wanglab/gogpt-training-data huggingface dataset:
Protein: Splicing factor proline and glutamine rich (Splicing factor proline/glutamine rich (Polypyrimidine tract binding protein associated)) (Q4KM71)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGGPKPPLPPPPPHQQQQQPPPQQPPPQQPPPHQQPPPHQPPHQQPPPPPQESKPVVPQGPGSAPGVSTAPPPAVSAPPANPPTTGAPPGPGPTPTPPPAVPSTAPGPPPPSTPSSGVSTTPPQTGGPPPPPAGGAGPGPKQGPGPGGPKGGKMPGGPKPGGGPGMGAPGGHPKPPHRGGGEPRGGRQHHAPYHQQHHQGPPPGGPGPRTEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHSQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGTMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF
Protein: Glucosylglycerol phosphorylase (GGoP) (EC 2.4.1.359) (2-O-alpha-D-glucopyranosylglycerol:phosphate alpha-D-glucosyltransferase) (2-O-alpha-D-glucosylglycerol phosphorylase (retaining)) (E4PMA5)
Organism: Marinobacter adhaerens (strain DSM 23420 / HP15)
Function: Catalyzes the reversible phosphorolysis of 2-O-alpha-D-glucosylglycerol with retention of the anomeric configuration, forming alpha-D-glucose 1-phosphate and glycerol. Has most likely a catabolic role, either regulating the intracellular levels of glucosylglycerol, which acts as a compatible solute, or degrading it when the environmental conditions change. Cannot catalyze the phosphorolysis of sucrose or glucosylglycerate.
Interaction partners:
- Amino acid transporter
- Glucosylglycerol-phosphate synthase
- Glycosyltransferase involved in cell wall biogenesis
- Mannosyl-3-phosphoglycerate phosphatase
Sequence:
MLLKNAVQLICYPDRIGNNLKDLYTVVDTHLSEAIGGLHILPFFPSNADGGFSPLTHKEVDPKVGTWDDIEAFTAKYDLCVDLTVNHISDESPEFTDFIANGFDSEYADLFVHVDKFGEISPDDMAKIHIRKEKEPFREVTLSDGTKTRVWCTFTEQQIDLNYESDLAYQLMESYIGFLTSKGVNLLRLDAFGYTTKRIGTSCFLVEPEVYQILDWVNQVALKHGAECLPEVHDHTSYQYAISRRNMHPYGFALPPLLLYSLLDANSTYLKNWLRMCPRNMVTVLDTHDGICIPDVEGVLPDEKIKVLIDNIDARSADPIMRRSAANIHSVGAIYQLTCTFYDALMQNDDAYIAARAIQFFTPGIPQVYYVGLLAGCNDHELMEQSGELRDINRHYYTLEEVEQDIQKPVVQRLLSLMKFRSNYPAFDGHFELNYSNNSSVAMAWRHGDYYCHLFVDLNFKTVKVTYTDVETGETRHLEC
Protein: Serine palmitoyltransferase 1 (Serine palmitoyltransferase-like protein (EC 2.3.1.50)) (Q6XFB3)
Organism: Leishmania major
Interaction partners:
- serine C-palmitoyltransferase
- 3-dehydrosphinganine reductase
- Inositol phosphosphingolipid phospholipase C-Like
- sphinganine-1-phosphate aldolase
- Phosphatidylinositol:ceramide inositolphosphotransferase
- Putative serine-threonine dehydratase
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
- cystathionine beta-synthase
- Uncharacterized protein
Sequence:
MSSLSETLSEPLMSRPFHRALELFVAAALAYFLLQRFHRRGRGKPPNPMSRLSAEEQERRIAAFQSIPFRAECSVTSNVPVPEYHGLTEVVGREGSHITIVRPGSSEAEECLDLATYDFHSFSTLPEVVEVARAAVNAYGVGSCGPRSFYGTIKPHLVVEQDLAKFLKTDDAVVYSFAYATVATLISCFSGRGDYLVYDDGVSSSVMEGCMLSRSDIRPYKHCSMTSLEERLQEVVAKDGYSKPHRRFVVTEGLFSDTGDICPLPQILGLCHKYRFRLLLEDSYGFGVLGKSGRGTPEQFDIPTMDVDVYIGSLSTSMGAVGGFCAGASRMIDHQRLTSTAYVFSASLPPYITASVSQSLAVLARDDTFVAKLRKHTKRMRRHLREAGFNAEKIKLVDSIDDASPVILLAVERAYVEREGLEKVESRLQRVINALQKKKVAVVRNVFTTDEPVNNVSGLRIVAKSLATEAEVTAALEAIETAVKAEFS
Protein: Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (E3 component of pyruvate complex) (P11959)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MVVGDFAIETETLVVGAGPGGYVAAIRAAQLGQKVTIVEKGNLGGVCLNVGCIPSKALISASHRYEQAKHSEEMGIKAENVTIDFAKVQEWKASVVKKLTGGVEGLLKGNKVEIVKGEAYFVDANTVRVVNGDSAQTYTFKNAIIATGSRPIELPNFKFSNRILDSTGALNLGEVPKSLVVIGGGYIGIELGTAYANFGTKVTILEGAGEILSGFEKQMAAIIKKRLKKKGVEVVTNALAKGAEEREDGVTVTYEANGETKTIDADYVLVTVGRRPNTDELGLEQIGIKMTNRGLIEVDQQCRTSVPNIFAIGDIVPGPALAHKASYEGKVAAEAIAGHPSAVDYVAIPAVVFSDPECASVGYFEQQAKDEGIDVIAAKFPFAANGRALALNDTDGFLKLVVRKEDGVIIGAQIIGPNASDMIAELGLAIEAGMTAEDIALTIHAHPTLGEIAMEAAEVALGTPIHIITK
Protein: Jabba, isoform B (LD47410p) (Q7K1Q6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAQETKTVATAKDQNQRDHIDEEEVIELHESRSFYDRVREQAERFASTRVGQFVIERADKALAMIEDTAKWSLPQDKSSAPLERPLPWAPFLMLIVLLRLTRIWLSVGALMIGNGPISPTDMVYFIQTRRRKLRAIRVHGLKVMRRRQQEVSYGSGKGMTQKLNQWFSRAMCRPGVQQDSSSRRVFVRHSEQGLSNFVVKRPREEDCNADADLTIDQMLAKYANENSEDDSDFVPNEEEEEEESSSSSGESESESGSSEGISSGEVDEVVSQPKQKSAGAVVENGVHKAEEKENDKGKLNITTTSNGNNDKEQADVGNGH
Protein: RING finger protein Z (Protein Z) (Zinc-binding protein) (Q6UY71)
Organism: Guanarito mammarenavirus (isolate Human/Venezuela/NH-95551/1990) (GTOV)
Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
Interaction partners:
Sequence:
MGNSKSKSNPSSSSESQKGAPTVTEFRRTAIHSLYGRYNCKCCWFADKNLIKCSDHYLCLRCLNVMLKNSDLCNICWEQLPTCITVPEEPSAPPE
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 4 (Q385S3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase 2A activator
Sequence:
MEYKSVFELRQHIADNVTPPKGRHRPPVSGCSGSSVESSPSSGYSGDAGMDAILDDPTALVCEVPGLDKLRALSVSLKNEEAVQNYVEARNLSVEEATRYIMNNGSTGQKKSLFQRLGDTLNGLEMTAMSQVLMIVVDFMWVQDPELQCFAPGALLGVLPLLSSSVVRELMMVTSTMLNVKTAEIRIAWNKLFLAFVDHLTAKQLDNDMVPLALKKAEHIEPQDQRELSCDLIGAVCHHLPRDIVERKLLNKVLALCQDTNVGVRRHMCQQLGTVARSLGVDKAKEKVAQELFELLNDEDQTVSRAAFSCLIDLVEFFGPAYRRERLYPIIRGFISHPPEEVVSLIVGEFGRFLWEIKADIQTSDDVAMFATFYQDAALKGDDHTRYRCAYNLPSVVASLPVDVFPTHLAPCCEALSTDVCESVCQSLASGLHELVKLIGDRAAEYLRKPFLNLLHSSKKSVLKALSGHTCVLLDCFSQQLKPADRTAFFSTIEDILLDLASRADRDWRIMEYVLNILCSYYKELNETSLHEKFLPVLLRYEKYGAYCLKNQCAEMCIKISAALCSVNSKVQFFSKLNNEYAHSPLASVRQGYLRFVRAACGEFSRRFIRERMLECCFELQHDNMEGVRLELARILPLLRKVLEPLTTGTVLDEYQDMVRRLQMDDSSEVRAVAVDSVDIIEARERELKRDAGKNKFEEESREDRRREMSEGQLLDVAKEYDKAERRSKLRDLLKSEREKEQAEATRKLGVGRRSMKPSSAQSQVKRPQQSPVRAPIAGPSRQKRH
Protein: Two-component response regulator ARR10 (Receiver-like protein 4) (O49397)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]GATT-3'. Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Could directly activate some type-A response regulators in response to cytokinins.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:12215502}.
Interaction partners:
- Histidine-containing phosphotransfer protein 3
- Ethylene-responsive transcription factor CRF6
- Histidine-containing phosphotransfer protein 5
- Pseudo histidine-containing phosphotransfer protein 6
- Histidine-containing phosphotransfer protein 2
- Histidine-containing phosphotransfer protein 4
- Histidine kinase 4
- Histidine kinase 2
- Histidine kinase 3
- Histidine-containing phosphotransfer protein 1
Sequence:
MTMEQEIEVLDQFPVGMRVLAVDDDQTCLRILQTLLQRCQYHVTTTNQAQTALELLRENKNKFDLVISDVDMPDMDGFKLLELVGLEMDLPVIMLSAHSDPKYVMKGVKHGACDYLLKPVRIEELKNIWQHVVRKSKLKKNKSNVSNGSGNCDKANRKRKEQYEEEEEEERGNDNDDPTAQKKPRVLWTHELHNKFLAAVDHLGVERAVPKKILDLMNVDKLTRENVASHLQKFRVALKKVSDDAIQQANRAAIDSHFMQMNSQKGLGGFYHHHRGIPVGSGQFHGGTTMMRHYSSNRNLGRLNSLGAGMFQPVSSSFPRNHNDGGNILQGLPLEELQINNNINRAFPSFTSQQNSPMVAPSNLLLLEGNPQSSSLPSNPGFSPHFEISKRLEHWSNAALSTNIPQSDVHSKPDTLEWNAFCDSASPLVNPNLDTNPASLCRNTGFGSTNAAQTDFFYPLQMNQQPANNSGPVTEAQLFRSSNPNEGLLMGQQKLQSGLMASDAGSLDDIVNSLMTQEQSQSDFSEGDWDLDGLAHSEHAYEKLHFPFSLSA
Protein: Polyketide cyclase/dehydrase and lipid transport superfamily protein (F4JYV3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- START
- Pleckstrin homology
- Protein ENHANCED DISEASE RESISTANCE 2-like
- ENHANCED DISEASE RESISTANCE protein
- Cell wall-plasma membrane linker protein
- START domain protein
- Homeobox-leucine zipper protein HDG8
- Homeobox-leucine zipper protein HDG12
- Putative homeodomain protein lipid-binding domain-containing protein)
- AT3G54800 protein
Sequence:
MALLESIILGLITGWLAFVIGLVIGWAWKPRWVSSSNNRQVKLQCSAPRSFDLSLPSSSPSSVVTSPLKGFGSAPCLKALVCDTWTMALRQQRQTVSPDSSSSSYDSSEQHLDLVSRVKKTKERLPNTVTELDLRHLVQLVERKDGGQAWIQMMDRFTPGMRYQAWLREPKNGPTEYRSRTVFEDATPVMLRDFFWDDEFRPTWDTMLSNSTTVEECPSTGTMIVRWIRKFPFFCSDREYVIGRRIWNCGNSYYCVTKGVSVPSIPPNNKQKRVDLFYSSWCIRPVESRRDDGVTSACEVLLFHHEDMGIPREIAKLGVKRGMWGAVKKMEPGLRAYQTHRLSDGGTKLSRSAFMAQINTKITQDHLISLSNGASPVTETPVTLNQGNRAANLKKLLIIGGAVAVVCSLSGGAFVPPAFLLGFGKRFVNGGRKRQLEGTTRSESQTTSS
Protein: Mannose-P-dolichol utilization defect 1 protein (Suppressor of Lec15 and Lec35 glycosylation mutation homolog) (SL15) (O75352)
Organism: Homo sapiens (Human)
Function: Required for normal utilization of mannose-dolichol phosphate (Dol-P-Man) in the synthesis of N-linked and O-linked oligosaccharides and GPI anchors.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dolichol-phosphate mannosyltransferase subunit 1
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyldiphosphatase 1
Sequence:
MAAEADGPLKRLLVPILLPEKCYDQLFVQWDLLHVPCLKILLSKGLGLGIVAGSLLVKLPQVFKILGAKSAEGLSLQSVMLELVALTGTMVYSITNNFPFSSWGEALFLMLQTITICFLVMHYRGQTVKGVAFLACYGLVLLVLLSPLTPLTVVTLLQASNVPAVVVGRLLQAATNYHNGHTGQLSAITVFLLFGGSLARIFTSIQETGDPLMAGTFVVSSLCNGLIAAQLLFYWNAKPPHKQKKAQ
Protein: Cofilin-1-B (ADF/cofilin-2) (XAC2) (P45593)
Organism: Xenopus laevis (African clawed frog)
Function: May play a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Required for formation of the cleavage furrow during cytokinesis.
Subcellular location: Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000269|PubMed:8603919}. Membrane {ECO:0000269|PubMed:8603919}. Note=Cellular localization varies throughout development and may be related to phosphorylation levels. Shows diffuse cortical cytoplasm localization in oocytes, with membrane-association increasing after fertilization, particularly in the vegetal hemisphere.
Interaction partners:
Sequence:
MASGVMVSDDVVKVFNDMKVRHQLSPEEAKKRKKAVIFCLSDDKKTIILEPGKEILQGDVGCNVEDPYKTFVKMLPRNDCRYALYDALYETKETKKEDLVFVFWAPEEASLKSKMIYASSKDAIRKRFTGIKHEWQTNTYDDINDPCNLADKLGGNTVVSLEGKSLRS
Protein: Sclareol synthase, chloroplastic (ScSCS) (SsSS) (EC 4.2.3.141) (Diterpene synthase 1132) (SsTps1132) (G8GJ94)
Organism: Salvia sclarea (Clary sage)
Function: Involved in the biosynthesis of labdane-type diterpenoid including sclareol, a diterpene-diol that is used as fragrance and flavoring, and has anticancer effects (able to kill leukemic and colon cancer cells by apoptosis) (Probable). Sclareol can also be used as synthesis precursor of ambergris substitution fragance products such as ambrox (Probable). Terpene synthase that catalyzes the conversion of 8-hydroxy-copalyl diphosphate to sclareol.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:22834731}.
Interaction partners:
Sequence:
MSLAFNVGVTPFSGQRVGSRKEKFPVQGFPVTTPNRSRLIVNCSLTTIDFMAKMKENFKREDDKFPTTTTLRSEDIPSNLCIIDTLQRLGVDQFFQYEINTILDNTFRLWQEKHKVIYGNVTTHAMAFRLLRVKGYEVSSEELAPYGNQEAVSQQTNDLPMIIELYRAANERIYEEERSLEKILAWTTIFLNKQVQDNSIPDKKLHKLVEFYLRNYKGITIRLGARRNLELYDMTYYQALKSTNRFSNLCNEDFLVFAKQDFDIHEAQNQKGLQQLQRWYADCRLDTLNFGRDVVIIANYLASLIIGDHAFDYVRLAFAKTSVLVTIMDDFFDCHGSSQECDKIIELVKEWKENPDAEYGSEELEILFMALYNTVNELAERARVEQGRSVKEFLVKLWVEILSAFKIELDTWSNGTQQSFDEYISSSWLSNGSRLTGLLTMQFVGVKLSDEMLMSEECTDLARHVCMVGRLLNDVCSSEREREENIAGKSYSILLATEKDGRKVSEDEAIAEINEMVEYHWRKVLQIVYKKESILPRRCKDVFLEMAKGTFYAYGINDELTSPQQSKEDMKSFVF
Protein: SRSF protein kinase 2 (EC 2.7.11.1) (SFRS protein kinase 2) (Serine/arginine-rich protein-specific kinase 2) (SR-protein-specific kinase 2) [Cleaved into: SRSF protein kinase 2 N-terminal; SRSF protein kinase 2 C-terminal] (O54781)
Organism: Mus musculus (Mouse)
Function: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression (By similarity). Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation (By similarity). Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 (By similarity). Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9446799}. Nucleus, nucleoplasm {ECO:0000269|PubMed:9446799}. Nucleus speckle {ECO:0000250|UniProtKB:P78362}. Chromosome {ECO:0000250|UniProtKB:P78362}. Note=Shuttles between the nucleus and the cytoplasm (By similarity). KAT5/TIP60 inhibits its nuclear translocation (By similarity). Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation (By similarity). Preferentially localizes across the entire gene coding region (By similarity). During transcription, accumulates at chromatin loci where unscheduled R-loops form and colocalizes with paused 'Ser-5'-phosphorylated POLR2A/RNA polymerase II and helicase DDX23 (By similarity). {ECO:0000250|UniProtKB:P78362}.
Interaction partners:
- Serine/arginine-rich splicing factor 1
- U1 small nuclear ribonucleoprotein 70 kDa
- Serine/arginine-rich splicing factor 6
- Splicing factor U2AF 65 kDa subunit
- Serine/arginine-rich splicing factor 2
- Serine/arginine-rich splicing factor 5
- Serine/arginine-rich splicing factor 4
- RNA-binding protein 39
Sequence:
MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPLPDPAPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKILEENITSAEASGEQDGEYQPEVTLKAADLEDTTEEETAKDNGEVEDQEEKEDAEKENAEKDEDDVEQELANLDPTWVESPKANGHIENGPFSLEQQLEDEEDDEDDCANPEEYNLDEPNAESDYTYSSSYEQFNGELPNGQHKTSEFPTPLFSGPLEPVACGSVISEGSPLTEQEESSPSHDRSRTVSASSTGDLPKTKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS
Protein: Nucleoprotein (Nucleocapsid protein) (NC) (Protein N) (P05991)
Organism: Porcine transmissible gastroenteritis coronavirus (strain FS772/70) (TGEV)
Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04095}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04095}. Host Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04095}. Host nucleus, host nucleolus {ECO:0000269|PubMed:11533198}. Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. {ECO:0000255|HAMAP-Rule:MF_04095}.
Interaction partners:
Sequence:
MANQGQRVSWGDESTKIRGRSNSRGRKSNNIPLSFFNPITLQQGSKFWNLCPRDFVPKGIGNRDQQIGYWNRQTRYRMVKGQRKELPERWFFYYLGTGPHADAKFKDKLDGVVWVAKDGAMNKPTTLGSRGANNESKALKFDGKVPGEFQLEVNQSRDNSRSRSQSRSRSRNRSQSRGRQQSNNKKDDSVEQAVLAALKKLGVDTEKQQQRSCSKSKERSNSKTRDTTPKNENKHTWKRTAGKGDVTRFYGARSSSANFGDSDLVANGSSAKHYPQLAECVPSVSSILFGSYWTSKEDGDQIEVTFTHKYHLPKDDPKTEQFLQQINAYARPSEVAKEQRKRKSRSKSAERSEQEVVPDALIENYTDVFDDTQVEMIDEVTN
Protein: Probable transmembrane reductase CYB561D1 (EC 7.2.1.3) (Cytochrome b561 domain-containing protein 1) (Q8N8Q1)
Organism: Homo sapiens (Human)
Function: Probable transmembrane reductase that may use ascorbate as an electron donor and transfer electrons across membranes to reduce monodehydro-L-ascorbate radical and iron cations Fe(3+) in another cellular compartment.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- BTB/POZ domain-containing protein KCTD21
Sequence:
MQPLEVGLVPAPAGEPRLTRWLRRGSGILAHLVALGFTIFLTALSRPGTSLFSWHPVFMALAFCLCMAEAILLFSPEHSLFFFCSRKARIRLHWAGQTLAILCAALGLGFIISSRTRSELPHLVSWHSWVGALTLLATAVQALCGLCLLCPRAARVSRVARLKLYHLTCGLVVYLMATVTVLLGMYSVWFQAQIKGAAWYLCLALPVYPALVIMHQISRSYLPRKKMEM
Protein: Protein COLD-REGULATED 15B, chloroplastic (AtCOR15B) (Q9SIN5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits cryoprotective activity toward stromal substrates in chloroplasts and in protoplasts and confers freezing tolerance to plants in a CBF-dependent manner. Protectant against various stresses (e.g. cold, drought and heat stress) by preventing protein aggregation and attenuating enzyme inactivation. Influences the intrinsic curvature of the inner membrane of the chloroplast envelope, and modulates the freeze-induced lamellar-to-hexagonal II phase transitions that occur in regions where the plasma membrane is brought into close apposition with the chloroplast envelope during freeze-induced osmotic contraction (By similarity). Mediates a shift in the melting curves of phospholipids-containing membranes to lower temperatures. Involved in the regulation of leaf senescence by abscisic acid (ABA) in a VNI2-dependent manner.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250|UniProtKB:Q42512}.
Interaction partners:
- Low-temperature-induced 78 kDa protein
- Dehydrin COR47
- Stress-induced protein KIN2
- Cold-regulated 413 plasma membrane protein 1
- Dehydration-responsive element-binding protein 1A
- Dehydrin ERD10
- Dehydration-responsive element-binding protein 1B
- At1g16880
- Low-temperature-induced 65 kDa protein
- Dehydration-responsive element-binding protein 1C
Sequence:
MAMSLSGAVLSGMGSSFHNVGAKQSGVGTVRVGRKSELVVVAQRKKSLIYAVKSDGNILDDLNEATKKASDFVTDKTKEALADGEKTKDYIVEKTIEANETATEEAKKALDYVTEKGKEAGNKAAEFVEGKAEEAKNATKS
Protein: G protein-coupled receptor 15-like (G protein-coupled receptor PGR15L) (Q80T54)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Insulin receptor substrate 4
- G-protein coupled receptor 83
- Insulin receptor substrate-3
- Insulin receptor substrate 1
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Insulin receptor substrate 2
- Inhibitor of nuclear factor kappa-B kinase subunit beta
Sequence:
MNTSFKGVSPFLSQMESAIDWLGENISWVPSIEDQSCNHTTQNGTNISSAEWGGPTGSVRRWLGGNPHIMAKIVLTFAYAVIIVISLFGNSLVCQVFVKHKEIKKSTGLLIFNLAISDILIILLNSPFALARFLSGQWVFGRIMCHVSRFAQYCSLHVSTLTLMAVAMDRHRVILHPMKPRLTHSQCLFVVAMIWSIAVFLALPHAIYQNLFTLVNMDGDTRSYCLPSFPGPSILVSKYVDLGTFILLYILPLLVIVVTYSHLGKRLWIQNAIGDASARQLMAHYQKRKKSIRMLILIVLVFAVCWFPLNFYVVLISSAGVENDSVLFYAFHWFAMSSTCYNPFIYCWLNRSFRAKLRSISSFRMQSLFVCSNSQVQQIKPQESHELRELQTSSLLRVPLAVPEPQVFEDPSLATGDNSQVSVQGEWEDPDPTLDEEPGPSTRDTYFCIHMQTSSH
Protein: Peroxin 3 (F4HYJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDFVRGFWRKHRRKVLVTAGCLGSGYLLYKLYNSHTRRLADLERELAHERENDEIIKTQMKAHFESIQMIVDSTTLPHAMQFLSIRISEEIDVSHVMDRLNQGKGMLSPPEKLQLWDELKILSFTRMVLSLWSVTMLSLYIRVQVNILGRHLYVDTARALGSSHLLCTLLISSPTSYFSGKLTGCSVKNFSRLPFKATAACPEEVDLIDRDDEQKFLSSADFLVTNAMPSLISDMQGSAEEVLKGKQLKDVITTRVLQETVMQIVDVFMSTGSPHHWVDYLMMPQDTKLSRTTSDSSDEAVSKFHQLMVETREVLISTEFTNIVEISLKCFTDVLVEEMETQTEAGGLATGKPLAKVLPQIEKTMNVITAEPSKNRFLQIIRDLPEVKLFFTLLYANMPQ
Protein: Probable CCR4-associated factor 1 homolog 11 (EC 3.1.13.4) (Q9FMS6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Transcription regulator
- Cell differentiation, Rcd1-like protein
- Cell differentiation, Rcd1-like protein
- Cell differentiation, Rcd1-like protein
- RNA binding
- RNA binding
- Carbon catabolite repressor protein 4 homolog 1
- Probable NOT transcription complex subunit VIP2
- Transcription regulator NOT2/NOT3/NOT5 family protein
- CCR4-NOT transcription complex subunit 11
Sequence:
MIKSEADLSDVIVIRDVWAYNLESEFDLIRGIVEDYPFISMDTEFPGVIYKADLDVLRRGNPNYLYNLLKSNVDALSLIQVGLTLSDADGNLPDLGGQKNRRYIWEFNFRDFDVERDPHAPDSIELLRRHGIDFERNRREGVESERFAELMMSSGLICNESVSWVTFHSAYDFGYLVKILTRRQLPVALREFLGLLRAFFGDRVYDVKHIMRFCEQRLYGGLDRVARSLEVNRAVGKCHQAGSDSLLTWQAFQRMRDLYFVEDGAEKHAGVLYGLEVF
Protein: Dynein heavy chain region D6 P-loop domain-containing protein (Q587E1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Rev7, putative
- Uncharacterized protein
- Non-specific serine/threonine protein kinase
- Cdc23 domain-containing protein
- Uncharacterized protein
- Cell division cycle protein, putative
- Uncharacterized protein
- Cell division cycle protein 16, putative
- Alanine--tRNA ligase
- separase
Sequence:
MFAYICATAQEFIGGVHFGPDNRVVSVNTSEYPSLSGIQCGMVLTSINGTRVGQSEEEKLRWKCAAGELMLVFNSRAPGQHDELDLSSAEEDENLLDSQKTLLSPNLECDEIVFGQRKSVDVLIDAVGRTGPGGCIIIMSEGVNPSYALTVAAEQSSRTTMYINAVARLKTRQPLTRAGEDFLKSLRKGLWIYIEQASKSMSLLYTLAESIEEARRSATIDANARVFLMCEPHPHFPEALLEGAVTLRSSLRPGTSEVMLEDNLLASEQKLRAVRGGSLVTSDGKAEITKVNARVKISHEVSIVPLEKNAFMELSRSATAPIEREAGREQGITRTARYTFGKNEKFISLCRVKDGCYAVGTLGGYVIMIDADGLPLIQFRPHKACIWDVAFASPHDFATACDDGASAILNYSLEAHEIRATSVASFQQEVFAVTYVTPDEPDSAVVSGGLSATICVLHSDRQVSSFISAGMTIQALRSTRQRHVIVGGGSGVCALIDPVASTILEESGRHKKKVPAVASYGALGVTGGFDKVVRLWDVRNGLRMVTEVAMPEVVTAVAAHGEHVAACCGSDLFVWDVRNLSRPLVRREKAWKDLTRGLVMCDNSIVTASADGVTRFWSLNATSE