wanglab/gogpt-training-data huggingface dataset:
Protein: General transcription and DNA repair factor IIH helicase subunit XPD (TFIIH subunit XPD) (EC 5.6.2.3) (DNA 5'-3' helicase XPD) (DNA excision repair cross-complementing protein-2 homolog) (DNA repair protein D) (TFIIH basal transcription factor complex helicase repD subunit) (Q55G81)
Organism: Dictyostelium discoideum (Social amoeba)
Function: ATP-dependent 5'-3' DNA helicase, 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 CAK, 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. The ATP-dependent helicase activity of XPD/repD is required for DNA opening. 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 CAK controls the initiation of transcription. XPD/repD acts by forming a bridge between CAK and the core-TFIIH complex.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P18074}.
Interaction partners:
- General transcription factor IIH subunit 1
- General transcription factor IIH subunit 3
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription factor IIH subunit 2
- CDK-activating kinase assembly factor MAT1
- General transcription factor IIH subunit 4
- Putative cyclin-H
- General transcription factor IIE subunit 1
- General transcription factor IIE subunit 2
- Cyclin-dependent kinase 7
Sequence:
MKFYIEDLLVYFPYSYIYPEQYSYMVALKRSLDNGGPCILEMPSGTGKTVSLLSLISSYQVKNPSIKLIYCSRTVPEIEQATEEARRVLQYRNSEMGEESPKTLCMSMSSRRNLCIQPRVSEERDGKVVDALCRELTSSWNRESPTSEKCKFFENFESNGKEILLEGVYSLEDLKEYGLKHQMCPYFLSRHMLNFANIVIFSYQYLLDPKIASLISSSFPSNSIVVFDEAHNIDNVCINALSINIDNKLLDTSSKNIAKINKQIEDIKKVDEKRLKDEYQRLVNGLARSGSTRADETTSDPVLPNDVIQEAVPGNIRKAEHFISLLRRVVDYLKSRLKSQMLLSESPLAFLQGLYHATQISSRTLRFCSSRLSSLLRTLRINDVNQFSGISLIADFATLVGTYNNGFLIIIEPYYQRQNNTYDQIFQFCCLDASIGMKPIFDKYRSVVITSGTLSPLDIYTKMLNFRPTVVERLTMSLNRNCICPCILTRGSDQISISTKFDVRSDTAVVRNYGALLVEVSAIVPDGIICFFTSYSYMEQIVSVWNEMGLLNNILTNKLIFVETSDPAESALALQNYKKACDSGRGAVLLSVARGKVSEGIDFDNQYGRCVILYGIPYINTESKVLRARLEFLRDRYQIRENEFLTFDAMRTASQCVGRVIRGKSDYGIMIFADKRYNRLDKRNKLPQWILQFCQPQHLNLSTDMAISLSKTFLREMGQPFSREEQLGKSLWSLEHVEKQSTSKPPQQQNSAINSTITTSTTTTTTTSTISETHLT
Protein: Family with sequence similarity 50 member A (B0S8I6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKSNIDKKFSAHYDAVEAELKSSTVGLVTLNDMKAKQEALVKEREKQLAKKEQSKELQMKLEKLREKERKKEAKRKISSLSFTLEEEEEGGEEEEEAAMYEEEMEREEITTKKRKLGKNPDVDTSFLPDRDREEEENRLREELRQEWEAKQEKIKSEEIEITFSYWDGSGHRRTVKMRKGNTMQQFLQKALEILRKDFSELRSAGVEQLMYIKEDLIIPHHHSFYDFIVTKARGKSGPLFNFDVHDDVRLLSDATVEKDE
Protein: COP9 signalosome complex subunit 7 (CSN complex subunit 7) (Protein FUSCA 5) (Q94JU3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. It is involved in repression of photomorphogenesis in darkness by regulating the activity of COP1-containing Ubl ligase complexes. The complex is also required for degradation of IAA6 by regulating the activity of the Ubl ligase SCF-TIR complex. Regulates the TSO2 subcellular localization. May be involved in nucleic acid binding.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11029466}. Nucleus {ECO:0000269|PubMed:11029466}.
Interaction partners:
- COP9 signalosome complex subunit 6b
- COP9 signalosome complex subunit 6a
- COP9 signalosome complex subunit 5b
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 5a
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 2
- COP9 signalosome complex-related / CSN complex-like protein
Sequence:
MDIEQKQAEIIDQLVKRASTCKSEALGPLIIEATSHPSLFAFSEILALPNVAQLEGTTDSVYLDLLRLFAHGTWGDYKCNATRLPHLSPDQILKLKQLTVLTLAESNKVLPYDTLMVELDVSNVRELEDFLINECMYAGIVRGKLDQLKRCFEVPFAAGRDLRPGQLGNMLHTLSNWLNTSENLLISIQDKIKWADNMSEMDKKHRKEAEEGVEEVKKSLSMKGDVDIRGNKEMFGEPSGVMDYEEDGIRPKRRRHPVTR
Protein: Eukaryotic translation initiation factor 4E-1 (eIF4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein) (Q4VQY3)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. Key component of recessive resistance to potyviruses.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}.
Interaction partners:
- Eukaryotic translation initiation factor 4G
- MI domain-containing protein
- MI domain-containing protein
- Polyadenylate-binding protein
- Polyadenylate-binding protein
- Polyadenylate-binding protein
- Eukaryotic translation initiation factor 4G
- MIF4G domain-containing protein
- CYRIA/CYRIB Rac1 binding domain-containing protein
- Polyadenylate-binding protein
Sequence:
MAAAEMERTMSFDAAEKLKAADGGGGEVDDELEEGEIVEESNDTASYLGKEITVKHPLEHSWTFWFDNPTTKSRQTAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLIMGADFHCFKHKIEPKWEDPVCANGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHGDEICGAVVSVRAKGEKIALWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRNAKNRYTV
Protein: Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Q2F905)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}.
Interaction partners:
Sequence:
MTNLVRWLFSTNHKDIGTLYFIFGAIAGVMGTCFSVLIRMELARPGDQILGGNHQLYNVLITAHAFLMIFFMVMPAMIGGFGNWFVPILIGAPDMAFPRLNNISFWLLPPSLLLLLSSALVEVGSGTGWTVYPPLSGITSHSGGAVDLAIFSLHLSGVSSILGSINFITTIFNMRGPGMTMHRLPLFVWSVLVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSRKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFYYWVGKIFGRTYPETLGQIHFWITFFGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVVAITSSSGKNKRCAESPWAVEQNPTTLEWLVQSPPAFHTFGELPAIKKTKS
Protein: GMP synthase (glutamine-hydrolyzing) (EC 6.3.5.2) (Glutamine amidotransferase) (A0A140VJK6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAAHSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPEEVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPHTLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDWESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILRESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVEVVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Protein: pH-response regulator protein palC (Q9P905)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Required for the proteolytic cleavage of the transcription factor pacC in response to alkaline ambient pH.
Interaction partners:
- Vacuolar-sorting protein snf7
- Calpain-like protease palB
- pH-response regulator protein palF/RIM8
- pH-response transcription factor pacC/RIM101
- pH-response regulator protein palH/RIM21
- Vacuolar protein-sorting protein bro1
- Vacuolar protein sorting-associated protein 27
- Endosomal sorting complex protein TSG101, putative
- pH-response regulator protein palA/RIM20
Sequence:
MVYPFELPTTSHLSFQSALSSHTHPSLPQSATTARHALRLALKAHNRLPRGFQRDSHLTSVLSAINDYLPYVVALAQGLNNGKPIDTTTPSTTTHLEEIRVAQRAELEPEWRATLASSSLRRPSTNRTRGTGVQYELAFILTTLGYILSSLARSGVTRTLYASTTPSAEQRTAAVQTATKHLLQASTIHSFLSSSPYFATVSEAATLPDLAPATQAALSSLALAEATLLTVLKDDSYVVACIQARNPNDKDWMVRAPEIPKVRAHLFARLCIRAAEYAEQAATGLSSVAAEGRKAGVDEDVARYAHVLGLVARARACRFFGVDAELAGKVGEGIAWLRAAKGALGLRNTGSASAEEVTTKSRGLSKLKLGFRERREERKLEKGAGGERVDKGGLGPGDNAGREEEGRVLEMLETKWVRANDTLNTQLIPSSADYVANLPSGRDVLPPQPPYTPPSLDEERLFQMRGPPTELELNPGSDDGDSDFESQAAGDAHTPGAFPGRADNAYY
Protein: Signal recognition particle subunit SRP54 (EC 3.6.5.4) (Signal recognition particle 54 kDa protein) (Q7ZVN5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). As part of the SRP complex, associates with the SRP receptor (SR) component srpra to target secretory proteins to the endoplasmic reticulum membrane. Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes. Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA. Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit srpra. SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER (By similarity). Requires the presence of srp9/srp14 and/or srp19 to stably interact with RNA (By similarity). Plays a role in proliferation and differentiation of granulocytic cells, neutrophils migration capacity and exocrine pancreas development.
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:P61011}. Cytoplasm {ECO:0000250|UniProtKB:P61011}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P61011}.
Interaction partners:
- Signal recognition particle subunit SRP72
- Signal recognition particle 14 kDa protein
- Signal recognition particle subunit SRP68
- Signal recognition particle 19 kDa protein
- Signal recognition particle 9 kDa protein
- SRP receptor subunit alpha
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL29
- FAU ubiquitin-like and ribosomal protein S30 fusion a ubiquitously expressed
Sequence:
MVLADLGRKITSALRSLSNATIINEEVLNAMLKEVCAALLEADVNIKLVKQLRENVKAAIDLEEMASGLNKRRMIQHAVFKELVKLVDPGVKAWTPTKGKNNVIMFVGLQGSGKTTTCSKLAYYFQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKFKSENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNELKLDDNEELIDKLKHGQFTLRDMYEQFQNIMKMGPFGQIMGMIPGFGTDFMSKGNEQESMARLKKLMTIMDSMNDQELDNKDGAKLFSKQPNRIQRVARGSGVATRDVQELLTQYTKFAQMVKKMGGIKGLFKGGDMSKNVNPSQMAKLNQQMAKMMDPRVLHHMGGMAGLQSMMRQFQQGAAGNMKGMMGFNNM
Protein: Serine protease hepsin (EC 3.4.21.106) [Cleaved into: Serine protease hepsin non-catalytic chain; Serine protease hepsin catalytic chain] (O35453)
Organism: Mus musculus (Mouse)
Function: Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL. Plays a role in cell growth and maintenance of cell morphology. Plays a role in the proteolytic processing of ACE2 (By similarity). Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:26673890}; Single-pass type II membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P05981}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P05981}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:9395459}.
Interaction partners:
- Kunitz-type protease inhibitor 1
- Hepatocyte growth factor
- Hepatocyte growth factor-like protein
- Immunoglobulin lambda-like polypeptide 1
- Kunitz-type protease inhibitor 2
Sequence:
MAKEDEEPGAHRGGSTCSRPQPGKGGRTAACCSRPKVAALIVGTLLFLTGIGAASWAIVTILLQSDQEPLYQVQLSPGDSRLAVFDKTEGTWRLLCSSRSNARVAGLGCEEMGFLRALAHSELDVRTAGANGTSGFFCVDEGGLPLAQRLLDVISVCDCPRGRFLTATCQDCGRRKLPVDRIVGGQDSSLGRWPWQVSLRYDGTHLCGGSLLSGDWVLTAAHCFPERNRVLSRWRVFAGAVARTSPHAVQLGVQAVIYHGGYLPFRDPTIDENSNDIALVHLSSSLPLTEYIQPVCLPAAGQALVDGKVCTVTGWGNTQFYGQQAMVLQEARVPIISNEVCNSPDFYGNQIKPKMFCAGYPEGGIDACQGDSGGPFVCEDSISGTSRWRLCGIVSWGTGCALARKPGVYTKVTDFREWIFKAIKTHSEASGMVTQP
Protein: Probable NADPH:adrenodoxin oxidoreductase, mitochondrial (AR) (Adrenodoxin reductase) (EC 1.18.1.6) (Ferredoxin--NADP(+) reductase) (Ferredoxin reductase) (Q54KG7)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P48360}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- 2Fe-2S ferredoxin-type domain-containing protein
- Cytochrome b5 heme-binding domain-containing protein
- Cytochrome b5 reductase
- Cytochrome b5 domain-containing protein
- Dihydropyrimidine dehydrogenase [NADP
- Dihydroorotate dehydrogenase
- Electron transfer flavoprotein subunit beta
- Glutamate dehydrogenase, mitochondrial
- Glutamate dehydrogenase 2
- Multifunctional protein pyr1-3
Sequence:
MINVLINKSSKLVNGVDSCINNKTIRLFCSSSSTNQVNKTPFNLCIIGSGPAGLYTAAKVHRQIPHANITILEKLPYPFGLVRSGISPDHQNEKKVKNTLEKVLLEHPHQIQFIGNVDIEKDIKFQYIKDNFHAVVLACGIEGDKKLGIPGELTLKNVYFAREFIGWLNGNLKDQHKQFDLSNENLAIVGQGNVALDVARLLLKKNSDELKKTDITSTSFDKINKSNVKNIHIIGRRGPLEVSFTNKEIREILTLQNVNTFINDISTLDVSEEDVSKLERAKKRTFELFKQHLKPFDQEIANNGNMNLIFHFLRSPVELLDKYGSSSGSGDGMVLSKIKLEKNKLIIDEKTQQKKAIGSGEFEIIECSSLFRSIGYTGTKQFPSVPFDFNSVSIPNKYGKVLEEPNSDKFINGLYVSGWLKGGPSGSIPNISANSEETASIIHQDYESNQFINNNNNNDGGHNSITSLLQPNHKIINFNDYKKIESEEVKRGKEKGKLLEKIIVFDELKNIINNS
Protein: Pico, isoform C (M9MSQ5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MINLRGILVGGAASSAGVAGAAAGGATTTTTTTTAAGFVAGGDCPVIGAGAGAGVKLRRHSDRPLTPEAKQLSHTYRISMANLEDSQESELDQILGELSLLEAQISYTEASMLPAMCAPSAGAQIAPPPGVTQLPGSAPTMVSMSASSSRSHSRTNSTISADVSSCSSSGISENGHGLGLVLGGPGSAGMMVQPPPPGGMTMGITLGVVTPREPRTESPDNDSAFSDTVSLLSSESSASSNTSLQQQQQQQQQQHHQHQQHHQHQQQQQKPQLAGAEKLHHHGVHGQHGGQQSGANSITKADKIQLALHKLESAPIRRLFVKAFTSDGASKSLLVDERMGCGHVTRLLADKNHVQMQSNWALVEHLGDLQMERLFEDHELLVDNLMTWHSDAGNRVLFQQRPDKVTLFLRPELYLPGPQMAPGCQHDEQTRQMLLDEFFDSHNQLQMDGPLYMKADPKKGWKRYHFVLRSSGLYYFPKEKTKNTRDLACLNLFHGHNVYTGLGWRKKWKSPTDYTFGFKAVGDSSLGKSCRSLKMLCAEDLPTLDRWLTAIRVCKYGKQLWDSHKSLLEDLCLSRDDAVSQSSFAASMRSESISSISSAVPSQCGSVSSAISSMSNSTSGRTSRASSSSSSGCLSDDNNAFDSEFTTGTIKRKPSMKPNLPLTTMTRQLKEVGEITICESAGGDASSPERSGTLTRRHSRRKSQESNGSGTLKRRPIAVPVATVVKQTEPMGSASSTSSSSNSTPTPTPSICAKPPPGDSASLMCSSTLSLDSLPPPPPPPALDGSEDQDVYGSQLSLASLPPPPPPEDVLAMNYAEPSSPSTPTPMSTPMIMPNSNGSLPPAVPAKPMKPAVKQAAGGLKAAPPYKAPPDYVGPALLPGPPLPPPPPAQKKVSFADSPVLLRRKMCSPEPVLPQRSPSTTLSCHSSSSAGSAYQTYAPGPMLPPRADVARLSSLSNGSSSEVTSPKRLQESASNPPRDFLKDLQRVMRKKWQVAQKCKAEPATTPHEVLGFRDFSNEDLLAAHNLNSGANSSHYYRETANVSHWVRKHYEYAHNALYENVHAQSAAAAGVPGSGEATTPPLPPPPGNSVAAKKRPPPPPPKRSDKTHLTNRV
Protein: GATA-type transcription factor sreA (Siderophore uptake regulator sreA) (Q4WV91)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: GATA-type transcription repressor that regulates iron- acquisition genes through specific binding the GATA sequence element 5'-ATCWGATAA-3' of target promoters. Iron acquisition regulation is critical for survival under both iron-limiting conditions (to acquire essential iron) and iron-replete conditions (to limit iron toxicity). SreA targets include genes encoding a number of key iron-regulated factors such as those involved in siderophore biosynthesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- bZIP transcription factor hapX
- High affinity iron permease ftrA
- MFS siderochrome iron transporter C
- MFS siderochrome iron transporter B
- GATA transcriptional activator AreA
- Transcription activator of gluconeogenesis acuK
- Homoaconitase, mitochondrial
- Cytochrome c
- L-ornithine N
- Nitrogen metabolite repression regulator NmrA
Sequence:
MLASVPQMDSVRSLPRNHDVVARHASAEDLDAAQQLISSAQAGREHTTDRHRDEKVTAPVRHQMKTSMNGQRWPEQQRTAPPAEKTSTSPKAQKDTSFLGHSCSNCGTKSTPLWRRSPTGAMICNACGLYLKARNVARPTKRNRMEPGSEAGGQQTGHGIAQSESASQGHCQSNSGGGSCPGGGNCNGTGGAEGCDGCPAYNNRVYKSAARGTVPIHSWRATNSGSDRPLAETENDAGKNGATVEGGNMLVSCQNCGTTVTPLWRRDENGHPICNACGLYYKLHGCYRPTTMKKSIIKRRKRVVPALRDQSPSGATYSSNGSSASPEASPAVLAHSHDDHYRYLSSDPTLQANHQRHYAVAPPPVDFTHFSATGSLSLPHHPPPPRLLEPERLSAPSHSPIPQFGRRSISPSTSGSAKKRTLAETTSSTDTASVPTTLESGSNQLPPIISTANPSPPGRLSSISTLLNHSGPHDESRLDPSLAALSRQQQHHKATPLPPHPPSQPLPGVSELESLKEDRRAKLQREAEEMREMLRAKERELAELGA
Protein: SNF7 family protein (AFU_orthologue AFUA_5G13890) (Q5AXR0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Vacuolar-sorting protein snf7
- SNF7 family protein
- SNF7 family protein
- Vacuolar sorting protein SNF7 family protein, putative
- SNF7 family protein Fti1/Did2, putative
- vesicle-fusing ATPase
- Vacuolar protein sorting-associated protein 28
- Vacuolar-sorting protein SNF8
- SNF7 family protein
- Endosomal sorting complex protein TSG101, putative
Sequence:
MESLKAVFFGPDPQTQMRKCNQLIRANTRQLDRDIAQLKALDGKTRQTIVNASKRAQRNPARAKQANLEAKMLARELVRVRRQTTRLTTSRAQLQSVQMQVNEAFAVRKIQGSLQKSTGIMKDVNTLIRLPQLSATMHQLATELVRAGIIEEMVDDAIPNNELLEDEEAEADEEVDKILQEILQGKLSQVDEVKPERPLEEPQQAEEEFEDQEAALAQMRGRLEALKS
Protein: Calcium-dependent protein kinase 3 (EC 2.7.11.1) (PbCDPK3) (A0A509AFG4)
Organism: Plasmodium berghei (strain Anka)
Function: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). In the mosquito midgut, regulates the gliding motility of the ookinete which is essential for the ookinete to invade the midgut epithelium. However, another study showed that while required for ookinete invasion of the midgut epithelium, is not required for ookinete gliding motility.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16430692}.
Interaction partners:
- non-specific serine/threonine protein kinase
Sequence:
MNQLCVERNLSISTAYIKSKPKKYIERIKKKKSSNKSIKSQHKFEGSKIANKNNELKDIKSKDPKHYENHINKNTKHKDILLKSKRSDNFKFSRRGFILSFTGNLEDFYNLSEEPLGKGTYGCVYKATDKLLKIQRAVKVVSKKKLKNIPRFRQEIDIMKNLDHPNVIKLLETFEDEEQIYLIMDLCTGGELFDKIIKKGSFVEMYASFIMKQIFSVLNYLHIRNICHRDIKPENFLFYDKSTESLIKIIDFGLAAYFNDIDYEMKTKAGTPYYVAPQVLTGCYDYKCDLWSAGVLFYIILCGYPPFYGESDHEILSMVKKGKYNFKGKEWNNISEEAKDLIKRCLTIDSGKRINASEALKHPWFKKKKGSFNLDVKMDIHVLENFKNYALLLKLQKLAMTIIAQQSNDYDLQQLKTVFLYLDEDGKGNITKNQLKKGLENSGLKLPQNFDVLLDQIDSDGSGRIDYTEFLAAALDRKHLSKKLIYCAFRVFDVDNDGEITTAELAHILYNGNKKGSITQKDVNQVKKMIQEVDKNNDGKIDFYEFCEMMKLKY
Protein: Dof zinc finger protein DOF3.5 (AtDOF3.5) (Q9SVC5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds specifically to a 5'-AA[AG]G-3' consensus core sequence.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MERAEALTSSFIWRPNANANAEITPSCPRCGSSNTKFCYYNNYSLTQPRYFCKGCRRYWTKGGSLRNVPVGGGCRKSRRPKSSSGNNTKTSLTANSGNPGGGSPSIDLALVYANFLNPKPDESILQENCDLATTDFLVDNPTGTSMDPSWSMDINDGHHDHYINPVEHIVEECGYNGLPPFPGEELLSLDTNGVWSDALLIGHNHVDVGVTPVQAVHEPVVHFADESNDSTNLLFGSWSPFDFTADG
Protein: Putative glutathione peroxidase 7, chloroplastic (EC 1.11.1.9) (Q9SZ54)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May constitute a glutathione peroxidase-like protective system against oxidative stresses.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione reductase, chloroplastic
- Glutathione S-transferase DHAR2
- Glutathione synthetase, chloroplastic
- L-ascorbate peroxidase 3
- Monodehydroascorbate reductase 3
- Glutathione S-transferase F9
- Glutathione S-transferase T1
- Glutathione S-transferase F6
- Glutathione S-transferase F8, chloroplastic
Sequence:
MAFSYASFSTPFNGFAANPSPITSAFLGPSLRFSTRTSKTRNPSNGVSVKSSNSHRFLVKSKNFSVYARAAAEKSVHDFTVKDIDGNDVSLDKFKGKPLLIVNVASRCGLTSSNYSELSQLYEKYKNQGFEILAFPCNQFGGQEPGSNPEIKQFACTRFKAEFPIFDKVDVNGPSTAPIYKFLKSNAGGFLGDIIKWNFEKFLVDKKGKVVERYPPTTSPFQIEKDIQKLLAA
Protein: Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (Q69ZA1)
Organism: Mus musculus (Mouse)
Function: Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis.
Subcellular location: Nucleus speckle {ECO:0000250}.
Interaction partners:
- Cyclin-K
- Cyclin-T1
- Cyclin-T2
- Cyclin-dependent kinase 9
- Bromodomain-containing protein 4
- Cyclin-dependent kinase 12
- Transcription elongation factor SPT5
- Cyclin-H
- DNA-directed RNA polymerase II subunit RPB1
- Parafibromin
Sequence:
MPSSSDTALGGGGGLSWAEKKLEERRKRRRFLSPQQPPLLLPLLQPQLLQPPPPPPPLLFLAAPGAAAAAAAAAAASSSCFSPGPPLEVKRLARGKRRPGGRQKRRRGPRAGQEAEKRRVFSLPQPQQDGGGGASSGGGVTPLVEYEDVSSQSEQGLLLGGASAATAATAAGGTGGNGGSPASSSGTQRRAEGSERRPRRDRRSSSGRSKERHREHRRRDGTRSGSEASKARSRHGHSGEERAEAAKSGSSSSSGGRRKSASATSSSSSSRKDRDLKAHRSRTKSSKEPPSAYKEPPKAYREDKSEPKAYRRRQRSLSPLGGRDESPVSHRASQSLRSRKSPSPAGGGSSPYSRRLPRSPSPYSRRRSPSYSRHSSYERGGDVSPSPYSSSSWRRSRSPYSPVLRRSAKSRSRSPYSSRHSRSRSRHRLSRSRSRHSSISPSTLTLKSSLAAELNKNKKARAAEAARAAEAAKAAEAAKAAEAAAKAAKASNASTPTKGNTETGASVSQTNHVKEVKKLKTEHAPSPSSGGTVKSDKAKTKPPLQVTKVDNNLTVEKATKKTVVGKESKPAATKEEPVSTKEKSKPLTPSTGAKEKEQHVALVTSTLPPLPLPPMLPEDKDADSLRGNISVKAVKKEVEKKLRCLLADLPLPPELPGGDDLSKSPEEKKTAAQLHSKRRPKICGPRYGEIKEKDIDWGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMPPPDLPLWQDCHELWSKKRRRQKQMGMTDDLSTIKAPRKDLSLGLDDSRTNTPQGVLPPAQLKSQSNSNVAPVITGPGQPLNHSELAILLNLLQSKSSVNMADFVQVLNIKVNSETQQQLNKINLPAGILATGEKQTDPSTPQQESSKSLGGVQPSQTIQPKVETDAAQAAVQSAFAVLLTQLIKAQQSKQKDAMLEERENGSGHEAPLQLRPPLEPSTPGSGQDDLIQHQDRRILELTPEPDRPRILPPDQRPPEPPEPPPVTEEDLDYRTENQHVPTTSSSLTDPHAGVKAALLQLLAQHQPQDDPKREGGIDYPTGDTYVPSSDYKDNFGSSFSAAPYVSSDGLGSSSAAAPLEARSFIGNSDIQSLDNYSTASSHTGGPPQTSAFTESFASSVAGYGDIYLNAGPMLFSGDKDHRFEYSHGPITVLTNSNDPSTGPESTHPLPAKMHNYNYGGNLQENPGGPSLMHGQTWTSPAQGPGYSQGYRGHISTSAGRGRGRGLPY