wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PP2A B subunit isoform B'-delta) (PP2A B subunit isoform B56-delta) (PP2A B subunit isoform PR61-delta) (PP2A B subunit isoform R5-delta) (Q14738)
Organism: Homo sapiens (Human)
Function: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
Subcellular location: Cytoplasm. Nucleus. Note=Nuclear in interphase, nuclear during mitosis.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Shugoshin 1
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- Kelch domain-containing protein 3
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
Sequence:
MPYKLKKEKEPPKVAKCTAKPSSSGKDGGGENTEEAQPQPQPQPQPQAQSQPPSSNKRPSNSTPPPTQLSKIKYSGGPQIVKKERRQSSSRFNLSKNRELQKLPALKDSPTQEREELFIQKLRQCCVLFDFVSDPLSDLKFKEVKRAGLNEMVEYITHSRDVVTEAIYPEAVTMFSVNLFRTLPPSSNPTGAEFDPEEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFVLALLDLFDSEDPRERDFLKTILHRIYGKFLGLRAYIRRQINHIFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKMFLIRVLLPLHKVKSLSVYHPQLAYCVVQFLEKESSLTEPVIVGLLKFWPKTHSPKEVMFLNELEEILDVIEPSEFSKVMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMSLISDNAARVLPIMFPALYRNSKSHWNKTIHGLIYNALKLFMEMNQKLFDDCTQQYKAEKQKGRFRMKEREEMWQKIEELARLNPQYPMFRAPPPLPPVYSMETETPTAEDIQLLKRTVETEAVQMLKDIKKEKVLLRRKSELPQDVYTIKALEAHKRAEEFLTASQEAL
Protein: Solute carrier family 25 member 3 (Phosphate carrier protein, mitochondrial) (Phosphate transport protein) (A0A024RBH9)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MFSSVAHLARANPFNTPHLQLVHDGLGDLRSSSPGPTGQPRRPRNLAAAAVEEQYSCDYGSGRFFILCGLGGIISCGTTHTALVPLDLVKCRMQVDPQKYKGIFNGFSVTLKEDGVRGLAKGWAPTFLGYSMQGLCKFGFYEVFKVLYSNMLGEENTYLWRTSLYLAASASAEFFADIALAPMEAAKVRIQTQPGYANTLRDAAPKMYKEEGLKAFYKGVAPLWMRQIPYTMMKFACFERTVEALYKFVVPKPRSECSKPEQLVVTFVAGYIAGVFCAIVSHPADSVVSVLNKEKGSSASLVLKRLGFKGVWKGLFARIIMIGTLTALQWFIYDSVKVYFRLPRPPPPEMPESLKKKLGLTQ
Protein: Heme chaperone HemW (P54304)
Organism: Bacillus subtilis (strain 168)
Function: Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9CGF7}.
Interaction partners:
- Coproporphyrinogen III oxidase
- Elongation factor 4
- Uroporphyrinogen decarboxylase
- Oxygen-independent coproporphyrinogen-III oxidase-like protein HemZ
- Coproporphyrin III ferrochelatase
- Probable dual-specificity RNA methyltransferase RlmN
- Heat-inducible transcription repressor HrcA
Sequence:
MKSAYIHIPFCEHICHYCDFNKYFIQSQPVDEYLNALEQEMINTIAKTGQPDLKTIFIGGGTPTSLSEEQLKKLMDMINRVLKPSSDLSEFAVEANPDDLSAEKLKILKEAGVNRLSFGVQTFEDDLLEKIGRVHKQKDVFTSFERAREIGFENISLDLMFGLPGQTLKHLEHSINTALSLDAEHYSVYSLIVEPKTVFYNLMQKGRLHLPPQEQEAEMYEIVMSKMEAHGIHQYEISNFAKAGMESKHNLTYWSNEQYFGFGAGAHGYIGGTRTVNVGPVKHYIDLIAEKGFPYRDTHEVTTEEQIEEEMFLGLRKTAGVSKKRFAEKYGRSLDGLFPSVLKDLAEKGLIHNSESAVYLTHQGKLLGNEVFGAFLGEL
Protein: Na[+]/H[+] hydrogen antiporter 2, isoform B (A0A0B4K6G5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSSDSDILDVVAGSEGPPLQAFRSSNPFEDSYQMSSCQQDFERDRDANLTPLHMLRRASETVTASILEPEKEHLLGDKPQVPPRAHGSTAPSAIEAKRSRQQPNQWQLQQQQQPSSNNNNTKRALAPGDNMTQGAAPQDSQGDILPTRPLHTKLDIQKIPEDEAGADATQNAATIILTPTSLNLTNTTTQNVAANNAGNSSTTTSTNTNYGPGSVSGYPTPNATPGDEYKGPKWWLYIRSHWVNTSELVALLAIFLGLWAMGWVLLPEYSQPPTVIMRIAFLFVGAQISGILVTFVHLPDMLGMLFFGVLYANLGLANFEGYQKFELFLREMALINIMLLAGLGLDGDAFKRLWFMILRLTLLPTIVEVAAIAGLANLTLSMPWLWGIALGLVITAVSPNVVVTVMLKLKEDRLGLNSGIHTLIYAMTTCNDVVAIFMFGVIISVIFSTTSLTQQVLQGPIGIGIGLVFGYLYGSMLQYLPSRNATYANGLRFVLTILGGTIAVMGSRVIGYTSAGALGCVTTAFIARIGWRREETRLTPQQLQAQQIASVPKRLDLMWKFLKPVSFALIGKEINFNVLQGHVIGYGALLVLVGSLFRLAFAYLSTYGGNLSRKERAYITISGFPKATVQAALGPVALDMARAASVASPEQLALAGNLLIISVLAIIFTAPLGAILMLRLAPYWLKHGDAVEAVDSPTTPIAPTLGSTNSSKGT
Protein: Dicer1 protein (Q4G034)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
EDDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTSCGERAAQLFLCSLGLKVLPVIKRTSRDKASYPAQENSSSQQKSPSGSCAAAVSPRSSAGKDLEYGCLKIPPRCMFDHPDAEKTLNHLISGFENFEKKINYIFKNKAYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLEVVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVELVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPLVPNS
Protein: Sec-independent protein translocase protein TATB, chloroplastic (Protein HIGH CHLOROPHYLL FLUORESCENCE 106) (Protein TWIN-ARGININE TRANSLOCATION B) (O48950)
Organism: Zea mays (Maize)
Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across the thylakoid membrane. Involved in delta pH-dependent protein transport required for chloroplast development, especially thylakoid membrane formation. TATC and TATB mediate precursor recognition, whereas TATA facilitates translocation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305|PubMed:9367960}; Single-pass membrane protein {ECO:0000305|PubMed:9367960}. Note=The C-terminus is located in the stroma.
Interaction partners:
- Sec-independent protein translocase protein TATC, chloroplastic
- Preprotein translocase subunit SECY, chloroplastic
- Small ribosomal subunit protein uS17c
- Sec-independent protein translocase protein TATA, chloroplastic
Sequence:
MTPTANLLLPAPPFVPISDVRRLQLPPRVRHQPRPCWKGVEWGSIQTRMVSSFVAVGSRTRRRNVICASLFGVGAPEALVIGVVALLVFGPKGLAEVARNLGKTLRAFQPTIRELQDVSREFRSTLEREIGIDEVSQSTNYRPTTMNNNQQPAADPNVKPEPAPYTSEELMKVTEEQIAASAAAAWNPQQPATSQQQEEAPTTPRSEDAPTSGGSDGPAAPARAVSDSDPNQVNKSQKAEGER
Protein: Mesenteric estrogen-dependent adipogenesis protein (Activated in W/Wv mouse stomach 3 homolog) (hAWMS3) (Mesenteric estrogen-dependent adipose 4) (MEDA-4) (Q5VYS4)
Organism: Homo sapiens (Human)
Function: Involved in processes that promote adipocyte differentiation, lipid accumulation, and glucose uptake in mature adipocytes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22510272}.
Interaction partners:
Sequence:
MAGAACEPVARPSLTSISSGELRSLWTCDCELALLPLAQLLRLQPGAFQLSGDQLVVARPGEPAAARGGFNVFGDGLVRLDGQLYRLSSYIKRYVELTNYCDYKDYRETILSKPMLFFINVQTKKDTSKERTYAFLVNTRHPKIRRQIEQGMDMVISSVIGESYRLQFDFQEAVKNFFPPGNEVVNGENLSFAYEFKADALFDFFYWFGLSNSVVKVNGKVLNLSSTSPEKKETIKLFLEKMSEPLIRRSSFSDRKFSVTSRGSIDDVFNCNLSPRSSLTEPLLAELPFPSVLESEETPNQFI
Protein: Inactive tyrosine-protein kinase transmembrane receptor ROR1 (mROR1) (Neurotrophic tyrosine kinase, receptor-related 1) (Q9Z139)
Organism: Mus musculus (Mouse)
Function: Has very low kinase activity in vitro and is unlikely to function as a tyrosine kinase in vivo (By similarity). Receptor for ligand WNT5A which activate downstream NFkB signaling pathway and may result in the inhibition of WNT3A-mediated signaling (By similarity). In inner ear, crucial for spiral ganglion neurons to innervate auditory hair cells.
Subcellular location: Membrane {ECO:0000269|PubMed:27162350}; Single-pass type I membrane protein. Cell projection, axon {ECO:0000269|PubMed:27162350}.
Interaction partners:
- Protein Wnt-5a
- Tyrosine-protein kinase transmembrane receptor ROR2
- Frizzled-1
- Frizzled-2
- Frizzled-8
- Frizzled-4
- Frizzled-7
- Frizzled-5
- Frizzled-10
- Frizzled-3
Sequence:
MHRPRRRGTRPPPLALLAALLLAARGADAQETELSVSAELVPTSSWNTSSEIDKGSYLTLDEPMNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATNGKKVVSTTGVLFVKFGPPPTASPGSSDEYEEDGFCQPYRGIACARFIGNRTVYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSSVPKPRDLCRDECEVLENVLCQTEYIFARSNPMILMRLKLPNCEDLPQPESPEAANCIRIGIPMADPINKNHKCYNSTGVDYRGTVSVTKSGRQCQPWNSQYPHTHSFTALRFPELNGGHSYCRNPGNQKEAPWCFTLDENFKSDLCDIPACDSKDSKEKNKMEILYILVPSVAIPLAIAFLFFFICVCRNNQKSSSPPVQRQPKPVRGQNVEMSMLNAYKPKSKAKELPLSAVRFMEELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRSWEGLSSHTSSTTPSGGNATTQTTSLSASPVSNLSNPRFPNYMFPSQGITPQGQIAGFIGPAIPQNQRFIPINGYPIPPGYAAFPAAHYQPAGPPRVIQHCPPPKSRSPSSASGSTSTGHVASLPSSGSNQEANVPLLPHMSIPNHPGGMGITVFGNKSQKPYKIDSKQSSLLGDSHIHGHTESMISAEV
Protein: Suppressor APC domain-containing protein 2 (Tumor specificity and mitosis phase-dependent expression protein) (TS/MDEP) (p42.3) (Q86UD0)
Organism: Homo sapiens (Human)
Function: Plays a role in planar mitotic spindle orientation in retinal progenitor cells (RPCs) and promotes the production of symmetric terminal divisions (By similarity). Negatively regulates the mitotic apical cortex localization of GPSM2. Involved also in positive regulation of cell proliferation and tumor cell growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17525738}. Nucleus {ECO:0000269|PubMed:17525738}. Cytoplasm, cell cortex {ECO:0000269|PubMed:26766442}. Apical cell membrane {ECO:0000250|UniProtKB:Q9D818}. Cell junction, tight junction {ECO:0000269|PubMed:26766442}. Note=Localized at the apical cortical region during the M phase. In horizontally retinal progenitor dividing cells, localized at the pole cortical region from prophase to telophase cells. In vertically retinal progenitor dividing cells, not detected at the pole cortical region at any stage of mitosis. {ECO:0000250|UniProtKB:Q9D818}.
Interaction partners:
Sequence:
MAGAAMAERGRVPPPAPAPSTEGLPRAFLQSLRTLFDILDDRRRGCVHLREIESRWQGTDARELPRGVLEGLRQVAPASGYLTFERFVAGLRTSLLSADGGPRDPTRAPARPGDQPPPPPQRLVFAPADEPRTVLERKPLPLGVRAPLAGPSAAARSPEQLCAPAEAAPCPAEPERSQSAALEPSSSADAGAVACRALEADSGDARRAPRARGERRRHTIASGVDCGLLKQMKELEQEKEVLLQGLEMMARGRDWYQQQLQRVQERQRRLGQSRASADFGAAGSPRPLGRLLPKVQEVARCLGELLAAACASRALPPSSSGPPCPALTSTSPPVWQQQTILMLKEQNRLLTQEVTEKSERITQLEQEKSALIKQLFEARALSQQDGGPLDSTFI
Protein: Plasma alpha-L-fucosidase (EC 3.2.1.51) (Alpha-L-fucoside fucohydrolase 2) (Alpha-L-fucosidase 2) (Q9BTY2)
Organism: Homo sapiens (Human)
Function: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Tissue alpha-L-fucosidase
- Beta-galactosidase
Sequence:
MRPQELPRLAFPLLLLLLLLLPPPPCPAHSATRFDPTWESLDARQLPAWFDQAKFGIFIHWGVFSVPSFGSEWFWWYWQKEKIPKYVEFMKDNYPPSFKYEDFGPLFTAKFFNANQWADIFQASGAKYIVLTSKHHEGFTLWGSEYSWNWNAIDEGPKRDIVKELEVAIRNRTDLRFGLYYSLFEWFHPLFLEDESSSFHKRQFPVSKTLPELYELVNNYQPEVLWSDGDGGAPDQYWNSTGFLAWLYNESPVRGTVVTNDRWGAGSICKHGGFYTCSDRYNPGHLLPHKWENCMTIDKLSWGYRREAGISDYLTIEELVKQLVETVSCGGNLLMNIGPTLDGTISVVFEERLRQMGSWLKVNGEAIYETHTWRSQNDTVTPDVWYTSKPKEKLVYAIFLKWPTSGQLFLGHPKAILGATEVKLLGHGQPLNWISLEQNGIMVELPQLTIHQMPCKWGWALALTNVI
Protein: Neurotransmitter-gated ion-channel transmembrane domain-containing protein (Q0PDK2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTVLTETHLMTGTNRRLPPVAYVKAVDVFLGFCYLLVILALIEYACVAYSKKKNEDRRRREKKTEHKPAPPTPDILHDVRLAECTCNAAPTSIIAVIKQSNRFCVSHSHIDIVSRAAFPLVFILFNTLFWLILLYKSKRLPYISEHEGDRCDAPDLH
Protein: Retinoblastoma-related protein 1 (NbRBR1) (Q66WV0)
Organism: Nicotiana benthamiana
Function: Regulator of biological processes that recruits a histone deacetylase to control gene transcription. Formation of stable complexes with geminiviridae replication-associated proteins may create a cellular environment which favors viral DNA replication (By similarity). May play a role in the entry into mitosis, negatively regulating the cell proliferation during leaf, stem, and flower development. Critical regulator of the endocycle.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MVELNNCSNSEETGGVDSLEVRFTDFCKNGLSMGESFVTEATKLFNDSKHLLLSNNSTIGVITQEGVERYWFVFVLYSVKRLSEKEAGNSNNGDKGNAFSLCQILRGAKLNVVDFFKELPQFILKVGPTLSNLYGSDWEKRLEVKELQTNFVHLSLLSKYYKRAYQELFLASGNNEDKPSATSNSAIHLPQYYRFGWLLFLSLRIHVFSRFKDLVTCTNGLVSVLAILMIHVPVRFRNFNIDDSSRFVKKGDKVDLLASLSKIYQTSIDDLRETMDKVNNLITEKLKKKPCLASEFRTENLDNLDTDGLTYFEDLMEESCLSSSVSTLEKDYSDAIQNKGELDERIFVNEEDSLLGSGSLSGGAVNMNGTKRKFDAMASPAKTVTSTLSPYRSPNCANSKMTAATPVSTAMTTARWLRTVIAPLQPKPSAELERFLSSCDRDVTADVIRRAQIILEAIFPSSGPAEHCAAGGSLQSTSLMDNIWAEQRRSEALKLYYRVLQTMCTAESQILNGNNLTSLLTNERFHRCMLACSAELVLATHKTVTMLFPAVLERTGITAFDLSKVIESFIRHEESLPRELRRHLNSLEERLLESMVWEKGSSMYNSLAVAKPSLAAEINRMGLLAEPMPSLDAIAMHINLSSGSLPPLPSLHKNNLAPNGQIGDIRSPKKVCSEYRSVLVERNSFTSPVKDRFLALNNIKSKFPPPALHSAFASPTRPNPGGGGETCAETAINVFFGKIVKLAAVRINGMIERLQLSQQIRETVYCLFQKILSQRTSLFFNRHIDQIILCSFYGVAKISQLNLTFKEIICNYRKQPQCKPQVFRSVFVDWTLARHNVRTGADHVDIITFYNEMFIPSVKPLLVELAPAGNNSEKNDHNDGQGPASPKPSPFPKLPDMSPKKVSAVHNVYVSPLRASKMDALISHSSKSYYACVGESTHAYQSPSKDLDVINNRLNGNRKLRGALNFDVDAGLVSDSIVANSLYLQNGNCRSPVAHVKTEQPES
Protein: Adaptive-response sensory kinase SasA (EC 2.7.13.3) (Sensor histidine kinase Hik8) (Sensor histidine kinase SasA) (Q55630)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Member of the two-component regulatory system SasA/RpaA involved in genome-wide circadian gene expression. One of several clock output pathways. Participates in the Kai clock protein complex, the main circadian regulator in cyanobacteria, via its interaction with KaiC. KaiC enhances the autophosphorylation activity of SasA, which then transfers its phosphate group to RpaA to activate it. In addition to its output function, recruits fold-shifted KaiB (KaiB(fs)) to KaiC to cooperatively form the KaiB(6):KaiC(6) complex (independent of SasA kinase activity). Required for robustness of the circadian rhythm of gene expression and is involved in clock output, also required for adaptation to light/dark cycles.
Interaction partners:
- DNA-binding dual master transcriptional regulator RpaA
- NarL subfamily
- CheY subfamily
- Putative sensor protein KdpD
- Slr1142 protein
- histidine kinase
- CheY subfamily
- OmpR subfamily
- Probable transcriptional regulator ycf27
- Circadian clock oscillator protein KaiC 1
Sequence:
MSSSSELGNASSVPLQFLLFIDDRPNSQDSVQEIGQCLTNLLDGHSHDLQILQISKHPHLVEHFRLVATPSLIKLQPEPRQVLAGSNIIQQLQKWWPRWQQELAMDPNPEDTGQSPSCPREISSVGYSGELMKMSDELFLLKKDKEELLQQIQFKDQILAMLAHDLRSPLTAASIAVDTLELLQHKPIEEQKPALRSQLLYQARKQFKIMDRLIEDILQASKNLNSQFQVHGRPLAIADLCQEVLELYQAKFSKKNLTITYDIPKDLPNVFADEELIRQVIANLLDNAIKYTPAHGSITVGALHRTTQKVQVSITDNGPGIPNSKQETIFEGHFRLQRDEQTDGYGLGLSLCRKIIQAHYGQIWVDSRPKQGSSFHFTLPVYR
Protein: Valacyclovir hydrolase (VACVase) (Valacyclovirase) (EC 3.1.-.-) (Biphenyl hydrolase-like protein) (Biphenyl hydrolase-related protein) (Bph-rp) (Breast epithelial mucin-associated antigen) (MCNAA) (Q86WA6)
Organism: Homo sapiens (Human)
Function: Serine hydrolase that catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. Activates valacyclovir to acyclovir. May play a role in detoxification processes. It is a specific alpha-amino acid ester hydrolase that prefers small, hydrophobic, and aromatic side chains and does not have a stringent requirement for the leaving group other than preferring a primary alcohol.
Interaction partners:
Sequence:
MVAVLGGRGVLRLRLLLSALKPGIHVPRAGPAAAFGTSVTSAKVAVNGVQLHYQQTGEGDHAVLLLPGMLGSGETDFGPQLKNLNKKLFTVVAWDPRGYGHSRPPDRDFPADFFERDAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYFARTCEKWVDGIRQFKHLPDGNICRHLLPRVQCPALIVHGEKDPLVPRFHADFIHKHVKGSRLHLMPEGKHNLHLRFADEFNKLAEDFLQ
Protein: Transcriptional repressor tup12 (Q9UUG8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transcriptional repressor.
Interaction partners:
- General transcriptional corepressor ssn6
- Transcription factor atf1
- Transcriptional repressor tup11
- Transcription factor pcr1
- Iron-sensing transcriptional repressor
- Zinc finger protein rst2
- Dual specificity protein kinase lkh1
- Set1 complex component ash2
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Set1 complex component swd1
Sequence:
MLFLVISQTTSFMITVRQFTFTIFKFQFMATSNVSSRVNELLEAVKKEFEDICQKTKTVEAQKDDFEYKAMISAQINEMALMKQTVMDLEMQQSKVKDRYEEEITSLKAQLEARRKEIASGVVPQSSKTKHGRNSVSFGKYGNAGPFNSDNSSKPLILNNGSSGGTPKNLRSPAIDSDGTVLAPIQTSNVDLGSQYYSSPHVRPAVGATMAGSAMRTFPSNLPLGHPPPPSDSANSSVTPIAAPLVVNGKVSGNPPYPAEIIPTSNVPNREEKDWTVTSNVPNKEPPISVQLLHTLEHTSVICYVRFSADGKFLATGCNRAAMVFNVETGKLITLLQEESSKREGDLYVRSVAFSPDGKYLATGVEDQQIRIWDIAQKRVYRLLTGHEQEIYSLDFSKDGKTLVSGSGDRTVCLWDVEAGEQKLILHTDDGVTTVMFSPDGQFIAAGSLDKVIRIWTSSGTLVEQLHGHEESVYSVAFSPDGKYLVSGSLDNTIKLWELQCVSNVAPSMYKEGGICKQTFTGHKDFILSVTVSPDGKWIISGSKDRTIQFWSPDSPHSQLTLQGHNNSVISVAVSPNGHCFATGSGDLRARIWSYEDL
Protein: FI21203p1 (FI21627p1) (Meiotic 218, isoform B) (Meiotic 218, isoform C) (Meiotic 218, isoform D) (Meiotic 218, isoform E) (Q0KHR4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- DNA replication licensing factor Mcm3
- DNA replication licensing factor Mcm5
- DNA replication licensing factor Mcm2
- DNA replication licensing factor Mcm7
- DNA replication licensing factor REC
- Meiotic 217
- DNA replication licensing factor MCM4
- Cell division control protein
- Double parked, isoform A
- Chromosome transmission fidelity 4
Sequence:
MSSTNKLEKKDPRRHIPLQLNVFLRNDDDGEVREVTQNANTSSIGTIPSNGLVESDVTPIMTPTPKAGVYKPNVNVWRLSKEVTKPDRSFVVSAEEYPDLGQRPKRFKQRTPRVRNQDDGGTVSCLASRFSRVKDPPVLGNFLPDFMLPKSSNSNHQSVTTWLSSVRPSDSQKSLSDQARCSSSTNITLLSKDSVQPLTPKSSAQSSPGEKNIQQEQNTPAKSQQEETSPANSVEHQQKTPNSPKEQQKSSVGFTNMQQMASANSLQQQNSSASSLQQQNSSVHSLQKRKSWVNSSQQQRSSVNFIQKQRSWVNSSHHQKSSASSLQQKSSENSPSKFQQQQQKSPANNERSQNNQKSPGIQHSWKQQQQQKPKILQNCPKTSVQQQMNPVNHTQSQSERPTELIYLHSRSPAKRASVTNNSSAPIRIAPRQQTTQSSGPSVVHNEDEDVMPPTPNQSERRQRRFPRRNHNPRMVRSLQAVSREFTESLLEGSSGKTPEKEVVPYQQQEKPRQVKSSPEIHASSHMRKLAMGSVLNSNAKEFHPTGESHLTHKVSRLSQRRCRQRFTRSLHAKKNNPREQLPNPDSAPEPILEYTSEIDDQPCPPRQTVDTPIEAIVPPAMIEVSATGNLPPVFYFDQQSGIIWSNSSPQIPVEIQSNSVSQSVFRLASLPCTGVGTTNMDIFTSSPPPIQHMSSSRLPSSISGPTQLSHTLSSPPVENQHQQHLWESCIHQDEDLMYSRPLLDMDQEETQPEQQDQEWQWESEIEPPSFQSENQVVADEHGEENAYLAKDAGPPLERHMIFRAPSQHGQEYPKPDLNCVPSSIKKLHHLISSQYSDYSFVYALSAQISQDCVPMDCFVYLKMILLASIVSIESDEVRAPISLCIIATDSLMANRLLNKVGQLAPRFLGPHEYGLQPTFNALPTRFNWIVASPLLLAQQGVYYAGDWNRLSKDQGCQLEKCIENGAVPVPQLHIDQPLKAAVWTYWQPNNSTNQTLALAKLCPIFGLPIYMGAQASNSLWNSIIQKHNAEGQIVVNDGLSIPEDDMRMLIHLLHQRKTTLTDGAQHMLQKYYVISRKERPNVFSSKTYIVLKQLAECFAKLALRLEVLESDVCVAIFHCEHFVQGIFGAKENQAPPAVFNFNVISCIDPYMNKFTRWLLQYLNSYEDEELGMHADKRRRTDSWDMP
Protein: Long-chain fatty acid transport protein 2 (Arachidonate--CoA ligase) (EC 6.2.1.15) (Fatty acid transport protein 2) (FATP-2) (Fatty-acid-coenzyme A ligase, very long-chain 1) (Long-chain-fatty-acid--CoA ligase) (EC 6.2.1.3) (Phytanate--CoA ligase) (EC 6.2.1.24) (Solute carrier family 27 member 2) (THCA-CoA ligase) (EC 6.2.1.7) (Very long-chain acyl-CoA synthetase) (VLACS) (VLCS) (EC 6.2.1.-) (Very long-chain-fatty-acid-CoA ligase) (O14975)
Organism: Homo sapiens (Human)
Function: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport across cell membranes, playing an important role in hepatic fatty acid uptake. Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake. Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. Can also activate branched-chain fatty acids such as phytanic acid and pristanic acid. May contribute to the synthesis of sphingosine-1-phosphate. Does not activate C24 bile acids, cholate and chenodeoxycholate. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. However, it is not critical for THCA activation and bile synthesis in vivo.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11980911, ECO:0000269|PubMed:22022213, ECO:0000269|PubMed:24269233}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:10198260, ECO:0000269|PubMed:10640429}; Peripheral membrane protein {ECO:0000269|PubMed:10640429}. Cell membrane {ECO:0000269|PubMed:20530735}; Multi-pass membrane protein {ECO:0000255}. Microsome {ECO:0000269|PubMed:10640429}.
Interaction partners:
- ATP-binding cassette sub-family D member 1
- Long-chain-fatty-acid--CoA ligase 1
- Long-chain-fatty-acid--CoA ligase ACSBG1
- Peroxisomal acyl-coenzyme A oxidase 1
- Long-chain-fatty-acid--CoA ligase 4
- ATP-binding cassette sub-family D member 2
- ATP-binding cassette sub-family D member 3
- Lysosomal cobalamin transporter ABCD4
- Sterol carrier protein 2
- Bifunctional coenzyme A synthase
Sequence:
MLSAIYTVLAGLLFLPLLVNLCCPYFFQDIGYFLKVAAVGRRVRSYGKRRPARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVTFSTPALYIYTSGTTGLPKAAMITHQRIWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKIITYDLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVCKITQLTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFNPAVIKDALYFLDDTAKMYVPMTEDIYNAISAKTLKL
Protein: Low density lipoprotein receptor-related protein 3 (E9Q711)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane, coated pit {ECO:0000256|ARBA:ARBA00037878}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MEKRAAAGPEGAPGARAPLAVVCLVNLFLTGRLSSAVPALAACSGKLEQHTERRGVIYSPAWPLNYPPGTNCSWYIQGDRGDMITISFRNFDVEESHQCSLDWLLLGPAAPPRQEAFRLCGSAIPPAFISARDHVWIFFHSDASSSGQAQGFRLSYIRGKLGQTSCQTDEFRCDNGKCLPGPWQCNMVDECGDGSDEGNCSAPASEPPGSLCPGGTFPCSGARSTRCLPVERRCDGTQDCGDGSDEAGCPDLACGRRLGSFYGSFASPDLFGAARGPSDLHCTWLVDTQDPRRVLLQLELRLGYDDYVQVYEGLGERGDRLLQTLSYRSNHRPVSLEAAQGRLTVAYHARARSAGHGFNATYQVKGYCLPWEQPCGSSEGDDDSTGEQGCFSEPQRCDGWWHCASGRDEQGCPACPPDQYPCEGGSGLCYAPADRCNNQKSCPDGADEKNCFSCQPGTFHCGTNLCIFETWRCDGQEDCQDGSDEHGCLAAVPRKVITAALIGSLVCGLLLVIALGCAFKLYSLRTQEYRAFETQMTRLEAEFVRREAPPSYGQLIAQGLIPPVEDFPVYSASQASVLQNLRTAMRRQMRRHASRRGPSRRRLGRLWNRLFHRPRAPRGQIPLLTAARTSQTVLGDGLLQAAPGPVPEPPAPNTDTGSPREAGDGPPSGSGHAPEVGPSVPPPPLNLRDPEYRPEDKERKACVEPLEDSPAPVDTPPEPCLAQDPHPQTPTASGTQDPHSAEPLGVCRSPPPPCSPILEASDDEALLVC
Protein: Coiled-coil domain containing 24 (Q3V0I8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLKALLQEIQSSQVSNSDPPSLLAPPPLLRDLIRQELRQLLQGLRLKAISEGRDQTQMWAQYSPRVLRFALEDTRCDSTQQELPMRADEPRAGMNNTERVMVTSPVSTCPRDLTVIKDQLNVSNIDQVVRHLRSLLEEECHMLQNEISDLQHCLEMEQMQACQPSKDTQMPTLGEIKDQKAAMERELQVSLGPSCTAAKHRQKPLRSSIPSLRPFPCLHGYMPTPPSERCPHPQGQTSTRRWGRQLRYSYRKETTSTSVSSAASQAPT