wanglab/gogpt-training-data huggingface dataset:
Protein: Nitrogen regulatory protein P-II (P9WN31)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed (By similarity).
Interaction partners:
- Bifunctional uridylyltransferase/uridylyl-removing enzyme
- Ammonium transporter
- Glutamine synthetase
- Acetylglutamate kinase
- Glutamine synthetase
- Probable glutamine synthetase GlnA4
- Probable glutamine synthetase GlnA3
- Glutamate synthase large chain
- Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
- Sulfotransferase
Sequence:
MKLITAIVKPFTLDDVKTSLEDAGVLGMTVSEIQGYGRQKGHTEVYRGAEYSVDFVPKVRIEVVVDDSIVDKVVDSIVRAARTGKIGDGKVWVSPVDTIVRVRTGERGHDAL
Protein: DEAD-box ATP-dependent RNA helicase 8 (EC 3.6.4.13) (Q8RXK6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping.
Subcellular location: Cytoplasm, P-body {ECO:0000250}. Note=Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. {ECO:0000250}.
Interaction partners:
- Transcription regulator
- mRNA-decapping enzyme-like protein
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- mRNA-decapping enzyme subunit 2
- Protein GOLVEN 6
- Sm-like protein LSM7
- Sm-like protein LSM4
- Transcription regulator NOT2/NOT3/NOT5 family protein
- DEAD-box ATP-dependent RNA helicase 12
- Sm-like protein LSM1A
Sequence:
MNNRGRYPPGIGAGRGAFNPNPNYQSRSGYQQHPPPQYVQRGNYAQNHQQQFQQAPSQPHQYQQQQQQQQQWLRRGQIPGGNSNGDAVVEVEKTVQSEVIDPNSEDWKARLKLPAPDTRYRTEDVTATKGNEFEDYFLKRELLMGIYEKGFERPSPIQEESIPIALTGRDILARAKNGTGKTAAFCIPVLEKIDQDNNVIQAVIIVPTRELALQTSQVCKELGKHLKIQVMVTTGGTSLKDDIMRLYQPVHLLVGTPGRILDLTKKGVCVLKDCSVLVMDEADKLLSQEFQPSVEHLISFLPESRQILMFSATFPVTVKDFKDRFLTNPYVINLMDELTLKGITQFYAFVEERQKIHCLNTLFSKLQINQSIIFCNSVNRVELLAKKITELGYSCFYIHAKMLQDHRNRVFHDFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPKNAETYLHRVGRSGRFGHLGLAVNLITYEDRFNLYRIEQELGTEIKQIPPHIDQAIYCQ
Protein: Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag] (P04590)
Organism: Human immunodeficiency virus type 2 subtype A (isolate ROD) (HIV-2)
Function: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi).
Subcellular location: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000250|UniProtKB:P12493}.
Interaction partners:
Sequence:
MGARNSVLRGKKADELERIRLRPGGKKKYRLKHIVWAANKLDRFGLAESLLESKEGCQKILTVLDPMVPTGSENLKSLFNTVCVIWCIHAEEKVKDTEGAKQIVRRHLVAETGTAEKMPSTSRPTAPSSEKGGNYPVQHVGGNYTHIPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAAEWDVQHPIPGPLPAGQLREPRGSDIAGTTSTVEEQIQWMFRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDIKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLVQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLMAEALKEVIGPAPIPFAAAQQRKAFKCWNCGKEGHSARQCRAPRRQGCWKCGKPGHIMTNCPDRQAGFLGLGPWGKKPRNFPVAQVPQGLTPTAPPVDPAVDLLEKYMQQGKRQREQRERPYKEVTEDLLHLEQGETPYREPPTEDLLHLNSLFGKDQ
Protein: SNF1-related protein kinase regulatory subunit gamma-like PV42b (AtPV42b) (AKIN subunit gamma-like PV42b) (CBS domain-containing protein CBSX4) (Q8GXI9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays redundant role with PV42a in regulating male gametogenesis and pollen tube guidance.
Interaction partners:
- Sucrose nonfermenting 4-like protein
- AT1G27990 protein
- SNF1-related protein kinase regulatory subunit beta-3
- Reticulon-like protein B13
- CBS domain-containing protein CBSCBSPB3
- CBS domain-containing protein CBSX3
- Histone acetyltransferase type B catalytic subunit
- CBS domain-containing protein CBSX2, chloroplastic
- CBS domain-containing protein CBSX1, chloroplastic
- Late embryogenesis abundant protein
Sequence:
MQSYSRLMQFKVKDLMIDKRRLVEVPDNATLGDALNTMVANRVRAVPVAAKPGQWLGAGGSMIVELDKQSGSARKQYIGMVTMLDVVAHIAGDDGESGLDKKMAAPVSSIIGHCPEGLSLWSLNPNTSIMDCMEMLSKGIHRVLVPLDSNTENITGPELVESASAYAMLSQMDLISFFFDQSSQLHGILSHTVTDLSAIHNTVLALTSQARVKDAIQCMSIAMLNAVPIVEASGEGEDHKQLVDGKNRRVVGTFSASDLKGCHLATLRSWLPLNALEFVEKIPRTLLFTAATSTPGRELVTCHVTSTLAQVIHMVTTKRVHRVWVVDQNGGLQGLVSLTDIIAVVRSALLSGAPDLF
Protein: Cinnamoyl-CoA reductase 2 (Mt-CCR2) (EC 1.2.1.44) (Caffeoyl-CoA reductase) (EC 1.2.1.-) (Coumaroyl-CoA reductase) (Feruloyl-CoA reductase) (Sinapoyl-CoA reductase) (G7JEE5)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Involved in the latter stages of lignin biosynthesis. Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes. Mediates the conversion of caffeoyl-CoA and coumaroyl-CoA to caffaldehyde and coumaraldehyde, respectively. Also active, with a lower efficiency, toward feruloyl-CoA and sinapoyl-CoA. Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A0A059TC02}.
Interaction partners:
- Caffeoyl-CoA O-methyltransferase
- Caffeoyl-CoA-O-methyltransferase
- Trans-cinnamate 4-monooxygenase
- caffeoyl-CoA O-methyltransferase
- Caffeoyl-CoA 3-O-methyltransferase
- Caffeoyl-CoA 3-O-methyltransferase
- Caffeoyl-CoA 3-O-methyltransferase
- Caffeoyl-CoA 3-O-methyltransferase
- Trans-cinnamate 4-monooxygenase
- Caffeoyl-CoA 3-O-methyltransferase
Sequence:
MPAYDNTSSVSGGDQTVCVTGAGGFIASWLVKLLLERGYTVRGTVRNPEDPKNGHLKELEGARERLTLHKVDLLDLQSIQSVVHGCHGVFHTASPVTDNPDEMLEPAVNGTKNVIIASAEAKVRRVVFTSSIGTVYMDPNTSRDVVVDESYWSDLEHCKNTKNWYCYGKTVAEQSAWDIAKENQVDLVVVNPVVVLGPLLQPTINASTIHILKYLNGAAKTYVNATQSYVHVKDVALAHLLVYETNSASGRYICCETALHRGEVVEILAKYFPEYPLPTKCSDEKNPRVKPYKFSNQKLKDLGLEFTPVKQCLYDTVRSLQEKGHLPIPPMQEDSA
Protein: Cold-shock domain family protein (O53883)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MPTGKVKWYDPDKGFGFLSQEGGEDVYVRSSALPTGVEALKAGQRVEFGIASGRRGPQALSLRLIEPPPSLSRPRREPAAEHKHSPDELHGMVEDMITLLESTVQPELRKGRYPDRKTARRVAEVVRAVAREFES
Protein: Phospholipase C A (PLC-A) (EC 3.1.4.3) (MTP40 antigen) (Mycobacterial phospholipase C A) (P9WIB5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in virulence. Induces cytotoxic effects on mouse macrophage cell lines, via direct or indirect enzymatic hydrolysis of cell membrane phospholipids. Hydrolyzes phosphatidylcholine and sphingomyelin. Does not have hemolytic activity.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:20736081}. Note=Remains associated with the cell. {ECO:0000269|PubMed:11050656, ECO:0000269|PubMed:20736081, ECO:0000269|PubMed:8757862}.
Interaction partners:
- Phospholipase C B
- Phospholipase C C
- Phosphatidylinositol-3-phosphatase
- Phospholipase C D
- Diacylglycerol kinase
- Probable inositol 1-monophosphatase ImpA
- Phosphatidylserine decarboxylase proenzyme
- Inositol-1-monophosphatase SuhB
- Putative cardiolipin synthase
- Uncharacterized GMC-type oxidoreductase Rv1279
Sequence:
MSASPLLGMSRREFLTKLTGAGAAAFLMDWAAPVIEKAYGAGPCPGHLTDIEHIVLLMQENRSFDHYFGTLSSTNGFNAASPAFQQMGWNPMTQALDPAGVTIPFRLDTTRGPFLDGECVNDPEHQWVGMHLAWNGGANDNWLPAQATTRAGPYVPLTMGYYTRQDIPIHYLLADTFTICDGYHCSLLTGTLPNRLYWLSANIDPAGTDGGPQLVEPGFLPLQQFSWRIMPENLEDAGVSWKVYQNKGLGRFINTPISNNGLVQAFRQAADPRSNLARYGIAPTYPGDFAADVRANRLPKVSWLVPNILQSEHPALPVALGAVSMVTALRILLSNPAVWEKTALIVSYDENGGFFDHVTPPTAPPGTPGEFVTVPNIDAVPGSGGIRGPLGLGFRVPCIVISPYSRGPLMVSDTFDHTSQLKLIRARFGVPVPNMTAWRDGVVGDMTSAFNFATPPNSTRPNLSHPLLGALPKLPQCIPNVVLGTTDGALPSIPYRVPYPQVMPTQETTPVRGTPSGLCS
Protein: Btbd2 protein (Q14BP4)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MFNGGMATTSTEIELPDVEPAAFLALLKFLYSDEVQIGPETVMTTLYTAKKYAVPALEAHCVEFLKKHLRADNAFMLLTQARLFDEPQLASLCLESIDKNTADAIAAEGFTDIDLDTLVAVLERDTLGIREVRLFNAVVRWSEAECQRQQLQVTPENKRKVLGKALSLIRFPLMTIEEFAAGPAQSGILVDREVVSLFLHFTVNPKPRVEFIDRPRCCLRGKECSINRFQQVESRWGYSGTSDRIRFSVNKRIFVVGFGLYGSIHGPTDYQVNIQIIHTDSNTVLGQNDTGFSCDGSASTFRVMFKEPVEVLPNVNYTACATLKGPDSHYGTKGLRKVTHESPTTGAKTCFTFCYAAGNNNGTSVEDGQIPEVIFYT
Protein: Delta(14)-sterol reductase LBR (Delta-14-SR) (EC 1.3.1.70) (3-beta-hydroxysterol Delta (14)-reductase) (C-14 sterol reductase) (C14SR) (Integral nuclear envelope inner membrane protein) (LMN2R) (Lamin-B receptor) (Sterol C14-reductase) (Q14739)
Organism: Homo sapiens (Human)
Function: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis. Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:32694168, ECO:0000269|PubMed:8157662}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21327084}. Cytoplasm {ECO:0000269|PubMed:21327084}. Nucleus {ECO:0000269|PubMed:21327084}. Note=Nucleus; nuclear rim. {ECO:0000269|PubMed:21327084}.
Interaction partners:
- Lamin-B1
- Lamin-B2
- Lanosterol 14-alpha demethylase
- Methylsterol monooxygenase 1
- Methyl-CpG-binding protein 2
- Emerin
- Chromobox protein homolog 3
- Delta
- Lathosterol oxidase
- Inner nuclear membrane protein Man1
Sequence:
MPSRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKENDIKPLTSFRQRKGGSTSSSPSRRRGSRSRSRSRSPGRPPKSARRSASASHQADIKEARREVEVKLTPLILKPFGNSISRYNGEPEHIERNDAPHKNTQEKFSLSQESSYIATQYSLRPRREEVKLKEIDSKEEKYVAKELAVRTFEVTPIRAKDLEFGGVPGVFLIMFGLPVFLFLLLLMCKQKDPSLLNFPPPLPALYELWETRVFGVYLLWFLIQVLFYLLPIGKVVEGTPLIDGRRLKYRLNGFYAFILTSAVIGTSLFQGVEFHYVYSHFLQFALAATVFCVVLSVYLYMRSLKAPRNDLSPASSGNAVYDFFIGRELNPRIGTFDLKYFCELRPGLIGWVVINLVMLLAEMKIQDRAVPSLAMILVNSFQLLYVVDALWNEEALLTTMDIIHDGFGFMLAFGDLVWVPFIYSFQAFYLVSHPNEVSWPMASLIIVLKLCGYVIFRGANSQKNAFRKNPSDPKLAHLKTIHTSTGKNLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHILPYFYIIYFTMLLVHREARDEYHCKKKYGVAWEKYCQRVPYRIFPYIY
Protein: Tachykinin-like peptide-V (P.nigriventer tachykinin peptides V) (PnTkP-V) (U29-ctenitoxin-Pn1e) (U29-CNTX-Pn1e) (P86302)
Organism: Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer)
Subcellular location: Secreted {ECO:0000269|PubMed:15573368}.
Interaction partners:
Sequence:
QKKDKKDRF
Protein: Ubiquitin associated and SH3 domain containing, B (F1LV21)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGRRWTCSCPWASPAPAHKKLWHPREEEAFKQHVTGWLFSHVGDPFLDDPLPREYVLYLRPTGPLAQKLSDFWQQSKQICGKNKAHNIFPHITLCQFFMCEDSKVDALGEALQTTVSRWRCKFSAPLPLELYTSSNFIGLFVKEDSAEVLKKFAADFAAEAASKTEVHVEPHKKQLHVTLAYHFQASHLPTLEKLAQNIDVKLGCDWVATIFSRDIRFANHETLQVIYPYSPQNDDELELVPGDFIFMSPMEQTSTSEGWIYGTSLTTGCSGLLPENYITKADECSTWIFHGSCSILNTVSSSALAFGDGALERRQYEDQGLGETTPLTIICQPMQPLRVNSQPGPQKRCLFVCRHGERMDVVFGKYWLSQCFDAKGRYIRTNLNMPHSLPQRSGSFRDYEKDAPITVFGCMQARLVGEALLESNTVIDHVYCSPSLRCVQTAHNILKGLQQDNHLKIRVEPGLFEWTKWVAGSTLPAWMPPSELAAANLSVDTTYRPHIPVSKLVISESYDTYINRSFQVTKEIISECKSKGNNILIVAHASSLEACTCQLQGLSPQNSKDFVQMVRKIPYLGFCSCEELGETGIWQLTDPPILPLTHGPTGGFNWRETLLQE
Protein: HIVEP zinc finger 1 (A0A0D9SFF3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPRTKQIHPRNLRDKIEEAQKELNGAEVSKKEILQAGVKGTSESLKGVKRKKIVAENHLKKIPKSPLRNPLQAKHKQNTEESSFAVLHSASESHKKQNYIPVKNGKQFTKQNGETPGIIAEASKSEESVSPKKPLFLQQPSELRRWRSEGADPAKFSDLDEQCDSSSLSSKTRTDNSECISSHCGTTSPSYTNTAFDVLLKAMEPELSTLSQKGSPCAIKTEKLRPNKTARSPPKLKNSSMDAPNQTSQELVAESQSSCTSYTVHMSAAQKNEQGAMQSASHLYHQHEHFVPKSNQHNQQLPGCSGFTGSLTNLQNQENAKLEQVYNIAVTSSVGLTSPSSRSQVTPQNQQMDSASPLSISPANSTQSPPMPIYNSTHVASVVNQSVEQMCNLLLKDQKPKKQGKYICEYCNRACAKPSVLLKHIRSHTGERPYPCVTCGFSFKTKSNLYKHKKSHAHTIKLGLVLQPDAGGLFLSHESPKALSIHSDVEDSGESEEEGATDERQHDLGAMELQPVHIIKRMSNAETLLKSSFTPSSPENVIGDFLLQDRSAESQAVTELPKVVVHHVTVSPLRTDSPKAMDPKPELSSAQKQKDLQVTNVQPLSANMSQGGVSRLETNENSHQKGDMNPLEGKQDSHVGTVHAQLQRQQATDYSQEQQGKLLSPRSLGSTDSGYFSRSESADQTVSPPTPFARRLPSTEQDSGRSNGPSAALVTTSTPSALPTGEKALLLPGQMRPPLATKTLEERISKLISDNEALVDDKQLDSVKPRRTSLSRRGSIDSPKSYIFKDSFQFDLKPVGRRTSSSSDIPKSPFTPTEKSKQVFLLSVPSLDCLPITRSNSMPTTGYSAVPANIIPPPHPLRGSQSFDDKIGAFYDDVFVSGPNAPVPQSGHPRTLVRQAAIEDSSANESHVLGTGQSLDESHQGCHAAGEAMSVRSKALAQGPHIEKKKSHQGRGTMFECETCRNRYRKLENFENHKKFYCSELHGPKTKVAMREPEHSPVPGGLQPQILHYRVAGSSGIWEQTPQIRKRRKMKSVGDDEELQQNESGTSPKSSEGLQFQNALGCNPSLPKHNVTIRSDQQHKNIQLQNSHIHLVARGPEQTMDPKLSTIMEQQISSAAQDKIELQRHGTGISVIQHTNSLSRPNSFDKPEPFERASPVSFQELNRTGKSGSLKVIGISQEESHPSRDGSHPHQLALSDALRGELQESSRKSPSERHVLGQPSRLVRQHNIQVPEILVTEEPDRDLEAQCHDQEKSEKFSWPQRSETLSKLPTEKLPPKKKRLRLAEIEHSSTESSFDSTLSRSLSRESSLSHTSSFSASLDIEDVSKTEASPKIDFLNKAEFLMIPAGLNTLNVPGCHREMRRTASEQINCTQTSMEVSDLRSKSFDCGSITPPQTTPLTELQPPSSPSRVGVTGHVPLLERRRGPLVRQISLNIAPDSHLSPVHPTSFQNTALPSVNAVPYQGPQLTSTSLAEFSANTLHSQTQVKDLQAETSNSSSTNVFPVQQLCDINLLNQIHAPPSHQSTQLSLQVSTQGSKPDKNSVLSGSSKSEDCFAPKYQLHCQVFTSGPSCSSNPVHSLPNQVISDPVGTDHCVTSATLPTKLIDSMSNSHPLLPPELRPLGSQVQKVPSSFMLPIRLQSSVPAYCFATLTSLPQILVTQDLPNQPICQTNHSVVPISEEQNSVPTLQKGHQNALPNPEKEFLCENVFSEMSQNSSLSESLPITQKISVGRLSPQQESSASSKRMLSPANSLDIAMEKHQKRAKDENGAVCATDVRPLEALSSRVNEASKQKKPILVRQVCTTEPLDGVMLEKDVFSQPEISNEAVNLTNVLPADNSSTGCSKFVVIEPISELQEFENIKSSTSLTLTVRSSPAPSENTHISPLKCTDNNQERKSPGVKNQGDKVNIQEQSQQPVTSLSLFNIKDTQQLAFPSLKTTTNFTWCYLLRQKSLHLPQKDQKTSAYTDWTVSASNPNPLGLPTKVALALLNSKQNTGKSLYCQAITTHSKSDLLVYSSKWKSSLSKRALGNQKSTVVEFSNKDASEINSEQDKENSLIKSEPRRIKIFDGGYKSNEEYVYVRGRGRGKYICEECGIRCKKPSMLKKHIRTHTDVRPYHCTYCNFSFKTKDEKQRFSYERSGYDLEESDGPDEDDNENEDDDEDSQAESVLSATPSVTASPQHLPSRSSLQDPVSTDEDVRITDCFSGVHTDPMDVLPRALLTRMTVLSTAQSDYNRKTLSPGKARQRAARDENDTIPSVDTSRSPCHQMSVDYPESEEILRSSMAGKAVAITQSPSSVRLPPAAAEHSPQTAAGMPSVASPHPDPQEQKQQITLQPTPGLPSPHTHLFSHLPLHSQQQSRTPYNMVPVGGIHVVPAGLTYSTFVPLQAGPVQLTIPAVSVVHRTLGTHRNTVTEVSGTTNPAGVAELSSVVPCIPIGQIRVPGLQNLSTPGLQSLPSLSMETVNIVGLANTNMAPQVHPPGLALNAVGLQVLTANPSSQSSPAPQAHIPGLQILNIALPTLIPSVSQVAVDAQGAPEMPASQSKACETQPKQTSVASANQVSRTESPQGLPTVQRENAKKVLNPPAPAGDHARLDGLSKMDTEKAASANHVKPKPELTSIQGQPASTSQPLLKAHSEVFTKPSGQQTLSPDRQVPRPTALPRRQPTVHFSDVSSDDDEDRLVIAT
Protein: Kelch repeat and BTB domain-containing protein 8 (T-cell activation kelch repeat protein) (TA-KRP) (Q8NFY9)
Organism: Homo sapiens (Human)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification. The BCR(KBTBD8) complex acts by mediating monoubiquitination of NOLC1 and TCOF1: monoubiquitination promotes the formation of a NOLC1-TCOF1 complex that acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23578279}. Golgi apparatus {ECO:0000269|PubMed:23578279}. Note=Translocates to the spindle apparatus during mitosis. {ECO:0000269|PubMed:23578279}.
Interaction partners:
- Cullin-3
- Kelch repeat and BTB domain-containing protein 7
- Kelch-like protein 25
- Gigaxonin
- Kelch-like protein 12
- Kelch-like protein 9
- Ectoderm-neural cortex protein 1
- Kelch-like protein 3
- E3 ubiquitin-protein ligase RBX1
- Kelch-like protein 13
Sequence:
MAASADLSKSSPTPNGIPSSDPASDAMDPFHACSILKQLKTMYDEGQLTDIVVEVDHGKTFSCHRNVLAAISPYFRSMFTSGLTESTQKEVRIVGVEAESMDLVLNYAYTSRVILTEANVQALFTAASIFQIPSIQDQCAKYMISHLDPQNSIGVFIFADHYGHQELGDRSKEYIRKKFLCVTKEQEFLQLTKDQLISILDSDDLNVDREEHVYESIIRWFEHEQNEREVHLPEIFAKCIRFPLMEDTFIEKIPPQFAQAIAKSCVEKGPSNTNGCTQRLGMTASEMIICFDAAHKHSGKKQTVPCLDIVTGRVFKLCKPPNDLREVGILVSPDNDIYIAGGYRPSSSEVSIDHKAENDFWMYDHSTNRWLSKPSLLRARIGCKLVYCCGKMYAIGGRVYEGDGRNSLKSVECYDSRENCWTTVCAMPVAMEFHNAVEYKEKIYVLQGEFFLFYEPQKDYWGFLTPMTVPRIQGLAAVYKDSIYYIAGTCGNHQRMFTVEAYDIELNKWTRKKDFPCDQSINPYLKLVLFQNKLHLFVRATQVTVEEHVFRTSRKNSLYQYDDIADQWMKVYETPDRLWDLGRHFECAVAKLYPQCLQKVL
Protein: Adhesion G protein-coupled receptor E1 (Cell surface glycoprotein F4/80) (EGF-like module receptor 1) (EGF-like module-containing mucin-like hormone receptor-like 1) (EMR1 hormone receptor) (Q61549)
Organism: Mus musculus (Mouse)
Function: Orphan receptor involved in cell adhesion and probably in cell-cell interactions specifically involving cells of the immune system. May play a role in regulatory T-cells (Treg) development.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q14246}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Integrin alpha-M
- Macrophage colony-stimulating factor 1 receptor
- Receptor-type tyrosine-protein phosphatase C
- Low affinity immunoglobulin gamma Fc region receptor III
- Macrophage mannose receptor 1
- Integrin alpha-X
- Lymphocyte antigen 6G
- Macrosialin
- Sialic acid-binding Ig-like lectin 5
- Lymphocyte antigen 6C2
Sequence:
MWGFWLLLFWGFSGMYRWGMTTLPTLGQTLGGVNECQDTTTCPAYATCTDTTDSYYCTCKRGFLSSNGQTNFQGPGVECQDVNECLQSDSPCGPNSVCTNILGRAKCSCLRGFSSSTGKDWILGSLDNFLCADVDECLTIGICPKYSNCSNSVGSYSCTCQPGFVLNGSICEDEDECVTRDVCPEHATCHNTLGSYYCTCNSGLESSGGGPMFQGLDESCEDVDECSRNSTLCGPTFICINTLGSYSCSCPAGFSLPTFQILGHPADGNCTDIDECDDTCPLNSSCTNTIGSYFCTCHPGFASSNGQLNFKDLEVTCEDIDECTQDPLQCGLNSVCTNVPGSYICGCLPDFQMDPEGSQGYGNFNCKRILFKCKEDLILQSEQIQQCQAVQGRDLGYASFCTLVNATFTILDNTCENKSAPVSLQSAATSVSLVLEQATTWFELSKEETSTLGTILLETVESTMLAALLIPSGNASQMIQTEYLDIESKVINEECKENESINLAARGDKMNVGCFIIKESVSTGAPGVAFVSFAHMESVLNERFFEDGQSFRKLRMNSRVVGGTVTGEKKEDFSKPIIYTLQHIQPKQKSERPICVSWNTDVEDGRWTPSGCEIVEASETHTVCSCNRMANLAIIMASGELTMEFSLYIISHVGTVISLVCLALAIATFLLCRAVQNHNTYMHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFFWMLVEAVMLFLMVRNLKVVNYFSSRNIKMLHLCAFGYGLPVLVVIISASVQPRGYGMHNRCWLNTETGFIWSFLGPVCMIITINSVLLAWTLWVLRQKLCSVSSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTIINSLQGAFIFLIHCLLNRQVRDEYKKLLTRKTDLSSHSQTSGILLSSMPSTSKMG
Protein: Plastidial pyruvate kinase 2 (PKp2) (EC 2.7.1.40) (Plastidial pyruvate kinase 1) (PKP1) (Pyruvate kinase III) (Pyruvate kinase isozyme B1, chloroplastic) (PKP-BETA1) (Plastidic pyruvate kinase beta subunit 1) (Q9FLW9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for plastidial pyruvate kinase activity. Involved in seed oil accumulation, embryo development and seed storage compounds mobilization upon germination.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000269|PubMed:12953116}.
Interaction partners:
- L-lactate dehydrogenase
- Enolase 1, chloroplastic
- Cytosolic enolase 3
- Bifunctional enolase 2/transcriptional activator
- Pyruvate dehydrogenase E1 component subunit alpha-3, chloroplastic
- D-lactate dehydrogenase [cytochrome], mitochondrial
- Glucose-6-phosphate isomerase, cytosolic
- Inosine triphosphate pyrophosphatase
- Pyruvate dehydrogenase E1 component subunit beta-3, chloroplastic
- Malate dehydrogenase 3, cytoplasmic
Sequence:
MAQVVATRSIQGSMLSPNGGSVSTRSEKLLKPASFAVKVLGNEAKRSGRVSVRSRRVVDTTVRSARVETEVIPVSPEDVPNREEQLERLLEMQQFGDTSVGMWSKPTVRRKTKIVCTVGPSTNTREMIWKLAEAGMNVARMNMSHGDHASHKKVIDLVKEYNAQTKDNTIAIMLDTKGPEVRSGDLPQPIMLDPGQEFTFTIERGVSTPSCVSVNYDDFVNDVEAGDMLLVDGGMMSFMVKSKTKDSVKCEVVDGGELKSRRHLNVRGKSATLPSITEKDWEDIKFGVENKVDFYAVSFVKDAQVVHELKKYLQNSGADIHVIVKIESADSIPNLHSIITASDGAMVARGDLGAELPIEEVPILQEEIINLCRSMGKAVIVATNMLESMIVHPTPTRAEVSDIAIAVREGADAVMLSGETAHGKFPLKAAGVMHTVALRTEATITSGEMPPNLGQAFKNHMSEMFAYHATMMSNTLGTSTVVFTRTGFMAILLSHYRPSGTIYAFTNEKKIQQRLALYQGVCPIYMEFTDDAEETFANALATLLKQGMVKKGEEIAIVQSGTQPIWRSQSTHNIQVRKV
Protein: WD repeat protein (F4IA30)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSSMTEKEKERDPPPPHQEIEETTPLLENSQPESELRSTTAAAKVPEVEIHLYKCGKGPIDVFKSNLGGYEQDQLEVRSILEKYGLKAIFAFNVEKGRAVPIRFHPRNGRSVLPYRDGAVIYIDGEPQDSLLKPITRIILGVVIVTLLITFLLKDPPAWIKNNISIGTFPPWVLACIVIVFTRARKRTRDFFKKYGW
Protein: Ranatuerin-2AVa (P86161)
Organism: Rana arvalis (Moor frog)
Function: Has antibacterial activity against the Gram positive bacterium L.lactis.
Subcellular location: Secreted {ECO:0000269|PubMed:19308951, ECO:0000269|PubMed:35820801}.
Interaction partners:
Sequence:
GLLDVVKGAAKNLLASALDKLKCKVTGC
Protein: Interferon regulatory factor 2-binding protein 2-B (IRF-2-binding protein 2-B) (IRF-2BP2-B) (Q7T2G1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as a transcriptional repressor.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Interferon regulatory factor 2.
- Vestigial-like family member 4b.
- CBFA2/RUNX1 partner transcriptional co-repressor 3.
Sequence:
MSSAAVAASRRQSCYLCDLPRMPWAMIWDFTEPVCRGCVNYEGADRIEFVIETARQLKRAHGFQEGRSPGPVGKPGKDMQSINHAEPGSRPPQPLDRYPLTSDRPPRLGAEYQRQANGIPVPNGFPKPDEPPELNRQSPNPRRTGAIPPNLVPLVNGSMPPVHALNGRSVQMGIPPGALAEHVGKRADDMKDKHRADSMSDPSDGHKRVDEWTQKGKTVREMMTLQTLDSRFKKEHAALPHRMSYESSSGALKTDRGKHSRGIKRKTSPEPDGEGIAVKLNGEGQPWLPSPSEVLKMPSAALPGFAAAPPSTISPHSRTTPPEAATAVQNSQSPMAALILAADNAGTGSPKDAGNQVHSTTTSAAGRRNSGSPQSPSAGQRRPALGATGTAHIPGMDPQAGHPHSIPDSSVPPSSVPLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRESIKQQGATGEVYCPSGEKCPLVGSNVPWAFMQGEIATILAGDVKVKKERDP
Protein: Vimentin (P48674)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P08670}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus matrix {ECO:0000250|UniProtKB:P31000}.
Interaction partners:
Sequence:
MNRTTSRQTTSSSSYKRMFGGEGRPSVGMARSTLSSRQYSSPVRSSRMSYSVSAPPSIYASKNVRLRSSAPMPRLSSDTVDFALSDAINSEFKANRTNEKAEMQHLNDRFASYIDKVRFLEQQNKILLAELEQLKGKGASRIGDLYEDEMRDLRRQVDQLTNEKAHVEVDRDNMGEDIERLREKLQDEMIQKEEAEHNLQSFRQDVDNASLARLDLERKVESLQEEIIFLRKLHDEEVAELQAQIQDQHVQIDMDVAKPDLTAALRDVRVQYETLASRNLQDSEDWYKSKFADLSEAANRNTDAIRQAKQEANEYRRQVQALTCEVDSLKGTNESMERQMRELEESFGCEANNFQDTISRLEDDIRNMKDEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRITTPMPNFSSFNLRESMLEARPMIDNLSKKVVIKTIETRDGHVINESTQNHDDLE