wanglab/gogpt-training-data huggingface dataset:
Protein: Chitin synthase regulatory factor 3 (Chs four homolog 1) (Q09897)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MKDSHSSRRKYEKEKLVFATNNGKRTEGTPAFLKSGNTASSSSPTLQFRPTSRYPTLSHEPVYTNVLDLSSRIDANRASIMSATMGTPPSALKFSKKKISRPVVSEDTFKDKLPRATIPVKPEPQPQYKIPAAPAPTSKRVVNRGLKLNTNLRQASPILPSPSLKLDRQDAPIQINHEQKEDFLVSIPRPTPMTNLDDGKDEIGQPDPHRKYMAPPRVNSISRVQRRMSYIPYGGFDDFLDNYYKDDDTVLEDNQLKSNSRIETLEEEDGAESDSITNTVSNASSDAEPAHRHLGPVYENSGHLPSKSHFSSTDSNTDSFGLESDERSLPSVSNDLKSSETLKNPRNDDLLTLQQPPRYPHSQMVMLPARSPVEVPAPTFDRRNVSRNSNNNSPEGYDNNRTNPTVNNLPSYPTNLARPKAIKPMPTSIHGQTSPLSPIPPVHTTHGLVSDIRPLPSVSSPIMRADSTPISHNLAVTPSFSPIPQQSNKSIGNHKNTSVANVSSKVANSKFERNISMMSNSNASSPAIFEVGAEAKEKTKDAIPCHPDDKLMIPSPKIVTHGDAMQEEQRLRQKSQITPDDEVELAKVYLNALETLENKPSLAPDQASYNTRINVYRTRAVELLKKNAYPSKTQNTVPEALFLIGQFHSQGVLGFRRDLGKAFELYSLAAKKGHPLSNYRVAVCLQTGTGVKPDTSKCVAIYKKAAEMDVVEAMFRIALIYLNGLLGQKRNISLGVQWLERACKSKGPESVRAMYELAKIYEQPDRYGVSATPERKFELYKQSAVYGYAAAQCKLGECYEHGLLGCLAEPRRSIFWYTRAAEQDYGEAELGLSGWYLTGSEGILPKNGEEALLWAHKAACKGLAKAQYAVGFMMEQGIGVAADPSSAHNWYIRAAKQGFPKAKKRLEEQALSSKQTHSKAPKKKQQEQCVVM
Protein: V-type proton ATPase proteolipid subunit (V-ATPase 16 kDa proteolipid subunit) (Vacuolar proton pump 16 kDa proteolipid subunit) (P54642)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subcellular location: Vacuole membrane; Multi-pass membrane protein.
Interaction partners:
- V-type proton ATPase subunit E
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d
- V-ATPase proteolipid subunit C-like domain-containing protein
- V-type proton ATPase subunit B
- V-type proton ATPase subunit D
- Vacuolar proton translocating ATPase 100 kDa subunit
- V-type proton ATPase subunit C
- V-type proton ATPase subunit F
- V-type proton ATPase subunit G
Sequence:
MFQLLSFLLSGEATAVERIITDACPVYAPFFGAMGVTAALVFTVMGAAYGTAKASVGISNMGVMKPDLVIKAFIPVIFAGVIAIYGLIICVILVGGIKPNANYTLMKSFTDLGAGLTVGLCGLAAGMAIGIVGDSGVRAFGQQPKLYVIMMLILIFSEALGLYGLIIGILLSSVSDTYCPGQALVPLNSGNVIGKN
Protein: Activin receptor type-2B (EC 2.7.11.30) (Activin receptor type IIB) (ACTR-IIB) (P38445)
Organism: Rattus norvegicus (Rat)
Function: Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q13705}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Growth/differentiation factor 8
- Activin receptor type-1B
- Growth/differentiation factor 11
- Bone morphogenetic protein 7
- TGF-beta receptor type-1
- Inhibin beta A chain
- Bone morphogenetic protein 2
- Activin receptor type-2A
- Bone morphogenetic protein 4
- Bone morphogenetic protein 6
Sequence:
MTAPWAALALLWGSLCAGSGRGEAETRECIYYNANWELERTNQSGLERCEGEQDKRLHCYASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEPGGPEVTYEPPPTAPTLLTVLAYSLLPIGGLSLIVLLAFWMYRHRKPPYGHVDIHEDPGPPPPSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGCSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCRGEGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEELQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERVSLIRRSVNSSTSDCLVSLVTSVTNVDLLPKESSI
Protein: Protein STRICTOSIDINE SYNTHASE-LIKE 13 (AtSSL13) (Protein LESS ADHERENT POLLEN 3) (Strictosidine synthase 11) (AtSS11) (Q9M1B4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the exine formation during pollen development.
Subcellular location: Vacuole {ECO:0000250}.
Interaction partners:
- Probable beta-1,3-galactosyltransferase 8
- Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial
- Probable glucan endo-1,3-beta-glucosidase A6
- Probable alkaline/neutral invertase B
Sequence:
MEKKGQHGTYESMMTHHPILCIIALSVLFIAIDPFHMSPIGGREFKPVKHEVAPYKEVMGSWPRDNLSRLGNHGKLEFVDQVFGPESLEFDSLGRGPYTGLADGRVVRWMGEAIGWETFSVVTSKWSEEACVRGVDSTTNKQWKHEKLCGRPLGLRFHKETGNLYIADAYYGLLVVGPEGGIATPLATHVEGKPILFANDLDIHRNGSIFFTDTSKRYDRANHFFILLEGESTGRLLRYDPPTKTTHIVLEGLAFPNGIQLSKDQSFLLFTETTNCRLVKYWLEGPKMGEVEVVADLPGFPDNVRINEEGQFWVAIDCCRTPAQEVLTNNPWIRSIYFRLPIPMKLLAKTMGMRMYTVISRFDEEGKVLEVLEDRQGKVMKLWIGTVAHNHIATLPYPLTMNQ
Protein: Possible acyltransferase (O07807)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible acyltransferase
- Conserved protein
- Possible acyltransferase
- Possible phosphotransferase
Sequence:
MEPVYGTVIRLARLSWRIQGLKITVTGVDNLPTSGGAVVAINHTSYLDFTFAGLPAYQQGLGRKVRFMAKQEVFDHKITGPIMRSLRHIPVDRQDGSASYDAAVRMLKAGELVGVYPEATISRSFEIKEFKTGAARMAIEAGVPIVPHIVWGAQRIWTKDRPKKLFRPKVPVTIVVGERIEPTLPTAELNGLLHSRMQHLLERAQELYGPHPAGEFWVPHRLGGGAPSLAEAARLDAQEAAVRAARRAQRAHPAGAPEQ
Protein: Moesin/ezrin/radixin homolog 1 (G5EBK3)
Organism: Caenorhabditis elegans
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cell projection, microvillus {ECO:0000256|ARBA:ARBA00004105}. Cell projection, rhabdomere {ECO:0000256|ARBA:ARBA00043944}.
Interaction partners:
- Intermediate filament protein ifb-2
- Na
- Protein Scribble homolog let-413
- Disks large homolog 1
- Actin
- Apical junction molecule ajm-1
- Protein kinase C-like 1
- Protein kinase C-like 3
- Netrin receptor unc-40
- Neuroglian
Sequence:
MVAAGDINVRVTSMDSELEFAIQSSTTGKQLFDQVVKTIGLREIWYFGLQYTDNKGFPTWLKLNKKVLSQDVKKDPTLVFKFRAKFYPEDVAEEIIQDVTMRLFYLQVKDGILSDEIYCPPETSVLLASYAMQAKYGDYVPETHVAGCLTADRLLPQRVLGQFKLNSEEWERRIMTWWADHRATTREQAMLEYLKIAQDLEMYGVNYFEIRNKKGTDLYLGVDALGLNIYDKADRLSPKVGFPWSEIRNISFNDKKFVIKPIDKKAHDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKQQAREDRALKIAEQEKLTREMSAREEAEQRQRDAEKRMAQMQEDMERARLELAEAHNTIHSLEAQLKQLQLAKQALEQKEYELRELTAQLQSEKAMSDGERRHLRDQVDAREREVFSMREEVERQTTVTRQLQTQIHSQQHTQHYSNSHHVSNGHAHDETATDDEDNGATELTNDADQNVPQHELERVTAAEKNIQIKNKLDMLTRELDSVKDQNAVTDYDVLHMENKKAGRDKYKTLRQIRGGNTKRRIDQYENM
Protein: Kelch-like protein 41 (Kelch repeat and BTB domain-containing protein 10) (A2AUC9)
Organism: Mus musculus (Mouse)
Function: Involved in skeletal muscle development and differentiation. Regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. Required for pseudopod elongation in transformed cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18178185, ECO:0000269|PubMed:22562206}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18178185}. Cell projection, pseudopodium {ECO:0000250|UniProtKB:Q9ER30}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9ER30}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:22562206}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:24268659}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24268659}. Note=Predominantly cytoplasmic but can colocalize with F-actin at the membrane ruffle-like structures at the tips of transformation-specific pseudopodia.
Interaction partners:
- Cullin-3
- Kelch-like protein 40
- Nebulin
- Leiomodin-3
- E3 ubiquitin-protein ligase RBX1
- Kelch-like protein 13
- Nebulin-related-anchoring protein
- Protein PTHB1
- Kelch-like protein 9
- Kelch-like protein 42
Sequence:
MDSQRELAEELRLYQSTLLQDGLKDLLEEKKFIDCTLKAGDKSFPCHRLILSACSPYFREYFLSEIEEEKKKEVALDNVDPAILDLIIKYLYSASIDLNDGNVQDIFALSSRFQIPSVFTVCVSYLQKRLAPGNCLAILRLGLLLDCPRLAISAREFVSDRFVQICKEEDFMQLSPQELISVISNDSLNVEKEEVVFEAVMKWVRTDKENRAKNLSEVFDCIRFRLMAEKYFKDHVEKDDIIKSNPEVQKKIKVLKDAFAGKLPEPSKNAEKAGAGEVNGDVGDEDLLPGYLNDIPRHGMFVKDLILLVNDTAAVAYDPMENECYLTALAEQIPRNHSSLVTQQNQVYVVGGLYVDEENKDQPLQSYFFQLDNVTSEWVGLPPLPSARCLFGLGEVDDKIYVVAGKDLQTEASLDSVLCYDPVAAKWSEVKNLPIKVYGHNVISHNGMIYCLGGKTDDKKCTNRVFIYNPKKGDWKDLAPMKTPRSMFGVAIHKGKIVIAGGVTEDGLSASVEAFDLKTNKWEVMTEFPQERSSISLVSLAGALYAIGGFAMIQLESKEFAPTEVNDIWKYEDDKKEWAGMLKEIRYASGASCLATRLNLFKLSKL
Protein: Uncharacterized protein (Q5AGX2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Fgr39p
- Uncharacterized protein
Sequence:
MNIGRRIRPRKLHLRLYSQVKVPWSLETPITPKTVTDILPHFVQLPIEEQDTLIEKHPKLLNVQLQIMLYSESDSLKTFKFICKYGQHLQSEFIQIFIYNLLLSNNLKATTTLLHQLLHENKEFQMSNELWALYMDKVCYMGDYLGATMIYHELVDNVKFYEETSYLVQTNNLMPFLINESTLVALAYIFRNNKDASRVGGIIQYFRRFYSFLRSQYIYKSLLILQIESYAELGDLEQCLKLFTAFGFNHNQSDVKRNRNVQAGWENIHKRHEAIQTNENPLLYKDSKYDLDIHQNLLAEICNTELFNPIIHRNVYSSSKTGHNPVINGSISVNDLPALETLITEKVATMEMRELLHLTKMSHQSINLFIVAGLCNVNKPHMALQYLKTLSHIFPTISRKNLIKNQNFIRILHATQDVELAKEVMNYYRDIHNDYINVQVLQA
Protein: Usher CupA3 (Q9I1Y5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|RuleBase:RU003884}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|RuleBase:RU003884}.
Interaction partners:
- Chaperone CupA5
- Chaperone CupA2
- Fimbrial subunit CupA1
- Chaperone CupB2
- Fimbrial subunit CupA4
- Chaperone CupC2
- Chaperone CupB4
- Probable pili assembly chaperone
- Transport permease protein
- Probable pili assembly chaperone
Sequence:
MTYRHERRCRTGTALMAGGMALAASAFGHAQPGYEFDDRLLLGSSLGGGDLSRFNQDGRIDPGRYHVDVYLNERFASRSEVSFRANPASGAVEPCLDEDFLRQRLGAKPGDDPRKSGDGRHCAFLGARLPGSRFSLDVARLRLDLSVPQALLDLKPRGYVSPEEWDAGDSMGFVNYDTNLYRSEYRGGESGRSDYAYVGLNSGINLGLWRLRHQSNYTYSRYNGQARRKWNSIRTYAQRALPAWRSELTAGESYTAGNLLGSIGYRGLSLATDDRMLPESLRRYAPQVRGTAATAARVVISQNGRKIREVNVAPGPFVIDDLYDSAYAGDLDVQVFEADGSVSSFSVPFASVPESMRPGLSRYSFTLGQARQYGDGDDLFADFTYQRGMSNALTANLGLRVADDYLAMLGGGVLATRFGAFGLNSTYSSARVEDGARKQGWRIGLDYSRTFQPTGTTLTLAGYRYSTEGYRELGDVLGSRDALRHGDTWDSGSYKQRNQFNLLVSQALGGYGNLYLSGSSSDFYDGKSRDTQLQFGYSNTWGQLSYNLAWSRQTTTYYQEQGDQDPGVELLRRDRRSGQRNDTLTLSVSMPLGSSSRAPTLSAMATRRSGDSRGGSLQTGLNGTLGDERTWSYALSANRDSEVADTTWNGTLQKQAALATVNAGYAQGDRYRQYSGGIRGALVAHRDGLTLGPSVGDTFALVEAKGASGAAIRGGQGARIDGNGYALAPSLSPYRYNPISLDPVGIDPDAELLETERKVAPYAGASVRVTFRTLTGHPLLIQARREDGSVLPLGAVVVDDGGAAIGMVGQGGQVYARAENQRGRLLVQWGTARKERCELPYDLAGVSRDQALIRLRGTCRAATTDSNLENAR
Protein: Cytochrome c oxidase subunit 6B1 (Cytochrome c oxidase subunit VIb isoform 1) (COX VIb-1) (P14854)
Organism: Homo sapiens (Human)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Peripheral membrane protein {ECO:0000269|PubMed:30030519}; Intermembrane side {ECO:0000269|PubMed:30030519}.
Interaction partners:
- Cytochrome c oxidase subunit NDUFA4
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 6A2, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 6C
- Cytochrome c oxidase subunit 2
Sequence:
MAEDMETKIKNYKTAPFDSRFPNQNQTRNCWQNYLDFHRCQKAMTAKGGDISVCEWYQRVYQSLCPTSWVTDWDEQRAEGTFPGKI
Protein: Aspartate carbamoyltransferase regulatory chain (P0A7F3)
Organism: Escherichia coli (strain K12)
Function: Involved in allosteric regulation of aspartate carbamoyltransferase.
Interaction partners:
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase large chain
- Carbamoyl phosphate synthase small chain
- Dihydroorotase
- 2-iminobutanoate/2-iminopropanoate deaminase
- Adenylosuccinate synthetase
- Argininosuccinate synthase
- Cytosine permease
- Aspartate--ammonia ligase
- Aspartate aminotransferase
Sequence:
MTHDNKLQVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQRITIGLNLPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQATVNRIDNYEVVGKSRPSLPERIDNVLVCPNSNCISHAEPVSSSFAVRKRANDIALKCKYCEKEFSHNVVLAN
Protein: DNA replication licensing factor MCM6 (EC 3.6.4.12) (p105MCM) (Q14566)
Organism: Homo sapiens (Human)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:16899510}. Chromosome {ECO:0000269|PubMed:16899510}. Note=Binds to chromatin during G1 and detaches from it during S phase. {ECO:0000269|PubMed:16899510}.
Interaction partners:
- DNA replication complex GINS protein SLD5
- Protein MCM10 homolog
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- Cell division cycle 7-related protein kinase
- DNA replication licensing factor MCM7
- Cell division control protein 6 homolog
- DNA replication licensing factor MCM3
- DNA replication complex GINS protein PSF3
- Cell division control protein 45 homolog
Sequence:
MDLAAAAEPGAGSQHLEVRDEVAEKCQKLFLDFLEEFQSSDGEIKYLQLAEELIRPERNTLVVSFVDLEQFNQQLSTTIQEEFYRVYPYLCRALKTFVKDRKEIPLAKDFYVAFQDLPTRHKIRELTSSRIGLLTRISGQVVRTHPVHPELVSGTFLCLDCQTVIRDVEQQFKYTQPNICRNPVCANRRRFLLDTNKSRFVDFQKVRIQETQAELPRGSIPRSLEVILRAEAVESAQAGDKCDFTGTLIVVPDVSKLSTPGARAETNSRVSGVDGYETEGIRGLRALGVRDLSYRLVFLACCVAPTNPRFGGKELRDEEQTAESIKNQMTVKEWEKVFEMSQDKNLYHNLCTSLFPTIHGNDEVKRGVLLMLFGGVPKTTGEGTSLRGDINVCIVGDPSTAKSQFLKHVEEFSPRAVYTSGKASSAAGLTAAVVRDEESHEFVIEAGALMLADNGVCCIDEFDKMDVRDQVAIHEAMEQQTISITKAGVKATLNARTSILAAANPISGHYDRSKSLKQNINLSAPIMSRFDLFFILVDECNEVTDYAIARRIVDLHSRIEESIDRVYSLDDIRRYLLFARQFKPKISKESEDFIVEQYKHLRQRDGSGVTKSSWRITVRQLESMIRLSEAMARMHCCDEVQPKHVKEAFRLLNKSIIRVETPDVNLDQEEEIQMEVDEGAGGINGHADSPAPVNGINGYNEDINQESAPKASLRLGFSEYCRISNLIVLHLRKVEEEEDESALKRSELVNWYLKEIESEIDSEEELINKKRIIEKVIHRLTHYDHVLIELTQAGLKGSTEGSESYEEDPYLVVNPNYLLED
Protein: Sphingomyelin phosphodiesterase 2 (EC 3.1.4.12) (Acid sphingomyelinase 2) (ASM-2) (Q23498)
Organism: Caenorhabditis elegans
Function: Sphingomyelin phosphodiesterase (sphingomyelinase) that converts sphingomyelin (N-acyl-sphingoid-1-phosphocholine) to ceramide (N-acyl-sphingoid base) and phosphocholine at acidic pH. Displays its enzymatic activity when secreted. May play distinct roles in signaling.
Subcellular location: Secreted {ECO:0000269|PubMed:9603947}. Note=Only the secreted form is enzymatically active. {ECO:0000269|PubMed:9603947}.
Interaction partners:
- Acid ceramidase
- Ceramide glucosyltransferase 1
- Ceramide glucosyltransferase 2
- Ceramide synthase hyl-2
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Probable acid ceramidase
- Putative neutral sphingomyelinase
- Putative sphingomyelin phosphodiesterase asm-3
- Putative phosphatidylcholine:ceramide cholinephosphotransferase 3
- Phosphatidylcholine:ceramide cholinephosphotransferase 2
Sequence:
MQQPLIILGIGIVLALVSNVESGVLRKPVDEHEYEKWTNARGNEAAVPPPKYKMLRYAKKAINEPENRKMSCLFCTFAVDGVQALIAQNSTDNEIAAFLVNLCDLFDVEQPHVCKNIIYAFKDEVVFVLERSVFTPEEICGAFIANCGHSDKPLTHMWNITIPGGKPPIKPWPKIPDNKPTFKVLHLSDIHIDHQYVVGTEAYCQLDSALGTYAMCCRDYSQDSQGAPTNLKDKPIYVPAGPWGMPYLCDLPYQTFESAMKHISKTFKDLDYIIITGDFEAHDSWDYTEDLTRENMNNMTNVFLEYFPGVPVYVSIGNHEGVPQDAMAPHTMPEYDTRGPQWLYKIMSEMWSHWIPQEALDTVQYRASYAVYPKPGLKLISLNTIYCSEFNFYLYVNEVDPDATLEWLIEELQDSENKGELVHIISHIPPGDNYCLKGWSWNFFEIVKRYENTIAQMFYGHTHYDQFMVYYDMDDPNRRPFHFNWISPSLTTYDWLNPAYRIYEIDGGYEGATYTVKDAKTYFANVTEANMKNKEPEWVLSYDTREHYQMADFSPQSWSDLSDKLWTNTTLFRDYVRLYYRNHYNNECYTDYKCRYTFVCDIKKGRSYDESFCDHLTK
Protein: Aquaporin (G5EEK0)
Organism: Caenorhabditis elegans
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- Aquaporin-3
- Aquaporin
- Putative aquaporin-10
- Aquaporin-9
- Aquaporin-9
- Aquaporin
- F-box domain-containing protein
- Probable delta-1-pyrroline-5-carboxylate synthase
Sequence:
MVSPYEEDSRPPYMSSYAEETWGQPATTNRKSSYTSRKKEYSLLTKCVAEFLGDLTFVYVGTMQASLFQYADGILHAAFAHGFTIFILVTAFGHISGGHFNPAVSWAIAGAGKMPIFHLPFYVVSQLLGGICGAFLTAAVLSQEQLTSCEAGATLLSPGSQWWQGLIAETVVTFFLVHTILITAADTDTVTLAPLAIGLTLSIDILSTGSITGASMNPARSLGPSIIGSIFATQKTSFYWNNHYIYWAGPLLGSTIALCIYKLFESREERIVR
Protein: At4g01560 (Ribosomal RNA processing Brix domain protein) (Q9M125)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT5g04600/T32M21_200
- 60S ribosome subunit biogenesis protein NIP7 homolog
- AT5g20600/F7C8_190
- Probable rRNA-processing protein EBP2 homolog
- Transducin/WD40 repeat-like superfamily protein
- Protein MAK16 homolog
- Ribosome assembly factor mrt4
- Pescadillo homolog
- Ribosome biogenesis protein WDR12 homolog
- Ribosome biogenesis protein BOP1 homolog
Sequence:
MGFKRKKDDGDGEEMESDVRGKSTFSGGEKRNVILPSMIKNKDKRSKVYAKQKHEKKLEKQKKIRARDAAEKRALELGEEPPQKMIPKTIENTRESDETVCRPDDEELFADIDADEFNPVLRREIAPKVLLTTCRFNSTRGPALISELLSVIPNSHYQKRGTYDLKKIVEYATKKDFTSLIVVHTNRREPDALLIIGLPNGPTAHFKLSNLVLRKDIKNHGNPTSHQPELVLNNFTTRLGNRVGRFFQSLFPPDPNFRGRRVVTFHNQRDFIFFRHHRYIFETKESKSDKGKEETIKPRLQECGPRFTLKLVTLQHGTFDTKGGEFEWVHKPEMDTSRRRFFL
Protein: Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3 (EC 3.2.1.113) (EC 3.2.1.209) (Q93Y37)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Class I alpha-mannosidase essential for early N-glycan processing. Removes preferentially alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). Involved in root development and cell wall biosynthesis.
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000305|PubMed:20023195}; Single-pass type II membrane protein {ECO:0000269|PubMed:20023195}.
Interaction partners:
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2
- Probable glucan 1,3-alpha-glucosidase
- Alpha-mannosidase 2
- Protein OS-9 homolog
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Dol-P-Man:Man
- Alpha-1,2-mannosyltransferase ALG9
- Calnexin homolog 1
- Dol-P-Man:Man
Sequence:
MSKSLPYSVKDIHYDNAKFRHRSPLKVFSQSLLTLSTKRNYASCSTGKFLILILFFGVACLMLMSKSPNESGLNEKGKVTFVGGLRLGGLLRKPPRLPPRLSPDEGQLRGSSTNGSTISNSDPKWAARQQSVKEAFDHAWSGYRKYAMGYDELMPISQKGVDGLGGLGATVVDALDTAMIMGLDNIVSEAGSWVETHLLERISQKGQVNLFETTIRVLGGLLSAYHLSGGEQGTVNMTHVGPKPVIYLNIAKDLADRLLSAFTSSPTPVPFCDVILHESTAHPAPGGASSTAEVASVQLEFNYLSSISGDPKYSTEAMKVLAHIKTLPKTEGLVPIYISPQTGDFVGENIRLGSRGDSYYEYLIKVWLQQGAKLNSNFTYLHDMYIEAMKGVRHLLVQNSIPKGLVFVGELPYGSKGEFSPKMDHLVCFLPGTLALGATKGLTKEQALKENLLSFEDLENLKLAEDLAKTCFEMYEVTATGLAPEIAYFHTKDYTEDGLDGGNKSSMYANDIIIKPADRHNLLRPETVESLFVLYRITKDTKYRDQGWQIFEAFEKYTKVKSGGYTSLDDVTEVPPHRRDKMETFFLGETLKYLYLLFGDDSVIPLDKFVFNTEAHPLPIRRNT
Protein: Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase (EC 2.1.1.57) (Q385S9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MNFPDSRVLSDEFPRRKYKPSSATRLEDIVLKGLHYGQRKLLLSEIEFLSAYLEGRQAGAKPTLVVYAGAANGSHLPFLFQLFEAVKFVLIDPAPFCDAVREISLNKQGPILDLVQGFCTDELCKQLSSSYGSTYDILLVSDIRSGVPEKQSNRENTLMIMRDNDMQRSWCWTLKAEAALLKFHPPYPPCRDRNSRHYDEADDTPESIEYLDGVRLFGVWAPKSSSELRLCVQGPFLQGTSFPMRRYDCTTHEEQCYFYNTDNRYTRDCAAESGILERYLQLFPSAPYSDPTALSMTISNFLGFPLFLPLDSSFSESDARWVTLLYSTRIPTCLELFTTLRGRVTHTVMKQLAEEWQSATTVPKGVSIDSVELTSEFWKAVCAGDLTEAYSFPNIRWRFANLLISRRRKRSASDRAP
Protein: Pentatricopeptide repeat-containing protein DOT4, chloroplastic (Protein DEFECTIVELY ORGANIZED TRIBUTARIES 4) (Protein FLAVODENTATA) (Q9SN39)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a major role in single RNA editing events in chloroplasts. Acts as a site-recognition transacting factor involved in the edition of the unique site (corresponding to cytidine-488) of rpoC1, which is a plastid-encoded subunit of the chloroplast DNA-directed RNA polymerase. May provide the catalytic activity for editing site conversion. Involved in leaf vasculature patterning.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Protein PROTON GRADIENT REGULATION 5
- Ferredoxin--NADP reductase, root isozyme 2, chloroplastic
- Ferredoxin--NADP reductase, root isozyme 1, chloroplastic
- Ferredoxin--NADP reductase, leaf isozyme 2, chloroplastic
- Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic
Sequence:
MAMLVTNLSSSSFCFFSSPHLQNQKEIRSGVRVRKYVIFNRASLRTVSDCVDSITTFDRSVTDANTQLRRFCESGNLENAVKLLCVSGKWDIDPRTLCSVLQLCADSKSLKDGKEVDNFIRGNGFVIDSNLGSKLSLMYTNCGDLKEASRVFDEVKIEKALFWNILMNELAKSGDFSGSIGLFKKMMSSGVEMDSYTFSCVSKSFSSLRSVHGGEQLHGFILKSGFGERNSVGNSLVAFYLKNQRVDSARKVFDEMTERDVISWNSIINGYVSNGLAEKGLSVFVQMLVSGIEIDLATIVSVFAGCADSRLISLGRAVHSIGVKACFSREDRFCNTLLDMYSKCGDLDSAKAVFREMSDRSVVSYTSMIAGYAREGLAGEAVKLFEEMEEEGISPDVYTVTAVLNCCARYRLLDEGKRVHEWIKENDLGFDIFVSNALMDMYAKCGSMQEAELVFSEMRVKDIISWNTIIGGYSKNCYANEALSLFNLLLEEKRFSPDERTVACVLPACASLSAFDKGREIHGYIMRNGYFSDRHVANSLVDMYAKCGALLLAHMLFDDIASKDLVSWTVMIAGYGMHGFGKEAIALFNQMRQAGIEADEISFVSLLYACSHSGLVDEGWRFFNIMRHECKIEPTVEHYACIVDMLARTGDLIKAYRFIENMPIPPDATIWGALLCGCRIHHDVKLAEKVAEKVFELEPENTGYYVLMANIYAEAEKWEQVKRLRKRIGQRGLRKNPGCSWIEIKGRVNIFVAGDSSNPETENIEAFLRKVRARMIEEGYSPLTKYALIDAEEMEKEEALCGHSEKLAMALGIISSGHGKIIRVTKNLRVCGDCHEMAKFMSKLTRREIVLRDSNRFHQFKDGHCSCRGFW