wanglab/gogpt-training-data huggingface dataset:
Protein: Protein LNK1 (Night light-inducible and clock-regulated 1) (A8MQN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional coactivator necessary for expression of the clock genes PRR5 and TOC1. Antagonizes REV8 function in the regulation of anthocyanin accumulation. Involved in red light input to the clock. Activates clock-controlled genes with afternoon peak. Mediates light inhibition of hypocotyl elongation.
Subcellular location: Nucleus {ECO:0000269|PubMed:25012192}.
Interaction partners:
- Protein REVEILLE 8
- Protein LHY
- Protein CCA1
- Protein LNK3
- Two-component response regulator-like APRR9
- Protein LNK4
- Protein REVEILLE 4
- Protein REVEILLE 6
- Two-component response regulator-like APRR7
- Two-component response regulator-like APRR5
Sequence:
MSDLYIHELGDYLSDEFHGNDDGIVPDSAYEDGGQFPILVSNRKKRRNDDMGSGTNHLKSNTFIKREANMLGKNPWPEKDSGGSSVSRDTGTGKDVQDMTLEDTNTSDHGFNGGHVDVVENFSTGDPMLCDTSAATNDGVYNYSLNSIPDAENDLSFFDNGDKEKNDLFYGWGDIGNFEDVDNMLRSCDSTFGLDSLNNEGDLGWFSSAQPNEETAGAMTDDLKPDKMLENQRTAMLQVEDFLNNSEPNHAVEDEYGYTIEDDSAQGKSSQNVFDTSLQKKDILMLDVEANLEKKQTDHLHHLDGKSDGFSENSFTLQHSGISREIMDTNQYYPPSAFQQRDVPYSHFNCEQPSVQVSACESKSGIKSENKPSPSSASNESYTSNHAQSIESLQGPTVDDRFRKVFETRANLLPGQDMPPSFAANTKKSSKTDSMVFPDAAPIQKIGLENDHRKAATELETSNMQGSSCVSSVVDDISLEATSFRQLQQVIEQLDVRTKLCIRDSLYRLAKSAEQRHHGGNRPEKGAGSHLVTGEADKYAGFMDIETDTNPIDRSIAHLLFHRPSDSSLSSDNNVLSYKSHPMIPQPNSSPSLRIEKQEETTELRPEAEVVTSDNN
Protein: Protein US2 (P13292)
Organism: Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)
Function: Plays a role in the activation of the host NF-kappa-B pathway by interacting with and thus activating the component MAP3K7.
Subcellular location: Virion {ECO:0000269|PubMed:23785212}. Host cytoplasm {ECO:0000269|PubMed:23785212, ECO:0000269|PubMed:9820154}. Host cell surface {ECO:0000269|PubMed:23785212}. Host nucleus {ECO:0000269|PubMed:9820154}. Note=Found in association with the nuclear matrix of infected cells.
Interaction partners:
Sequence:
MGVVVVSVVTLLDQRNALPRTSADASPALWSFLLRQCRILASEPLGTPVVVRPANLRRLAEPLMDLPKFTRPIVRTRSCRCPPNTTTGLFAEDDPLESIEILDAPACFRLLHQERPGPHRLYHLWVVGAADLCVPFFEYAQKTRLGFRFIATKTNDAWVGEPWPLPDRFLPERTVSWTPFPAAPNHPLENLLSRYEYQYGVVVPGDRERSCLRWLRSLVAPHNKPRPASSRPHPATHPTQRPCFTCMGRPEIPDEPSWQTGDDDPQNPGPPLAVGDEWPPSSHVCYPITNL
Protein: Mitochondrial import inner membrane translocase subunit tim22 (P87146)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q12328}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit tim9
- Mitochondrial import inner membrane translocase subunit tim10
- Mitochondrial import inner membrane translocase subunit tim54
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Mitochondrial import inner membrane translocase subunit tim23
- Mitochondrial import inner membrane translocase subunit tim8
- Mitochondrial import inner membrane translocase subunit tim13
- Mitochondrial import inner membrane translocase subunit tim14
- Mitochondrial import inner membrane translocase subunit tim44
- Uncharacterized mitochondrial carrier C12D12.05c
Sequence:
MSLSGLLPPNLGGNSPNADGNLTPEEKAALQQAKIIGYMNRISESCVFKSSMAGVLGFGLGGIFGMFISSLDLQHIDPKIYEKPFREQIRIQARDMGSRSFSTAKNFGLLGLIYSGSECCIEAFRAKTDIYNAIAAGVFTGGALAVRSGPKAIVLGGAGFGLFSYGIEKYMHWGE
Protein: DNA ligase (EC 6.5.1.1) (A7E283)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MESVSKSDAKPQAFVAAQVPFIHLCTVLEKIQKTKLRPDKSKILKEFIDSWRNFHAALHKDNPDTADSFYAAMRLIVPSFERERMAYGIKENMLAKLYIEVLGLPKNGDEANKLLNYRAPTTSQGEAGDFALMAYFVLKKRCTSQGNLSIKEVNDFLGSVATNNASKQKDQVKKSLLHLITQSSALEQKWLIRMILKDMKLGISKETVLQVFHPDAPEFYNVTTDLNKVCRQLHDPSVSLSEVSIDLFSAFKPMLAAVANIRQIEKQMGNRPFYIETKLDGERIQLHKAGDVYKYYTRNSYEYTQQFGASPLEGSLTPYIHTVFSPHVVNCILDGEMMAYNPKTETFMQKGSKFDIKRLVDDSDLQTCFCVFDVLLINNQKFGKEPLKKRYESLETVFSPIKGRIHLVSKSEGRTMQEVVNSLNEAIDNREEGIMVKDPMSIYKPDKRGEGWLKIKPEYVDGLMDELDLLIVGGYWGKGRRSGMLSHFLCAVAEVPSPGEKPTVFHTLCRIGSGYTLKELYDLGVKLAKHWKVYNKNNPPAAILCGTEKPEVYIEPRNSVILQVKAAEIVTSEMYKTDCTLRFPRIERIREDKEWHQCMTLDDLNQFRSKASGKLASRHLNIHEDQPEKKKRKIVAKPKKTIGVIDHFKSQDLSKVAKETDMFEEVEFCVINGDDEHSKAELEKGVARCGGIVVQNPGKDTYCAIAAVQNMRVKNLISSDQHDVVWATWLLECLENKQVIPWQPRHMIHMSPSTREHFAKEYDQYGDSYYVDTSEQQLRDVIERISSAEVKSLSVAQIEAENAWDDLPTSIFRPYSAYFDRCADIGDPKSVICGTCLDTRALEFRFHGGKVVEKLKEGISHVVVEDMKRALDLKTLRRLHAKKFKIVHESWVTDSIKAGHVKDEIDYLI
Protein: Teosinte-branching 1 (Q7Y1X7)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLPFFDSPSPMDIPLYQQLQLTPPSPKPDHHHHHHSTFFYYHHHPPPSPSFPSFPSPAAATIASPSPAMHPFMDLELEPHGQQLAAAEEDGAGGQGVDAGVPFGVDGAAAAAAARKDRHSKISTAGGMRDRRMRLSLDVARKFFALQDMLGFDKASKTVQWLLNMSKAAIREIMSDDASSVCEEDGSSSLSVDGKQQQHSNPADRGGGAGDHKGAAHGHSDGKKPAKPRRAAANPKPPRRLANAHPVPDKESRAKARERARERTKEKNRMRWVTLASAISVEAATAAAAAGEDKSPTSPSNNLNHSSSTNLVSTELEDGSSSTRHNGVGVSGGRMQEISAASEASDVIMAFANGGAYGDSGSYYLQQQHQQDQWELGGVVYANSRHYC
Protein: Caldesmon (CDM) (P12957)
Organism: Gallus gallus (Chicken)
Function: Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also plays an essential role during cellular mitosis and receptor capping.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P13505}. Cytoplasm, myofibril {ECO:0000250|UniProtKB:P13505}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:P13505}. Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle). {ECO:0000250|UniProtKB:P13505}.
Interaction partners:
Sequence:
MDDFERRRELRRQKREEMRLEAERLSYQRNDDDEEEAARERRRRARQERLRQKEEGDVSGEVTEKSEVNAQNSVAEEETKRSTDDEAALLERLARREERRQKRLQEALERQKEFDPTITDGSLSVPSRREVNNVEENEITGKEEKVETRQGRCEIEETETVTKSYQRNNWRQDGEEEGKKEEKDSEEEKPKEVPTEENQVDVAVEKSTDKEEVVETKTLAVNAENDTNAMLEGEQSITDAADKEKEEAEKEREKLEAEEKERLKAEEEKKAAEEKQKAEEEKKAAEERERAKAEEEKRAAEERERAKAEEERKAAEERERAKAEEERKAAEERAKAEEERKAAEERAKAEEERKAAEERAKAEKERKAAEERERAKAEEEKRAAEEKARLEAEKLKEKKKMEEKKAQEEKAQANLLRKQEEDKEAKVEAKKESLPEKLQPTSKKDQVKDNKDKEKAPKEEMKSVWDRKRGVPEQKAQNGERELTTPKLKSTENAFGRSNLKGAANAEAGSEKLKEKQQEAAVELDELKKRREERRKILEEEEQKKKQEEAERKIREEEEKKRMKEEIERRRAEAAEKRQKVPEDGVSEEKKPFKCFSPKGSSLKIEERAEFLNKSAQKSGMKPAHTTAVVSKIDSRLEQYTSAVVGNKAAKPAKPAASDLPVPAEGVRNIKSMWEKGNVFSSPGGTGTPNKETAGLKVGVSSRINEWLTKTPEGNKSPAPKPSDLRPGDVSGKRNLWEKQSVEKPAASSSKVTATGKKSETNGLRQFEKEP
Protein: FAST kinase domain-containing protein 5, mitochondrial (Q7L8L6)
Organism: Homo sapiens (Human)
Function: Plays an important role in the processing of non-canonical mitochondrial mRNA precursors.
Subcellular location: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:20869947, ECO:0000269|PubMed:25683715}. Note=Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids. {ECO:0000269|PubMed:25683715}.
Interaction partners:
- NLR family member X1
- FAST kinase domain-containing protein 2
- G-rich sequence factor 1
Sequence:
MAATLKSLKLVRYRAFCSPSAFGAVRSVSYWNVSSTQHGGQDPPEHISLCHSAKKVKNICSTFSSRRILTTSSAHPGLEFSKTSSSKASTLQLGSPRATGVDEEDVEVFDSFENMRVFLQLRPEYRVHSYNASETSQLLSVSEGELILHKVRVNQNNLQAQVIVDYLCKLSSLPAEQHPVLLGSTSFALLCQLSVKKIQLFDTQDLINVLKAFVILGIPHSHSMLDVYETKCCHQVWEMNMDQLLLVADLWRYLGRKVPRFLNIFSSYLNLHWKDLSLSQLVHLIYVIGENRQVSQDLMQKLESLILKYIDLINLEEVGTICLGFFKSSTNLSEFVMRKIGDLACANIQHLSSRSLVNIVKMFRFTHVDHINFMKQIGEIAPQRIPSLGVQGVMHLTLYCSALRFLNEGVMNAVAASLPPRVAHCRSKDVAKILWSFGTLNYKPPNAEEFYSSLISEIHRKMPEFNQYPEHLPTCLLGLAFLEYFPVELIDFALSPGFVRLAQERTKFDLLKELYTLDGTVGIECPDYRGNRLSTHLQQEGSELLWYLAEKDMNSKPEFLETVFLLETMLGGPQYVKHHMILPHTRSSDLEVQLDVNLKPLPFNREATPAENVAKLRLEHVGVSLTDDLMNKLLKGKARGHFQGKTESEPGQQPMELENKAAVPLGGFLCNVADKSGAMEMAGLCPAACMQTPRMKLAVQFTNRNQYCYGSRDLLGLHNMKRRQLARLGYRVVELSYWEWLPLLKRTRLEKLAFLHEKVFTSAL
Protein: DnaJ homolog subfamily B member 4 (Heat shock 40 kDa protein 1 homolog) (HSP40 homolog) (Heat shock protein 40 homolog) (Human liver DnaJ-like protein) (Q9UDY4)
Organism: Homo sapiens (Human)
Function: Probable chaperone. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18837411}. Cell membrane {ECO:0000269|PubMed:16542645}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:36264506}. Note=Cytoplasmic according to PubMed:18837411 and membrane-associated according to PubMed:16542645.
Interaction partners:
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 1A
- Heat shock cognate 71 kDa protein
- Heat shock protein 105 kDa
- Heat shock 70 kDa protein 6
- Heat shock 70 kDa protein 1-like
- Endoplasmic reticulum chaperone BiP
- Heat shock 70 kDa protein 14
- DnaJ homolog subfamily B member 5
- DnaJ homolog subfamily B member 1
Sequence:
MGKDYYCILGIEKGASDEDIKKAYRKQALKFHPDKNKSPQAEEKFKEVAEAYEVLSDPKKREIYDQFGEEGLKGGAGGTDGQGGTFRYTFHGDPHATFAAFFGGSNPFEIFFGRRMGGGRDSEEMEIDGDPFSAFGFSMNGYPRDRNSVGPSRLKQDPPVIHELRVSLEEIYSGCTKRMKISRKRLNADGRSYRSEDKILTIEIKKGWKEGTKITFPREGDETPNSIPADIVFIIKDKDHPKFKRDGSNIIYTAKISLREALCGCSINVPTLDGRNIPMSVNDIVKPGMRRRIIGYGLPFPKNPDQRGDLLIEFEVSFPDTISSSSKEVLRKHLPAS
Protein: Progonadoliberin-1 (Progonadoliberin I) (B7TCB2)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MEKPRRRMVATVLLCVLAVGLGLAQHWSYGLQPGGKRSTQLLLGPFQEIANEMEKLEEEQQSACPGSHQNSRSGALREAMERLLEEQGRRKNV
Protein: Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (EC 2.7.11.19) (Phosphorylase kinase subunit gamma-1) (Serine/threonine-protein kinase PHKG1) (EC 2.7.11.1, EC 2.7.11.26) (P00518)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3.
Interaction partners:
- Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
- Phosphorylase b kinase regulatory subunit beta
- Phosphorylase b kinase regulatory subunit alpha, liver isoform
- Calmodulin
- Calmodulin like 5
- phosphorylase kinase
- Glycogen phosphorylase, muscle form
- cAMP-dependent protein kinase
- Doublecortin
- Alpha-1,4 glucan phosphorylase
Sequence:
MTRDAALPGSHSTHGFYENYEPKEILGRGVSSVVRRCIHKPTCKEYAVKIIDVTGGGSFSAEEVQELREATLKEVDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEKLREVCGTPSYLAPEIIECSMNDNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDYSDTVKDLVSRFLVVQPQKRYTAEEALAHPFFQQYVVEEVRHFSPRGKFKVICLTVLASVRIYYQYRRVKPVTREIVIRDPYALRPLRRLIDAYAFRIYGHWVKKGQQQNRAALFENTPKAVLFSLAEDDY
Protein: Renalase (EC 1.6.3.5) (Q48MT7)
Organism: Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6))
Function: Catalyzes the oxidation of the 1,2-dihydro- and 1,6-dihydro- isomeric forms of beta-NAD(P) back to beta-NAD(P)+. Has a preference for 1,2-dihydro-beta-NAD as substrate. May serve to protect primary metabolism dehydrogenases from inhibition by the 1,2-dihydro- and 1,6-dihydro-beta-NAD(P) isomers.
Interaction partners:
Sequence:
MTVPIAIIGTGIAGLSAAQALTSAGHQVHLFDKSRGSGGRMSSKRSDAGSLDMGAQYFTARDRRFATAVKQWQAQGHVSEWTPLLYNFHGGRLSPSPDEQVRWVGEPGMSAITRAMRGDLPVSFSCRITDVFRGEQHWNLLDAEGENHGPFSHVIIATPAPQATALLAAAPKLASVVAGVKMDPTWAVALAFETPLQTPMQGCFVQDSPLDWLARNRSKPGRDDTLDSWVLHATSQWSRQNLDASREQVIEHLHGAFAELIDCAMPAPVFSLAHRWLYARPAGSHEWGALSDADLGIYVCGDWCLSGRVEGAWLSGQEAARRLLEHLQ
Protein: PR domain zinc finger protein 4 (EC 2.1.1.-) (PR domain-containing protein 4) (Q80V63)
Organism: Mus musculus (Mouse)
Function: May function as a transcription factor involved in cell differentiation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 16
- Protein arginine N-methyltransferase 5
Sequence:
MNDMNLSPVGMEQLSSSSVSNALPVSGSHLGLAASPSHSAIPAPGLPVAIPNLGPSLSSLPSALSLMLPVGIGDRGVMCGLPERNYTLPPPPYPHLESSYFRTILPGILSYLADRPPPQYIHPNSINVDGNTALSITNNPSALDPYQANGNVGLELGIVSIDSRSVNTHGAQSLHPNDGHEVALDTTITMENVSRVTSPISTDGMAEELTMDGVTGEHPQIPNGSRSHEPLSVDSVSNSLTAEAVGHGGVIPIHGNGLELPVVMETDHIANRVNGMSDSTLSDSIHTVAMSTNSVSVALSTSHNLASLESVSLHEVGLSLEPVAVSSITQEVAMGTGHVDVSSDSLSFVPSSLQMEDSNSNKENMATLFTIWCTLCDRAYPSDCPDHGPVTFVPDTPIESRARLSLPKQLVLRQSIVGTDVVGVLPLIGVWTAETIPVRTCFGPLIGQQSHSLEVAEWTDKAVNHVWKIYHTGVLEFCIITTDENECNWMMFVRKARNREEQNLVAYPHDGKIYFCTSQDIPPESELLFYYSRNYAQQIGVPEHPDVHLCNCGKECSSYSEFKAHLTSHIHNHLPSQGHSSSHGPSHSKERKWKCSMCPQAFISPSKLHVHFMGHMGMKPHKCDFCSKAFSDPSNLRTHLKIHTGQKNYRCTLCDKSFTQKAHLESHMVIHTGEKNLKCDYCDKLFMRRQDLKQHVLIHTQERQIKCPKCDKLFLRTNHLKKHLNSHEGKRDYVCEKCTKAYLTKYHLTRHLKTCKEPSSSSSAQEEEDDESEEEDLADSMRTEDCRMGSAVYSTDESLSAHK
Protein: Interleukin-10 (IL-10) (Cytokine synthesis inhibitory factor) (CSIF) (P43480)
Organism: Bos taurus (Bovine)
Function: Major immune regulatory cytokine that acts on many cells of the immune system where it has profound anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Mechanistically, IL10 binds to its heterotetrameric receptor comprising IL10RA and IL10RB leading to JAK1 and STAT2-mediated phosphorylation of STAT3. In turn, STAT3 translocates to the nucleus where it drives expression of anti-inflammatory mediators. Targets antigen-presenting cells (APCs) such as macrophages and monocytes and inhibits their release of pro-inflammatory cytokines including granulocyte-macrophage colony-stimulating factor /GM-CSF, granulocyte colony-stimulating factor/G-CSF, IL-1 alpha, IL-1 beta, IL-6, IL-8 and TNF-alpha. Interferes also with antigen presentation by reducing the expression of MHC-class II and co-stimulatory molecules, thereby inhibiting their ability to induce T cell activation (By similarity). In addition, controls the inflammatory response of macrophages by reprogramming essential metabolic pathways including mTOR signaling (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P22301}.
Interaction partners:
- Interleukin-10 receptor subunit alpha
- Interleukin-10 receptor subunit beta
- Interleukin-6
- Interleukin-4
- Interleukin-5
- Interferon gamma
- Interleukin-1 beta
- Tumor necrosis factor
- Interleukin-2
- Interleukin-7
Sequence:
MHSSALLCCLVFLAGVAASRDASTLSDSSCIHLPTSLPHMLRELRAAFGKVKTFFQMKDQLHSLLLTQSLLDDFKGYLGCQALSEMIQFYLEEVMPQAENHGPDIKEHVNSLGEKLKTLRLRLRRCHRFLPCENKSKAVEKVKRVFSELQERGVYKAMSEFDIFINYIETYMTTKMQK
Protein: Alpha-1,2 mannosyltransferase KTR1 (EC 2.4.1.-) (P27810)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mannosyltransferase that transfers a mannose residue from GDP-mannose to a range of acceptors in vitro, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
- Glycolipid 2-alpha-mannosyltransferase
- Probable mannosyltransferase KTR3
- Alpha-1,2-mannosyltransferase MNN2
- Alpha-1,2-mannosyltransferase MNN5
Sequence:
MAKIMIPASKQPVYKKLGLLLVAVFTVYVFFHGAQYARGSAPSPKYSTVLSSGSGYKYSKVELPKYTGPREKATFVTLVRNRDLYSLAESIKSVEDRFNSKFNYDWVFLNDEEFTDEFKNVTSALVSGTTKYGVIPKEHWSFPEWIDEEKAAQVRKEMGEKRIIYGDSISYRHMCRFESGFFYRHPLMDDYDWYWRVEPDIKLHCDIDYDVFKFMKDNKKKYAFAISIKEYEATIPTLWETTRKFMEAHPELIHENNMLDFVSDDQGLSYNLCHFWSNFEIAALDLWRSPAYSAYFDYLDREGGFFYERWGDAPVHSIGAALFLDRSEIHHFGDIGYYHVPFHSCPIDTSIRLANKCDCDPSKDFTWHSYSCTTKFYNINKLPKPAGWQNHIG
Protein: WD repeat-containing protein 54 (Q9H977)
Organism: Homo sapiens (Human)
Function: When cross-linked to form dimers and trimers, it has a regulatory effect on ERK signaling pathway activity in response to EGF stimulation. Colocalizes with the EGF receptor in WDR54-specific vesicle where it sustains the internalization and controls the degradation of the EGF receptor after EGF stimulation.
Subcellular location: Vesicle {ECO:0000269|PubMed:30458214}. Cytoplasm {ECO:0000250|UniProtKB:D3ZX63}. Cell membrane {ECO:0000250|UniProtKB:D3ZX63}. Note=Aggregates in vesicles when cross-linked. {ECO:0000269|PubMed:30458214}.
Interaction partners:
- Protein OSCP1
Sequence:
MFRWERSIPLRGSAAALCNNLSVLQLPARNLTYFGVVHGPSAQLLSAAPEGVPLAQRQLHAKEGAGVSPPLITQVHWCVLPFRVLLVLTSHRGIQMYESNGYTMVYWHALDSGDASPVQAVFARGIAASGHFICVGTWSGRVLVFDIPAKGPNIVLSEELAGHQMPITDIATEPAQGQDCVADMVTADDSGLLCVWRSGPEFTLLTRIPGFGVPCPSVQLWQGIIAAGYGNGQVHLYEATTGNLHVQINAHARAICALDLASEVGKLLSAGEDTFVHIWKLSRNPESGYIEVEHCHGECVADTQLCGARFCDSSGNSFAVTGYDLAEIRRFSSV
Protein: RRM domain-containing protein (Q57YB8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAEGVPAPSSSFAQKMHQLLQIRAERQPLAEGYMRCPLNPTHQVPIAAIVTHLSKAHQQDSLDIAPDAMYGVNTRSRRSEFLKEQLQRMQPVDESDLSESGYSNHRRKRYRRSSSQSYSSDMGSSSSCCSNGRSNVSRQSNSSRSSGKHRHYEERPYNNRRREEQPTQRSFHGNNTTNWHDPSNVFKRLLGRYPFGASINKQRLTEFLICFGPLQSFNFLANGTEFVVEFESSVAASKCLQAATPNLLIDDVCVRMYPVPLPSPGVAPEFSYGGAEIMRTPPPWPDDAAPPTVVSSLPAAQQNQPWPPTDITPSVAVGVGAGSKSVGVPVLSNVDDLVDAFTSVSSARITSNTAILSCAVRTTCGKNVTTEDIWKELWHFGEMRNILLVGPRVVVEFSDGRGVRRATQAMELEPGKFKFCSLLGEGEGR
Protein: Oligopeptide ABC transporter, ATP-binding protein (Q5LU45)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004417}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004417}.
Interaction partners:
- Oligopeptide ABC transporter, permease protein
- N-acetyltaurine ABC transporter, permease protein
- Peptide/opine/nickel uptake family ABC transporter, permease protein
- Glutathione transport system permease protein GsiC
- Dipeptide ABC transporter, permease protein
- Peptide/opine/nickel uptake family ABC transporter, permease protein
- Oligopeptide/dipeptide ABC transporter, permease protein
- Peptide/nickel/opine uptake family ABC transporter, permease protein
- Oligopeptide/dipeptide ABC transporter, permease protein
- Peptidase, M20/M25/M40 family
Sequence:
MRNGYRVEPMVDHKYALEVDGLTVSLPTNADRPNAVENISFTVAPGEIVCVVGESGSGKSVTASAVMGLLPDALRPIAGRTLLEGEDTLAADKNRLRDLRGTRMAMIFQEPMTALNPVTRVGEQIAEVLEIHTTMSAAERRQRAIEVMESVHLPDPERMVDSFPHQLSGGQRQRIMIAMALVLDPILLIADEPTTALDVTTQAQILKLIKEMQERRGTGVLFITHDFGVVAEIADRIVVMQNGRIVEYGDRDEVLQRPKAPYTQMLMRSVPSMTPPDRSAKTDKTAVEVTALNKVYGRTGWLSKDRIVHAVQDVDLQVRKGETLGIVGESGSGKSTVARCIARLIDPTSGSIGLHGAEIAHLTQGQLHPYRRKVQIVFQDPYRSLNPRRTIGQSLIEAPMNYGMTRDQALTVARDLMELVGLSGDALDRYPHQFSGGQRQRICIARALAVEPDILIADEAVSALDVSVQAQVLKLLDDIRVKYNLAMLFITHDLRVAAQICDRLIVMQKGVVVEHGPTRQVYQDPQHAYTRLLLEAAPGQGMRFGSQIQPTVAQGS
Protein: Protein psiM (Q54P69)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Latrophilin receptor-like protein A
Sequence:
MKKINNNKIFVLFLTILLYLLNITTAQKPVSINIKIFDQLPLYNDNFGSQSRAATIKSMVATSLNTTFKTPSLGSATSSLPSPQLFQYWFQSNFANETKNSGLNAPLTRTITLNYDSDSGNYIFNNPNFFLIDTDGFDKTASNRIYKDSTGTYHNYHYCVAFNYVFKPDGQGKEMFKFTGNDDVWVFVNNKLLLDGGGVRSPEATTVDFTKAGLVKSQETPLDFFYCERSTNSPPSFKIETNLGGLYCKAYDYCGVCNGDGGTCCNPQTDCLTQLENGTLINDKCTIPICPPLDTQIDKNLGIGFFCQHSQIPDPYAGSLCEKGECDSLTGIWTRNTSICPTDKDLAPQCRKQATCDPKLGCQSTYLCNNVCDIGTCNNGTCTQKTSNDCVQELDRGVEDKCFTYKCVPNVGCSKTPICPRGTDPCKNYTCSGGICGTVDIPQSECSCPCPGLNKCNTRICNPDNTCTLFNLTEINDGNPCTDDLCDPVTGDITHVMTTRCSGCNTCDVKTGKCVAQDSHCDDGNPCTDNACVASANSTANSQVGQCTQTPTAKCDLGDKCMVYSCTLEGGCNATQRVCPNSGACKIGYCEPGFGCKLKDRVCSSDWYCIEAQCDAKYGCIQFDRRCAPDNSKCQEGVCVNNTAIGKNDGKCISEDYDPKPFVCQKAALVSTAVIASVVVVGAVVLGAAIFAGKKGYDAWKTSQGNVMAASQANPLYTQSSNGGENPLYNSPT
Protein: Casein kinase II subunit alpha-1 (CK II) (EC 2.7.11.1) (Casein kinase alpha 1) (AtCKA1) (Q08467)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates casein in vitro. The alpha chain contains the catalytic site. The tetrameric holoenzyme CK2, composed of two alpha and two beta subunits, phosphorylates the transcription factor GBFl, resulting in stimulation of its DNA binding activity. CK2 phosphorylates the transcription factor PIF1 after an exposure to light, resulting in a proteasome-dependent degradation of PIF1 and promotion of photomorphogenesis. CK2 phosphorylates translation initiation factors. May participate in the regulation of the initiation of translation. Acts as circadian clock component that maintains the correct period length through phosphorylation of CCA1. Required for the maintenance and control of genomic stability and chromatin structure. May act as an ectokinase that phosphorylates several extracellular proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:16926165}. Nucleus, nucleolus {ECO:0000269|PubMed:16926165}. Note=Enriched in the nucleolus. {ECO:0000269|PubMed:16926165}.
Interaction partners:
- Casein kinase II subunit beta-1
- Casein kinase II subunit beta-3
- Casein kinase II subunit beta-2
- Putative casein kinase II subunit beta-4
- UPF0235 protein At5g63440
- Protein CCA1
- FACT complex subunit SSRP1
- FACT complex subunit SPT16
- At1g09850
- Probable cysteine protease RD21B
Sequence:
MIDTLFFLFFLFFDSPLRRLLLLCAVLALRAPTAHSPILRSSIVTPTARAVSEVSGCTTIDPDFLVEISDSNQTRAMSKARVYTEVNVIRPKDYWDYESLIVQWGEQDDYEVVRKVGRGKYSEVFEGINVNSKEKCIIKILKPVKKKKIRREIKILQNLCGGPNIVKLLDVVRDQHSKTPSLIFEYVNSTDFKVLYPTLTDYDIRYYIYELLKALDFCHSQGIMHRDVKPHNVMIDHELRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDLQDYDYSLDMWSLGCMFAGMIFRKEPFFYGHDNQDQLVKIAKVLGTDELNAYLNKYQLELDPQLEALVGRHSRKPWSKFINADNQHLVSPEAIDFLDKLLRYDHQDRLTAKEAMAHAYFAQVRAAETSRMRSQ
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (P82205)
Organism: Bombyx mori (Silk moth)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P00441}.
Interaction partners:
- Sod_Cu domain-containing protein.
- DJ-1 beta
- Glutathione peroxidase
- Superoxide dismutase
Sequence:
MPAKAVCVLRGDVSGTVFFDQQDEKSPVVVSGEVQGLTKGKHGFHVHEFGDNTNGCTSAGAHFNPEKQDHGGPSSAVRHVGDLGNIEAIEDSGVTKVSIQDSQISLHGPNSIIGRTLVVHADPDDLGLGGHELSKTTGNAGGRIACGVIGLAKI
Protein: Leucine-rich repeat protein kinase family protein (F4K685)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MGCGFSGQIPESIGSLEQLVTLSLNSNKFNGTIPASIGLLSKLYWFDIADNQIEGKLPVSDGASLPGLDMLLQTKHFHFGKNKLSGDIPEKLFSANMTLKHLLFDGNLLTGEIPQSLSLVKTLTVLRLDRNRLSGEIPPSLNNLTNLQELYLSDNKFTGSLPSLTSLTSLSTLAVSNNRLTSSQISSWISLLPTSLATLRMAGLQLQGPIPTSLFSLPELQTVILKRNWLNETLDFGTNKSQNLDFVDLQYNDITEYIKQPANKGSSRIVILANNPVCPEVGNPPNEYCIEVEHNSSYSSPKNTCGRCSGEDREPIPTTCRCVYPITGTLTFRSPSFSGYSNNDTFENLRLNLTGFFENRNYTVDSVAIRNIREDEDDHYLLIDLSLFPYKQDRFNETGMDSVISRFSTQTYKPPNTFGPYIFKANKYNKFPAGGSNSSHIIGAVVGSTVFLLILMIAGIYALKQKRRAEKANDQINPFGKDVLLSGKTDKILIAFFLYVTAKWDANQNSVDAPQLMGTKAFTFEEMRKCANNFSVANDVGGGGYGQVYKGILPSGQLIAIKRAQPGSLQGALEFKTEIELLSRVHHKNVVKLLGFCFDRGEQMLVYEYIPNGSLRDSLSGKSGIRLDWTRRLRIALGSGKGLAYLHELADPPIIHRDVKSSNVLLDESLTAKVADFGLSQLVEDAEKANVTAQVKGTMGYLDPEYYMTNQLTEKSDVYGFGVMMLELLTGKIPIENGKYVVKEMKMKMNKSKNLYDLQDFLDTTISATSNRNLKGFEKYVDVALRCVDPEGVKRPSMNEVVKEIENIMQYAGLNPNVESYASSRTYDEASKESGDLYGNNSFEYSASFPTTNLEPQ