wanglab/gogpt-training-data huggingface dataset:
Protein: Bis(monoacylglycero)phosphate synthase CLN5 (BMP synthase CLN5) (EC 2.3.1.-) (Ceroid-lipofuscinosis neuronal protein 5) (Protein CLN5) (Palmitoyl protein thioesterase CLN5) (EC 3.1.2.22) (S-depalmitoylase CLN5) [Cleaved into: Bis(monoacylglycero)phosphate synthase CLN5, secreted form] (O75503)
Organism: Homo sapiens (Human)
Function: Plays a role in influencing the retrograde trafficking of lysosomal sorting receptors SORT1 and IGF2R from the endosomes to the trans-Golgi network by controlling the recruitment of retromer complex to the endosomal membrane. Regulates the localization and activation of RAB7A which is required to recruit the retromer complex to the endosomal membrane.
Subcellular location: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Lysosome {ECO:0000269|PubMed:11971870, ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:24058541, ECO:0000269|PubMed:28442266, ECO:0000269|PubMed:37708259}.; SUBCELLULAR LOCATION: [Bis(monoacylglycero)phosphate synthase CLN5]: Membrane {ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:28442266}; Single-pass type II membrane protein {ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:28442266}. Note=An amphipathic anchor region facilitates its association with the membrane. {ECO:0000269|PubMed:24038957}.
Interaction partners:
- Battenin
- Ceroid-lipofuscinosis neuronal protein 6
- Protein CLN8
- Palmitoyl-protein thioesterase 1
- Major facilitator superfamily domain-containing protein 8
- DnaJ homolog subfamily C member 5
- Transcription factor BTF3
- Cathepsin D
- BTB/POZ domain-containing protein KCTD7
- Tripeptidyl-peptidase 1
Sequence:
MAQEVDTAQGAEMRRGAGAARGRASWCWALALLWLAVVPGWSRVSGIPSRRHWPVPYKRFDFRPKPDPYCQAKYTFCPTGSPIPVMEGDDDIEVFRLQAPVWEFKYGDLLGHLKIMHDAIGFRSTLTGKNYTMEWYELFQLGNCTFPHLRPEMDAPFWCNQGAACFFEGIDDVHWKENGTLVQVATISGNMFNQMAKWVKQDNETGIYYETWNVKASPEKGAETWFDSYDCSKFVLRTFNKLAEFGAEFKNIETNYTRIFLYSGEPTYLGNETSVFGPTGNKTLGLAIKRFYYPFKPHLPTKEFLLSLLQIFDAVIVHKQFYLFYNFEYWFLPMKFPFIKITYEEIPLPIRNKTLSGL
Protein: Uncharacterized protein C2E12.03c (Q10227)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Vacuolar arginine/histidine antiporter stm1
Sequence:
MPSSTTTAPPGTHPNATASTVFAILGTVCWCVQLIPQIIKNYRAKSTEGLDTLFILSWVVASIPLSVYNQVQELNIALKVQPELFQALAFTTFFQCLYYGSKWPLRKALFVVISFMLFSGGLQAMLILTIKLGIRRHVEWPVVFMGVLATVLVNIGFLPQYISIFRARAVTGISYLFLAIDSSGSLFSFLSLPFDRWDVLAAVDYGLLFIIEMGVFVLAFIFNVLLKNKSTPTDEDVTFTEEDGDEKDEEYSDIFSIKGKFNTRPNAWQNAYDSDTKSAIQIP
Protein: Methylated-DNA--protein-cysteine methyltransferase (EC 2.1.1.63) (6-O-methylguanine-DNA methyltransferase) (MGMT) (O-6-methylguanine-DNA-alkyltransferase) (P24528)
Organism: Rattus norvegicus (Rat)
Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Alkyl transferase
- N-glycosylase/DNA lyase
- Isocitrate dehydrogenase cytoplasmic
- DNA-3-methyladenine glycosylase
- DNA mismatch repair protein Mlh1
- Isocitrate dehydrogenase, mitochondrial
- DNA mismatch repair protein
- Receptor protein-tyrosine kinase
- Cellular tumor antigen p53
Sequence:
MAEICKMKYTVLDSPLGKIELSGCERGLHGIRFLSGKTPNTDPTEAPACPEVLGGPEGVPEPLVQCTAWLEAYFHEPAATEGLPLPALHHPVFQQDSFTRQVLWKLLKVVKFGEMVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVIRSDGAIGNYSGGGQTVKEWLLAHEGIPTGQPASKGLGLIGSWLKPSFESSSPKPSG
Protein: DNA-binding transcriptional regulator CRP (Q5E2H1)
Organism: Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri)
Interaction partners:
- RNA polymerase sigma factor RpoD
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit omega
- Adenylate cyclase
Sequence:
MVLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAWVRAKSPCEVAEISFKKFRQLIQVNPDILMRLSAQMATRLQITSQKVGDLAFLDVTGRIAQTLLNLAKQPDAMTHPDGMQIKITRQEIGQIVGCSRETVGRILKMLEEQNLISAHGKTIVVYGTR
Protein: Phospholipase A and acyltransferase 1 (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (HRAS-like suppressor 1) (HRSL1) (Phospholipid-metabolizing enzyme A-C1) (Q9QZU4)
Organism: Mus musculus (Mouse)
Function: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (By similarity).
Subcellular location: [Isoform 1]: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10542256, ECO:0000269|PubMed:27623847}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:27623847}. Cytoplasm {ECO:0000269|PubMed:27623847}.
Interaction partners:
- Mitochondrial disaggregase
Sequence:
MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPIDGIRSSFTSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFPIGQEVAYDLLVNNCEHFVTLLRYGEGVSEQANRAIGTIGLVAAGIDIFTFLGLFPKRQRTKY
Protein: Gap junction beta-5 protein (Connexin-31.1) (Cx31.1) (Q02739)
Organism: Mus musculus (Mouse)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
Interaction partners:
Sequence:
MNWSVFEGLLSGVNKYSTAFGRIWLSLVFVFRVLVYLVTAERVWGDDQKDFDCNTRQPGCTNVCYDEFFPVSHVRLWALQLILVTCPSLLVVMHVAYRKAREKKYQEKIGEGYLYPNPGKKRGGLWWTYVFSLSFKATIDIIFLYLFHAFYPRYTLPSMVKCHAEPCPNTVDCFIAKPSEKNIFIVFMVVTAVICILLNLVELIYLVIKRCSECAQLRRPPTAHAKNDPNWANSPSKEKDFLSCDLIFLGSDAHPPLLPDRPRAHVKKTIL
Protein: Zgc:66419 (Q7SXD7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSLNKHQLSDSLFIWLQSFQVPSCASKHELTSGVAIAHVLNKIDSTWFNETWLSRIKEDGGTNWRLKVSNLKKILQSMMEYYHDVLSQQVSDEHVPDVRLLEERNHVYMQRTCELEEEQRRATAIRSQLDSYKRQAHEMSAKHSAEAMKAEKWQFEYKNLNDKYETLLKEREKLISERDTLRETTEELRCAQVQQQCLTDSMIGDAGAVGSLASEIMPTEFRDTVVRLQQENKMLCVQEESYRHRLEELQTQLEEAQRRQNTLETQNRLSQQQISDLSAQVEELQRALQEQDSRNEDVISSLLKKKLEEHLEKLHEAHSDLQKKREVIDDLEPPLDINMAKKVDELQEILKKKDEDMRRMEDRYKRYVEKARTVIKTLEPKQKLNPVPVEVQALKNQLSEKDRKIQHLEHDFEKTRSRHDQEEKLIISAWYNMGMALHQRVAGERSSSSSSSAQSFLAQQRQSTQARRGFSRLQPR
Protein: Vitamin D-binding protein (DBP) (VDB) (Gc protein-derived macrophage activating factor) (Gc-MAF) (GcMAF) (Gc-globulin) (Group-specific component) (Gc) (Vitamin D-binding protein-macrophage activating factor) (DBP-maf) (P02774)
Organism: Homo sapiens (Human)
Function: Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation.
Subcellular location: Secreted {ECO:0000269|PubMed:2423133}.
Interaction partners:
- Cubilin
- Low-density lipoprotein receptor-related protein 2
- Albumin
- Actin, aortic smooth muscle
- Actin, alpha cardiac muscle 1
- Alpha-2-HS-glycoprotein
- Fibrinogen beta chain
- Protein AMBP
- Mitochondrial glutamate carrier 2
- Haptoglobin
Sequence:
MKRVLVLLLAVAFGHALERGRDYEKNKVCKEFSHLGKEDFTSLSLVLYSRKFPSGTFEQVSQLVKEVVSLTEACCAEGADPDCYDTRTSALSAKSCESNSPFPVHPGTAECCTKEGLERKLCMAALKHQPQEFPTYVEPTNDEICEAFRKDPKEYANQFMWEYSTNYGQAPLSLLVSYTKSYLSMVGSCCTSASPTVCFLKERLQLKHLSLLTTLSNRVCSQYAAYGEKKSRLSNLIKLAQKVPTADLEDVLPLAEDITNILSKCCESASEDCMAKELPEHTVKLCDNLSTKNSKFEDCCQEKTAMDVFVCTYFMPAAQLPELPDVELPTNKDVCDPGNTKVMDKYTFELSRRTHLPEVFLSKVLEPTLKSLGECCDVEDSTTCFNAKGPLLKKELSSFIDKGQELCADYSENTFTEYKKKLAERLKAKLPDATPTELAKLVNKHSDFASNCCSINSPPLYCDSEIDAELKNIL
Protein: E3 ubiquitin-protein ligase RMA1 (EC 2.3.2.27) (Protein RING membrane-anchor 1) (RING-type E3 ubiquitin transferase RMA1) (O64425)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of aquaporin PIP2-1. Forms a ubiquitin ligase complex in cooperation with the E2 enzymes UCB8/UCB10.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11329381, ECO:0000269|PubMed:19224217, ECO:0000269|PubMed:19234086}; Single-pass type IV membrane protein {ECO:0000269|PubMed:11329381, ECO:0000269|PubMed:19224217, ECO:0000269|PubMed:19234086}.
Interaction partners:
- Protein OS-9 homolog
- ERAD-associated E3 ubiquitin-protein ligase component HRD3A
- E3 ubiquitin-protein ligase SDIR1
- Ubiquitin-conjugating enzyme E2 32
- E3 ubiquitin protein ligase DRIP1
- ERAD-associated E3 ubiquitin-protein ligase HRD1A
- Tubby-like F-box protein 9
- Probable E3 ubiquitin ligase SUD1
- E3 ubiquitin protein ligase DRIP2
- ERAD-associated E3 ubiquitin-protein ligase HRD1B
Sequence:
MALDQSFEDAALLGELYGEGAFCFKSKKPEPITVSVPSDDTDDSNFDCNICLDSVQEPVVTLCGHLFCWPCIHKWLDVQSFSTSDEYQRHRQCPVCKSKVSHSTLVPLYGRGRCTTQEEGKNSVPKRPVGPVYRLEMPNSPYASTDLRLSQRVHFNSPQEGYYPVSGVMSSNSLSYSAVLDPVMVMVGEMVATRLFGTRVMDRFAYPDTYNLAGTSGPRMRRRIMQADKSLGRIFFFFMCCVVLCLLLF
Protein: DNA mismatch repair protein Mlh1 (MutL protein homolog 1) (Q9JK91)
Organism: Mus musculus (Mouse)
Function: Heterodimerizes with Pms2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (Msh2-Msh6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of Pms2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (Mlh1-Pms2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with Mlh3 to form MutL gamma which plays a role in meiosis (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P40692}. Chromosome {ECO:0000269|PubMed:30949703}. Note=Recruited to chromatin in a MCM9-dependent manner. {ECO:0000250|UniProtKB:P40692}.
Interaction partners:
- Mismatch repair endonuclease PMS2
- DNA mismatch repair protein Msh6
- MutL homolog 3
- DNA mismatch repair protein Msh2
- Fanconi anemia group J protein homolog
- DNA mismatch repair protein Msh3
- Fanconi-associated nuclease 1
- RecQ-like DNA helicase BLM
- Exonuclease 1
- PMS1 homolog 1, mismatch repair system component)
Sequence:
MAFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTNIQVVVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQTFEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLQAPPKPCAGNQGTLITVEDLFYNIITRRKALKNPSEEYGKILEVVGRYSIHNSGISFSVKKQGETVSDVRTLPNATTVDNIRSIFGNAVSRELIEVGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESAALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILQRVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEAARPTTGVASSSTSGSGDKVYAYQMVRTDSREQKLDAFLQPVSSLGPSQPQDPAPVRGARTEGSPERATREDEEMLALPAPAEAAAESENLERESLMETSDAAQKAAPTSSPGSSRKRHREDSDVEMVENASGKEMTAACYPRRRIINLTSVLSLQEEISERCHETLREMLRNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPAPLFDLAMLALDSPESGWTEDDGPKEGLAEYIVEFLKKKAEMLADYFSVEIDEEGNLIGLPLLIDSYVPPLEGLPIFILRLATEVNWDEEKECFESLSKECAMFYSIRKQYILEESTLSGQQSDMPGSTSKPWKWTVEHIIYKAFRSHLLPPKHFTEDGNVLQLANLPDLYKVFERC
Protein: Zgc:109932 (Q504E3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAWGVCSRALVWIITALIWWSHSGLMGFCSSSTVSVPESLLFVSTLDGNLHAVSKISGTIKWTLKEDPVLQVPTHVSEPAFLPDPNDGSLYSLGGKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDVRYVVDLLTGEKKQTLTSSYAEMLCPSSSLFYLGRTEYTITMYDTKSRELRWNATYSDYAFTLPDEDTKYNMAHFVSNGDGLVVTVDSESGDVQWVQNYNSPVVAVYIWQREGLRKVPHTNVAVETLRYLTFMSGEVGRITQWKYPFPREKKKESQTGLEG
Protein: Voltage-dependent calcium channel gamma-2 subunit (Q6PFS3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363085}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363085}.
Interaction partners:
- Glutamate receptor
- Glutamate receptor, ionotropic, AMPA 2a.
- Voltage-dependent calcium channel gamma-1 subunit
- Protein shisa-6 precursor
- Glutamate receptor
- Glutamate receptor
- Transmembrane protein 91.
- Voltage-dependent calcium channel gamma-1 subunit
- Glutamate receptor
- Glutamate receptor, ionotropic, AMPA 1a.
Sequence:
MGVFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVCKIKTNNENETSKKNEEVMTHSGLWRTCCLEGNFKGLCKQIDHFPEDTDYEADASEYFLRAVRASSIFPILSVILLFMGGLCIAASEFYKSRHNIILSAGILFVSAGLSNIIGMIVYISANAGDPSKSDSKKNSYSYGWSFYFGALSFIMAEMVGVLAVHMFIDRHRELRAGARAADYLQGSAITRIPSYRYRYRRRSRSSSRSTDPSHSRDASPVGLKGFGALPSTEISMYTLTRGGDTLKGGHGTPTATYNSERDHNFLQVHNCIQKDLKDSSNTANRRTTPV
Protein: Mediator of RNA polymerase II transcription subunit 24 (Mediator complex subunit 24) (Protein lessen) (Thyroid hormone receptor-associated protein 4 homolog) (Trap100 homolog) (Q2PW47)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). Required for proliferation of enteric nervous system precursors. Required for the development of dopaminergic amacrine cells and rod photoreceptor cells in the retina.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 15
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 29
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 4
Sequence:
MKVVNLKQAILQAWKERWSDYQWAINIKKNCPKGATWDYLNLAEALLEQAMIGPSPNPLILSYLKYAISSQMVSYSSVLTAISKFDDFSRELCVKSLLEIMDMFSNRLSCHGKAEECIGLCRAMLCTVVWLLQGCAWYCERLRDPNDFSALESSLRACLERMANLLHSTKNRALVHIARLEEQASWTNVEQAVLKLTENLSAVTNPTLKESLEECVSLVKSIPQMLCLQCDPPVHTTFPSVHAFIMLEGTMNLTGETQPLVEQLMMIKRMQRIPAPLFVLEIWKACFTGLIESPEGNEELKWTAFTFLKIPQVLLRLKKYPQGEKTQDFTEDVNVAFEYLLNLTPLLDKADQRCNCDCLSLLLQECNKLGLLSEANTATLTAKRSEDREHAPRLKTAENANIQPNPGLILRAEPTVTNILKTVDADHSKSPEGLLGVLGHMLSGKSLDLLLAAAAATGKLKSFARKFIKLNEFPKHISGEGSKSASVRALLFDISFLMLCHVVQTYGSEVILSDPSPSSETPFFETWLQTCMPEEGKTLNPDHPCFRPESGKVESLVALLNSSSEMKLVQMKWHEICLSTPAAILEVLNAWENGVLSVEAVQKITDNIKGKVCSMAICAVAWLVAHVRMLGLDEREKPQTMIRQLMTPMSGENTLQFYHERVVIMSSILEHMCADVFQQTGLSLRPAVEGQEPIPYRNLLPARLPIRQALQSQFRKVLEKGWVDSHAFHLFENLLHMGGVFWFTNNLVKELLKETRKEWASRVVELLYSIFCLDTQQITLTLLGHILPRLLTDPAHWHSLADPPGRALAKLSVWCALSSYSSHHKGQASARQRKRHREDIEDYTSLFPLDDTQPSKLMRLLSSNEDENSMLSSPGDRSISSSLSASQLHTVNMRDPLNRVLANLFLLISSQLGSKTAGPHTQFVQSFVEECVDCSEQGSRSSILQFMPFTMISELVKLQSLAKPKTVLSITDLSLPLGRRMAAKAIAAL
Protein: Fibrosin-1-like protein (AUTS2-like protein) (HBV X-transactivated gene 9 protein) (HBV XAg-transactivated protein 9) (Q9HCM7)
Organism: Homo sapiens (Human)
Interaction partners:
- RING1 and YY1-binding protein
- DDB1- and CUL4-associated factor 7
- YY1-associated factor 2
- Casein kinase II subunit alpha'
- Polycomb group RING finger protein 5
- Polycomb group RING finger protein 3
Sequence:
MEAKVRPSRRSRAQRDRGRRREAARDARAQSPSSGDEPEPSPGKENAGLRGAPPRGAAPAPRTARPPRRRRRESSSQEEEVIDGFAIASFSTLEALEKDMALKPHERKEKWERRLIKKPRESETCPPAEPSENRRPLEAGSPGQDLEPACDGARKVPLQPSKQMKVTVSKGGDRDSDDDSVLEATSSRDPLSDSSAHAVSGRGYSCDSESGPDDKASVGSEKLFAPGTDKGPALEKSEAKAGPVPKVSGLERSRELSAESFLPTASPAPHAAPCPGPPPGSRANPLVKKEPPAPHRHTPQPPPPQPRGLLPTHVPASLGAFAGHSQAAANGLHGLSRSSSAPLGLGKHVSLSPHGPGPHLSTSHLALRSQAQHQLHAAMFAAPPTLPPPPALPASSLVLPGHPADHELLRQELNTRFLVQSAERPGASLGPGALLRAEFHQHQHTHQHTHQHTHQHQHTFAPFPAGLPPTPPAAPPPFDKYAPKLDSPYFRHSSVSFFPSFPPAIPGLPTLLPHPGPFGSLQGAFQPKVSDPYRAVVKVSTCWEGPWQGRTLVPPGRPRGARDSRSLQKTWVGVAPAPLSASILSQKPGRWCAVHVQIAWQIYRHQQKIKEMQLDPHKLEVGAKLDLFGRPPAPGVFAGFHYPQDLARPLFPSTGAAHPASNPFGPSAHPGSFLPTGPLTDPFSRPSTFGGLGSLSSHAFGGLGSHALAPGGSIFAPKEGSSVHGLPSPHEAWNRLHRAPPSFPAPPPWPKSVDAERVSALTNHDREPDNGKEEQERDLLEKTRLLSRASPATPAGHPVSGLLLRAQSELGRSGAPAEREAEPRVKESRSPAKEEAAKMPARASPPHSKAAPGDVKVKEERGEDEASEPPAGGLHPAPLQLGLGRERLGAPGFAWEPFRGLELPRRAFPAAAPAPGSAALLEPPERPYRDREPHGYSPERLRGELERARAPHLPPAAPALDGALLPSLGALHFPRLSPAALHNGLLARTPPAAAALGAPPPLVTAAGPPTPPGPPRSRTTPLGGLGPGEARDYSPSRNPPEVEAR
Protein: Nucleolar protein 16 (Q94402)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9Y3C1}.
Interaction partners:
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Brix domain-containing protein ZK795.3
- Ribosome assembly factor mrt4
- UPF0642 protein YBL028C
- RRM domain-containing protein
- Protein BCCIP homolog
- Putative H/ACA ribonucleoprotein complex subunit 2-like protein
- Ribosome biogenesis protein WDR12 homolog
Sequence:
MARDVKKRGKPAYTNRRNRQKYLKKKDNKKKLSKSAVPIIKYTWDETKTPRENVRDMGIAFNPNDAVPIAEHRKEIIDAEPIDGVSIVVPKPEKKVTGRKKNEKQAAHIISNLEQQVKEEEEARAGQDRKFRLFHRETELCVYMLARHGEDFQAMTRDPKNLWQYTPKQWAKKIRTHKESEMCKFLETA
Protein: Proteasome subunit beta type-3 (Proteasome chain 13) (Proteasome component C10-II) (Proteasome subunit beta-3) (beta-3) (Proteasome theta chain) (P49720)
Organism: Homo sapiens (Human)
Function: Non-catalytic component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000269|PubMed:34711951}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 13
- Proteasome subunit alpha type-6
- Proteasome subunit beta type-1
- 26S proteasome non-ATPase regulatory subunit 7
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-4
- Proteasome subunit beta type-2
- 26S proteasome non-ATPase regulatory subunit 14
- Proteasome subunit beta type-9
- 26S proteasome regulatory subunit 4
Sequence:
MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD
Protein: Reticulocalbin-3 (EF-hand calcium-binding protein RLP49) (Q96D15)
Organism: Homo sapiens (Human)
Function: Probable molecular chaperone assisting protein biosynthesis and transport in the endoplasmic reticulum. Required for the proper biosynthesis and transport of pulmonary surfactant-associated protein A/SP-A, pulmonary surfactant-associated protein D/SP-D and the lipid transporter ABCA3 (By similarity). By regulating both the proper expression and the degradation through the endoplasmic reticulum-associated protein degradation pathway of these proteins plays a crucial role in pulmonary surfactant homeostasis (By similarity). Has an anti-fibrotic activity by negatively regulating the secretion of type I and type III collagens. This calcium-binding protein also transiently associates with immature PCSK6 and regulates its secretion.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:16433634}.
Interaction partners:
Sequence:
MMWRPSVLLLLLLLRHGAQGKPSPDAGPHGQGRVHQAAPLSDAPHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWDTYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDIVIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVGSQATNYGEDLTRHHDEL
Protein: Transcription factor SOX-7 (mSOX7) (P40646)
Organism: Mus musculus (Mouse)
Function: Binds to and activates the CDH5 promoter, hence plays a role in the transcriptional regulation of genes expressed in the hemogenic endothelium and blocks further differentiation into blood precursors. May be required for the survival of both hematopoietic and endothelial precursors during specification. May play a role in skeletal myogenesis and up-regulate the expression of muscle markers, such as PAX3/PAX7 and Meox1. Competes with GATA4 for binding and activation of the FGF3 promoter. Represses Wnt/beta-catenin-stimulated transcription. Probably acts by targeting CTNNB1 to proteasomal degradation. Binds the DNA sequence 5'-AACAAT-3'.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:11691915}. Cytoplasm {ECO:0000269|PubMed:11691915}.
Interaction partners:
- Transcription factor GATA-6
- POU domain, class 5, transcription factor 1
- Catenin beta-1
- Cadherin-5
- Transcription factor SOX-17
- Transcription factor GATA-4
- Transcription factor SOX-18
Sequence:
MASLLGAYPWTEGLECPALEAELSDGLSPPAVPRPSGDKSSESRIRRPMNAFMVWAKDERKRLAVQNPDLHNAELSKMLGKSWKALTLSQKRPYVDEAERLRLQHMQDYPNYKYRPRRKKQGKRLCKRVDPGFLLSSLSRDQNTLPEKNGIGRGEKEDRGEYSPGATLPGLHSCYREGAAAAPGSVDTYPYGLPTPPEMSPLDALEPEQTFFSSSCQEEHGHPHHLPHLPGPPYSPEFTPSPLHCSHPLGSLALGQSPGVSMMSSVSGCPPSPAYYSHATYHPLHPNLQAHLGQLSPPPEHPGFDTLDQLSQVELLGDMDRNEFDQYLNTPGHPDSAAGVGTLTGHVPLSQGTPTGPTETSLISVLADATATYYNSYSVS
Protein: Alpha-defensin 31 (Alpha-defensin-related sequence 7) (Cryptdin-related protein 4C-2) (CRS4C2) (Defensin-related cryptdin-related sequence 7) (P50715)
Organism: Mus musculus (Mouse)
Function: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MKKLVLLFALVLLAFQVQADSIQNTDEETKTEEQQGEEDQAVSVSFGDPQGSGLQDAALGWGRRCPRCPPCPRCSWCPRCPTCPRCNCNPK