wanglab/gogpt-training-data huggingface dataset:
Protein: LIM domain and actin-binding protein 1 (Epithelial protein lost in neoplasm) (Q9UHB6)
Organism: Homo sapiens (Human)
Function: Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments. Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity).
Subcellular location: Cytoplasm. Cell junction, focal adhesion {ECO:0000269|PubMed:10618726, ECO:0000269|PubMed:24694988}. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:10618726}. Cell membrane {ECO:0000250|UniProtKB:Q9ERG0}. Cell projection, ruffle {ECO:0000269|PubMed:32496561}. Note=Expressed in the brush border membrane of the small intestine and colocalizes with NPC1L1 and MYO5B (PubMed:29880681). Colocalizes with PXN at focal adhesions in mesangial cells (PubMed:24694988). Colocalizes with actin stress fibers in quiescent cells. PDGF stimulation induced disassembly of stress fibers and formation of peripheral and dorsal ruffles, where LIMA1 is relocalized (By similarity). {ECO:0000250|UniProtKB:Q9ERG0, ECO:0000269|PubMed:24694988, ECO:0000269|PubMed:29880681}.
Interaction partners:
- Catenin beta-1
- Catenin delta-1
- Cadherin-1
- Catenin alpha-1
- Vinculin
- Cadherin-17
Sequence:
MESSPFNRRQWTSLSLRVTAKELSLVNKNKSSAIVEIFSKYQKAAEETNMEKKRSNTENLSQHFRKGTLTVLKKKWENPGLGAESHTDSLRNSSTEIRHRADHPPAEVTSHAASGAKADQEEQIHPRSRLRSPPEALVQGRYPHIKDGEDLKDHSTESKKMENCLGESRHEVEKSEISENTDASGKIEKYNVPLNRLKMMFEKGEPTQTKILRAQSRSASGRKISENSYSLDDLEIGPGQLSSSTFDSEKNESRRNLELPRLSETSIKDRMAKYQAAVSKQSSSTNYTNELKASGGEIKIHKMEQKENVPPGPEVCITHQEGEKISANENSLAVRSTPAEDDSRDSQVKSEVQQPVHPKPLSPDSRASSLSESSPPKAMKKFQAPARETCVECQKTVYPMERLLANQQVFHISCFRCSYCNNKLSLGTYASLHGRIYCKPHFNQLFKSKGNYDEGFGHRPHKDLWASKNENEEILERPAQLANARETPHSPGVEDAPIAKVGVLAASMEAKASSQQEKEDKPAETKKLRIAWPPPTELGSSGSALEEGIKMSKPKWPPEDEISKPEVPEDVDLDLKKLRRSSSLKERSRPFTVAASFQSTSVKSPKTVSPPIRKGWSMSEQSEESVGGRVAERKQVENAKASKKNGNVGKTTWQNKESKGETGKRSKEGHSLEMENENLVENGADSDEDDNSFLKQQSPQEPKSLNWSSFVDNTFAEEFTTQNQKSQDVELWEGEVVKELSVEEQIKRNRYYDEDEDEE
Protein: Mitochondrial basic amino acids transporter (Carnitine/acylcarnitine translocase-like) (CACT-like) (Mitochondrial carnitine/acylcarnitine carrier protein CACL) (Mitochondrial ornithine transporter 3) (Solute carrier family 25 member 29) (Q8BL03)
Organism: Mus musculus (Mouse)
Function: Mitochondrial transporter of arginine, lysine, homoarginine, methylarginine (By similarity). Transports with a much lesser extent, ornithine and histidine. Does not transport carnitine nor acylcarnitines. Functions by both counter-exchange and uniport mechanisms. Plays a physiolocical role in the import of basic amino acids into mitochondria for mitochondrial protein synthesis and amino acid degradation (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:12882971, ECO:0000269|PubMed:19287344}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial carnitine/acylcarnitine carrier protein
Sequence:
MALDFLAGCAGGVAGVIVGHPFDIVKVRLQVQSTEKPQYRGTLHCFQSIIKQESVLGLYKGLGSPLMGLTFINALVFGVQGNTLRALGQDSPLNQFLAGAAAGAIQCVICCPMELAKTRLQLQAVGPARTYKGSLDCLVQIYRHEGLRGINRGMVSTLLRETPSFGVYFLTYDVMTRAMGCEPGDRLLVPKLLLAGGTSGITSWLSTYPMDVVKSRLQADGLQGTPRYRGIVDCMRQSYQAEGWQVFTRGLASTLLRAFPVNAATFATVTVVLTYTRGEEAQVDSEAALGTSPTPAGSALAQPSSL
Protein: Single-strand DNA-binding protein (63.5 kDa virulence protein) (P08062)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Involved in DNA transformation; mediates the nuclear uptake of single-stranded DNA copies of the transferred DNA (T-DNA) element. Binds single-stranded but not double-stranded DNA regardless of nucleotide sequence composition.
Subcellular location: Secreted {ECO:0000269|PubMed:1615325}. Host nucleus {ECO:0000250}. Note=In infected cells, it is found in the nucleus.
Interaction partners:
Sequence:
MDPKAEGNGENITETAAGNVETSDFVNLKRQKREGVNSTGMSEIDMTGSQETPEHNMHGSPTHTDDLGPRLDADMLDSQSSHVSSSAQGNRSEVENELSNLFAKMALPGHDRRTDEYILVRQTGQDKFAGTTKCNLDHLPTKAEFNASCRLYRDGVGNYYPPPLAFERIDIPEQLAAQLHNLEPREQSKQCFQYKLEVWNRAHAEMGITGTDIFYQTDKNIKLDRNYKLRPEDRYIQTEKYGRREIQKRYEHQFQAGSLLPDILIKTPQNDIHFSYRFAGDAYANKRFEEFERAIKTKYGSDTEIKLKSKSGIMHDSKYLESWERGSADIRFAEFAGENRAHNKQFPAATVNMGRQPDGQGGMTRDRHVSVDYLLQNLPNSPWTQALKEGKLWDRVQVLARDGNRYMSPSRLEYSDPEHFTQLMDQVGLPVSMGRQSHANSVKFEQFDRQAAVIVADGPNLREVPDLSPEKLQQLSQKDVLIADRNEKGQRTGTYTNVVEYERLMMKLPSDAAQLLAEPSDRYSRAFVRPEPALPPISDSRRTYESRPRGPTVNSL
Protein: Uncharacterized protein (Q38AL1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDALRRVGCPNSSQEHRKGNEYLGDAAVRYARRGFPDQMCFGECCADARQVLQHLQFLYQVNGVVEYGKHDYSGEGSTAFPALLSFFFLMIFFVLCFLPVWVSRRSDDRKHRAFSIWMQGKVFQFSAFGERKGCFAPLQWKLSKRRRLN
Protein: L-type lectin-domain containing receptor kinase V.4 (Arabidopsis thaliana lectin-receptor kinase c1) (AthlecRK-c1) (LecRK-V.4) (EC 2.7.11.1) (O22833)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9LSR8}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSRTIGSRVIFLILALFCCTENSRGKLVMQGSAGFFKGYRTLTSTKKHAYGQAFEDEIVPFKNSANDTVTSFSVTFFFAIAPEDKHKGAHGMAFVISPTRGITGASADQYLGIFNKANNGDSSNHVIAVELDINKDEEFGDINDNHVGININGMRSIKFAPAGYYDQEGQFKDLSLISGSLLRVTILYSQMEKQLNVTLSSPEEAYYPNKPLLSLNQDLSPYILENMYVGFSASTGSVRAMHYMLSWFVHGGVDVPNLDLGIPTFPPYPKEKSLVYRIVLVTSLALVLFVALVASALSIFFYRRHKKVKEVLEEWEIQCGPHRFAYKELFKATKGFKQLLGKGGFGQVFKGTLPGSDAEIAVKRISHDSKQGMQEFLAEISTIGRLRHQNLVRLQGYCRYKEELYLVYDFMPNGSLDKYLYHRANQEQLTWNQRFKIIKDIASALCYLHHEWVQVVIHRDIKPANVLIDHQMNARLGDFGLAKLYDQGYDPQTSRVAGTFWYIAPELIRSGRATTGTDVYAFGLFMLEVSCGRRLIERRTASDEVVLAEWTLKCWENGDILEAVNDGIRHEDNREQLELVLKLGVLCSHQAVAIRPDMSKVVQILGGDLQLPDNLLDIVKAEKVRMWSETSESVLGVLTSQGSIGTLTLTEPFTSRGR
Protein: Delta-like protein 3 (Drosophila Delta homolog 3) (Delta3) (Q9NYJ7)
Organism: Homo sapiens (Human)
Function: Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 4
- Delta-like protein 1
- Delta-like protein 4
- Serrate RNA effector molecule homolog
- Mesoderm posterior protein 2
- Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe
- Pro-epidermal growth factor
Sequence:
MVSPRMSGLLSQTVILALIFLPQTRPAGVFELQIHSFGPGPGPGAPRSPCSARLPCRLFFRVCLKPGLSEEAAESPCALGAALSARGPVYTEQPGAPAPDLPLPDGLLQVPFRDAWPGTFSFIIETWREELGDQIGGPAWSLLARVAGRRRLAAGGPWARDIQRAGAWELRFSYRARCEPPAVGTACTRLCRPRSAPSRCGPGLRPCAPLEDECEAPLVCRAGCSPEHGFCEQPGECRCLEGWTGPLCTVPVSTSSCLSPRGPSSATTGCLVPGPGPCDGNPCANGGSCSETPRSFECTCPRGFYGLRCEVSGVTCADGPCFNGGLCVGGADPDSAYICHCPPGFQGSNCEKRVDRCSLQPCRNGGLCLDLGHALRCRCRAGFAGPRCEHDLDDCAGRACANGGTCVEGGGAHRCSCALGFGGRDCRERADPCAARPCAHGGRCYAHFSGLVCACAPGYMGARCEFPVHPDGASALPAAPPGLRPGDPQRYLLPPALGLLVAAGVAGAALLLVHVRRRGHSQDAGSRLLAGTPEPSVHALPDALNNLRTQEGSGDGPSSSVDWNRPEDVDPQGIYVISAPSIYAREVATPLFPPLHTGRAGQRQHLLFPYPSSILSVK
Protein: Protein fmp32, mitochondrial (O14042)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable proline dehydrogenase, mitochondrial
- Probable delta-1-pyrroline-5-carboxylate dehydrogenase
- Putative ribosomal recycling factor
- Phosphomannomutase
Sequence:
MYLKIPCNSIYHQFQPLFRARTVHKVRSLGLNGFYRKYHGFNSLRFVRVLQEAGIDDKKSETLMRLISNVYSDMHEKISDFSVTKEQQDRVMYQQKVDFAHLRSELQSIERQEMVALHSQVEQLFSDVERLKTSFRDQLNNSTSEARLQLNIDRLNHYDETASQDLKLRELSAEIDTEMSNFRTQLASFKTQTLQWVFGIVTGSGALLLAYVRLII
Protein: Dynamin-type G domain-containing protein (G5ECC3)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Endosome membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004125}.
Interaction partners:
- FYVE-type domain-containing protein
- Amphiphysin
- Ras-related protein Rab-10
- ADP-ribosylation factor 6
- EH domain-binding protein 1
- small monomeric GTPase
- SH3 domain-containing protein
- Apoptosis-linked gene 2-interacting protein X 1
- Ras-related protein Rab-7a
- Ras-related protein rab-11.1
Sequence:
MESVNSEEHKINEAPAPPVIVINSSTKEEQEATQTDRIEGQMKKIDSVFDEQNVASLEGVNSKNEISGSVSSSSFEELNAETEDLSERSEVEKDEDLGRVVEEHKEPAQVPVESETPETSKKEIHQEEEISELEKVPETVEEEIEVVNTSVEITEVKKEVIEEVKISGLKEEETPVPKMRAQQQVPVAADRPIRRLSIARASMMTPKASPKLAKYMEPVREEGQKKKKTRSMFSWLGGDSSKKKNKEVLETVSEGLRKIYKQKLLPLEEFHKFHDFHSPALDDPDFDAKPMILLVGQYSTGKTTFIRYLLESDFPGIRIGPEPTTDRFIAVMHGDEEGSIPGNALVVDAKKQFRALSGFGNAFLNRFQCSTLPNQVLESVTIVDTPGILSGEKQRIDRGYDFTGVLEWFAERVDRIILLFDAHKLDISDEFKRCIEALAGNEDKIRIVLNKSDMVDHQQLMRVYGALMWSLGKVFKTPEVSRVYLGSFWDHPLHYDLNRRLFQDEQHDLFQDLQALPRNAALRKLNDLIKRARLAKVHAYIIAELRKQMPSMIGKDKKKKDLIQNLDKIYEQLQREHNISPGDFPDVNKMREKLQTQDFSKFNPLKPKLLEVVDGMLATDIARLMAQIPKEEAAAPAGSNGSADPTVRGGAFSQTTEAETPFGFGRYDARWGEGFDKGADEAEWVVSRERTTADSTFESLGPVNGYLSGRAAKEHMVKSKLPNSVLGKVWKLADIDKDGQLDADEFALANYLINLKLEGHEIPSELPKHLIPPSKRGEQDPVYPSLNDNDE
Protein: VRK serine/threonine kinase 3 (M0R025)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MISFCPDCGKSIQAAFKFCPYCGNSLPVEEHVGSQTFVNPHVSSFQGSKRGLNSSFETSPKKVKWSSTVTSPRLSLFSDGDSSESEDTLSSSERSKGSGSRPPTPKSSPQKTRKSPQVTRGSPQKTSCSPQKTRQSPQTLKRSRVTTSLEALPTGTVLTDKSGRQWKLKSFQTRDNQGILYE
Protein: Magnesium transport protein CorA (O50455)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU362010}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362010}.
Interaction partners:
- Haloalkane dehalogenase 2
- Malate dehydrogenase
Sequence:
MFPGFDALPEVLRPVARPQPPNAHPVAQPPAQALVDCGVYVCGQRLPGKYTYAAALREVREIELTGQEAFVWIGLHEPDENQMQDVADVFGLHPLAVEDAVHAHQRPKLERYDETLFLVLKTVNYVPHESVVLAREIVKTGEIMIFVGKDFVVTVRHGEHGGLSEVRKRMDADPEHLRLGPYAVMHAIADYVVDHYLEVTNLMETDIDSIEEVAFAPGRKLDIEPIYLLKREVVELRRCVNPLSTAFQRMQTESKDLISKEVRRYLRDVADHQTEAADQIASYDDMLNSLVQAALARVGMQQNMDMRKISAWAGIIAVPTMIAGIYGMNFHFMPELDSRWGYPTVIGGMVLICLFLYHVFRNRNWL
Protein: Small ribosomal subunit protein RACK1 (40S ribosomal protein ASC1) (Absence of growth suppressor of Cyp1 protein 1) (Cytoplasmic antigenic protein 1) (Guanine nucleotide-binding protein subunit beta-like protein) (P83774)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, it serves as a scaffold protein that can recruit other proteins to the ribosome (By similarity). Involved in the negative regulation of translation of a specific subset of proteins (By similarity). Plays a role in morphogenesis and pathogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15378761}.
Interaction partners:
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein eL19
- 60S acidic ribosomal protein P0
- Small ribosomal subunit protein eS10
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL27
- Large ribosomal subunit protein uL22
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein uL24
Sequence:
MADQEVLVLRGTLEGHNGWVTSLATTPAHPDLLLSGSRDKTLIKWKLTGGEDNQYGIPKKSFKGHSHIVQDVTISADGAYALSASWDRTLRLWDLETGETTQRFVGHKGDVLSVSIAKNLRQIVSASRDKTVKVWNTIGECMATLTGHNDWVSAVRISPSDQSSTVISASWDKTVKSWDLADYSVNADFIGHTGYISCITLSPDGSLCASAGKDGVIILWDLNKNKTLYTLEAKAEVHALAFSPNRYWLAAATTSGIKIFKLQERSLLDELKPEFAVGATAKDPEAISLAWSADGQNLFAGYTDNVIRVWQVMTPSA
Protein: Anti-sigma F factor (EC 2.7.11.1) (Stage II sporulation protein AB) (O32727)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.
Interaction partners:
Sequence:
MRNEMHLQFSARSENESFARVTVAAFVAQLDPTTDELTEIKTVVSEAVTNAIIHGYNNDPNGIVSISVIIEDGVVHLTVRDEGVGIPDIEEARQPLFTTKPELERSGMGFTIMENFMDEVIVESEVNKGTTVYLKKAYCEKQTLCN
Protein: Homeobox-leucine zipper protein ATHB-53 (HD-ZIP protein ATHB-53) (Homeodomain transcription factor ATHB-53) (Q9LVR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that may play a regulatory role in auxin/cytokinin signaling during root development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor TCP18
- Transcription factor TCP12
- Protein SPEAR4
- Protein SPEAR2
- Protein SPEAR1
- At2g18850
- Protein SPEAR3
- Homeobox-leucine zipper protein HDG11
- 9-cis-epoxycarotenoid dioxygenase NCED3, chloroplastic
Sequence:
MDHGRLMDDQMMLGSQVYPYTTQPQNSHCIIVNQIDGGEESKPVKRRRKRRSKGSSATNEEDVAEIGGMLRKRKLTDEQVNMLEYSFGNEHKLESGRKEKIAGELGLDPRQVAVWFQNRRARWKNKKLEEEYAKLKNHHDNVVLGQCQLESQILKLTEQLSEAQSEIRKLSERLEEMPTNSSSSSLSVEANNAPTDFELAPETNYNIPFYMLDNNYLQSMEYWDGLYV
Protein: All-trans-retinol dehydrogenase [NAD(+)] ADH7 (EC 1.1.1.105) (Alcohol dehydrogenase class 4 mu/sigma chain) (EC 1.1.1.1) (Alcohol dehydrogenase class IV mu/sigma chain) (Gastric alcohol dehydrogenase) (Omega-hydroxydecanoate dehydrogenase ADH7) (EC 1.1.1.66) (Retinol dehydrogenase) (P40394)
Organism: Homo sapiens (Human)
Function: Catalyzes the NAD-dependent oxidation of all-trans-retinol, alcohol, and omega-hydroxy fatty acids and their derivatives. Oxidizes preferentially all trans-retinol, all-trans-4-hydroxyretinol, 9-cis-retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such as juniperic acid. In vitro can also catalyzes the NADH-dependent reduction of all-trans-retinal and aldehydes and their derivatives. Reduces preferentially all trans-retinal, all-trans-4-oxoretinal and hexanal. Catalyzes in the oxidative direction with higher efficiency. Therefore may participate in retinoid metabolism, fatty acid omega-oxidation, and elimination of cytotoxic aldehydes produced by lipid peroxidation.
Subcellular location: Cytoplasm.
Interaction partners:
- Aldehyde dehydrogenase, mitochondrial
- Vasopressin-neurophysin 2-copeptin
- Cytochrome P450 2E1
- Catechol O-methyltransferase
- Cytochrome P450 26A1
- Lecithin retinol acyltransferase
- Aldehyde oxidase
- Aldehyde dehydrogenase 1A1
- Amine oxidase [flavin-containing] A
- All-trans-retinol 13,14-reductase
Sequence:
MFAEIQIQDKDRMGTAGKVIKCKAAVLWEQKQPFSIEEIEVAPPKTKEVRIKILATGICRTDDHVIKGTMVSKFPVIVGHEATGIVESIGEGVTTVKPGDKVIPLFLPQCRECNACRNPDGNLCIRSDITGRGVLADGTTRFTCKGKPVHHFMNTSTFTEYTVVDESSVAKIDDAAPPEKVCLIGCGFSTGYGAAVKTGKVKPGSTCVVFGLGGVGLSVIMGCKSAGASRIIGIDLNKDKFEKAMAVGATECISPKDSTKPISEVLSEMTGNNVGYTFEVIGHLETMIDALASCHMNYGTSVVVGVPPSAKMLTYDPMLLFTGRTWKGCVFGGLKSRDDVPKLVTEFLAKKFDLDQLITHVLPFKKISEGFELLNSGQSIRTVLTF
Protein: Scaffold attachment factor B, isoform B (Q8IMV6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein, isoform C
- Acinus, isoform A
Sequence:
MPEAGKKIAELRVCDLKSELEKRELETVGPKAVLIERLEKSLRAEGLDPATHLIVPGAKAKKPFAMPMKDLQSEVVIKEEPIDANEEEVKVEQQDDYQNGNDYSHHADDDGHEIDQVGDVDDECVILDDDDEEDEDHVYDDEPQSGDGDAEGKAQDDGAENNGDDKAIIHGEEENTGDTGNMDNDESINLTIGEDEQKLLHDEASDDKSIKSVKPANKSEKSNSKDADKKNDDGARSKKRDEKSGDKKDSSEQKSSGKSSNQKDDKEKSTAAPGGATSSTASSAAGSKSGSGSSAGNGTGANSNNKQATLSRNLWVSGLSTLTRASDLKAIFSKFGKVIGAKVVTNTRTPGTRCYGYVTMSSSADASRCIENLHRTELHGRIISVERTKNEIGGSLNSKEGKGKAPGDAGNKKKEDDSGKKSGSGKGSSSNSGDDKKGGDGNGDSKSVGGDLKRDGKESNRARSRRNDDRGKSLASQDRPRHDRERSAKGSQDHRSGRNPRDVDREIQQRQRERERRQREMLSYQKIREERERQRLRERERELREEERRRREARERQRIEEERLQEERRKLAVERERLEREKAELLRMERERQKLEREKIELERLELKRQQMKIMESRDDPGKRGVSKRADDRYGDVTDRKRTAIFDAPPPPRFDTNLVSSRSTYDKKHDDYGSSSSTKRVLDDYSSSSKRLDYSSKRNDYSSSSGSKRGAVDDYTAVPTKRSNDYSASSSSKRDDYKRDEVRHLPLSGTVGGGSSSSYLHKNNTAGGGAGSYVHKNNTSGTGGRYNDSDRSNTSSYRRDDSHSLGNKRYDNSSGGGGAYGSSSNSVNIWAPSSGGSSSHLGSGGGGGNQIKSYGNNGMSSNMHSTNSWQKSAPVDDNGWRQVPARFDRGYNERSTGYQGQSGGGGAGGMYGASRPAQDRYSGPVSRY
Protein: Ankyrin 1 (A0A8I6ABK4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MAERPRRSGSDPAADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTSMVKLLLENDASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVQLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVAQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLKVVTDETSVVLVSDKHRMSYPETVDEILDVSEDEGTAHISLTGDELVGSKAERRDSRDVGEEKELLDFVPKLDQVVESPAIPRIPCVTPETVVIRSEDQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLSTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHKSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLRSKLVPLVQATFPENAVTKKVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLVYANECANFTTNVSARFWLSDCPRTAEAVHFATLLYKELTAVPYMAKFVIFAKMNDPREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAIPVKVRDSSREPGGFLSFLRKPMKYEDAQHILCHLNVTMPPCTKGSGAEDRRRTLTPLTLRYSILSESRLGFTSDTDRVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLEGSGRQSRNLKPDRRHGDREYSLSPSQVNGYSSLQDELLSPASLHYALPSPLCADQYWNEVAVIDAIPLAATEHDTMLEMSDMQVWSSGLTPSLVTAEDSSLECSKAEDSDAIPEWKLEGAHSEDTQGPELGSQDLVEDDTVDSDATNGLADLLGQEEGQQRVHARITDSPSVRQVLDRSQARTVDWYKQGSAASYPQEAAQSSWQEEVTQGPQSFQRRITTIQGPEPGTLQEYEQVVVSTREHVQRGPPESDSPKAGKDPSLWASESAFSQEVQGDELQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQVDSSGAIDTQQHEEVELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ
Protein: CHK kinase-like domain-containing protein (Q9VBT3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAENVDSAQFNADEVDAPAWLNAELIEGALRAYEKDPELHVTDLKISPATLQGDHYASVMFRAVSHYSTAKGNFSKALIVKTMPEQEGHKKDMLSNSPIFKTEILMYSKALPELERILREAGDTTKLYAPCIYHSLEPHQVMIFEDLVPQGYTVIRDRYPNKEELQKAFFKLAKWHAASMKVLNERPDFLKEFKYGLWGMPNFLNDSIVTTGVPCFLEMLDKVPELTKYKPYFEKIKDNYIQQMSAVMEEYRTNPKPNRYYVLCHGDFHGRNMMFRYNKETGSFEDVMLVDFQISNVCPLSIDLIYSIFMVMDTEDRWDLGKEYINYYFSVLADTLKKIGFKGEMPTQTGVWEHIHGHKDYEFFMMTSFLPLVAAMNTKTFKSMDSFFDPQTKQKSFFLDEYITDVKMLLRKFEELGYFKDL
Protein: CCAAT/enhancer-binding protein beta (C/EBP beta) (Transcription factor NF-M) (CCR protein) (Q05826)
Organism: Gallus gallus (Chicken)
Function: Important transcriptional activator regulating the expression of genes involved in immune and inflammatory responses. Binds to regulatory regions of several acute-phase and cytokines genes and probably plays a role in the regulation of acute-phase reaction, inflammation and hemopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Functions in brown adipose tissue (BAT) differentiation. Regulates the transcriptional induction of peroxisome proliferator-activated receptor gamma (PPARG). Binds to the MGF and MIM-1 promoters and activates the transcription of these genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cyclic AMP-dependent transcription factor ATF-4
- Peroxisome proliferator-activated receptor gamma
- E1A binding protein p300.
- C/EBP-like protein
- CCAAT enhancer binding protein delta
- PR/SET domain 16
- Mitogen-activated protein kinase.
- Runt-related transcription factor
- Signal transducer and activator of transcription 3
- Transcription factor Jun
Sequence:
MQRLVAWDAACLPIQPPAFKSMEVANFYYEADCLAALNKLHPRAAGGRSMTELTVGDHERAIDFSPYLDPLAASQQPAQPPPPAAAAGGNFEPACSSGGQDFLSDLFAEDYKGSGGGKKPDYTYISLTRHGHPCGSQSHKPGVLPGCFPPQIVETKVEPVFETLDSCKGPRKEEGGAGPGPGGMSSPYGSTVRSYLGYQSVPSGSSGNLSTSSSSSPPGTPNPSESSKSAAGAGGYSGPPAGKNKPKKCVDKHSDEYKLRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASSPRC
Protein: Protein disulfide-isomerase TMX3 (EC 5.3.4.1) (Thioredoxin domain-containing protein 10) (Thioredoxin-related transmembrane protein 3) (Q96JJ7)
Organism: Homo sapiens (Human)
Function: Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15623505}; Single-pass membrane protein {ECO:0000269|PubMed:15623505}.
Interaction partners:
Sequence:
MAAWKSWTALRLCATVVVLDMVVCKGFVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQQMFEHMQKRHRVFFVYVGGESPLKEKYIDAASELIVYTYFFSASEEVVPEYVTLKEMPAVLVFKDETYFVYDEYEDGDLSSWINRERFQNYLAMDGFLLYELGDTGKLVALAVIDEKNTSVEHTRLKSIIQEVARDYRDLFHRDFQFGHMDGNDYINTLLMDELTVPTVVVLNTSNQQYFLLDRQIKNVEDMVQFINNILDGTVEAQGGDSILQRLKRIVFDAKSTIVSIFKSSPLMGCFLFGLPLGVISIMCYGIYTADTDGGYIEERYEVSKSENENQEQIEESKEQQEPSSGGSVVPTVQEPKDVLEKKKD
Protein: Dolichol-phosphate mannosyltransferase (EC 2.4.1.83) (Dolichol-phosphate mannose synthase) (DPM synthase) (Dolichyl-phosphate beta-D-mannosyltransferase) (Mannose-P-dolichol synthase) (MPD synthase) (PfDPMS) (Q8U4M3)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKVSVIIPTYNERENLEELFSRIDNALQGLNYEIVVVDDDSPDRTWEKAQELSSKYPVKVIRRTKEKGLSSAVIRGFKEASGDVFVVMDADLQHPPEVIPKLIEAIKNGSDIAIGSRYVKGGKVENWPFYRKLISKGAIMVGRIALPKIRDIKDPVSGFFALRKEVVEGVELNPIGFKILMEILIKGKYSKVVEVPFTFGIRARGESKLKGKTIFEYLRHIYRLMKWEGEIDRIVKFSIVGLSGILVNEGFLWLFVNLGIPKEIAVIPAVELSILNNFFWNDIWTFKDIRRGSIFSRLLKFHIAALSGAVVNFIVYWILLFLGIHYLIANLVGIVLSFGVRYVINRHVTWAT