wanglab/gogpt-training-data huggingface dataset:
Protein: DNA excision repair protein ERCC-6-like (EC 3.6.4.12) (ATP-dependent helicase ERCC6-like) (PLK1-interacting checkpoint helicase) (Tumor antigen BJ-HCC-15) (Q2NKX8)
Organism: Homo sapiens (Human)
Function: DNA helicase that acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. Functions as ATP-dependent DNA translocase. Can promote Holliday junction branch migration (in vitro).
Subcellular location: Chromosome, centromere {ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:17989990}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:17218258}. Chromosome {ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:17671160, ECO:0000269|PubMed:17989990}. Note=Localizes to kinetochores, inner centromeres and thin threads connecting separating chromosomes even during anaphase. In prometaphase cells, it mostly concentrates in between kinetochores. In metaphase, it localizes to numerous thin threads that stretch between sister kinetochores of the aligned chromosomes and are composed of catenated centromeric DNA. Evolution from inner centromeres to thin threads takes place in response to tension. Resolution of thin threads requires topoisomerase 2-alpha (TOP2A) after anaphase onset. {ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:17671160, ECO:0000269|PubMed:17956945, ECO:0000269|PubMed:17989990}.
Interaction partners:
- Serine/threonine-protein kinase PLK1
- RecQ-mediated genome instability protein 1
- DNA topoisomerase 3-alpha
- RecQ-like DNA helicase BLM
- Centromere protein I
- Mitotic spindle assembly checkpoint protein MAD2A
- BEN domain-containing protein 3
- Cyclin-dependent kinase 1
- Cell division cycle protein 20 homolog
- Exonuclease 1
Sequence:
MEASRRFPEAEALSPEQAAHYLRYVKEAKEATKNGDLEEAFKLFNLAKDIFPNEKVLSRIQKIQEALEELAEQGDDEFTDVCNSGLLLYRELHNQLFEHQKEGIAFLYSLYRDGRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTPGMRVKTFHGPSKDERTRNLNRIQQRNGVIITTYQMLINNWQQLSSFRGQEFVWDYVILDEAHKIKTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDFACQGSLLGTLKTFKMEYENPITRAREKDATPGEKALGFKISENLMAIIKPYFLRRTKEDVQKKKSSNPEARLNEKNPDVDAICEMPSLSRKNDLIIWIRLVPLQEEIYRKFVSLDHIKELLMETRSPLAELGVLKKLCDHPRLLSARACCLLNLGTFSAQDGNEGEDSPDVDHIDQVTDDTLMEESGKMIFLMDLLKRLRDEGHQTLVFSQSRQILNIIERLLKNRHFKTLRIDGTVTHLLEREKRINLFQQNKDYSVFLLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQAVDRVYRIGQKENVVVYRLITCGTVEEKIYRRQVFKDSLIRQTTGEKKNPFRYFSKQELRELFTIEDLQNSVTQLQLQSLHAAQRKSDIKLDEHIAYLQSLGIAGISDHDLMYTCDLSVKEELDVVEESHYIQQRVQKAQFLVEFESQNKEFLMEQQRTRNEGAWLREPVFPSSTKKKCPKLNKPQPQPSPLLSTHHTQEEDISSKMASVVIDDLPKEGEKQDLSSIKVNVTTLQDGKGTGSADSIATLPKGFGSVEELCTNSSLGMEKSFATKNEAVQKETLQEGPKQEALQEDPLESFNYVLSKSTKADIGPNLDQLKDDEILRHCNPWPIISITNESQNAESNVSIIEIADDLSASHSALQDAQASEAKLEEEPSASSPQYACDFNLFLEDSADNRQNFSSQSLEHVEKENSLCGSAPNSRAGFVHSKTCLSWEFSEKDDEPEEVVVKAKIRSKARRIVSDGEDEDDSFKDTSSINPFNTSLFQFSSVKQFDASTPKNDISPPGRFFSSQIPSSVNKSMNSRRSLASRRSLINMVLDHVEDMEERLDDSSEAKGPEDYPEEGVEESSGEASKYTEEDPSGETLSSENKSSWLMTSKPSALAQETSLGAPEPLSGEQLVGSPQDKAAEATNDYETLVKRGKELKECGKIQEALNCLVKALDIKSADPEVMLLTLSLYKQLNNN
Protein: Peroxisome assembly protein, putative (Q387S9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004585}.
Interaction partners:
- RING-type E3 ubiquitin transferase
- Peroxisome targeting signal 1 receptor
- Peroxisomal membrane protein PEX14
- Peroxin-13
- Peroxin 19
- Nonspecific lipid-transfer protein, putative
- propanoyl-CoA C-acyltransferase
- Peroxin-7
- Peroxisomal ATPase PEX1
- Peroxisomal ATPase PEX6
Sequence:
MIESNLLSQVNTASPLPTFMEVELVNSINTTVGKAFQFAHVFLAEKCDYLAALLPYNSEIWLVLHALLEHRLLFHADTSFAEMMFSLCRGTIISPSRPLPSQGRLSWLLRGPPPVPPLEARMMDTPAATDSRAVGEAMVGMKAGEIAAADRAPYGHLKFRPLTNRQKYITLFLLTVKPYLQQRLASWYEANKDAQVAGESQSGSALSRQTLGARLKQLALQLYPALHAGWEGLNLAFKILFLLELTPYTAPLHRIFSIVLRRPTGDDLIAASNPRAQAALMLGRVLIVVLLLGFRLMEFSGNTGGASPSHANSDDLAIPRPPEWGVDVVVPPGTPDPQPGVCPVCERPVTNAAVCTVSGVVGCYPCLTQFAREKNACPVTRAPMSLECVRRIYEC
Protein: SD04011p (Q960F5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNCFRDRSTTSSSSSQAQHAYVRGHSVTSSTLFRLEGSGGSNCTLDKAGKQDTGRPEAVVLLRELKTRPNKLALLKSSSSKDLTRLFLDDSTNTAVLVSNTSIDVCSSNSSSGGSPAVGRSKSGRDRRNGLECCSSCSKRWHDLKQRMHTLEQDLLVQTTYSQELEQKVGEMSRQLTELLQERDRERDKDKARFAAAGGVAAPGKRTAHGSPNVRPSRLVAWMNLSNWFKSRPSVETLREQRIFFDEPCFDTELEMVLKHDQHRTVPRIVVDCCDLIEQKYRRSTQPIEGIYRQCGDYNKIQTLRFSIDANDYDSLRQPDVDIHTLTGVLKLFLREIKSPLVSVNEAKTFIGQPNQWLLTDLSAKLDSLKRLIRSLPESNRDTMDYIFGHFNRITKVPLQQISAETLSISVTPSIFHTVPQGVHMQDIQQLLREGETLADCVKLMIEYQGRIFE
Protein: Lysophospholipase 2 (EC 3.1.1.5) (Phospholipase B 2) (Q8TG06)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Catalyzes the release of fatty acids from lysophospholipids (By similarity). Phospholipase B may well contribute to pathogenicity by abetting the fungus in damaging and traversing host cell membranes, processes which likely increase the rapidity of disseminated infection (By similarity).
Subcellular location: Secreted {ECO:0000305}. Secreted, cell wall {ECO:0000269|PubMed:18806209, ECO:0000269|PubMed:26546455}.
Interaction partners:
- Lysophospholipase NTE1
- Lysophospholipase 1
- Lysophospholipase
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Patatin-like phospholipase domain-containing protein
Sequence:
MQLSVLIASVLAAGAAVDAASYTPQNVSCPDNANFIRNAADGLSPAEKEWLKKRDPITRDALQTFLRRAFANVSTEITSALFNDTENVPKLGIAVAGGGYRAMFVGAGAFAAMDNRTDGANEHGLGGLLQAATYMAGLSGGNWLTGTLAYNNFTSVQQILEEGDKADAIWNITNSFLNPYDKDFSKTLARWTAIGSQVQGKRDAGFNVTITDLWSRALAYGWFPTLPNAGAGLTWSSLRDNEIFMNGEMPMPISVADGRYPGTTVINLNATVFEMTPFEIGSWDPSLNAFSDIKYLGTQVTDGKPETERCINGFDDASFIMGTSSSLFNEFTMSNDSAVAYTYLNTLSSTLVKGIDKENNDIAMYAPNPFKGSKYVDSNYTTSIVDSDSLFLVDGGEDLQGIPFVPLLKQERDLDIIFAIDVDTETSDNYPAGGPMMKTYERQFSKQGKGMAFPYVPDMTTFVNLGLGGKPSFYGCDANNLTDLEYIPPLIVYIPNSYHSFESNVSTFKLNYNYSERVGMIRNAFEATTRNNLTEDADYVTCVGCAIIRRKQQSLNLTLPDICDKCFTNYCWNGTIDNTPTKLLTPNNQDPAAISSAIAAVTDDSPIGALLNTGSGTKSNSSSKTNSTLVTSSRATSTGTLISNSSSNSTVSSTAARSSTSSTAKKNAGSVLKLEFSKSASVMVAIAAAAVASLI
Protein: Cytochrome P450 3A29 (EC 1.14.14.1) (CYPIIIA29) (P79401)
Organism: Sus scrofa (Pig)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 1A
- Cytochrome P450 family 1 subfamily A member 1
- Cytochrome P450 2C42
- Cytochrome P450 2E1
- Cytochrome P450 2C8 isoform a
- Cytochrome P450 family 2 subfamily B member 6B
- Cytochrome P450 7A1
- Cytochrome P450 family 4 subfamily A member 90
- Aromatase 3
- Cytochrome P450 2J2
Sequence:
MDLIPGFSTETWVLLATSLVLLYLYGTYSHGLFKKLGIPGPRPLPYFGNILGYRKGVDHFDKKCFQQYGKMWGVYDGRQPLLAVTDPNMIKSVLVKECYSVFTNRRSFGPLGAMRNALSLAEDEEWKRIRTLLSPTFTSGKLKEMFPIISHYGDLLVSNLRKEAEKGKPVTMKDIFGAYSMDVITSTAFGVNIDSLNNPQDPFVENSKKLLKFSFFDPFLLSLIFFPFLTPIFEVLNITLFPKSSVNFFTKSVKRMKESRLTDQQKRRVDLLQLMINSQNSKEMDPHKSLSNEELVAQGIIFIFAGYETTSSALSLLAYELATHPDVQQKLQEEIEATFPNKAPPTYDALAQMEYLDMVVNETLRLYPIAARLERACKKDVEIHGVFVPKGTVVVVPVFVLHRDPDLWPEPEEFRPERFSKKHKDTINPYTYLPFGTGPRNCIGMRFALMNMKLALVRVLQNFSFKPCKETQIPLKLTTQGLTQPEKPVVLKILPRDGTVSGA
Protein: Peptidyl-prolyl cis-trans isomerase FKBP35 (EC 5.2.1.8) (PfFKBP35) (Q8I4V8)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Has peptidylprolyl isomerase (PPIase) and co-chaperone activities. Assists protein folding by catalyzing the peptidyl conversion of cis and trans rotamers of the prolyl amide bond of protein substrates. Inhibits calcineurin phosphatase activity in vitro. Plays an essential role in merozoite egress from host erythrocytes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15850699}. Nucleus {ECO:0000269|PubMed:15850699}. Note=During the asexual blood stage, predominantly localizes to the cytoplasm of ring stage parasites and then translocates to the nucleus during the differentiation into trophozoites and schizonts. {ECO:0000269|PubMed:15850699}.
Interaction partners:
- HSP90 co-chaperone p23
- Glutamic acid-rich protein GARP
- Heat shock protein 90
- Heat shock protein 90, putative
- Endoplasmin, putative
Sequence:
MTTEQEFEKVELTADGGVIKTILKKGDEGEENIPKKGNEVTVHYVGKLESTGKVFDSSFDRNVPFKFHLEQGEVIKGWDICVSSMRKNEKCLVRIESMYGYGDEGCGESIPGNSVLLFEIELLSFREAKKSIYDYTDEEKVQSAFDIKEEGNEFFKKNEINEAIVKYKEALDFFIHTEEWDDQILLDKKKNIEISCNLNLATCYNKNKDYPKAIDHASKVLKIDKNNVKALYKLGVANMYFGFLEEAKENLYKAASLNPNNLDIRNSYELCVNKLKEARKKDKLTFGGMFDKGPLYEEKKNSAN
Protein: Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5) (Q784Z8)
Organism: Hepatitis B virus (HBV)
Subcellular location: Virion {ECO:0000256|HAMAP-Rule:MF_04076}. Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04076}.
Interaction partners:
Sequence:
MDIDPYKEFGASVELLSFLPSDFFPSIRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMNLATWVGSNLEDPASRELVVSYVNVNMGLKIRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC
Protein: Rhodopsin (P29403)
Organism: Xenopus laevis (African clawed frog)
Function: Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:26492040}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08100}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:22276148, ECO:0000269|PubMed:26492040}. Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia. {ECO:0000269|PubMed:22276148}.
Interaction partners:
Sequence:
MNGTEGPNFYVPMSNKTGVVRSPFDYPQYYLAEPWQYSALAAYMFLLILLGLPINFMTLFVTIQHKKLRTPLNYILLNLVFANHFMVLCGFTVTMYTSMHGYFIFGPTGCYIEGFFATLGGEVALWSLVVLAVERYIVVCKPMANFRFGENHAIMGVAFTWIMALSCAAPPLFGWSRYIPEGMQCSCGVDYYTLKPEVNNESFVIYMFIVHFTIPLIVIFFCYGRLLCTVKEAAAQQQESLTTQKAEKEVTRMVVIMVVFFLICWVPYAYVAFYIFTHQGSNFGPVFMTVPAFFAKSSAIYNPVIYIVLNKQFRNCLITTLCCGKNPFGDEDGSSAATSKTEASSVSSSQVSPA
Protein: Thioredoxin-like fold domain-containing protein MRL7L, chloroplastic (Protein MESOPHYLL-CELL RNAI LIBRARY LINE 7-LIKE) (AtMRL7-L) (Protein NUCLEAR CONTROL OF PEP ACTIVITY) (Protein SUPPRESSOR OF VARIEGATION 4-LIKE) (Q9SKB6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an essential role in early steps of chloroplast development. Involved in the regulation of plastid gene expression. Required for the proper function of the plastid transcriptional machinery and protein accumulation in thylakoid membranes. May function as molecular chaperone to ensure proper organization of the nucleoids in chloroplasts. Is a necessary component of phytochrome signaling for photosynthesis-associated plastid-encoded genes (PhAPGs) activation. Mediates the degradation of two repressors of chloroplast biogenesis, PIF1 and PIF3 in nucleus. Promotes the assembly of the plastid-encoded RNA polymerase (PEP) complex for PhAPG transcription in plastids.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:21515910, ECO:0000269|PubMed:24111559, ECO:0000269|PubMed:31201314}. Nucleus {ECO:0000269|PubMed:31201314}.
Interaction partners:
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 12, chloroplastic
- At1g36320/F7F23_4
- Protein CHLOROPLAST IMPORT APPARATUS 2
Sequence:
MILPFSTQFTCPVQDNGFSPSSLLSHCKRDRFEVTSLRYDSFGSVKTASSSKWNVMRSRRNVKAFGLVDKLGKKVWRKKEEDSDSEDEEDEVKEETFGGKEASLDDPVERREWRKTIREVIDKHPDIEEDEEIDMVEKRRKMQKLLADYPLVVNEEDPNWPEDADGWGFSFNQFFNKITIKNEKKEEEDDDEDSEGDDSEKEIVWQDDNYIRPIKDLTTAEWEEAVFKDISPLMVLVHNRYKRPKENEKFREELEKAIQVIWNCGLPSPRCVAVDAVVETDLVSALKVSVFPEIIFTKAGKILYREKGIRTADELSKIMAFFYYGAAKPPCLNGVVNSQEQIPLVDVSVN
Protein: Cutinase 2 (EC 3.1.1.74) (Cutin hydrolase 2) (P86012)
Organism: Colletotrichum kahawae (Coffee berry disease fungus)
Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:17043825}.
Interaction partners:
Sequence:
DINGGA
Protein: Acidic phospholipase A2 (MdumPLA2) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (C0HKB8)
Organism: Micrurus dumerilii (Coral snake)
Function: Snake venom phospholipase A2 (PLA2) that shows strong myotoxicity and induces edema in mice. Shows no cytotoxicity in vitro. Has a strong anticoagulant effect in vitro. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000269|PubMed:28315380}.
Interaction partners:
Sequence:
NLIDFKNMIKCTTKRSVLDFADYGCYCGSGGSGTPVDDLDRCCKVHDDCYGEAEKVHGCWPKWTLYSYDCSNGQLTCKDNNTKCKDFVCNCDRTAAICFAKAPYDDNNFMINNPRCQ
Protein: Meiotic coiled-coil protein 7 (Meiotically up-regulated gene 32 protein) (Q09739)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for meiotic recombination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Homologous-pairing protein 2
- Meiotic recombination protein dmc1
- DNA repair protein rhp51
- Proliferating cell nuclear antigen
- Protein byr4
- Folliculin-like protein bhd1
- Serine/threonine-protein kinase crk1
- Uncharacterized protein C30C2.07
- Cell division control protein 16
Sequence:
MPPKGLSLAEKRRRLEAIFHDSKDFFQLKEVEKLGSKKQIVLQTVKDVLQSLVDDNIVKTEKIGTSNYYWSFPSDAKRSRESVLGSLQAQLDDLKQKSKTLDENISFEKSKRDNEGTENDANQYTLELLHAKESELKLLKTQLSNLNHCNPETFELKNENTKKYMEAANLWTDQIHTLIAFCRDMGADTNQIREYCSIPEDLDDLQLPIL
Protein: Metal response element binding transcription factor 2, isoform CRA_c (cDNA FLJ50106, highly similar to Metal-response element-binding transcriptionfactor 2) (B4DZG1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVCTICQEEYSEAPNEMVICDKCGQGYHQLCHTPHIDSSVIDSDEKWLCRQCVFATTTKRGGALKKGPNAKALQVMKQTLPYSVADLEWDAGHKTNVQQCYCYCGGPGDWYLKMLQCCKCKQWFHEACVQCLQKPMLFGDRFYTFICSVCSSGPEYLKRLPLQWVDIAHLCLYNLSVIHKKKYFDSELELMTYINENWDRLHPGELADTPKSERYEHVLEALNDYKTMFMSGKEIKKKKHLFGLRIRVPPVPPNVAFKAEKEPEGTSHEFKIKGRKASKPISDSREVSNGIEKKGKKKSVGRPPGPYTRKMIQKTAEPLLDKESISENPTLDLPCSIGRTEGTAHSSNTSDVDFTGASSAKETTSSSISRHYGLSDSRKRTRTGRSWPAAIPHLRRRRGRLPRRALQTQNSEIVKDDEGKEDYQFDELNTEILNNLADQELQLNHLKNSITSYFGAAGRIACGEKYRVLARRVTLDGKVQYLVEWEGATAS
Protein: Protein crumbs homolog 3 (A0A5F4BST2)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Involved in the establishment of cell polarity in mammalian epithelial cells (By similarity). Regulates the morphogenesis of tight junctions (By similarity). Involved in promoting phosphorylation and cytoplasmic retention of transcriptional coactivators YAP1 and WWTR1/TAZ which leads to suppression of TGFB1-dependent transcription of target genes such as CCN2/CTGF, SERPINE1/PAI1, SNAI1/SNAIL1 and SMAD7 (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:12527193, ECO:0000269|PubMed:12771187}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000269|PubMed:12527193}. Note=Localizes primarily to the apical membrane with a small fraction in the upper part of tight junctions of epithelial cells. {ECO:0000250|UniProtKB:Q9BUF7}.
Interaction partners:
- Protein PALS1
- PATJ crumbs cell polarity complex component.
- Par-6 family cell polarity regulator gamma.
- Par-6 family cell polarity regulator alpha.
- Ubiquitin-protein ligase E3A
- Crumbs cell polarity complex component 2.
- Crumbs cell polarity complex component 1.
- Blood vessel epicardial substance.
Sequence:
MASPGLGLLLALGLPLLPARWGRAWGQTLDPHVNENGTITPSAPGSGSNGALSQEAITAIIVVFSLLAAVLLAVGLVLLLRKLREKRQTQGTYRPSSEEQFNHAAEARAPQDSKETVRGCLPI
Protein: Nucleolar GTP-binding protein 2 (Q57TY2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU364023}.
Interaction partners:
- Ribosome biogenesis protein NOP53
- Nucleolar GTP-binding protein 1
- Ribosome biogenesis protein NSA2 homolog
- 60S ribosomal protein L24, putative
- Eukaryotic translation initiation factor 6
- Pescadillo homolog
- Ribosome production factor 2 homolog
- Aminopeptidase, putative
- Ribosome assembly factor mrt4
- Protein SDA1
Sequence:
MGKPGKKAGKGLLAPTNVNRRVDPTKTSLRDQRTIKRLKMYTSKIVRDEKGHIVKGSVLKASDRVEQQMVRVAPDRRWFGNTRVIGQEALQKFRTEMGAKYRDPYSVVIKQSKLPLSLLTMTEKEEGSVRQLMEWEKTFGDKSNRKRIRLDTVDMEDFARKAESKNTEYLTHKKGTDRDLVKKSETERLDRSKNQGLLRKGQSNRIWNELYKVIDSSDVVLYVLDARDPLGTRSAYLEDYMRKEKKYKHFVFILNKCDLIPLWATARWLQVLSKDYPTVAFHASVNHPFGKGSVISLLRQFSKLQNVTHRGSSRTKTPISVGIIGYPNVGKSSLINTLRRKSVCKVAPIPGETKVWQYVALTRNIFLIDCPGVVYDRETNNDVQAVLKGVVRVERLGNADKTDVVNTVLDIVKPKDIAATYGISSWRDVNDFLEKLAKLRGKLVTGGEPDTEAAARMVLYDWQRGRIPWFSAPPFESNKHYRDTMGLSEAKHMKVIEHYSSFNIVDGVMDHKDEPYCSEDEEERPAEGVQGDATKRVEPKFSGKPPDPNTTVATFALRQEPTKKKGLRKKDLHEPSSISTEPGDGPNDDELWRRFLLAAQD
Protein: Calcium/calmodulin-dependent protein kinase type 1D (EC 2.7.11.17) (CaM kinase I delta) (CaM kinase ID) (CaM-KI delta) (CaMKI delta) (CaMKID) (CaMKI-like protein kinase) (CKLiK) (Q8IU85)
Organism: Homo sapiens (Human)
Function: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, activates CREB-dependent gene transcription, regulates calcium-mediated granulocyte function and respiratory burst and promotes basal dendritic growth of hippocampal neurons. In neutrophil cells, required for cytokine-induced proliferative responses and activation of the respiratory burst. Activates the transcription factor CREB1 in hippocampal neuron nuclei. May play a role in apoptosis of erythroleukemia cells. In vitro, phosphorylates transcription factor CREM isoform Beta.
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. Note=Predominantly cytoplasmic. Nuclear localization increases upon activation by KCl treatment in hippocampal neurons.
Interaction partners:
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 4
- Calmodulin-like protein 6
- Nitric oxide synthase 3
- Neuronal migration protein doublecortin
- Translation initiation factor eIF2 assembly protein
- Cyclic AMP-responsive element-binding protein 1
Sequence:
MARENGESSSSWKKQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTALNKNIHESVSAQIRKNFAKSKWRQAFNATAVVRHMRKLHLGSSLDSSNASVSSSLSLASQKDCLAPSTLCSFISSSSGVSGVGAERRPRPTTVTAVHSGSK
Protein: Protein E6 (P54667)
Organism: Human papillomavirus 68
Function: Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including BAK1, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006}.
Interaction partners:
Sequence:
MALFHNPEERPYKLPDLCRTLDTTLHDVTIDCVYCRRQLQRTEVYEFAFSDLCVVYRDGVPFAACQSCIKFYAKIRELRYYSESVYATTLETITNTKLYNLLIRCMSCLKPLCPAEKLRHLTTKRRLHKIAGNFTGQCRHCWTSKREDRRRIRQETQV
Protein: UPAR/Ly6 domain-containing protein qvr (Protein quiver) (Protein sleepless) (B5A5T4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excitability.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18635795}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18635795}; Extracellular side {ECO:0000269|PubMed:26828958}. Membrane raft {ECO:0000269|PubMed:21813698}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18635795}; Extracellular side {ECO:0000269|PubMed:26828958}.
Interaction partners:
- Potassium voltage-gated channel protein Shaker
- Adenosine deaminase-like protein
Sequence:
MWTQRNAVGNWLLVLTAVIGFLTFIWIPQTSAECQTRSIYCYECDSWTDARCKDPFNYTALPRDQPPLMTCNGCCVKMVRHQRSPYEVVRRMCTSQLQINLFMVDHVCMMESSGNGHMCFCEEDMCNSSKNLHTNGCQLHLIPIAVAVSWLMGQLLSR
Protein: Carene synthase 3, chloroplastic (PsTPS-3car3) (EC 4.2.3.107) ((+)-car-3-ene synthase 3) (3-carene cyclase 3) (F1CKI9)
Organism: Picea sitchensis (Sitka spruce) (Pinus sitchensis)
Function: Terpene synthase (TPS) involved in defensive oleoresin formation in conifers in response to insect attack or other injury.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
MSVISIVPLASKSCLYKSLMSSTHELKALCRPIATLGMCRRGKSVMASMSTSLTTAVSDDGVQRRIGHHHSNLWDDNFIQSLSSPYGASSYAESAKKLIGEVKEIFNSLSMAAGGLMSPVDDLLQHLSMVDNVERLGIDRHFQTEIKVSLDYVYSYWSEKGIGSGRDIVCTDLNTTALGFRILRLHGYTVFPDVFEHFKDQMGRIACSANHTERQISSILNLFRASLIAFPGEKVMEEAEIFSATYLKEALQTIPVSSLSQEIQYVLQYRWHSNLPRLEARTYIDILQENTKNQMLDVNTKKVLELAKLEFNIFHSLQQNELKSVSRWWKESGFPDLNFIRHRHVEFYTLVSGIDMEPKHSTFRLSFVKMCHLITVLDDMYDTFGTIDELRLFTAAVKRWDPSTTQCLPEYMKGVYTVLYETVNEMAQEAQKSQGRDTLNYVRQALEAYIGAYHKEAEWISSGYLPTFDEYFENGKVSSGHRIATLQPIFMLDIPFPHHVLQEIDFPSNFNDFACSILRLRCDTRCYQADRARGEEASCISCYMKDHPGSTQEDALNHINNMIEETIKKLNWELMKPDNNVPISSKKPAFDISRGLHHFYNYRDGYTVSSNETKNLVIKTVLEPVPM