that dephosphorylates phosphatidylinositol 3-phosphate (PI3P), a membrane trafficking regulatory lipid essential for phagosomal acquisition of lysosomal constituents. Therefore, SapM eliminates PI3P from the phagosomal membrane by catalyzing its hydrolysis, and thus contributes to inhibition of phagosome maturation. Also interferes with autophagy: SapM blocks autophagosome-lysosome fusion in macrophages by binding to the small GTPase RAB7, which prevents RAB7 from being involved in this process and thus negatively regulates autophagy flux. In vitro, displays phosphatase activity with broad specificity; can dephosphorylate a variety of phosphoester substrates, with the highest activity against phosphoenolpyruvate, glycerophosphate, GTP, NADPH, phosphotyrosine and trehalose-6-phosphate. In contrast, the enzyme exhibits poor activity against glucose-6-phosphate, phosphothreonine, and a number of nucleotides (NADP, ATP, AMP, and GMP).
Subcellular location: Secreted {ECO:0000269|PubMed:11073936, ECO:0000269|PubMed:15753315}. Host cytoplasmic vesicle, host phagosome {ECO:0000305|PubMed:15753315}. Note=It remains to be determined how SapM, once secreted into the phagosomal lumen, gains access to PI3P within the cytofacial membrane leaflet. It is possible that SapM is exported to the cytosolic side, or alternatively there may be a mechanism for PI3P presentation to SapM remaining on the luminal side. {ECO:0000305|PubMed:15753315}.
Interaction partners:
- Phospholipase C A
- Phospholipase C C
- Phospholipase C D
- Phospholipase C B
- Triple specificity protein phosphatase PtpB
- Low molecular weight protein-tyrosine phosphatase A
- Conserved protein
- Uracil phosphoribosyltransferase
Sequence:
MLRGIQALSRPLTRVYRALAVIGVLAASLLASWVGAVPQVGLAASALPTFAHVVIVVEENRSQAAIIGNKSAPFINSLAANGAMMAQAFAETHPSEPNYLALFAGNTFGLTKNTCPVNGGALPNLGSELLSAGYTFMGFAEDLPAVGSTVCSAGKYARKHVPWVNFSNVPTTLSVPFSAFPKPQNYPGLPTVSFVIPNADNDMHDGSIAQGDAWLNRHLSAYANWAKTNNSLLVVTWDEDDGSSRNQIPTVFYGAHVRPGTYNETISHYNVLSTLEQIYGLPKTGYATNAPPITDIWGD
Protein: ATPase MORC2A (EC 3.6.1.-) (MORC family CW-type zinc finger protein 2A) (Zinc finger CW-type coiled-coil domain protein 1) (Q69ZX6)
Organism: Mus musculus (Mouse)
Function: Essential for epigenetic silencing by the HUSH complex. Recruited by HUSH to target site in heterochromatin, the ATPase activity and homodimerization are critical for HUSH-mediated silencing (By similarity). Represses germ cell-related genes and L1 retrotransposons in collaboration with SETDB1 and the HUSH complex, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression. During DNA damage response, regulates chromatin remodeling through ATP hydrolysis (By similarity). During DNA damage response, may regulate chromatin remodeling through ATP hydrolysis (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:29728365}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y6X9}. Chromosome {ECO:0000250|UniProtKB:Q9Y6X9}. Nucleus matrix {ECO:0000250|UniProtKB:Q9Y6X9}. Note=Mainly located in the nucleus. Upon phosphorylation at Ser-737, recruited to damaged chromatin. {ECO:0000250|UniProtKB:Q9Y6X9}.
Interaction partners:
Sequence:
MAFTNYSSLNRAQLTFEYLHTNSTTHEFLFGALAELVDNARDADATRIDIYAERREDLRGGFMLCFLDDGAGMDPSDAASVIQFGKSAKRTPESTQIGQYGNGLKSGSMRIGKDFILFTKKEDTMTCLFLSRTFHEEEGIDEVIVPLPTWNARTREPITDNVEKFAIETELVYKYSPFHTEEQVMNQFMKIPGNSGTLVIIFNLKLMDNGEPELDIISNPKDIQMAETSPEGTKPERRSFRAYAAVLYIDPRMRIFIHGHKVQTKRLSCCLYKPRMYKYTSSRFKTRAEQEVKKAEHVARIAEEKAREAESKARTLEVRMGGDLTRDSRVMLRQVQNTAITLRREADVKKRIKDAKQRALKEPKELNFVFGVNIEHRDLDGMFIYNCSRLIKMYEKVGPQLEGGMACGGVVGVVDVPYLVLEPTHNKQDFADAKEYRHLLRAMGEHLAQYWKDIAIAQRGIIKFWDEFGYLSANWNQPPSSELRFKRRRAMEIPTTIQCDLCLKWRTLPFQLSSVETDYPDTWVCSMNPDPEQDRCEASEQKQKVPLGTLKKDPKTQEEKQKQLTEKIRQQQEKLEALQKTTPIRSQADLKKLPLEVTTRPIEEPVRRPQRPRSPPLPAVIKNAPSRPPSIQTPRPSTQLRKTSVISLPKPPTTAARGETSTSRLLQPTEAPRKPANPPIKTVPRPTPPVHTPPLSLIPSSKSLREVPAQKAIKTPVVKKPEPPVKQSVATSGRKRSLAVSDEEEAEEEAEKRRERCKRGKLAVKEEKKEANELSDSAGEDHPAELRKAQKDKGLHVEVRVNREWYTGRVTAVEVGKNAVRWKVKFDYVPTDTTPRDRWVEKGSEDVRLMKPPSPEHQSPDTQQEGGEEEEAMVARQAVALPEPSTSDGLPIEPDTTATSPSHETIDLLVQILRNCLRYFLPPSFPISKKELSVMNSEELISFPLKEYFKQYEVGLQNLCHSYQSRADSRAKASEESLRTSEKKLRETEEKLQKLRTNIVALLQKVQEDIDINTDDELDAYIEDLITKGD
Protein: Spectrin alpha chain (G4S034)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MADSNDTHAPPEPVLEVPPPQEIRILETADDIHQRRQEVLGHYSIFKDHSQTKRDRLEEARQFQYFKRDADELNVWILEKLQTAQEENFRDPSNLQAKIQKHEAFEAEVQAHAKTIANLDKTGNAMIQHNHFASEHIKKRLEELHALWDKLFFKLKDKGIKLQQALKLLHFIRQCDEILYWIREKETYVTAEDMGMDLEHVEILQRKFDDFLKELGNHQYRINEINQAADKLVEEGHSEHDQIYKKRDDVNDAWHRLNTLAATRKEGLFGAHQVQRFNRDADETLAWIGEKDLALSSDDYGRDLNNVQALQRKHEGTERDLAALEGKMLQLEKEAHKLAETHPDRAEAIHQKNDDTKAAWNALKEKAQHRKDGLERSFQLHRFLADYRDLISWIGDMKAVIGADELAKDVAGAEALLESHQEHKGEIDARADSFNQTASAGQKLVEMGIPESPEVQEKLEKLDHEKSSLLGLWEERRILYEQCMDLQLFYRDTEQAETWMNKQEAFLANTDLGDSLDSVEHLIKKHEDFEKSLAAQEEKINALDEFATKLIQGQHYAADDVAERRQALLDRRRRLLDRARQRGNALKESYKRQTFDRDCDEMVSWITEKLSTARDDSYLDPTNIRGKLQKHINFEQELKANENRLDDIRSTGEQIIDSGHFAADHIGDRLRQVNNLWNELVDATNKKGAKLREAGNEQQFNRNIEDVEAWLSELEGQVASEDYGKDLVSVQNLQKKIGLIESDFNAHNDRVDGIKQLAQQFQEEEHFNAPVIVRKQENLQQRYNALRDPLEKRKRKLGESHQGNQLFRDIEDELAWIREKEQVAGSTNRGRDLIGVQNLIKKQQALIAEIANHDSQIESVSSAANDMIQQGHFLAPEIRDKLAQLRDNWRILKSKAEKRRTDLDDSLQAHQYLSDANEADAWMSEKEPIVGSTDYGKDEDSAEALLKKHRALLSDLEAFKGTIEDLRKQASQCKYQEQPMGQLGRDCVLALYDYQEKSPREVSMKKGDVLTLLNASNRDWWKVEVNDRQGFVPAAYVKRIEPGTAQQHAQQQVNSIGGKQSEIEDKYQRLMMLGETRKRKLEEACKGYQLLREANDLAEWIKSREAVAAQQEIGTDLEQVEVLQKKFDDFKGDLKANEVRLQEMNQIATALTSVGQTETAVRIRQQIEDLNARWRALEEQTEQREQQLGSAHEVQRFHRDVDETRDWIQEKDDALDSEDFGRDLRSVQALQRKHEGVERDLAALGDKIKSLDEKANRLRQSHPEAAEQIYDLQRELNEQWNRLTSKANNRKEKLLDSYDYQRFLSDYRDLMQWIASMNQLVSSQELANDVTGAEALLERHQEYRTEIDSRAATFQAFDQFGNQLLNSHHYAAGDIENRLQGVNEARKGLEDAWVARRNILDQCLELQLFYRDCEQADTWMSAREAFLAQEDPSGDNVESLIKKHEDFDKAINTQEEKIKGLKLFAESLIKNNHYDSPAVTRKRDQILDRWNGLKEALIQKRFKLGESQTLQQFSRDADEIENWMTEKFQIAQEENYRDPTNIQQKHQKQQAFEAELHANSDRIAAIIQAGNNLIENAKCGGGEAAVSARLKALNDQWDLLVKTTTEKSYRLKEANKQKSFMAAVKDLEFWLGEVEILLQSEDYGKDLASVENLLKKHSLLEADIVAHQDRVGEMNEQADSLLENDQFQGQQIAERRKLIADRYDGVKKMATDRRDKLSKALNVHQFFRDIDDEESWIKEKKLLVSSDDYGRDLPGVQNLRRKHRRIDTELASHEPQVSLVKLKGEELLRSAAEAGVGEDQIKKRMEDLEQSWGQIRDLTGNRHQRLDESEAFQAFLGDVEEEEAWMNEKQQILGSDNFGENMAGVQGLLKKHDTFQVDLELHKQRVADLINKGDTLIHNGNHHAPHIKQRCDQLRARLIEIESMAEGRLAKLRDNSAYLQFMWKCDVVESWIAEKEQQVRSEDFGRDLSSVQILLTKQEAFDAGLNAFEHEGIQRITELKDQLVSSEHQQSPAIEKRHTNVIQRWQNLLAHSEARRQKLLKMQQQFKQIEELYLAFAKKASTFNSWFENAEEDLTDPVRCNSLEEIRALRDAHGEFQRSLSSAEEDFRQLQDLDRRIKSFNVGPNPYTWFTMDALEDTWRNLQRIIKEREQELAREHQRQEENDKLRREFAKLANAFHAWLTNTRQEMMEAGGTLEEQLDAVERKAKEIKANKGQLRQIEEKGAMLERNLILDNRYTEHSTVGIAQAWDQLDQLAMRMQHNLEQQIQARNQSGVSEEALREFSMMFKHFDKEKTGRLDHQQFKSCLRALGYDLPMVDEGQPEPEFQRILDIVDPNRDGYVTLQEYMAFMISKETENIQSSEEIEMAFRALSKEFRPYVTAEELYANLTPEQAEFCIRRMKPYMDAISGRSIQGGLDYEQFVHALFQS
Protein: Monocarboxylate transporter 10 (MCT 10) (Aromatic amino acid transporter 1) (Solute carrier family 16 member 10) (T-type amino acid transporter 1) (Q91Y77)
Organism: Rattus norvegicus (Rat)
Function: Sodium- and proton-independent thyroid hormones and aromatic acids transporter. Mediates both uptake and efflux of 3,5,3'-triiodothyronine (T3) and 3,5,3',5'-tetraiodothyronine (T4) with high affinity, suggesting a role in the homeostasis of thyroid hormone levels (By similarity). Responsible for low affinity bidirectional transport of the aromatic amino acids, such as phenylalanine, tyrosine, tryptophan and L-3,4-dihydroxyphenylalanine (L-dopa). Plays an important role in homeostasis of aromatic amino acids (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8TF71}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:11278508}; Multi-pass membrane protein {ECO:0000255}. Note=In the epithelial cells is detected in the basolateral membrane but not in the apical membrane.
Interaction partners:
- Monocarboxylate transporter 8
- Solute carrier organic anion transporter family member 1C1
- Large neutral amino acids transporter small subunit 2
Sequence:
MVPSQEEPAAAERETNEAQPPGPAPSDDAPLPVPGPSDVSDGSVEKVEVELTRSTGNQEPPEPPEGGWGWLVMLAAMWCNGSVFGIQNAYGVLFVSMLETFGAKDDDNMAFKAAWVGSLSMGMIFFCCPIVSVFTDMFGCRRTAVLGAAVGFVGLMSSSFVSSIEPLYFTYGVVFACGCSFAYQPSLVILGHYFKKRLGLVNGIVTAGSSVFTILLPLLLGNLTSTVGLCYTLRILCIFMFVLFLAGFTYRPLVPSSKEKESEDSRSSFFSRRKLSPPKKIFNFALFKETAYAVWAAGIPLALFGYFVPYVHLMNHVKERFKDVNNKEVLFMCIGVTSGVGRLLFGRIADYLPGVKKVYLQVLSFFFIGLTSMMIPLCSVFGALIALCLIMGLFDGCFISIMAPIAFELVGPQDASQAIGFLLGFMSIPMTVGPPVAGLLHDKLGSYDLAFYLAGIPPFIGGAVLCLIPWIHSKKQREISKNTGGEKMEKMLANQSSLLSSSSGIFKKESDSII
Protein: Stearoyl-CoA desaturase (EC 1.14.19.1) (Acyl-CoA desaturase) (Delta(9)-desaturase) (Delta-9 desaturase) (Fatty acid desaturase) (Q9TT94)
Organism: Bos taurus (Bovine)
Function: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (By similarity). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P13516}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Elongation of very long chain fatty acids protein 6
- Fatty acid synthase S-acetyltransferase; [Acyl-carrier-protein] S-malonyltransferase; 3-oxoacyl-[acyl-carrier-protein] synthase; 3-oxoacyl-[acyl-carrier-protein] reductase; 3-hydroxyacyl-[acyl-carrier-protein] dehydratase; Enoyl-[acyl-carrier-protein] reductase; Acyl-[acyl-carrier-protein] hydrolase]
- Very-long-chain 3-oxoacyl-CoA reductase
- Acetyl-CoA carboxylase 1
- Very-long-chain
- Very-long-chain enoyl-CoA reductase
- 17beta-estradiol 17-dehydrogenase
- Very-long-chain
- Stearoyl-CoA desaturase 5
- Very-long-chain
Sequence:
MPAHLLQEEISSSYTTTTTITAPPSRVLQNGGGKLEKTPLYLEEDIRPEMRDDIYDPTYQDKEGPKPKLEYVWRNIILMSLLHLGALYGITLIPTCKIYTYIWVLFYYLMGALGITAGAHRLWSHRTYKARLPLRVFLIIGNTMAFQNDVFEWSRDHRAHHKFSETDADPHNSRRGFFFSHVGWLLVRKHPAVKEKGSTLNLSDLRAEKLVMFQRRYYKPGVLLLCFILPTLVPWYLWDETFQNSLFFATLFRYALGLNVTWLVNSAAHMYGYRPYDKTINPRENILVSLGAAGEGFHNYHHTFPYDYSASEYRWHINFTTFFIDCMAAIGLAYDRKKVSKAAILARIKRTGEESYKSG
Protein: Deoxycytidine kinase (dCK) (EC 2.7.1.74) (Deoxyadenosine kinase) (EC 2.7.1.76) (Deoxyguanosine kinase) (EC 2.7.1.113) (P43346)
Organism: Mus musculus (Mouse)
Function: Phosphorylates the deoxyribonucleosides deoxycytidine, deoxyguanosine and deoxyadenosine.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P27707}.
Interaction partners:
- Cytidine deaminase
- Deoxycytidylate deaminase
- UMP-CMP kinase
- Cytosolic purine 5'-nucleotidase
- Cytosolic 5'-nucleotidase 1A
- Adenosine deaminase
- Adenine phosphoribosyltransferase
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
- 5'
Sequence:
MATPPKRFCPSPSTSSEGTRIKKISIEGNIAAGKSTFVNILKQASEDWEVVPEPVARWCNVQSTQEEFEELTTSQKSGGNVLQMMYEKPERWSFTFQSYACLSRIRAQLASLNGKLKDAEKPVLFFERSVYSDRYIFASNLYESDCMNETEWTIYQDWHDWMNSQFGQSLELDGIIYLRATPEKCLNRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTSFDYLQEVPVLTLDVNEDFKDKHESLVEKVKEFLSTL
Protein: Regulator of microtubule dynamics protein 1 (Protein FAM82B) (Q54XR4)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSSAQKIVDKVDQLHLEREFVKISELLTEGHKQYPEDVEIMWRLARSYFDKNEEVANKDEKKKLIEQALELTNKASTINPNHWAVHKWLAILISALGDHISSKEKIANAFKIKDHAVKANELKPNDATTLHLLGRWCFSISSIGWIERTAASALFGTPPTSTYDEALTYFLEAYKCDPTNIRNALFTGDTYAALKDNAKAKEFYKIAAAIEPKSEFDKNLVKEAQNKAK
Protein: N-terminal acetyltransferase A complex subunit-like protein C418.02 (NatA complex subunit-like protein C418.02) (Q9Y7X2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Non-catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- N-terminal acetyltransferase A complex catalytic subunit ard1
- Uncharacterized N-acetyltransferase C663.13c
- N-terminal acetyltransferase B complex subunit arm1
- N-terminal acetyltransferase B complex catalytic subunit naa20
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 30
- Pre-mRNA-splicing factor cwf24
- N-terminal acetyltransferase A complex subunit nat1
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
Sequence:
MSKLSEKEAFLFDRSIDQFEKGQYSKSLKTIQSVLKKKPKHPDSVALLGLNLCKLHDSRSALLKCGYASSIDPKSQFCWHALAIVYRETKDYNNSLKCYQNALAISPNNESLWYDAAYLQAQLGLYQPLFDNWNRLLQLDSSNLEYRLCFTLSAFLSGNYKESLEQIQYLISSCNLSPLVVSRLISFLPRICEHIENGSQTVLEILLMNQNSFLNNFNFEHIKADFAFRQKNYEESIYLYARLLIKFPNRLDYSEKYLNSLWNFYKSGGLALDLLLKRTDSLIKTFSEILQTGISVLIFLLSKNLDYDFCLNHLISYSMHHFIPSFISLLKIPLKTNDAFSKKLITMLSNFREGDSAKNIPTHKLWCTYCLCLAHYKLGDYEESNYWLNLAIDHTPTYPELFLAKAKIFLCMGEIEEALCSFKRSVELDKSDRALASKYAKYLIRMDRNEEAYIVLSKFSRFRFGGVCNYLAETECVWFLVEDGESLLRQKLYGLALKRFHSIYQIYKKWSFLKFDYFTQCAEDGEFQEYVELVEWSDNLWSSTDYLRATLGALTIYLLLFESKFNMYGNKAEEISHMSEVEQIAYAREDNKKIMKLQKIEEDKIKSYIPSESEEPLVIDEDYFGHKLLITDDPLTEAMRFLQPICWHKIKGWGFLKILSSKLYKLKGIIFCYYALTNNIEGLHQKANSLETSVL
Protein: Integrin beta 2 alpha subunit (Q9JI30)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MTLKVLLATVLTLCHGFNLDTENPMTFQENASGFGQSVIQLGETRVVVAAPQEVKAVNQTGALYQCDYSTNRCDPIPLQVPPEAVNMSLGLSLAATTVPPQLLACGPTVHQNCKENTYVNGLCYLFGSNLLRKPQQFPEALRGCPQQESNIAFLIDGSGSINTIDFQKMKEFVSTVMDQFQKSKTLFSLMQYSDEFRTHFTFNDFKRNPDPKSHVRPIRQLNGRTKTASGIRKVVRELFQKINGARDNAAKILVVITDGEKFGDPLNYEDVIPEAEEAGIIRYVIGVGNAFHKPQSRRELDTIASKPAGDHVFQVDNFEALNTIRNQLQEKIFAIEGTQTGSTSSFEHEMSQEGFSAAITSNGPLLGSVGSFDWAGGAFLYPSKDKASFINTTRIDSDMNDAYLGYASAVISRNRVQSLVLGAPRYQHIGLVVMFKQNFGAWEPHTDIKGSQIGSYFGASLCSVDMDADGNTNLILIGAPHHYEKTRGGQVSVCPLPRGRARWQCEAILHGDQGHPWGRFGAALTVLGDVNGDKLTDVAIGAPGEQENQGAVYIFHGASVASISTPHSQRIAGARFSPGLQYFGQSLSGGKDLTMDGLMDLAVGAQGRLLLIRAQPVLRLEATMEFSPKNLARSVFACQEEVVKNKDAGEVRVCLQVRKNTKDRLREGDIQSTVTYDLALDPGRSVVRAFFDETKNGILRRIRVFGLTQKCETLKLILPDCVDNSVSPIILRLNYTLVGEPLRSSRDLRPVLAMEAQRIFTAMFPFEKNCGNDTICQDDLSITVSSTRVNTLVVGDSRDFDVSVTLRNDGEDSYGTKVTCYYPSGLSYRKVSASQNQFSKKPWRVIAEPSSSEGQGVLKSTIWDINHPIFPANSEVTFNVTFDVDSDASLGNKLLLKVVVTSENNVSRTDKTESQLELPVKYAIYMVVTSGESSIKYLNFTASEMTSKVIQHQYQFNNLGQRSFPVSVVFWIPVQINKVTIWDPPQVTFSQNLSSVCRTEQKSPSHSKFQDELERTPVLNCSVAVCKRIQCDIPSFNSKEIFNVTLQGNLLFDWYIETSHDHLLLVSTAEILFNDSAFALLPGQETFVKAQTETKVEPYTVHNPVPLIVGSSVGGLVLLALITAGLYKLGFFKRQYKDMMNEAGGQDGPPQ
Protein: Myocyte enhancer factor 2C (A0A0D9SGF3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MISRQRLCAVPPPNFEMPVSIPVSSHNSLVYSNPVSSLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNMQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGLNIKSEPVSPPRDRTTTPSRYPQHTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT
Protein: ACP53C14C (Q6GUV0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKSKQVFYIAFSLLLLGSLLPNEVESLRVDLNKLAECTESGLKVATTLLVRAIPCVKKLAKCADFRAIKTKDLDITALTLLGYQYLQTVVNNQRCLLISLKDGYDAVSPHLDKLISGKCLPGLS
Protein: Repressor activator protein 1 (Q387L4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTDVDGGSGASWKRLRFFVCADTLLTFQPVDSSHLEGRPGQPEQRYLLVDGEYRPITSYPTSSLFLETLKLAGSTVVVIAPWKRAKTKKLLSLFGWTAFDEIRSIHPEPGRDKLHLACIGCSADEYSTSVIVATSRADWSPSMYPQLVEVKHGVNQVPHSLALLRALSSCLRLAEWQVRLPHVPISSCATLCRSRLFSHCRFFLEPVVSEDATVALSINEHGGYIVTRREDATHCVVSGSLPNLPGDISNLPPGGCAAKAVKECSVLPTSAEGRSAEPKSAKVDTDSVSLVKNEVDESDDSIKDEFSYSAGNAATAMVECGDEGVWNEENADDEDPVTMIPPGTFSEDDEDDAPGGLEEADGETVTTVTTQWLKDCAEGLFMYPPQVSHTSKDGSDWNITGLLLATILPTSDAEPLLLSSFNTFAERSGFEPLQLNSADEGGLAEVMQRQWGGVLCMEEKDGDFLLSQTNIYTEAFSDEMDKHLTFVANRFCEAWKDAVQRRRALLGSDAGTQTTVSITVTFGTNTEVEVAPSVQPPPPPPPAPQPTTASAAANEGSKESATPALPFLMRALGPAEWAKEVEAPRSPPPSAVPDIPLKQDPVPSGEGVATAENSVGNDQKESTSRQVAGDAGDTANVAEATEEIAALDQPFEKCFIPTEALGSDREGLDRTQLERQLPFRNYPIKLNVSKSGIFCQFPTVSDAKRFYEEGTVEILNRSLPIKPVFEKRNETVAPAERKRRRSVSPGGVHPQTAAVSALSRRGIQGATYARTQRSRTDNGWKAEGDRNPFVLTEEENSLLTSLGITYTYALENVPLLEHYAQKDLSSKVYRKEKGVLVKMLEKLKAVKGTTSKAPQ
Protein: U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2-like (CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 1) (SP2) (U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1) (U2(RNU2) small nuclear RNA auxiliary factor 1-like 1) (Q64707)
Organism: Mus musculus (Mouse)
Function: Plays a role in splicing of the U12-type introns. Implicated also in removal of U2 introns positioned adjacent to a U12 intron.
Subcellular location: Nucleus.
Interaction partners:
- Splicing factor 3B subunit 1
- Splicing factor U2AF 65 kDa subunit
- RNA-binding region-containing protein 3
- Small nuclear ribonucleoprotein E
- COMM domain-containing protein 1
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 6
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D3
Sequence:
MASRQTAIPEKLSRKQYKAAMKKEKRKKRRQKMARLRALEAPPEEDDDVSANEELAERLLEIERQRLHEEWLLREEKAQEEFRIKKKKEEAARKQKEEQERQIKAEWEEQQKKQREEEEQKLQEKREREEAVQKMLDQAENERIWQNPEPPKDLRLEKYRPSCPFYNKTGACRFGNRCSRKHDFPTSSPTLLVKSMFTTFGMEQCRRDDYDSDANLEYSEEETYQQFLDFYHDVLPEFKNVGKVIQFKVSCNLEPHLRGNVYVQYQSEEECQAALSLFNGRWYAGRQLQCEFCPVTRWKVAICGLFEMQKCPKGKHCNFLHVFRNPNNEFREANRDIYMSPPAWTGSSGKNSDRRERKDHHEEYYSKSRSYHSGSYHSSKRNRESERKSPHRWKKSHKQTTKSHERHSSRRGREEDSSPGPQSQSHRT
Protein: Integral membrane transport protein (Q382V4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MGCLSFGSISEVVGWSFFDIQLANALIGIGTSVAVPIVTMVGREIGYEQGKIASYVSLINAFHVIADIPSSLVADCVDLRRLMSFSVFAQAAGCMPVVLLGCTSTSLAAFCVINGFSTGAFFLARHIYVARRLNPDHCGMVMAFLSGLLRLAHMLGPIFLGVIASLWGDTRYFFFVPMGASLLAWCCIQFSPYCLRVGRNAPQGRADATTATQLEEAKKLDEGSVGGETVPILPGDSLIKGPVLEEGLTRRVVSYGAVNTLNTDNAHSNVESVVSEVGIACSHECCSLQIEGSKGGTAPATYCSVIMDQWNVIWRLGIYVILFVALRANRKLLLTFAAMRMGFTDVQLSFLLSLSFSFDAFLFPLGGILLDNCSRRFARLPAVLGLGIAFLLLPLQHSGQWLYVMAAVFGVVDALGCGLIMTLVADYRHQYFGGLFFGIMRTVQDMGHVISSAAVSLMIHRFDFAICSNFWGVLGIFAAVWGWYGVPNPTR
Protein: Bud site selection protein 7 (Q08754)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Member of the CHS5-ARF1P-binding proteins (CHAPS) which mediates export of specific cargo proteins, including chitin synthase CHS3. May be involved in positioning the proximal bud pole signal.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16498409, ECO:0000269|PubMed:17000877}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16498409, ECO:0000269|PubMed:17000877}. Note=Trans-Golgi network location requires interaction with CHS5 and with myristoylated GTP-bound ARF1 for the recruitment to the membranes.
Interaction partners:
- Chitin biosynthesis protein CHS5
- Chitin biosynthesis protein CHS6
- Protein BCH1
- Protein BCH2
- ADP-ribosylation factor 1
- Chitin synthase 3
- Bud site selection protein 9
- [PSI+] induction protein 2
- Putative uncharacterized protein YOR300W
Sequence:
MITQNSIPEVKEDFIGYALHERRIRLPQFQDLGPADLVTLTKYLPTSSNTNAINSTSRNGAAIIQSPAAVVADDSAASMATNGDASDTAVTTNYTNASIYSSSRNANDGAPMVAELHPLDKLKDEVGTFFYSMGVDTSGPTSIAIFLKEISEVISEKPQVWFGRKKTFNVARISFSTWNAFRRCDINVVVHIPGSIQNFIVDCNGESQNIEMCADYDLIWAETFVSGVVRSIMLMKENAEEGELQNLVETLILNPFTAGQIDDVPEMFIDLFPIVYHKGPLLGAPYYITNVTNTNNYLVETLVEIVKLTRNVSRAEIMLKNLATDNPEAIIILIKIFLVCDQELDAIKLTYDMLSQDKIINNTNNRMDYKSELLCLQAQFLIDKRQDYSLAQNIAQEAVNCSPSEFRPWYLLSKVYVKLNDIENALLILNSCPMSPLKEKYVLKRVAPLPSNNSLHLPLPIDVVLDEVTSLNPQDVQNEHRSADPMLVNLAASNLKSTFQLAYRLLTEIVQITGWENLLKYRSNIFVMEEEYQKSSSSLPKDVNKQEEQPLRAKRLCERWLDNLFMLLYEDLKMYTLWQTEQLYMDAQNNNHNKLTFEWELFGLCARRLGHFPEAAKAFQNGLSQRFSSRCARKLLEYCINERQRVKNFINSPNSHDMVPEIVSSRIRELDNSIIDLCVKICCWNHRWYTEFSISLLDCLSVVIQDMSLTKVSNEISSRYPETVLNLVQENLLNFFTTCTIGCYDA