wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin-ribosomal protein eS31A fusion protein [Cleaved into: Ubiquitin; Small ribosomal subunit protein eS31A (40S ribosomal protein S27a)] (P0C016)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31A]: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31B fusion protein
- Elongation factor 3
- mRNA export factor elf1
- Small ribosomal subunit protein eS27
- Ubiquitin-activating enzyme E1 1
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS7
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGGKKRKKKTYTTPKKIKHKHKKVELAVLKYYKVEDDGSVKRLRRECPNCGASTFMANHKDRLYCGRCHLTLKLEN
Protein: Prostaglandin reductase 2 (PRG-2) (EC 1.3.1.48) (15-oxoprostaglandin 13-reductase) (Zinc-binding alcohol dehydrogenase domain-containing protein 1) (Q8VDQ1)
Organism: Mus musculus (Mouse)
Function: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha with highest activity towards 15-keto-PGE2. Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MIIQRVVLNSRPGKNGNPVAENFRVEEFSLPDALNEGQVQVRTLYLSVDPYMRCKMNEDTGTDYLAPWQLAQVADGGGIGVVEESKHQKLTKGDFVTSFYWPWQTKAILDGNGLEKVDPQLVDGHLSYFLGAIGMPGLTSLIGVQEKGHISAGSNQTMVVSGAAGACGSLAGQIGHLLGCSRVVGICGTQEKCLFLTSELGFDAAVNYKTGNVAEQLREACPGGVDVYFDNVGGDISNAVISQMNENSHIILCGQISQYSNDVPYPPPLPPAVEAIRKERNITRERFTVLNYKDKFEPGILQLSQWFKEGKLKVKETMAKGLENMGVAFQSMMTGGNVGKQIVCISEDSSL
Protein: Multidrug resistance protein homolog 49 (EC 7.6.2.2) (P-glycoprotein 49) (Q00449)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- ABC-type xenobiotic transporter
- Multidrug resistance protein homolog 65
- Uncharacterized protein, isoform A
- Sodium/potassium-transporting ATPase subunit alpha
- Sodium/potassium-transporting ATPase subunit beta-2
- Sodium/potassium-transporting ATPase subunit beta-1
Sequence:
MVKKEESRLPQAGDFQLKEGSVVDATRKYSYFDLFRYSTRCERFLLVVSLLVATAASAFIPYFMIIYGEFTSLLVDRTVGVGTSSPAFALPMFGGGQQLTNASKEENNQAIIDDATAFGIGSLVGSVAMFLLITLAIDLANRIALNQIDRIRKLFLEAMLRQDIAWYDTSSGSNFASKMTEDLDKLKEGIGEKIVIVVFLIMTFVIGIVSAFVYGWKLTLVVLSCVPFIIAATSVVARLQGSLAEKELKSYSDAANVVEEVFSGIRTVFAFSGQEKEKERFGKLLIPAENTGRKKGLYSGMGNALSWLIIYLCMALAIWYGVTLILDERDLPDRVYTPAVLVIVLFAVIMGAQNLGFASPHVEAIAVATAAGQTLFNIIDRPSQVDPMDEKGNRPENTAGHIRFEGIRFRYPARPDVEILKGLTVDVLPGQTVAFVGASGCGKSTLIQLMQRFYDPEAGSVKLDGRDLRTLNVGWLRSQIGVVGQEPVLFATTIGENIRYGRPSATQADIEKAARAANCHDFITRLPKGYDTQVGEKGAQISGGQKQRIAIARALVRQPQVLLLDEATSALDPTSEKRVQSALELASQGPTTLVVAHRLSTITNADKIVFLKDGVVAEQGTHEELMERRGLYCELVSITQRKEATEADEGAVAGRPLQKSQNLSDEETDDDEEDEEEDEEPELQTSGSSRDSGFRASTRRKRRSQRRKKKKDKEVVSKVSFTQLMKLNSPEWRFIVVGGIASVMHGATFPLWGLFFGDFFGILSDGDDDVVRAEVLKISMIFVGIGLMAGLGNMLQTYMFTTAGVKMTTRLRKRAFGTIIGQDIAYFDDERNSVGALCSRLASDCSNVQGATGARVGTMLQAVATLVVGMVVGFVFSWQQTLLTLVTLPLVCLSVYLEGRFIMKSAQKAKASIEEASQVAVEAITNIRTVNGLCLERQVLDQYVQQIDRVDIACRRKVRFRGLVFALGQAAPFLAYGISMYYGGILVAEERMNYEDIIKVAEALIFGSWMLGQALAYAPNVNDAILSAGRLMDLFKRTSTQPNPPQSPYNTVEKSEGDIVYENVGFEYPTRKGTPILQGLNLTIKKSTTVALVGPSGSGKSTCVQLLLRYYDPVSGSVNLSGVPSTEFPLDTLRSKLGLVSQEPVLFDRTIAENIAYGNNFRDDVSMQEIIEAAKKSNIHNFISALPQGYDTRLGKTSQLSGGQKQRIAIARALVRNPKILILDEATSALDLESEKVVQQALDEARSGRTCLTIAHRLTTVRNADLICVLKRGVVVEHGTHDELMALNKIYANLYLMQQVSG
Protein: Expressed protein (Ribosomal L18p/L5e family protein) (Q9LJA1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT3G20230 protein
- Large ribosomal subunit protein uL18c
- F18K10.11 protein
- At1g65370/T8F5_15
- tRNA
- Probable receptor-like protein kinase At5g39030
- Periodic tryptophan protein 2
- Serine/threonine-protein kinase STY46
Sequence:
MALMVLRRKCLRLPDFISVFRPAPRCFSSRFSNSESGKVTVTGLSGCGIETVDDDVWHVSSSLSQAWRQFQADTAKNSPVTIQGVRETILDDEDPDHDEIDNMRIRGDLFFKLDRGSKEFEEYNYDFHRKNQHKNAKKEQNQEEETKIKKDNKKEVRDEYKKRNDSFTGETDHPNEAVKKRERTFTFNQLTAPFHYPFCLDIYISKESVRACVIHRVTSKVVTVAHSISKDMKFDLGSRRNVAACAAVGAVLAQRSLEDDIHDVIYTPRKGDKIEGKLQVVLQALIDNGVNVKVKLKQRKLKKKTSHLMMA
Protein: Calcitonin receptor (CT-R) (P25117)
Organism: Sus scrofa (Pig)
Function: This is a receptor for calcitonin. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The calcitonin receptor is thought to couple to the heterotrimeric guanosine triphosphate-binding protein that is sensitive to cholera toxin. The receptor can also couple to an additional signaling pathway via a pertussis toxin-sensitive g protein in isolated osteoclasts and in LLC-PK1 cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30988}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30988}.
Interaction partners:
- Receptor activity-modifying protein 1
- Calcitonin
- Receptor activity-modifying protein 2
- Receptor activity-modifying protein 3
- Calcitonin receptor-stimulating peptide 1
- Calcitonin receptor-stimulating peptide 2
- Calcitonin receptor-stimulating peptide 3
- Pro-adrenomedullin
- Islet amyloid polypeptide
- Parathyroid hormone
Sequence:
MRFTLTRWCLTLFIFLNRPLPVLPDSADGAHTPTLEPEPFLYILGKQRMLEAQHRCYDRMQKLPPYQGEGLYCNRTWDGWSCWDDTPAGVLAEQYCPDYFPDFDAAEKVTKYCGEDGDWYRHPESNISWSNYTMCNAFTPDKLQNAYILYYLAIVGHSLSILTLLISLGIFMFLRYFNLLAPFNALLYPTRSISCQRVTLHKNMFLTYVLNSIIIIVHLVVIVPNGELVKRDPPICKVLHFFHQYMMSCNYFWMLCEGVYLHTLIVVSVFAEGQRLWWYHVLGWGFPLIPTTAHAITRAVLFNDNCWLSVDTNLLYIIHGPVMAALVVNFFFLLNILRVLVKKLKESQEAESHMYLKAVRATLILVPLLGVQFVVLPWRPSTPLLGKIYDYVVHSLIHFQGFFVAIIYCFCNHEVQGALKRQWNQYQAQRWAGRRSTRAANAAAATAAAAAALAETVEIPVYICHQEPREEPAGEEPVVEVEGVEVIAMEVLEQETSA
Protein: Protein lin-7 homolog C (Lin-7C) (Mammalian lin-seven protein 3) (MALS-3) (Vertebrate lin-7 homolog 3) (Veli-3) (Q792I0)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Basolateral cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction {ECO:0000250}. Postsynaptic density membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Note=Mainly basolateral in renal epithelial cells. {ECO:0000250}.
Interaction partners:
- Peripheral plasma membrane protein CASK
- Amyloid-beta A4 precursor protein-binding family A member 1
- Peripheral plasma membrane protein CASK
- Disks large homolog 1
- MAGUK p55 subfamily member 7
- Disks large homolog 4
- Protein PALS1
- ATP-sensitive inward rectifier potassium channel 12
Sequence:
MAALGEPVRLERDICRAIELLEKLQRSGEVPPQKLQALQRVLQSEFCNAVREVYEHVYETVDISSSPEVRANATAKATVAAFAASEGHSHPRVVELPKTEEGLGFNIMGGKEQNSPIYISRIIPGGIADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGKVKLVVRYTPKVLEEMESRFEKMRSAKRRQQT
Protein: Dystroglycan 1 (Dystroglycan) (Dystrophin-associated glycoprotein 1) [Cleaved into: Alpha-dystroglycan (Alpha-DG); Beta-dystroglycan (Beta-DG)] (Q14118)
Organism: Homo sapiens (Human)
Function: The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.
Subcellular location: [Alpha-dystroglycan]: Secreted, extracellular space.; SUBCELLULAR LOCATION: [Beta-dystroglycan]: Cell membrane {ECO:0000269|PubMed:18764929, ECO:0000269|PubMed:26848865}; Single-pass type I membrane protein. Cytoplasm, cytoskeleton. Nucleus, nucleoplasm {ECO:0000269|PubMed:18764929}. Cell membrane, sarcolemma {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}. Note=The monomeric form translocates to the nucleus via the action of importins and depends on RAN. Nuclear transport is inhibited by Tyr-892 phosphorylation. In skeletal muscle, this phosphorylated form locates to a vesicular internal membrane compartment. In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs) in the presence of ANK2 (By similarity). In peripheral nerves, localizes to the Schwann cell membrane. Colocalizes with ERM proteins in Schwann-cell microvilli. {ECO:0000250}.
Interaction partners:
- Utrophin
- Laminin subunit alpha-2
- Agrin
- Dystrophin
- Alpha-sarcoglycan
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Delta-sarcoglycan
- Sarcospan
- Neurexin-1
- Neurexin-2
Sequence:
MRMSVGLSLLLPLSGRTFLLLLSVVMAQSHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEGLPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRTASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTMTIPGYVEPTAVATPPTTTTKKPRVSTPKPATPSTDSTTTTTRRPTKKPRTPRPVPRVTTKVSITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDRAPARFKAKFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTITLQNITRGSIVVEWTNNTLPLEPCPKEQIAGLSRRIAEDDGKPRPAFSNALEPDFKATSITVTGSGSCRHLQFIPVVPPRRVPSEAPPTEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQDTMGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP
Protein: Zinc finger protein 79 (ZNFpT7) (Q15937)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Collagen alpha-1
Sequence:
MLEEGVLPSPGPALPQEENTGEEGMAAGLLTAGPRGSTFFSSVTVAFAQERWRCLVSTPRDRFKEGIPGKSRSLVLLGLPVSQPGMNSQLEQREGAWMLEGEDLRSPSPGWKIISGSPPEQALSEASFQDPCVEMPPGDSDHGTSDLEKSFNLRPVLSPQQRVPVEARPRKCETHTESFKNSEILKPHRAKPYACNECGKAFSYCSSLSQHQKSHTGEKPYECSECGKAFSQSSSLIQHQRIHTGEKPYKCSECGRAFSQNANLTKHQRTHTGEKPYRCSECEKAFSDCSALVQHQRIHTGEKPYECSDCGKAFRHSANLTNHQRTHTGEKPYKCSECGKAFSYCAAFIQHQRIHTGEKPYRCAACGKAFSQSANLTNHQRTHTGEKPYKCSECGKAFSQSTNLIIHQKTHTGEKPYKCNECGKFFSESSALIRHHIIHTGEKPYECNECGKAFNQSSSLSQHQRIHTGVKPYECSECGKAFRCSSAFVRHQRLHAGE
Protein: Endo-beta-N-acetylglucosaminidase EndoSd (EC 3.2.1.96) (Endoglycosidase Sd) (A0A191T6Q6)
Organism: Streptococcus dysgalactiae
Function: Endoglucosidase that acts as a host immune evasion factor by mediating hydrolysis of the N-linked glycan from the Fc region of host immunoglobulin-gamma (IgG) during infection. Specifically catalyzes the hydrolysis of the beta-1,4 linkage between the first two N-acetylglucosamine residues of the complex-type N-linked glycan located on 'Asn-297' of the Fc region of IgG antibodies (IGHG1, IGHG2, IGHG3 or IGHG4), thereby preventing interaction between IgGs and Fc receptors and ability to activate the complement pathway (By similarity). Shows a specificity for biantennary complex type N-glycans; does neither cleave larger complex type glycans nor oligomannose and nor hybrid-type glycans. Specifically acts on IgGs; does not act on immunoglobulin alpha, beta, delta or mu.
Subcellular location: Secreted {ECO:0000269|PubMed:27200457}. Host extracellular space {ECO:0000250|UniProtKB:Q99Y92}. Note=Secretion is tightly regulated by carbohydrate composition in the growth medium. {ECO:0000269|PubMed:27200457}.
Interaction partners:
Sequence:
MDKRLLVKRTLGCVCAATLMGAILATHHDSLISVKAEEKTVQTGKTDQQIGAKLVQEIREGKRGPLYAGYFRTWHDRASTGADGKQQHPENTMAEVPKEVDILFVFHDHTASDSPFWSELKDSYVHKLHQQGTALVQTIGVNELNGRTGLSKDYPDIPEGNKALAAAIVKTFVTDRGVDGLDIDIEHEFTNKRTPEEDARALNVFKEIAQLIGKNGSDKSKLLIMDTTLSVENNPIFKGIAEDLDYLLRQYYGSQGGEAEVDTINSDWNQYQNYIDASQFMIGFSFFEESAPKGNLWFDVNEYDPKNPERGKDIEGTRAKKYAEWQPSTGGLKAGIFSYAIDRDGVAHVGKEYSQRTYQELEAGLKKHPVVDNISHTDYTVSRKLKALMAEDKRYDVIDQKDIPDAALREQVIQQVGQYKGDLERYNKTLVLTVDKIHSLKGLEKLSHLQKLELCQLSNVKEVTPDILPESMKKDAELVMTGMTGLEKLNLRGLNRQTLDGIDVNGLTHLTSFDISHNSLDLSEKSADRKLLMTLMEQVSNHQKITVKNTAFENQKPKGYYPQTYDTKEGHYDVDNAEHDILTDFVFGTVTKRDTFIGDEEAFAMYKEGAIDGRQYVAKDYTYEAFRKDYQGYKVHLTASNLGESDTSKVTATTDETYLVDVFDGEKIVPHMTLHVGNGATIMENLAKGAKVIGTSGDISLAEKVVDGVVADSFWTWDTKNWIAFDLNSQVIAKEWRLFNGETDPRFKDKELNIQKGRLQILKDKTIHLENMSKDERDSYLADEQNWITVSEITSNQKIYNGSITDITSRYWRFCVDEGVSSKSPQYTELQILGQRLSSDIASTVQD
Protein: Protein FMP32, mitochondrial (Found in mitochondrial proteome protein 32) (P43557)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12514182, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YDL241W
- Protein YSY6
- Phosphomannomutase
Sequence:
MLKRIVGLPARRCFHRTSFLLGSDFETVHIPNTNHFKDLLIENGKFQEDQATTIVEIMTDAIRGGVNHVSQDLAKREKLTQLSYQQRVDFAKLRDQLLSADRSEFHNIQNEYESVKNDLEKLRNKLREEITKTNAGFKLDLSLEKGRIREESSHHDLQIKEIDTKIEQEVTNMKMQIDSVKTQVMQWLIGVCTGTFALVLAYMRLLT
Protein: Probable multidrug-efflux transporter Rv1634 (P9WJX3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Could be involved in fluoroquinolones efflux.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- UvrABC system protein B
- Dihydropteroate synthase
- Uncharacterized protein Rv2325c
Sequence:
MTETASETGSWRELLSRYLGTSIVLAGGVALYATNEFLTISLLPSTIADIGGSRLYAWVTTLYLVGSVVAATTVNTMLLRVGARSSYLMGLAVFGLASLVCAAAPSMQILVAGRTLQGIAGGLLAGLGYALINSTLPKSLWTRGSALVSAMWGVATLIGPATGGLFAQLGLWRWAFGVMTLLTALMAMLVPVALGAGGVGPGGETPVGSTHKVPVWSLLLMGAAALAISVAALPNYLVQTAGLLAAAALLVAVFVVVDWRIHAAVLPPSVFGSGPLKWIYLTMSVQMIAAMVDTYVPLFGQRLGHLTPVAAGFLGAALAVGWTVGEVASASLNSARVIGHVVAAAPLVMASGLALGAVTQRADAPVGIIALWALALLIIGTGIGIAWPHLTVRAMDSVADPAESSAAAAAINVVQLISGAFGAGLAGVVVNTAKGGEVAAARGLYMAFTVLAAAGVIASYQATHRDRRLPR
Protein: alpha-1,2-Mannosidase (EC 3.2.1.-) (M9PCV1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MSTTSSESFVRGQRLMLIFLVAMCIVVACVLSTETTMPTQNMSNKERAELREEARDMFYHAYNAYMQNAYPADELMPLSCKGRYRGVTPSRGDMDDILGNFSMTLVDTLDTLVLLGDFTEFDHAVKLVIRDVQFDSDIIVSVFETNIRMVGGLLSAHILAEYLQKHADTMHWYKGELLEMSRELGYRLLPAFNTSTGIPHARVNLRLGMKDPMLKKSRETCTACAGTILLEFAALSRLTGDPIFEVRAHAAMDALWKLRHRGSDLMGTVLNVHSGDWVRRDSGVGAGIDSYYEYLFKSYVLLGDDKYLARFNRHYNAVMKYVSEGPMLLDVLMHRPHAKSKNFMDSLLAFWPGLQVLSGDLKPAVQTHEMLYQVMQMHTFIPEAFTVDFQIHWGQHPLRPEFIESTYFLYRATGDHHYLQVGKKALKTLQQHAKVSCGYAAVNDVRTGKHEDRMDSFVLSETIKYLFLLFSDPQDLIINVDEFVFTTEAHLLPLSIAQLGNATFSFRQTDEHNVLDFMRTCPSSNRLFPEKVRKPLRNFITGSCPRTTAGKRLSALDFQASNADHLRAVYDMGITMVSVGDRSQGKAKSHEEGEMGLQFMQEMLELTKMQSINQLAQLQAVAYATDENSQDWIALMAGPSHFSPELTGDQFVEGDVILAKPLRACDESLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGSSGETQPMFAMSGDGKDDVLIPVVFMYSMEFGKLSAVMQRRKQPLRVRVMQMVEFKRWQLAKEQRQNQTASVAQKPEKEL
Protein: Interferon alpha-11 (IFN-alpha-11) (Limitin) (Q61716)
Organism: Mus musculus (Mouse)
Function: Has antiviral and antiproliferative activities. Produced by macrophages and stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase (By similarity). During viral infection, mediates antiviral effect, either directly by inducing interferon-stimulated genes, either indirectly through stimulation of natural killer cells enabling them to control viral replication.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Interferon alpha/beta receptor 1
- Interferon alpha-6
- Interferon 1ai2
- Interferon alpha-9
- Tyrosine-protein kinase JAK2
- Interferon alpha-5
- Interferon regulatory factor 3
- Interferon regulatory factor 7
- Interferon gamma receptor 1
- Epidermal growth factor receptor
Sequence:
MARLCAFLMILIVMSYWSTCSLGCDLPHTYNLRNKRALKVLAQMRRLTPLSCLKDRKDFGFPLEKVDAQQIQKAQSIPVLRDLTQQILNLFASKDSSAAWNATLLDSFCNDLHQQLNDLQGCLMQQVGVQESPLTQEDSLLAVRIYFHRITVFLREKKHSPCAWEVVRAEVWRALSSSANVLGRLREEKA
Protein: E3 ubiquitin-protein ligase synoviolin (EC 2.3.2.27) (RING-type E3 ubiquitin transferase synoviolin) (Synovial apoptosis inhibitor 1) (Q86TM6)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis. Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1 (By similarity). During the early stage of B cell development, required for degradation of the pre-B cell receptor (pre-BCR) complex, hence supporting further differentiation into mature B cells (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:12646171, ECO:0000269|PubMed:14593114, ECO:0000269|PubMed:16186510, ECO:0000269|PubMed:26471130}; Multi-pass membrane protein {ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:12646171, ECO:0000269|PubMed:14593114, ECO:0000269|PubMed:16186510}.
Interaction partners:
- Protein sel-1 homolog 1
- Protein OS-9
- Derlin-1
- Transitional endoplasmic reticulum ATPase
- Derlin-2
- Endoplasmic reticulum lectin 1
- Protein FAM8A1
- Lipid droplet-regulating VLDL assembly factor AUP1
- Ubiquitin-conjugating enzyme E2 J1
- Selenoprotein S
Sequence:
MFRTAVMMAASLALTGAVVAHAYYLKHQFYPTVVYLTKSSPSMAVLYIQAFVLVFLLGKVMGKVFFGQLRAAEMEHLLERSWYAVTETCLAFTVFRDDFSPRFVALFTLLLFLKCFHWLAEDRVDFMERSPNISWLFHCRIVSLMFLLGILDFLFVSHAYHSILTRGASVQLVFGFEYAILMTMVLTIFIKYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKVLLYMAFMTIMIKVHTFPLFAIRPMYLAMRQFKKAVTDAIMSRRAIRNMNTLYPDATPEELQAMDNVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLRASLPAQSPPPPEPADQGPPPAPHPPPLLPQPPNFPQGLLPPFPPGMFPLWPPMGPFPPVPPPPSSGEAVAPPSTSAAALSRPSGAATTTAAGTSATAASATASGPGSGSAPEAGPAPGFPFPPPWMGMPLPPPFAFPPMPVPPAGFAGLTPEELRALEGHERQHLEARLQSLRNIHTLLDAAMLQINQYLTVLASLGPPRPATSVNSTEETATTVVAAASSTSIPSSEATTPTPGASPPAPEMERPPAPESVGTEEMPEDGEPDAAELRRRRLQKLESPVAH
Protein: Collagen type VI alpha 2 chain (A0A8I5ZTZ9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTTTTKMLQGSFSVLLLGGLLGVLHAQQQEAISPDISTTDRNNNCPEKADCPVNVYFVLDTSESVAMQSPTDSLLYHMQQFVPQFISQLQNEFYLEQVALSWRYGGLHFSDQVEVFSPPGSDRASFTKSLQGIRSFRRGTFTDCALANMTQQIRQHVGRGVVNFAVVITDGHVTGNPCGGIKMQAERAREEGIRLFAVAPNRNLNEQGLRDIANTPHELYRNNYATMRPDSTEIDQDTINRIIKVMKHEAYGECYKVSCLEIPGPHGPKGYRGQKGAKGNMGEPGEPGQKGRQGDPGIEGPIGFPGPKGVPGFKGEKGEFGSDGRKGAPGLAGKNGTDGQKGKLGRIGPPGCKGDPGSRGPDGYPGEAGSPGEQGDQGAKGDSGRPGRRGPPGNPGDKGSKGYRGNSGAPGSPGVKGGKGGPGPRGPKGEPGRRGDPGTKGGPGSDGPKGEKGDPGPEGPRGLAGEIGSKGAKGDRGLPGPRGPQGALGEPGKQGSRGDPGDAGPRGDSGQPGPKGDPGRPGFSYPGPRGTPGEKGEPGPPGPEGGRGDFGLKGAPGRKGEKGEPADPGPPGEPGPRGPRGIPGPEGEPGPPGDPGLTECDVMTYVRETCGCCDCEKRCGALDVVFVIDSSESIGYTNFTLEKNFVINVVNRLGAIAKDPKSETGTRVGVVQYSHEGTFEAIRLDDERVNSLSSFKEAVKNLEWIAGGTWTPSALKFAYNQLIKESRRQKTRVFAVVITDGRHDPRDDDLNLRALCDRDVTVTAIGIGDMFHETHESENLYSIACDKPQQVRNMTLFSDLVAEKFIDDMEDVLCPDPQIVCPELPCQTELYVAQCTQRPVDIVFLLDGSERLGEQNFYKARRFVEEVSRRLTLARRDDDPLNARMALLQYGSQNQQQVAFPLTYNVTTIHEALERTTYLNSFSHVGTGIVHAINNVVRGARGGARRHAELSFVFLTDGVTGNDSLEESVHSMR
Protein: ELL-associated factor 1 (Q6IQD2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Elongation factor RNA polymerase II.
- RNA polymerase II elongation factor ELL2
- Elongation factor for RNA polymerase II 2
- AF4/FMR2 family member 4 isoform X2
- ELL-associated factor 2
- DNA-directed RNA polymerase subunit
- MLLT1 super elongation complex subunit a.
- MLLT3 super elongation complex subunit.
- Transcription elongation factor
- Ring finger and SPRY domain-containing 1.
Sequence:
MNGSSNPPLDKEEHVLKLGDSFEKRPKSSFHTIRYDFKPASIDTSCEGDLQVGKGDEVTITLPHIPGSTPPMTVFKGNKRPYQKDCVLIINHDTGEFMLEKLSSSIQVKKTRAEGSSKIQARIEQQSVRANQLTTPQFRTPNKPGLGAKTSPTKDNPSPEPQLDDIKRELRAEVDMIEQMSSSGSSSSSESASCSGSGNDDSSCSDGEQETHLSPSRNNMANGMNKSQGNNQLMNTLRNDLQLSESGSDSDID
Protein: Peptidoglycan recognition protein L1 (M9PNP3)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MSGAQGVEDSMISPMEPHWKWCLTLLVVLVSAHTDTKVTSSQHMDDFIRVLEQVEYRNPGLQPVNVLRGLRRAAGLRDEFMQHFLGTIREDSTSEAPVMDSNLSDFIGRAVRHQVTERGREEGVVLTADGTTVAMSPVLLGIEAGLVSKTRCQVRGLYPLTLARNLGLSFQRFHSSLLSHRLGPDGCWDDVTSPQVFTLSDKPSLATDALVNGGMDGVILGMEVSAQSQRPLKLSSLLRTYYCHHLEVEGLDTAPRLISRLRRENFRELARPPLLQRQVVRSLVLQRRLIDHSTMLSQEKEELTAVVREGIKEFVHKYMDCPAIIPRCQWGAAPYRGTPTPLSLPLSFMYIHHTYQPGQPCLTFQQCSADMRSMQRFHQDDRGWDDIGYSFVAGSDGYLYRGRGWHWQGAHTKGYNSKGYGVSFIGDYTSRLPSQQTMELVRDRLASCAVGGGRLVGNFTLYGHRQLVKTSCPGDALYSEITGWEHFGEVQN
Protein: Chaperone (O76224)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MGIDYYKVLGVSRDASPSDIKKAYHQLALKYHPDKASGNREEAERLFKEVAEAYDVLSDEKKKKIYDSYGEEGLKGGVPDGSSGGPGGAGFHGFSSGGGTYNFSNRDAFKVFESFFGSNDPFAGGDMFGGGPGLHRVFRGFGGPHGFMSGFGSPEMSPAHEVPPLEYTFSCTLEEIYSGCTKKFNVLRPLPTGEEKKLFEVAVLPGYKKGTKVRFVGEGGIVQGYPPNVMADLVFVLDEKPHPRFKRDGADVLTTVQINLKQALLGTTISVLCLDGTTQSLPLTGVSKNGRKLRVSGKGLPNRKTKQNGDMYVTIEVVMPTSLNEATKRLVEKCEF