wanglab/gogpt-training-data huggingface dataset:
Protein: Proteasome subunit alpha type-6 (Macropain subunit PRE5) (Multicatalytic endopeptidase complex subunit PRE5) (Proteasome component PRE5) (Proteinase YSCE subunit PRE5) (P40302)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase RPN11
- 26S proteasome regulatory subunit RPN1
- Proteasome subunit alpha type-3
- 26S proteasome regulatory subunit RPN10
- Proteasome subunit beta type-6
- 26S proteasome regulatory subunit RPN6
- 26S proteasome regulatory subunit RPN12
- Proteasome maturation factor UMP1
- 26S proteasome regulatory subunit RPN5
- Proteasome subunit beta type-4
Sequence:
MFRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLDTFIKIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI
Protein: Dyschronic, isoform J (M9PI53)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
MRLGGSGIPYDGDPLTMSAAGNDYAELCDLGPSRWSARPYGYNATAAAAASFGLGPSMGGTQSSSSVPTGGSAGLSGHHLRSSGAPGPSSFEAEDIGMAFGMISPPPGSGPYVGSSAAAGGSRVGNSTSSLRGAGGRSGLYYSPPGTSYTIVERPHSPHYYFNSAGVPTKGGSLPGRGSAYLSSSPASHMAAGTAGTLPTSTAASGRSMGQHASSNGNKKRPISPEQVLRMFGATQSSSVPTSSYHYSNGGTRDRDRTGRRSPASSPPSTTHQIYRDRERERDRSVPNIHELTTRTVSMSRDQQIDHGFGICVKGGKDSGLGVYISRIEENSVAERAGLRPGDTILEVNGTPFTSINHEEALKILKSSRQISMTVRAPPTLNSTAPLHGFGPPSRDPMYASMAPPLHPQNQAAAAAAAAAASGAGLPFRQTCSWMDRHGRPASPPMEYGGRRSERRDRIRRVELLIEPGQSLGLMIRGGVEYGLGIFVTGVDKDSVADRSGLMIGDEILEVNGQSFLDVTHDEAVGQLKYHKRMSLVIRDVGKVPHSCTSIEMEPWDAYSPTGTRARRKGQIATMVEEKARSLLPRHHFASLSYYIAEYSAKAMTIDAFVAVLLEMLDTYEKHTLVTEIRELVFPEDRTRYDELVYRRERDPYSVDRHRRKGDPARDLPVTADDLEIIAATGRSPSSDSGLGMTVTDIYKRPALQLPHRPMSAGPILHRSQPASHYQTGSNQSSSSLSPPQQQQQQQQHYQPHHASLRHLGGIGGNVGSGRHHHHPLGPSQLKFRQTKDNQQQEYGCDEHRTRRGSETLLPEYEPDAGGYLDGLRSHLGGLTQRVKSWYWGRPLSMQRLSAEQNGGSTTEQTHEHNPNVVPDHRGNLHITVKKTKPILGIAIEGGANTKHPLPRIINIHENGAAFEAGGLEVGQLILEVDGTKVEGLHHQEVARLIAECFANREKAEITFLVVEAKKSNLEPKPTALIFLEA
Protein: Formate dehydrogenase, nitrate-inducible, major subunit (EC 1.17.5.3) (Anaerobic formate dehydrogenase major subunit) (Formate dehydrogenase-N subunit alpha) (FDH-N subunit alpha) (P24183)
Organism: Escherichia coli (strain K12)
Function: Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).
Subcellular location: Periplasm {ECO:0000269|PubMed:11884747}.
Interaction partners:
- Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit
- Formate dehydrogenase, nitrate-inducible, cytochrome b556
- Formate dehydrogenase-O iron-sulfur subunit
- Formate dehydrogenase, cytochrome b556
- Protein FdhE
- Respiratory nitrate reductase 1 alpha chain
- Formate dehydrogenase-O major subunit
- Sulfur carrier protein FdhD
- Probable Ni/Fe-hydrogenase 2 b-type cytochrome subunit
- Selenocysteine-specific elongation factor
Sequence:
MDVSRRQFFKICAGGMAGTTVAALGFAPKQALAQARNYKLLRAKEIRNTCTYCSVGCGLLMYSLGDGAKNAREAIYHIEGDPDHPVSRGALCPKGAGLLDYVNSENRLRYPEYRAPGSDKWQRISWEEAFSRIAKLMKADRDANFIEKNEQGVTVNRWLSTGMLCASGASNETGMLTQKFARSLGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANVVMVMGGNAAEAHPVGFRWAMEAKNNNDATLIVVDPRFTRTASVADIYAPIRSGTDITFLSGVLRYLIENNKINAEYVKHYTNASLLVRDDFAFEDGLFSGYDAEKRQYDKSSWNYQLDENGYAKRDETLTHPRCVWNLLKEHVSRYTPDVVENICGTPKADFLKVCEVLASTSAPDRTTTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLLSTSLPGYLTLPSEKQVDLQSYLEANTPKATLADQVNYWSNYPKFFVSLMKSFYGDAAQKENNWGYDWLPKWDQTYDVIKYFNMMDEGKVTGYFCQGFNPVASFPDKNKVVSCLSKLKYMVVIDPLVTETSTFWQNHGESNDVDPASIQTEVFRLPSTCFAEEDGSIANSGRWLQWHWKGQDAPGEARNDGEILAGIYHHLRELYQSEGGKGVEPLMKMSWNYKQPHEPQSDEVAKENNGYALEDLYDANGVLIAKKGQLLSSFAHLRDDGTTASSCWIYTGSWTEQGNQMANRDNSDPSGLGNTLGWAWAWPLNRRVLYNRASADINGKPWDPKRMLIQWNGSKWTGNDIPDFGNAAPGTPTGPFIMQPEGMGRLFAINKMAEGPFPEHYEPIETPLGTNPLHPNVVSNPVVRLYEQDALRMGKKEQFPYVGTTYRLTEHFHTWTKHALLNAIAQPEQFVEISETLAAAKGINNGDRVTVSSKRGFIRAVAVVTRRLKPLNVNGQQVETVGIPIHWGFEGVARKGYIANTLTPNVGDANSQTPEYKAFLVNIEKA
Protein: 40S ribosomal protein rpS31e (E6PBU9)
Organism: Tetrahymena thermophila
Interaction partners:
Sequence:
MQVQVKTLEGETKIYTLEQGTSVLDLKSQISQDMGFEIDMMTLVNNGFIAPNTELVTDDVTYYLSLKLLGGKKKKKKKSYTTKKKTKHRHVHTKLGALAFYKLENNGKVSLQQKGCPKCGPGIFMAKHYDRHYCGKCHLTLKIDAETAKKNLEELKKKQDAKKSGAAATDAGAGGAGKKDAKKGKKGKK
Protein: Aly/REF export factor 2 (Alyref) (RNA and export factor-binding protein 2) (Q9JJW6)
Organism: Mus musculus (Mouse)
Function: Export adapter involved in spliced and unspliced mRNA nuclear export. Binds mRNA which is transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway); enhances NXF1-NXT1 RNA-binding activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q86V81}. Cytoplasm {ECO:0000250|UniProtKB:Q86V81}.
Interaction partners:
- Spliceosome RNA helicase Ddx39b
- THO complex subunit 1
- Nuclear RNA export factor 1
- SAP domain-containing ribonucleoprotein
- THO complex subunit 5 homolog
- THO complex subunit 2
- THO complex subunit 3
- Eukaryotic initiation factor 4A-III
- Serine/arginine-rich splicing factor 1
- Tip-associated protein
Sequence:
MADKMDMSLDDIIKLNRNQRRVNRGGGPRRNRPAIARGGRNRPAPYSRPKPLPDKWQHDLFDSGCGGGEGVETGAKLLVSNLDFGVSDADIQELFAEFGTLKKAAVDYDRSGRSLGTADVHFERRADALKAMKQYKGVPLDGRPMDIQLVASQIDPQRRPAQSGNRGGMTRSRGSGGFGGRGSQGRGRGTGRNSKQQQLSAEELDAQLDAYNARMDTS
Protein: Deoxyribonucleoside regulator (P39140)
Organism: Bacillus subtilis (strain 168)
Function: Negative regulator of the dra-nupC-pdp operon. DeoR binds cooperatively to the operator DNA, which consists of a palindrome and a direct repeat sequence located 3' to the palindrome.
Interaction partners:
- Pyrimidine-nucleoside phosphorylase
- Nucleoside permease NupC
- Deoxyribose-phosphate aldolase
- HTH-type transcriptional repressor CutR
- Gluconate operon transcriptional repressor
Sequence:
MDREKQQLSIEAARLYYQSDYSQQQIAEQLNISRPTVSRLLQYAKEKGYVQIRVMDPFEDLDALGSILEEKYGLLEAHVVFSPTPDYAGITHDLSRYGAEYMHETVKDGDIVGVSWGTTMYQIAQNMQPKQVKGVEVVQLKGGISHSRVNTYSAETIQLFAEAFQTMPRYLPLPVVFDNADVKRMVEKDRHIERIIEMGKQANIALFTVGTVRDEALLFRLGYFNEEEKALLKKQAVGDICSRFFDAKGNICSSAINDRTIGVELQDLRLKERSILVAGGSRKVSSIHGALTGKYANVLIIDQHTARALVNDL
Protein: Uncharacterized MFS-type transporter C530.15c (O74829)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAERTSESSSESASFDLEKQQSNHHDRYQSSVSSELEESLKKYPVISNPQDFIVTLDGPDDPDLAVNWPLAKKLRNVAVMGSACLCAGFGSSIFSGAVPEVMVKFHVCRTVALLGISLYVLGFASGPVVWAPMCELFGRRRPMIIAVFIFCIFHIAVATAKDIQTVMICRFFCGFFGSSPITTVAGSFSDMFSARTRGLVIAVYSAIIFNGPLMSPIVGGFIGKSYLGWRWTSYITAIMGFTAFTSMIIFHRETYTRTITEIRASKVRVLTGNYCLHAKSEEEPLEFSYFFHKYFTFPLRLLIFEPILLVVSTYTAFVYGILYGLLEAYPVIFGESRKWRLGVESLPYLAIFVGVCIGCSSVALFQPYYFKKMDENKGRPVPEARLPSMMIGCIVFPIGIFWLAWTGNYPWIHWIVPTLAGSFIGFGIITIFQQTINYIIDCYSGCSASAIAANTLLRSSFGAAFPLFTTQMFNNLGIGWAGSLVGFVAVGLIPVPFMLFLYGPKLRQMSKHCLKD
Protein: DnaJ heat shock protein family (Hsp40) member B6a (DnaJ homolog subfamily B member 6a) (Zgc:92148) (Q6DHR2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock cognate 71 kDa protein
- Immunoglobulin binding protein
- Heat shock protein 9
- Heat shock 70 kDa protein 14
- Heat shock 70 kDa protein 4a
- Si:ch211-199o1.2
- Novel protein similar to heat shock cognate 70-kd protein
- Heat shock cognate 71 kDa protein
- Heat shock cognate 71 kDa protein
Sequence:
MADYYQVLGVQKTASPDDIKKAYRKLALRWHPDKNPDNKEDAEKKFKELSEAYEVLSDANKRSLYDRYGKEGLTPGGGGGREHHFGGGGFTFRNPEDVFREFFGGQDPFADFFGADPFGDDFFGGRRHYHHHHQRGMSRSRTGGSFFGGFGGFPPFGAGFTSFDAGFTPFGHMGGGFTSFSTSSFGGGGGGGGGGGGGGGGMGSFRSVSTSTKFINGRKITTKRIFENGQERVEVEEDGQLKSLTINGKAQDIGMLDCQRQRKELPDSSSSSSSSSHSARHSAQREEQNRTPGKEQSGVKRKRMTVNGETKKPKES
Protein: RRM domain-containing protein (D5MCR4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPPTAQNSQQPYPRSDKAGGHLLHYSSSSHQHQNHQHYHSSSSNQQFNRPPPPPHNSQHHHHHNNSRMNASSAPQQQQQQQQPQQGQAPQQQQQGPPQHQYQQQRPFHGRVQNHMRGSGPFGNSNGYGRYTAPRGDQQHHDSTPLSSTNLYIRGLMPNTNDDLLREMCSKYGNIASTKAIMDKATNNCKGYGFVDFESPQAAAAAVDGLNTEGVQAQMAKLQQQEQDPTNLYIANLPLDFTEQMLETELNKFGMVISTRILRTPDNQSRGVGFARMDSKEKCEVIISALNGGRFDTMSKEGPALLIKQADTGRKSKHSMNNPEMLQRMQYPQVYQSYYGYHPAAVYQQHYDVNSLASQMGGMHVGGGNPQANGGGDMYGAHMYGQNAGGQGGQGVGQGGQGGNQQFYNPNNGRNKKYFQPMNPQ
Protein: Myosin-binding protein 1 (F4HXQ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Membrane-anchored myosin receptors that define a distinct, plant-specific transport vesicle compartment.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:23995081}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Myosin-17
- Pentatricopeptide repeat-containing protein At1g05600
- RBR-type E3 ubiquitin transferase
- Protein CHLOROPLAST J-LIKE DOMAIN 1
- Myosin-like protein
- Probable protein phosphatase 2C 76
- Myosin-5
- Myosin-6
- UBP1-associated proteins 1B
- Probable inactive shikimate kinase like 2, chloroplastic
Sequence:
MGSRSFTRALALAFNEWLLMFMLFVNSIFSYVIARFADYSELQSPCLMCSNLDHILRRTKDLKKTHWDIICSKHKSEISSLVYCHAHGKLVDVRGMCETCLFSFATTNKSNAETYRLLVGKLGEDSHFGSKSDRSKYPNCSKLTDCTCCNQLWTPQTAATQVAEREILPKIGLLGKIRTGKQSAPKKSVSFNHLPDVGYTELKIHSDTESEAVFSDTEPKQESSLNHLPPVGYNEPKIGLVGDVRTGKPSTPKKSVSFNHLPDVGYTELKIHSDTESEAVFSEDECVVLKDEDHKYQIVDLQTHPIITLPYDLATDKLLNFDFPLEPFVTRNDREEVQLQETNWRTYSSFPVLIPVNDVPETSEKVFKEEEINSLDNLFLTSRAMKHFAAAKVKEEPIRLQDISSTPDVKENPANASLMEETELICLSDVTATSGAMEHSEVILKEREELIHLQDISVTPDFKENPANASLLEETELICLNDVTSPLRAVEHSAVLLKDKVEPIRLQDGGSLTPDFMENSANASILEETELICVNDVTSTSRTMGHSSVVLKENEEPIRFQDSSLTPDFKENPASTFLVEETELICLNDVTSPSRAMEHSTVFIEEKEELVRHQNITLTQDFMENPANSSLREETELICLNDVTSTSEVAETPEDVLEGIELMSIHDISLDEVSESVTTNQTSVEISKERDTDQADITSLESEYIVVPSPNSMPENSTDNCVSDKKEMKETSLRISSLSEMAPRDVTSHTEAALESESSSFNSMSVAAETNQYSGELLDLADAYNIVVGNEGHYDSNGRQQIENWMKKDTSRVSEDLKALLTQISASRGIEFLSPRDVSPKISVNSSDQETKNLDHDMQLLLQKRMLERNESNLSLEGVSVTEIEGESEGDRLKRQVDYDRKLLTGLYKELEEERSASAVATNQAMAMITRLQEEKASFQMEALQNLRMMEEQAEYDMEAIQRLNDLLVEREKLIQDLEAEIEYFRDQTPQKKNKLDVAEKVTEMDSPSEGMSNKIQSCLVGFDEERLYITSCLEKIENRVNGKAHDDNLPAQESVSELHERVERLKGDLYFLEQVMNSLGHGNEGVQFVKEIASHLQTLRSLSMKRQDQTEC
Protein: Golgin subfamily A member 6-like protein 9 (A6NEM1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWPQPRLPPHPAMSEKTQQGKLAAAKKKLKAYWQRKSPGIPAGANRKKKINGSSPDTFTSGGYHSPGDSATGIYGEGRASSTTLQDLESQYQELAVALDSSSAIISQLTENINSLVRTSKEEKKHEIHLVQKLGRSLFKLKNQTAEPLAPQPPAGPSKMEQLQDETNHLRKELESVGRQLQAEVENNQMLSLLNRRQEERLREQEERLREQEERLCEQEERLCEQEERLREQEERLCEQEKLPGQERLLEEVEKLLEQERRQEEQERLLERERLLDEVEELLEQERLRQQDERLWQQETLRELERLRELERMLELGWEALYEQRAEPRSGFEELNNENKSTLQLEQQVKELEKSGGAEEPRGSESAAAARPVAGAPVPQGAWMCGQAGWTPQEHPGLSGEAVGTGEAAGGAGEAACHSFRAAENRELNITII
Protein: Colicin-D (P17998)
Organism: Escherichia coli
Function: Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.
Interaction partners:
Sequence:
MSDYEGSGPTEGIDYGHSMVVWPSTGLISGGDVKPGGSSGIAPSMPPGWGDYSPQGIALVQSVLFPGIIRRIILDKELEEGDWSGWSVSVHSPWGNEKVSAARTVLENGLRGGLPEPSRPAAVSFARLEPASGNEQKIIRLMVTQQLEQVTDIPASQLPAAGNNVPVKYRLMDLMQNGTQYMAIIGGIPMTVPVVDAVPVPDRSRPGTNIKDVYSAPVSPNLPDLVLSVGQMNTPVLSNPEIQEEGVIAETGNYVEAGYTMSSNNHDVIVRFPEGSDVSPLYISTVEILDSNGLSQRQEAENKAKDDFRVKKEEAVARAEAEKAKAELFSKAGVNQPPVYTQEMMERANSVMNEQGALVLNNTASSVQLAMTGTGVWTAAGDIAGNISKFFSNALEKVTIPEVSPLLMRISLGALWFHSEEAGAGSDIVPGRNLEAMFSLSAQMLAGQGVVIEPGATSVNLPVRGQLINSNGQLALDLLKTGNESIPAAVPVLNAVRDTATGLDKITLPAVVGAPSRTILVNPVPQPSVPTDTGNHQPVPVTPVHTGTEVKSVEMPVTTITPVSDVGGLRDFIYWRPDAAGTGVEAVYVMLNDPLDSGRFSRKQLDKKYKHAGDFGISDTKKNRETLTKFRDAIEEHLSDKDTVEKGTYRREKGSKVYFNPNTMNVVIIKSNGEFLSGWKINPDADNGRIYLETGEL
Protein: Chloride channel protein 2 (ClC-2) (P35525)
Organism: Rattus norvegicus (Rat)
Function: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport. Involved in the regulation of aldosterone production. The opening of CLCN2 channels at hyperpolarized membrane potentials in the glomerulosa causes cell membrane depolarization, activation of voltage-gated Ca2+ channels and increased expression of aldosterone synthase, the rate-limiting enzyme for aldosterone biosynthesis (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12163466, ECO:0000269|PubMed:22405205}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51788}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendritic spine membrane {ECO:0000269|PubMed:11068136}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:11068136}. Note=Sorting to the basolateral membrane is mediated by AP-1 clathrin adapter (By similarity). Localizes at axon initial segments and dendritic shaft and spikes. Colocalizes with HEPACAM and GFAP at astrocyte end-foot in contact with brain capillaries and other glial cells (PubMed:11068136, PubMed:22405205). {ECO:0000250|UniProtKB:P51788, ECO:0000269|PubMed:11068136, ECO:0000269|PubMed:22405205}.
Interaction partners:
- Voltage-dependent T-type calcium channel subunit alpha-1H
Sequence:
MAAATAAAATVAGEGMEPRALQYEQTLMYGRYTQELGAFAKEEAARIRLGGPEPWKGSPSARATPELLEYGQSRCARCRICSVRCHKFLVSRVGEDWIFLVLLGLLMALVSWAMDYAIAVCLQAQQWMSRGLNTNILLQYLAWVTYPVVLITFSAGFTQILAPQAVGSGIPEMKTILRGVVLKEYLTLKTFVAKVIGLTCALGSGMPLGKEGPFVHIASMCAALLSKFLSLFGGIYENESRNTEMLAAACAVGVGCCFAAPIGGVLFSIEVTSTFFAVRNYWRGFFAATFSAFIFRVLAVWNRDEETITALFKTRFRLDFPFDLQELPAFAVIGIASGFGGALFVYLNRKIVQVMRKQKTINRFLMKKRLLFPALVTLLISTLTFPPGFGQFMAGQLSQKETLVTLFDNRTWVRQGLVEDLGAPSTSQAWSPPRANVFLTLVIFILMKFWMSALATTIPVPCGAFMPVFVIGAAFGRLVGESMAAWFPDGIHTDSSTYRIVPGGYAVVGAAALAGAVTHTVSTAVIVFELTGQIAHILPVMIAVILANAVAQSLQPSLYDSIIRIKKLPYLPELGWGRHQQYRVRVEDIMVRDVPHVALSCTFRDLRLALHRTKGRMLALVESPESMILLGSIERSQVVALLGAQLSPARRRQHMQKLRKAQMSPPSDQESPPSSETSIRFQVNTEDSGFPGAHGQTHKPLKPALKRGPSNATSLQEGTTGNMESAGIALRSLFCGSPPLESTTSELEKSESCDKRKLKRVRISLASDSDLEGKMSPEEILEWEEQQLDEPVNFSDCKIDPAPFQLVERTSLHKTHTIFSLLGVDHAYVTSIGRLIGIVTLKELRKAIEGSVTAQGVKVRPPLASFRDSATSSSDTETTEVHALWGPRSRHGLPREGTPSDSDDKCQ
Protein: Sodium/potassium-transporting ATPase subunit alpha (F1MR06)
Organism: Bos taurus (Bovine)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta
- Sodium/potassium-transporting ATPase subunit beta-2
- Sodium/potassium-transporting ATPase subunit gamma
- Sodium/potassium-transporting ATPase subunit beta-3
- Protein ATP1B4
- Sodium/potassium-transporting ATPase subunit alpha-2
- cGMP-dependent protein kinase 1
- Mitogen-activated protein kinase 1
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
RPKGRDRAPRAGPARDTAAQPQGRCPPVTPSRPQSGGSDSYRVATSQDKKDDKGSPKKSKGTKDRRDLDDLKKEVAMVSPTLCFSERVLCESCVPQGLTHSKAQEILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAGTEDDPSGDNLYLGIVLAAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIREGEKMQVNAEEVVVGDLVEIKGGDRVPADLRIISAHGCKVDNSSLTGESEPQTRSPDCTHDNPLETRNITFFSTNCVEGTARGVVVATGDRTVMGRIATLASGLEVGKTPIAIEIEHFIQLITGVAVFLGVSFFILSLILGYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGTSFDKSSHTWVALSHIAGLCNRAVFKGGQDNVPVLKRDVAGDASESALLKCIELSSGSVKLMRERNKKVAEIPFNSTNKYQLSIHETEDPNDNRYLLVMKGAPERILDRCSTILLHGKEQPLDEEMKEAFQNAYLELGGLGERVLGFCHYYLPEEQFPKGFAFDCDDVNFTTDNLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVIHGTDLKDFTSEQIDEILQNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIMANIPLPLGTITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRTDKLVNERLISMAYGQIGMIQALGGFFSYFVILAENGFLPGNLVGIRLNWDDRTVNDLEDSYGQQWTYEQRKVVEFTCHTAFFVSIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMDVALRMYPLKPSWWFCAFPYSFLIFVYDEIRKLILRRNPGAWHERGSHGISKSSNHRVLDPTRISMRTL
Protein: Phospholemman-like protein (PLMS) (P83009)
Organism: Lamna nasus (Porbeagle shark) (Squalus nasus)
Function: Induces a hyperpolarization-activated chloride current when expressed in Xenopus oocytes. May have a functional role in muscle contraction.
Subcellular location: Microsome membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
VSDVPNNDDRFTY
Protein: Amyloid beta precursor like protein 1 (Amyloid beta (A4) precursor-like protein 1) (Amyloid-like protein 1) (APLP) (APLP-1) [Cleaved into: C30] (P51693)
Organism: Homo sapiens (Human)
Function: May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding (By similarity). Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I.
Subcellular location: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [C30]: Cytoplasm. Note=C-terminally processed in the Golgi complex.
Interaction partners:
- Amyloid beta precursor protein binding family B member 1
- Amyloid beta precursor protein binding family B member 2
- Contactin-5
- Beta-secretase 1
- Amyloid-beta A4 precursor protein-binding family B member 3
- Amyloid-beta A4 precursor protein-binding family A member 1
- C-Jun-amino-terminal kinase-interacting protein 1
- Spondin-1
- Presenilin-1
- Major prion protein
Sequence:
MGPASPAARGLSRRPGQPPLPLLLPLLLLLLRAQPAIGSLAGGSPGAAEAPGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLRDPQRVLEYCRQMYPELQIARVEQATQAIPMERWCGGSRSGSCAHPHHQVVPFRCLPGEFVSEALLVPEGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGVEYVCCPPPGTPDPSGTAVGDPSTRSWPPGSRVEGAEDEEEEESFPQPVDDYFVEPPQAEEEEETVPPPSSHTLAVVGKVTPTPRPTDGVDIYFGMPGEISEHEGFLRAKMDLEERRMRQINEVMREWAMADNQSKNLPKADRQALNEHFQSILQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQADPPQAERVLLALRRYLRAEQKEQRHTLRHYQHVAAVDPEKAQQMRFQVHTHLQVIEERVNQSLGLLDQNPHLAQELRPQIQELLHSEHLGPSELEAPAPGGSSEDKGGLQPPDSKDDTPMTLPKGSTEQDAASPEKEKMNPLEQYERKVNASVPRGFPFHSSEIQRDELAPAGTGVSREAVSGLLIMGAGGGSLIVLSMLLLRRKKPYGAISHGVVEVDPMLTLEEQQLRELQRHGYENPTYRFLEERP
Protein: Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Neural apoptosis-regulated convertase 1) (NARC-1) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9) (P59996)
Organism: Rattus norvegicus (Rat)
Function: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}.
Interaction partners:
- Very low-density lipoprotein receptor
- Low-density lipoprotein receptor
- Apolipoprotein B-100
- Sterol regulatory element-binding protein 2
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Annexin A2
- Golgi phosphoprotein 3
- Golgi phosphoprotein 3-like
- P-type phospholipid transporter
- Angiopoietin-related protein 3
Sequence:
MGIRCSTWLRWPLSPQLLLLLLLCPTGSRAQDEDGDYEELMLALPSQEDSLVDEASHVATATFRRCSKEAWRLPGTYVVVLMEETQRLQVEQTAHRLQTWAARRGYVIKVLHVFYDLFPGFLVKMSSDLLGLALKLPHVEYIEEDSLVFAQSIPWNLERIIPAWQQTEEDSSPDGSSQVEVYLLDTSIQSGHREIEGRVTITDFNSVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGTSLHSLRVLNCQGKGTVSGTLIGLEFIRKSQLIQPSGPLVVLLPLAGGYSRILNTACQRLARTGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGKDIIGASSDCSTCYMSQSGTSQAAAHVAGIVAMMLNRDPALTLAELRQRLILFSTKDVINMAWFPEDQRVLTPNRVATLPPSTQETGGQLLCRTVWSAHSGPTRTATATARCAPEEELLSCSSFSRSGRRRGDRIEAIGGQQVCKALNAFGGEGVYAVARCCLLPRVNCSIHNTPAARAGPQTPVHCHQKDHVLTGCSFHWEVENLRAQQQPLLRSRHQPGQCVGHQEASVHASCCHAPGLECKIKEHGIAGPAEQVTVACEAGWTLTGCNVLPGASLPLGAYSVDNVCVARIRDAGRADRTSEEATVAAAICCRSRPSAKASWVHQ
Protein: FHA domain-containing protein (Q57XA2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTEHICASLVLTRGPEGLQRRLPVRLPLSGKPITIGRAIDNDVVLEMDLIFSSQWHCQMFAQKCEPETSERVEEREAASDPSRCEGRHVDCEGQTEIPVKEQYSLWLVDVGSSNGTFVNGIRVASSAPTPLHHGDVIVLGGMRDVEVGKSLPMEDLPLEIVTWRVAMEGKSEEGFGFVATPPVFLSMEFVISQARQRALGALQDSPDPKVSTTSPLKLPLKRMRHEQETGSNKLYDDGDVTPKRRIREVSYPSGEDRSGGELARRSGTVAAYLDPNEANAWEVTTNSSSDVASTTGLPCPSSKATASRGYCNSDALAEPTKEDARETRVAPAVARETVQ
Protein: Uncharacterized protein, isoform A (Uncharacterized protein, isoform B (EC 2.3.1.225)) (Q9VPM2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Palmitoyltransferase
- Palmitoyltransferase
- Palmitoyltransferase
- Palmitoyltransferase
- Palmitoyltransferase
- Palmitoyltransferase
- Palmitoyltransferase
- tRNA-dihydrouridine
- Palmitoyl-protein thioesterase 1
Sequence:
MSTTAAGLKSGPKGAYGVRSETDHIITISTAGLTESHSESPAKGVVTPVRKPHSLGSEDSPENIIPGEQAETNKKPLHLCRLSQLVSYQSNIADVQHRKGRRLHGLQLPLHPLQIFGWLVLLLFGVASYWVLIPAFHARIQGPLYGLITGLYLVHIASHLTALLTDPADKELRRVHRNDRIVPEFDRSKHSHVIENGRCHLCNIRTSSNRTKHCSVCNKCVGKFDHHCKWLNHCIGSRNYVAFLMCVVSAVVATLVIVAAVVAQIVFYYIQPDWLSFYWCPTESSHTIESGDFINITLSLSNGTMMLIEQHTSEEDVHQEMWDEEQANMTISTLPTLLENFTAIIEASATRPGISPTNHTETQPVVTGIGLNETIFMFLLGVLGLLAAVSAGLLLHLCFFHIYISFLGLTTYEYIRNHRQAQDAKTKQLLEGAPGVRAPKNGNVHFSASLPEPHNPSKSLPGGQQLYCCSSAPHPSQHSQESVGQTEQSLRLHCCASSREFHQSGQAIYVCSLLEEAVPQIQVEPDTLSSFHCCSSFAASSLQRRVSLAKGSLISAEPRHLRPATYLQYTEQCTLCTFRLRRGSGPGTGSSGAVSSAGGSSSTRTLTSQTGGSSASATAAGNISKHQRWRRKWNCCAAVPDSPDLPNDLLAALTFRESEEAAAAAKLNAQELPIQFIRTLNGGLDQELPLKATTATPTPPRSSRLRYMLRLLGRYRRPRCRHGAHHGIAAKEHQNIGGSAIKQNQIRPLQLQAAGRGYANSTATPTPPASSPSRSSLESSDLSTSTSPSCGKKELMLLPTSVIRDDSVTTYTLTLPPALPPPTRRKMNQTTQELAELAETLGFASNLQHSQHNSQTNSRTLPSFGNVYRRQRRKHFLRTRSPTLSPIHESGLSNPTSPQPLRHHHQNLANSNSNPAKAMSSPMLNRNSGSANSSALLVQNLCSLAGETLRNSASNSSLQSLSSNSSST