wanglab/gogpt-training-data huggingface dataset:
Protein: Protein arginine N-methyltransferase (Q8ID96)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Voldacs domain-containing protein, putative
- Polyadenylation factor subunit 2, putative
- WD repeat-containing protein, putative
- non-specific serine/threonine protein kinase
- Gametocyte surface protein P230
- Histone H4
Sequence:
MTIKNKYGYLKLGIEIEYHKIPQCEENNIDPDFFACKLFNDNTKNIYNELTTNESLNNSSMINGNGKRCSYEIDPLFGNIYEDKNIWEKNIYGLMSTWINPDDENENSSLYSMDALNKELQWSTYISISKLIINVPNIKCDNYARYINSCINNYNMLSLIMRIPIVIKKKKPFHKESYNNNMTCDIINGWNLWAKFISYCNFNYSHLGLALELSNINNIDLSNIQLDVWKSEPVKLIIIPLDAFLLDTKTGYPYLPKKLKDFLIYFFRKNIEVLLITNEDINKMNNHFIHLKNEYCNEYQHNICNNEMDSYDINDNNNNNNNNYNISNSIHTKTNNNYYLKCCIYYIKRLFMSIENFDNDSLFDSFYWDYLQIPLQPLKDNLSSQTYEVFEKDRKKYEQYELATSKYLSNWKKGKKINNKNKQSNKNKNNNNNNNMEEQQNDHKITIFVVGAGRGPLVDTTLSALQKNEMTDYEIYAIEKNDSAIIILNNRVQTEEWKNVKVIHSDIRYLDIPKKADIIISELLGSFGDNELFPECMDGIKKFLKDDGISIPMNCVSYLEPISCSALYHKVMENNISGGNESFYVVNMYSYTKISQESSKECFFFQVPPIHTKQDNSHNYRYKNINFKIKMDTYIHGFLCYFKSQLYDDVYISIEPKTHTPNLHSWFPLYIPINKIQFLKKGQNLSFSIWRLTDHQKIWYEWCINEPITTSIHNYNARYFSIGR
Protein: Uncharacterized hydrolase YOR131C (EC 3.-.-.-) (Q12486)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Histidine biosynthesis trifunctional protein
- Histidinol-phosphate aminotransferase
- Imidazole glycerol phosphate synthase hisHF
- Alanine--glyoxylate aminotransferase 1
- Ribulose-phosphate 3-epimerase
- mRNA 3'-end-processing protein RNA14
Sequence:
MTKLQGLQGLKHIKAVVFDMDGTLCLPQPWMFPAMRNAIGLEDKSIDILHFIDTLPTEKEKKEAHDRIELVEAKAMKEMQPQPGLVDIMRYLTKNGISKNICTRNVGAPVETFVKRFIPSELSRFDYIVTREFRPTKPQPDPLLHIASKLNIRPLEMIMVGDSFDDMKSGRSAGCFTVLLKNHVNGHLLLEHKELVDVSVEDLSEIIELIQNMNKESF
Protein: Thromboxane A2 receptor (Prostanoid TP receptor) (D0EXE3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MHHANSSGAVPLNPFSNRSQWEGQAGSLSLADPSNVTSSRPILSGPIAAMLSMTLGILSNIVALLIPANAYARLRRRSKAFLLFAGSLVATDFVGHVIPGAIVMRLYLSGGVPAEEYNRADPLCQFLGGSMVFFGLCPLFLGCAMAAERCLGVTKPLLHASLVTTTRTKLSLSVIWLAALCVALLPCFQLGSYTYQYPGTWCFIKVLEDAEKADMAFVMLFSGLGLTSLAVALVCNTISGLTLVLGRIRKKPCNRRSARSHDIEMVVQLVGIMVTSCICWSPLLIVGLITVKQSYEHSIGDDLATYKTLMIMGVRIASWNQILDPWVYILLRRSVLQKIYFITKRQTDLKESTLRCWEIHSFPSSEKNPVSRV
Protein: Trans-2-enoyl-CoA reductase (TER1) (EC 1.3.1.38) (EC 1.3.1.44) (EC 1.3.1.86) (Q5EU90)
Organism: Euglena gracilis
Function: Catalyzes reduction of trans-2-enoyl-CoA to acyl-CoA, an important step in the fatty acid biosynthesis pathway, which is performed in mitochondria under anaerobiosis. Preferably catalyzes the reduction of short chain length substrates such as crotonyl-CoA ((2E)-butenoyl-CoA) and (2E)-hexenoyl-CoA. Can use both NADH and NADPH as electron donor, with 2-3-fold higher specific activities for NADH relative to NADPH. Originally thought to contribute to wax ester production under anaerobic conditions. Later shown to be dispensable for wax ester production under anaerobic conditions, but involved in the greening process (chlorophyll synthesis and/or chloroplast development).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15569691, ECO:0000269|PubMed:30650145}.
Interaction partners:
Sequence:
MSCPASPSAAVVSAGALCLCVATVLLATGSNPTALSTASTRSPTSLVRGVDRGLMRPTTAAALTTMREVPQMAEGFSGEATSAWAAAGPQWAAPLVAAASSALALWWWAARRSVRRPLAALAELPTAVTHLAPPMAMFTTTAKVIQPKIRGFICTTTHPIGCEKRVQEEIAYARAHPPTSPGPKRVLVIGCSTGYGLSTRITAAFGYQAATLGVFLAGPPTKGRPAAAGWYNTVAFEKAALEAGLYARSLNGDAFDSTTKARTVEAIKRDLGTVDLVVYSIAAPKRTDPATGVLHKACLKPIGATYTNRTVNTDKAEVTDVSIEPASPEEIADTVKVMGGEDWELWIQALSEAGVLAEGAKTVAYSYIGPEMTWPVYWSGTIGEAKKDVEKAAKRITQQYGCPAYPVVAKALVTQASSAIPVVPLYICLLYRVMKEKGTHEGCIEQMVRLLTTKLYPENGAPIVDEAGRVRVDDWEMAEDVQQAVKDLWSQVSTANLKDISDFAGYQTEFLRLFGFGIDGVDYDQPVDVEADLPSAAQQ
Protein: HCG1643967 (Hypothetical FLJ23584) (cDNA: FLJ23584 fis, clone LNG14307) (Q9H5C5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNPVPHWGEVFLLVGGEGEHLASQGTTPARDHRVGISPASQQAQPESWRRRQRDKGVDPEKAPSLTRQSQNPPSLTAPLGMPSACSCLPCGPAPEAAIILAGPPTALTVLPKGTGLKKSKRLLLESLMRRRIAHLKWGLPRRILESYFLFNFLGSCSLTLAGARLSGLNTGQELQAQQERYCEAQGSPPGLKSPERFQRVQRPDRKSSKLPIQARALERNRPHMSEPIKHFHPA
Protein: Radical SAM core domain-containing protein (Q92KK9)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Interaction partners:
Sequence:
MNDLSQLKQGVYAPGNSVDVAEALVAGSGIRIDVDRRRGRGAALNISGRFEQKSREVFDDGWQTLEELPPFKTEVQIEKPKTAITRNESPDISFDRSINPYRGCEHGCIYCFARPTHAYMGLSAGLDFEAKLFAKPDAPRLLERELAKPDYKLRPIAIGTNTDPYQPIEKEWRIMRQILEVLKEANHPVMIVTKSAMVTRDIDLLAPMAEKGLARVGISVTTLDRKLARSMEPRASTPTKRLEALRAISEAGIPAGVLVAPIIPALNDHEIERVLDSAKSAGASDASYVLLRLPLEVSPLFRDWLLRNYPDRYRHVMSLIRSMRCGKDYDAEFGKRMKGSGPYAWQIGRRFELAAKRLGLNLTRRQLRSDLFVPPLGMGVQLSLL
Protein: Somatostatin receptor type 2 (SS-2-R) (SS2-R) (SS2R) (SST2) (SRIF-1) (P30874)
Organism: Homo sapiens (Human)
Function: Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and PLC via pertussis toxin insensitive as well as sensitive G proteins. Inhibits calcium entry by suppressing voltage-dependent calcium channels. Acts as the functionally dominant somatostatin receptor in pancreatic alpha- and beta-cells where it mediates the inhibitory effect of somatostatin-14 on hormone secretion. Inhibits cell growth through enhancement of MAPK1 and MAPK2 phosphorylation and subsequent up-regulation of CDKN1B. Stimulates neuronal migration and axon outgrowth and may participate in neuron development and maturation during brain development. Mediates negative regulation of insulin receptor signaling through PTPN6. Inactivates SSTR3 receptor function following heterodimerization.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cytoplasm. Note=Located mainly at the cell surface under basal conditions. Agonist stimulation results in internalization to the cytoplasm.
Interaction partners:
- Somatostatin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Cortistatin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- D
- Guanine nucleotide-binding protein G
- Appetite-regulating hormone
Sequence:
MDMADEPLNGSHTWLSIPFDLNGSVVSTNTSNQTEPYYDLTSNAVLTFIYFVVCIIGLCGNTLVIYVILRYAKMKTITNIYILNLAIADELFMLGLPFLAMQVALVHWPFGKAICRVVMTVDGINQFTSIFCLTVMSIDRYLAVVHPIKSAKWRRPRTAKMITMAVWGVSLLVILPIMIYAGLRSNQWGRSSCTINWPGESGAWYTGFIIYTFILGFLVPLTIICLCYLFIIIKVKSSGIRVGSSKRKKSEKKVTRMVSIVVAVFIFCWLPFYIFNVSSVSMAISPTPALKGMFDFVVVLTYANSCANPILYAFLSDNFKKSFQNVLCLVKVSGTDDGERSDSKQDKSRLNETTETQRTLLNGDLQTSI
Protein: Bradykinin-releasing enzyme KR-E-1 (Snake venom serine protease) (SVSP) (Thrombin-like enzyme defibrase) (EC 3.4.21.-) (Q7SZE2)
Organism: Gloydius ussuriensis (Ussuri mamushi) (Gloydius blomhoffii ussuriensis)
Function: Bradykinin-releasing enzyme. Releases bradykinin from bovine HMW kininogen. Has anticoagulant activity. Increases permeability of capillaries by intradermal injection into rabbits.
Subcellular location: Secreted.
Interaction partners:
Sequence:
VIGGDECNINEHRSLVAFFNSTGFFCSGTLVNEEWVLSAAHCDSTNFQMKLGVHSKKVLNEDEQTRNPKEKFICPNKKNDEVLDKDIMLIKLDSRVSNSEHIAPLSLPSSPPSVGSVCHIMGWGSITPIKETYPDVPYCANINLLDDEVCQAGYPELLAEYRTLCAGILEGGKDTCGGDSGGPLICNGQFQGIVSYGAHPCGQSLKPGIYTKVFDYSDWIQSIIAGNTDASCPP
Protein: Septum site-determining protein MinC (Q01463)
Organism: Bacillus subtilis (strain 168)
Function: Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. The MinCD complex plays an important role in asymmetric septum formation during sporulation of B.subtilis cells.
Interaction partners:
- Septum site-determining protein MinD
- Cell division protein FtsZ
- Cell division topological determinant MinJ
- Rod shape-determining protein MreD
- Septum site-determining protein DivIVA
- Cell shape-determining protein MreC
- Cell shape-determining protein MreB
- Cell division protein SepF
- Cell division protein FtsA
- Cell division protein ZapA
Sequence:
MKTKKQQYVTIKGTKNGLTLHLDDACSFDELLDGLQNMLSIEQYTDGKGQKISVHVKLGNRFLYKEQEEQLTELIASKKDLFVHSIDSEVITKKEAQQIREEAEIISVSKIVRSGQVLQVKGDLLLIGDVNPGGTVRAGGNIFVLGSLKGIAHAGFNGNNQAVIAASEMLPTQLRINHVLNRSPDHIQKGNEMECAYLDTDGNMVIERLQHLAHLRPDLTRLEGGM
Protein: ZNF248 protein (Q05CR2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNKSQEQVSFKDVCVDFTQEEWYLVDPAQKILYRDVILENYSNLVSVGYCITKPEVIFKIEQGEEPWILEKGFPSQCHPERKWKVDDVLESSQENEDDHFWELLFHNNKTH
Protein: Matrix metalloproteinase-14 (MMP-14) (EC 3.4.24.80) (Membrane-type matrix metalloproteinase 1) (MT-MMP 1) (MTMMP1) (Membrane-type-1 matrix metalloproteinase) (MT-MMP) (MT1-MMP) (MT1MMP) (Q10739)
Organism: Rattus norvegicus (Rat)
Function: Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15 in association with pro-MMP2. Involved in the formation of the fibrovascular tissues in association with pro-MMP2. Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P50281}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P50281}. Melanosome {ECO:0000250|UniProtKB:P50281}. Cytoplasm {ECO:0000250|UniProtKB:P50281}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Forms a complex with BST2 and localizes to the cytoplasm. {ECO:0000250|UniProtKB:P50281}.
Interaction partners:
- Metalloproteinase inhibitor 2
- Metalloproteinase inhibitor 1
- 72 kDa type IV collagenase
- Proheparin-binding EGF-like growth factor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Decorin
- Acireductone dioxygenase-requiring))
- Metalloproteinase inhibitor 3
Sequence:
MSPAPRPSRSLLLPLLTLGTTLASLGWAQSSNFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQRFYGLQVTGKADSDTMKAMRRPRCGVPDKFGTEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMILFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVQNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGSKSGSPTKMPPQPRTTSRPSVPDKPRNPTYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEEFRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGSGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPKRLLYCQRSLLDKV
Protein: 4-nitrophenylphosphatase (PNPPase) (EC 3.1.3.41) (G8BCM7)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
Sequence:
MSVKITEKSQVQNLILDKYDYFLFDCDGVLWLGDHLLPSIGEALDYLKQQNKTVIFVTNNSTKSRTDYLSKFNKMGISNITKSEIFGSSFASAVYVEKILKLPKDKKVWVLGEEGIEKELHELGYSTVGGTDPKLVKEGVKFDPNTTLFDNLDPNVGCVVCGLTFNINYLKLSLTMQYLLKDNKSIPFIATNIDSTFPMKGKLLIGAGSIIETVAYASGRQPDAICGKPNQSMMNSIKAQLPGLEKNPKKGLMIGDRLNTDMKFGRDGGLDTMLVLTGIETESNVKQLSKEDAPTYYIEKLGDIYEFTH
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (H7BYJ1)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MKAGATSMWASCCGLLNEVMGTGAVRGQQSAFAGATGPFRFTPNPEFSTYPPAATEGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSVCSVLQENLRRCSTCHLLQETAFQRPQLMRLKVKDLRQYLILRNIPIDTCREKEDLVDLVLCHHGLGSEDDMDTSSLNSSRSQTSSFFTRSFFSNYTAPSATMSSFQGELMDGDQTSRSGVPAQVQSEITSANTEDDDDDDDEDDDDEEENAEDRNPGLSKERVRASLSDLSSLDDVEGMSVRQLKEILARNFVNYSGCCEKWELVEKVNRLYKENEENQKSYGERLQLQDEEDDSLCRICMDAVIDCVLLECGHMVTCTKCGKRMRMSSCKGRLRNGPESSAVTIQKDQRKVSAHSSPKRVVEQLLPWKDLQNGIALWSVVPRSKWKIKALIFVKSLPSQSPPRIYILILGLTQFLQEFFFYLPKLDTHRHLGYELLTAFLGDLLAVPQVNMTDVSTAFEEGQALISDLIAVCREEIVM
Protein: Jasmonate-induced oxygenase 4 (EC 1.14.11.-) (2-oxoglutarate-dependent dioxygenase JOX4) (Anthocyanidin synthase) (Jasmonic acid oxidase 4) (O80449)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 2-oxoglutarate-dependent dioxygenase involved in the oxidation of jasmonate (JA), a stress-induced phytohormone synthesized in response to attack by pathogens and herbivores, which triggers the activation of defense responses via the JA-mediated signaling pathway. Converts JA to 12-hydroxyjasmonate (12OH-JA), an inactive form of JA. Is specific to free JA, and cannot oxidize the bioactive form jasmonoyl-L-isoleucine (JA-Ile) or other JA-amino acid conjugates. Prevents over-accumulation of JA and indirectly its bioactive form JA-Ile under stress response. Acts as negative regulator of JA-mediated defense signaling, by contributing to 12OH-JA accumulation, which represses JA defense responses upon infection by the fungal pathogen Botrytis cinerea. Acts as negative regulator of JA-mediated defense responses upon infestation by the herbivorous caterpillar Mamestra brassicae.
Interaction partners:
- Dihydroflavonol 4-reductase
- Chalcone synthase
- Flavonoid 3'-monooxygenase
- Anthocyanidin 3-O-glucoside 2'''-O-xylosyltransferase
- Anthocyanidin reductase
- Phenylalanine ammonia-lyase 1
- Trans-cinnamate 4-monooxygenase
- Phenylalanine ammonia-lyase 3
- Phenylalanine ammonia-lyase 2
- Phenylalanine ammonia-lyase 4
Sequence:
MATCWPEPIVSVQSLSQTGVPTVPNRYVKPAHQRPVFNTTQSDAGIEIPVLDMNDVWGKPEGLRLVRSACEEWGFFQMVNHGVTHSLMERVRGAWREFFELPLEEKRKYANSPDTYEGYGSRLGVVKDAKLDWSDYFFLNYLPSSIRNPSKWPSQPPKIRELIEKYGEEVRKLCERLTETLSESLGLKPNKLMQALGGGDKVGASLRTNFYPKCPQPQLTLGLSSHSDPGGITILLPDEKVAGLQVRRGDGWVTIKSVPNALIVNIGDQLQILSNGIYKSVEHQVIVNSGMERVSLAFFYNPRSDIPVGPIEELVTANRPALYKPIRFDEYRSLIRQKGPCGKNQVDSLLLTR
Protein: Inactive serine/threonine-protein kinase PLK5 (Polo-like kinase 5) (PLK-5) (Q496M5)
Organism: Homo sapiens (Human)
Function: Inactive serine/threonine-protein kinase that plays a role in cell cycle progression and neuronal differentiation.
Subcellular location: Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:21245385}.
Interaction partners:
- Separin
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein kinase PLK4
Sequence:
MYTVLTGTPPFMASPLSEMYQNIREGHYPEPAHLSANARRLIVHLLAPNPAERPSLDHLLQDDFFTQGFTPDRLPAHSCHSPPIFAIPPPLGRIFRKVGQRLLTQCRPPCPFTPKEASGPGEGGPDPDSMEWDGESSLSAKEVPCLEGPIHLVAQGTLQSDLAGPEGSRRPEVEAALRHLQLCLDVGPPATQDPLGEQQPILWAPKWVDYSSKYGFGYQLLDGGRTGRHPHGPATPRREGTLPTPVPPAGPGLCLLRFLASEHALLLLFSNGMVQVSFSGVPAQLVLSGEGEGLQLTLWEQGSPGTSYSLDVPRSHGCAPTTGQHLHHALRMLQSI
Protein: Nsp1_C domain-containing protein (O01576)
Organism: Caenorhabditis elegans
Interaction partners:
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein 5
- Nucleoporin Nup54 alpha-helical domain-containing protein
- Nucleoporin NUP35
- Nuclear Pore complex Protein
- Nuclear Pore complex Protein
- Nuclear pore protein
- Nuclear pore complex protein 14
- Nucleoporin SEH1
- Nuclear pore complex protein 15
Sequence:
MFGGSAPKPSIFGGTAATTTASSGFSFGNSSTSTANTGGNTNTTGGFSFGSAQPSTGSTGLFGNSTATGSMFGGSSAAAPAPASAGIFGNSGAAAPAPASTSIFGSSANSAAPATVTFGASAPSAGAGMFGANKPAAPTGGLFGSSTSTATTAPTGGLFGSSTAAPSSGLFGSTAAPAAPGGLFGSTSTSTAAPSGGLFGSSAAPTSTAPAPSGGLFGAAPATSNAAPTSGLFGNSAPAATASSGGLFGAAPKPAAPSGGLFGSTAPATTAATTTATSGLFGAPTSAPSSAPATGGLFGASTAPAAATGGLFSIGAASASTPSVGLFGNSSASTTAAAAPATAPAAASTGGLFGATTAAAAAPTSSTTGGLFGSTAAAPAASLPTGGLFGSSTPAKTPAAPTAGLFGASSTTTTSAPATGSLFGTAPATTTATSAAPAASTGGLFGASSTTTPASTAPTGGLFGAATTTAPAAAAPTGGLFGAATTTAPATVGPTGGLFGAATTTTPATAATLGQTPSTVSATPSLPTTTSTTSTLPKPAEATPTLGLGLGLTSTPLAKGTGWTTSGLKGAATTSAGLKIGASGSDTLSEEEIKAGLGGNDTKAFFTALQEVVNSYHSEIAKQERVFHNKMLELNAYDRELITLEPKVLGLYNEMDDLSGSCKKLHFNVASMTSVLNDIEQNVVELENKLSLPEWHTLDYKFPLDSRFASRHDVQRVQIAQMMLNVDSQMKCADFDLDQITKSLNTMQSTVLKTKTETPLEKTELIMKKQLQKLMDLSTQHDATRDKLNKLKDDHNLKTNNSSKA
Protein: General transcription and DNA repair factor IIH subunit tfb2 (TFIIH subunit tfb2) (RNA polymerase II transcription factor B subunit 2) (P87303)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- General transcription and DNA repair factor IIH subunit tfb1
- General transcription and DNA repair factor IIH subunit tfb4
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription and DNA repair factor IIH subunit ssl1
- RNA polymerase II transcription factor B subunit 3
- General transcription and DNA repair factor IIH subunit tfb5
- Transcription initiation factor IIE subunit alpha
- General transcription and DNA repair factor IIH helicase subunit XPD
- Transcription initiation factor IIE subunit beta
- Cyclin mcs2
Sequence:
MQAEFKSSINDFLEQLPNHARLYQKPAACLAVFRLLPILARQYVMSMLFNPMPVALSDFDLWIKLSSKVYQSESFNKLVRMHIFQFDGQYITLNSEFRKQFITALTGGGNHNSFGVPCTDEDKHLVTVDFLDAYAKETWETILHFMVGTPEAKFPGEGVLSLLKRGGLMSGPKNQLRITRAGFQFLLQDINAQIWTLLLDYLKLSEDTHMDPVQVLHFLFMLGSLDLGRAYSVDFLTDTQQIMLEDLREYGLVYQRKITSKRFYPTRLATGLTTDYRSLHGKQSENDDDKGFIIVETNYRLYAYTSSPLQIAIIGLFANLRARFSNLVVGVITRDSIRRALMNGIAAEQIITYLTTHAHPQMRSNVPLLPPTLVDQIYLWELEKNRLRATPGILFRDFLTDSGFDQAVEYAKELGVLVWDSSLKRMFFITTTGAQPMIAYLKRRAVK
Protein: Conserved oligomeric Golgi complex subunit 2 (COG complex subunit 2) (Component of oligomeric Golgi complex 2) (LDLC protein homolog) (Q21444)
Organism: Caenorhabditis elegans
Function: Required for normal Golgi morphology and function.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 5
- Conserved oligomeric Golgi complex subunit 8
- Immediate early response 3-interacting protein 1
- Macro domain-containing protein
- BET1 homolog
- Nucleolar complex protein 3 homolog
Sequence:
MGTLHGEKTMFASPNTFYIDESKLCFNKTHFNREDFNVERFMNLARQKSDLKTIQQDLRLYLKSVQNSMIELINDDYADFVHLSSNLVSLQDSLNKIEQDINRIWDEFKESTRESVGMAERIEQKCDELCSNREKQIEIRDRIYFLVAIEKLSEMLLHPPRKCSALWLQKAASFASELKGSTFPHSEEENAAEKIILSQLEAVLCAEGVRSAAGDCQNLPLIYSILSLTESTHSLTALLVSDLLYAEFVNEKHDESNQLKLLKQVFESVKKMRETWAEKMGTEHFRGNIRRFLDETLLTFILTFIDKCMGAVAVPSDTRLFHECFLLTQEFIDNWPSSHTCRAMLKSIRDKFNLLVYFKLETHRFGKQCDQLMSPEMFAEPETSENRENTPQLHCGVSRAIITAIEHVWSDDVYLPPIVDKLWDFTLKLLLKHFSWSQTMKNYFMEEKRDWTSMVTLRSDTGNLHQLVFDFALESIWGKFHDITVDTAPFGQCLTKHGRSIDSLCVQIDDSIIEMFSEVLHQEIAQVSDVPKQYRWTKKSPPTTHSKYVVTAIEMVENLKEKLCCEEHPHTDEIVRKVNLSAFNYFVGKGNEVLDSVEATGSSLSRFKRKTTTDSGSTVTDDDKIKQQIYHDAKYFLSYAENLVFSQADLTGLQEVVNRFDKDARSAIVQEKNQNEEAGNA
Protein: Focadhesin (Q5VW36)
Organism: Homo sapiens (Human)
Function: Required for the maintenance of SKIC2 and SKIC3 proteostatic levels in the liver. May be involved in the regulation of RNA degradation by the exosome complex. Potential tumor suppressor in gliomas.
Subcellular location: Cell junction, focal adhesion {ECO:0000269|PubMed:22427331}. Cytoplasm, cytosol {ECO:0000269|PubMed:35864190}. Note=In astrocytes, colocalizes with VCL to the end of actin stress fibers, which normally terminate at focal adhesions. In hepatocytes, it is found in the cytosol. {ECO:0000269|PubMed:22427331, ECO:0000269|PubMed:35864190}.
Interaction partners:
Sequence:
MSDDIRKRFEFPNSLIQSQAVGHLIAAVLKENGFSEKIHQSTNQTPALNLLWEKCCSDNVVVRTACCEGLVALVAQDHAEFSYVLNGILNLIPSTRNTHGLIKAIMHLLQMQALKEGQGGEKNIQSIYTIRNHPHPLITVLEHRPDCWPVFLQQLTAFFQQCPERLEVSCIQIMAPFLWYLYCEPSQLQEYAKLRLALLKVLLQPQVLCDKDQPSILEQQILQLCCDIVPCLQVKDLIQTTEAMMFIEEVCLSLLRHPVFWKIQLTQMSLQLLCVSEVSLKITGECSSSIHLLEHSVELLKEDFPVELVIIGIALLLLQTPASQQKPILNLALKLLSVTEDQKIPKSSLLLVMPILQILSSTALEDCISVDEEGPSRQQLALNLLEMIQQECYRDDHQKLSYKLVCPVTSMYGTIFTAWRILEVMTDSSAASDWLASVESLLPITAVIPAPAFLLLAHLLVEDKGQNLHQILKVTTELAQADSSQVPNLIPVLMFKLGRPLEPILYNDILYTLPKLGVHKVCIGQILRIIQLLGTTPRLRAVTLRLLTSLWEKQDRVYPELQRFMAVSDVPSLSVGKEVQWEKLIAKAASIRDICKQRPYQHGADMLAAISQVLNECTKPDQATPAALVLQGLHALCQAEVVCIRSTWNALSPKLSCDTRPLILKTLSELFSLVPSLTVNTTEYENFKVQVLSFLWTHTQNKDPIVANAAYRSLANFSAGEHTILHLPEKIRPEIPIPEELDDDEDVEDVDLSVPGSCYLKLLSLTPPLVLPALEEFFTSLVKQEMVNMPRGIYHSALKGGARSDQGKTVAGIPNFILKMYETNKQPGLKPGLAGGMLFCYDVSMYQSKDGKPLNRLMASRGRSFKQTSLALVHEVHIQLSEWHRAIFLPQAWLAYMNRAYHAILQGRLGELELQLKHGKEEPEEVQYKKSTAWLWVRDMLTDEITKAAAKESPVVKGNALLALSSLAVVVSRHEASLSSDSDGLLEVQPNFLSMKEWVSMVLDTLLVIVDSHYQPRGQLLSWFYYKSYSGENTASAIARSAAATALSLLVPVFIISCKEKVEEILNMLTARLPGKPSADESQAVQIHMGLALGMFLSRLCEEKLSDISGQEMNLLLMKSLDALENCCFDTSLEYNTGCILGVGLVLSLMSHSSQMQSRVHVAALLRKLSAHVDDSGSQSRTFQEVLAYTLSCVCTSAFSAGIIEATEAEDVMNKLRLLVENSQQTSGFALALGNIVHGLSVCGHGKAEDLGSKLLPAWIRIVLTEGTPTMLCLAALHGMVALVGSEGDVMQLKSEAIQTSHFQGRLNEVIRTLTQVISVSGVIGLQSNAVWLLGHLHLSTLSSSQSRASVPTDYSYLPESSFIGAAIGFFITGGKKGPESVPPSLLKVVMKPIATVGESYQYPPVNWAALLSPLMRLNFGEEIQQLCLEIMVTQAQSSQNAAALLGLWVTPPLIHSLSLNTKRYLLISAPLWIKHISDEQILGFVENLMVAVFKAASPLGSPELCPSALHGLSQAMKLPSPAHHLWSLLSEATGKIFDLLPNKIRRKDLELYISIAKCLLEMTDDDANRIAQVTKSNIEKAAFVKLYLVSQGRFPLVNLTDMLSVAVQHREKEVLAWMILHSLYQARIVSHANTGVLKRMEWLLELMGYIRNVAYQSTSFHNTALDKALDFFLLIFATAVVAWADHTAPLLLGLSASWLPWHQENGPAGPVPSFLGRSPMHRVTLQEVLTLLPNSMALLLQKEPWKEQTQKFIDWLFSIMESPKEALSAQSRDLLKATLLSLRVLPEFKKKAVWTRAYGW