wanglab/gogpt-training-data huggingface dataset:
Protein: Myb-related protein B (B-Myb) (Myb-like protein 2) (P10244)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene.
Subcellular location: Nucleus.
Interaction partners:
- Protein lin-54 homolog
- Protein lin-52 homolog
- Protein lin-9 homolog
- Protein lin-37 homolog
- Forkhead box protein M1
- Histone-binding protein RBBP4
- Cyclin-A2
- Cyclin-A1
- Cyclin-dependent kinase 2
- Transcription factor E2F4
Sequence:
MSRRTRCEDLDELHYQDTDSDVPEQRDSKCKVKWTHEEDEQLRALVRQFGQQDWKFLASHFPNRTDQQCQYRWLRVLNPDLVKGPWTKEEDQKVIELVKKYGTKQWTLIAKHLKGRLGKQCRERWHNHLNPEVKKSCWTEEEDRIICEAHKVLGNRWAEIAKMLPGRTDNAVKNHWNSTIKRKVDTGGFLSESKDCKPPVYLLLELEDKDGLQSAQPTEGQGSLLTNWPSVPPTIKEEENSEEELAAATTSKEQEPIGTDLDAVRTPEPLEEFPKREDQEGSPPETSLPYKWVVEAANLLIPAVGSSLSEALDLIESDPDAWCDLSKFDLPEEPSAEDSINNSLVQLQASHQQQVLPPRQPSALVPSVTEYRLDGHTISDLSRSSRGELIPISPSTEVGGSGIGTPPSVLKRQRKRRVALSPVTENSTSLSFLDSCNSLTPKSTPVKTLPFSPSQFLNFWNKQDTLELESPSLTSTPVCSQKVVVTTPLHRDKTPLHQKHAAFVTPDQKYSMDNTPHTPTPFKNALEKYGPLKPLPQTPHLEEDLKEVLRSEAGIELIIEDDIRPEKQKRKPGLRRSPIKKVRKSLALDIVDEDVKLMMSTLPKSLSLPTTAPSNSSSLTLSGIKEDNSLLNQGFLQAKPEKAAVAQKPRSHFTTPAPMSSAWKTVACGGTRDQLFMQEKARQLLGRLKPSHTSRTLILS
Protein: BBSome complex member bbs-5 (Bardet-Biedl syndrome 5 protein homolog) (Q21626)
Organism: Caenorhabditis elegans
Function: Component of the BBSome complex (By similarity). The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia (By similarity). The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function (By similarity). Required for BBSome complex ciliary localization but not for the proper complex assembly (By similarity). Required, redundantly with bbs-4, for cilia biogenesis and both the assembly and movement of intraflagellar transport proteins along the ciliary axoneme. Plays a role in the removal of degraded mechanosensory receptors within the cilia.
Subcellular location: Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q8N3I7}. Cytoplasm {ECO:0000250|UniProtKB:Q8N3I7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9CZQ9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q8N3I7}. Note=Localizes to basal bodies. {ECO:0000250|UniProtKB:Q9CZQ9}.
Interaction partners:
- BBSome complex member bbs-4
- Protein pthb1 homolog
- BBSome complex member bbs-2
- BBSome complex member BBS1
- BBSome complex member bbs-7
- Tetratricopeptide repeat protein 8
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 20 homolog
- Intraflagellar transport protein 74 homolog
- Polycystin-2
Sequence:
MERVNGEDIWQDREIRFDVDHKLLRLINGEIQVAKIEHVEDTKGNNGDRGTMRVTNLRLIWHAASMPRINITIGWNAITGVQSKQTTSLVTRNRGISNEAIYVLAKVSATTTKFEFIFTTTNPASHSKLFNTISSISRAYETTKMYRELKMRGVFIREDGTLKILPQETIIEKVNGVWNLSTETGSLGVFVITNIRVVWYAEMNIGYNVSVPYITLYSVRVRESKFGMALVLETTTSSGEYVLGFRVDPAERLQNLLKTVQSLHKAHLLKPIFGVSYVKEIAEKVEPRKDDDEIDIIDNNEDDVEIDDKIRPDAFASYFDGEHTATDEKQLPVLNPELGLAIEPIRNGFTLHDLWNIHVDV
Protein: Leishmanolysin-like peptidase (EC 3.4.24.-) (Invadolysin) (Q96KR4)
Organism: Homo sapiens (Human)
Function: Metalloprotease.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15557119}. Lipid droplet {ECO:0000269|PubMed:19706689}. Note=Found in ring-like structures resembling invadopodia. In migrating cells it relocalizes from internal structures to the leading edge of cells. {ECO:0000269|PubMed:19706689}.
Interaction partners:
- Complement C3
- Fibronectin
Sequence:
MAAEWGGGVGYSGSGPGRSRWRWSGSVWVRSVLLLLGGLRASATSTPVSLGSSPPCRHHVPSDTEVINKVHLKANHVVKRDVDEHLRIKTVYDKSVEELLPEKKNLVKNKLFPQAISYLEKTFQVRRPAGTILLSRQCATNQYLRKENDPHRYCTGECAAHTKCGPVIVPEEHLQQCRVYRGGKWPHGAVGVPDQEGISDADFVLYVGALATERCSHENIISYAAYCQQEANMDRPIAGYANLCPNMISTQPQEFVGMLSTVKHEVIHALGFSAGLFAFYHDKDGNPLTSRFADGLPPFNYSLGLYQWSDKVVRKVERLWDVRDNKIVRHTVYLLVTPRVVEEARKHFDCPVLEGMELENQGGVGTELNHWEKRLLENEAMTGSHTQNRVLSRITLALMEDTGRQMLSPYCDTLRSNPLQLTCRQDQRAVAVCNLQKFPKPLPQEYQYFDELSGIPAEDLPYYGGSVEIADYCPFSQEFSWHLSGEYQRSSDCRILENQPEIFKNYGAEKYGPHSVCLIQKSAFVMEKCERKLSYPDWGSGCYQVSCSPQGLKVWVQDTSYLCSRAGQVLPVSIQMNGWIHDGNLLCPSCWDFCELCPPETDPPATNLTRALPLDLCSCSSSLVVTLWLLLGNLFPLLAGFLLCIWH
Protein: Thiamin pyrophosphokinase thiamin-binding domain-containing protein (Q55GR8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Probable adenylate kinase B
- Adenylate kinase
- Low molecular weight phosphotyrosine protein phosphatase
- Alkaline phosphatase
- Probable acid phosphatase DDB_G0284755
- pantothenate kinase
Sequence:
MEKQEEEVQQQQQQQQQQQQPDKNNKETITWDVAEYGGYLFDKKLKAHNPLNHQMPLQYHHSQSTPHIPSSLSTSSTTSIKKPSSSLSDDESGGSSSSTPHSSNTPRKQFSFDDHCALILANQKLPKKLVDYFWDKCSVRICADGGANRLYSLGTKINQSSRWIPDYIKGDLDSLHEGVSDFFSKKGSSIVLDSSQDTSDLQKCFELIIDLEKGSGIKYRKIFILGGLGGSFSHEFANVNTLFDHPGRKIILASKDNLAWLLSSTYNHNIICRSETKCSLIPLSSKASQVTTSGLKWNLVKQSLNFGELISTSNVSLDNKVCVETSNPLIFIVDINP
Protein: COP9 signalosome complex subunit 4 (Signalosome subunit 4) (Q9N359)
Organism: Caenorhabditis elegans
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. The CSN complex plays an essential role in embryogenesis and oogenesis and is required to regulate microtubule stability in the early embryo. Mediates mei-3/katanin targeting for degradation at the meiosis to mitosis transition via deneddylation of cul-3.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12781129}. Nucleus {ECO:0000269|PubMed:12781129}.
Interaction partners:
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 3
- Ubiquitin-like protein NEDD8
- COP9/Signalosome and eIF3 complex-shared subunit 1
- RING-box protein 1
- Uncharacterized protein
- Cullin-4
Sequence:
MSGEIERSQEVAVIFAQDTDHKAQYEALAKLCNKYLPQNAMGRVDTAEIIKIIDTVIALETGSMVVSRQFVSLITERLDNQHLESECVKAISEGILAIIKTRTISYEDQVCILRLMLASLYEKEGRIKDAAQALIAINSDTSPKFNGPQAAKEGAKAQLCIRITKLLLDCSEIDEAEQYVNRTSILMVDLGANPDIQIEHKALQARVSDAKRRFVEAAQRYYELSATEQLPNSDKLTALGKAIVCVLLAKPGPQRSRLLTLIFKDERAPKCASFELIAKMYLTKVIHKDELEEFEHQLQDHQKADEHGESILKGVIQEHNITAISQLYINISFKTLGQLLGVDTEAAESMAGEMISSERLHGYIDQTNGILHFEDSNPMRVWDSQILSTLEQINKVSDMIVARHSEFAEFLT
Protein: Putative protein SPATA31J1 (A6NFR6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPRAQLPEDSSAVDMDILFPLDSVIGTELCPSPIPQIIHFVLFVVFSLVILIILRLYIPREPSSVPPREEDSENDQAEVGEWLRIGNKYITLKDYRILLKELENLEIYTFLSKKCLKKLSREGSSHHLPRQVRPGPVYKPAPARNHRPRGGRGKASPTSFHVSPRAPLAPLASMPSSVPKTSVESLGSPSSLSSSKPREPLCPLKHPSHQPPASTLSPNPTSSTESLGYLSSLSSSQPPEPLRPLKHPSHKPRGRSLPRRRNPGWVSWSDSMQADSETDTIICPMCKAPERSCPHTWWVPSSPRVIRGVGRCSDPNLGLSWRQEAARAWCHCTSSQFPFKHPNLPTHLPKASF
Protein: DNA-binding protein (Q8GKU0)
Organism: Shigella flexneri 2a
Subcellular location: Cytoplasm, nucleoid {ECO:0000256|ARBA:ARBA00004453}.
Interaction partners:
Sequence:
MSGALKSLNNIRTLRAQGRELPLEILEELLEKLSVVVEERRQEESSKEAELKARLEKIESLRQLMLEDGIDPEELLSPFSAKSGAPKKVREPRPAKYKYTDVNGETKTWTGQGRTPKALAEQLEAGKTLDDFLI
Protein: Spermine oxidase (A0A8I5Y9C4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MQSCESSGDSADDPLSRGLRRRGQPRVVVIGAGLAGLAAARALLEQGFTDVTVLEASSHIGGRVQSVKLGHATFELGATWIHGSHGNPIYQLAEANGLLEETTDGERSVGRISLYSKNGVACYLTNRGRRIPKDVVEEFSDLYNEVYNLTQEFFRNGKPVNAESQNSVGVFTREKVRNRIRDDPDDTEATKRLKLAMIQQYLKGTPIYQNLGESCAQPGAATHTSGVPIHTHRWAQVGQMWRSW
Protein: TTLL7 protein (I6L9D0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPSLPQEGVIQGPSPLDLNTELPYQSTMKRKVRKKKKKGTITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDSAVQQEKISELQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYVKELKKKRKQKTFIVKRANGAMGHGISLIRNGDKLPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQANQHDVAKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSDWEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIYPPEDKALLEKYENLLAVAFQTFLSGRAASFQRELNNPLKRMKEEDILDLLEQCEIDDEKLMGKTTKTRGPKGRITHYVVKLFKNT
Protein: Semaphorin-3A (Collapsin-1) (COLL-1) (Q90607)
Organism: Gallus gallus (Chicken)
Function: Induces the collapse and paralysis of neuronal growth cones. Could serve as a ligand that guides specific growth cones by a motility-inhibiting mechanism. Binds to neuropilin.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Neuropilin-1
- Plexin-A4
- Plexin-D1
- Plexin A1.
- Plexin A2.
- Netrin-1
- Netrin-3
- Uncharacterized protein.
- Dihydropyrimidinase-related protein 1
- Protein kinase domain-containing protein.
Sequence:
MGWLRGIALLSLGVLLAGRVNCQHVKNNVPRLKLSYKEMLESNNIVNFNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKEYQKIVWPVSHSRRDECKWAGKDILRECANFIKVLKTYNQTHLYACGTGAFHPMCTYIEVGSHPEDNIFRMEDSHFENGRGKSPYDPKLLTASLLVDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKIYFFFRENAIDGEHTGKATHARIGQICKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMTDVRRVFLGPYAHRDGPNYQWVPYQGRVPYPRPGTCPSKTFGGFDSTKDLPDEVITFARSHPAMYNPVFPINSRPIMIKTDVDYQFTQIVVDRVDAEDGQYDVMFIGTDIGTVLKVVSIPKETWHELEEVLLEEMTVFREPTVISAMKISTKQQQLYIGSATGVSQLPLHRCDVYGKACAECCLARDPYCAWDGSSCSRYFPTAKRRTRRQDIRNGDPLTHCSDLQHHDNPSGQTLEEKIIYGVENSSTFLECSPKSQRAIVYWQFQKQNDDHKVEIKVDDRMIRTEQGLLLRSLQRRDSGIYFCHAVEHGFIQTLLKVTLEVIDTDHLEELLHKEEDADASKTKDATNSMTPSQKIWYRDFMQLINHPNLNTMDEFCEQVWKRDRKQRRQRPANAQVNTNKWKHLQENKKGRNRRTHEFERAPRSV
Protein: Aldehyde dehydrogenase 2 family member (A0A286XPF7)
Organism: Cavia porcellus (Guinea pig)
Interaction partners:
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- 4-aminobutyrate aminotransferase, mitochondrial
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Acetyl-coenzyme A synthetase
- Propionate--CoA ligase
- S-
- Aldo-keto reductase family 1 member A1
- Delta-1-pyrroline-5-carboxylate synthase
- 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- Beta-ureidopropionase
Sequence:
MLRAAALAASGLGPRLGRRLLSAAAAQAVPTPNQQPEVFYNQIFINNEWHDAVSKKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGSPWRRMDASERGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCIRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGYGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQESVYEEFVERSIARAKARVVGNPFDSRTEQGPQVDETQFKKILGYIKSGKEEGAKLLCGGGAAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNTKYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Protein: Putative colanic acid biosynthesis glycosyltransferase WcaL (EC 2.4.-.-) (P71243)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Colanic acid biosynthesis protein WcaK
- Colanic acid biosynthesis protein WcaM
- Putative colanic acid biosynthesis glycosyl transferase WcaC
- Putative colanic acid biosynthesis glycosyl transferase WcaA
- UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase
- Lipopolysaccharide biosynthesis protein WzxC
- Putative colanic acid biosynthesis glycosyl transferase WcaE
- Putative colanic acid biosynthesis glycosyl transferase WcaI
- Putative colanic acid biosynthesis acetyltransferase WcaB
- Putative colanic acid biosynthesis acetyltransferase WcaF
Sequence:
MKVGFFLLKFPLSSETFVLNQITAFIDMGFEVEILALQKGDTQNTHAAWTKYNLAARTRWLQDEPTGKVAKLRHRASQTLRGIHRKNTWQALNLKRYGAESRNLILSAICGQVATPFRADVFIAHFGPAGVTAAKLRELGVIRGKIATIFHGIDISSREVLNHYTPEYQQLFRRGDLMLPISDLWAGRLQKMGCPREKIAVSRMGVDMTRFSPRPVKAPATPLEIISVARLTEKKGLHVAIEACRQLKEQGVAFRYRILGIGPWERRLRTLIEQYQLEDVVEMPGFKPSHEVKAMLDDADVFLLPSVTGADGDMEGIPVALMEAMAVGIPVVSTLHSGIPELVEADKSGWLVPENDARALAQRLAAFSQLDTDELAPVVKRAREKVEHDFNQQVINRELASLLQAL
Protein: GDP-fucose protein O-fucosyltransferase 2 (EC 2.4.1.221) (Protein O-fucosyltransferase 2) (W7K6N5)
Organism: Plasmodium falciparum (isolate NF54)
Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively (By similarity). O-fucosylates sporozoite proteins CSP and TRAP (By similarity). O-fucosylation regulates stability and intracellular trafficking of TRAP but not of CSP. Probably by regulating protein O-fucosylation, may play a role in parasite transmission to the mosquito vector and/or infection of the vertebrate host hepatocytes; however, POFUT2 involvement in transmission/infection is controversial.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:28916755}.
Interaction partners:
Sequence:
MKFIIVLLLFFFFKVIDRVICVTPQKLICLKEDVYLGDFFFFLKRKKYIMYDVNIGEGFNLQKEIFYRLSLVIYNLNKKDKINIYYLVLPPWCYVTHWNIRKGNNLRWEFFFNTDIMKKVIPIIEYEEYEKLYGNYSDIMINSKYILDNYKEKSFLILPFEECNINVNRFKQFCKKCEHKYNVLYSGYCTTINTKQSECYSYNMISNYFITSILENLFLYNITSVLIKQSTNILVPFVNELYQSNLEDILLFNNKLLSYGNNYISNILKTNHYISSHLRYTDFKYISRYNVPPIHIALLKLLYIMFINNCRIIFIASDEKVEIQKVINKDFHQYKKHFYFYNNQNNLHEGEFSIIEQWICTRSYIFIGNIFSRFTMNINWERHLINKGQINQNIDLCSYHINDDNDQDIKNSYKKIVHIFNHKALQKIKNIYDNYSDRDKKYINTICYNFLSHFPNNRSIYRKEYITNT
Protein: Melanocortin receptor 3 (MC3-R) (P33033)
Organism: Mus musculus (Mouse)
Function: Receptor for MSH (alpha, beta and gamma) and ACTH. This receptor is mediated by G proteins which activate adenylate cyclase. Required for expression of anticipatory patterns of activity and wakefulness during periods of limited nutrient availability and for the normal regulation of circadian clock activity in the brain.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Pro-opiomelanocortin
- Agouti-related protein
- Growth hormone secretagogue receptor type 1
- Melanocortin-2 receptor accessory protein 2
- Appetite-regulating hormone
- Pro-neuropeptide Y
- Leptin
Sequence:
MNSSCCLSSVSPMLPNLSEHPAAPPASNRSGSGFCEQVFIKPEVFLALGIVSLMENILVILAVVRNGNLHSPMYFFLCSLAAADMLVSLSNSLETIMIAVINSDSLTLEDQFIQHMDNIFDSMICISLVASICNLLAIAIDRYVTIFYALRYHSIMTVRKALTLIGVIWVCCGICGVMFIIYSESKMVIVCLITMFFAMVLLMGTLYIHMFLFARLHVQRIAVLPPAGVVAPQQHSCMKGAVTITILLGVFIFCWAPFFLHLVLIITCPTNPYCICYTAHFNTYLVLIMCNSVIDPLIYAFRSLELRNTFKEILCGCNSMNLG
Protein: Klotho (EC 3.2.1.31) [Cleaved into: Klotho peptide] (Q9UEF7)
Organism: Homo sapiens (Human)
Function: May have weak glycosidase activity towards glucuronylated steroids. However, it lacks essential active site Glu residues at positions 239 and 872, suggesting it may be inactive as a glycosidase in vivo. May be involved in the regulation of calcium and phosphorus homeostasis by inhibiting the synthesis of active vitamin D (By similarity). Essential factor for the specific interaction between FGF23 and FGFR1 (By similarity).
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:15135068}; Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:O35082}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O35082}. Note=Isoform 1 shedding leads to a soluble peptide. {ECO:0000250|UniProtKB:O35082}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:15135068}.; SUBCELLULAR LOCATION: [Klotho peptide]: Secreted {ECO:0000250|UniProtKB:O35082}.
Interaction partners:
- Fibroblast growth factor 23
- Fibroblast growth factor receptor 1
- Fibroblast growth factor 8
- Fibroblast growth factor 18
- Fibroblast growth factor receptor 4
- Fibroblast growth factor 9
- Fibroblast growth factor 22
- Fibroblast growth factor 17
- Fibroblast growth factor 5
- Fibroblast growth factor 3
Sequence:
MPASAPPRRPRPPPPSLSLLLVLLGLGGRRLRAEPGDGAQTWARFSRPPAPEAAGLFQGTFPDGFLWAVGSAAYQTEGGWQQHGKGASIWDTFTHHPLAPPGDSRNASLPLGAPSPLQPATGDVASDSYNNVFRDTEALRELGVTHYRFSISWARVLPNGSAGVPNREGLRYYRRLLERLRELGVQPVVTLYHWDLPQRLQDAYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNPYVVAWHGYATGRLAPGIRGSPRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGQVSIALSSHWINPRRMTDHSIKECQKSLDFVLGWFAKPVFIDGDYPESMKNNLSSILPDFTESEKKFIKGTADFFALCFGPTLSFQLLDPHMKFRQLESPNLRQLLSWIDLEFNHPQIFIVENGWFVSGTTKRDDAKYMYYLKKFIMETLKAIKLDGVDVIGYTAWSLMDGFEWHRGYSIRRGLFYVDFLSQDKMLLPKSSALFYQKLIEKNGFPPLPENQPLEGTFPCDFAWGVVDNYIQVDTTLSQFTDLNVYLWDVHHSKRLIKVDGVVTKKRKSYCVDFAAIQPQIALLQEMHVTHFRFSLDWALILPLGNQSQVNHTILQYYRCMASELVRVNITPVVALWQPMAPNQGLPRLLARQGAWENPYTALAFAEYARLCFQELGHHVKLWITMNEPYTRNMTYSAGHNLLKAHALAWHVYNEKFRHAQNGKISIALQADWIEPACPFSQKDKEVAERVLEFDIGWLAEPIFGSGDYPWVMRDWLNQRNNFLLPYFTEDEKKLIQGTFDFLALSHYTTILVDSEKEDPIKYNDYLEVQEMTDITWLNSPSQVAVVPWGLRKVLNWLKFKYGDLPMYIISNGIDDGLHAEDDQLRVYYMQNYINEALKAHILDGINLCGYFAYSFNDRTAPRFGLYRYAADQFEPKASMKHYRKIIDSNGFPGPETLERFCPEEFTVCTECSFFHTRKSLLAFIAFLFFASIISLSLIFYYSKKGRRSYK
Protein: Cyclin-dependent kinase 5 activator (Q9Y0G0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGTVLSFNPRDRHPIYSSQPNFQYNHSTDMRNENDSTGSIDSHLNNFSYEQLNNAKNRENKKSACHPMAKNVIGQPGGQCGGVHINLQTQTQLSSHNLNNLANASKDTITNVLDTHNENSVLKAEKSSFEKNLKKHSIFINALSWKKLSTSHNKKKIENKNKCANLPTACFKAQLLESSFASSSDKNRNIQLHCNRIDEHNQQHCNQHPHPHPHPHQHQLQLQNQHQHQNQNQNQNQNQVQDIREEVMTGPPGKSQNPSKAKDPVKVNNKNSMSNHNKLIQKQPLTLSLPQQVQASSIQIKNTNQIPRKTVIQASTSELLKCLGMFLHCRCQRLNNFDAGDAVMWLRAVDRSLLLQGWQDVAFINPANVVFVYMLVRELVSGEESKESDLQASVLTCLYLSYSYMGNEISYPLKPFLVEDSKEKFWDRCLVIVNKLSDKMLKINAEPGFFTEVFTELKSCGQYHPTIKSYCGGA
Protein: Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (MCAD) (EC 1.3.8.7) (P45952)
Organism: Mus musculus (Mouse)
Function: Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P08503}.
Interaction partners:
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Peroxisomal bifunctional enzyme
- Peroxisomal acyl-coenzyme A oxidase 1
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- 3-ketoacyl-CoA thiolase B, peroxisomal
Sequence:
MAAAFRRGCRVLRSVSHFECRTQHSKAAHKQEPGLGFSFELTEQQKEFQATARKFAREEIIPVAPEYDKSGEYPFPLIKRAWELGLINAHIPESCGGLGLGTFDACLITEELAYGCTGVQTAIEANSLGQMPVILAGNDQQKKKYLGRMTEQPMMCAYCVTEPSAGSDVAAIKTKAEKKGDEYVINGQKMWITNGGKANWYFLLARSNPDPKVPASKAFTGFIVEADTPGIHIGKKELNMGQRCSDTRGIAFEDVRVPKENVLIGEGAGFKIAMGAFDRTRPTVAAGAVGLAQRALDEATKYALDRKTFGKLLVEHQGVSFLLAEMAMKVELARLSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQIFGGYGFNTEYPVEKLMRDAKIYQIYEGTAQIQRLIIAREHIEKYKN
Protein: Dendritic cell nuclear protein 1 (Dendritic cell nuclear protein-1) (Dendritic cell-associated nuclear protein) (Q8TF63)
Organism: Homo sapiens (Human)
Function: Binds with and transactivates the corticotropin-releasing hormone (CRH) promoter.
Subcellular location: Nucleus {ECO:0000269|PubMed:11798177, ECO:0000269|PubMed:20693543}. Cytoplasm {ECO:0000269|PubMed:20693543}. Note=Particularly on the periphery. Colocalizes with corticotropin-releasing hormone (CRH) in parvocellular neurons in the paraventricular nucleus. {ECO:0000269|PubMed:20693543}.
Interaction partners:
- Macrosialin
Sequence:
MHYGAATHIQNSRSHGLETVPGHQRLERGAGGETPEFPGCHSPAPPENFGNELLPLSAPLQGLSEGLYPPGRNKTLPAGVLREGAVQFLHRGLCNSNLSSEASARPSGTQDELHSSRRKTGQTRREGARKHLVCSFRLYPFTVHTVSPGNSHLALYQVFKAVKLCPSETSFFLSRKSLKSSDPWHPPSLSPNSWNRQAGFRAWSSHLISLSLTCSDSQSRRVSSSQQPPLHSLSSHRRAAHVPE
Protein: Extracellular matrix protein (Q54LG5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Extracellular matrix protein A
- Prestalk protein
Sequence:
MKLLYSLVALLGVSSVAFGDNSCNQLLSSLADPSKCVQVSISGVHSQSLAQEGYKGNLVFASGEFVLRESLYNLQTYETTCSRGGLVQPFAADDQFRVEDFSIRLSDGNLRLKQINTQLTCNGNVGFFNLNNFYYALALKSYDTCPRLYYGEPCNTPTVTPTTTPSPTTKPPTGPLKFNYKLDIDWQWDSNNVHYYQYRVTVTNNDSTAIKSIQIHSDNWNPTEFWNVEKNAQTGNLGFPSFVNTLPVGDSFSFGFVSAVVNPTFSTVSFERV
Protein: Nucleoporin ndc-1 (Nucleoporin npp-22) (Q8I4N3)
Organism: Caenorhabditis elegans
Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope (By similarity). Plays a role in postmitotic nuclear pore complex assembly potentially by promoting localization of nuclear pore complex proteins to the nuclear rim.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q6AX31}. Nucleus membrane {ECO:0000269|PubMed:35852146}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6AX31}. Note=Central core structure of the nuclear pore complex (By similarity). Localizes to the nuclear envelope at non-core regions after mitosis (PubMed:35852146). {ECO:0000250|UniProtKB:Q6AX31, ECO:0000269|PubMed:35852146}.
Interaction partners:
- BIG2 domain-containing protein
- Nucleoporin NUP35
- Nucleoporin_N domain-containing protein
- Nsp1_C domain-containing protein
- Nuclear pore protein
- Nucleoporin SEH1
- Nuclear Pore complex Protein
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein 14
Sequence:
MMGDSHSSFTTTTDEHLYNQFSPGRRKNDFPAASSSSSSPNLRRSPNRTVSSPRVQQKPITIFDQIVDWFQAEISVRKRLAGAACGYLSTIFFIVTVSILKLTIWAPFSSVQDSLAWWIYPNAWASIIFVGIASVAMSLFSIIKFCKVDQLPRLAATDTFALAGVALEFVTRLTFVYTAFCVADFSFSREFAFVAISLAIAISSALVVFRSDYQLNFSHIQVNSVKTLIDFGTSLPYANISEICGIDAAISYTAAVALILVVGPMVSGFSAWWLLLNIPFHVVLFGLCFTQQFYSKISMKIVNQIVMKPISFPFPPPYTVHSPTPEQTRTLPNVIETDDSLLKFFALHDLRTIAWNDEKRRVDVFSLSQPGKHPRNWKAVSLPCVRMLDELCSRMTVSAARLVGYSWDDHDIENEDVPRDALLMPRKMREMAYRGTGQSRQQKSMAPIRSHNTQTVGLLSKISNFLGFGVTEKLVISRFDAHMNAYAAEALYMLVVDSMGEDRFGVVQKDLKDLITLLCKLIAAIDTYERAKASVADKSDVTFLRIVDASLKSSLQRVVTTFGSHLSSLNLPEEHSRTIRMICLTDEL
Protein: TIL domain-containing protein (Q7KUM2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MWKWETFTLVVLCSFSAVKCFAEKVDCSVNGTQTDCPTACPETCDTKGKPNCTLICGGPCVCKPGYVVNRMIPACVLRSDCPKIVLQSDRARRLTNFNCFSGENTCTQLKHSSSKRNND
Protein: Interferon C (C1IRY0)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MPCQLQGQLVRITHNLLRDMGGNFPLECLQENVFVAFPATAFASSGAPQLSSSGAKAIYETLKNIDILFEADDPPTQWDQQKLENFQNIVYRQIEESKCMMGSVDTSDYLIRTEGLNTYFGNIAAVLKEKNFSYC