wanglab/gogpt-training-data huggingface dataset:
Protein: Prostaglandin E synthase 3 (EC 5.3.99.3) (Cytosolic prostaglandin E2 synthase) (cPGES) (Hsp90 co-chaperone) (Progesterone receptor complex p23) (Sid 3177) (Telomerase-binding protein p23) (Q9R0Q7)
Organism: Mus musculus (Mouse)
Function: Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q3ZBF7}.
Interaction partners:
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- Prostaglandin E synthase 2
- Prostaglandin E synthase
- Stress-induced-phosphoprotein 1
- Peptidyl-prolyl cis-trans isomerase FKBP4
- Peptidyl-prolyl cis-trans isomerase FKBP5
- Glucocorticoid receptor
- AH receptor-interacting protein
- Serine/threonine-protein phosphatase 5
Sequence:
MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMDHMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE
Protein: Transmembrane protein 53 (Q9TZH8)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein
- BTB domain-containing protein
- Serine or cysteine protease inhibitor
- Trafficking protein particle complex subunit 11 domain-containing protein
- TUG ubiquitin-like domain-containing protein
- Homogentisate 1,2-dioxygenase
Sequence:
MFASRRLLPKIAKSTSSTSSAVISTCIQKRNYFTRHVPEPKMMIHLSKSQDVTVDSIVLSDSHHDEKKPVILMVGWAGANPKHIDKYIKVYNDEGYRVVSLCPPCYHYSIPNSRVGFYMSPLFRAIDAKPGDFRSFAKCPIIVHSFSMNGVRGLISFWKWTEAEEKPQLRERIKGIIFDSAPSRPYGKQDATAMVISTPPIDAFERWISEQTRISVLTWFLNLRAYLQIPLLTMVPFLRSFVSIYYYLQTHIALPRDQLYLYSKADTMIKAKHVEKFIEKQKEKGNSVTAIDFVDSEHVAHIRTHPKDYRTACLNFVRHVEASYK
Protein: HIG1 domain-containing protein C25B8.07c, mitochondrial (Q9UTB1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion membrane {ECO:0000255|PROSITE-ProRule:PRU00836, ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 2
- Respiratory supercomplex factor 2 homolog C1565.01
- Probable mitochondrial-processing peptidase subunit beta
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome c oxidase subunit 6B-like protein new16
Sequence:
MSSKLPKKSEENLELPTFPASEESLSRSEKLKYVFVRNPFIPLGCLMTVGTFLASGYYIRRENHLMANKFMRYRVMSQGFTLAALAFSVLFIGPPRREAPSNSSGSINSEIKK
Protein: Voltage-gated potassium channel regulatory subunit KCNF1 (Potassium voltage-gated channel subfamily F member 1) (Voltage-gated potassium channel subunit Kv5.1) (Q7TSH7)
Organism: Mus musculus (Mouse)
Function: Putative voltage-gated potassium channel.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q14721}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Voltage-gated potassium channel subunit beta-3
- Voltage-gated potassium channel subunit beta-1
- Voltage-gated potassium channel subunit beta-2
Sequence:
MDASAEQSLPEPGSQDSVAGEDIEIVVNVGGVRQVLYGDLLSQYPETRLAELINCLAGGYDTIFSLCDDYDPGKREFYFDRDPDAFKCVIEVYYFGEVHMKKGICPICFKNEMDFWKVDLKFLDDCCKSHLSEKREELEEIARRVQLILDDLGVDAAEGRWRRCQKCVWKFLEKPESSCPARVVAVLSFLLILVSSVVMCMGTIPELQVVDSEGNRVEHPTLENVETACIGWFTLEYLLRLFSSPNKLHFALSFMNIVDVLAILPFYVSLTLTHLGARMMELTNVQQAVQALRIMRIARIFKLARHSSGLQTLTYALKRSFKELGLLLMYLAVGIFVFSALGYTMEQSHPETLFKSIPQSFWWAIITMTTVGYGDIYPKTTLGKLNAAISFLCGVIAIALPIHPIINNFVRYYNKQRVLETAAKHELELMELNSSSAEGKPGGSRSDLDTLPPEPAAREGPSWGSRLKLSHSDTFIPLLTEEKHHRTRLQSCK
Protein: Alkyldihydroxyacetonephosphate synthase, peroxisomal (Alkyl-DHAP synthase) (EC 2.5.1.26) (Alkylglycerone-phosphate synthase) (Q9EQR2)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the exchange of the acyl chain in acyl-dihydroxyacetonephosphate (acyl-DHAP) for a long chain fatty alcohol, yielding the first ether linked intermediate, i.e. alkyl-dihydroxyacetonephosphate (alkyl-DHAP), in the pathway of ether lipid biosynthesis.
Subcellular location: Peroxisome membrane {ECO:0000250|UniProtKB:P97275}. Peroxisome {ECO:0000269|PubMed:2340111}.
Interaction partners:
- Dihydroxyacetone phosphate acyltransferase
- Peroxisomal targeting signal 2 receptor
- Peroxisomal targeting signal 1 receptor
- Fatty acyl-CoA reductase 1
- Peroxisomal membrane protein PEX14
- Peroxisome biogenesis factor 10
- Peroxisome assembly protein 12
- Phytanoyl-CoA dioxygenase, peroxisomal
- Fatty acyl-CoA reductase
- Peroxisomal membrane protein PEX13
Sequence:
MAEAAGEAGASERDPDAVRARRRLRVLSGHLLGRPQEAPSTNECKARRAASAAGASPAASPAAPESGTIPKKRQELMKWNGWGYNDSKFLLNKKGQVELTGKRYPLSGLALPTLKDWIQNTLGVNLEHKTTSKPSINPSEAPPSIVNEDFLQELKEAHISYSQDADDRVFRAHGHCLHEIFLLREGMFERIPDIVVWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQDLERQLKESGYCTGHEPDSLEFSIVGGWISTRASGMKKNVYGNIEDLVVHMKMVTPRGVIEKSSQGPRMSTGPDIHHFIMGSEGTLGVITEATIKIRPTPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNQQFQFGHALKPQVSSIFTSFLDGFKKFYITKFKGFDPNQISVATLLFEGDREKVLQHEKQVYDIAAKFGGLAAGEDNGQRGYLLTYVIAYMRDLGLEYYVVGESFETSAPWDRVIDLCRNVKERIRRECKERGVQFAPLSTCRVTQTYDAGACIYFYFAFNYRGISDPLTVFEQTEAAARDEILANGGSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKDYVDPSNIFGNRNLL
Protein: Carbamoyl phosphate synthase pyrimidine-specific large chain (EC 6.3.4.16) (EC 6.3.5.5) (Carbamoyl phosphate synthetase ammonia chain) (P25994)
Organism: Bacillus subtilis (strain 168)
Interaction partners:
- Carbamoyl phosphate synthase arginine-specific small chain
- Dihydroorotate dehydrogenase B
- Dihydroorotase
- Orotate phosphoribosyltransferase
- Carbamoyl phosphate synthase pyrimidine-specific small chain
- Aspartate carbamoyltransferase catalytic subunit
- Dihydroorotate dehydrogenase B
- Orotidine 5'-phosphate decarboxylase
- Ornithine carbamoyltransferase
- Uracil permease
Sequence:
MPKRVDINKILVIGSGPIIIGQAAEFDYAGTQACLALKEEGYEVILVNSNPATIMTDTEMADRVYIEPLTPEFLTRIIRKERPDAILPTLGGQTGLNLAVELSERGVLAECGVEVLGTKLSAIQQAEDRDLFRTLMNELNEPVPESEIIHSLEEAEKFVSQIGFPVIVRPAYTLGGTGGGICSNETELKEIVENGLKLSPVHQCLLEKSIAGYKEIEYEVMRDSQDHAIVVCNMENIDPVGIHTGDSIVVAPSQTLSDREYQLLRNVSLKLIRALGIEGGCNVQLALDPDSFQYYIIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLSLDEMMNPVTGKTYAAFEPALDYVVSKIPRWPFDKFESANRKLGTQMKATGEVMAIGRTLEESLLKAVRSLEADVYHLELKDAADISDELLEKRIKKAGDERLFYLAEAYRRGYTVEDLHEFSAIDVFFLHKLFGIVQFEKELKANAGDTDVLRRAKELGFSDQYISREWKMKESELYSLRKQAGIAPVFKMVDTCAAEFESETPYFYSTYEEENESVVTDKKSVMVLGSGPIRIGQGVEFDYATVHSVWAIKQAGYEAIIVNNNPETVSTDFSISDKLYFEPLTIEDVMHIIDLEQPMGVVVQFGGQTAINLADELSARGVKILGTSLEDLDRAEDRDKFEQALGELGVPQPLGKTATSVNQAVSIASDIGYPVLVRPSYVLGGRAMEIVYHEEELLHYMKNAVKINPQHPVLIDRYLTGKEIEVDAVSDGETVVIPGIMEHIERAGVHSGDSIAVYPPQSLTEDIKKKIEQYTIALAKGLNIVGLLNIQFVLSQGEVYVLEVNPRSSRTVPFLSKITGIPMANLATKIILGQKLAAFGYTEGLQPEQQGVFVKAPVFSFAKLRRVDITLGPEMKSTGEVMGKDSTLEKALYKALIASGIQIPNYGSVLLTVADKDKEEGLAIAKRFHAIGYNILATEGTAGYLKEASIPAKVVGKIGQDGPNLLDVIRNGEAQFVINTLTKGKQPARDGFRIRRESVENGVACLTSLDTAEAILRVLESMTFRADQMPAVNTNQEAAVTI
Protein: BLOC-1-related complex subunit 8 (MEF2B neighbor) (Q96FH0)
Organism: Homo sapiens (Human)
Function: As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor.
Subcellular location: Lysosome membrane {ECO:0000305|PubMed:25898167}.
Interaction partners:
- BLOC-1-related complex subunit 6
- BLOC-1-related complex subunit 5
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- KxDL motif-containing protein 1
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- BLOC-1-related complex subunit 7
- SNARE-associated protein Snapin
Sequence:
MEEPEMQLKGKKVTDKFTESVYVLANEPSVALYRLQEHVRRSLPELAQHKADMQRWEEQSQGAIYTVEYACSAVKNLVDSSVYFRSVEGLLKQAISIRDHMNASAQGHSPEEPPPPSSA
Protein: Partitioning defective protein 3 (Abnormal embryonic partitioning of cytoplasm protein 3) (Q17353)
Organism: Caenorhabditis elegans
Function: In cooperation with pkc-3, required for establishing cell polarity and regulating spindle orientation in the early embryo. Localization is crucial for recruiting par-6 and pkc-3 to the peripheral apical cortex and restricting par-2 to basolateral surfaces. Necessary for apicobasal and anterior-posterior asymmetries associated with cell adhesion and gastrulation during the first few cycles of embryogenesis, and also for epithelial cell polarity in the distal spermatheca. Regulates the asymmetric localization of csnk-1, ppk-1 and gpr-1/2 during the first embryonic division.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8521491}. Note=Cytoplasmic and cell periphery.
Interaction partners:
- Protein kinase C-like 3
- Partitioning defective protein 6
- RING-type domain-containing protein
- Serine/threonine-protein kinase par-1
- LGL-1
- Cell division control protein 42 homolog
- 14-3-3-like protein 1
- Tetratricopeptide repeat protein 28
- Myosin-11
- Protein let-99
Sequence:
MSASSTSSSSTSCPEGGEPSGSCKSSDEGESTLKKRMQQYGIASGYANSSISTLDRSQYQSLPLNGTRRVTVQFGRMKIVVPWKESDQTVGQLADAALLRYKKARGMANEDRIHVHRLECASDGGILDMDDVLEEVFDLNYDQILAITDEANGGSTTPTYSQIQKQQHHYAQPLPYARKFDGGPSTPIASAFGSVTVNHQAHRAASPYNVGFARSNSRDFAPQPTHSKERRDSVVEVSSFDQIPQSGLRVSTPKPSRQSEDVIDGKPMNQPILRSSLRTEASGSRTEEATPVKQSRVTLSPEVEKKLAEQDERKSERRKHYDKNPGRFARGSDRKSRITDALLDARDRIADQLESQNPAEETKSQMIRVKIDQGPMPGTSLVTFPPIPEKSENEKQLGIEVNAVFDESSELPGTSEPTKLSSVQIMKIEDGGRIAKDGRIRVGDCIVAIDGKPVDQMSIIRVRASISDLAAVTSRPVTLIINRSLESFLEQESSAKPIQSALQQANTQYIGHTTVVELIKSSNGFGFTVTGRETAKGERLFYIGTVKPYGVALGHLKSGDRLLEINGTPTGQWTQSEIVEKLKETMVGEKIKFLVSRVSQSAIMSTSASSENKENEETLKVVEEEKIPQKLPLPALMTPPVPKDTPALSPSGASRFEIVIPFINGSSSAGLGVSLKARVSKKSNGSKVDCGIFIKNVMHGGAAFKEGGLRVDDRIVGVEDIDLEPLDNREAQAALAKKLKEVGMISSNVRLTISRYNECNPGQISRDLSRITVDASSPSPSSRMSSHTAPDSLLPSPATRGTSSSGADSSHSRQSSASSAVPAVPARLTERDSIVSDGTSRNDESELPDSADPFNREGLGRKSLSEKRGMGAAADPQHIKLFQDIKHQRQNSAPTSSTQKRSKSQPRSSSQRNYRSPMKLVDLPTTAAASASTNSQNLDDSDMLNRRSQSMESINRPVESILRGTGQIPTGSSSKVQFMQAASPDQHPFPPGAALLRLKNEESRSRDKSRRKSMGNPFSAMRNFFGFGSKSRDASPEKTPTESVQLRSVERPKSIIDERNNGSSERAPPPLPPHQSQRRGSGGNVFVDYGEPYGLIPQYPHNTTSGYESYADSELYDRYAAHRYHPRGGPIIDEDEYIYRQQSTSGNSPINTSSYVNYGLPASNAYHVGSRIPPQTSSGSISKTSGAMRRVYPAEYDEDVAYHQQIPQQSTRYQQGSGSGRGNADYHHMFNSWFAYTGGGAVGAAPVIKSSYGSSPVRIAAASAIERGESFVVEPVSGSSASATDRRGRSTSSGAVASGSSSTGFQYAAKEKYADARSGKFNGGSTRLFIPRHGGGLSAAAFATNFGGEAYETRGGGAGGSPSQYRRRDQGPPHRFPQY
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (Q5J1R9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MKVPKNTPLVVFLAFFSLTEGLQRAPRITTLLETVDSSLDHNATFICEVDSYPQADIIWTRNNYPIRYYDSRYVIQENGQMLIIPNVKDSDSGEYCCIANNGVGEAKSCGALQLKMKPQIKRHPTNMTLILESKAVLPCLSLGYPKPEISWIKEDDLIKANNRIAILESGSLKITNIKKEDAGQYRCVARNSFGIAFSRPVTIEVQAPAKILKVPKEKRVQIGSEVTLECNATGNPIPSITWLENGNTISGASVVETLVGEVILSVLQVVVHKPALYTCQATNRHSGGENTVKATAKITVSEWRLYKGHAGYCSTYRGDVCRNVLRRDALVFFNYSLPNPEDAQEYLAQSAWPELDGVSSFCRPAARSLLCHSTFQDCNPSGLGPAPKPVCREHCLTVKELYCYKEWRSAEERSQRGFQHITLPECTSLPSQQADPSSCTAVPYVDIKKDQVTSTCYNDKGRFYQGTHNVTASSIPCQRWNQQDPHQHRLSVDVIPELRNAENYCRNPGGESDRPWCYTTNPNVRWEYCLVPKCGEVISIRTAPSITKPAHFYPPPSVSTAYSMSVIIFVIAGFAGAAFFTVLILMCHRRKKMWKKRKSRVLETPTLTTLPSELLLDRLHPNPMYQRLPLLLNSKLLSLEYPRNNIEYVRDIGEGAFGRVFQARAPGLLPTEPFTMVAVKMLKEEASTDMQNDFQREAALMSEFDHPNIVRLLGVCAVGKPMCLMFEYMAYGDLNEFLRRRCATQQPSLSRDTLTSSSLVSEPERYPPLSCQEQLSISKQVAAGMAYLSERKFVHRDLATRNCLVAENLVVKIADFGLSRNIYAADYYKASENDAIPIRWMPPESIFYNRYTSESDVWAYGVVLWEIFSYGMQPYYGMAHEEVIYYVRDGNVLSCPENCPQELYNLMRLCWSGHPTDRPSFASIHRILERMHDQMLKSGLS
Protein: N-acetylneuraminate-9-phosphate synthase (EC 2.5.1.57) (3-deoxy-D-glycero-D-galacto-nononate 9-phosphate synthase) (EC 2.5.1.132) (Sialic acid synthase) (Q9VG74)
Organism: Drosophila melanogaster (Fruit fly)
Function: Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively. Essential for biosynthesis of sialic acids in neurons of the central nervous system.
Interaction partners:
- CMP-sialic acid synthase
- LD15807p)
- beta-galactoside alpha-
Sequence:
MLLNDIISGKLVDSVYIIAEIGQNHQGCVETAKKMIWEAKKAGCHCVKFQKSDLPAKFTRSALDREYISDHAWGKTYGEHKEYLEFSKDQYLQLQAHCKELNVDFTASAMDERSLEFLSALNVPFIKIGSGDANNFPLLKKAANLNLPLVISTGMQTMQTVERIVQTMRESGKEDYALMHCVSSYPTDPKDCSLQLISVLRTRFPNVAIGYSGHELGVIISQAAVLLGARIVERHFTLDKSQKGSDHRCSLEPQELKALTTAITNFKLSSVPMPPQEIVKKLNGDEELEAALQHVESKTILPCELPCRNKLGKSIVAARNLNKGYRLQLADMAIKVSEPSGLTAEDFLDLVGKELADNIGEDEPILGNSIIN
Protein: FI03803p (Myosuppressin receptor 2, isoform A) (Myosuppressin receptor 2, isoform B) (Q9W027)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MVTNMSQPHYCGTGIDDFHTNYKYFHGYFSLIVCILGTIANTLNIIVLTRREMRSPTNAILTGLAVADLAVMLEYIPYTVHDYILSVRLPREEQLSYSWACFIKFHSVFPQVLHTISIWLTVTLAVWRYIAVSYPQRNRIWCGMRTTLITIATAYVVCVLVVSPWLYLVTAIAKFLETLDANGKTIASVPLSQYILDYNRQDEVTMQVMSSTTPDVSWAIPSDSANGTAVSLLSLTTVIPLTTLSTGVTTSSSLGERNVTVYKLYHSALALRDRQFRNATFLIYSVLIKLIPCFALTILSVRLIGALLEAKRRRKILACHAANDMQPIVNGKVVIPTQPKSCKLLEKEKQTDRTTRMLLAVLLLFLVTEFPQGIMGLLNVLLGDAFFLQCYLKLSDLMDILALINSSINFILYCSMSRQFRSTFALLFRPRWLDKWLPLSQHDGEGRVGGSGGLGGYGGYGRQRLLHTDAVSKSMAIDLGLTTQVTNV
Protein: Nuclear egress protein 2 (Q6SW81)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network.
Subcellular location: Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:29743376}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04024}. Note=Also localizes at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
Interaction partners:
Sequence:
MEMNKVLHQDLVQATRRILKLGPSELRVTDAGLICKNPNYSVCDAMLKTDTVYCVEYLLSYWESRTDHVPCFIFKNTGCAVSLCCFVRAPVKLVSPARHVGEFNVLKVNESLIVTLKDIEEIKPSAYGVLTKCVVRKSNSASVFNIELIAFGPENEGEYENLLRELYAKKAASTSLAVRNHVTVSSHSGSGPSLWRARMSAALTRTAGKRSPRTASPPPPPPRHPSCSPTMVAAGGAAAGPRPPPPPMAAGSWRLCRCEACMGRCGCASEGDADEEEEELLALAGEGKAAAAAAGQDIGGSARRPLEEHVSRRRGVSTHHRHPPSPPCTPSLERTGYRWAPSSWWRARSGPSRPQSGPWLPARFATLGPLVLALLLVLALLWRGHGQSSSPTRSAHRD
Protein: Transforming growth factor beta-2 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)] (P30371)
Organism: Gallus gallus (Chicken)
Function: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively.
Subcellular location: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-2]: Secreted {ECO:0000250|UniProtKB:P01137}.
Interaction partners:
- TGF-beta receptor type-2
- TGF-beta receptor type-1
- Receptor protein serine/threonine kinase
- Uncharacterized protein.
- Decorin
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta-3 proprotein
- Fibromodulin
- TGF-beta family profile domain-containing protein
- Inhibin beta B chain
Sequence:
MHCYLLSVFLTLDLAAVALSLSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPDEYPEPEEVPPEVISIYNSTRDLLQEKANHRAATCERERSDEEYYAKEVYKIDMQPFYPENAIPPSYYSLYFRIVRFDVSAMEKNASNLVKAEFRVFRLQNSKARVSEQRIELYQVLKSKELSSPGQRYIDSKVVKTRAEGEWLSFDVTEAVHEWLHHRDRNLGFKISLHCPCCTFVPSNNYIIPNKSEEPEARFAGIDDYTYSSGDVKALKSNRKKYSGKTPHLLLMLLPSYRLESQQPSRRKKRALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYHANFCAGACPYLWSSDTQHSRVLSLYNTINPEASASPCCVSQDLEPLTILYYIGKTPKIEQLSNMIVKSCKCS
Protein: Collagen type XI alpha 2 chain (A0A8I6A830)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGREAQSPQQGSTITPMAMGMIIVRRPSLALPSLRRQITQEPPHWGLHVCLPQVAHGPRGLKGEKGEPAVLEPGMFVEGPPGPEGPAGLAGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGPPGPPGTSLMLPFRFGSSGGDKGPVVAAQEAQAQAILQQARLALRGPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQVTTPTSSVQPSVPPLCPGRAGADGARGMPGEPGVKGDRGFDGLPGLPGEKGQRGDRPLEGKLGPQSKSRRGDDGEIGPRGLPGESGPRGLLGPKGPPGIPGPPPCLGLVWPSLAACF
Protein: Small ribosomal subunit protein uS13B (40S ribosomal protein S18-B) (P0CT67)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein eS24B
- Small ribosomal subunit protein eS10B
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS9A
- Small ribosomal subunit protein eS28A
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS7
Sequence:
MSLVVPDNFQHILRLLNTNVDGKVKVMFAMTQIKGVGRRYANIVCKKADIDMSKRAGELTTEELERIVTIIQNPSQFKIPSWFLNRQKDINDGKSFQLLANNVDSKLREDLERLKKIQTHRGLRHALDLRVRGQHTKTTGRRGKTVGVSKKK
Protein: Polyglutamine-binding protein 1 (PQBP-1) (Polyglutamine tract-binding protein 1) (Q6PCT5)
Organism: Rattus norvegicus (Rat)
Function: Intrinsically disordered protein that acts as a scaffold, and which is involved in different processes, such as pre-mRNA splicing, transcription regulation, innate immunity and neuron development. Interacts with splicing-related factors via the intrinsically disordered region and regulates alternative splicing of target pre-mRNA species. May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery. May be involved in ATXN1 mutant-induced cell death. The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit. Involved in the assembly of cytoplasmic stress granule, possibly by participating in the transport of neuronal RNA granules. Also acts as an innate immune sensor of infection by retroviruses, by detecting the presence of reverse-transcribed DNA in the cytosol. Directly binds retroviral reverse-transcribed DNA in the cytosol and interacts with CGAS, leading to activate the cGAS-STING signaling pathway, triggering type-I interferon production.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O60828}. Nucleus speckle {ECO:0000250|UniProtKB:Q91VJ5}. Cytoplasmic granule {ECO:0000250|UniProtKB:O60828}. Note=Colocalizes with SRSF2 in nuclear speckles (By similarity). Colocalized with POU3F2. Colocalized with ATXN1 in nuclear inclusion bodies. Localizes to cytoplasmic stress granules (By similarity). {ECO:0000250|UniProtKB:O60828, ECO:0000250|UniProtKB:Q91VJ5}.
Interaction partners:
- WW domain-binding protein 11
- Thioredoxin-like protein
- Beta-catenin-like protein 1
- Thioredoxin-like protein
- Pre-mRNA-splicing factor SPF27
- Spliceosome-associated protein CWC15 homolog
- Cell division cycle 5-like protein
- Pleiotropic regulator 1
- Heat shock cognate 71 kDa protein
- Pre-mRNA-processing factor 19
Sequence:
MPLPVALQTRLAKRGILKHLEPEPEEEIIAEDYDDDPVDYEATRIEGLPPSWYKVFDPSCGLPYYWNVETDLVSWLSPHDPNFVVSKSAKKLRNSNADAEDKSERNLEKVDRNHEKSDRSHEKPDRSHEKADRNHEKSDRERERNYDKVDRERDRDRERERAFDKADREDGKDRRHHRREELAPYPKNKKATSRKDEELDPMDPSSYSDAPRGTWSTGLPKRNEAKTGADTTAAGPLFQQRPYPSPGAVLRANAEASRSKQQD
Protein: Glutathione peroxidase 3 (GPx-3) (GSHPx-3) (EC 1.11.1.9) (Plasma glutathione peroxidase) (GPx-P) (GSHPx-P) (P46412)
Organism: Mus musculus (Mouse)
Function: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.
Subcellular location: Secreted.
Interaction partners:
- Glutathione reductase, mitochondrial
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Glutathione synthetase
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Polyunsaturated fatty acid 5-lipoxygenase
- Polyunsaturated fatty acid lipoxygenase ALOX8
- Glutathione-specific gamma-glutamylcyclotransferase 1
- Putative glutathione-specific gamma-glutamylcyclotransferase 2
- Thioredoxin
- Hematopoietic prostaglandin D synthase
Sequence:
MARILRASCLLSLLLAGFVPPGRGQEKSKTDCHGGMSGTIYEYGALTIDGEEYIPFKQYAGKYILFVNVASYUGLTDQYLELNALQEELGPFGLVILGFPSNQFGKQEPGENSEILPSLKYVRPGGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPPTAELLGSPGRLFWEPMKIHDIRWNFEKFLVGPDGIPVMRWYHRTTVSNVKMDILSYMRRQAALSARGK
Protein: Nucleolar protein 8 (Nucleolar protein Nop132) (Q76FK4)
Organism: Homo sapiens (Human)
Function: Plays an essential role in the survival of diffuse-type gastric cancer cells. Acts as a nucleolar anchoring protein for DDX47. May be involved in regulation of gene expression at the post-transcriptional level or in ribosome biogenesis in cancer cells.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15132771, ECO:0000269|PubMed:16963496}. Note=Localizes in the nucleolar-organizing region during ribosome biogenesis.
Interaction partners:
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Ras-related GTP-binding protein C
- Ras-related GTP-binding protein D
- U3 small nucleolar ribonucleoprotein protein MPP10
- Probable ATP-dependent RNA helicase DDX10
- Nucleolar pre-ribosomal-associated protein 1
- Protein SDA1 homolog
- Ras-related GTP-binding protein A
- ATP-dependent RNA helicase DDX51
- Unhealthy ribosome biogenesis protein 2 homolog
Sequence:
MKVNRETKRLYVGGLSQDISEADLQNQFSRFGEVSDVEIITRKDDQGNPQKVFAYINISVAEADLKKCMSVLNKTKWKGGTLQIQLAKESFLHRLAQEREAAKAKKEESTTGNANLLEKTGGVDFHMKAVPGTEVPGHKNWVVSKFGRVLPVLHLKNQHKRKIIKYDPSKYCHNLKKIGEDFSNTIPISSLTWELEGGNDPMSKKRRGEFSDFHGPPKKIIKVQKDESSTGSLAMSTRPRRVIERPPLTQQQAAQKRTCDSITPSKSSPVPVSDTQKLKNLPFKTSGLETAKKRNSISDDDTDSEDELRMMIAKEENLQRTTQPSINESESDPFEVVRDDFKSGVHKLHSLIGLGIKNRVSCHDSDDDIMRNDREYDSGDTDEIIAMKKNVAKVKNSTEFSQMEKSTKKTSFKNRENCELSDHCIKLQKRKSNVESALSHGLKSLNRKSPSHSSSSEDADSASELADSEGGEEYNAMMKNCLRVNLTLADLEQLAGSDLKVPNEDTKSDGPETTTQCKFDRGSKSPKTPTGLRRGRQCIRPAEIVASLLEGEENTCGKQKPKENNLKPKFQAFKGVGCLYEKESMKKSLKDSVASNNKDQNSMKHEDPSIISMEDGSPYVNGSLGEVTPCQHAKKANGPNYIQPQKRQTTFESQDRKAVSPSSSEKRSKNPISRPLEGKKSLSLSAKTHNIGFDKDSCHSTTKTEASQEERSDSSGLTSLKKSPKVSSKDTREIKTDFSLSISNSSDVSAKDKHAEDNEKRLAALEARQKAKEVQKKLVHNALANLDGHPEDKPTHIIFGSDSECETEETSTQEQSHPGEEWVKESMGKTSGKLFDSSDDDESDSEDDSNRFKIKPQFEGRAGQKLMDLQSHFGTDDRFRMDSRFLETDSEEEQEEVNEKKTAEEEELAEEKKKALNVVQSVLQINLSNSTNRGSVAAKKFKDIIHYDPTKQDHATYERKRDDKPKESKAKRKKKREEAEKLPEVSKEMYYNIAMDLKEIFQTTKYTSEKEEGTPWNEDCGKEKPEEIQDPAALTSDAEQPSGFTFSFFDSDTKDIKEETYRVETVKPGKIVWQEDPRLQDSSSEEEDVTEETDHRNSSPGEASLLEKETTRFFFFSKNDERLQGSDLFWRGVGSNMSRNSWEARTTNLRMDCRKKHKDAKRKMKPK
Protein: PAP-associated domain-containing protein (Q09408)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein lin-28
- Argonaute protein wago-4
- Poly
Sequence:
MTVIQKSSPTVKGVKTTTSDCTERRHSSSSPCKMSQNGSSGYYEGDVLLDDDALVSMPEATLIECFGNLAVTKRPAHLRPPAAFCLPFVSMNNDLTSGHALKHITLTSVFDALHPYVAMPYINRMDICSAMNVYWIRNCLEAEQSDLFHRFALEMQVHLSACFGCRVVLDIYGSTRNGFGTRFCDVDMSLSFSPSPPSWATNSDRVMRAVAKALVDFPKAVDERYVNAKVPIVRFRSSDMDMEADISYKNDLALHNTQLLQQYCKWDPERLPTLGVWVKAWAKRSGVGDASKGSLSSYAWIVMLIHYLQQVEPIPVLPCLQEMNHQKSENVYVQGYNTYYWKFVDTARTRRCRASVVDLFVGFLDYYATYFDYSTNVIQMVSKKLEFKPDRWCKYPMCIADPFETDHNLAQGVDMPMFEYIRSCMEHSKKVFTDRRMRSEFLSGYGFDVDEFDARHRGEMNMEMASQFGEFLLHKCIMVKQAPNRQFRDRSMSQSTSISNTSSISSSG