wanglab/gogpt-training-data huggingface dataset:
Protein: ABC transporter NFT1 (New full-length MRP-type transporter 1) (P0CE68)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Putative uncharacterized protein YKR104W
- ATP-dependent permease PDR11
Sequence:
MIKNGTCPYWERDDLSECARREYIEFKFPLFILLTGMIYAFCKVFRAFYLRGKNHTNEAPEFEEQGNGNHEYARFSVLRLKSAWESRSFCNVNNRSTFDKFKKFIEGAFIVLQLTIHLYILSSMPMDNKKFFHQGFLVQMFLWILLLVVITLRLISASQSFRWVLACKRDLWAVSFYSYASLFTLSILPLRSVFIGKIKDKIMVKYIISETFIDLALLLLLSTSSIEGTRYSFLVENENKKLPPAPTVFGLLTFSRIDRLIWKAYKHCLGNADIWDLDINNKSIAILANFEMSSKKGRLLPNIICYFKAVFISQLFLAFVSSFLNFVPSLLMPRILSYVNDPKSKSWNLVSLYVSSMLVSKIIATTCRGQGLFLGEKGTMQLRTVLISNIYSKTLRRTILKDSTTSLQKNASTSFEENPDSSEAEPRKKSSRKDNSVNNVMSIDAFKVSEAMNTFYLACEAVFMTVTALMILYSLLGWSAFAGTFALLAMIPLNFWCATFYGNYQADQLILTDKRTSGISEALNSIRVIKLLAWENLFYQKIINVRDGEIRLLKKKATIFFLNHLIWFFGPTLVSAITFSVFIKFQNQTLTPTIAFTALSLFAILRTPMDQIASTVSLLIQSFISLERIQDYLNESETRKYEILEQSNTKFGFEDASMEWEAAETSFKLKNISIDFKLNSLNAIIGPTGSGKSSLLLGLLGELNLLSGKIYVPTVESRDDLEIGKDGMTNSMAYCSQTPWLISGTIKDNVVFGEIFNKQKFDDVMKSCCLDKDIKAMTAGIRTDVGDGGFSLSGGQQQRIALARAIYSSSRYLILDDCLSAVDPETALYIYEECLCGPMMKGRTCIITSHNISLVTKRADWLVILDRGEVKSQGKPSDLIKSNEFLRESINNDSKNTTHNQIDLKRSTTSKKTKNGDPEGGNSQDEVCAEVENFEETKMEGSVKFSAYKWLADYFGGLGVVFVFTSSSILIHGITLSQGFWLRYWLDTGSSGSKSTWLYRIVEGHSNIYFLLTYIIIGLVSSFLTSGKVWIAIISGTNVTKKIFAKLLSSILYAKLRFHNVTPTGRIMNRFSKDMDIIDQQLIPNFEGLSYSVVVCLWIILLIGYVTPQFLLFAIPLCALYYTVCTLYLRASRELKRIDNINISPIHQLFAEAIKGVTTIRALADERRFITQSLVAIDRSNAPFFYLNMATEWITYRVDIIGTLVLFSSSVMIIMKAS
Protein: Casein kinase I isoform alpha (CKI-alpha) (EC 2.7.11.1) (CK1) (Q8BK63)
Organism: Mus musculus (Mouse)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates (By similarity). Can phosphorylate a large number of proteins (By similarity). Participates in Wnt signaling (By similarity). Phosphorylates CTNNB1 at 'Ser-45' (By similarity). May phosphorylate PER1 and PER2. May play a role in segregating chromosomes during mitosis (By similarity). May play a role in keratin cytoskeleton disassembly and thereby, it may regulate epithelial cell migration (By similarity). Acts as an inhibitor of NLRP3 inflammasome assembly by mediating phosphorylation of NLRP3.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P48729}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P48729}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P48729}. Nucleus speckle {ECO:0000250|UniProtKB:P48729}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25644602}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:31338967}. Note=Localizes to the centrosome in interphase cells, and to kinetochore fibers during mitosis. Also recruited to the keratin cytoskeleton. {ECO:0000250|UniProtKB:P48729}.
Interaction partners:
- Axin-1
- Glycogen synthase kinase-3 beta
- Catenin beta-1
- Adenomatous polyposis coli protein
- Axin-2
- Protein cereblon
- APC membrane recruitment protein 1
- Beta-adrenergic receptor kinase 1
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- Speckle targeted PIP5K1A-regulated poly
Sequence:
MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGKQTDKTKSNMKGF
Protein: Claudin-3 (Clostridium perfringens enterotoxin receptor 2) (CPE-R 2) (CPE-receptor 2) (Rat ventral prostate.1 protein homolog) (hRVP1) (O15551)
Organism: Homo sapiens (Human)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:28028216}. Cell membrane {ECO:0000269|PubMed:28028216}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Occludin
- Tight junction protein 1
- Tight junction protein ZO-3
- Claudin-12
- Claudin-5
- MARVEL domain-containing protein 2
- Claudin-16
- Claudin-7
- Claudin-19
- Claudin-4
Sequence:
MSMGLEITGTALAVLGWLGTIVCCALPMWRVSAFIGSNIITSQNIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALIVVAILLAAFGLLVALVGAQCTNCVQDDTAKAKITIVAGVLFLLAALLTLVPVSWSANTIIRDFYNPVVPEAQKREMGAGLYVGWAAAALQLLGGALLCCSCPPREKKYTATKVVYSAPRSTGPGASLGTGYDRKDYV
Protein: Olfactory receptor 10S1 (Olfactory receptor OR11-279) (Q8NGN2)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MTSRSVCEKMTMTTENPNQTVVSHFFLEGLRYTAKHSSLFFLLFLLIYSITVAGNLLILLTVGSDSHLSLPMYHFLGHLSFLDACLSTVTVPKVMAGLLTLDGKVISFEGCAVQLYCFHFLASTECFLYTVMAYDRYLAICQPLHYPVAMNRRMCAEMAGITWAIGATHAAIHTSLTFRLLYCGPCHIAYFFCDIPPVLKLACTDTTINELVMLASIGIVAAGCLILIVISYIFIVAAVLRIRTAQGRQRAFSPCTAQLTGVLLYYVPPVCIYLQPRSSEAGAGAPAVFYTIVTPMLNPFIYTLRNKEVKHALQRLLCSSFRESTAGSPPP
Protein: Tyrosyl-DNA phosphodiesterase 2 (5'-tyrosyl-DNA phosphodiesterase) (A0A384MDM5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
Interaction partners:
Sequence:
MELGSCLEGGREAAEEEGEPEVKKRRLLCVEFASVASCDAAVAQCFLAENDWEMERALNSYFEPPVEESALERRPETISEPKTYVDLTNEETTDSTTSKISPSEDTQQENGSMFSLITWNIDGLDLNNLSERARGVCSYLALYSPDVIFLQEVIPPYYSYLKKRSSNYEIITGHEEGYFTAIMLKKSRVKLKSQEIIPFPSTKMMRNLLCVHVNVSGNELCLMTSHLESTRGHAAERMNQLKMVLKKMQEAPESATVIFAGDTNLRDREVTRCGGLPNNIVDVWEFLGKPKHCQYTWDTQMNSNLGITAACKLRFDRIFFRAAAEEGHIIPRSLDLLGLEKLDCGRFPSDHWGLLCNLDIIL
Protein: E3 ubiquitin-protein ligase ZNRF1 (EC 2.3.2.27) (Nerve injury-induced gene 283 protein) (RING-type E3 ubiquitin transferase ZNRF1) (Zinc/RING finger protein 1) (Q91V17)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that mediates the ubiquitination of AKT1 and GLUL, thereby playing a role in neuron cells differentiation. Plays a role in the establishment and maintenance of neuronal transmission and plasticity. Regulates Schwann cells differentiation by mediating ubiquitination of GLUL. Promotes Wallerian degeneration, a neurodegeneration disorder, by mediating 'Lys-48'-linked polyubiquitination and subsequent degradation of AKT1 in axons: degradation of AKT1 prevents AKT1-mediated phosphorylation of GSK3B, leading to GSK3B activation and phosphorylation of DPYSL2/CRMP2 followed by destabilization of microtubule assembly in axons.
Subcellular location: Endosome. Lysosome. Membrane; Peripheral membrane protein. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Associated with synaptic vesicle membranes in neurons.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 N
Sequence:
MGGKQSTAARSRGPFPGVSTDDSAVPPPGGAPHFGHYRTGGGAMGLRSRSVSSVAGMGMDPSTAGGVPFSLYTPASRGTGDSERAPGGGGSTSDSTYAHGNGYQETGGGHHRDGMLYLGSRASLADALPLHIAPRWFSSHSGFKCPICSKSVASDEMEMHFIMCLSKPRLSYNDDVLTKDAGECVICLEELLQGDTIARLPCLCIYHKSCIDSWFEVNRSCPEHPAD
Protein: Bacterial microcompartment shell protein EutK (Ethanolamine utilization protein EutK) (P76540)
Organism: Escherichia coli (strain K12)
Function: Probably a minor component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation. It might bind nucleic acids.
Subcellular location: Bacterial microcompartment {ECO:0000305|PubMed:20044574}.
Interaction partners:
- Bacterial microcompartment shell protein EutL
- Bacterial microcompartment shell vertex protein EutN
- Bacterial microcompartment shell protein EutS
- Ethanolamine ammonia-lyase small subunit
- Acetate kinase EutQ
- Ethanolamine utilization protein EutJ
- Probable acetate kinase EutP
- Ethanolamine ammonia-lyase reactivase EutA
- HTH-type DNA-binding transcriptional activator EutR
- Probable ethanolamine permease EutH
Sequence:
MINALGLLEVDGMVAAIDAADAMLKAANVRLLSHEVLDPGRLTLVVEGDLAACRAALDAGCAAAMRTGRVISRKEIGRPDDDTQWLVTGFNRQPKQPVREPDAPVIVAESADELLALLTSVRQGMTAGEVAAHFGWPLEKARNALEQLFSAGTLRKRSSRYRLKPH
Protein: C-terminal-binding protein 1 (CtBP1) (EC 1.1.1.-) (50 kDa BFA-dependent ADP-ribosylation substrate) (BARS-50) (C-terminal-binding protein 3) (CtBP3) (Q9Z2F5)
Organism: Rattus norvegicus (Rat)
Function: Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q13363}. Nucleus {ECO:0000269|PubMed:25652077}. Synapse, synaptosome {ECO:0000269|PubMed:25652077}.
Interaction partners:
- DNA endonuclease RBBP8
- C-terminal-binding protein 2
- Histone deacetylase 1
- Histone deacetylase 2
- Histone deacetylase 1
- Zinc finger protein 217
- Zinc finger E-box-binding homeobox 1
- Transcription factor 7
- MDS1 and EVI1 complex locus
- Lymphoid enhancer-binding factor 1
Sequence:
MSGVRPPIMNGPMHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGIERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYSRYPPGVVSVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHTTDQL
Protein: Coatomer subunit gamma-1 (Gamma-1-coat protein) (Gamma-1-COP) (Q4AEF8)
Organism: Rattus norvegicus (Rat)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it (By similarity). About 70% of the COPG1-containing coatomers are found in the cis-Golgi apparatus. {ECO:0000250, ECO:0000269|PubMed:17360540}.
Interaction partners:
- Coatomer subunit beta'
- Coatomer subunit beta
- Coatomer subunit zeta
- Coatomer subunit delta
- Coatomer subunit alpha
- Coatomer subunit epsilon
- Coatomer subunit zeta
- ADP-ribosylation factor GTPase-activating protein 2
- ADP-ribosylation factor 1
- ADP-ribosylation factor GTPase-activating protein 3
Sequence:
MLKKFDKKDEESGGGSNPLQHLEKSAVLQEARVFNETPINPRKCAHILTKILYLINQGEHLGTTEATEAFFAMTKLFQSNDPTLRRMCYLTIKEMSCIAEDVIIVTSSLTKDMTGKEDNYRGPAVRALCQITDSTMLQAVERYMKQAIVDKVPSVSSSALVSSLHLLKCSFDVVKRWVNEAQEAASSDNIMVQYHALGLLYHVRKNDRLAVSKMISKFTRHGLKSPFAYCMMIRVASKQLEEEDGSRDSPLFDFIESCLRNKHEMVVYEAASAIVNLPGCSAKELAPAVSVLQLFCSSPKAALRYAAVRTLNKVAMKHPSAVTACNLDLENLVTDSNRSIATLAITTLLKTGSESSIDRLMKQISSFMSEISDEFKVVVVQAISALCQKYPRKHAVLMNFLFTMLREEGGFEYKRAIVDCIISIIEENSESKETGLSHLCEFIEDCEFTVLATRILHLLGQEGPKTNNPSKYIRFIYNRVVLEHEEVRAGAVSALAKFGAQNEEMLPSILVLLKRCVMDDDNEVRDRATFYLNVLEQKQKALNAGYILNGLTVSIPGLEKALQQYTLEPSEKPFDLKSVPLATTPMTEQRPESTSTAAVKQPEKVAATRQEIFQEQLAAVPEFQGLGPLFKSSPEPVALTESETEYVIRCTKHTFSDHLVFQFDCTNTLNDQTLENVTVQMEPTEAYEVLSYVPVRSLPYNQPGTCYTLVALPKEDPTAVACTFSCVMKFTVKDCDPNTGEIDEEGYEDEYVLEDLEVTVADHIQKVMKVNFEAAWDEVGDEFEKEETFTLSTIKTLEEAVGNIVKFLGMHPCERSDKVPENKNTHTLLLAGVFRGGHDILVRSRLLLLDTVTMQVTARSSEELPVDIILASVG
Protein: Dodecenoyl-CoA delta-isomerase (EC 5.3.3.8) (Q9W0M0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- Enoyl-CoA delta isomerase 1, mitochondrial
- Enoyl-CoA delta isomerase 1, mitochondrial
- Enoyl-CoA delta isomerase 1, mitochondrial
- Peroxisomal multifunctional enzyme type 2
- Sterol carrier protein 2
- Acyl-coenzyme A oxidase
- Delta
- Acyl-coenzyme A oxidase
- GH04973p
- Dehydrogenase/reductase 4
Sequence:
MTYQGYKELLVEQQGKLLVAKFNNPKKKNCINRVAYQEMTRVLTEVNDDEGVTIVVFTGVGDIFTSGNDLSQSSNTDDIDAFFKQSNATFKAMVLSFVNCRKIVLALVNGPAIGIGATIVGLCDVAWCSETTYFYTPFTKLGLVPEGGSSYMLPLILGRSKASEILLLSEPLSAQEAYQFNFVSRIFKASELESVIWPKLRQYSELPTNSLLQGKRLVKDGFLENLIKANEAECKQLLQQFQHPEFAQAIIDFASRKNKAKL
Protein: PHEX protein (O35812)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MEAEAGSTMETGKGTNRGIRIALALFITGTLVLGTLLFLVSQGLLSFQAKQEYCLKPECIEAAAAIMSKVNLSVDPCENFFRFACDGWISNNPIPEDMPSYGVYPWLRHNVDLKLKALLEKSVSRRRDTEAVQKAKILYSSCMNEKAIEKADAKPLLHILRHSPFRWPVLEANIGPEGVWSERKFSLLQTLATFRGQYSNSVFIRLYVSPDDKASNEHILKLDQATLSLAVREDFLDNTTEAKSYRDALYKFMVDTAVLLGANSSRAEHDMKSVLRLEIKIAEIMIPHENRTSEAMYNKMNISELSAMIPQFDWLGYIKKVIDTRLYPHLKDIGPSENVVVRVPQYFKDLFRILGAERKKTIANYLVWRMVYSRIPNLSRRFQYRWLEFSRVIQGTTTLLPQWDKCVNFIESALPYVVGKMFVNVHFQEDKKEMMEELIEGVRWAFIDMLEKENEWMDAGTKRKAQEKARAVLAKVGYPEFIMNDTYVNEDLKAIKFSESDYFGNVLQTRKYLAQSDFFWLKKAVPKTEWFTNPTTVNAFYSASTNQIRFPAGELQKPFFWGTEYPRSLSYGAIGVIVGHEFTHGFDNNGRKYDKNGNLDPWWSVDSEEKFKEKTKCMINQYSNYYWKKAGLNVKGKRTLGENIADNGGLREAFRAYRKWINDRRQGVEEPLLPGITFTNNQLFFLSYAHVRCNSYRPEAAREQVQIGAHSPPQFRVNGAISNFEEFQKAFNCPANSTMNRGADSCRLW
Protein: Zinc finger protein 575 (Q86XF7)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MLERGAESAAGATDPSPTGKEPVTKEAPHQGPPQKPSQSAPGPTASAGSPPRPRRRPPPQRPHRCPDCDKAFSYPSKLATHRLAHGGARPHPCPDCPKAFSYPSKLAAHRLTHSGARPHPCPHCPKSFGHRSKLAAHLWTHAPTRPYPCPDCPKSFCYPSKLAAHRHTHHATDARPYPCPHCPKAFSFPSKLAAHRLCHDPPTAPGSQATAWHRCSSCGQAFGQRRLLLLHQRSHHQVEHKGERD
Protein: ATP synthase subunit s, mitochondrial (ATP synthase-coupling factor B) (FB) (Distal membrane arm assembly complex 2-like protein) (Mitochondrial ATP synthase regulatory component factor B) (Q99766)
Organism: Homo sapiens (Human)
Function: Involved in regulation of mitochondrial membrane ATP synthase. Necessary for H(+) conduction of ATP synthase. Facilitates energy-driven catalysis of ATP synthesis by blocking a proton leak through an alternative proton exit pathway.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P22027}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22027}.
Interaction partners:
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MMPFGKISQQLCGVKKLPWSCDSRYFWGWLNAVFNKVDYDRIRDVGPDRAASEWLLRCGAMVRYHGQERWQKDYNHLPTGPLDKYKIQAIDATDSCIMSIGFDHMEGLEHVEKIRLCKCHYIEDDCLLRLSQLENLQKTILEMEIISCGNITDKGIIALRHLRNLKYLLLSDLPGVREKENLVQAFKTALPSLELKLQLK
Protein: Ubiquitin thioesterase otulin (EC 3.4.19.12) (Deubiquitinating enzyme otulin) (OTU domain-containing deubiquitinase with linear linkage specificity) (Ubiquitin thioesterase Gumby) (Q3UCV8)
Organism: Mus musculus (Mouse)
Function: Deubiquitinase that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. Required during angiogenesis, craniofacial and neuronal development by regulating the canonical Wnt signaling together with the LUBAC complex. Acts as a negative regulator of NF-kappa-B by regulating the activity of the LUBAC complex (By similarity). OTULIN function is mainly restricted to homeostasis of the LUBAC complex: acts by removing 'Met-1'-linked autoubiquitination of the LUBAC complex, thereby preventing inactivation of the LUBAC complex. Acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. In myeloid cell, required to prevent unwarranted secretion of cytokines leading to inflammation and autoimmunity by restricting linear polyubiquitin formation. Plays a role in innate immune response by restricting linear polyubiquitin formation on LUBAC complex in response to NOD2 stimulation, probably to limit NOD2-dependent pro-inflammatory signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23708998}.
Interaction partners:
- E3 ubiquitin-protein ligase RNF31
- Sorting nexin-27
- Sharpin
- Ubiquitin-ribosomal protein eS31 fusion protein
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- Polyubiquitin-C
- Ubiquitin carboxyl-terminal hydrolase CYLD
- OTU domain-containing protein 3
- Polyubiquitin-B
- Tripartite motif-containing protein 14
Sequence:
MSRGTMPQPGAWPGASCAETPAREAGAAARDGGKVTAGAQPRAATRCPAEHEEDMYRAADEIEKEKELLIHERGISEPRLSVAPEMDIMDYCKKEWRGNTQKATCMKKGYEEVSQKFTSIRRVRGDNYCALRATLFQAMSQLAELPPWLQDLELILLPEKLINKYTWIKQWKLGLKFDGKSEDLVEKIKESLALLRKKWVSLAAMKTAEARQTACDELFTNEEEEYSLYEAVKFLMLNRAIELYDDKEKGKEVPFFSVLLFARDTSNDPEQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHSIRVYRLSKYNTEEFITVYPTDPPKDWPMVTLIAEDDRHYNIPVRVCEETSV
Protein: ETS translocation variant 5 (Ets-related protein ERM) (P41161)
Organism: Homo sapiens (Human)
Function: Binds to DNA sequences containing the consensus nucleotide core sequence 5'-GGAA.-3'.
Subcellular location: Nucleus.
Interaction partners:
- E3 ubiquitin-protein ligase COP1
- DET1 homolog
- Double homeobox protein 4-like protein 2
- Serine/threonine-protein kinase 40
- Solute carrier family 45 member 3
- Glial cell line-derived neurotrophic factor
- Transmembrane protease serine 2
- B-cell CLL/lymphoma 6 member B protein
Sequence:
MDGFYDQQVPFMVPGKSRSEECRGRPVIDRKRKFLDTDLAHDSEELFQDLSQLQEAWLAEAQVPDDEQFVPDFQSDNLVLHAPPPTKIKRELHSPSSELSSCSHEQALGANYGEKCLYNYCAYDRKPPSGFKPLTPPTTPLSPTHQNPLFPPPQATLPTSGHAPAAGPVQGVGPAPAPHSLPEPGPQQQTFAVPRPPHQPLQMPKMMPENQYPSEQRFQRQLSEPCHPFPPQPGVPGDNRPSYHRQMSEPIVPAAPPPPQGFKQEYHDPLYEHGVPGMPGPPAHGFQSPMGIKQEPRDYCVDSEVPNCQSSYMRGGYFSSSHEGFSYEKDPRLYFDDTCVVPERLEGKVKQEPTMYREGPPYQRRGSLQLWQFLVTLLDDPANAHFIAWTGRGMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCDPDALFSMAFPDNQRPFLKAESECHLSEEDTLPLTHFEDSPAYLLDMDRCSSLPYAEGFAY
Protein: V-type proton ATPase subunit H (V-ATPase subunit H) (V-ATPase 54 kDa subunit) (Vacuolar proton pump subunit H) (O14265)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity). This subunit is essential for activity, but not assembly, of the enzyme complex (By similarity). This subunit is also required for silencing the ATPase activity of V-ATPase when V1 is detached from V0 (By similarity).
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:P41807}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit E
- V-type proton ATPase subunit d
- V-type proton ATPase subunit B
- V-type proton ATPase subunit a
- V-type proton ATPase subunit c
- Probable V-type proton ATPase 20 kDa proteolipid subunit
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C
- V-type proton ATPase subunit F
- V-type proton ATPase subunit G
Sequence:
MSNSDLELSNAASPPPVELDNSQVDEIINNVRCVAIPWQGYQRSGSLEENELQEIENLTGKPLSAYVKTAEEDTTAYSNLFLKLLSMKDTPDVVNFALVKLADTLLNSNKFLSAFGPAFYDFLEKDESYINYLDDDSKLLFARVFALCSSSSPCSVAKAFTLFLEYLGKLMQSLNPLTRLFAVQCLNGVLTLKAHRYALWAENTCSFRLAELLRNSIGDTQLQYYSLFCFWQLTFESHIAQDINKRFDLIKLLVQIIRSDTKTKVYRLVLAILVNLIDKAPKDTISTMLLEHVDKAVQLLQKRKWADEDITNYLDFITSTLDESSKHLSTFDMYKSELDTGILHWSPSHRSEDFWHQNAKRLNEDNYALLKKLFHIVQYNEDNTSLAVACHDLGAYIRSYPEGRSLIIKYGAKQRIMDLMSHPDPEVRFEALSTVQLLMTEVCFLSKITL
Protein: 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (OHCU decarboxylase) (EC 4.1.1.97) (Parahox neighbor) (Ureidoimidazoline (2-oxo-4-hydroxy-4-carboxy-5-) decarboxylase) (Q283N4)
Organism: Mus musculus (Mouse)
Function: Catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.
Subcellular location: Peroxisome {ECO:0000305}.
Interaction partners:
- 5-hydroxyisourate hydrolase
Sequence:
MDMVKVNSMDFGEFVDVFGNIVEKCPLIAAAVWSQRPFSGLEDLENHFFAFIDALPRSGQEGILRCHPDLAGRDLQQGTLTAESQREQSQAGLTSLDTDDRLRLQQLNAQYRERFGFPFVLAARLSDRATVPRELARRLQCQPESELRTALGEVKKISHLRLTDLLGAHSHSARVELP
Protein: Probable small nuclear ribonucleoprotein Sm D2 (Sm-D2) (snRNP core protein D2) (Q9VI10)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P62316}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62316}.
Interaction partners:
- Probable small nuclear ribonucleoprotein E
- U1 small nuclear ribonucleoprotein 70 kDa
- Small nuclear ribonucleoprotein-associated protein B
- Small nuclear ribonucleoprotein F
- U1 small nuclear ribonucleoprotein C
- Probable small nuclear ribonucleoprotein G
- Probable small nuclear ribonucleoprotein Sm D1
- U6 snRNA-associated Sm-like protein LSm2
- Small nuclear ribonucleoprotein Sm D3
- Lsm10
Sequence:
MALVKPKSELTPEELARQEEEEFNTGPLSVLTQSVKNNTQVLINCRNNKKLLGRVKAFDRHCNMVLENVKEMWTELPRTGKGKKKVKPVNKDRFISKMFLRGDSVILVLRNPLATAAGK
Protein: Factor arrest protein 7 (P43592)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Participates in the control of the reentry into the cell cycle following pheromone treatment.
Interaction partners:
- Factor arrest protein 3
- Vacuolar protein sorting-associated protein 64
- Factor arrest protein 8
- Factor arrest protein 10
- Factor arrest protein 11
- Serine/threonine-protein phosphatase PP2A-like PPG1
Sequence:
MSDQINVLSMQQQQQQQQQQQQVYMSPQAENLNHMYLLVNKLVKQLRENQAEKAKILRNIDILSGSLNKYETSEEPHDTTENIALFNRFLEQRGKAPITEKEQLSNNLDENAKDDVMLGVLKRQNSMLRKSLQESKQVTLESMDLLSYSEDSLNYIVAQLRGNILMHHKETIKLIRQKFQTETIPLEDEEFKMYLENVNGLQKLTDISHTYRLLLRLHAQD