wanglab/gogpt-training-data huggingface dataset:
Protein: 40S ribosomal protein S21 (Q8WVC2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Rough endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004427}.
Interaction partners:
Sequence:
MQNDAGEFVDLYVPRKCSASNRIIGAKDHASIQMNVAEVDKVTGRFNGQFKTYAICGAIRRMGESDDSILRLAKADGIVSK
Protein: Prohibitin-3, mitochondrial (Atphb3) (Protein ENHANCED ETHYLENE RESPONSE 3) (O04331)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins (By similarity). Necessary for mitochondrial and cell metabolism and biogenesis. Required to regulate the ethylene-mediated signaling; involved in growth maintenance in the presence of ethylene. Functions in nitric oxide (NO)-mediated responses and in hydrogen peroxide-induced NO accumulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130}. Mitochondrion inner membrane {ECO:0000269|PubMed:12837548, ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17883375, ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:21841088, ECO:0000269|PubMed:9132067}; Single-pass type II membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:17525078}. Cytoplasm {ECO:0000269|PubMed:17525078}.
Interaction partners:
- Prohibitin-6, mitochondrial
- Prohibitin-1, mitochondrial
- Prohibitin-2, mitochondrial
- Prohibitin-7, mitochondrial
- Gamma carbonic anhydrase 2, mitochondrial
- At5g54100
- SPFH/Band 7/PHB domain-containing membrane-associated protein family
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Prohibitin-4, mitochondrial
Sequence:
MGSQQAAVSFLSNLAKAAFGLGTAATVLNTSLFTVDGGERAVIFDRFRGVMDQTVGEGTHFLIPILQRPHIFDIRTKPHTFSSISGTKDLQMVNLTLRVLSRPEVSRLPYIFQTLGLEYDEKVLPSIGNEVLKAVVAQFNADQLLTERPHVSALVRESLITRAKDFNIVLDDVAITHLSYGVEFSRAVEQKQVAQQEAERSKFVVMKADQERRAAVIRAEGESEAAQLISDATAKAGMGLIELRRIEASREIASTLARSPNVAYLPGGQSMLFALNR
Protein: Killer cell lectin-like receptor subfamily I member 2 (Q5DT37)
Organism: Rattus norvegicus (Rat)
Function: Lectin-like receptor for natural killer (NK) cells. Heterodimer formation with KLRE1 mediates NK cell cytolytic activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15650876, ECO:0000269|PubMed:18713988}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Killer cell lectin-like receptor subfamily E member 1
- Killer cell lectin-like receptor subfamily H, member 1
Sequence:
MPRKKQNERGTNKQEIINIETKSSTFQEKQRQSKTDQISTVWRKEQKKQELKVHTELHPQHRTGFNEDKGTDPWLTTWRIITVILGTSCIILVTKVGFLIPNLFSRGEKRSRELSLLDSLCLKNNDSFCDLCSHDWIAFGNNFYLFFRGTKTWAESKSACEELNSYLLDIDSRAELENLLLFEINGWILFKTDAINRSLRKNYIKIHQTLFNDSEKKNHSCHYLSGNQFSAGDCSSKKAYTCEFNLQ
Protein: Alanine--glyoxylate aminotransferase 2 homolog 2, mitochondrial (EC 2.6.1.44) (Beta-alanine-pyruvate aminotransferase 2) (Q94AL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305|PubMed:25732537}.
Interaction partners:
- Serine--glyoxylate aminotransferase
- Branched-chain-amino-acid aminotransferase 2, chloroplastic
- Glutamate--glyoxylate aminotransferase 2
- Alanine aminotransferase 2, mitochondrial
- Glutamate--glyoxylate aminotransferase 1
- Alanine aminotransferase 1, mitochondrial
- Aldehyde dehydrogenase family 7 member B4
- Aldehyde dehydrogenase family 3 member I1, chloroplastic
- Aldehyde dehydrogenase family 3 member F1
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
Sequence:
MQRFAAKRSVQNISVSLWRRCISSTSQAATASVKDSDEFQARLPPFAYTPPPYTGPSADVILSKRKEFLSPSMFCLYRKPLNIVDGKMQYLFDESGRRYLDAFAGIAVVNCGHCHPDVVEPVINQIKRLQHPTVLYLNHAIADFSEALASKLPGDLKVVFFTNSGTEANELALMMAKLYTGCQDIVAVRNGYHGNAAATMGATGQSMWKFNVVQNSVHHALNPDPYRGVFGSDGEKYAKDLQDLIQYGTTGHIAGFICEAIQGVGGIVELAPGYLSAAYDTVKKAGGLFIADEVQSGFARTGNFWGFEAHNVVPDIVTMAKGIGNGFPLGAVVTTPEIAGVLTRRSYFNTFGGNSVSTTAGLAVLNVIEKEKLQENAAMVGSYLKEKLTQLKEKHEIIGDVRGRGLMLGVELVSDRKLKTPATAETLHIMDQMKELGVLIGKGGYFGNVFRITPPLCFTKDDADFLVEAMDYSMSKM
Protein: WAP four-disulfide core domain protein 12 (Elafin-like protein II) (Single WAP motif protein 2) (Whey acidic protein 2) (Q9JHY3)
Organism: Mus musculus (Mouse)
Function: Antibacterial protein which inhibits the growth of E.coli and S.aureus. Putative acid-stable proteinase inhibitor.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- WAP four-disulfide core domain 5
- WAP four-disulfide core domain protein 15B
Sequence:
MWPNSILVLMTLLISSTLVTGGGVKGEEKRVCPPDYVRCIRQDDPQCYSDNDCGDQEICCFWQCGFKCVLPVKDNSEEQIPQSKV
Protein: Cyclin CCL1 (P37366)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulatory component of the TFIIK complex (KIN28-CCL1 dimer) which is the protein kinase component of transcription factor IIH (TFIIH) and phosphorylates the C-terminal domain of RNA polymerase II during transition from transcription to elongation after preinitiation complex (PIC) formation, thereby positively regulating transcription. TFIIH (or factor B) is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has DNA-dependent ATPase activity and is essential for polymerase II transcription in vitro.
Interaction partners:
- General transcription and DNA repair factor IIH helicase subunit XPD/RAD3
- RNA polymerase II transcription factor B subunit 3
- General transcription and DNA repair factor IIH subunit TFB4
- General transcription and DNA repair factor IIH subunit SSL1
- Transcription initiation factor IIE subunit alpha
- Transcription initiation factor IIE subunit beta
- Serine/threonine-protein kinase KIN28
- General transcription and DNA repair factor IIH subunit TFB1
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB/SSL2
- General transcription and DNA repair factor IIH subunit TFB2
Sequence:
MTDIQLNGKSTLDTPSATMSAKEKEAKLKSADENNKPPNYKRISDDDLYRHSSQYRMWSYTKDQLQEKRVDTNARAIAYIEENLLKFREAHNLTEEEIKVLEAKAIPLTMEEELDLVNFYAKKVQVIAQHLNLPTEVVATAISFFRRFFLENSVMQIDPKSIVHTTIFLACKSENYFISVDSFAQKAKSTRDSVLKFEFKLLESLKFSLLNHHPYKPLHGFFLDIQNVLYGKVDLNYMGQIYDRCKKRITAALLTDVVYFYTPPQITLATLLIEDEALVTRYLETKFPSREGSQESVPGNEKEEPQNDASTTEKNKEKSTESEEYSIDSAKLLTIIRECKSIIEDCKPPSTEEAKKIAAKNYYCQNPSTLIQKLKRKLNGEDTSSTVEKKQKT
Protein: 1-acylglycerol-3-phosphate O-acyltransferase PNPLA3 (EC 2.3.1.51) (Acylglycerol transacylase) (Adiponutrin) (ADPN) (Calcium-independent phospholipase A2-epsilon) (iPLA2-epsilon) (EC 3.1.1.4) (Lysophosphatidic acid acyltransferase) (Patatin-like phospholipase domain-containing protein 3) (EC 3.1.1.3) (Q9NST1)
Organism: Homo sapiens (Human)
Function: Specifically catalyzes coenzyme A (CoA)-dependent acylation of 1-acyl-sn-glycerol 3-phosphate (2-lysophosphatidic acid/LPA) to generate phosphatidic acid (PA), an important metabolic intermediate and precursor for both triglycerides and glycerophospholipids. Does not esterify other lysophospholipids. Acyl donors are long chain (at least C16) fatty acyl-CoAs: arachidonoyl-CoA, linoleoyl-CoA, oleoyl-CoA and at a lesser extent palmitoyl-CoA. Additionally possesses low triacylglycerol lipase and CoA-independent acylglycerol transacylase activities and thus may play a role in acyl-chain remodeling of triglycerides. In vitro may express hydrolytic activity against glycerolipids triacylglycerol, diacylglycerol and monoacylglycerol, with a strong preference for oleic acid as the acyl moiety. However, the triacylglycerol hydrolase activity is controversial and may be very low. Possesses phospholipase A2 activity.
Subcellular location: Membrane {ECO:0000269|PubMed:15364929, ECO:0000269|PubMed:22560221}; Single-pass type II membrane protein {ECO:0000269|PubMed:15364929}. Lipid droplet {ECO:0000269|PubMed:20034933, ECO:0000269|PubMed:22560221}.
Interaction partners:
- Hepatic triacylglycerol lipase
- Pancreatic triacylglycerol lipase
- Lipoprotein lipase
- Phospholipid phosphatase 5
- Phospholipid phosphatase 4
- Monoglyceride lipase
- Alanine aminotransferase 1
- Sorting and assembly machinery component 50 homolog
- Endothelial lipase
- Gastric triacylglycerol lipase
Sequence:
MYDAERGWSLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIGIFHPSFNLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDGGVSDNVPFIDAKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRGYLDAFRFLEEKGICNRPQPGLKSSSEGMDPEVAMPSWANMSLDSSPESAALAVRLEGDELLDHLRLSILPWDESILDTLSPRLATALSEEMKDKGGYMSKICNLLPIRIMSYVMLPCTLPVESAIAIVQRLVTWLPDMPDDVLWLQWVTSQVFTRVLMCLLPASRSQMPVSSQQASPCTPEQDWPCWTPCSPKGCPAETKAEATPRSILRSSLNFFLGNKVPAGAEGLSTFPSFSLEKSL
Protein: Mitomycin biosynthesis 6-O-methyltransferase (EC 2.1.1.316) (Mitomycin 7-O-methyltransferase) (Q9X5T6)
Organism: Streptomyces lavendulae
Function: Involved in the biosynthesis of the quinone methoxy group present in the mitomycin A and B, which are used as anticancer agents. In vitro, catalyzes the 6-O-methylation of both C9-beta- and C9-alpha-configured 6-hydroxymitomycins via the transfer of the S-methyl group of S-adenosyl-L-methionine (AdoMet) to the 6-demethylmitomycin A and B. It can also use hydroxyquinone as substrate.
Interaction partners:
Sequence:
MTVEQTPENPGTAARAAAEETVNDILQGAWKARAIHVAVELGVPELLQEGPRTATALAEATGAHEQTLRRLLRLLATVGVFDDLGHDDLFAQNALSAVLLPDPASPVATDARFQAAPWHWRAWEQLTHSVRTGEASFDVANGTSFWQLTHEDPKARELFNRAMGSVSLTEAGQVAAAYDFSGAATAVDIGGGRGSLMAAVLDAFPGLRGTLLERPPVAEEARELLTGRGLADRCEILPGDFFETIPDGADVYLIKHVLHDWDDDDVVRILRRIATAMKPDSRLLVIDNLIDERPAASTLFVDLLLLVLVGGAERSESEFAALLEKSGLRVERSLPCGAGPVRIVEIRRA
Protein: Putative thiosulfate sulfurtransferase (EC 2.8.1.1) (Rhodanese-like protein) (P9WHF9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May be a sulfotransferase involved in the formation of thiosulfate.
Interaction partners:
- Putative thiosulfate sulfurtransferase SseB
- Adenosine 5'-phosphosulfate reductase
- Uncharacterized protein Rv3118
- IscS-like cysteine desulfurase
- Sulfite reductase [ferredoxin]
- Putative thiosulfate sulfurtransferase SseA
- Putative cystathionine beta-lyase
- cysteine-S-conjugate beta-lyase
- Cystathionine gamma-synthase
- O-acetylserine sulfhydrylase
Sequence:
MARCDVLVSADWAESNLHAPKVVFVEVDEDTSAYDRDHIAGAIKLDWRTDLQDPVKRDFVDAQQFSKLLSERGIANEDTVILYGGNNNWFAAYAYWYFKLYGHEKVKLLDGGRKKWELDGRPLSSDPVSRPVTSYTASPPDNTIRAFRDEVLAAINVKNLIDVRSPDEFSGKILAPAHLPQEQSQRPGHIPGAINVPWSRAANEDGTFKSDEELAKLYADAGLDNSKETIAYCRIGERSSHTWFVLRELLGHQNVKNYDGSWTEYGSLVGAPIELGS
Protein: Mitochondrial amidoxime reducing component 2 (mARC2) (EC 1.7.-.-) (Molybdenum cofactor sulfurase C-terminal domain-containing protein 2) (MOSC domain-containing protein 2) (Moco sulfurase C-terminal domain-containing protein 2) (Q922Q1)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reduction of N-oxygenated molecules, acting as a counterpart of cytochrome P450 and flavin-containing monooxygenases in metabolic cycles. As a component of prodrug-converting system, reduces a multitude of N-hydroxylated prodrugs particularly amidoximes, leading to increased drug bioavailability. May be involved in mitochondrial N(omega)-hydroxy-L-arginine (NOHA) reduction, regulating endogenous nitric oxide levels and biosynthesis. Postulated to cleave the N-OH bond of N-hydroxylated substrates in concert with electron transfer from NADH to cytochrome b5 reductase then to cytochrome b5, the ultimate electron donor that primes the active site for substrate reduction.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P0C2C3}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0C2C3}. Peroxisome {ECO:0000269|PubMed:17768142}.
Interaction partners:
- Cytochrome b5 type B
Sequence:
MGSSSSTALARLGLPGQPRSTWLGVAALGLAAVALGTVAWRRTRPRRRRQLQQVGTVSKVWIYPIKSCKGVSVCETECTDMGLRCGKVRDRFWMVVKEDGHMVTARQEPRLVLVSITLENNYLTLEAPGMEQIVLPIKLPSSNKIHNCRLFGLDIKGRDCGDEVAQWFTNYLKTQAYRLVQFDTSMKGRTTKKLYPSESYLQNYEVAYPDCSPVHLISEASLVDLNTRLKKKVKMEYFRPNIVVSGCEAFEEDTWDELLIGDVEMKRVLSCPRCVLTTVDPDTGIIDRKEPLETLKSYRLCDPSVKSIYQSSPLFGMYFSVEKLGSLRVGDPVYRMVD
Protein: Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase (EC 4.2.1.134) (F4KGW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU363109}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363109}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAGFLSVVRRVYLTLYNWIVFAGWAQVLYLAITTLKETGYENVYDAIEKPLQLAQTAAVLEILHGLVGLVRSPVSATLPQIGSRLFLTWGILYSFPEVRSHFLVTSLVISWSITEFPITTWIVEIIRYSFFGFKEALGFAPSWHLWLRYSSFLLLYPTGITSEVGLIYLALPHIKTSEMYSVRMPNILNFSFDFFYATILVLAIYVPGSPHMYRYMLGQRKRALSKSKRE
Protein: NADH-ubiquinone oxidoreductase chain 1 (EC 7.1.1.2) (NADH dehydrogenase subunit 1) (P03887)
Organism: Bos taurus (Bovine)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I. Essential for the assembly of complex I (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:25209663}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 3
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH-ubiquinone oxidoreductase chain 6
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 4L
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- Cytochrome c oxidase subunit 1
Sequence:
MFMINILMLIIPILLAVAFLTLVERKVLGYMQLRKGPNVVGPYGLLQPIADAIKLFIKEPLRPATSSASMFILAPIMALGLALTMWIPLPMPYPLINMNLGVLFMLAMSSLAVYSILWSGWASNSKYALIGALRAVAQTISYEVTLAIILLSVLLMSGSFTLSTLITTQEQMWLILPAWPLAMMWFISTLAETNRAPFDLTEGESELVSGFNVEYAAGPFALFFMAEYANIIMMNIFTAILFLGTSHNPHMPELYTINFTIKSLLLTMSFLWIRASYPRFRYDQLMHLLWKNFLPLTLALCMWHVSLPILTSGIPPQT
Protein: Glomulin (FK506-binding protein-associated protein) (FAP) (FKBP-associated protein) (Q8BZM1)
Organism: Mus musculus (Mouse)
Function: Regulatory component of cullin-RING-based SCF (SKP1-Cullin-F-box protein) E3 ubiquitin-protein ligase complexes. Inhibits E3 ubiquitin ligase activity by binding to the RING domain of RBX1 and inhibiting its interaction with the E2 ubiquitin-conjugating enzyme CDC34. Inhibits RBX1-mediated neddylation of CUL1 (By similarity). Required for normal stability and normal cellular levels of key components of SCF ubiquitin ligase complexes, including FBXW7, RBX1, CUL1, CUL2, CUL3, CUL4A, and thereby contributes to the regulation of CCNE1 and MYC levels. Essential for normal development of the vasculature. Contributes to the regulation of RPS6KB1 phosphorylation (By similarity).
Interaction partners:
- HEAT repeat-containing protein 1
- Protein RRP5 homolog
- WD repeat domain 36
- RNA cytidine acetyltransferase
- DDB1- and CUL4-associated factor 13
- Periodic tryptophan protein 2 homolog
- WD repeat-containing protein 75
- Nucleolar protein 14
- BMS1 homolog, ribosome assembly protein
- Transducin beta-like protein 3
Sequence:
MAVEELQSIIKRCQILEEHDFKEEDFGLFQLAGQRCIEDGYINQLLEIIQDEKNKTIIKSMGWNLVGPVVRCLLRGREEDKREECFLIFDLLVKLCNPKELLLGLLELIEEPSGKQISQIILLLLQPLQTVIQKLPNNKAYSVGLALSTLWSQLSLLPVPHSEEQIQADDYGLCQCCKALIEFTKPFVEEVISDKENKENAKLKDELLKFCFKGLKCPLLTAQFLEQSEDVGNDPFRCFASEIIGFLSKIGHPVPQIILNHGRKKRTWDYLEFEEEEDKQLAESVASLTYLVFVQGIGIDQLPMVLSPSYLLQLNMEHIEVFLQRTEQSIYSKGLELLETSLLRLEDNSLCYQYLEIKSFLAVPQGLVKVMTLCPIETLRKKGLSMLQLFIDKLDSQGKYTLFRCLLNTSNHSGVEAFVIQNIKNQIDLSFKKTYNKWFAGAQLISLLDLVLSLPEGAETDLLQNSDRIMASLNLLRYLVIKDNEDDNQTGLWTELGKIENNFLKPLHIGLNMSKAHYEAEIKNSQQNNQVASMCKGVCSVTVGGEEIPSMPPEMQLKVLHSALFTFDLIESVLARVEELIEIKSKSTSEENVGIK
Protein: Poly (ADP-ribose) polymerase family, member 6 (A0A8I6GHS7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDIKGQFWNDDDSEGDNESEEFLYGVQGSCAADLYRHPQLDADIEAVKEIYSENSVSIREYGTIDDVDIDLHINISFLDEEVSTAWKVLRTEPIVLRLRFSLSQYLDGPEPSIEVFQPSNKEGFGLGLQLKKILYMFTSQQWKHLSNDLLKTQQEKRHSWFKASGSIRKFRAGLSIFSPIPKSPSFPIIQDSMLKGKLGVPELRVGRLMNRSISCTMKNPKVEVFGYPPSPQAGLLCPQHVGLPPPARTSPLVSGHCKNIPTLEYGFLVQIMKYAEQRVPTLNEYCVVCDEQHVFQNGSMLKPAVCTRELCVFSFYTLGVMSGAAEEVATGAEVVDLLVAMCRAALESPRKSIIFEPYPSVVDPTDPKTLAFNPKKKNYERLQKALDSVMSIREMTQGSYLEIKKQMDKLDPLAHPLLQWIISSNRSHIVKLPLSRQLKFMHTSHQFLLLSSPPAKEARFRTAKKLYGSTFAFQNGQRTAQDAFQGRAGPEIQQDEHHPPDPIHSVKVPAESESKLYSTL
Protein: Expressed protein (HSP20-like chaperones superfamily protein) (SLT1 protein) (O80926)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein NDL1
- AT3g18240
- Protein NDL3
- Small ribosomal subunit protein eS27y
- Alpha/beta-Hydrolases superfamily protein
- Protein NDL2
- Uncharacterized protein
- At3g26990
- At1g44770
- Elongation factor
Sequence:
MENHHPSTLLSMDSSASSHEELDLEMNNNRQSLLSGPPDINLPLSAERSPPPPPWNLDACDILDVGLGSQAYETENYMSVVPKVGRKCAKRVDSIWGAWFFFSFYFKPALNEKSKAKIVRDSNGISGFDKSDLKLDVFLVQHDMENMYMWVFKERPENALGKMQLRSYMNGHSRQGDRLFPFSVEKGFVRSHRMQRKHYRGLSNPQCVHGIELVPLPNLTCLDEEERKRWMELTGRDLNFTIPPEASDFGSWRNLPNTDFELERPTPSLKNPTANHSKKLLNGSGLNLSTQPSNHSNGEATDLSPSSHKKRKDLFSNGIHEEECCLTVNPQPPVIEAHQNELPTWSNEFTGAMKNVYGPVTAAKTIYEDEEGYLIIISLPFVDLNSVKVSWRNTLTHGIIKVSCLSTSRVPFIKRHDRTFKLTDSASEHCPPGEFVREIPLSNRIPEDANIEAYYDGPGSVLEILVPKLRAGPEEHEVRVCLRPNLGGNDLMLT
Protein: Torsin-like protein (Abnormal oocyte formation protein 5) (Q95NU5)
Organism: Caenorhabditis elegans
Function: May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|Ref.2}.
Interaction partners:
- Chloride channel CLIC-like protein 1
- Torsin-1B
- GEX Interacting protein
- MEiosis-to-MItosis transition associated
- Nucleoporin ndc-1
- Zygote defective protein 12
Sequence:
MKLDYVLLLLFHLCFVNTELISVITGKIKDSGTTIAISAGAFWGLKDRLKCYLYECCHEPDVNFNYHTLDADIANLLFGQHLVKDVVVNSIKSHWYNENPRKPLVLSFHGYTGSGKNYVAEIIANNTFRLGLRSTFVQHIVATNDFPDKNKLEEYQVELRNRILTTVQKCQRSIFIFDEADKLPEQLLGAIKPFLDYYSTISGVDFRRSIFILLSNKGGGEIARITKEQYESGYPREQLRLEAFERELMNFSYNEKGGLQMSELISNHLIDHFVPFLPLQREHVRSCVGAYLRKRGRGDLVSNVDFVERVLNSLQYFPESSKAFSSSGCKRVDAKTDLEMAKIRPLLSSVHFDDEL
Protein: Claudin (A0A2R8QM21)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, tight junction {ECO:0000256|RuleBase:RU060637}. Cell membrane {ECO:0000256|RuleBase:RU060637}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU060637}.
Interaction partners:
Sequence:
MSTGVQLLGFLMCLGGWLLSFISLLNDSWRVSSFSDQLITSQWYYQNLWQTCAKASTGVTNCKEFESMLSLAGYIQACRALMIIALILGLLSVVLASMGLKCTKLGSTSEEAKGKISLTAGIMFILSGLCVIVAVSWYAARVVQEFNDPFYGGTKYELGAGLYLGWAAAALCILGGGTLCTSFKGSSPAQTRGPGYNYSAAQPQKIYRSAPSDNSITKAYV
Protein: Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Jumonji domain-containing protein 6) (Phosphatidylserine receptor) (dPSR) (Q9VD28)
Organism: Drosophila melanogaster (Fruit fly)
Function: Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase.
Subcellular location: Nucleus {ECO:0000269|PubMed:17522160, ECO:0000269|PubMed:28701701}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28701701}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6NYC1}. Cytoplasm {ECO:0000250|UniProtKB:Q6NYC1}. Note=Mainly found throughout the nucleoplasm. {ECO:0000250|UniProtKB:Q6NYC1}.
Interaction partners:
Sequence:
MSEEFKLPKRSRKRTREVKRKARPELDGENAWSAMRYCEKFEPFWDFTDNLERIEESQVPESEFIERFERPYKPVVIRGCTDGWLALEKWTLARLAKKYRNQKFKCGEDNEGYSVKMKMKYYVEYMQSTRDDSPLYIFDSSFGEHHRRRKLLDDYVVPKYFRDDLFQYCGENRRPPYRWFVMGPARSGTGIHIDPLGTSAWNTLIRGHKRWCLFPTQTPKELLKVTSAMGGKQRDEAITWFSTIYPRTQLPSWPEQYRPIEVLQGAGETVFVPGGWWHVVLNMDDTIAITQNFSSQTNFPCVWHKTVRGRPKLSRKWLRVLRDQRPELAQIADSINLNESTGFASDSSSNSSSSSSSSSSSSEEEESDDGGDSNTDSGQESLTAKKKKKRRMAGGGSGSGSMGGSSRS
Protein: BTB-V protein domain (Q7JPL8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
QYFSLRWNNYQNTMTSVFQQLREDLSFVDVTLSCEHGSLKAHKVVLSACSTYFQKLLLENPCKHPTIILPADIIFTDLKTIIDFVYRGEIDVTESELQ
Protein: Interleukin (O42396)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MMCKVLIFGCISVATLMTTAYGASLSSAKRKPLQTLIKDLEILENIKNKIHLELYTPTETQECTQQTLQCYLGEVVTLKKETEDDTEIKEEFVTAIQNIEKNLKSLTGLNHTGSECKICEANNKKKFPDFLHELTNFVRYLQK
Protein: U1 snRNP-associated protein usp109 (O94621)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-processing factor 39
- U1 small nuclear ribonucleoprotein 70 kDa homolog
- U1 snRNP-associated protein usp107
- U1 snRNP-associated protein usp106
- U1 small nuclear ribonucleoprotein C
- U1 snRNP-associated protein usp108
- U1 small nuclear ribonucleoprotein usp102
- Pre-mRNA-processing protein prp40
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein E
Sequence:
MSTSLWLNNLEEWMNEDYIRAIFENVRKVNYYEDGESGAILKTCCIEFESQDAARNALERQSTQRLISGNPISLDVVPEWQKPSYYMLFISNIDPEVSENDIKYLFQRYNFISARVLRCVDGTSTSIAFIWLANESDIQNAQVEMQGAFCLKRSILVHSVKSDKNTYLSSPGFYGTPQPLNQFTDPNNTAVYVHQLPENITTQELRSYFLHFGEILYTQVNNNSGRIVFAQRYFAEQAINEMNNFPLHGVRIQLSWARPPSMALLPSKQSTYWPALAAPVYPSMKDVPNNPFTPFSPINPYYAKSWNHTASAPLLPPGLKNGSDYPYLSVPPDILNDSYLAMCEAVNSRLDAESTMLLPVHYSQA
Protein: Cysteine protease atg-4.2 (EC 3.4.22.-) (Autophagy-related protein 4 homolog 2) (Q9U1N6)
Organism: Caenorhabditis elegans
Function: Cysteine protease required for autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins lgg-1, to reveal a C-terminal glycine (Probable). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (Probable). Its cleavage activity is functionally redundant to atg-4.1, but it cleaves lgg-1 precursors less efficiently than atg-4.1 (Probable). In contrast to atg-4.1, plays a more significant role in the later phases of autophagy and in addition has a role in autophagosome maturation. Acts redundantly with atg-4.1 to promote the lgg-1 delipidation to release the protein from membranes, which facilitates multiple events during macroautophagy. Regulates the accumulation of autophagic structures in neurons and is specifically, required for the maturation and elimination of autophagosomes from the synaptic region of AIY interneurons.
Subcellular location: Cytoplasm {ECO:0000255|RuleBase:RU363115, ECO:0000269|PubMed:30880001}.
Interaction partners:
- Protein lgg-1
- Protein lgg-2
- Ubiquitin-like-conjugating enzyme ATG3
- Serine/threonine-protein kinase unc-51
- Cysteine protease atg-4.1
- Ubiquitin-like modifier-activating enzyme ATG7
- Ubiquitin-like protein atg-12
- Autophagy-related protein 9
- Autophagy-related protein 5
- Beclin homolog
Sequence:
MNNIPDDFKKIASSSRLPRKYCSSESSLSDDDGHEIEHVLKHGAPEEALTPDTERMVVLGQDVVQSAPASLVPGGNLSWMSKIKSAGASMMGSIRPSSSSQDVHSTGEIEKHSKKKWKARLWSTWNNIKYSSTWMSDRSDEYGGENDVVFLGRRYSTSVDESGLRSGFENFCSDYYSRLWITYRTDFPALLDTDTTTDCGWGCMIRTTQMMVAQAIMVNRFGRDWRFTRRKRSHVAAHGDEDDFDREKIQEWMILKLFEDKPTAPLGIHKMVGIAAMGKGKKAVGSWYSPSEAVFIMKKALTESSSPLTGNTAMLLSIDGRVHIRDIEVETKNWMKKLILVIVVRLGAAELNPIYVPHLMRLFAMESCLGITGGRPDHSSWFVGYYGDQIIYLDPHVAHEYIPIDINPNTNVVDSDSKKAKKCPEKSYHCRLLSKMHFFDMDPSCALCFQFESREQFDNDMRQLNLSQFIDIDQGEEHGMKRVRDPMFSVVYGERRQPPSYEREVSETEQAQADKHGFEML
Protein: Uncharacterized protein YBR085C-A (O43137)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Proteasome subunit beta type-6
Sequence:
MSSALYKQSTNFTHSTGSFLQSAPVELTTVSGYQEFLKKQEKKNYEIQTVLSEDKSHGYVLKDGEVIANIIGEAKDYLLDLAGQA